|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5230 |
| Enzyme 1 Name |
Deoxycytidylate deaminase |
| Enzyme 1 Synonyms |
- dCMP deaminase
|
| Enzyme 1 Gene Name |
DCTD |
| Enzyme 1 Protein Sequence |
>Deoxycytidylate deaminase
MSEVSCKKRDDYLEWPEYFMAVAFLSAQRSKDPNSQVGACIVNSENKIVGIGYNGMPNGC
SDDVLPWRRTAENKLDTKYPYVCHAELNAIMNKNSTDVKGCSMYVALFPCNECAKLIIQA
GIKEVIFMSDKYHDSDEATAARLLFNMAGVTFRKFIPKCSKIVIDFDSINSRPSQKLQ
|
| Enzyme 1 Number of Residues |
178 |
| Enzyme 1 Molecular Weight |
20015.8 |
| Enzyme 1 Theoretical pI |
7.65 |
| Enzyme 1 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- ion binding
- metal ion binding
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in zinc ion binding |
| Enzyme 1 Specific Function |
Supplies the nucleotide substrate for thymidylate synthetase |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- dCMP + H2O = dUMP + NH3 [RN:R01663]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
61742819  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P32321 |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
DCTD_HUMAN |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>537 bp
ATGAGTGAAGTTTCCTGCAAGAAACGGGACGACTATTTGGAATGGCCAGAGTATTTTATG
GCTGTGGCCTTCTTATCAGCACAGAGAAGCAAAGATCCAAATTCCCAGGTCGGCGCCTGC
ATCGTGAATTCAGAAAACAAGATTGTCGGGATTGGGTACAATGGGATGCCAAATGGGTGC
AGTGATGACGTGTTGCCTTGGAGAAGGACAGCAGAGAATAAGCTGGACACCAAATACCCG
TACGTGTGCCATGCGGAGCTGAATGCCATCATGAACAAAAATTCGACCGATGTGAAAGGC
TGTAGTATGTATGTTGCCTTGTTCCCTTGTAATGAATGCGCTAAGCTCATCATCCAGGCA
GGTATAAAAGAAGTGATTTTCATGTCTGATAAATACCATGATAGTGACGAGGCAACTGCT
GCGAGGCTCCTGTTTAATATGGCCGGGGTGACATTCCGGAAATTCATACCGAAGTGCAGC
AAGATTGTCATTGACTTTGATTCAATTAACAGCAGACCGAGTCAAAAGCTTCAGTGA
|
| Enzyme 1 GenBank Gene ID |
NM_001921.2 |
| Enzyme 1 GeneCard ID |
DCTD |
| Enzyme 1 GenAtlas ID |
DCTD |
| Enzyme 1 HGNC ID |
HGNC:2710 |
| Enzyme 1 Chromosome Location |
4 |
| Enzyme 1 Locus |
4q35.1 |
| Enzyme 1 SNPs |
SNPJam Report |
| Enzyme 1 General References |
- Weiner KX, Weiner RS, Maley F, Maley GF: Primary structure of human deoxycytidylate deaminase and overexpression of its functional protein in Escherichia coli. J Biol Chem. 1993 Jun 15;268(17):12983-9. [PubMed ]
- Weiner KX, Ciesla J, Jaffe AB, Ketring R, Maley F, Maley GF: Chromosomal location and structural organization of the human deoxycytidylate deaminase gene. J Biol Chem. 1995 Aug 11;270(32):18727-9. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5232 |
| Enzyme 2 Name |
Cytosolic 5'-nucleotidase 1B |
| Enzyme 2 Synonyms |
- cN1B
- Autoimmune infertility-related protein
- Cytosolic 5'-nucleotidase IB
- cN-IB
|
| Enzyme 2 Gene Name |
NT5C1B |
| Enzyme 2 Protein Sequence |
>Cytosolic 5'-nucleotidase 1B
MSQTSLKQKKNEPGMRSSKESLEAEKRKESDKTGVRLSNQMRRAVNPNHSLRCCPFQGHS
SCRRCLCAAEGTALGPCHTIRIYIHMCLLWEQGQQITMMRGSQESSLRKTDSRGYLVRSQ
WSRISRSPSTKAPSIDEPRSRNTSAKLPSSSTSSRTPSTSPSLHDSSPPPLSGQPSLQPP
ASPQLPRSLDSRPPTPPEPDPGSRRSTKMQENPEAWAQGIVREIRQTRDSQPLEYSRTSP
TEWKSSSQRRGIYPASTQLDRNSLSEQQQQQREDEDDYEAAYWASMRSFYEKNPSCSRPW
PPKPKNAITIALSSCALFNMVDGRKIYEQEGLEKYMEYQLTNENVILTPGPAFRFVKALQ
YVNARLRDLYPDEQDLFDIVLMTNNHAQVGVRLINSVNHYGLLIDRFCLTGGKDPIGYLK
AYLTNLYIAADSEKVQEAIQEGIASATMFDGAKDMAYCDTQLRVAFDGDAVLFSDESEHF
TKEHGLDKFFQYDTLCESKPLAQGPLKGFLEDLGRLQKKFYAKNERLLCPIRTYLVTARS
AASSGARVLKTLRRWGLEIDEALFLAGAPKSPILVKIRPHIFFDDHMFHIEGAQRLGSIA
AYGFNKKFSS
|
| Enzyme 2 Number of Residues |
610 |
| Enzyme 2 Molecular Weight |
68803.1 |
| Enzyme 2 Theoretical pI |
9.03 |
| Enzyme 2 GO Classification |
| Function |
- 5'-nucleotidase activity
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- magnesium ion binding
- metal ion binding
- nucleotidase activity
- nucleotide binding
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 2 General Function |
Involved in nucleotide binding |
| Enzyme 2 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides. Helps to regulate adenosine levels |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
50593110 |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q96P26 |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
5NT1B_HUMAN |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1833 bp
ATGAGTCAAACATCTCTCAAACAGAAAAAGAATGAGCCTGGAATGAGGTCCTCAAAAGAG
AGTCTAGAAGCAGAAAAAAGAAAGGAATCTGACAAAACAGGAGTTCGTCTGAGCAATCAG
ATGAGGCGTGCAGTCAATCCGAATCACTCGCTGAGATGTTGCCCCTTCCAGGGTCACTCG
TCGTGTAGACGCTGCCTTTGTGCAGCTGAGGGAACAGCCCTTGGCCCCTGCCACACAATA
CGTATTTATATTCACATGTGCCTGTTGTGGGAGCAGGGCCAGCAGATCACCATGATGAGG
GGATCACAAGAATCATCACTGCGGAAGACAGACTCTCGAGGGTACCTTGTGCGCAGTCAA
TGGTCTAGAATATCCCGGAGCCCATCCACCAAGGCTCCATCCATAGATGAGCCTAGAAGC
AGGAACACCAGTGCTAAGCTCCCCAGCAGCTCCACGAGCTCCCGGACTCCATCCACCTCC
CCAAGCCTGCATGACTCCTCACCGCCGCCGCTGTCCGGGCAGCCCTCGCTCCAGCCACCC
GCGTCGCCCCAGCTGCCCCGGTCGCTGGACTCGCGGCCTCCCACGCCCCCAGAGCCCGAT
CCTGGCTCCCGGCGCAGCACCAAAATGCAAGAGAATCCGGAGGCCTGGGCCCAAGGCATC
GTGCGGGAAATCCGCCAGACCCGGGACTCGCAGCCGCTGGAATATTCGCGCACGTCCCCC
ACCGAGTGGAAGTCCTCCAGCCAGCGCAGGGGGATCTACCCCGCCTCCACCCAGCTGGAC
CGCAACTCTCTGTCCGAGCAGCAGCAGCAGCAGCGGGAGGACGAGGACGACTACGAGGCT
GCCTACTGGGCATCCATGAGGTCGTTCTACGAGAAGAACCCGAGCTGCTCGCGCCCCTGG
CCGCCCAAACCCAAGAACGCCATCACCATTGCTCTCTCATCCTGCGCGCTCTTCAACATG
GTGGACGGCAGGAAAATCTACGAGCAAGAGGGTCTGGAAAAGTACATGGAGTATCAGCTC
ACCAATGAGAACGTCATCCTGACCCCGGGCCCGGCGTTCCGCTTCGTCAAGGCACTACAG
TATGTCAATGCTAGACTCCGTGATCTATATCCTGATGAACAGGACTTATTTGATATTGTA
CTGATGACTAATAACCATGCCCAAGTGGGAGTGCGGCTTATAAACAGCGTCAATCACTAC
GGCTTACTGATTGACCGCTTCTGTCTGACCGGGGGAAAAGACCCCATTGGCTATTTGAAG
GCATATCTTACCAACTTGTATATTGCTGCAGATTCTGAAAAAGTGCAAGAGGCAATACAA
GAAGGTATTGCCTCTGCGACAATGTTTGATGGAGCCAAAGACATGGCTTACTGTGACACT
CAGCTCCGTGTAGCCTTTGATGGGGATGCTGTCCTCTTCTCTGATGAGTCTGAACATTTT
ACCAAGGAGCATGGGCTCGACAAATTCTTCCAGTATGATACATTATGTGAAAGTAAGCCT
CTTGCTCAGGGTCCCCTAAAAGGCTTTCTGGAAGATTTAGGCAGACTGCAAAAGAAGTTC
TATGCCAAAAATGAACGGTTACTTTGTCCTATCAGGACCTACCTGGTTACAGCTAGGAGT
GCAGCCAGTTCAGGCGCCCGTGTGCTGAAGACCCTTCGACGCTGGGGTCTAGAGATAGAC
GAAGCTCTTTTCCTTGCTGGAGCCCCCAAAAGTCCCATCTTGGTGAAGATCCGGCCCCAC
ATCTTCTTTGATGACCACATGTTCCACATTGAAGGGGCACAGAGGTTAGGTTCCATCGCA
GCTTATGGCTTTAATAAAAAATTCAGTAGTTAG
|
| Enzyme 2 GenBank Gene ID |
NM_001002006.2 |
| Enzyme 2 GeneCard ID |
NT5C1B |
| Enzyme 2 GenAtlas ID |
NT5C1B |
| Enzyme 2 HGNC ID |
HGNC:17818 |
| Enzyme 2 Chromosome Location |
2 |
| Enzyme 2 Locus |
2p24.2 |
| Enzyme 2 SNPs |
SNPJam Report |
| Enzyme 2 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Sala-Newby GB, Newby AC: Cloning of a mouse cytosolic 5'-nucleotidase-I identifies a new gene related to human autoimmune infertility-related protein. Biochim Biophys Acta. 2001 Oct 31;1521(1-3):12-8. [PubMed ]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5233 |
| Enzyme 3 Name |
Cytosolic 5'-nucleotidase 1A |
| Enzyme 3 Synonyms |
- cN1A
- Cytosolic 5'-nucleotidase IA
- cN-I
- cN-IA
|
| Enzyme 3 Gene Name |
NT5C1A |
| Enzyme 3 Protein Sequence |
>Cytosolic 5'-nucleotidase 1A
MEPGQPREPQEPREPGPGAETAAAPVWEEAKIFYDNLAPKKKPKSPKPQNAVTIAVSSRA
LFRMDEEQQIYTEQGVEEYVRYQLEHENEPFSPGPAFPFVKALEAVNRRLRELYPDSEDV
FDIVLMTNNHAQVGVRLINSINHYDLFIERFCMTGGNSPICYLKAYHTNLYLSADAEKVR
EAIDEGIAAATIFSPSRDVVVSQSQLRVAFDGDAVLFSDESERIVKAHGLDRFFEHEKAH
ENKPLAQGPLKGFLEALGRLQKKFYSKGLRLECPIRTYLVTARSAASSGARALKTLRSWG
LETDEALFLAGAPKGPLLEKIRPHIFFDDQMFHVAGAQEMGTVAAHVPYGVAQTPRRTAP
AKQAPSAQ
|
| Enzyme 3 Number of Residues |
368 |
| Enzyme 3 Molecular Weight |
41020.1 |
| Enzyme 3 Theoretical pI |
6.52 |
| Enzyme 3 GO Classification |
| Function |
- 5'-nucleotidase activity
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- magnesium ion binding
- metal ion binding
- nucleotidase activity
- nucleotide binding
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 3 General Function |
Involved in nucleotide binding |
| Enzyme 3 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides and has a broad substrate specificity. Helps to regulate adenosine levels in heart during ischemia and hypoxia |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- a 5'-ribonucleotide + H2O = a ribonucleoside + phosphate [RN:R07297]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
12659324 |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9BXI3 |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
5NT1A_HUMAN |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1107 bp
ATGGAACCTGGGCAGCCCCGGGAGCCCCAGGAGCCCCGCGAGCCCGGGCCAGGAGCGGAG
ACCGCTGCGGCCCCGGTCTGGGAGGAAGCCAAGATTTTCTACGACAACCTCGCGCCCAAG
AAGAAACCCAAATCGCCCAAGCCTCAGAATGCAGTCACCATCGCTGTGTCCTCCCGAGCC
TTGTTTCGCATGGACGAGGAGCAGCAGATCTACACGGAGCAGGGCGTGGAGGAGTACGTG
CGCTACCAGCTGGAACATGAGAACGAACCCTTCAGTCCCGGGCCAGCCTTCCCTTTTGTG
AAGGCTCTGGAGGCCGTGAACAGGCGGCTGCGGGAGCTGTACCCTGATAGTGAGGACGTC
TTCGACATCGTCCTCATGACTAACAACCATGCTCAAGTGGGTGTCCGCCTCATCAACAGT
ATCAACCACTATGACCTGTTCATCGAGAGGTTCTGCATGACAGGTGGGAACAGCCCGATC
TGCTACCTCAAGGCCTATCACACCAACCTCTACTTGTCAGCCGATGCGGAAAAAGTGCGA
GAAGCCATTGATGAGGGGATCGCAGCTGCCACCATCTTCAGCCCCAGCAGGGATGTGGTT
GTGTCCCAGAGTCAGCTGCGCGTGGCCTTCGATGGGGACGCCGTGCTCTTCTCGGACGAG
TCGGAGCGCATCGTCAAGGCCCACGGGCTGGACCGATTCTTCGAGCATGAGAAGGCCCAC
GAGAACAAGCCTCTGGCTCAGGGCCCCTTAAAGGGCTTTCTGGAGGCACTGGGTAGGTTG
CAGAAGAAGTTCTACTCCAAAGGCCTGCGGCTGGAGTGCCCAATTCGTACCTACTTGGTG
ACAGCACGCAGTGCAGCCAGTTCCGGGGCCCGGGCTCTCAAGACCCTGCGCAGCTGGGGC
CTGGAGACAGATGAAGCCTTGTTCCTTGCTGGAGCGCCCAAGGGCCCTCTCCTTGAGAAG
ATCCGCCCACACATCTTCTTTGATGACCAGATGTTCCATGTGGCTGGGGCTCAGGAGATG
GGCACTGTGGCCGCCCATGTGCCTTATGGTGTGGCACAGACACCCCGGCGGACTGCACCT
GCAAAGCAGGCCCCATCTGCACAGTAG
|
| Enzyme 3 GenBank Gene ID |
AF331801 |
| Enzyme 3 GeneCard ID |
NT5C1A |
| Enzyme 3 GenAtlas ID |
NT5C1A |
| Enzyme 3 HGNC ID |
HGNC:17819 |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p34.3-p33 |
| Enzyme 3 SNPs |
SNPJam Report |
| Enzyme 3 General References |
- Hunsucker SA, Spychala J, Mitchell BS: Human cytosolic 5'-nucleotidase I: characterization and role in nucleoside analog resistance. J Biol Chem. 2001 Mar 30;276(13):10498-504. Epub 2000 Dec 22. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5234 |
| Enzyme 4 Name |
5'(3')-deoxyribonucleotidase, cytosolic type |
| Enzyme 4 Synonyms |
- Cytosolic 5',3'-pyrimidine nucleotidase
- Deoxy-5'-nucleotidase 1
- dNT-1
|
| Enzyme 4 Gene Name |
NT5C |
| Enzyme 4 Protein Sequence |
>5'(3')-deoxyribonucleotidase, cytosolic type
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADK
VASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHL
GPQFVERIILTRDKTVVLGDLLIDDKDTVRGQEETPSWEHILFTCCHNRHLVLPPTRRRL
LSWSDNWREILDSKRGAAQRE
|
| Enzyme 4 Number of Residues |
201 |
| Enzyme 4 Molecular Weight |
23382.5 |
| Enzyme 4 Theoretical pI |
6.63 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in metal ion binding |
| Enzyme 4 Specific Function |
Dephosphorylates the 5' and 2'(3')-phosphates of deoxyribonucleotides, with a preference for dUMP and dTMP, intermediate activity towards dGMP, and low activity towards dCMP and dAMP |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
7524492 |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q8TCD5 |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
NT5C_HUMAN |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>606 bp
ATGGCGCGGAGCGTGCGCGTGCTGGTGGACATGGACGGCGTCCTGGCCGACTTCGAGGCC
GGCCTCCTGCGGGGCTTCCGCCGCCGCTTCCCTGAGGAGCCGCACGTGCCGCTGGAGCAA
CGCCGCGGCTTCCTGGCCCGCGAGCAGTACCGCGCCCTGCGGCCCGACCTGGCGGATAAA
GTGGCCAGTGTGTACGAAGCCCCGGGCTTTTTCCTGGACCTGGAGCCCATCCCGGGAGCC
TTGGACGCTGTGCGGGAGATGAACGACCTACCGGACACGCAGGTCTTCATCTGCACCAGC
CCCCTGCTGAAGTACCACCACTGTGTGGGTGAGAAGTACCGCTGGGTGGAGCAGCACCTG
GGGCCCCAGTTCGTAGAACGAATTATCCTGACAAGGGACAAGACGGTGGTCTTGGGGGAC
CTGCTCATTGATGACAAGGACACAGTTCGAGGCCAGGAGGAGACCCCAAGCTGGGAGCAC
ATCTTGTTCACCTGCTGCCACAATCGGCACCTGGTCCTGCCCCCGACAAGGAGACGGCTG
CTCTCCTGGAGTGACAACTGGAGGGAGATCTTAGATAGCAAGCGCGGAGCTGCGCAGCGG
GAATGA
|
| Enzyme 4 GenBank Gene ID |
AF154829 |
| Enzyme 4 GeneCard ID |
NT5C |
| Enzyme 4 GenAtlas ID |
Not Available |
| Enzyme 4 HGNC ID |
Not Available |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
17q25.1 |
| Enzyme 4 SNPs |
SNPJam Report |
| Enzyme 4 General References |
- Rampazzo C, Johansson M, Gallinaro L, Ferraro P, Hellman U, Karlsson A, Reichard P, Bianchi V: Mammalian 5'(3')-deoxyribonucleotidase, cDNA cloning, and overexpression of the enzyme in Escherichia coli and mammalian cells. J Biol Chem. 2000 Feb 25;275(8):5409-15. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Rampazzo C, Kost-Alimova M, Ruzzenente B, Dumanski JP, Bianchi V: Mouse cytosolic and mitochondrial deoxyribonucleotidases: cDNA cloning of the mitochondrial enzyme, gene structures, chromosomal mapping and comparison with the human orthologs. Gene. 2002 Jul 10;294(1-2):109-17. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Wallden K, Rinaldo-Matthis A, Ruzzenente B, Rampazzo C, Bianchi V, Nordlund P: Crystal structures of human and murine deoxyribonucleotidases: insights into recognition of substrates and nucleotide analogues. Biochemistry. 2007 Dec 4;46(48):13809-18. Epub 2007 Nov 7. [PubMed ]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5236 |
| Enzyme 5 Name |
5'(3')-deoxyribonucleotidase, mitochondrial |
| Enzyme 5 Synonyms |
- 5',3'-nucleotidase, mitochondrial
- Deoxy-5'-nucleotidase 2
- dNT-2
|
| Enzyme 5 Gene Name |
NT5M |
| Enzyme 5 Protein Sequence |
>5'(3')-deoxyribonucleotidase, mitochondrial
MIRLGGWCARRLCSAAVPAGRRGAAGGLGLAGGRALRVLVDMDGVLADFEGGFLRKFRAR
FPDQPFIALEDRRGFWVSEQYGRLRPGLSEKAISIWESKNFFFELEPLPGAVEAVKEMAS
LQNTDVFICTSPIKMFKYCPYEKYAWVEKYFGPDFLEQIVLTRDKTVVSADLLIDDRPDI
TGAEPTPSWEHVLFTACHNQHLQLQPPRRRLHSWADDWKAILDSKRPC
|
| Enzyme 5 Number of Residues |
228 |
| Enzyme 5 Molecular Weight |
25861.5 |
| Enzyme 5 Theoretical pI |
8.12 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in phosphatase activity |
| Enzyme 5 Specific Function |
Dephosphorylates specifically the 5' and 2'(3')- phosphates of uracil and thymine deoxyribonucleotides, and so protects mitochondrial DNA replication from excess dTTP. Has only marginal activity towards dIMP and dGMP |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9NPB1 |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
NT5M_HUMAN |
| Enzyme 5 PDB ID |
1Q92 |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>687 bp
ATGATCCGGCTGGGCGGCTGGTGTGCGCGGCGGCTCTGCAGCGCGGCGGTTCCCGCGGGG
CGGCGCGGGGCGGCGGGCGGGCTGGGCCTGGCGGGAGGCCGCGCCCTACGGGTGCTGGTG
GACATGGACGGCGTGCTGGCTGACTTCGAGGGCGGATTCCTCAGGAAGTTCCGCGCGCGC
TTTCCCGACCAGCCCTTCATCGCGCTGGAGGACCGGCGCGGCTTCTGGGTGTCGGAGCAG
TACGGCCGCCTGCGGCCAGGGCTGAGCGAGAAGGCCATCAGCATTTGGGAGTCAAAGAAT
TTCTTTTTTGAACTTGAGCCTCTGCCAGGGGCCGTGGAAGCTGTCAAGGAGATGGCCAGC
CTACAAAACACTGACGTCTTCATCTGCACAAGCCCCATCAAGATGTTCAAGTACTGTCCC
TATGAGAAGTATGCCTGGGTGGAGAAGTACTTTGGCCCTGACTTTCTGGAGCAGATTGTG
CTGACCAGAGACAAGACCGTGGTCTCTGCTGACCTTCTCATAGACGACCGGCCGGACATC
ACAGGGGCCGAGCCAACCCCCAGCTGGGAGCATGTCCTCTTCACCGCCTGCCACAACCAG
CACCTGCAGCTGCAGCCCCCCCGCCGCAGGCTGCACTCGTGGGCGGACGACTGGAAGGCC
ATTCTGGACAGCAAGCGGCCCTGCTGA
|
| Enzyme 5 GenBank Gene ID |
AF210652 |
| Enzyme 5 GeneCard ID |
NT5M |
| Enzyme 5 GenAtlas ID |
NT5M |
| Enzyme 5 HGNC ID |
HGNC:15769 |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
17p11.2 |
| Enzyme 5 SNPs |
SNPJam Report |
| Enzyme 5 General References |
- Rampazzo C, Gallinaro L, Milanesi E, Frigimelica E, Reichard P, Bianchi V: A deoxyribonucleotidase in mitochondria: involvement in regulation of dNTP pools and possible link to genetic disease. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8239-44. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Rinaldo-Matthis A, Rampazzo C, Reichard P, Bianchi V, Nordlund P: Crystal structure of a human mitochondrial deoxyribonucleotidase. Nat Struct Biol. 2002 Oct;9(10):779-87. [PubMed ]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5253 |
| Enzyme 6 Name |
Acyl-coenzyme A thioesterase 12 |
| Enzyme 6 Synonyms |
- Acyl-CoA thioesterase 12
- Acyl-CoA thioester hydrolase 12
- Cytoplasmic acetyl-CoA hydrolase 1
- CACH-1
- hCACH-1
- START domain-containing protein 15
- StARD15
|
| Enzyme 6 Gene Name |
ACOT12 |
| Enzyme 6 Protein Sequence |
>Acyl-coenzyme A thioesterase 12
MERPAPGEVVMSQAIQPAHATARGELSAGQLLKWIDTTACLAAEKHAGVSCVTASVDDIQ
FEETARVGQVITIKAKVTRAFSTSMEISIKVMVQDMLTGIEKLVSVAFSTFVAKPVGKEK
IHLKPVTLLTEQDHVEHNLAAERRKVRLQHEDTFNNLMKESSKFDDLIFDEEEGAVSTRG
TSVQSIELVLPPHANHHGNTFGGQIMAWMETVATISASRLCWAHPFLKSVDMFKFRGPST
VGDRLVFTAIVNNTFQTCVEVGVRVEAFDCQEWAEGRGRHINSAFLIYNAADDKENLITF
PRIQPISKDDFRRYRGAIARKRIRLGRKYVISHKEEVPLCIHWDISKQASLSDSNVEALK
KLAAKRGWEVTSTVEKIKIYTLEEHDVLSVWVEKHVGSPAHLAYRLLSDFTKRPLWDPHF
VSCEVIDWVSEDDQLYHITCPILNDDKPKDLVVLVSRRKPLKDGNTYTVAVKSVILPSVP
PSPQYIRSEIICAGFLIHAIDSNSCIVSYFNHMSASILPYFAGNLGGWSKSIEETAASCI
QFLENPPDDGFVSTF
|
| Enzyme 6 Number of Residues |
555 |
| Enzyme 6 Molecular Weight |
62033.5 |
| Enzyme 6 Theoretical pI |
6.76 |
| Enzyme 6 GO Classification |
Not Available |
| Enzyme 6 General Function |
Lipid transport and metabolism |
| Enzyme 6 Specific Function |
Hydrolyzes acetyl-CoA to acetate and CoA |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- acetyl-CoA + H2O = CoA + acetate [RN:R00227]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
18307694 |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q8WYK0 |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
ACO12_HUMAN |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1668 bp
ATGGAGCGGCCGGCGCCCGGCGAGGTGGTCATGAGCCAAGCCATCCAGCCGGCGCACGCC
ACTGCGCGCGGCGAGCTGAGCGCGGGGCAGCTGCTCAAGTGGATCGACACCACCGCCTGC
CTGGCGGCTGAGAAACATGCTGGAGTTTCCTGCGTTACAGCCTCAGTGGATGACATACAG
TTTGAGGAGACAGCTAGAGTTGGACAAGTTATAACCATCAAAGCAAAAGTTACTAGAGCA
TTCAGCACAAGCATGGAGATCAGTATCAAGGTCATGGTACAGGATATGCTCACTGGCATT
GAGAAGCTTGTTAGTGTGGCTTTCTCCACATTTGTAGCCAAACCAGTTGGAAAAGAAAAG
ATTCATTTAAAACCAGTCACACTTCTAACTGAACAAGATCATGTGGAACATAATCTGGCT
GCTGAGAGAAGGAAAGTTCGATTACAACATGAAGATACCTTTAACAATTTAATGAAGGAA
AGTAGCAAATTTGATGATCTCATTTTTGATGAAGAGGAAGGAGCGGTTTCCACAAGGGGC
ACCTCCGTTCAGAGCATTGAACTGGTCCTCCCACCCCATGCAAACCATCACGGAAATACA
TTTGGTGGCCAGATTATGGCGTGGATGGAGACAGTGGCTACTATTTCTGCAAGCCGCCTG
TGTTGGGCTCATCCCTTTCTGAAGTCCGTAGATATGTTTAAGTTCCGGGGACCATCTACA
GTTGGAGATCGTCTTGTCTTCACTGCCATTGTCAACAATACATTTCAGACCTGTGTTGAA
GTTGGAGTTCGCGTGGAGGCCTTTGACTGTCAGGAATGGGCCGAGGGCCGAGGGCGTCAC
ATCAACAGTGCTTTTCTCATTTACAATGCTGCTGATGATAAGGAAAATCTCATCACGTTT
CCCAGAATCCAACCCATTTCAAAGGATGATTTCAGACGCTATCGGGGAGCTATTGCACGC
AAGCGAATTCGCCTAGGCAGAAAATATGTTATTTCCCACAAAGAAGAGGTTCCACTTTGC
ATACACTGGGATATCAGCAAGCAGGCATCCCTGAGTGACAGCAATGTGGAGGCCCTCAAA
AAACTGGCAGCCAAAAGGGGTTGGGAGGTTACCAGCACTGTGGAAAAGATAAAAATATAT
ACTCTGGAAGAGCATGATGTTTTATCTGTTTGGGTTGAAAAGCACGTGGGAAGTCCAGCA
CATTTGGCTTATCGTCTCTTGTCTGACTTTACAAAGCGACCTTTGTGGGACCCCCATTTT
GTGTCCTGTGAAGTCATAGACTGGGTGAGTGAAGATGATCAGCTGTATCACATCACCTGT
CCTATACTGAATGATGACAAACCCAAAGACTTGGTAGTACTCGTATCACGAAGAAAACCC
CTCAAAGATGGTAACACTTACACAGTGGCAGTGAAGTCGGTCATTTTGCCATCGGTCCCC
CCGTCTCCACAGTACATCAGAAGTGAAATCATATGTGCCGGATTTCTCATCCATGCTATT
GACAGCAATTCATGCATCGTATCTTACTTTAACCATATGTCTGCTAGCATCCTTCCTTAC
TTTGCTGGAAATCTTGGTGGCTGGTCAAAATCCATTGAAGAAACAGCAGCCTCTTGTATA
CAGTTCTTAGAGAATCCTCCTGATGATGGGTTTGTAAGCACATTTTAA
|
| Enzyme 6 GenBank Gene ID |
AB078619 |
| Enzyme 6 GeneCard ID |
ACOT12 |
| Enzyme 6 GenAtlas ID |
ACOT12 |
| Enzyme 6 HGNC ID |
HGNC:24436 |
| Enzyme 6 Chromosome Location |
5 |
| Enzyme 6 Locus |
5q14.1 |
| Enzyme 6 SNPs |
SNPJam Report |
| Enzyme 6 General References |
- Suematsu N, Isohashi F: Molecular cloning and functional expression of human cytosolic acetyl-CoA hydrolase. Acta Biochim Pol. 2006;53(3):553-61. Epub 2006 Sep 2. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5264 |
| Enzyme 7 Name |
Fatty acid synthase |
| Enzyme 7 Synonyms |
- [Acyl-carrier-protein] S-acetyltransferase
- [Acyl-carrier-protein] S-malonyltransferase
- 3-oxoacyl-[acyl-carrier-protein] synthase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
- Enoyl-[acyl-carrier-protein] reductase
- Oleoyl-[acyl-carrier-protein] hydrolase
|
| Enzyme 7 Gene Name |
FASN |
| Enzyme 7 Protein Sequence |
>Fatty acid synthase
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
|
| Enzyme 7 Number of Residues |
2511 |
| Enzyme 7 Molecular Weight |
273424.1 |
| Enzyme 7 Theoretical pI |
6.41 |
| Enzyme 7 GO Classification |
| Function |
- acyl carrier activity
- amino acid binding
- binding
- carboxylic acid binding
- catalytic activity
- cation binding
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- oxidoreductase activity
- phosphopantetheine binding
- substrate-specific transporter activity
- transferase activity
- transition metal ion binding
- transporter activity
- zinc ion binding
|
| Process |
- biosynthetic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in transferase activity |
| Enzyme 7 Specific Function |
Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- a (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = a hexadec-2-enoyl-[acyl-carrier protein] + H2O [RN:R04462]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
41872631 |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
P49327 |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
FAS_HUMAN |
| Enzyme 7 PDB ID |
1XKT |
| Enzyme 7 PDB File |
Show |
| Enzyme 7 3D Structure |
|
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>7536 bp
ATGGAGGAGGTGGTGATTGCCGGCATGTCCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCGGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGTCACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAATGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCCGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
CGGGTGTACGCCACCATCCTGAACGCCGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCCTCAGGGGATATCCAGGAGCAGCTCATCCGCTCGTTGTACCAGTCGGCC
GGAGTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGCACAGGCACCAAGGTGGGC
GACCCCCAGGAGCTGAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTG
CTCATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTGGCAGCC
CTGGCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCAT
AGCCCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCC
CTGCCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACGTG
CACATCATCCTGAGGCCCAACACGCAGCCGCCCCCCGCACCCGCCCCACATGCCACCCTG
CCCCGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAG
GGCCTCCGGCACAGCCAGGACCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTC
CCCGCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGCGCGGTGGCCCA
GAGGTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGC
ACACAGTGGCGCGGGATGGGGCTGAGCCTCATGCGCCTGGACCGCTTCCGAGATTCCATC
CTACGCTCCGATGAGGCTGTGAAGCCATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGC
ACAGACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAG
ATAGGCCTCATAGACCTGCTGAGCTGCATGGGGCTGAGGCCAGATGGCATCGTCGGCCAC
TCCCTGGGGGAGGTGGCCTGTGGCTACGCCGACGGCTGCCTGTCCCAGGAGGAGGCCGTC
CTCGCTGCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCATCTCCCGCCGGGCGCCATG
GCAGCCGTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCGGGCGTGGTGCCC
GCCTGCCACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAG
TTCGTGGAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATG
GCCTTCCACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAG
GTGATCCGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCC
CAGTGGCACAGCAGCCTGGCACGCACGTCCTCCGCCGAGTACAATGTCAACAACCTGGTG
AGCCCTGTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAG
ATCGCGCCCCACGCCCTGCTGCAGGCTGTCCTGAAGCGTGGCCTGAAGCCGAGCTGCACC
ATCATCCCCCTGATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATC
GGCAGGCTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAG
TTCCCAGCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTG
GCCTGGGACGTGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCGCC
ATCTACAACATCGACACCAGCTCCGAGTCTCCTGACCACTACCTGGTGGACCACACCCTC
GACGGTCGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCC
CGCGCCCTGGGCCTGGGCGTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCTGCAC
CAGGCCACCATCCTGCCCAAGACTGGGACAGTGTCCCTGGAGGTACGGCTCCTGGAGGCC
TCCCGTGCCTTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAG
TGGGATGACCCTGACCCCAGGCTCTTCGACCACCCGGAAAGCCCCACCCCCAACCCCACG
GAGCCCCTCTTCCTGGCCCAGGCTGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGAC
TACGGCCCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTG
CTGTGGAAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGC
TCGGCCAAGCACGGCCTGTACCTGCCCACCCGTGTCACCGCCATCCACATCGACCCTGCC
ACCCACAGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTG
AGCAGGTGGCTGAGGGTCACAGTGGCCGGAGGCGTCCACATCTCCGGGCTCCACACTGAG
TCGGCCCCGCGGCGGCAGCAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACT
CCCCACACGGAGGAGGGGTGCCTGTCTGAGCGCGCTGCCCTGCAGGAGGAGCTGCAACTG
TGCAAGGGGCTGGTGCAGGCACTGCAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTG
GTGCCCGGACTGGATGGGGCCCAGATCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGG
CTGTTGTCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAG
GTGCTGGCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGAC
TCCCCGGCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATG
AAGGTGGTGGAGGTGCTGGCTGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTC
AGCCCCCATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTG
GAGGCTGCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCA
GACCCTGCCCCCAGCGCCCTGGGCAGCGCCGACCTCCTGGTGTGCAACTGTGCTGTGGCT
GCCCTCGGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGC
TTTCTGCTCCTGCACACACTGCTCCGGGGGCACCCCCTCGGGGACATCGTGGCCTTCCTC
ACCTCCACTGAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTC
TTCTCCAGGGTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCTCCACGCTC
TTCCTGTGCCGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACC
AGCTTCCGCTGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCT
GTGTGGCTGAAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTC
CGCCGAGAGCCCGGCGGGAACCGCCTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACC
TCCCACGTCCCGGAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGAC
CTGGTGATGAACGTCTACCGCGACGGGGCCTGGGGGGCTTTCCGCCACTTCCTGCTGGAG
GAGGACAAGCCTGAGGAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGAC
CTGTCCTCCATCCGCTGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGC
GCCCAGCTCTGCACGGTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACT
GGCAAGCTGTCCCCTGATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGT
ATGGAGTTCTCGGGCCGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAG
GGCCTGGCCACCTCTGTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGG
ACGCTGGAGGAGGCGGCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTG
GTGCGTGGGCGGGTGCGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTG
GGCCAGGCCGCCATCGCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGG
TCGGCTGAGAAGCGGGCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTC
GCCAACTCCCGGGACACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGC
GTTGACCTGGTCTTGAACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTG
GCTACGCACGGTCGCTTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTC
GGCATGGCTATCTTCCTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTC
AACGAGAGCAGTGCTGACTGGCGGGAGGTGTGGGCGCTTGTGCAGGCCGGCATCCGGGAT
GGGGTGGTACGGCCCCTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTC
CGCTACATGGCCCAAGGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAG
CCGGAGGCAGTGCTGAAGGGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTC
TGCCCGGCCCACAAGAGCTACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTG
GCGCAGTGGCTGATACAGCGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATC
CGGACAGGCTACCAGGCCAAGCAGGTCCGCCGGTGGAGGCGCCAGGGCGTACAGGTGCAG
GTGTCCACCAGCAACATCAGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCG
CAGCTTGGGCCCGTGGGCGGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTG
GAGAACCAGACCCCAGAGTTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTG
AACCTGGACAGGGTGACCCGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCC
TCTGTGAGCTGCGGGCGTGGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCC
ATGGAGCGTATCTGTGAGAAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGG
GGCGCCATCGGCGACGTGGGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTC
AGTGGCACGCTGCCCCAGCGCATGGCGTCCTGCCTGGAGGTGCTGGACCTCTTCCTGAAC
CAGCCCCACATGGTCCTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGAC
AGGGACAGCCAGCGGGACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTG
GCTGCTGTCAACCTGGACAGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGTG
GAGGTGCGCCAGACGCTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGG
CAACTCACGCTCCGGAAACTGCAGGAGCTGTCCTCAAAGGCGGATGAGGCCAGCGAGCTG
GCATGCCCCACGCCCAAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGC
TCCCTGCTGGTGAACCCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCG
GAGCGGCCCCTGTTCCTGGTGCACCCAATCGAGGGCTCCACCACCGTGTTCCACAGCCTG
GCCTCCCGGCTCAGCATCCCCACCTATGGCCTGCAGTGCACCCGAGCTGCGCCCCTTGAC
AGCATCCACAGCCTGGCTGCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGC
CCCTACCGCGTGGCCGGCTACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAG
CTGCAGGCCCAGCAGAGCCCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCG
CCCACCTACGTACTGGCCTACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTGAG
GCTGAGGCTGAGACGGAGGCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCAC
AACAGGGTGCTGGAGGCGCTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCC
GTGGACCTGATCATCAAGAGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCC
CGGTCCTTCTACTACAAGCTGCGTGCCGCTGAGCAGTACACACCCAAGGCCAAGTACCAT
GGCAACGTGATGCTACTGCGCGCCAAGACGGGTGGCGCCTACGGCGAGGACCTGGGCGCG
GACTACAACCTCTCCCAGGTATGCGACGGGAAAGTATCCGTCCACGTCATCGAGGGTGAC
CACCGCACGCTGCTGGAGGGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCC
CTGGCTGAGCCACGCGTGAGCGTGCGGGAGGGCTAG
|
| Enzyme 7 GenBank Gene ID |
NM_004104.4 |
| Enzyme 7 GeneCard ID |
FASN |
| Enzyme 7 GenAtlas ID |
FASN |
| Enzyme 7 HGNC ID |
HGNC:3594 |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
17q25 |
| Enzyme 7 SNPs |
SNPJam Report |
| Enzyme 7 General References |
- Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed ]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed ]
- Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed ]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Brink J, Ludtke SJ, Yang CY, Gu ZW, Wakil SJ, Chiu W: Quaternary structure of human fatty acid synthase by electron cryomicroscopy. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):138-43. Epub 2001 Dec 26. [PubMed ]
- Chakravarty B, Gu Z, Chirala SS, Wakil SJ, Quiocho FA: Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15567-72. Epub 2004 Oct 26. [PubMed ]
- Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U: Mechanism and substrate recognition of human holo ACP synthase. Chem Biol. 2007 Nov;14(11):1243-53. [PubMed ]
- Pemble CW 4th, Johnson LC, Kridel SJ, Lowther WT: Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nat Struct Mol Biol. 2007 Aug;14(8):704-9. Epub 2007 Jul 8. [PubMed ]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5269 |
| Enzyme 8 Name |
Hydroxymethylglutaryl-CoA synthase, mitochondrial |
| Enzyme 8 Synonyms |
- HMG-CoA synthase
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
|
| Enzyme 8 Gene Name |
HMGCS2 |
| Enzyme 8 Protein Sequence |
>Hydroxymethylglutaryl-CoA synthase, mitochondrial
MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALE
VYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLP
WDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWM
ESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYD
FYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIF
HTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKAS
QDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASF
FSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPG
DTNSLFPGTWYLERVDEQHRRKYARRPV
|
| Enzyme 8 Number of Residues |
508 |
| Enzyme 8 Molecular Weight |
56634.9 |
| Enzyme 8 Theoretical pI |
8.28 |
| Enzyme 8 GO Classification |
| Function |
- catalytic activity
- hydroxymethylglutaryl-CoA synthase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- cellular lipid metabolic process
- isoprenoid biosynthetic process
- isoprenoid metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in hydroxymethylglutaryl-CoA synthase activity |
| Enzyme 8 Specific Function |
This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase |
| Enzyme 8 Pathways |
- Butyrate Metabolism (map00650 )
- Synthesis and Degradation of Ketone Bodies (map00072 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 8 Reactions |
- acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA [RN:R01978]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
56205097 |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P54868 |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
HMCS2_HUMAN |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1527 bp
ATGCAGCGTCTGTTGACTCCAGTGAAGCGCATTCTGCAACTGACAAGAGCGGTGCAGGAA
ACCTCCCTCACACCTGCTCGCCTGCTCCCAGTAGCCCACCAAAGGTTTTCTACAGCCTCT
GCTGTCCCCCTGGCCAAAACAGATACTTGGCCAAAGGACGTGGGCATCCTGGCCCTGGAG
GTCTACTTCCCAGCCCAATATGTGGACCAAACTGACCTGGAGAAGTATAACAATGTGGAA
GCAGGAAAGTATACAGTGGGCTTGGGCCAGACCCGTATGGGCTTCTGCTCAGTCCAAGAG
GACATCAACTCCCTGTGCCTGACGGTGGTGCAACGGCTGATGGAGCGCATACAGCTCCCA
TGGGACTCTGTGGGCAGGCTGGAAGTAGGCACTGAGACCATCATTGACAAGTCCAAAGCT
GTCAAAACAGTGCTCATGGAACTCTTCCAGGATTCAGGCAATACTGATATTGAGGGCATA
GATACCACCAATGCCTGCTACGGTGGTACTGCCTCCCTCTTCAATGCTGCCAACTGGATG
GAGTCCAGTTCCTGGGATGGTCGTTATGCCATGGTGGTCTGTGGAGACATTGCCGTCTAT
CCCAGTGGTAATGCTCGTCCCACAGGTGGGGCCGGAGCTGTGGCTATGCTGATTGGGCCC
AAGGCCCCTCTGGCCCTGGAGCGAGGGCTGAGGGGAACCCATATGGAGAATGTGTATGAC
TTCTACAAACCAAATTTGGCCTCGGAGTACCCAATAGTGGATGGGAAGCTTTCCATCCAG
TGCTACTTGCGGGCCTTGGATCGATGTTACACATCATACCGTAAAAAAATCCAGAATCAG
TGGAAGCAAGCTGGCAGCGATCGACCCTTCACCCTTGACGATTTACAGTACATGATCTTT
CATACACCCTTTTGCAAGATGGTCCAGAAGTCTCTGGCTCGCCTGATGTTCAATGACTTC
CTGTCAGCCAGCAGTGACACACAAACCAGCTTATATAAGGGGCTGGAGGCTTTCGGGGGG
CTAAAGCTGGAAGACACCTACACCAACAAGGACCTGGATAAAGCACTTCTAAAGGCCTCT
CAGGACATGTTCGACAAGAAAACCAAGGCTTCCCTTTACCTCTCCACTCACAATGGGAAC
ATGTACACCTCATCCCTGTACGGGTGCCTGGCCTCGCTTCTGTCCCACCACTCTGCCCAA
GAACTGGCTGGCTCCAGGATTGGTGCCTTCTCTTATGGCTCTGGTTTAGCAGCAAGTTTC
TTTTCATTTCGAGTATCCCAGGATGCTGCTCCAGGCTCTCCCCTGGACAAGTTGGTGTCC
AGCACATCAGACCTGCCAAAACGCCTAGCCTCCCGAAAGTGTGTGTCTCCTGAGGAGTTC
ACAGAAATAATGAACCAAAGAGAGCAATTCTACCATAAGGTGAATTTCTCCCCACCTGGT
GACACAAACAGCCTTTTCCCAGGTACTTGGTACCTGGAGCGAGTGGACGAGCAGCATCGC
CGAAAGTATGCCCGGCGTCCCGTCTAA
|
| Enzyme 8 GenBank Gene ID |
AL589734 |
| Enzyme 8 GeneCard ID |
HMGCS2 |
| Enzyme 8 GenAtlas ID |
HMGCS2 |
| Enzyme 8 HGNC ID |
HGNC:5008 |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1p13-p12 |
| Enzyme 8 SNPs |
SNPJam Report |
| Enzyme 8 General References |
- Mascaro C, Buesa C, Ortiz JA, Haro D, Hegardt FG: Molecular cloning and tissue expression of human mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase. Arch Biochem Biophys. 1995 Mar 10;317(2):385-90. [PubMed ]
- Boukaftane Y, Mitchell GA: Cloning and characterization of the human mitochondrial 3-hydroxy-3-methylglutaryl CoA synthase gene. Gene. 1997 Aug 22;195(2):121-6. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Boukaftane Y, Duncan A, Wang S, Labuda D, Robert MF, Sarrazin J, Schappert K, Mitchell GA: Human mitochondrial HMG CoA synthase: liver cDNA and partial genomic cloning, chromosome mapping to 1p12-p13, and possible role in vertebrate evolution. Genomics. 1994 Oct;23(3):552-9. [PubMed ]
- Camarero N, Mascaro C, Mayordomo C, Vilardell F, Haro D, Marrero PF: Ketogenic HMGCS2 Is a c-Myc target gene expressed in differentiated cells of human colonic epithelium and down-regulated in colon cancer. Mol Cancer Res. 2006 Sep;4(9):645-53. Epub 2006 Aug 28. [PubMed ]
- Aledo R, Zschocke J, Pie J, Mir C, Fiesel S, Mayatepek E, Hoffmann GF, Casals N, Hegardt FG: Genetic basis of mitochondrial HMG-CoA synthase deficiency. Hum Genet. 2001 Jul;109(1):19-23. [PubMed ]
- Bouchard L, Robert MF, Vinarov D, Stanley CA, Thompson GN, Morris A, Leonard JV, Quant P, Hsu BY, Boneh A, Boukaftane Y, Ashmarina L, Wang S, Miziorko H, Mitchell GA: Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase deficiency: clinical course and description of causal mutations in two patients. Pediatr Res. 2001 Mar;49(3):326-31. [PubMed ]
- Wolf NI, Rahman S, Clayton PT, Zschocke J: Mitochondrial HMG-CoA synthase deficiency: identification of two further patients carrying two novel mutations. Eur J Pediatr. 2003 Apr;162(4):279-80. Epub 2003 Feb 11. [PubMed ]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5272 |
| Enzyme 9 Name |
Citrate synthase, mitochondrial |
| Enzyme 9 Synonyms |
Not Available |
| Enzyme 9 Gene Name |
CS |
| Enzyme 9 Protein Sequence |
>Citrate synthase, mitochondrial
MALLTAAARLLGTKNASCLVLAARHASASSTNLKDILADLIPKEQARIKTFRQQHGKTVV
GQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGFSIPECQKLLPKAKGGEEPLPEGLF
WLLVTGHIPTEEQVSWLSKEWAKRAALPSHVVTMLDNFPTNLHPMSQLSAAVTALNSESN
FARAYAQGISRTKYWELIYEDSMDLIAKLPCVAAKIYRNLYREGSGIGAIDSNLDWSHNF
TNMLGYTDHQFTELTRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAAMNGLAGPL
HGLANQEVLVWLTQLQKEVGKDVSDEKLRDYIWNTLNSGRVVPGYGHAVLRKTDPRYTCQ
REFALKHLPNDPMFKLVAQLYKIVPNVLLEQGKAKNPWPNVDAHSGVLLQYYGMTEMNYY
TVLFGVSRALGVLAQLIWSRALGFPLERPKSMSTEGLMKFVDSKSG
|
| Enzyme 9 Number of Residues |
466 |
| Enzyme 9 Molecular Weight |
51712.0 |
| Enzyme 9 Theoretical pI |
8.53 |
| Enzyme 9 GO Classification |
| Function |
- catalytic activity
- citrate (Si)-synthase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- acetyl-CoA catabolic process
- acetyl-CoA metabolic process
- carbohydrate metabolic process
- cellular carbohydrate metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
- primary metabolic process
- tricarboxylic acid cycle
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer |
| Enzyme 9 Specific Function |
Acetyl-CoA + H(2)O + oxaloacetate = citrate + CoA |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- acetyl-CoA + H2O + oxaloacetate = citrate + CoA [RN:R00351]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
3288815 |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
O75390 |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
CISY_HUMAN |
| Enzyme 9 PDB ID |
4CTS |
| Enzyme 9 PDB File |
Show |
| Enzyme 9 3D Structure |
|
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1401 bp
ATGGCTTTACTTACTGCGGCCGCCCGGCTCTTGGGAACCAAGAATGCATCTTGTCTTGTT
CTTGCAGCCCGGCATGCTAGTGCTTCCTCCACGAATTTGAAAGACATATTGGCTGACCTG
ATACCTAAGGAGCAGGCCAGAATTAAGACTTTCAGGCAGCAACATGGCAAGACGGTGGTG
GGCCAAATCACTGTGGACATGATGTATGGTGGCATGAGAGGCATGAAGGGATTGGTGTAT
GAAACATCAGTTCTTGATCCTGATGAGGGCATCCGTTTCCGAGGCTTTAGTATCCCTGAA
TGCCAGAAACTGCTACCCAAGGCTAAGGGTGGGGAAGAACCCCTGCCTGAGGGCTTATTT
TGGCTGCTGGTAACTGGATGTATCCCAACAGAGGAACAGGTATCTTGGCTCTCAAAAGAG
TGGGCAAAGAGGGCAGCTCTGCCTTCCCATGTGGTCACCATGCTGGACAACTTTCCCACC
AATCTACACCCCATGTCTCAGCTGAGTGCAGCTGTTACAGCCCTCAACAGTGAAAGTAAC
TTTGCCCAAGCATATGCACGGGGTATCAGCCGAACCAAGTACTGGGAGTTGATTTATGAA
GATTCTGTGGATCTAATAGCAAAGCTACCTTGTGTTGCAGCAAAGATCTACCGAAATCTC
TACTGGGAAGGCAGCGGTATTGGGGCCATTGACTCTAACCTGGACTGGTCTCACAATTTC
ACCAACATGTTAGGCTATACTGATCATCAGTTCACTGAGCTCATGCGCCTGTACCTCACC
ATCCACAGTGACCATGAGGGTGGCAATGTAAGTGCCCATACCAGCCACTTGGTGGGCAGT
GCCCTTTCCGACCCTTACCTGTCCTTTGCAGCAGCCATGAACGGGCTGGCAGGGCCTCTC
CATGGACTGGCAAATCAGGAAGTGCTTGTCTGGCTAACACAGCTGCAGAAGGAAGTTGGC
AAAGATGTGTCAGATGAGAAGTTACGAGACTACATCTGGAACACACTCAACTCAGGACGG
GTTGTTCCAGGCTATGGCCATGCAGTACTAAGGAAGACTGATCCGCGATATACCTGTCAG
CGAGAGTTTGCTCTGAAACACCTGCCTAATGACCCCATGTTTAAGTTGGTTGCTCAGCTG
TACAAGATTGTGCCCAATGTCCTCTTAGAGCAGGGTAAAGCCAAGAATCCTTGGCCCAAT
GTAGATGCTCACAGTGGGGTGCTGCTCCAGTATTATGGCATGACGGAGATGAATTACTAC
ACGGTCCTGTTTGGGGTGTCACGAGCATTGGGTGTACTGGCACAGCTCATCTGGAGCCGA
GCCTTAGGCTTCCCTCTAGAAAGGCCCAAGTCCATGAGCACAGAGGGTCTGATGAAGTTT
GTGGACTCTAAGTCAGGGTAA
|
| Enzyme 9 GenBank Gene ID |
AF047042 |
| Enzyme 9 GeneCard ID |
CS |
| Enzyme 9 GenAtlas ID |
CS |
| Enzyme 9 HGNC ID |
HGNC:2422 |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
12q13.2 |
| Enzyme 9 SNPs |
SNPJam Report |
| Enzyme 9 General References |
- Goldenthal MJ, Marin-Garcia J, Ananthakrishnan R: Cloning and molecular analysis of the human citrate synthase gene. Genome. 1998 Oct;41(5):733-8. [PubMed ]
- Liu Q, Yu L, Han XF, Fu Q, Zhang JX, Tang H, Zhao SY: [Cloning and tissue expression pattern analysis of the human citrate synthase cDNA] Shi Yan Sheng Wu Xue Bao. 2000 Sep;33(3):207-14. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5282 |
| Enzyme 10 Name |
Hydroxymethylglutaryl-CoA synthase, cytoplasmic |
| Enzyme 10 Synonyms |
- HMG-CoA synthase
- 3-hydroxy-3-methylglutaryl coenzyme A synthase
|
| Enzyme 10 Gene Name |
HMGCS1 |
| Enzyme 10 Protein Sequence |
>Hydroxymethylglutaryl-CoA synthase, cytoplasmic
MPGSLPLNAEACWPKDVGIVALEIYFPSQYVDQAELEKYDGVDAGKYTIGLGQAKMGFCT
DREDINSLCMTVVQNLMERNNLSYDCIGRLEVGTETIIDKSKSVKTNLMQLFEESGNTDI
EGIDTTNACYGGTAAVFNAVNWIESSSWDGRYALVVAGDIAVYATGNARPTGGVGAVALL
IGPNAPLIFERGLRGTHMQHAYDFYKPDMLSEYPIVDGKLSIQCYLSALDRCYSVYCKKI
HAQWQKEGNDKDFTLNDFGFMIFHSPYCKLVQKSLARMLLNDFLNDQNRDKNSIYSGLEA
FGDVKLEDTYFDRDVEKAFMKASSELFSQKTKASLLVSNQNGNMYTSSVYGSLASVLAQY
SPQQLAGKRIGVFSYGSGLAATLYSLKVTQDATPGSALDKITASLCDLKSRLDSRTGVAP
DVFAENMKLREDTHHLVNYIPQGSIDSLFEGTWYLVRVDEKHRRTYARRPTPNDDTLDEG
VGLVHSNIATEHIPSPAKKVPRLPATAAEPEAAVISNGEH
|
| Enzyme 10 Number of Residues |
520 |
| Enzyme 10 Molecular Weight |
57293.1 |
| Enzyme 10 Theoretical pI |
5.05 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- hydroxymethylglutaryl-CoA synthase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups, acyl groups converted into alkyl on transfer
|
| Process |
- cellular lipid metabolic process
- isoprenoid biosynthetic process
- isoprenoid metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in hydroxymethylglutaryl-CoA synthase activity |
| Enzyme 10 Specific Function |
This enzyme condenses acetyl-CoA with acetoacetyl-CoA to form HMG-CoA, which is the substrate for HMG-CoA reductase |
| Enzyme 10 Pathways |
- Butyrate Metabolism (map00650 )
- Synthesis and Degradation of Ketone Bodies (map00072 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
|
| Enzyme 10 Reactions |
- acetyl-CoA + H2O + acetoacetyl-CoA = (S)-3-hydroxy-3-methylglutaryl-CoA + CoA [RN:R01978]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
30009 |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q01581 |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
HMCS1_HUMAN |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1563 bp
ATGCCTGGATCACTTCCTTTGAATGCAGAAGCTTGCTGGCCAAAAGATGTGGGAATTGTT
GCCCTTGAGATCTATTTTCCTTCTCAATATGTTGATCAAGCAGAGTTGGAAAAATATGAT
GGTGTAGATGCTGGAAAGTATACCATTGGCTTGGGCCAGGCCAAGATGGGCTTCTGCACA
GATAGAGAAGATATTAACTCTCTTTGCATGACTGTGGTTCAGAATCTTATGGAGAGAAAT
AACCTTTCCTATGATTGCATTGGGCGGCTGGAAGTTGGAACAGAGACAATCATCGACAAA
TCAAAGTCTGTGAAGACTAATTTGATGCAGCTGTTTGAAGAGTCTGGGAATACAGATATA
GAAGGAATCGACACAACTAATGCATGCTATGGAGGCACAGCTGCTGTCTTCAATGCTGTT
AACTGGATTGAGTCCAGCTCTTGGGATGGACGGTATGCCCTGGTAGTTGCAGGAGATATT
GCTGTATATGCCACAGGAAATGCTAGACCTACAGGTGGAGTTGGAGCAGTAGCTCTGCTA
ATTGGGCCAAATGCTCCTTTAATTTTTGAACGAGGGCTTCGTGGGACACATATGCAACAT
GCCTATGATTTTTACAAGCCTGATATGCTATCTGAATATCCTATAGTAGATGGAAAACTC
TCCATACAGTGCTACCTCAGTGCATTAGACCGCTGCTATTCTGTCTACTGCAAAAAGATC
CATGCCCAGTGGCAGAAAGAGGCAAATGATAACGATTTTACCTTGAATGATTTTGGCTTC
ATGATCTTTCACTCACCATATTGTAAACTGGTTCAGAAATCTCTAGCTCGGATGTTGCTG
AATGACTTCCTTAATGACCAGAATAGAGATAAAAATAGTATCTATAGTGGCCTGAAGGCC
TTTGGGGATGTTAAGTTAGAAGACACCTACTTTGATAGAGATGTGGAGAAGGCATTTATG
AAGGCTAGCTCTGAACTCTTCAGTCAGAAAACAAAGGCATCTTTACTTGTATCAAATCAA
AATGGAAATATGTACACATCTTCAGTATATGGTTCCCTTGCATCTGTTCTAGCACAGTAC
TCACCTCAGCATTTAGCAGGGAAGAGAATTGGAGTGTTTTCTTATGGTTCTGGTTTGGCT
GCCACTCTGTACTCTCTTAAAGTCACACAAGATGCTACACCGGGGTCTGCTCTTGATAAA
ATAACAGCAAGTTTATGTGATCTTAAATCAAGGCTTGATTCAAGAACTGGTGTGGCACAA
GATGTCTTCGCTGAAAACATGAAGCTCAGAGAGGACACCCATCATTTGGTCAACTATATT
CCCCAGGGTTCAATAGATTCACTCTTTGAAGGAACGTGGTACTTAGTTAGGGTGGATGAA
AAGCACAGAAGAACTTACGCTCGGCGTCCCACTCCAAATGATGACACTTTGGATGAAGGA
GTAGGACTTGTGCATTCAAACATAGCAACTGAGCATATTCCAAGCCCTGCCAAGAAAGTA
CCAAGACTCCCTGCTACAGCAGCAGAACCTGAAGCAGCAGTTATTAGTAATGGGGTATGG
TAA
|
| Enzyme 10 GenBank Gene ID |
X66435 |
| Enzyme 10 GeneCard ID |
HMGCS1 |
| Enzyme 10 GenAtlas ID |
HMGCS1 |
| Enzyme 10 HGNC ID |
HGNC:5007 |
| Enzyme 10 Chromosome Location |
5 |
| Enzyme 10 Locus |
5p14-p13 |
| Enzyme 10 SNPs |
SNPJam Report |
| Enzyme 10 General References |
- Russ AP, Ruzicka V, Maerz W, Appelhans H, Gross W: Amplification and direct sequencing of a cDNA encoding human cytosolic 3-hydroxy-3-methylglutaryl-coenzyme A synthase. Biochim Biophys Acta. 1992 Oct 20;1132(3):329-31. [PubMed ]
- Rokosz LL, Boulton DA, Butkiewicz EA, Sanyal G, Cueto MA, Lachance PA, Hermes JD: Human cytoplasmic 3-hydroxy-3-methylglutaryl coenzyme A synthase: expression, purification, and characterization of recombinant wild-type and Cys129 mutant enzymes. Arch Biochem Biophys. 1994 Jul;312(1):1-13. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5285 |
| Enzyme 11 Name |
Acyl-protein thioesterase 1 |
| Enzyme 11 Synonyms |
- APT-1
- hAPT1
- Lysophospholipase 1
- Lysophospholipase I
- LPL-I
- LysoPLA I
|
| Enzyme 11 Gene Name |
LYPLA1 |
| Enzyme 11 Protein Sequence |
>Acyl-protein thioesterase 1
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRP
VTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQ
GGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLM
FGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
|
| Enzyme 11 Number of Residues |
230 |
| Enzyme 11 Molecular Weight |
24669.4 |
| Enzyme 11 Theoretical pI |
6.77 |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in hydrolase activity |
| Enzyme 11 Specific Function |
Hydrolyzes fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has depalmitoylating activity and also low lysophospholipase activity |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
5453722 |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
O75608 |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
LYPA1_HUMAN |
| Enzyme 11 PDB ID |
1FJ2 |
| Enzyme 11 PDB File |
Show |
| Enzyme 11 3D Structure |
|
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>693 bp
ATGTGCGGCAATAACATGTCAACCCCGCTGCCCGCCATCGTGCCCGCCGCCCGGAAGGCC
ACCGCTGCGGTGATTTTCCTGCATGGATTGGGAGATACTGGGCACGGATGGGCAGAAGCC
TTTGCAGGTATCAGAAGTTCACATATCAAATATATCTGCCCGCATGCGCCTGTTAGGCCT
GTTACATTAAATATGAACGTGGCTATGCCTTCATGGTTTGATATTATTGGGCTTTCACCA
GATTCACAGGAGGATGAATCTGGGATTAAACAGGCAGCAGAAAATATAAAAGCTTTGATT
GATCAAGAAGTGAAGAATGGCATTCCTTCTAACAGAATTATTTTGGGAGGGTTTTCTCAG
GGAGGAGCTTTATCTTTATATACTGCCCTTACCACACAGCAGAAACTGGCAGGTGTCACT
GCACTCAGTTGCTGGCTTCCACTTCGGGCTTCCTTTCCACAGGGTCCTATCGGTGGTGCT
AATAGAGATATTTCTATTCTCCAGTGCCACGGGGATTGTGACCCTTTGGTTCCCCTGATG
TTTGGTTCTCTTACGGTGGAAAAACTAAAAACATTGGTGAATCCAGCCAATGTGACCTTT
AAAACCTATGAAGGTATGATGCACAGTTCGTGTCAACAGGAAATGATGGATGTCAAGCAA
TTCATTGATAAACTCCTACCTCCAATTGATTGA
|
| Enzyme 11 GenBank Gene ID |
NM_006330.2 |
| Enzyme 11 GeneCard ID |
LYPLA1 |
| Enzyme 11 GenAtlas ID |
LYPLA1 |
| Enzyme 11 HGNC ID |
HGNC:6737 |
| Enzyme 11 Chromosome Location |
8 |
| Enzyme 11 Locus |
8q11.23 |
| Enzyme 11 SNPs |
SNPJam Report |
| Enzyme 11 General References |
- Devedjiev Y, Dauter Z, Kuznetsov SR, Jones TL, Derewenda ZS: Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A. Structure. 2000 Nov 15;8(11):1137-46. [PubMed ]
- Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Dekker FJ, Rocks O, Vartak N, Menninger S, Hedberg C, Balamurugan R, Wetzel S, Renner S, Gerauer M, Scholermann B, Rusch M, Kramer JW, Rauh D, Coates GW, Brunsveld L, Bastiaens PI, Waldmann H: Small-molecule inhibition of APT1 affects Ras localization and signaling. Nat Chem Biol. 2010 Jun;6(6):449-56. Epub 2010 Apr 25. [PubMed ]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5286 |
| Enzyme 12 Name |
Group XV phospholipase A2 |
| Enzyme 12 Synonyms |
- 1-O-acylceramide synthase
- ACS
- LCAT-like lysophospholipase
- LLPL
- Lysophospholipase 3
- Lysosomal phospholipase A2
- LPLA2
|
| Enzyme 12 Gene Name |
PLA2G15 |
| Enzyme 12 Protein Sequence |
>Group XV phospholipase A2
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTV
VHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGK
TFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREM
IEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVL
ASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQ
DIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGD
GTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
|
| Enzyme 12 Number of Residues |
412 |
| Enzyme 12 Molecular Weight |
46657.4 |
| Enzyme 12 Theoretical pI |
6.72 |
| Enzyme 12 GO Classification |
| Function |
- O-acyltransferase activity
- acyltransferase activity
- catalytic activity
- phosphatidylcholine-sterol O-acyltransferase activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in phosphatidylcholine-sterol O-acyltransferase activity |
| Enzyme 12 Specific Function |
Has transacylase and calcium-independent phospholipase A2 activity. Catalyzes the formation of 1-O-acyl-N- acetylsphingosine and the concomitant release of a lyso- phospholipid. May have weak lysophospholipase activity |
| Enzyme 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
Not Available |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q8NCC3 |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PAG15_HUMAN |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1239 bp
ATGGGCCTCCACCTCCGCCCCTACCGTGTGGGGCTGCTCCCGGATGGCCTCCTGTTCCTC
TTGCTGCTGCTAATGCTGCTCGCGGACCCAGCGCTCCCGGCCGGACGTCACCCCCCAGTG
GTGCTGGTCCCTGGTGATTTGGGTAACCAACTGGAAGCCAAGCTGGACAAGCCGACAGTG
GTGCACTACCTCTGCTCCAAGAAGACCGAAAGCTACTTCACAATCTGGCTGAACCTGGAA
CTGCTGCTGCCTGTCATCATTGACTGCTGGATTGACAATATCAGGCTGGTTTACAACAAA
ACATCCAGGGCCACCCAGTTTCCTGATGGTGTGGATGTACGTGTCCCTGGCTTTGGGAAG
ACCTTCTCACTGGAGTTCCTGGACCCCAGCAAAAGCAGCGTGGGTTCCTATTTCCACACC
ATGGTGGAGAGCCTTGTGGGCTGGGGCTACACACGGGGTGAGGATGTCCGAGGGGCTCCC
TATGACTGGCGCCGAGCCCCAAATGAAAACGGGCCCTACTTCCTGGCCCTCCGCGAGATG
ATCGAGGAGATGTACCAGCTGTATGGGGGCCCCGTGGTGCTGGTTGCCCACAGTATGGGC
AACATGTACACGCTCTACTTTCTGCAGCGGCAGCCGCAGGCCTGGAAGGACAAGTATATC
CGGGCCTTCGTGTCACTGGGTGCGCCCTGGGGGGGCGTGGCCAAGACCCTGCGCGTCCTG
GCTTCAGGAGACAACAACCGGATCCCAGTCATCGGGCCCCTGAAGATCCGGGAGCAGCAG
CGGTCAGCTGTCTCCACCAGCTGGCTGCTGCCCTACAACTACACATGGTCACCTGAGAAG
GTGTTCGTGCAGACACCCACAATCAACTACACACTGCGGGACTACCGCAAGTTCTTCCAG
GACATCGGCTTTGAAGATGGCTGGCTCATGCGGCAGGACACAGAAGGGCTGGTGGAAGCC
ACGATGCCACCTGGCGTGCAGCTGCACTGCCTCTATGGCACTGGCGTCCCCACACCAGAC
TCCTTCTACTATGAGAGCTTCCCTGACCGTGACCCTAAAATCTGCTTTGGTGACGGCGAT
GGTACTGTGAACTTGAAGAGTGCCCTGCAGTGCCAGGCCTGGCAGAGCCGCCAGGAGCAC
CAAGTGTTGCTGCAGGAGCTGCCAGGCAGCGAGCACATCGAGATGCTGGCCAACGCCACC
ACCCTGGCCTATCTGAAACGTGTGCTCCTTGGGCCCTGA
|
| Enzyme 12 GenBank Gene ID |
AB017494 |
| Enzyme 12 GeneCard ID |
PLA2G15 |
| Enzyme 12 GenAtlas ID |
PLA2G15 |
| Enzyme 12 HGNC ID |
HGNC:17163 |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
16q22.1 |
| Enzyme 12 SNPs |
SNPJam Report |
| Enzyme 12 General References |
- Taniyama Y, Shibata S, Kita S, Horikoshi K, Fuse H, Shirafuji H, Sumino Y, Fujino M: Cloning and expression of a novel lysophospholipase which structurally resembles lecithin cholesterol acyltransferase. Biochem Biophys Res Commun. 1999 Apr 2;257(1):50-6. [PubMed ]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed ]
- Hiraoka M, Abe A, Shayman JA: Cloning and characterization of a lysosomal phospholipase A2, 1-O-acylceramide synthase. J Biol Chem. 2002 Mar 22;277(12):10090-9. Epub 2002 Jan 14. [PubMed ]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5287 |
| Enzyme 13 Name |
Calcium-dependent phospholipase A2 |
| Enzyme 13 Synonyms |
- Group V phospholipase A2
- PLA2-10
- Phosphatidylcholine 2-acylhydrolase 5
|
| Enzyme 13 Gene Name |
PLA2G5 |
| Enzyme 13 Protein Sequence |
>Calcium-dependent phospholipase A2
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
|
| Enzyme 13 Number of Residues |
138 |
| Enzyme 13 Molecular Weight |
15674.1 |
| Enzyme 13 Theoretical pI |
8.48 |
| Enzyme 13 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Involved in phospholipase A2 activity |
| Enzyme 13 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L- alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
10862735 |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P39877 |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PA2G5_HUMAN |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>417 bp
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
|
| Enzyme 13 GenBank Gene ID |
AL158172 |
| Enzyme 13 GeneCard ID |
PLA2G5 |
| Enzyme 13 GenAtlas ID |
PLA2G5 |
| Enzyme 13 HGNC ID |
HGNC:9038 |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
1p36-p34 |
| Enzyme 13 SNPs |
SNPJam Report |
| Enzyme 13 General References |
- Chen J, Engle SJ, Seilhamer JJ, Tischfield JA: Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J Biol Chem. 1994 Jan 28;269(4):2365-8. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5288 |
| Enzyme 14 Name |
Group IIF secretory phospholipase A2 |
| Enzyme 14 Synonyms |
- GIIF sPLA2
- sPLA2-IIF
- Phosphatidylcholine 2-acylhydrolase 2F
|
| Enzyme 14 Gene Name |
PLA2G2F |
| Enzyme 14 Protein Sequence |
>Group IIF secretory phospholipase A2
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
|
| Enzyme 14 Number of Residues |
168 |
| Enzyme 14 Molecular Weight |
18658.0 |
| Enzyme 14 Theoretical pI |
4.94 |
| Enzyme 14 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in phospholipase A2 activity |
| Enzyme 14 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
12276060 |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9BZM2 |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PA2GF_HUMAN |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>507 bp
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
|
| Enzyme 14 GenBank Gene ID |
AF306566 |
| Enzyme 14 GeneCard ID |
PLA2G2F |
| Enzyme 14 GenAtlas ID |
PLA2G2F |
| Enzyme 14 HGNC ID |
HGNC:30040 |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
1p35 |
| Enzyme 14 SNPs |
SNPJam Report |
| Enzyme 14 General References |
- Valentin E, Singer AG, Ghomashchi F, Lazdunski M, Gelb MH, Lambeau G: Cloning and recombinant expression of human group IIF-secreted phospholipase A(2). Biochem Biophys Res Commun. 2000 Dec 9;279(1):223-8. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5289 |
| Enzyme 15 Name |
Cytosolic phospholipase A2 |
| Enzyme 15 Synonyms |
- cPLA2
- Phospholipase A2 group IVA
- Phospholipase A2
- Phosphatidylcholine 2-acylhydrolase
- Lysophospholipase
|
| Enzyme 15 Gene Name |
PLA2G4A |
| Enzyme 15 Protein Sequence |
>Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
|
| Enzyme 15 Number of Residues |
749 |
| Enzyme 15 Molecular Weight |
85210.2 |
| Enzyme 15 Theoretical pI |
5.03 |
| Enzyme 15 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- phospholipase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in metabolic process |
| Enzyme 15 Specific Function |
Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
Not Available |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P47712 |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
PA24A_HUMAN |
| Enzyme 15 PDB ID |
1CJY |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>2250 bp
ATGTCATTTATAGATCCTTACCAGCACATTATAGTGGAGCACCAGTATTCCCACAAGTTT
ACGGTAGTGGTGTTACGTGCCACCAAAGTGACAAAGGGGGCCTTTGGTGACATGCTTGAT
ACTCCAGATCCCTATGTGGAACTTTTTATCTCTACAACCCCTGACAGCAGGAAGAGAACA
AGACATTTCAATAATGACATAAACCCTGTGTGGAATGAGACCTTTGAATTTATTTTGGAT
CCTAATCAGGAAAATGTTTTGGAGATTACGTTAATGGATGCCAATTATGTCATGGATGAA
ACTCTAGGGACAGCAACATTTACTGTATCTTCTATGAAGGTGGGAGAAAAGAAAGAAGTT
CCTTTTATTTTCAACCAAGTCACTGAAATGGTTCTAGAAATGTCTCTTGAAGTTTGCTCA
TGCCCAGACCTACGATTTAGTATGGCTCTGTGTGATCAGGAGAAGACTTTCAGACAACAG
AGAAAAGAACACATAAGGGAGAGCATGAAGAAACTCTTGGGTCCAAAGAATAGTGAAGGA
TTGCATTCTGCACGTGATGTGCCTGTGGTAGCCATATTGGGTTCAGGTGGGGGTTTCCGA
GCCATGGTGGGATTCTCTGGTGTGATGAAGGCATTATACGAATCAGGAATTCTGGATTGT
GCTACCTACGTTGCTGGTCTTTCTGGCTCCACCTGGTATATGTCAACCTTGTATTCTCAC
CCTGATTTTCCAGAGAAAGGGCCAGAGGAGATTAATGAAGAACTAATGAAAAATGTTAGC
CACAATCCCCTTTTACTTCTCACACCACAGAAAGTTAAAAGATATGTTGAGTCTTTATGG
AAGAAGAAAAGCTCTGGACAACCTGTCACCTTTACTGATATCTTTGGGATGTTAATAGGA
GAAACACTAATTCATAATAGAATGAATACTACTCTGAGCAGTTTGAAGGAAAAAGTTAAT
ACTGCACAATGCCCTTTACCTCTTTTCACCTGTCTTCATGTCAAACCTGACGTTTCAGAG
CTGATGTTTGCAGATTGGGTTGAATTTAGTCCATACGAAATTGGCATGGCTAAATATGGT
ACTTTTATGGCTCCCGACTTATTTGGAAGCAAATTTTTTATGGGAACAGTCGTTAAGAAG
TATGAAGAAAACCCCTTGCATTTCTTAATGGGTGTCTGGGGCAGTGCCTTTTCCATATTG
TTCAACAGAGTTTTGGGCGTTTCTGGTTCACAAAGCAGAGGCTCCACAATGGAGGAAGAA
TTAGAAAATATTACCACAAAGCATATTGTGAGTAATGATAGCTCGGACAGTGATGATGAA
TCACACGAACCCAAAGGCACTGAAAATGAAGATGCTGGAAGTGACTATCAAAGTGATAAT
CAAGCAAGTTGGATTCATCGTATGATAATGGCCTTGGTGAGTGATTCAGCTTTATTCAAT
ACCAGAGAAGGACGTGCTGGGAAGGTACACAACTTCATGCTGGGCTTGAATCTCAATACA
TCTTATCCACTGTCTCCTTTGAGTGACTTTGCCACACAGGACTCCTTTGATGATGATGAA
CTGGATGCAGCTGTAGCAGATCCTGATGAATTTGAGCGAATATATGAGCCTCTGGATGTC
AAAAGTAAAAAGATTCATGTAGTGGACAGTGGGCTCACATTTAACCTGCCGTATCCCTTG
ATACTGAGACCTCAGAGAGGGGTTGATCTCATAATCTCCTTTGACTTTTCTGCAAGGCCA
AGTGACTCTAGTCCTCCGTTCAAGGAACTTCTACTTGCAGAAAAGTGGGCTAAAATGAAC
AAGCTCCCCTTTCCAAAGATTGATCCTTATGTGTTTGATCGGGAAGGGCTGAAGGAGTGC
TATGTCTTTAAACCCAAGAATCCTGATATGGAGAAAGATTGCCCAACCATCATCCACTTT
GTTCTGGCCAACATCAACTTCAGAAAGTACAAGGCTCCAGGTGTTCCAAGGGAAACTGAG
GAAGAGAAAGAAATCGCTGACTTTGATATTTTTGATGACCCAGAATCACCATTTTCAACC
TTCAATTTTCAATATCCAAATCAAGCATTCAAAAGACTACATGATCTTATGCACTTCAAT
ACTCTGAACAACATTGATGTGATAAAAGAAGCCATGGTTGAAAGCATTGAATATAGAAGA
CAGAATCCATCTCGTTGCTCTGTTTCCCTTAGTAATGTTGAGGCAAGAAGATTTTTCAAC
AAGGAGTTTCTAAGTAAACCCAAAGCATAG
|
| Enzyme 15 GenBank Gene ID |
M72393 |
| Enzyme 15 GeneCard ID |
PLA2G4A |
| Enzyme 15 GenAtlas ID |
PLA2G4A |
| Enzyme 15 HGNC ID |
HGNC:9035 |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1q25 |
| Enzyme 15 SNPs |
SNPJam Report |
| Enzyme 15 General References |
- Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL: A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043-51. [PubMed ]
- Sharp JD, White DL, Chiou XG, Goodson T, Gamboa GC, McClure D, Burgett S, Hoskins J, Skatrud PL, Sportsman JR, et al.: Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. J Biol Chem. 1991 Aug 15;266(23):14850-3. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ: cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269-78. [PubMed ]
- Sharp JD, Pickard RT, Chiou XG, Manetta JV, Kovacevic S, Miller JR, Varshavsky AD, Roberts EF, Strifler BA, Brems DN, et al.: Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1994 Sep 16;269(37):23250-4. [PubMed ]
- Borsch-Haubold AG, Bartoli F, Asselin J, Dudler T, Kramer RM, Apitz-Castro R, Watson SP, Gelb MH: Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. J Biol Chem. 1998 Feb 20;273(8):4449-58. [PubMed ]
- Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J Biol Chem. 1998 Jan 16;273(3):1596-604. [PubMed ]
- Xu GY, McDonagh T, Yu HA, Nalefski EA, Clark JD, Cumming DA: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J Mol Biol. 1998 Jul 17;280(3):485-500. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5290 |
| Enzyme 16 Name |
Phospholipase A2 |
| Enzyme 16 Synonyms |
- Group IB phospholipase A2
- Phosphatidylcholine 2-acylhydrolase 1B
|
| Enzyme 16 Gene Name |
PLA2G1B |
| Enzyme 16 Protein Sequence |
>Phospholipase A2
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
|
| Enzyme 16 Number of Residues |
148 |
| Enzyme 16 Molecular Weight |
16359.5 |
| Enzyme 16 Theoretical pI |
7.91 |
| Enzyme 16 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in phospholipase A2 activity |
| Enzyme 16 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
Not Available |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P04054 |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
PA21B_HUMAN |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>447 bp
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTATGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
|
| Enzyme 16 GenBank Gene ID |
M21054 |
| Enzyme 16 GeneCard ID |
PLA2G1B |
| Enzyme 16 GenAtlas ID |
PLA2G1B |
| Enzyme 16 HGNC ID |
HGNC:9030 |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
12q23-q24.1 |
| Enzyme 16 SNPs |
SNPJam Report |
| Enzyme 16 General References |
- Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK: Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA. 1986 Dec;5(6):519-27. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C: Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. Eur J Biochem. 1982 Feb;122(1):111-7. [PubMed ]
- Verheij HM, Westerman J, Sternby B, De Haas GH: The complete primary structure of phospholipase A2 from human pancreas. Biochim Biophys Acta. 1983 Sep 14;747(1-2):93-9. [PubMed ]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5291 |
| Enzyme 17 Name |
Group XIIB secretory phospholipase A2-like protein |
| Enzyme 17 Synonyms |
- Group XIII secretory phospholipase A2-like protein
- GXIII sPLA2-like
- sPLA2-GXIIB
- GXIIB
|
| Enzyme 17 Gene Name |
PLA2G12B |
| Enzyme 17 Protein Sequence |
>Group XIIB secretory phospholipase A2-like protein
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
|
| Enzyme 17 Number of Residues |
195 |
| Enzyme 17 Molecular Weight |
21658.5 |
| Enzyme 17 Theoretical pI |
5.81 |
| Enzyme 17 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
|
|
| Enzyme 17 General Function |
Involved in phospholipase A2 activity |
| Enzyme 17 Specific Function |
Not known; does not seem to have catalytic activity |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
15824793 |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q9BX93 |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
PG12B_HUMAN |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>588 bp
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCAGCCTGTGATTCC
CTGGTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGT
CAGCGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
|
| Enzyme 17 GenBank Gene ID |
AF339053 |
| Enzyme 17 GeneCard ID |
PLA2G12B |
| Enzyme 17 GenAtlas ID |
PLA2G12B |
| Enzyme 17 HGNC ID |
HGNC:18555 |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
10q22.1 |
| Enzyme 17 SNPs |
SNPJam Report |
| Enzyme 17 General References |
- Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry. 2003 Oct 7;42(39):11494-503. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed ]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5292 |
| Enzyme 18 Name |
Group 10 secretory phospholipase A2 |
| Enzyme 18 Synonyms |
- Group X secretory phospholipase A2
- GX sPLA2
- sPLA2-X
- Phosphatidylcholine 2-acylhydrolase 10
|
| Enzyme 18 Gene Name |
PLA2G10 |
| Enzyme 18 Protein Sequence |
>Group 10 secretory phospholipase A2
MGPLPVCLPIMLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPI
AYMKYGCFCGLGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGP
AENKCQELLCKCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
|
| Enzyme 18 Number of Residues |
165 |
| Enzyme 18 Molecular Weight |
18153.0 |
| Enzyme 18 Theoretical pI |
6.46 |
| Enzyme 18 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in phospholipase A2 activity |
| Enzyme 18 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
Not Available |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
O15496 |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
PA2GX_HUMAN |
| Enzyme 18 PDB ID |
1LE7 |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>498 bp
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
|
| Enzyme 18 GenBank Gene ID |
U95301 |
| Enzyme 18 GeneCard ID |
PLA2G10 |
| Enzyme 18 GenAtlas ID |
PLA2G10 |
| Enzyme 18 HGNC ID |
HGNC:9029 |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
16p13.1-p12 |
| Enzyme 18 SNPs |
SNPJam Report |
| Enzyme 18 General References |
- Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [PubMed ]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5294 |
| Enzyme 19 Name |
Group IIE secretory phospholipase A2 |
| Enzyme 19 Synonyms |
- GIIE sPLA2
- sPLA2-IIE
- Phosphatidylcholine 2-acylhydrolase 2E
|
| Enzyme 19 Gene Name |
PLA2G2E |
| Enzyme 19 Protein Sequence |
>Group IIE secretory phospholipase A2
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
|
| Enzyme 19 Number of Residues |
142 |
| Enzyme 19 Molecular Weight |
15988.5 |
| Enzyme 19 Theoretical pI |
8.28 |
| Enzyme 19 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in phospholipase A2 activity |
| Enzyme 19 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
Not Available |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NZK7 |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
PA2GE_HUMAN |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>429 bp
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
|
| Enzyme 19 GenBank Gene ID |
AF189279 |
| Enzyme 19 GeneCard ID |
PLA2G2E |
| Enzyme 19 GenAtlas ID |
PLA2G2E |
| Enzyme 19 HGNC ID |
HGNC:13414 |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
1p36.13 |
| Enzyme 19 SNPs |
SNPJam Report |
| Enzyme 19 General References |
- Suzuki N, Ishizaki J, Yokota Y, Higashino K, Ono T, Ikeda M, Fujii N, Kawamoto K, Hanasaki K: Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s. J Biol Chem. 2000 Feb 25;275(8):5785-93. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5295 |
| Enzyme 20 Name |
Acyl-protein thioesterase 2 |
| Enzyme 20 Synonyms |
- APT-2
- Lysophospholipase II
- LPL-II
- LysoPLA II
|
| Enzyme 20 Gene Name |
LYPLA2 |
| Enzyme 20 Protein Sequence |
>Acyl-protein thioesterase 2
MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAP
RIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGG
FSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAILQCHGELDPMVP
VRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPPV
|
| Enzyme 20 Number of Residues |
231 |
| Enzyme 20 Molecular Weight |
24736.7 |
| Enzyme 20 Theoretical pI |
7.25 |
| Enzyme 20 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 20 General Function |
Involved in hydrolase activity |
| Enzyme 20 Specific Function |
May hydrolyze fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS. Has lysophospholipase activity |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
9966764 |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
O95372 |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
LYPA2_HUMAN |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>696 bp
ATGTGTGGTAACACCATGTCTGTGCCCCTGCTCACCGATGCTGCCACCGTGTCTGGAGCT
GAGCGGGAAACGGCCGCGGTTATTTTTTTACATGGACTTGGAGACACAGGGCACAGCTGG
GCTGACGCCCTCTCCACCATCCGGCTCCCTCACGTCAAGTACATCTGTCCCCATGCGCCT
AGGATCCCTGTGACCCTCAACATGAAGATGGTGATGCCCTCCTGGTTTGACCTGATGGGG
CTGAGTCCAGATGCCCCAGAGGACGAGGCTGGCATCAAGAAGGCAGCAGAGAACATCAAG
GCCTTGATTGAGCATGAAATGAAGAACGGGATCCCTGCCAATCGAATCGTCCTGGGAGGC
TTTTCACAGGGCGGGGCCCTGTCCCTCTACACGGCCCTCACCTGCCCCCACCCTCTGGCT
GGCATCGTGGCGTTGAGCTGCTGGCTGCCTCTGCACCGGGCCTTCCCCCAGGCAGCTAAT
GGCAGTGCCAAGGACCTGGCCATACTCCAGTGCCATGGGGAGCTGGACCCCATGGTGCCC
GTACGGTTTGGGGCCCTGACGGCTGAGAAGCTCCGGTCTGTTGTCACACCTGCCAGGGTC
CAGTTCAAGACATACCCGGGTGTCATGCACAGCTCCTGTCCTCAGGAGATGGCAGCTGTG
AAGGAATTTCTTGAGAAGCTGCTGCCTCCTGTCTAA
|
| Enzyme 20 GenBank Gene ID |
NM_007260.2 |
| Enzyme 20 GeneCard ID |
LYPLA2 |
| Enzyme 20 GenAtlas ID |
LYPLA2 |
| Enzyme 20 HGNC ID |
HGNC:6738 |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
1p36.11 |
| Enzyme 20 SNPs |
SNPJam Report |
| Enzyme 20 General References |
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5297 |
| Enzyme 21 Name |
85 kDa calcium-independent phospholipase A2 |
| Enzyme 21 Synonyms |
- CaI-PLA2
- iPLA2
- Group VI phospholipase A2
- GVI PLA2
|
| Enzyme 21 Gene Name |
PLA2G6 |
| Enzyme 21 Protein Sequence |
>85 kDa calcium-independent phospholipase A2
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHG
VPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHL
LCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGM
YFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFR
NYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNP
TLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKT
VFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVN
ALWETEVYIYEHREEFQKLIQLLLSP
|
| Enzyme 21 Number of Residues |
806 |
| Enzyme 21 Molecular Weight |
89902.3 |
| Enzyme 21 Theoretical pI |
7.28 |
| Enzyme 21 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in metabolic process |
| Enzyme 21 Specific Function |
Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
3142700 |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
O60733 |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
PA2G6_HUMAN |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>2421 bp
ATGCAGTTCTTTGGCCGCCTGGTCAATACCTTCAGTGGCGTCACCAACTTGTTCTCTAAC
CCATTCCGGGTGAAGGAGGTGGCTGTGGCCGACTACACCTCGAGTGACCGAGTTCGGGAG
GAAGGGCAGCTGATTCTGTTCCAGAACACTCCCAACCGCACCTGGGACTGCGTCCTGGTC
AACCCCAGGAACTCACAGAGTGGATTCCGACTCTTCCAGCTGGAGTTGGAGGCTGACGCC
CTAGTGAATTTCCATCAGTATTCTTCCCAGCTGCTACCCTTCTATGAGAGCTCCCCTCAG
GTCCTGCACACTGAGGTCCTGCAGCACCTGACCGACCTCATCCGTAACCACCCCAGCTGG
TCAGTGGCCCACCTGGCTGTGGAGCTAGGGATCCGCGAGTGCTTCCATCACAGCCGTATC
ATCAGCTGTGCCAATTGCGCGGAGAACGAGGAGGGCTGCACACCCCTGCACCTGGCCTGC
CGCAAGGGTGATGGGGAGATCCTGGTGGAGCTGGTGCAGTACTGCCACACTCAGATGGAT
GTCACCGACTACAAGGGAGAGACCGTCTTCCATTATGCTGTCCAGGGTGACAATTCTCAG
GTGCTGCAGCTCCTTGGAAGGAACGCAGTGGCTGGCCTGAACCAGGTGAATAACCAAGGG
CTGACCCCGCTGCACCTGGCCTGCCAGCTGGGGAAGCAGGAGATGGTCCGCGTGCTGCTG
CTGTGCAATGCTCGGTGCAACATCATGGGCCCCAACGGCTACCCCATCCACTCGGCCATG
AAGTTCTCTCAGAAGGGGTGTGCGGAGATGATCATCAGCATGGACAGCAGCCAGATCCAC
AGCAAAGACCCCCGTTACGGAGCCAGCCCCCTCCACTGGGCCAAGAACGCAGAGATGGCC
CGCATGCTGCTGAAACGGGGCTGCAACGTGAACAGCACCAGCTCCGCGGGGAACACGGCC
CTGCACGTGGCGGTGATGCGCAACCGCTTCGACTGTGCCATAGTGCTGCTGACCCACGGG
GCCAACGCGGATGCCCGCGGAGAGCACGGCAACACCCCGCTGCACCTGGCCATGTCGAAA
GACAACGTGGAGATGATCAAGGCCCTCATCGTGTTCGGAGCAGAAGTGGACACCCCGAAT
GACTTTGGGGAGACTCCTACATTCCTAGCCTCCAAAATCGGCAGACTTGTCACCAGGAAG
GCGATCTTGACTCTGCTGAGAACCGTGGGGGCCGAATACTGCTTCCCACCCATCCACGGG
GTCCCCGCGGAGCAGGGCTCTGCAGCGCCACATCATCCCTTCTCCCTGGAAAGAGCTCAG
CCCCCACCGATCAGCCTAAACAACCTAGAACTACAGGATCTCATGCACATCTCACGGGCC
CGGAAGCCAGCGTTCATCCTGGGCTCCATGAGGGACGAGAAGCGGACCCACGACCACCTG
CTGTGCCTGGATGGAGGAGGAGTGAAAGGCCTCATCATCATCCAGCTCCTCATCGCCATC
GAGAAGGCCTCGGGTGTGGCCACCAAGGACCTGTTTGACTGGGTGGCGGGCACCAGCACT
GGAGGCATCCTGGCCCTGGCCATTCTGCACAGTAAGTCCATGGCCTACATGCGCGGCATG
TACTTTCGCATGAAGGATGAGGTGTTCCGGGGCTCCAGGCCCTACGAGTCGGGGCCCCTG
GAGGAGTTCCTGAAGCGGGAGTTTGGGGAGCACACCAAGATGACGGACGTCAGGAAACCC
AAGGTGATGCTGACAGGGACACTGTCTGACCGGCAGCCGGCTGAACTCCACCTCTTCCGG
AACTACGATGCTCCAGAAACTGTCCGGGAGCCTCGTTTCAACCAGAACGTTAACCTCAGG
CCTCCAGCTCAGCCCTCAGACCAGCTGGTGTGGCGGGCGGCCCGAAGCAGCGGGGCAGCT
CCTACTTACTTCCGACCCAATGGGCGCTTCCTGGACGGTGGGCTGCTGGCCAACAACCCC
ACGCTGGATGCCATGACCGAGATCCATGAGTACAATCAGGACCTGATCCGCAAGGGTCAG
GCCAACAAGGTGAAGAAACTCTCCATCGTTGTCTCCCTGGGGACAGGGAGGTCCCCACAA
GTGCCTGTGACCTGTGTGGATGTCTTCCGTCCCAGCAACCCCTGGGAGCTGGCCAAGACT
GTTTTTGGGGCCAAGGAACTGGGCAAGATGGTGGTGGACTGTTGCACGGATCCAGACGGG
CGGGCTGTGGACCGGGCACGGGCCTGGTGCGAGATGGTCGGCATCCAGTACTTCAGATTG
AACCCCCAGCTGGGGACGGACATCATGCTGGATGAGGTCAGTGACACAGTGCTGGTCAAC
GCCCTCTGGGAGACCGAGGTCTACATCTATGAGCACCGCGAGGAGTTCCAGAAGCTCATC
CACCTGCTGCTCTCACCCTGA
|
| Enzyme 21 GenBank Gene ID |
AF064594 |
| Enzyme 21 GeneCard ID |
PLA2G6 |
| Enzyme 21 GenAtlas ID |
PLA2G6 |
| Enzyme 21 HGNC ID |
HGNC:9039 |
| Enzyme 21 Chromosome Location |
2 |
| Enzyme 21 Locus |
22q13.1 |
| Enzyme 21 SNPs |
SNPJam Report |
| Enzyme 21 General References |
- Larsson PK, Claesson HE, Kennedy BP: Multiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activity. J Biol Chem. 1998 Jan 2;273(1):207-14. [PubMed ]
- Ma Z, Wang X, Nowatzke W, Ramanadham S, Turk J: Human pancreatic islets express mRNA species encoding two distinct catalytically active isoforms of group VI phospholipase A2 (iPLA2) that arise from an exon-skipping mechanism of alternative splicing of the transcript from the iPLA2 gene on chromosome 22q13.1. J Biol Chem. 1999 Apr 2;274(14):9607-16. [PubMed ]
- Larsson Forsell PK, Kennedy BP, Claesson HE: The human calcium-independent phospholipase A2 gene multiple enzymes with distinct properties from a single gene. Eur J Biochem. 1999 Jun;262(2):575-85. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Malhotra A, Edelman-Novemsky I, Xu Y, Plesken H, Ma J, Schlame M, Ren M: Role of calcium-independent phospholipase A2 in the pathogenesis of Barth syndrome. Proc Natl Acad Sci U S A. 2009 Feb 17;106(7):2337-41. Epub 2009 Jan 21. [PubMed ]
- Khateeb S, Flusser H, Ofir R, Shelef I, Narkis G, Vardi G, Shorer Z, Levy R, Galil A, Elbedour K, Birk OS: PLA2G6 mutation underlies infantile neuroaxonal dystrophy. Am J Hum Genet. 2006 Nov;79(5):942-8. Epub 2006 Sep 19. [PubMed ]
- Morgan NV, Westaway SK, Morton JE, Gregory A, Gissen P, Sonek S, Cangul H, Coryell J, Canham N, Nardocci N, Zorzi G, Pasha S, Rodriguez D, Desguerre I, Mubaidin A, Bertini E, Trembath RC, Simonati A, Schanen C, Johnson CA, Levinson B, Woods CG, Wilmot B, Kramer P, Gitschier J, Maher ER, Hayflick SJ: PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron. Nat Genet. 2006 Jul;38(7):752-4. Epub 2006 Jun 18. [PubMed ]
- Paisan-Ruiz C, Bhatia KP, Li A, Hernandez D, Davis M, Wood NW, Hardy J, Houlden H, Singleton A, Schneider SA: Characterization of PLA2G6 as a locus for dystonia-parkinsonism. Ann Neurol. 2009 Jan;65(1):19-23. [PubMed ]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5299 |
| Enzyme 22 Name |
Eosinophil lysophospholipase |
| Enzyme 22 Synonyms |
- Charcot-Leyden crystal protein
- CLC
- Galectin-10
- Gal-10
- Lysolecithin acylhydrolase
|
| Enzyme 22 Gene Name |
CLC |
| Enzyme 22 Protein Sequence |
>Eosinophil lysophospholipase
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR
|
| Enzyme 22 Number of Residues |
142 |
| Enzyme 22 Molecular Weight |
16480.8 |
| Enzyme 22 Theoretical pI |
7.50 |
| Enzyme 22 GO Classification |
| Function |
- binding
- carbohydrate binding
- sugar binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in sugar binding |
| Enzyme 22 Specific Function |
May have both lysophospholipase and carbohydrate-binding activities |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
3399666 |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q05315 |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
LPPL_HUMAN |
| Enzyme 22 PDB ID |
1QKQ |
| Enzyme 22 PDB File |
Show |
| Enzyme 22 3D Structure |
|
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>429 bp
ATGTCCCTGCTACCCGTGCCATACACAGAGGCTGCCTCTTTGTCTACTGGTTCTACTGTG
ACAATCAAAGGGCGACCACTTGTCTGTTTCTTGAATGAACCATATCTGCAGGTGGATTTC
CACACTGAGATGAAGGAGGAATCAGACATTGTCTTCCATTTCCAAGTGTGCTTTGGTCGT
CGTGTGGTCATGAACAGCCGTGAGTATGGGGCCTGGAAGCAGCAGGTGGAATCCAAGAAC
ATGCCCTTTCAGGATGGCCAAGAATTTGAACTGAGCATCTCAGTGCTGCCAGATAAGTAC
CAGGTAATGGTCAATGGCCAATCCTCTTACACCTTTGACCATAGAATCAAGCCTGAGGCT
GTGAAGATGGTGCAAGTGTGGAGAGATATCTCCCTGACCAAATTTAATGTCAGCTATTTA
AAGAGATAA
|
| Enzyme 22 GenBank Gene ID |
AC005393 |
| Enzyme 22 GeneCard ID |
CLC |
| Enzyme 22 GenAtlas ID |
CLC |
| Enzyme 22 HGNC ID |
HGNC:2014 |
| Enzyme 22 Chromosome Location |
1 |
| Enzyme 22 Locus |
19q13.1 |
| Enzyme 22 SNPs |
SNPJam Report |
| Enzyme 22 General References |
- Ackerman SJ, Corrette SE, Rosenberg HF, Bennett JC, Mastrianni DM, Nicholson-Weller A, Weller PF, Chin DT, Tenen DG: Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily. J Immunol. 1993 Jan 15;150(2):456-68. [PubMed ]
- Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ: Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. Genomics. 1992 May;13(1):240-2. [PubMed ]
- Dyer KD, Handen JS, Rosenberg HF: The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes. Genomics. 1997 Mar 1;40(2):217-21. [PubMed ]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Ghafouri B, Irander K, Lindbom J, Tagesson C, Lindahl M: Comparative proteomics of nasal fluid in seasonal allergic rhinitis. J Proteome Res. 2006 Feb;5(2):330-8. [PubMed ]
- Leonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR: Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure. 1995 Dec 15;3(12):1379-93. [PubMed ]
- Swaminathan GJ, Leonidas DD, Savage MP, Ackerman SJ, Acharya KR: Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution. Biochemistry. 1999 Oct 19;38(42):13837-43. [PubMed ]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5302 |
| Enzyme 23 Name |
Group IID secretory phospholipase A2 |
| Enzyme 23 Synonyms |
- GIID sPLA2
- sPLA2-IID
- PLA2IID
- Phosphatidylcholine 2-acylhydrolase 2D
- Secretory-type PLA, stroma-associated homolog
|
| Enzyme 23 Gene Name |
PLA2G2D |
| Enzyme 23 Protein Sequence |
>Group IID secretory phospholipase A2
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
|
| Enzyme 23 Number of Residues |
145 |
| Enzyme 23 Molecular Weight |
16546.1 |
| Enzyme 23 Theoretical pI |
8.28 |
| Enzyme 23 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in phospholipase A2 activity |
| Enzyme 23 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
5771420 |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9UNK4 |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PA2GD_HUMAN |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>438 bp
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
|
| Enzyme 23 GenBank Gene ID |
AF112982 |
| Enzyme 23 GeneCard ID |
PLA2G2D |
| Enzyme 23 GenAtlas ID |
PLA2G2D |
| Enzyme 23 HGNC ID |
HGNC:9033 |
| Enzyme 23 Chromosome Location |
1 |
| Enzyme 23 Locus |
1p36.12 |
| Enzyme 23 SNPs |
SNPJam Report |
| Enzyme 23 General References |
- Ishizaki J, Suzuki N, Higashino K, Yokota Y, Ono T, Kawamoto K, Fujii N, Arita H, Hanasaki K: Cloning and characterization of novel mouse and human secretory phospholipase A(2)s. J Biol Chem. 1999 Aug 27;274(35):24973-9. [PubMed ]
- Shakhov AN, Rubtsov AV, Lyakhov IG, Tumanov AV, Nedospasov SA: SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000 Feb;1(3):191-9. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5309 |
| Enzyme 24 Name |
Phospholipase D2 |
| Enzyme 24 Synonyms |
- PLD 2
- hPLD2
- Choline phosphatase 2
- PLD1C
- Phosphatidylcholine-hydrolyzing phospholipase D2
|
| Enzyme 24 Gene Name |
PLD2 |
| Enzyme 24 Protein Sequence |
>Phospholipase D2
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
|
| Enzyme 24 Number of Residues |
933 |
| Enzyme 24 Molecular Weight |
105986.1 |
| Enzyme 24 Theoretical pI |
7.68 |
| Enzyme 24 GO Classification |
| Function |
- binding
- catalytic activity
- lipid binding
- phosphoinositide binding
- phospholipid binding
- protein binding
|
| Process |
- cell communication
- cellular process
- metabolic process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in protein binding |
| Enzyme 24 Specific Function |
May have a role in signal-induced cytoskeletal regulation and/or endocytosis |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
2645858 |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
O14939 |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
PLD2_HUMAN |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>2802 bp
ATGACGGCGACCCCTGAGAGCCTCTTCCCCACTGGGGACGAACTGGACTCCAGCCAGCTC
CAGATGGAGTCCGATGAGGTGGACACCCTGAAGGAGGGAGAGGACCCAGCCGACCGGATG
CACCCGTTTCTGGCCATCTATGAGCTTCAGTCTCTGAAAGTGCACCCCTTGGTGTTCGCA
CCTGGGGTCCCTGTCACAGCCCAGGTGGTGGGCACCGAAAGATATACCAGCGGATCCAAG
GTGGGAACCTGCACTCTGTATTCTGTCCGCTTGACTCACGGCGACTTTTCCTGGACAACC
AAGAAGAAATACCGTCATTTTCAGGAGCTGCATCGGGACCTCCTGAGACACAAAGTCTTG
ATGAGTCTGCTCCCTCTGGCTCGATTTGCCGTTGCCTATTCTCCAGCCCGAGATGCAGGC
AACAGAGAGATGCCCTCTCTACCCCGGGCAGGTCCTGAGGGCTCCACCAGACATGCAGCC
AGCAAACAGAAATACCTGGAGAATTACCTCAACTGTCTCTTGACCATGTCTTTCTATCGC
AACTACCATGCCATGACAGAGTTCCTGGAAGTCAGTCAGCTGTCCTTTATCCCGGACTTG
GGCCGCAAAGGACTGGAGGGGATGATCCGGAAGCGCTCAGGTGGCCACCGTGTTCCTGGC
CTCACCTGCTGTGGCCGAGACCAAGTTTGTTATCGCTGGTCCAAGAGGTGGCTGGTGGTG
AAGGACTCCTTCCTGCTGTACATGTGCCTCGAGACAGGTGCCATCTCATTTGTTCAGCTC
TTTGACCCTGGCTTTGAGGTGCAAGTGGGGAAAAGGAGCACGGAGGCACGGCACGGCGTG
CGGATCGATACCTCCCACAGGTCCTTGATTCTCAAGTGCAGCAGCTACCGGCAGGCACGG
TGGTGGGCCCAAGAGATCACTGAGCTGGCACAGGGCCCAGGCAGAGACTTCCTACAGCTG
CACCGGCATGACAGCTACGCCCCACCCCGGCCTGGGACCTTGGCCCGGTGGTTTGTGAAT
GGGGCAGGTTACTTTGCTGCTGTGGCAGATGCCATCCTTCGAGCTCAAGAGGAGATTTTC
ATCACAGACTGGTGGTTGAGTCCTGAGGTTTACCTGAAGCGTCCGGCCCATTCAGATGAC
TGGAGACTGGACATTATGCTCAAGAGGAAGGCGGAGGAAGGTGTCCGTGTGTCTATTCTG
CTGTTTAAAGAAGTGGAATTGGCCTTGGGCATCAACAGTGGCTATAGCAAGAGGGCGCTG
ATGCTGCTGCACCCCAACATAAAGGTGATGCGTCACCCAGACCAAGTGACGTTGTGGGCC
CATCATGAGAAGCTCCTGGTGGTGGACCAAGTGGTAGCATTCCTGGGGGGACTGGACCTT
GCCTATGGCCGCTGGGATGACCTGCACTACCGACTGACTGACCTTGGAGACTCCTCTGAA
TCAGCTGCCTCCCAGCCTCCCACCCCGCGCCCAGACTCACCAGCCACCCCAGACCTCTCT
CACAACCAATTCTTCTGGCTGGGCAAGGACTACAGCAATCTTATCACCAAGGACTGGGTG
CAGCTGGACCGGCCTTTCGAAGATTTCATTGACAGGGAGACGACCCCTCGGATGCCATGG
CGGGACGTTGGGGTGGTCGTCCATGGCCTACCGGCCCGGGACCTTGCCCGGCACTTCATC
CAGCGCTGGAACTTCACCAAGACCACCAAGGCCAAGTACAAGACTCCCACATACCCCTAC
CTGCTTCCCAAGTCTACCAGCACGGCCAATCAGCTCCCCTTCACACTTCCAGGAGGGCAG
TGCACCACCGTACAGGTCTTGCGATCAGTGGACCGCTGGTCAGCAGGGACTCTGGAGAAC
TCCATCCTCAATGCCTACCTGCACACCATCAGGGAGAGCCAGCACTTCCTCTACATTGAG
AATCAGTTCTTCATTAGCTGCTCAGATGGGCGGACGGTTCTGAACAAGGTGGGCGATGAG
ATTGTGGACAGAATCCTGAAGGCCCACAAACAGGGGTGGTGTTACCGAGTCTACGTGCTT
TTGCCCTTACTCCCTGGCTTCGAGGGTGACATCTCCACGGGCGGTGGCAACTCCATCCAG
GCCATTCTGCACTTTACTTACAGGACCCTGTGTCGTGGGGAGTATTCAATCCTGCATCGC
CTTAAAGCAGCCATGGGGACAGCATGGCGGGACTATATTTCCATCTGCGGGCTTCGTACA
CACGGAGAGCTGGGCGGGCACCCCGTCTCGGAGCTCATCTACATCCACAGCAAGGTGCTC
ATCGCAGATGACCGGACAGTCATCATTGGTTCTGCAAACATCAATGACCGGAGCTTGCTG
GGGAAGCGGGACAGTGAGCTGGCCGTGCTGATCGAGGACACAGAGACGGAACCATCCCTC
ATGAATGGGGCAGAGTATCAGGCGGGCAGGTTTGCCTTGAGTCTGCGGAAGCACTGCTTC
GGTGTGATTCTTGGAGCAAATACCCGGCCAGACTTGGATCTCCGAGACCCCATCTGTGAT
GACTTCTTCCAGTTGTGGCAAGACATGGCTGAGAGCAACGCCAATATCTATGAGCAGATC
TTCCGCTGCCTGCCATCCAATGCCACGCGTTCCCTGCGGACTCTCCGGGAGTACGTGGCC
GTGGAGCCCTTGGCCACGGTCAGTCCCCCCTTGGCTCGGTCTGAGCTCACCCAGGTCCAG
GGCCACCTGGTCCACTTCCCCCTCAAGTTCCTAGAGGATGAGTCTTTGCTGCCCCCGCTG
GGTAGCAAGGAGGGCATGATCCCCCTAGAAGTGTGGACATAG
|
| Enzyme 24 GenBank Gene ID |
AF033850 |
| Enzyme 24 GeneCard ID |
PLD2 |
| Enzyme 24 GenAtlas ID |
PLD2 |
| Enzyme 24 HGNC ID |
HGNC:9068 |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
17p13.1 |
| Enzyme 24 SNPs |
SNPJam Report |
| Enzyme 24 General References |
- Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed ]
- Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Divecha N, Roefs M, Halstead JR, D'Andrea S, Fernandez-Borga M, Oomen L, Saqib KM, Wakelam MJ, D'Santos C: Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity. EMBO J. 2000 Oct 16;19(20):5440-9. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5313 |
| Enzyme 25 Name |
Ectonucleoside triphosphate diphosphohydrolase 1 |
| Enzyme 25 Synonyms |
- NTPDase 1
- Ecto-ATP diphosphohydrolase 1
- Ecto-ATPDase 1
- Ecto-ATPase 1
- Ecto-apyrase
- Lymphoid cell activation antigen
- CD39 antigen
|
| Enzyme 25 Gene Name |
ENTPD1 |
| Enzyme 25 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 1
MEDTKESNVKTFCSKNILAILGFSSIIAVIALLAVGLTQNKALPENVKYGIVLDAGSSHT
SLYIYKWPAEKENDTGVVHQVEECRVKGPGISKFVQKVNEIGIYLTDCMERAREVIPRSQ
HQETPVYLGATAGMRLLRMESEELADRVLDVVERSLSNYPFDFQGARIITGQEEGAYGWI
TINYLLGKFSQKTRWFSIVPYETNNQETFGALDLGGASTQVTFVPQNQTIESPDNALQFR
LYGKDYNVYTHSFLCYGKDQALWQKLAKDIQVASNEILRDPCFHPGYKKVVNVSDLYKTP
CTKRFEMTLPFQQFEIQGIGNYQQCHQSILELFNTSYCPYSQCAFNGIFLPPLQGDFGAF
SAFYFVMKFLNLTSEKVSQEKVTEMMKKFCAQPWEEIKTSYAGVKEKYLSEYCFSGTYIL
SLLLQGYHFTADSWEHIHFIGKIQGSDAGWTLGYMLNLTNMIPAEQPLSTPLSHSTYVFL
MVLFSLVLFTVAIIGLLIFHKPSYFWKDMV
|
| Enzyme 25 Number of Residues |
510 |
| Enzyme 25 Molecular Weight |
57964.1 |
| Enzyme 25 Theoretical pI |
6.29 |
| Enzyme 25 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 25 General Function |
Involved in hydrolase activity |
| Enzyme 25 Specific Function |
In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Could also be implicated in the prevention of platelet aggregation. Hydrolyzes ATP and ADP equally well |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
45580700 |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P49961 |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
ENTP1_HUMAN |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1533 bp
ATGGAAGATACAAAGGAGTCTAACGTGAAGACATTTTGCTCCAAGAATATCCTAGCCATC
CTTGGCTTCTCCTCTATCATAGCTGTGATAGCTTTGCTTGCTGTGGGGTTGACCCAGAAC
AAAGCATTGCCAGAAAACGTTAAGTATGGGATTGTGCTGGATGCGGGTTCTTCTCACACA
AGTTTATACATCTATAAGTGGCCAGCAGAAAAGGAGAATGACACAGGCGTGGTGCATCAA
GTAGAAGAATGCAGGGTTAAAGGTCCTGGAATCTCAAAATTTGTTCAGAAAGTAAATGAA
ATAGGCATTTACCTGACTGATTGCATGGAAAGAGCTAGGGAAGTGATTCCAAGGTCCCAG
CACCAAGAGACACCCGTTTACCTGGGAGCCACGGCAGGCATGCGGTTGCTCAGGATGGAA
AGTGAAGAGTTGGCAGACAGGGTTCTGGATGTGGTGGAGAGGAGCCTCAGCAACTACCCC
TTTGACTTCCAGGGTGCCAGGATCATTACTGGCCAAGAGGAAGGTGCCTATGGCTGGATT
ACTATCAACTATCTGCTGGGCAAATTCAGTCAGAAAACAAGGTGGTTCAGCATAGTCCCA
TATGAAACCAATAATCAGGAAACCTTTGGAGCTTTGGACCTTGGGGGAGCCTCTACACAA
GTCACTTTTGTACCCCAAAACCAGACTATCGAGTCCCCAGATAATGCTCTGCAATTTCGC
CTCTATGGCAAGGACTACAATGTCTACACACATAGCTTCTTGTGCTATGGGAAGGATCAG
GCACTCTGGCAGAAACTGGCCAAGGACATTCAGGTTGCAAGTAATGAAATTCTCAGGGAC
CCATGCTTTCATCCTGGATATAAGAAGGTAGTGAACGTAAGTGACCTTTACAAGACCCCC
TGCACCAAGAGATTTGAGATGACTCTTCCATTCCAGCAGTTTGAAATCCAGGGTATTGGA
AACTATCAACAATGCCATCAAAGCATCCTGGAGCTCTTCAACACCAGTTACTGCCCTTAC
TCCCAGTGTGCCTTCAATGGGATTTTCTTGCCACCACTCCAGGGGGATTTTGGGGCATTT
TCAGCTTTTTACTTTGTGATGAAGTTTTTAAACTTGACATCAGAGAAAGTCTCTCAGGAA
AAGGTGACTGAGATGATGAAAAAGTTCTGTGCTCAGCCTTGGGAGGAGATAAAAACATCT
TACGCTGGAGTAAAGGAGAAGTACCTGAGTGAATACTGCTTTTCTGGTACCTACATTCTC
TCCCTCCTTCTGCAAGGCTATCATTTCACAGCTGATTCCTGGGAGCACATCCATTTCATT
GGCAAGATCCAGGGCAGCGACGCCGGCTGGACTTTGGGCTACATGCTGAACCTGACCAAC
ATGATCCCAGCTGAGCAACCATTGTCCACACCTCTCTCCCACTCCACCTATGTCTTCCTC
ATGGTTCTATTCTCCCTGGTCCTTTTCACAGTGGCCATCATAGGCTTGCTTATCTTTCAC
AAGCCTTCATATTTCTGGAAAGATATGGTATAG
|
| Enzyme 25 GenBank Gene ID |
NM_001776.5 |
| Enzyme 25 GeneCard ID |
ENTPD1 |
| Enzyme 25 GenAtlas ID |
ENTPD1 |
| Enzyme 25 HGNC ID |
HGNC:3363 |
| Enzyme 25 Chromosome Location |
1 |
| Enzyme 25 Locus |
10q24 |
| Enzyme 25 SNPs |
SNPJam Report |
| Enzyme 25 General References |
- Maliszewski CR, Delespesse GJ, Schoenborn MA, Armitage RJ, Fanslow WC, Nakajima T, Baker E, Sutherland GR, Poindexter K, Birks C, et al.: The CD39 lymphoid cell activation antigen. Molecular cloning and structural characterization. J Immunol. 1994 Oct 15;153(8):3574-83. [PubMed ]
- Robson SC, Kaczmarek E, Siegel JB, Candinas D, Koziak K, Millan M, Hancock WW, Bach FH: Loss of ATP diphosphohydrolase activity with endothelial cell activation. J Exp Med. 1997 Jan 6;185(1):153-63. [PubMed ]
- Matsumoto M, Sakurai Y, Kokubo T, Yagi H, Makita K, Matsui T, Titani K, Fujimura Y, Narita N: The cDNA cloning of human placental ecto-ATP diphosphohydrolases I and II. FEBS Lett. 1999 Jun 25;453(3):335-40. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
- Christoforidis S, Papamarcaki T, Galaris D, Kellner R, Tsolas O: Purification and properties of human placental ATP diphosphohydrolase. Eur J Biochem. 1995 Nov 15;234(1):66-74. [PubMed ]
- Makita K, Shimoyama T, Sakurai Y, Yagi H, Matsumoto M, Narita N, Sakamoto Y, Saito S, Ikeda Y, Suzuki M, Titani K, Fujimura Y: Placental ecto-ATP diphosphohydrolase: its structural feature distinct from CD39, localization and inhibition on shear-induced platelet aggregation. Int J Hematol. 1998 Oct;68(3):297-310. [PubMed ]
- Kaczmarek E, Koziak K, Sevigny J, Siegel JB, Anrather J, Beaudoin AR, Bach FH, Robson SC: Identification and characterization of CD39/vascular ATP diphosphohydrolase. J Biol Chem. 1996 Dec 20;271(51):33116-22. [PubMed ]
- Wang TF, Guidotti G: CD39 is an ecto-(Ca2+,Mg2+)-apyrase. J Biol Chem. 1996 Apr 26;271(17):9898-901. [PubMed ]
- Koziak K, Kaczmarek E, Kittel A, Sevigny J, Blusztajn JK, Schulte Am Esch J 2nd, Imai M, Guckelberger O, Goepfert C, Qawi I, Robson SC: Palmitoylation targets CD39/endothelial ATP diphosphohydrolase to caveolae. J Biol Chem. 2000 Jan 21;275(3):2057-62. [PubMed ]
- Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5314 |
| Enzyme 26 Name |
Soluble calcium-activated nucleotidase 1 |
| Enzyme 26 Synonyms |
- SCAN-1
- Apyrase homolog
- Putative MAPK-activating protein PM09
- Putative NF-kappa-B-activating protein 107
|
| Enzyme 26 Gene Name |
CANT1 |
| Enzyme 26 Protein Sequence |
>Soluble calcium-activated nucleotidase 1
MPVQLSEHPEWNESMHSLRISVGGLPVLASMTKAADPRFRPRWKVILTFFVGAAILWLLC
SHRPAPGRPPTHNAHNWRLGQAPANWYNDTYPLSPPQRTPAGIRYRIAVIADLDTESRAQ
EENTWFSYLKKGYLTLSDSGDKVAVEWDKDHGVLESHLAEKGRGMELSDLIVFNGKLYSV
DDRTGVVYQIEGSKAVPWVILSDGDGTVEKGFKAEWLAVKDERLYVGGLGKEWTTTTGDV
VNENPEWVKVVGYKGSVDHENWVSNYNALRAAAGIQPPGYLIHESACWSDTLQRWFFLPR
RASQERYSEKDDERKGANLLLSASPDFGDIAVSHVGAVVPTHGFSSFKFIPNTDDQIIVA
LKSEEDSGRVASYIMAFTLDGRFLLPETKIGSVKYEGIEFI
|
| Enzyme 26 Number of Residues |
401 |
| Enzyme 26 Molecular Weight |
44839.2 |
| Enzyme 26 Theoretical pI |
5.98 |
| Enzyme 26 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- ion binding
- metal ion binding
- pyrophosphatase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in calcium ion binding |
| Enzyme 26 Specific Function |
Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP |
| Enzyme 26 Pathways |
|
| Enzyme 26 Reactions |
- a nucleoside diphosphate + H2O = a nucleotide + phosphate [RN:R00329]
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
229577440 |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q8WVQ1 |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
CANT1_HUMAN |
| Enzyme 26 PDB ID |
1S1D |
| Enzyme 26 PDB File |
Show |
| Enzyme 26 3D Structure |
|
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1206 bp
ATGCCCGTGCAGCTGTCTGAGCACCCGGAATGGAATGAGTCTATGCACTCCCTCCGGATC
AGTGTGGGGGGCCTTCCTGTGCTGGCGTCCATGACCAAGGCCGCGGACCCCCGCTTCCGC
CCCCGCTGGAAGGTGATCCTGACGTTCTTTGTGGGTGCTGCCATCCTCTGGCTGCTCTGC
TCCCACCGCCCGGCCCCCGGCAGGCCCCCCACCCACAATGCACACAACTGGAGGCTCGGC
CAGGCGCCCGCCAACTGGTACAATGACACCTACCCCCTGTCTCCCCCACAAAGGACACCG
GCTGGGATTCGGTATCGAATCGCAGTTATCGCAGACCTGGACACAGAGTCAAGGGCCCAA
GAGGAAAACACCTGGTTCAGTTACCTGAAAAAGGGCTACCTGACCCTGTCAGACAGTGGG
GACAAGGTGGCCGTGGAATGGGACAAAGACCATGGGGTCCTGGAGTCCCACCTGGCGGAG
AAGGGGAGAGGCATGGAGCTATCCGACCTGATTGTTTTCAATGGGAAACTCTACTCCGTG
GATGACCGGACGGGGGTCGTCTACCAGATCGAAGGCAGCAAAGCCGTGCCCTGGGTGATT
CTGTCCGACGGCGACGGCACCGTGGAGAAAGGCTTCAAGGCCGAATGGCTGGCAGTGAAG
GACGAGCGTCTGTACGTGGGCGGCCTGGGCAAGGAGTGGACGACCACTACGGGTGATGTG
GTGAACGAGAACCCGGAGTGGGTGAAGGTGGTGGGCTACAAGGGCAGCGTGGACCACGAG
AACTGGGTGTCCAACTACAACGCCCTGCGGGCTGCTGCCGGCATCCAGCCGCCAGGCTAC
CTCATCCATGAGTCTGCCTGCTGGAGTGACACGCTGCAGCGCTGGTTCTTCCTGCCGCGC
CGCGCCAGCCAGGAGCGCTACAGCGAGAAGGACGACGAGCGCAAGGGCGCCAACCTGCTG
CTGAGCGCCTCCCCTGACTTCGGCGACATCGCTGTGAGCCACGTCGGGGCGGTGGTCCCC
ACTCACGGCTTCTCGTCCTTCAAGTTCATCCCCAACACCGACGACCAGATCATTGTGGCC
CTCAAATCCGAGGAGGACAGCGGCAGAGTCGCCTCCTACATCATGGCCTTCACGCTGGAC
GGGCGCTTCCTGTTGCCGGAGACCAAGATCGGAAGCGTGAAATACGAAGGCATCGAGTTC
ATTTAA
|
| Enzyme 26 GenBank Gene ID |
NM_001159772.1 |
| Enzyme 26 GeneCard ID |
CANT1 |
| Enzyme 26 GenAtlas ID |
CANT1 |
| Enzyme 26 HGNC ID |
HGNC:19721 |
| Enzyme 26 Chromosome Location |
1 |
| Enzyme 26 Locus |
17q25.3 |
| Enzyme 26 SNPs |
SNPJam Report |
| Enzyme 26 General References |
- Smith TM, Hicks-Berger CA, Kim S, Kirley TL: Cloning, expression, and characterization of a soluble calcium-activated nucleotidase, a human enzyme belonging to a new family of extracellular nucleotidases. Arch Biochem Biophys. 2002 Oct 1;406(1):105-15. [PubMed ]
- Matsuda A, Suzuki Y, Honda G, Muramatsu S, Matsuzaki O, Nagano Y, Doi T, Shimotohno K, Harada T, Nishida E, Hayashi H, Sugano S: Large-scale identification and characterization of human genes that activate NF-kappaB and MAPK signaling pathways. Oncogene. 2003 May 22;22(21):3307-18. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Failer BU, Braun N, Zimmermann H: Cloning, expression, and functional characterization of a Ca(2+)-dependent endoplasmic reticulum nucleoside diphosphatase. J Biol Chem. 2002 Oct 4;277(40):36978-86. Epub 2002 Aug 6. [PubMed ]
- Yang M, Kirley TL: Site-directed mutagenesis of human soluble calcium-activated nucleotidase 1 (hSCAN-1): identification of residues essential for enzyme activity and the Ca(2+)-induced conformational change. Biochemistry. 2004 Jul 20;43(28):9185-94. [PubMed ]
- Dai J, Liu J, Deng Y, Smith TM, Lu M: Structure and protein design of a human platelet function inhibitor. Cell. 2004 Mar 5;116(5):649-59. [PubMed ]
- Huber C, Oules B, Bertoli M, Chami M, Fradin M, Alanay Y, Al-Gazali LI, Ausems MG, Bitoun P, Cavalcanti DP, Krebs A, Le Merrer M, Mortier G, Shafeghati Y, Superti-Furga A, Robertson SP, Le Goff C, Muda AO, Paterlini-Brechot P, Munnich A, Cormier-Daire V: Identification of CANT1 mutations in Desbuquois dysplasia. Am J Hum Genet. 2009 Nov;85(5):706-10. Epub 2009 Oct 22. [PubMed ]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5318 |
| Enzyme 27 Name |
Ectonucleoside triphosphate diphosphohydrolase 3 |
| Enzyme 27 Synonyms |
- NTPDase 3
- CD39 antigen-like 3
- Ecto-ATP diphosphohydrolase 3
- Ecto-ATPDase 3
- Ecto-ATPase 3
- Ecto-apyrase 3
- HB6
|
| Enzyme 27 Gene Name |
ENTPD3 |
| Enzyme 27 Protein Sequence |
>Ectonucleoside triphosphate diphosphohydrolase 3
MFTVLTRQPCEQAGLKALYRTPTIIALVVLLVSIVVLVSITVIQIHKQEVLPPGLKYGIV
LDAGSSRTTVYVYQWPAEKENNTGVVSQTFKCSVKGSGISSYGNNPQDVPRAFEECMQKV
KGQVPSHLHGSTPIHLGATAGMRLLRLQNETAANEVLESIQSYFKSQPFDFRGAQIISGQ
EEGVYGWITANYLMGNFLEKNLWHMWVHPHGVETTGALDLGGASTQISFVAGEKMDLNTS
DIMQVSLYGYVYTLYTHSFQCYGRNEAEKKFLAMLLQNSPTKNHLTNPCYPRDYSISFTM
GHVFDSLCTVDQRPESYNPNDVITFEGTGDPSLCKEKVASIFDFKACHDQETCSFDGVYQ
PKIKGPFVAFAGFYYTASALNLSGSFSLDTFNSSTWNFCSQNWSQLPLLLPKFDEVYARS
YCFSANYIYHLFVNGYKFTEETWPQIHFEKEVGNSSIAWSLGYMLSLTNQIPAESPLIRL
PIEPPVFVGTLAFFTAAALLCLAFLAYLCSATRRKRHSEHAFDHAVDSD
|
| Enzyme 27 Number of Residues |
529 |
| Enzyme 27 Molecular Weight |
59104.8 |
| Enzyme 27 Theoretical pI |
6.40 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 27 General Function |
Involved in hydrolase activity |
| Enzyme 27 Specific Function |
Has a threefold preference for the hydrolysis of ATP over ADP |
| Enzyme 27 Pathways |
|
| Enzyme 27 Reactions |
- ATP + 2 H2O = AMP + 2 phosphate [RN:R00085]
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
13817037 |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
O75355 |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
ENTP3_HUMAN |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1590 bp
ATGTTCACTGTGCTGACCCGCCAACCATGTGAGCAAGCAGGCCTCAAGGCCCTCTACCGA
ACTCCAACCATCATTGCCTTGGTGGTCTTGCTTGTGAGTATTGTGGTACTTGTGAGTATC
ACTGTCATCCAGATCCACAAGCAAGAGGTCCTCCCTCCAGGACTGAAGTATGGTATTGTG
CTGGATGCCGGGTCTTCAAGAACCACAGTCTACGTGTATCAATGGCCAGCAGAAAAAGAG
AATAATACCGGAGTGGTCAGTCAAACCTTCAAATGTAGTGTGAAAGGCTCTGGAATCTCC
AGCTATGGAAATAACCCCCAAGATGTCCCCAGAGCCTTTGAGGAGTGTATGCAAAAAGTC
AAGGGGCAGGTTCCATCCCACCTCCACGGATCCACCCCCATTCACCTGGGAGCCACGGCT
GGGATGCGCTTGCTGAGGTTGCAAAATGAAACAGCAGCTAATGAAGTCCTTGAAAGCATC
CAAAGCTACTTCAAGTCCCAGCCCTTTGACTTTAGGGGTGCTCAAATCATTTCTGGGCAA
GAAGAAGGGGTATATGGATGGATTACAGCCAACTATTTAATGGGAAATTTCCTGGAGAAG
AACCTGTGGCACATGTGGGTGCACCCGCATGGAGTGGAAACCACGGGTGCCCTGGACTTA
GGTGGTGCCTCCACCCAAATATCCTTCGTGGCAGGAGAGAAGATGGATCTGAACACCAGC
GACATCATGCAGGTGTCCCTGTATGGCTACGTATACACGCTCTACACACACAGCTTCCAG
TGCTATGGCCGGAATGAGGCTGAGAAGAAGTTTCTGGCAATGCTCCTGCAGAATTCTCCT
ACCAAAAACCATCTCACCAATCCCTGTTACCCTCGGGATTATAGCATCAGCTTCACCATG
GGCCATGTATTTGATAGCCTGTGCACTGTGGACCAGAGGCCAGAAAGTTATAACCCCAAT
GATGTCATCACTTTTGAAGGAACTGGGGACCCATCTCTGTGTAAGGAGAAGGTGGCTTCC
ATATTTGACTTCAAAGCTTGCCATGATCAAGAAACCTGTTCTTTTGATGGGGTTTATCAG
CCAAAGATTAAAGGGCCATTTGTGGCTTTTGCAGGATTCTACTACACAGCCAGTGCTTTA
AATCTTTCAGGTAGCTTTTCCCTGGACACCTTCAACTCCAGCACCTGGAATTTCTGCTCA
CAGAATTGGAGTCAGCTCCCACTGCTGCTCCCCAAATTTGATGAGGTATATGCCCGCTCT
TACTGCTTCTCAGCCAACTACATCTACCACTTGTTTGTGAACGGTTACAAATTCACAGAG
GAGACTTGGCCCCAAATACACTTTGAAAAAGAAGTGGGGAATAGCAGCATAGCCTGGTCT
CTTGGCTACATGCTCAGCCTGACCAACCAGATCCCAGCTGAAAGCCCTCTGATCCGTCTG
CCCATAGAACCACCTGTCTTTGTGGGCACCCTCGCTTTCTTCACAGCGGCAGCCTTGCTG
TGTCTGGCATTTCTTGCATACCTGTGTTCAGCAACCAGAAGAAAGAGGCACTCCGAGCAT
GCCTTTGACCATGCAGTGGATTCTGACTGA
|
| Enzyme 27 GenBank Gene ID |
AF034840 |
| Enzyme 27 GeneCard ID |
ENTPD3 |
| Enzyme 27 GenAtlas ID |
ENTPD3 |
| Enzyme 27 HGNC ID |
HGNC:3365 |
| Enzyme 27 Chromosome Location |
3 |
| Enzyme 27 Locus |
3p21.3 |
| Enzyme 27 SNPs |
SNPJam Report |
| Enzyme 27 General References |
- Chadwick BP, Frischauf AM: The CD39-like gene family: identification of three new human members (CD39L2, CD39L3, and CD39L4), their murine homologues, and a member of the gene family from Drosophila melanogaster. Genomics. 1998 Jun 15;50(3):357-67. [PubMed ]
- Smith TM, Kirley TL: Cloning, sequencing, and expression of a human brain ecto-apyrase related to both the ecto-ATPases and CD39 ecto-apyrases1. Biochim Biophys Acta. 1998 Jul 28;1386(1):65-78. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Smith TM, Lewis Carl SA, Kirley TL: Mutagenesis of two conserved tryptophan residues of the E-type ATPases: inactivation and conversion of an ecto-apyrase to an ecto-NTPase. Biochemistry. 1999 May 4;38(18):5849-57. [PubMed ]
- Yang F, Hicks-Berger CA, Smith TM, Kirley TL: Site-directed mutagenesis of human nucleoside triphosphate diphosphohydrolase 3: the importance of residues in the apyrase conserved regions. Biochemistry. 2001 Apr 3;40(13):3943-50. [PubMed ]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5319 |
| Enzyme 28 Name |
Tyrosinase |
| Enzyme 28 Synonyms |
- LB24-AB
- Monophenol monooxygenase
- SK29-AB
- Tumor rejection antigen AB
|
| Enzyme 28 Gene Name |
TYR |
| Enzyme 28 Protein Sequence |
>Tyrosinase
MLLAVLYCLLWSFQTSAGHFPRACVSSKNLMEKECCPPWSGDRSPCGQLSGRGSCQNILL
SNAPLGPQFPFTGVDDRESWPSVFYNRTCQCSGNFMGFNCGNCKFGFWGPNCTERRLLVR
RNIFDLSAPEKDKFFAYLTLAKHTISSDYVIPIGTYGQMKNGSTPMFNDINIYDLFVWMH
YYVSMDALLGGSEIWRDIDFAHEAPAFLPWHRLFLLRWEQEIQKLTGDENFTIPYWDWRD
AEKCDICTDEYMGGQHPTNPNLLSPASFFSSWQIVCSRLEEYNSHQSLCNGTPEGPLRRN
PGNHDKSRTPRLPSSADVEFCLSLTQYESGSMDKAANFSFRNTLEGFASPLTGIADASQS
SMHNALHIYMNGTMSQVQGSANDPIFLLHHAFVDSIFEQWLRRHRPLQEVYPEANAPIGH
NRESYMVPFIPLYRNGDFFISSKDLGYDYSYLQDSDPDSFQDYIKSYLEQASRIWSWLLG
AAMVGAVLTALLAGLVSLLCRHKRKQLPEEKQPLLMEKEDYHSLYQSHL
|
| Enzyme 28 Number of Residues |
529 |
| Enzyme 28 Molecular Weight |
60392.7 |
| Enzyme 28 Theoretical pI |
6.05 |
| Enzyme 28 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 28 General Function |
Involved in oxidoreductase activity |
| Enzyme 28 Specific Function |
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6-dihydroxyindole to indole-5,6 quinone |
| Enzyme 28 Pathways |
- Riboflavin Metabolism (map00740 )
- Stilbene, coumarine and lignin biosynthesis (map00940 )
- Tyrosine Metabolism (map00350 )
|
| Enzyme 28 Reactions |
- L-tyrosine + L-dopa + O2 = L-dopa + dopaquinone + H2O [RN:R02078]
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
340037 |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
P14679 |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
TYRO_HUMAN |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>1590 bp
ATGCTCCTGGCTGTTTTGTACTGCCTGCTGTGGAGTTTCCAGACCTCCGCTGGCCATTTC
CCTAGAGCCTGTGTCTCCTCTAAGAACCTGATGGAGAAGGAATGCTGTCCACCGTGGAGC
GGGGACAGGAGTCCCTGTGGCCAGCTTTCAGGCAGAGGTTCCTGTCAGAATATCCTTCTG
TCCAATGCACCACTTGGGCCTCAATTTCCCTTCACAGGGGTGGATGACCGGGAGTCGTGG
CCTTCCGTCTTTTATAATAGGACCTGCCAGTGCTCTGGCAACTTCATGGGATTCAACTGT
GGAAACTGCAAGTTTGGCTTTTGGGGACCAAACTGCACAGAGAGACGACTCTTGGTGAGA
AGAAACATCTTCGATTTGAGTGCCCCAGAGAAGGACAAATTTTTTGCCTACCTCACTTTA
GCAAAGCATACCATCAGCTCAGACTATGTCATCCCCATAGGGACCTATGGCCAAATGAAA
AATGGATCAACACCCATGTTTAACGACATCAATATTTATGACCTCTTTGTCTGGATGCAT
TATTATGTGTCAATGGATGCACTGCTTGGGGGATCTGAAATCTGGAGAGACATTGATTTT
GCCCATGAAGCACCAGCTTTTCTGCCTTGGCATAGACTCTTCTTGTTGCGGTGGGAACAA
GAAATCCAGAAGCTGACAGGAGATGAAAACTTCACTATTCCATATTGGGACTGGCGGGAT
GCAGAAAAGTGTGACATTTGCACAGATGAGTACATGGGAGGTCAGCACCCCACAAATCCT
AACTTACTCAGCCCAGCATCATTCTTCTCCTCTTGGCAGATTGTCTGTAGCCGATTGGAG
GAGTACAACAGCCATCAGTCTTTATGCAATGGAACGCCCGAGGGACCTTTACGGCGTAAT
CCTGGAAACCATGACAAATCCAGAACCCCAAGGCTCCCCTCTTCAGCTGATGTAGAATTT
TGCCTGAGTTTGACCCAATATGAATCTGGTTCCATGGATAAAGCTGCCAATTTCAGCTTT
AGAAATACACTGGAAGGATTTGCTAGTCCACTTACTGGGATAGCGGATGCCTCTCAAAGC
AGCATGCACAATGCCTTGCACATCTATATGAATGGAACAATGTCCCAGGTACAGGGATCT
GCCAACGATCCTATCTTCCTTCTTCACCATGCATTTGTTGACAGTATTTTTGAGCAGTGG
CTCCGAAGGCACCGTCCTCTTCAAGAAGTTTATCCAGAAGCCAATGCACCCATTGGACAT
AACCGGGAATCCTACATGGTTCCTTTTATACCACTGTACAGAAATGGTGATTTCTTTATT
TCATCCAAAGATCTGGGCTATGACTATAGCTATCTACAAGATTCAGACCCAGACTCTTTT
CAAGACTACATTAAGTCCTATTTGGAACAAGCGAGTCGGATCTGGTCATGGCTCCTTGGG
GCGGCGATGGTAGGGGCCGTCCTCACTGCCCTGCTGGCAGGGCTTGTGAGCTTGCTGTGT
CGTCACAAGAGAAAGCAGCTTCCTGAAGAAAAGCAGCCACTCCTCATGGAGAAAGAGGAT
TACCACAGCTTGTATCAGAGCCATTTATAA
|
| Enzyme 28 GenBank Gene ID |
M27160 |
| Enzyme 28 GeneCard ID |
TYR |
| Enzyme 28 GenAtlas ID |
TYR |
| Enzyme 28 HGNC ID |
HGNC:12442 |
| Enzyme 28 Chromosome Location |
1 |
| Enzyme 28 Locus |
11q14-q21 |
| Enzyme 28 SNPs |
SNPJam Report |
| Enzyme 28 General References |
- Giebel LB, Strunk KM, Spritz RA: Organization and nucleotide sequences of the human tyrosinase gene and a truncated tyrosinase-related segment. Genomics. 1991 Mar;9(3):435-45. [PubMed ]
- Kwon BS, Haq AK, Pomerantz SH, Halaban R: Isolation and sequence of a cDNA clone for human tyrosinase that maps at the mouse c-albino locus. Proc Natl Acad Sci U S A. 1987 Nov;84(21):7473-7. [PubMed ]
- Bouchard B, Fuller BB, Vijayasaradhi S, Houghton AN: Induction of pigmentation in mouse fibroblasts by expression of human tyrosinase cDNA. J Exp Med. 1989 Jun 1;169(6):2029-42. [PubMed ]
- Chintamaneni CD, Halaban R, Kobayashi Y, Witkop CJ Jr, Kwon BS: A single base insertion in the putative transmembrane domain of the tyrosinase gene as a cause for tyrosinase-negative oculocutaneous albinism. Proc Natl Acad Sci U S A. 1991 Jun 15;88(12):5272-6. [PubMed ]
- Brichard V, Van Pel A, Wolfel T, Wolfel C, De Plaen E, Lethe B, Coulie P, Boon T: The tyrosinase gene codes for an antigen recognized by autologous cytolytic T lymphocytes on HLA-A2 melanomas. J Exp Med. 1993 Aug 1;178(2):489-95. [PubMed ]
- Martinez-Arias R, Comas D, Andres A, Abello MT, Domingo-Roura X, Bertranpetit J: The tyrosinase gene in gorillas and the albinism of 'Snowflake'. Pigment Cell Res. 2000 Dec;13(6):467-70. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Kikuchi H, Miura H, Yamamoto H, Takeuchi T, Dei T, Watanabe M: Characteristic sequences in the upstream region of the human tyrosinase gene. Biochim Biophys Acta. 1989 Dec 22;1009(3):283-6. [PubMed ]
- Takeda A, Tomita Y, Okinaga S, Tagami H, Shibahara S: Functional analysis of the cDNA encoding human tyrosinase precursor. Biochem Biophys Res Commun. 1989 Aug 15;162(3):984-90. [PubMed ]
- Murphy WJ, Eizirik E, Johnson WE, Zhang YP, Ryder OA, O'Brien SJ: Molecular phylogenetics and the origins of placental mammals. Nature. 2001 Feb 1;409(6820):614-8. [PubMed ]
- Oetting WS, King RA: Molecular basis of type I (tyrosinase-related) oculocutaneous albinism: mutations and polymorphisms of the human tyrosinase gene. Hum Mutat. 1993;2(1):1-6. [PubMed ]
- Oetting WS, King RA: Molecular basis of albinism: mutations and polymorphisms of pigmentation genes associated with albinism. Hum Mutat. 1999;13(2):99-115. [PubMed ]
- Basrur V, Yang F, Kushimoto T, Higashimoto Y, Yasumoto K, Valencia J, Muller J, Vieira WD, Watabe H, Shabanowitz J, Hearing VJ, Hunt DF, Appella E: Proteomic analysis of early melanosomes: identification of novel melanosomal proteins. J Proteome Res. 2003 Jan-Feb;2(1):69-79. [PubMed ]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed ]
- Spritz RA, Strunk KM, Giebel LB, King RA: Detection of mutations in the tyrosinase gene in a patient with type IA oculocutaneous albinism. N Engl J Med. 1990 Jun 14;322(24):1724-8. [PubMed ]
- Giebel LB, Strunk KM, King RA, Hanifin JM, Spritz RA: A frequent tyrosinase gene mutation in classic, tyrosinase-negative (type IA) oculocutaneous albinism. Proc Natl Acad Sci U S A. 1990 May;87(9):3255-8. [PubMed ]
- Giebel LB, Tripathi RK, Strunk KM, Hanifin JM, Jackson CE, King RA, Spritz RA: Tyrosinase gene mutations associated with type IB ("yellow") oculocutaneous albinism. Am J Hum Genet. 1991 Jun;48(6):1159-67. [PubMed ]
- Tripathi RK, Strunk KM, Giebel LB, Weleber RG, Spritz RA: Tyrosinase gene mutations in type I (tyrosinase-deficient) oculocutaneous albinism define two clusters of missense substitutions. Am J Med Genet. 1992 Jul 15;43(5):865-71. [PubMed ]
- Spritz RA, Strunk KM, Hsieh CL, Sekhon GS, Francke U: Homozygous tyrosinase gene mutation in an American black with tyrosinase-negative (type IA) oculocutaneous albinism. Am J Hum Genet. 1991 Feb;48(2):318-24. [PubMed ]
- Giebel LB, Tripathi RK, King RA, Spritz RA: A tyrosinase gene missense mutation in temperature-sensitive type I oculocutaneous albinism. A human homologue to the Siamese cat and the Himalayan mouse. J Clin Invest. 1991 Mar;87(3):1119-22. [PubMed ]
- King RA, Mentink MM, Oetting WS: Non-random distribution of missense mutations within the human tyrosinase gene in type I (tyrosinase-related) oculocutaneous albinism. Mol Biol Med. 1991 Feb;8(1):19-29. [PubMed ]
- Oetting WS, King RA: Molecular analysis of type I-A (tyrosinase negative) oculocutaneous albinism. Hum Genet. 1992 Nov;90(3):258-62. [PubMed ]
- Tripathi RK, Bundey S, Musarella MA, Droetto S, Strunk KM, Holmes SA, Spritz RA: Mutations of the tyrosinase gene in Indo-Pakistani patients with type I (tyrosinase-deficient) oculocutaneous albinism (OCA). Am J Hum Genet. 1993 Dec;53(6):1173-9. [PubMed ]
- Gershoni-Baruch R, Rosenmann A, Droetto S, Holmes S, Tripathi RK, Spritz RA: Mutations of the tyrosinase gene in patients with oculocutaneous albinism from various ethnic groups in Israel. Am J Hum Genet. 1994 Apr;54(4):586-94. [PubMed ]
- Breimer LH, Winder AF, Jay B, Jay M: Initiation codon mutation of the tyrosinase gene as a cause of human albinism. Clin Chim Acta. 1994 Jun;227(1-2):17-22. [PubMed ]
- Summers CG, Oetting WS, King RA: Diagnosis of oculocutaneous albinism with molecular analysis. Am J Ophthalmol. 1996 Jun;121(6):724-6. [PubMed ]
- Morell R, Spritz RA, Ho L, Pierpont J, Guo W, Friedman TB, Asher JH Jr: Apparent digenic inheritance of Waardenburg syndrome type 2 (WS2) and autosomal recessive ocular albinism (AROA). Hum Mol Genet. 1997 May;6(5):659-64. [PubMed ]
- Spritz RA, Oh J, Fukai K, Holmes SA, Ho L, Chitayat D, France TD, Musarella MA, Orlow SJ, Schnur RE, Weleber RG, Levin AV: Novel mutations of the tyrosinase (TYR) gene in type I oculocutaneous albinism (OCA1). Hum Mutat. 1997;10(2):171-4. [PubMed ]
- Oetting WS, Fryer JP, King RA: Mutations of the human tyrosinase gene associated with tyrosinase related oculocutaneous albinism (OCA1). Mutations in brief no. 204. Online. Hum Mutat. 1998;12(6):433-4. [PubMed ]
- Passmore LA, Kaesmann-Kellner B, Weber BH: Novel and recurrent mutations in the tyrosinase gene and the P gene in the German albino population. Hum Genet. 1999 Sep;105(3):200-10. [PubMed ]
- Tsai CH, Tsai FJ, Wu JY, Lin SP, Chang JG, Yang CF, Lee CC: Insertion/deletion mutations of type I oculocutaneous albinism in chinese patients from Taiwan. Hum Mutat. 1999 Dec;14(6):542. [PubMed ]
- Camand O, Marchant D, Boutboul S, Pequignot M, Odent S, Dollfus H, Sutherland J, Levin A, Menasche M, Marsac C, Dufier JL, Heon E, Abitbol M: Mutation analysis of the tyrosinase gene in oculocutaneous albinism. Hum Mutat. 2001 Apr;17(4):352. [PubMed ]
- Nakamura E, Miyamura Y, Matsunaga J, Kano Y, Dakeishi-Hara M, Tanita M, Kono M, Tomita Y: A novel mutation of the tyrosinase gene causing oculocutaneous albinism type 1 (OCA1). J Dermatol Sci. 2002 Feb;28(2):102-5. [PubMed ]
- Opitz S, Kasmann-Kellner B, Kaufmann M, Schwinger E, Zuhlke C: Detection of 53 novel DNA variations within the tyrosinase gene and accumulation of mutations in 17 patients with albinism. Hum Mutat. 2004 Jun;23(6):630-1. [PubMed ]
- Stokowski RP, Pant PV, Dadd T, Fereday A, Hinds DA, Jarman C, Filsell W, Ginger RS, Green MR, van der Ouderaa FJ, Cox DR: A genomewide association study of skin pigmentation in a South Asian population. Am J Hum Genet. 2007 Dec;81(6):1119-32. Epub 2007 Oct 15. [PubMed ]
- Sulem P, Gudbjartsson DF, Stacey SN, Helgason A, Rafnar T, Magnusson KP, Manolescu A, Karason A, Palsson A, Thorleifsson G, Jakobsdottir M, Steinberg S, Palsson S, Jonasson F, Sigurgeirsson B, Thorisdottir K, Ragnarsson R, Benediktsdottir KR, Aben KK, Kiemeney LA, Olafsson JH, Gulcher J, Kong A, Thorsteinsdottir U, Stefansson K: Genetic determinants of hair, eye and skin pigmentation in Europeans. Nat Genet. 2007 Dec;39(12):1443-52. Epub 2007 Oct 21. [PubMed ]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5321 |
| Enzyme 29 Name |
Serum paraoxonase/lactonase 3 |
| Enzyme 29 Synonyms |
Not Available |
| Enzyme 29 Gene Name |
PON3 |
| Enzyme 29 Protein Sequence |
>Serum paraoxonase/lactonase 3
MGKLVALVLLGVGLSLVGEMFLAFRERVNASREVEPVEPENCHLIEELESGSEDIDILPS
GLAFISSGLKYPGMPNFAPDEPGKIFLMDLNEQNPRAQALEISGGFDKELFNPHGISIFI
DKDNTVYLYVVNHPHMKSTVEIFKFEEQQRSLVYLKTIKHELLKSVNDIVVLGPEQFYAT
RDHYFTNSLLSFFEMILDLRWTYVLFYSPREVKVVAKGFCSANGITVSADQKYVYVADVA
AKNIHIMEKHDNWDLTQLKVIQLGTLVDNLTVDPATGDILAGCHPNPMKLLNYNPEDPPG
SEVLRIQNVLSEKPRVSTVYANNGSVLQGTSVASVYHGKILIGTVFHKTLYCEL
|
| Enzyme 29 Number of Residues |
354 |
| Enzyme 29 Molecular Weight |
39607.2 |
| Enzyme 29 Theoretical pI |
5.10 |
| Enzyme 29 GO Classification |
| Function |
- arylesterase activity
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
|
|
| Enzyme 29 General Function |
Involved in arylesterase activity |
| Enzyme 29 Specific Function |
Has low activity towards the organophosphate paraxon and aromatic carboxylic acid esters. Rapidly hydrolyzes lactones such as statin prodrugs (e.g. lovastatin). Hydrolyzes aromatic lactones and 5- or 6-member ring lactones with aliphatic substituents but not simple lactones or those with polar substituents |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
- an aryl dialkyl phosphate + H2O = dialkyl phosphate + an aryl alcohol [RN:R03979]
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
29788996 |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q15166 |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
PON3_HUMAN |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1065 bp
ATGGGGAAGCTCGTGGCGCTGGTCCTGCTGGGGGTCGGCCTGTCCTTAGTCGGGGAGATG
TTCCTGGCGTTTAGAGAAAGGGTGAATGCCTCTCGAGAAGTGGAGCCAGTAGAACCTGAA
AACTGCCACCTTATTGAGGAACTTGAAAGTGGCTCTGAAGATATTGATATACTTCCTAGT
GGGCTGGCTTTTATCTCCAGTGGATTAAAATATCCAGGCATGCCAAACTTTGCGCCAGAT
GAACCAGGAAAAATCTTCTTGATGGATCTGAATGAACAAAACCCAAGGGCACAAGCGCTA
GAAATCAGTGGTGGATTTGACAAAGAATTATTTAATCCACATGGGATCAGTATTTTCATC
GACAAAGACAATACTGTGTATCTTTATGTTGTGAATCATCCCCACATGAAGTCCACTGTG
GAGATATTTAAATTTGAGGAACAACAACGTTCTCTGGTATACCTGAAAACTATAAAACAT
GAACTTCTCAAAAGTGTGAATGACATTGTGGTTCTTGGACCAGAACAGTTCTATGCCACC
AGAGACCACTATTTTACCAACTCCCTCCTGTCATTTTTTGAGATGATCTTGGATCTTCGC
TGGACTTATGTTCTTTTCTACAGCCCAAGGGAGGTTAAAGTGGTGGCCAAAGGATTTTGT
AGTGCCAATGGGATCACAGTCTCAGCAGACCAGAAGTATGTCTATGTAGCTGATGTAGCA
GCTAAGAACATTCACATAATGGAAAAACATGATAACTGGGATTTAACTCAACTGAAGGTG
ATACAGTTGGGCACCTTAGTGGATAACCTGACTGTCGATCCTGCCACAGGAGACATTTTG
GCAGGATGCCATCCTAATCCTATGAAGCTACTGAACTATAACCCTGAGGACCCTCCAGGA
TCAGAAGTACTTCGCATCCAGAATGTTTTGTCTGAGAAGCCCAGGGTGAGCACCGTGTAT
GCCAACAATGGCTCTGTGCTTCAGGGCACCTCTGTGGCTTCTGTGTACCATGGGAAAATT
CTCATAGGCACCGTATTTCACAAAACTCTGTACTGTGAGCTCTAG
|
| Enzyme 29 GenBank Gene ID |
NM_000940.2 |
| Enzyme 29 GeneCard ID |
PON3 |
| Enzyme 29 GenAtlas ID |
PON3 |
| Enzyme 29 HGNC ID |
HGNC:9206 |
| Enzyme 29 Chromosome Location |
7 |
| Enzyme 29 Locus |
7q21.3 |
| Enzyme 29 SNPs |
SNPJam Report |
| Enzyme 29 General References |
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Primo-Parmo SL, Sorenson RC, Teiber J, La Du BN: The human serum paraoxonase/arylesterase gene (PON1) is one member of a multigene family. Genomics. 1996 May 1;33(3):498-507. [PubMed ]
- Draganov DI, Teiber JF, Speelman A, Osawa Y, Sunahara R, La Du BN: Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities. J Lipid Res. 2005 Jun;46(6):1239-47. Epub 2005 Mar 16. [PubMed ]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5322 |
| Enzyme 30 Name |
Alkaline phosphatase, placental type |
| Enzyme 30 Synonyms |
- Alkaline phosphatase Regan isozyme
- Placental alkaline phosphatase 1
- PLAP-1
|
| Enzyme 30 Gene Name |
ALPP |
| Enzyme 30 Protein Sequence |
>Alkaline phosphatase, placental type
MLGPCMLLLLLLLGLRLQLSLGIIPVEEENPDFWNREAAEALGAAKKLQPAQTAAKNLII
FLGDGMGVSTVTAARILKGQKKDKLGPEIPLAMDRFPYVALSKTYNVDKHVPDSGATATA
YLCGVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAG
TYAHTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFRMGTPDPEYP
DDYSQGGTRLDGKNLVQEWLAKRQGARYVWNRTELMQASLDPSVTHLMGLFEPGDMKYEI
HRDSTLDPSLMEMTEAALRLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAI
ERAGQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPG
YVLKDGARPDVTESESGSPEYRQQSAVPLDEETHAGEDVAVFARGPQAHLVHGVQEQTFI
AHVMAFAACLEPYTACDLAPPAGTTDAAHPGRSVVPALLPLLAGTLLLLETATAP
|
| Enzyme 30 Number of Residues |
535 |
| Enzyme 30 Molecular Weight |
57953.3 |
| Enzyme 30 Theoretical pI |
6.24 |
| Enzyme 30 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 30 General Function |
Involved in catalytic activity |
| Enzyme 30 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 30 Pathways |
- Folate and Pterine Biosynthesis (map00790 )
- gamma-Hexachlorocyclohexane Degradation (map00361 )
|
| Enzyme 30 Reactions |
- a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
178474 |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
P05187 |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
PPB1_HUMAN |
| Enzyme 30 PDB ID |
1EW2 |
| Enzyme 30 PDB File |
Show |
| Enzyme 30 3D Structure |
|
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>1608 bp
ATGCTGGGGCCCTGCATGCTGCTGCTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCC
CTGGGCATCATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCGAGGCAGCCGAG
GCCCTGGGTGCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATC
TTCCTGGGCGATGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAG
AAGAAGGACAAACTGGGGCCTGAGATACCCCTGGCCATGGACCGCTTCCCATATGTGGCT
CTGTCCAAGACATACAATGTAGACAAACATGTGCCAGACAGTGGAGCCACAGCCACGGCC
TACCTGTGCGGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTT
AACCAGTGCAACACGACACGCGGCAACGAGGTCATCTCCGTGATGAATCGGGCCAAGAAA
GCAGGGAAGTCAGTGGGAGTGGTAACCACCACACGAGTGCAGCACGCCTCGCCAGCCGGC
ACCTACGCCCACACGGTGAACCGCAACTGGTACTCGGACGCCGACGTGCCTGCCTCGGCC
CGCCAGGAGGGGTGCCAGGACATCGCTACGCAGCTCATCTCCAACATGGACATTGACGTG
ATCCTAGGTGGAGGCCGAAAGTACATGTTTCCCATGGGAACCCCAGACCCTGAGTACCCA
GATGACTACAGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTG
GCGAAGCGCCAGGGTGCCCGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCTTCCCTG
GACCCGTCTGTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATC
CACCGAGACTCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTG
CTGAGCAGGAACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGT
CATCATGAAAGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATT
GAGAGGGCGGGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCAC
TCCCACGTCTTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCC
CCTGGCAAGGCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGC
TATGTGCTCAAGGACGGCGCCCGGCCGGATGTTACCGAGAGCGAGAGCGGGAGCCCCGAG
TATCGGCAGCAGTCAGCAGTGCCCCTGGACGAAGAGACCCACGCAGGCGAGGACGTGGCG
GTGTTCGCGCGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATA
GCGCACGTCATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCC
CCCGCCGGCACCACCGACGCCGCGCACCCGGGGCGGTCCGTGGTCCCCGCGTTGCTTCCT
CTGCTGGCCGGGACCCTGCTGCTGCTGGAGACGGCCACTGCTCCCTGA
|
| Enzyme 30 GenBank Gene ID |
M13077 |
| Enzyme 30 GeneCard ID |
ALPP |
| Enzyme 30 GenAtlas ID |
ALPP |
| Enzyme 30 HGNC ID |
HGNC:439 |
| Enzyme 30 Chromosome Location |
2 |
| Enzyme 30 Locus |
2q37 |
| Enzyme 30 SNPs |
SNPJam Report |
| Enzyme 30 General References |
- Knoll BJ, Rothblum KN, Longley M: Nucleotide sequence of the human placental alkaline phosphatase gene. Evolution of the 5' flanking region by deletion/substitution. J Biol Chem. 1988 Aug 25;263(24):12020-7. [PubMed ]
- Millan JL: Molecular cloning and sequence analysis of human placental alkaline phosphatase. J Biol Chem. 1986 Mar 5;261(7):3112-5. [PubMed ]
- Henthorn PS, Knoll BJ, Raducha M, Rothblum KN, Slaughter C, Weiss M, Lafferty MA, Fischer T, Harris H: Products of two common alleles at the locus for human placental alkaline phosphatase differ by seven amino acids. Proc Natl Acad Sci U S A. 1986 Aug;83(15):5597-601. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Kam W, Clauser E, Kim YS, Kan YW, Rutter WJ: Cloning, sequencing, and chromosomal localization of human term placental alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1985 Dec;82(24):8715-9. [PubMed ]
- Ezra E, Blacher R, Udenfriend S: Purification and partial sequencing of human placental alkaline phosphatase. Biochem Biophys Res Commun. 1983 Nov 15;116(3):1076-83. [PubMed ]
- Ovitt CE, Strauss AW, Alpers DH, Chou JY, Boime I: Expression of different-sized placental alkaline phosphatase mRNAs in placenta and choriocarcinoma cells. Proc Natl Acad Sci U S A. 1986 Jun;83(11):3781-5. [PubMed ]
- Micanovic R, Bailey CA, Brink L, Gerber L, Pan YC, Hulmes JD, Udenfriend S: Aspartic acid-484 of nascent placental alkaline phosphatase condenses with a phosphatidylinositol glycan to become the carboxyl terminus of the mature enzyme. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1398-402. [PubMed ]
- Micanovic R, Gerber LD, Berger J, Kodukula K, Udenfriend S: Selectivity of the cleavage/attachment site of phosphatidylinositol-glycan-anchored membrane proteins determined by site-specific mutagenesis at Asp-484 of placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1990 Jan;87(1):157-61. [PubMed ]
- Lowe ME: Site-specific mutations in the COOH-terminus of placental alkaline phosphatase: a single amino acid change converts a phosphatidylinositol-glycan-anchored protein to a secreted protein. J Cell Biol. 1992 Feb;116(3):799-807. [PubMed ]
- Kozlenkov A, Manes T, Hoylaerts MF, Millan JL: Function assignment to conserved residues in mammalian alkaline phosphatases. J Biol Chem. 2002 Jun 21;277(25):22992-9. Epub 2002 Apr 5. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Le Du MH, Stigbrand T, Taussig MJ, Menez A, Stura EA: Crystal structure of alkaline phosphatase from human placenta at 1.8 A resolution. Implication for a substrate specificity. J Biol Chem. 2001 Mar 23;276(12):9158-65. Epub 2000 Dec 20. [PubMed ]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5325 |
| Enzyme 31 Name |
Intestinal-type alkaline phosphatase |
| Enzyme 31 Synonyms |
- IAP
- Intestinal alkaline phosphatase
|
| Enzyme 31 Gene Name |
ALPI |
| Enzyme 31 Protein Sequence |
>Intestinal-type alkaline phosphatase
MQGPWVLLLLGLRLQLSLGVIPAEEENPAFWNRQAAEALDAAKKLQPIQKVAKNLILFLG
DGLGVPTVTATRILKGQKNGKLGPETPLAMDRFPYLALSKTYNVDRQVPDSAATATAYLC
GVKANFQTIGLSAAARFNQCNTTRGNEVISVMNRAKQAGKSVGVVTTTRVQHASPAGTYA
HTVNRNWYSDADMPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPADA
SQNGIRLDGKNLVQEWLAKHQGAWYVWNRTELMQASLDQSVTHLMGLFEPGDTKYEIHRD
PTLDPSLMEMTEAALRLLSRNPRGFYLFVEGGRIDHGHHEGVAYQALTEAVMFDDAIERA
GQLTSEEDTLTLVTADHSHVFSFGGYTLRGSSIFGLAPSKAQDSKAYTSILYGNGPGYVF
NSGVRPDVNESESGSPDYQQQAAVPLSSETHGGEDVAVFARGPQAHLVHGVQEQSFVAHV
MAFAACLEPYTACDLAPPACTTDAAHPVAASLPLLAGTLLLLGASAAP
|
| Enzyme 31 Number of Residues |
528 |
| Enzyme 31 Molecular Weight |
56811.7 |
| Enzyme 31 Theoretical pI |
5.70 |
| Enzyme 31 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 31 General Function |
Involved in catalytic activity |
| Enzyme 31 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 31 Pathways |
- Folate and Pterine Biosynthesis (map00790 )
- gamma-Hexachlorocyclohexane Degradation (map00361 )
|
| Enzyme 31 Reactions |
- a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
178432 |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P09923 |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
PPBI_HUMAN |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1587 bp
ATGCAGGGGCCCTGGGTGCTGCTGCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCGTC
ATCCCAGCTGAGGAGGAGAACCCGGCCTTCTGGAACCGCCAGGCAGCTGAGGCCCTGGAT
GCTGCCAAGAAGCTGCAGCCCATCCAGAAGGTCGCCAAGAACCTCATCCTCTTCCTGGGC
GATGGGTTGGGGGTGCCCACGGTGACAGCCACCAGGATCCTAAAGGGGCAGAAGAATGGC
AAACTGGGGCCTGAGACGCCCCTGGCCATGGACCGCTTCCCATACCTGGCTCTGTCCAAG
ACATACAATGTGGACAGACAGGTGCCAGACAGCGCAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGCCAACTTCCAGACCATCGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAATGAGGTCATCTCCGTGATGAACCGGGCCAAGCAAGCAGGAAAG
TCAGTAGGAGTGGTGACCACCACACGGGTGCAGCACGCCTCGCCAGCCGGCACCTACGCA
CACACAGTGAACCGCAACTGGTACTCAGATGCTGACATGCCTGCCTCAGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACTCAGCTCATCTCCAACATGGACATTGACGTGATCCTTGGC
GGAGGCCGCAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGCTGATGCC
AGCCAGAATGGAATCAGGCTGGACGGGAAGAACCTGGTGCAGGAATGGCTGGCAAAGCAC
CAGGGTGCCTGGTATGTGTGGAACCGCACTGAGCTCATGCAGGCGTCCCTGGACCAGTCT
GTGACCCATCTCATGGGCCTCTTTGAGCCCGGAGACACGAAATATGAGATCCTCCGAGAC
CCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCGCCTGCTGAGCAGG
AACCCCCGCGGCTTCTACCTCTTTGTGGAGGGCGGCCGCATCGACCATGGTCATCATGAG
GGTGTGGCTTACCAGGCAGTCACTGAGGCGGTCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGACCCTCGTCACCGCTGACCACTCCCATGTC
TTCTCCTTTGGTGGCTACACCTTGCGAGGGAGCTCCATCTTCGGGTTGGCCCCCAGCAAG
GCTCAGGACAGCAAAGCCTACACGTCCATCCTGTACGGCAATGGCCCGGGCTACGTGTTC
AACTCAGGCGTGCGACCAGACGTGAATGAGAGCGAGAGCGGGAGCCCCGATTACCAGCAG
CAGGCGGCGGTGCCCCTGTCGTCCGAGACCCACGGAGGCGAAGACGTGGCGGTGTTTGCG
CGCGGCCCGCAGGCGCACCTGGTGCATGGTGTGCAGGAGCAGAGCTTCGTAGCGCATGTC
ATGGCCTTCGCTGCCTGTCTGGAGCCCTACACGGCCTGCGACCTGGCGCTCCCCGCCTGC
ACCACCGACGCCGCGCACCCAGTTGCCGCGTCGCTGCCACTGCTGGCCGGGACCCTGCTG
CTGCTGGGGGCGTCCGCTGCTCCCTGA
|
| Enzyme 31 GenBank Gene ID |
M15694 |
| Enzyme 31 GeneCard ID |
ALPI |
| Enzyme 31 GenAtlas ID |
ALPI |
| Enzyme 31 HGNC ID |
HGNC:437 |
| Enzyme 31 Chromosome Location |
2 |
| Enzyme 31 Locus |
2q37.1 |
| Enzyme 31 SNPs |
SNPJam Report |
| Enzyme 31 General References |
- Berger J, Garattini E, Hua JC, Udenfriend S: Cloning and sequencing of human intestinal alkaline phosphatase cDNA. Proc Natl Acad Sci U S A. 1987 Feb;84(3):695-8. [PubMed ]
- Henthorn PS, Raducha M, Edwards YH, Weiss MJ, Slaughter C, Lafferty MA, Harris H: Nucleotide and amino acid sequences of human intestinal alkaline phosphatase: close homology to placental alkaline phosphatase. Proc Natl Acad Sci U S A. 1987 Mar;84(5):1234-8. [PubMed ]
- Henthorn PS, Raducha M, Kadesch T, Weiss MJ, Harris H: Sequence and characterization of the human intestinal alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12011-9. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Millan JL: Promoter structure of the human intestinal alkaline phosphatase gene. Nucleic Acids Res. 1987 Dec 23;15(24):10599. [PubMed ]
- Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed ]
- Hua JC, Berger J, Pan YC, Hulmes JD, Udenfriend S: Partial sequencing of human adult, human fetal, and bovine intestinal alkaline phosphatases: comparison with the human placental and liver isozymes. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2368-72. [PubMed ]
- Nishihara Y, Hayashi Y, Adachi T, Koyama I, Stigbrand T, Hirano K: Chemical nature of intestinal-type alkaline phosphatase in human kidney. Clin Chem. 1992 Dec;38(12):2539-42. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
5328 |
| Enzyme 32 Name |
Alkaline phosphatase, tissue-nonspecific isozyme |
| Enzyme 32 Synonyms |
- AP-TNAP
- TNSALP
- Alkaline phosphatase liver/bone/kidney isozyme
|
| Enzyme 32 Gene Name |
ALPL |
| Enzyme 32 Protein Sequence |
>Alkaline phosphatase, tissue-nonspecific isozyme
MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYALELQKLNTNVAKNVIMFLGD
GMGVSTVTAARILKGQLHHNPGEETRLEMDKFPFVALSKTYNTNAQVPDSAGTATAYLCG
VKANEGTVGVSAATERSRCNTTQGNEVTSILRWAKDAGKSVGIVTTTRVNHATPSAAYAH
SADRDWYSDNEMPPEALSQGCKDIAYQLMHNIRDIDVIMGGGRKYMYPKNKTDVEYESDE
KARGTRLDGLDLVDTWKSFKPRYKHSHFIWNRTELLTLDPHNVDYLLGLFEPGDMQYELN
RNNVTDPSLSEMVVVAIQILRKNPKGFFLLVEGGRIDHGHHEGKAKQALHEAVEMDRAIG
QAGSLTSSEDTLTVVTADHSHVFTFGGYTPRGNSIFGLAPMLSDTDKKPFTAILYGNGPG
YKVVGGERENVSMVDYAHNNYQAQSAVPLRHETHGGEDVAVFSKGPMAHLLHGVHEQNYV
PHVMAYAACIGANLGHCAPASSAGSLAAGPLLLALALYPLSVLF
|
| Enzyme 32 Number of Residues |
524 |
| Enzyme 32 Molecular Weight |
57304.4 |
| Enzyme 32 Theoretical pI |
6.66 |
| Enzyme 32 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 32 General Function |
Involved in catalytic activity |
| Enzyme 32 Specific Function |
This isozyme may play a role in skeletal mineralization |
| Enzyme 32 Pathways |
- Folate and Pterine Biosynthesis (map00790 )
- gamma-Hexachlorocyclohexane Degradation (map00361 )
|
| Enzyme 32 Reactions |
- a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
28738 |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
P05186 |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
PPBT_HUMAN |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1575 bp
ATGATTTCACCATTCTTAGTACTGGCCATTGGCACCTGCCTTACTAACTCCTTAGTGCCA
GAGAAAGAGAAAGACCCCAAGTACTGGCGAGACCAAGCGCAAGAGACACTGAAATATGCC
CTGGAGCTTCAGAAGCTCAACACCAACGTGGCTAAGAATGTCATCATGTTCCTGGGAGAT
GGGATGGGTGTCTCCACAGTGACGGCTGCCCGCATCCTCAAGGGTCAGCTCCACCACAAC
CCTGGGGAGGAGACCAGGCTGGAGATGGACAAGTTCCCCTTCGTGGCCCTCTCCAAGACG
TACAACACCAAAGCCCAGGTCCCTGACAGCGCCGGCACCGCCACCGCCTACCTGTGTGGG
GTGAAGGCCAATGAGGGCACCGTGGGGGTAAGCGCAGCCACTGAGCGTTCCCGGTGCAAC
ACCACCCAGGGGAACGAGGTCACCTCCATCCTGCGCTGGGCCAAGGACGCTGGGAAATCT
GTGGGCATTGTGACCACCACGAGAGTGAACCATGCCACCCCCAGCGCCGCCTACGCCCAC
TCGGCTGACCGGGACTGGTACTCAGACAACGAGATGCCCCCTGAGGCCTTGAGCCAGGGC
TGTAAGGACATCGCCTACCAGCTCATGCATAACATCAGGGACATTGACGTGATCATGGGG
GGTGGCCGGAAATACATGTACCCCAAGAATAAAACTGATGTGGAGTATGAGAGTGACGAG
AAAGCCAGGGGCACGAGGCTGGACGGCCTGGACCTCGTTGACACCTGGAAGAGCTTCAAA
CCGAGACACAAGCACTCCCACTTCATCTGGAACCGCACGGAACTCCTGACCCTTGACCCC
CACAATGTGGACTACCTATTGGGTCTCTTCGAGCCGGGGGACATGCAGTACGAGCTGAAC
AGGAACAACGTGACGGACCCGTCACTCTCCGAGATGGTGGTGGTGGCCATCCAGATCCTG
CGGAAGAACCCCAAAGGCTTCTTCTTGCTGGTGGAAGGAGGCAGAATTGACCACGGGCAC
CATGAAGGAAAAGCCAAGCAGGCCCTGCATGAGGCGGTGGAGATGGACCGGGCCATCGGG
CAGGCAGGCAGCTTGACCTCCTCGGAAGACACTCTGACCGTGGTCACTGCGGACCATTCC
CACGTCTTCACATTTGGTGGATACACCCCCCGTGGCAACTCTATCTTTGGTCTGGCCCCC
ATGCTGAGTGACACAGACAAGAAGCCCTTCACTGCCATCCTGTATGGCAATGGGCCTGGC
TACAAGGTGGTGGGCGGTGAACGAGAGAATGTCTCCATGGTGGACTATGCTCACAACAAC
TACCAGGCGCAGTCTGCTGTGCCCCTGCGCCACGAGACCCACGGCGGGGAGGACGTGGCC
GTCTTCTCCAAGGGCCCCATGGCGCACCTGCTGCACGGCGTCCACGAGCAGAACTACGTC
CCCCACGTGATGGCGTATGCAGCCTGCATCGGGGCCAACCTCGGCCACTGTGCTCCTGCC
AGCTCGGCAGGCAGCCTTGCTGCAGGCCCCCTGCTGCTCGCGCTGGCCCTCTACCCCCTG
AGCGTCCTGTTCTGA
|
| Enzyme 32 GenBank Gene ID |
X14174 |
| Enzyme 32 GeneCard ID |
ALPL |
| Enzyme 32 GenAtlas ID |
ALPL |
| Enzyme 32 HGNC ID |
HGNC:438 |
| Enzyme 32 Chromosome Location |
1 |
| Enzyme 32 Locus |
1p36.12 |
| Enzyme 32 SNPs |
SNPJam Report |
| Enzyme 32 General References |
- Weiss MJ, Henthorn PS, Lafferty MA, Slaughter C, Raducha M, Harris H: Isolation and characterization of a cDNA encoding a human liver/bone/kidney-type alkaline phosphatase. Proc Natl Acad Sci U S A. 1986 Oct;83(19):7182-6. [PubMed ]
- Weiss MJ, Ray K, Henthorn PS, Lamb B, Kadesch T, Harris H: Structure of the human liver/bone/kidney alkaline phosphatase gene. J Biol Chem. 1988 Aug 25;263(24):12002-10. [PubMed ]
- Kishi F, Matsuura S, Kajii T: Nucleotide sequence of the human liver-type alkaline phosphatase cDNA. Nucleic Acids Res. 1989 Mar 11;17(5):2129. [PubMed ]
- Sugimoto N, Iwamoto S, Hoshino Y, Kajii E: A novel missense mutation of the tissue-nonspecific alkaline phosphatase gene detected in a patient with hypophosphatasia. J Hum Genet. 1998;43(3):160-4. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Garattini E, Hua JC, Pan YC, Udenfriend S: Human liver alkaline phosphatase, purification and partial sequencing: homology with the placental isozyme. Arch Biochem Biophys. 1986 Mar;245(2):331-7. [PubMed ]
- Nishihara Y, Hayashi Y, Adachi T, Koyama I, Stigbrand T, Hirano K: Chemical nature of intestinal-type alkaline phosphatase in human kidney. Clin Chem. 1992 Dec;38(12):2539-42. [PubMed ]
- Elortza F, Nuhse TS, Foster LJ, Stensballe A, Peck SC, Jensen ON: Proteomic analysis of glycosylphosphatidylinositol-anchored membrane proteins. Mol Cell Proteomics. 2003 Dec;2(12):1261-70. Epub 2003 Sep 29. [PubMed ]
- Elortza F, Mohammed S, Bunkenborg J, Foster LJ, Nuhse TS, Brodbeck U, Peck SC, Jensen ON: Modification-specific proteomics of plasma membrane proteins: identification and characterization of glycosylphosphatidylinositol-anchored proteins released upon phospholipase D treatment. J Proteome Res. 2006 Apr;5(4):935-43. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
- Weiss MJ, Cole DE, Ray K, Whyte MP, Lafferty MA, Mulivor RA, Harris H: A missense mutation in the human liver/bone/kidney alkaline phosphatase gene causing a lethal form of hypophosphatasia. Proc Natl Acad Sci U S A. 1988 Oct;85(20):7666-9. [PubMed ]
- Henthorn PS, Raducha M, Fedde KN, Lafferty MA, Whyte MP: Different missense mutations at the tissue-nonspecific alkaline phosphatase gene locus in autosomal recessively inherited forms of mild and severe hypophosphatasia. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9924-8. [PubMed ]
- Greenberg CR, Taylor CL, Haworth JC, Seargeant LE, Philipps S, Triggs-Raine B, Chodirker BN: A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal (lethal) form of hypophosphatasia in Canadian mennonites. Genomics. 1993 Jul;17(1):215-7. [PubMed ]
- Orimo H, Hayashi Z, Watanabe A, Hirayama T, Hirayama T, Shimada T: Novel missense and frameshift mutations in the tissue-nonspecific alkaline phosphatase gene in a Japanese patient with hypophosphatasia. Hum Mol Genet. 1994 Sep;3(9):1683-4. [PubMed ]
- Ozono K, Yamagata M, Michigami T, Nakajima S, Sakai N, Cai G, Satomura K, Yasui N, Okada S, Nakayama M: Identification of novel missense mutations (Phe310Leu and Gly439Arg) in a neonatal case of hypophosphatasia. J Clin Endocrinol Metab. 1996 Dec;81(12):4458-61. [PubMed ]
- Mornet E, Taillandier A, Peyramaure S, Kaper F, Muller F, Brenner R, Bussiere P, Freisinger P, Godard J, Le Merrer M, Oury JF, Plauchu H, Puddu R, Rival JM, Superti-Furga A, Touraine RL, Serre JL, Simon-Bouy B: Identification of fifteen novel mutations in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in European patients with severe hypophosphatasia. Eur J Hum Genet. 1998 Jul-Aug;6(4):308-14. [PubMed ]
- Goseki-Sone M, Orimo H, Iimura T, Takagi Y, Watanabe H, Taketa K, Sato S, Mayanagi H, Shimada T, Oida S: Hypophosphatasia: identification of five novel missense mutations (G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific alkaline phosphatase gene among Japanese patients. Hum Mutat. 1998;Suppl 1:S263-7. [PubMed ]
- Zurutuza L, Muller F, Gibrat JF, Taillandier A, Simon-Bouy B, Serre JL, Mornet E: Correlations of genotype and phenotype in hypophosphatasia. Hum Mol Genet. 1999 Jun;8(6):1039-46. [PubMed ]
- Taillandier A, Zurutuza L, Muller F, Simon-Bouy B, Serre JL, Bird L, Brenner R, Boute O, Cousin J, Gaillard D, Heidemann PH, Steinmann B, Wallot M, Mornet E: Characterization of eleven novel mutations (M45L, R119H, 544delG, G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with severe hypophosphatasia. Mutations in brief no. 217. Online. Hum Mutat. 1999;13(2):171-2. [PubMed ]
- Mochizuki H, Saito M, Michigami T, Ohashi H, Koda N, Yamaguchi S, Ozono K: Severe hypercalcaemia and respiratory insufficiency associated with infantile hypophosphatasia caused by two novel mutations of the tissue-nonspecific alkaline phosphatase gene. Eur J Pediatr. 2000 May;159(5):375-9. [PubMed ]
- Taillandier A, Cozien E, Muller F, Merrien Y, Bonnin E, Fribourg C, Simon-Bouy B, Serre JL, Bieth E, Brenner R, Cordier MP, De Bie S, Fellmann F, Freisinger P, Hesse V, Hennekam RC, Josifova D, Kerzin-Storrar L, Leporrier N, Zabot MT, Mornet E: Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S, 997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with hypophosphatasia. Hum Mutat. 2000 Mar;15(3):293. [PubMed ]
- Muller HL, Yamazaki M, Michigami T, Kageyama T, Schonau E, Schneider P, Ozono K: Asp361Val Mutant of alkaline phosphatase found in patients with dominantly inherited hypophosphatasia inhibits the activity of the wild-type enzyme. J Clin Endocrinol Metab. 2000 Feb;85(2):743-7. [PubMed ]
- Sergi C, Mornet E, Troeger J, Voigtlaender T: Perinatal hypophosphatasia: radiology, pathology and molecular biology studies in a family harboring a splicing mutation (648+1A) and a novel missense mutation (N400S) in the tissue-nonspecific alkaline phosphatase (TNSALP) gene. Am J Med Genet. 2001 Oct 15;103(3):235-40. [PubMed ]
- Lia-Baldini AS, Muller F, Taillandier A, Gibrat JF, Mouchard M, Robin B, Simon-Bouy B, Serre JL, Aylsworth AS, Bieth E, Delanote S, Freisinger P, Hu JC, Krohn HP, Nunes ME, Mornet E: A molecular approach to dominance in hypophosphatasia. Hum Genet. 2001 Jul;109(1):99-108. [PubMed ]
- Taillandier A, Lia-Baldini AS, Mouchard M, Robin B, Muller F, Simon-Bouy B, Serre JL, Bera-Louville A, Bonduelle M, Eckhardt J, Gaillard D, Myhre AG, Kortge-Jung S, Larget-Piet L, Malou E, Sillence D, Temple IK, Viot G, Mornet E: Twelve novel mutations in the tissue-nonspecific alkaline phosphatase gene (ALPL) in patients with various forms of hypophosphatasia. Hum Mutat. 2001;18(1):83-4. [PubMed ]
- Orimo H, Girschick HJ, Goseki-Sone M, Ito M, Oda K, Shimada T: Mutational analysis and functional correlation with phenotype in German patients with childhood-type hypophosphatasia. J Bone Miner Res. 2001 Dec;16(12):2313-9. [PubMed ]
- Watanabe H, Hashimoto-Uoshima M, Goseki-Sone M, Orimo H, Ishikawa I: A novel point mutation (C571T) in the tissue-non-specific alkaline phosphatase gene in a case of adult-type hypophosphatasia. Oral Dis. 2001 Nov;7(6):331-5. [PubMed ]
- Litmanovitz, Reish O, Dolfin T, Arnon S, Regev R, Grinshpan G, Yamazaki M, Ozono K: Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline phosphatase gene in neonatal hypophosphatasia associated with convulsions. J Inherit Metab Dis. 2002 Feb;25(1):35-40. [PubMed ]
- Mumm S, Jones J, Finnegan P, Henthorn PS, Podgornik MN, Whyte MP: Denaturing gradient gel electrophoresis analysis of the tissue nonspecific alkaline phosphatase isoenzyme gene in hypophosphatasia. Mol Genet Metab. 2002 Feb;75(2):143-53. [PubMed ]
- Spentchian M, Merrien Y, Herasse M, Dobbie Z, Glaser D, Holder SE, Ivarsson SA, Kostiner D, Mansour S, Norman A, Roth J, Stipoljev F, Taillemite JL, van der Smagt JJ, Serre JL, Simon-Bouy B, Taillandier A, Mornet E: Severe hypophosphatasia: characterization of fifteen novel mutations in the ALPL gene. Hum Mutat. 2003 Jul;22(1):105-6. [PubMed ]
- Herasse M, Spentchian M, Taillandier A, Keppler-Noreuil K, Fliorito AN, Bergoffen J, Wallerstein R, Muti C, Simon-Bouy B, Mornet E: Molecular study of three cases of odontohypophosphatasia resulting from heterozygosity for mutations in the tissue non-specific alkaline phosphatase gene. J Med Genet. 2003 Aug;40(8):605-9. [PubMed ]
- Draguet C, Gillerot Y, Mornet E: [Childhood hypophosphatasia: a case report due to a novel mutation] Arch Pediatr. 2004 May;11(5):440-3. [PubMed ]
- Brun-Heath I, Taillandier A, Serre JL, Mornet E: Characterization of 11 novel mutations in the tissue non-specific alkaline phosphatase gene responsible for hypophosphatasia and genotype-phenotype correlations. Mol Genet Metab. 2005 Mar;84(3):273-7. Epub 2004 Dec 19. [PubMed ]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
5329 |
| Enzyme 33 Name |
Tartrate-resistant acid phosphatase type 5 |
| Enzyme 33 Synonyms |
- TR-AP
- Tartrate-resistant acid ATPase
- TrATPase
- Type 5 acid phosphatase
|
| Enzyme 33 Gene Name |
ACP5 |
| Enzyme 33 Protein Sequence |
>Tartrate-resistant acid phosphatase type 5
MDMWTALLILQALLLPSLADGATPALRFVAVGDWGGVPNAPFHTAREMANAKEIARTVQI
LGADFILSLGDNFYFTGVQDINDKRFQETFEDVFSDRSLRKVPWYVLAGNHDHLGNVSAQ
IAYSKISKRWNFPSPFYRLHFKIPQTNVSVAIFMLDTVTLCGNSDDFLSQQPERPRDVKL
ARTQLSWLKKQLAAAREDYVLVAGHYPVWSIAEHGPTHCLVKQLRPLLATYGVTAYLCGH
DHNLQYLQDENGVGYVLSGAGNFMDPSKRHQRKVPNGYLRFHYGTEDSLGGFAYVEISSK
EMTVTYIEASGKSLFKTRLPRRARP
|
| Enzyme 33 Number of Residues |
325 |
| Enzyme 33 Molecular Weight |
36598.5 |
| Enzyme 33 Theoretical pI |
8.95 |
| Enzyme 33 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 33 General Function |
Involved in hydrolase activity |
| Enzyme 33 Specific Function |
Involved in osteopontin/bone sialoprotein dephosphorylation. Its expression seems to increase in certain pathological states such as Gaucher and Hodgkin diseases, the hairy cell, the B-cell, and the T-cell leukemias |
| Enzyme 33 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361 )
- Riboflavin Metabolism (map00740 )
|
| Enzyme 33 Reactions |
- a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
178006 |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
P13686 |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
PPA5_HUMAN |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>972 bp
ATGGACATGTGGACGGCGCTGCTCATCCTGCAAGCCTTGTTGCTACCCTCCCTGGCTGAT
GGTGCCACCCCTGCCCTGCGCTTTGTAGCCGTGGGTGACTGGGGAGGGGTCCCCAATGCC
CCATTCCACACGGGCCCGGAAATGGCCAATGCCAAGGAGATCGCTCGGACTGTGCAGATC
CTGGGTGCAGACTTCATCCTGTCTCTAGGGGACAATTTTTACTTCACTGGTGTGCAAGAC
ATCAATGACAAGAGGTTCCAGGAGACCTTTGAGGACGTATTCTCTGACCGCTCCCTTCGC
AAAGTGCCCTGGTACGTGCTAGCCGGAAACCATGACCACCTTGGCAATGTCTCTGCCCAG
ATTGCATACTCTAAGATCTCCAAGCGCTGGAACTTCCCCAGCCCTTTCTACCGCCTGCAC
TTCAAGATCCCACAGACCAATGTGTCTGTGGCCATTTTTATGCTGGACACAGTGACACTA
TGTGGCAACTCAGATGACTTCCTCAGCCAGCAGCCTGAGAGGCCCCGACTAACTGCCCGC
ACACAGCTGTCCTGGCTCAAGAAACAGCTGGCGGCGGCCAGGGAGGACTACGTGCTGGTG
GCTGGCCACTACCCCGTGTGGTCCATAGCCGAGCACGGGCCTACCCACTGCCTGGTCAAG
CAGCTACGGCCACTGCTGGCCACATACGGGGTCACTGCCTACCTGTGCGGCCACGATCAC
AATCTGCAGTACCTGCAAGATGAGAATGGCGTGGGCTACGTGCTGAGTGGGGCTGGGAAT
TTCATGGACCCCTCAAAGCGGCACCAGCGCAAGGTCCCCAACGGCTATCTGCGCTTCCAC
TATGGGACTGAAGACTCACTGGGTGGCTTTGCCTATGTGGAGATCAGCTCCAAAGAGATG
ACTGTCACTTACATCGAGGCCTCGGGCAAGTCCCTCTTTAAGACCAGGCTGCCGAGGCGA
GCCAGGCCCTGA
|
| Enzyme 33 GenBank Gene ID |
J04430 |
| Enzyme 33 GeneCard ID |
ACP5 |
| Enzyme 33 GenAtlas ID |
ACP5 |
| Enzyme 33 HGNC ID |
HGNC:124 |
| Enzyme 33 Chromosome Location |
1 |
| Enzyme 33 Locus |
19p13.3-p13.2 |
| Enzyme 33 SNPs |
SNPJam Report |
| Enzyme 33 General References |
- Ketcham CM, Roberts RM, Simmen RC, Nick HS: Molecular cloning of the type 5, iron-containing, tartrate-resistant acid phosphatase from human placenta. J Biol Chem. 1989 Jan 5;264(1):557-63. [PubMed ]
- Lord DK, Cross NC, Bevilacqua MA, Rider SH, Gorman PA, Groves AV, Moss DW, Sheer D, Cox TM: Type 5 acid phosphatase. Sequence, expression and chromosomal localization of a differentiation-associated protein of the human macrophage. Eur J Biochem. 1990 Apr 30;189(2):287-93. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Cassady AI, King AG, Cross NC, Hume DA: Isolation and characterization of the genes encoding mouse and human type-5 acid phosphatase. Gene. 1993 Aug 25;130(2):201-7. [PubMed ]
- Hayman AR, Warburton MJ, Pringle JA, Coles B, Chambers TJ: Purification and characterization of a tartrate-resistant acid phosphatase from human osteoclastomas. Biochem J. 1989 Jul 15;261(2):601-9. [PubMed ]
- Janckila AJ, Latham MD, Lam KW, Chow KC, Li CY, Yam LT: Heterogeneity of hairy cell tartrate-resistant acid phosphatase. Clin Biochem. 1992 Dec;25(6):437-43. [PubMed ]
- Stepan JJ, Lau KH, Mohan S, Kraenzlin M, Baylink DJ: Purification and N-terminal sequence of two tartrate-resistant acid phosphatases type-5 from the hairy cell leukemia spleen. Biochem Biophys Res Commun. 1989 Dec 29;165(3):1027-34. [PubMed ]
- Stepan JJ, Lau KH, Mohan S, Singer FR, Baylink DJ: Purification and N-terminal amino acid sequence of the tartrate-resistant acid phosphatase from human osteoclastoma: evidence for a single structure. Biochem Biophys Res Commun. 1990 Apr 30;168(2):792-800. [PubMed ]
- Hayman AR, Dryden AJ, Chambers TJ, Warburton MJ: Tartrate-resistant acid phosphatase from human osteoclastomas is translated as a single polypeptide. Biochem J. 1991 Aug 1;277 ( Pt 3):631-4. [PubMed ]
- Strater N, Jasper B, Scholte M, Krebs B, Duff AP, Langley DB, Han R, Averill BA, Freeman HC, Guss JM: Crystal structures of recombinant human purple Acid phosphatase with and without an inhibitory conformation of the repression loop. J Mol Biol. 2005 Aug 5;351(1):233-46. Epub 2005 Apr 26. [PubMed ]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
5330 |
| Enzyme 34 Name |
Prostatic acid phosphatase |
| Enzyme 34 Synonyms |
Not Available |
| Enzyme 34 Gene Name |
ACPP |
| Enzyme 34 Protein Sequence |
>Prostatic acid phosphatase
MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKE
SSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNL
AALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKR
LHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSE
LSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMAL
DVYNGLLPPYASCHLTELYFEKGEYFVEMYYRNETQHEPYPLMLPGCSPSCPLERFAELV
GPVIPQDWSTECMTTNSHQGTEDSTD
|
| Enzyme 34 Number of Residues |
386 |
| Enzyme 34 Molecular Weight |
44565.7 |
| Enzyme 34 Theoretical pI |
6.19 |
| Enzyme 34 GO Classification |
| Function |
- acid phosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 34 General Function |
Involved in acid phosphatase activity |
| Enzyme 34 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 34 Pathways |
- gamma-Hexachlorocyclohexane Degradation (map00361 )
- Riboflavin Metabolism (map00740 )
|
| Enzyme 34 Reactions |
- a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
189621 |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
P15309 |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
PPAP_HUMAN |
| Enzyme 34 PDB ID |
1ND6 |
| Enzyme 34 PDB File |
Show |
| Enzyme 34 3D Structure |
|
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>1161 bp
ATGAGAGCTGCACCCCTCCTCCTGGCCAGGGCAGCAAGCCTTAGCCTTGGCTTCTTGTTT
CTGCTTTTTTTCTGGCTAGACCGAAGTGTACTAGCCAAGGAGTTGAAGTTTGTGACTTTG
GTGTTTCGGCATGGAGACCGAAGTCCCATTGACACCTTTCCCACTGACCCCATAAAGGAA
TCCTCATGGCCACAAGGATTTGGCCAACTCACCCAGCTGGGCATGGAGCAGCATTATGAA
CTTGGAGAGTATATAAGAAAGAGATATAGAAAATTCTTGAATGAGTCCTATAAACATGAA
CAGGTTTATATTCGAAGCACAGACGTTGACCGGACTTTGATGAGTGCTATGACAAACCTG
GCAGCCCTGTTTCCCCCAGAAGGTGTCAGCATCTGGAATCCTATCCTACTCTGGCAGCCC
ATCCCGGTGCACACAGTTCCTCTTTCTGAAGATCAGTTGCTATACCTGCCTTTCAGGAAC
TGCCCTCGTTTTCAAGAACTTGAGAGTGAGACTTTGAAATCAGAGGAATTCCAGAAGAGG
CTGCACCCTTATAAGGATTTTATAGCTACCTTGGGAAAACTTTCAGGATTACATGGCCAG
GACCTTTTTGGAATTTGGAGTAAAGTCTACGACCCTTTATATTGTGAGAGTGTTCACAAT
TTCACTTTACCCTCCTGGGCCACTGAGGACACCATGACTAAGTTGAGAGAATTGTCAGAA
TTGTCCCTCCTGTCCCTCTATGGAATTCACAAGCAGAAAGAGAAATCTAGGCTCCAAGGG
GGTGTCCTGGTCAATGAAATCCTCAATCACATGAAGAGAGCAACTCAGATACCAAGCTAC
AAAAAACTTATCATGTATTCTGCGCATGACACTACTGTGAGTGGCCTACAGATGGCGCTA
GATGTTTACAACGGACTCCTTCCTCCCTATGCTTCTTGCCACTTGACGGAATTGTACTTT
GAGAAGGGGGAGTACTTTGTGGAGATGTACTATCGGAATGAGACGCAGCACGAGCCGTAT
CCCCTCATGCTACCTGGCTGCAGCCCTAGCTGTCCTCTGGAGAGGTTTGCTGAGCTGGTT
GGCCCTGTGATCCCTCAAGACTGGTCCACGGAGTGTATGACCACAAACAGCCATCAAGGT
ACTGAGGACAGTACAGATTAG
|
| Enzyme 34 GenBank Gene ID |
M34840 |
| Enzyme 34 GeneCard ID |
ACPP |
| Enzyme 34 GenAtlas ID |
ACPP |
| Enzyme 34 HGNC ID |
HGNC:125 |
| Enzyme 34 Chromosome Location |
3 |
| Enzyme 34 Locus |
3q21-q23 |
| Enzyme 34 SNPs |
SNPJam Report |
| Enzyme 34 General References |
- Sharief FS, Li SS: Structure of human prostatic acid phosphatase gene. Biochem Biophys Res Commun. 1992 May 15;184(3):1468-76. [PubMed ]
- Van Etten RL, Davidson R, Stevis PE, MacArthur H, Moore DL: Covalent structure, disulfide bonding, and identification of reactive surface and active site residues of human prostatic acid phosphatase. J Biol Chem. 1991 Feb 5;266(4):2313-9. [PubMed ]
- Sharief FS, Lee H, Leuderman MM, Lundwall A, Deaven LL, Lee CL, Li SS: Human prostatic acid phosphatase: cDNA cloning, gene mapping and protein sequence homology with lysosomal acid phosphatase. Biochem Biophys Res Commun. 1989 Apr 14;160(1):79-86. [PubMed ]
- Vihko P, Virkkunen P, Henttu P, Roiko K, Solin T, Huhtala ML: Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 1988 Aug 29;236(2):275-81. [PubMed ]
- Tailor PG, Govindan MV, Patel PC: Nucleotide sequence of human prostatic acid phosphatase determined from a full-length cDNA clone. Nucleic Acids Res. 1990 Aug 25;18(16):4928. [PubMed ]
- Sharief FS, Li SS: Nucleotide sequence of human prostatic acid phosphatase ACPP gene, including seven Alu repeats. Biochem Mol Biol Int. 1994 Jun;33(3):561-5. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Schroder B, Wrocklage C, Pan C, Jager R, Kosters B, Schafer H, Elsasser HP, Mann M, Hasilik A: Integral and associated lysosomal membrane proteins. Traffic. 2007 Dec;8(12):1676-86. Epub 2007 Sep 26. [PubMed ]
- LaCount MW, Handy G, Lebioda L: Structural origins of L(+)-tartrate inhibition of human prostatic acid phosphatase. J Biol Chem. 1998 Nov 13;273(46):30406-9. [PubMed ]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
5331 |
| Enzyme 35 Name |
Alkaline phosphatase, placental-like |
| Enzyme 35 Synonyms |
- ALP-1
- Alkaline phosphatase Nagao isozyme
- Germ cell alkaline phosphatase
- GCAP
- Placental alkaline phosphatase-like
- PLAP-like
|
| Enzyme 35 Gene Name |
ALPPL2 |
| Enzyme 35 Protein Sequence |
>Alkaline phosphatase, placental-like
MQGPWVLLLLGLRLQLSLGIIPVEEENPDFWNRQAAEALGAAKKLQPAQTAAKNLIIFLG
DGMGVSTVTAARILKGQKKDKLGPETFLAMDRFPYVALSKTYSVDKHVPDSGATATAYLC
GVKGNFQTIGLSAAARFNQCNTTRGNEVISVMNRAKKAGKSVGVVTTTRVQHASPAGAYA
HTVNRNWYSDADVPASARQEGCQDIATQLISNMDIDVILGGGRKYMFPMGTPDPEYPDDY
SQGGTRLDGKNLVQEWLAKHQGARYVWNRTELLQASLDPSVTHLMGLFEPGDMKYEIHRD
STLDPSLMEMTEAALLLLSRNPRGFFLFVEGGRIDHGHHESRAYRALTETIMFDDAIERA
GQLTSEEDTLSLVTADHSHVFSFGGYPLRGSSIFGLAPGKARDRKAYTVLLYGNGPGYVL
KDGARPDVTESESGSPEYRQQSAVPLDGETHAGEDVAVFARGPQAHLVHGVQEQTFIAHV
MAFAACLEPYTACDLAPRAGTTDAAHPGPSVVPALLPLLAGTLLLLGTATAP
|
| Enzyme 35 Number of Residues |
532 |
| Enzyme 35 Molecular Weight |
57376.5 |
| Enzyme 35 Theoretical pI |
6.31 |
| Enzyme 35 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 35 General Function |
Involved in catalytic activity |
| Enzyme 35 Specific Function |
A phosphate monoester + H(2)O = an alcohol + phosphate |
| Enzyme 35 Pathways |
- Folate and Pterine Biosynthesis (map00790 )
- gamma-Hexachlorocyclohexane Degradation (map00361 )
|
| Enzyme 35 Reactions |
- a phosphate monoester + H2O = an alcohol + phosphate [RN:R00626]
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
62988701 |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
P10696 |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
PPBN_HUMAN |
| Enzyme 35 PDB ID |
1EW2 |
| Enzyme 35 PDB File |
Show |
| Enzyme 35 3D Structure |
|
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>1599 bp
ATGCAGGGGCCCTGGGTGCTGCTCCTGCTGGGCCTGAGGCTACAGCTCTCCCTGGGCATC
ATCCCAGTTGAGGAGGAGAACCCGGACTTCTGGAACCGCCAGGCAGCCGAGGCCCTGGGT
GCCGCCAAGAAGCTGCAGCCTGCACAGACAGCCGCCAAGAACCTCATCATCTTCCTGGGT
GACGGGATGGGGGTGTCTACGGTGACAGCTGCCAGGATCCTAAAAGGGCAGAAGAAGGAC
AAACTGGGGCCTGAGACCTTCCTGGCCATGGACCGCTTCCCGTACGTGGCTCTGTCCAAG
ACATACAGTGTAGACAAGCATGTGCCAGACAGTGGAGCCACAGCCACGGCCTACCTGTGC
GGGGTCAAGGGCAACTTCCAGACCATTGGCTTGAGTGCAGCCGCCCGCTTTAACCAGTGC
AACACGACACGCGGCAACGAGGTCATCTCCGTGATGAATCGGGCCAAGAAAGCAGGAAAG
TCAGTGGGAGTGGTAACCACCACACGGGTGCAGCATGCCTCGCCAGCCGGCGCCTACGCC
CACACGGTGAACCGCAACTGGTACTCGGATGCCGACGTGCCTGCCTCGGCCCGCCAGGAG
GGGTGCCAGGACATCGCCACGCAGCTCATCTCCAACATGGACATTGATGTGATCCTAGGT
GGAGGCCGAAAGTACATGTTTCCCATGGGGACCCCAGACCCTGAGTACCCAGATGACTAC
AGCCAAGGTGGGACCAGGCTGGACGGGAAGAATCTGGTGCAGGAATGGCTGGCGAAGCAC
CAGGGTGCCCGGTACGTGTGGAACCGCACTGAGCTCCTGCAGGCTTCCCTGGACCCGTCT
GTGACCCATCTCATGGGTCTCTTTGAGCCTGGAGACATGAAATACGAGATCCACCGAGAC
TCCACACTGGACCCCTCCCTGATGGAGATGACAGAGGCTGCCCTGCTCCTGCTGAGCAGG
AACCCCCGCGGCTTCTTCCTCTTCGTGGAGGGTGGTCGCATCGACCATGGTCATCATGAA
AGCAGGGCTTACCGGGCACTGACTGAGACGATCATGTTCGACGACGCCATTGAGAGGGCG
GGCCAGCTCACCAGCGAGGAGGACACGCTGAGCCTCGTCACTGCCGACCACTCCCACGTC
TTCTCCTTCGGAGGCTACCCCCTGCGAGGGAGCTCCATCTTCGGGCTGGCCCCTGGCAAG
GCCCGGGACAGGAAGGCCTACACGGTCCTCCTATACGGAAACGGTCCAGGCTATGTGCTC
AAGGACGGCGCCCGGCCGGATGTTACGGAGAGCGAGAGCGGGAGCCCCGAGTATCGGCAG
CAGTCAGCAGTGCCCCTGGACGGAGAGACCCACGCAGGCGAGGACGTGGCGGTGTTCGCG
CGCGGCCCGCAGGCGCACCTGGTTCACGGCGTGCAGGAGCAGACCTTCATAGCGCACGTC
ATGGCCTTCGCCGCCTGCCTGGAGCCCTACACCGCCTGCGACCTGGCGCCCCGCGCCGGC
ACCACCGACGCCGCGCACCCGGGGCCGTCCGTGGTCCCCGCGTTGCTTCCTCTGCTGGCA
GGGACCTTGCTGCTGCTGGGGACGGCCACTGCTCCCTGA
|
| Enzyme 35 GenBank Gene ID |
AC068134 |
| Enzyme 35 GeneCard ID |
ALPPL2 |
| Enzyme 35 GenAtlas ID |
ALPPL2 |
| Enzyme 35 HGNC ID |
HGNC:441 |
| Enzyme 35 Chromosome Location |
2 |
| Enzyme 35 Locus |
2q37 |
| Enzyme 35 SNPs |
SNPJam Report |
| Enzyme 35 General References |
- Millan JL, Manes T: Seminoma-derived Nagao isozyme is encoded by a germ-cell alkaline phosphatase gene. Proc Natl Acad Sci U S A. 1988 May;85(9):3024-8. [PubMed ]
- Watanabe S, Watanabe T, Li WB, Soong BW, Chou JY: Expression of the germ cell alkaline phosphatase gene in human choriocarcinoma cells. J Biol Chem. 1989 Jul 25;264(21):12611-9. [PubMed ]
- Gum JR, Hicks JW, Sack TL, Kim YS: Molecular cloning of complementary DNAs encoding alkaline phosphatase in human colon cancer cells. Cancer Res. 1990 Feb 15;50(4):1085-91. [PubMed ]
- Lowe ME, Strauss AW: Expression of a Nagao-type, phosphatidylinositol-glycan anchored alkaline phosphatase in human choriocarcinomas. Cancer Res. 1990 Jul 1;50(13):3956-62. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Knoll BJ, Rothblum KN, Longley M: Two gene duplication events in the evolution of the human heat-stable alkaline phosphatases. Gene. 1987;60(2-3):267-76. [PubMed ]
- Shen LP, Liu H, Kan YW, Kam W: 5' nucleotide sequence of a putative human placental alkaline phosphatase-like gene. Nucleic Acids Res. 1988 Jun 24;16(12):5694. [PubMed ]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
5340 |
| Enzyme 36 Name |
Ribonucleoside-diphosphate reductase large subunit |
| Enzyme 36 Synonyms |
- Ribonucleoside-diphosphate reductase subunit M1
- Ribonucleotide reductase large subunit
|
| Enzyme 36 Gene Name |
RRM1 |
| Enzyme 36 Protein Sequence |
>Ribonucleoside-diphosphate reductase large subunit
MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLA
AETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKST
LDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHK
EDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCAL
ISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIY
LEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLD
EVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNL
GTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKI
IDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGAL
EASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIA
PMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQII
ACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKL
TSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCS
LENRDECLMCGS
|
| Enzyme 36 Number of Residues |
792 |
| Enzyme 36 Molecular Weight |
90069.4 |
| Enzyme 36 Theoretical pI |
7.16 |
| Enzyme 36 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH or CH2 groups
- oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
- protein binding
- purine nucleoside binding
- ribonucleoside-diphosphate reductase activity
|
| Process |
- DNA metabolic process
- DNA replication
- cellular macromolecule metabolic process
- macromolecule metabolic process
- metabolic process
- oxidation reduction
|
| Component |
- macromolecular complex
- protein complex
- ribonucleoside-diphosphate reductase complex
|
|
| Enzyme 36 General Function |
Involved in oxidation reduction |
| Enzyme 36 Specific Function |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides |
| Enzyme 36 Pathways |
|
| Enzyme 36 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
36065 |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
P23921 |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
RIR1_HUMAN |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>2379 bp
ATGCATGTGATCAAGCGAGATGGCCGCCAAGAACGAGTCATGTTTGACAAAATTACATCT
CGAATCCAGAAGCTTTGTTATGGACTCAATATGGATTTTGTTGATCCTGCTCAGATCACC
ATGAAAGTAATCCAAGGCTTGTACAGTGGGGTCACCACAGTGGAACTAGATACTTTGGCT
GCTGAAACAGCTGCAACCTTGACTACTAAGCACCCTGACTATGCTATCCTGGCAGCCAGG
ATCGCTGTCTCTAACTTGCACAAAGAAACAAAGAAAGTGTTCAGTGATGTGATGGAAGAC
CTCTATAACTACATAAATCCACATAATGGCAAACACTCTCCCATGGTGGCCAAGTCAACA
TTGGATATTGTTCTGGCCAATAAAGATCGCCTGAATTCTGCTATTATCTATGACCGAGAT
TTCTCTTACAATTACTTCGGCTTTAAGACGCTAGAGCGGTCTTATTTGTTGAAGATCAAT
GGAAAAGTGGCTGAAAGACCACAACATATGTTGATGAGAGTATCTGTTGGGATCCACAAA
GAAGACATTGATGCAGCAATTGAAACATATAATCTTCTTTCTGAGAGGTGGTTTACTCAT
GCTTCGCCCACTCTCTTCAATGCTGGTACCAACCGCCCACAACTTTCTAGCTGTTTTCTT
CTGAGTATGAAAGATGACAGCATTGAAGGCATTTATGACACTCTAAAGCAATGTGCATTG
ATTTCTAAGTCTGCTGGAGGAATTGGTGTTGCTGTGAGTTGTATTCGGGCTACTGGCAGC
TACATTGCTGGGACTAATGGCAATTCCAATGGCCTTGTACCGATGCTGAGAGTATATAAC
AACACAGCTCGATATGTGGATCAAGGTGGGAACAAGCGTCCTGGGGCATTTGCTATTTAC
CTGGAGCCTTGGCATTTAGACATCTTTGAATTCCTTGATTTAAAGAAGAACACAGGAAAG
GAAGAGCAGCGTGCCAGAGATCTTTTCTTTGCTCTTTGGATTCCGGATCTCTTCATGAAA
CGAGTGGAGACTAATCAGGACTGGTCTTTGATGTGTCCAAATGAGTGTCCTGGTCTGGAT
GAGGTTTGGGGAGAGGAATTTGAGAAACTATATGCAAGTTATGAGAAACAAGGTCGTGTC
CGCAAAGTTGTAAAAGCTCAGCAGCTTTGGTATGCCATCATTGAGTCTCAGACGGAAACA
GGCACCCCGTATATGCTCTACAAAGATTCCTGTAATCGAAAGAGCAACCAGCAGAACCTG
GGAACCATCAAATGCAGCAACCTGTGCACAGAAATAGTGGAGTACACCAGCAAAGATGAG
GTTGCTGTTTGTAATTTGGCTTCCCTGGCCCTGAATATGTATGTCACATCAGAACACACA
TACGACTTTAAGAAGTTGGCTGAAGTCACTAAAGTCGTTGTCCGAAACTTGAATAAAATT
ATTGATATAAACTACTATCCTGTACCAGAGGCATGCCTATCAAATAAACGCCATCGCCCC
ATTGGAATTGGGGTACAAGGTCTGGCAGATGCTTTTATCCTGATGAGATACCCTTTTGAG
AGTGCAGAAGCCCAGTTACTGAATAAGCAGATCTTTGAAACTATTTATTATGGTGCTCTG
GAAGCCAGCTGTGACCTTGCCAAGGAGCAGGGCCCATACGAAACCTATGAGGGCTCTCCA
GTTAGCAAAGGAATTCTTCAGTATGATATGTGGAATGTTACTCCTACAGACCTATGGGAC
TGGAAGGTTCTCAAGGAGAAGATTGCAAAGTATGGTATAAGAAACAGTTTACTTATTGCC
CCGATGCCTACAGCTTCCACTGCTCAGATCCTGGGGAATAATGAGTCCATTGAACCTTAC
ACCAGCAACATCTATACTCGCAGAGTCTTGTCAGGAGAATTTCAGATTGTAAATCCTCAC
TTATTGAAAGATCTTACCGAGCGGGGCCTATGGCATGAAGAGATGAAAAACCAGATTATT
GCATGCAATGGCTCTATTCAGAGCATACCAGAAATTCCTGATGACCTGAAGCAACTTTAT
AAAACTGTGTGGGAAATCTCTCAGAAAACTGTTCTCAAGATGGCAGCTGAGAGAGGTGCT
TTCATTGATCAAAGCCAATCTTTGAACATCCACATTGCTGAGCCTAACTATGGCAAACTC
ACTAGTATGCACTTCTACGGCTGGAAGCAGGGTTTGAAGACTGGGATGTATTATTTAAGG
ACGAGACCAGCAGCTAATCCAATCCAGTTCACTCTAAATAAGGAGAAGCTAAAAGATAAA
GAAAAGGTATCAAAAGAGGAAGAAGAGAAGGAGAGGAACACAGCAGCCATGGTGTGCTCT
TTGGAGAATAGAGATGAATGTCTGATGTGTGGATCCTGA
|
| Enzyme 36 GenBank Gene ID |
X59543 |
| Enzyme 36 GeneCard ID |
RRM1 |
| Enzyme 36 GenAtlas ID |
RRM1 |
| Enzyme 36 HGNC ID |
HGNC:10451 |
| Enzyme 36 Chromosome Location |
1 |
| Enzyme 36 Locus |
11p15.5 |
| Enzyme 36 SNPs |
SNPJam Report |
| Enzyme 36 General References |
- Parker NJ, Begley CG, Fox RM: Human M1 subunit of ribonucleotide reductase: cDNA sequence and expression in stimulated lymphocytes. Nucleic Acids Res. 1991 Jul 11;19(13):3741. [PubMed ]
- Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed ]
- Bepler G, O'briant KC, Kim YC, Schreiber G, Pitterle DM: A 1.4-Mb high-resolution physical map and contig of chromosome segment 11p15.5 and genes in the LOH11A metastasis suppressor region. Genomics. 1999 Jan 15;55(2):164-75. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Parker NJ, Begley CG, Fox RM: Human R1 subunit of ribonucleotide reductase (RRM1): 5' flanking region of the gene. Genomics. 1994 Jan 1;19(1):91-6. [PubMed ]
- Harrington JA, Spector T: Human ribonucleotide reductase. Activation and inhibition by analogs of ATP. Biochem Pharmacol. 1991 Jul 25;42(4):759-63. [PubMed ]
- Xue L, Zhou B, Liu X, Qiu W, Jin Z, Yen Y: Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits. Cancer Res. 2003 Mar 1;63(5):980-6. [PubMed ]
- Qiu W, Zhou B, Darwish D, Shao J, Yen Y: Characterization of enzymatic properties of human ribonucleotide reductase holoenzyme reconstituted in vitro from hRRM1, hRRM2, and p53R2 subunits. Biochem Biophys Res Commun. 2006 Feb 10;340(2):428-34. Epub 2005 Dec 15. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
5343 |
| Enzyme 37 Name |
Ribonucleoside-diphosphate reductase subunit M2 |
| Enzyme 37 Synonyms |
- Ribonucleotide reductase small chain
- Ribonucleotide reductase small subunit
|
| Enzyme 37 Gene Name |
RRM2 |
| Enzyme 37 Protein Sequence |
>Ribonucleoside-diphosphate reductase subunit M2
MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKT
KAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLK
PEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLI
DTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSF
ASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIE
QEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTN
FFEKRVGEYQRMGVMSSPTENSFTLDADF
|
| Enzyme 37 Number of Residues |
389 |
| Enzyme 37 Molecular Weight |
44877.2 |
| Enzyme 37 Theoretical pI |
5.05 |
| Enzyme 37 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH or CH2 groups
- oxidoreductase activity, acting on CH or CH2 groups, disulfide as acceptor
- ribonucleoside-diphosphate reductase activity
- transition metal ion binding
|
| Process |
- cellular nitrogen compound metabolic process
- deoxyribonucleoside diphosphate metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside diphosphate metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 37 General Function |
Involved in oxidoreductase activity |
| Enzyme 37 Specific Function |
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides. Inhibits Wnt signaling |
| Enzyme 37 Pathways |
|
| Enzyme 37 Reactions |
- 2'-deoxyribonucleoside diphosphate + thioredoxin disulfide + H2O = ribonucleoside diphosphate + thioredoxin [RN:R04294]
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
36155 |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
P31350 |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
RIR2_HUMAN |
| Enzyme 37 PDB ID |
1H0N |
| Enzyme 37 PDB File |
Show |
| Enzyme 37 3D Structure |
|
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>1170 bp
ATGCTCTCCCTCCGTGTCCCGCTCGCGCCCATCACGGACCCGCAGCAGCTGCAGCTCTCG
CCGCTGAAGGGGCTCAGCTTGGTCGACAAGGAGAACACGCCGCCGGCCCTGAGCGGGACC
CGCGTCCTGGCCAGCAAGACCGCGAGGAGGATCTTCCAGGAGCCCACGGAGCCGAAAACT
AAAGCAGCTGCCCCCGGCGTGGAGGATGAGCCGCTGCTGAGAGAAAACCCCCGCCGCTTT
GTCATCTTCCCCATCGAGTACCATGATATCTGGCAGATGTATAAGAAGGCAGAGGCTTCC
TTTTGGACCGCCGAGGAGGTTGACCTCTCCAAGGACATTCAGCACTGGGAATCCCTGAAA
CCCGAGGAGAGATATTTTATATCCCATGTTCTGGCTTTCTTTGCAGCAAGCGATGGCATA
GTAAATGAAAACTTGGTGGAGCGATTTAGCCAAGAAGTTCAGATTACAGAAGCCCGCTGT
TTCTATGGCTTCCAAATTGCCATGGAAAACATACATTCTGAAATGTATAGTCTTCTTATT
GACACTTACATAAAAGATCCCAAAGAAAGGGAATTTCTCTTCAATGCCATTGAAACGATG
CCTTGTGTCAAGAAGAAGGCAGACTGGGCCTTGCGCTGGATTGGGGACAAAGAGGCTACC
TATGGTGAACGTGTTGTAGCCTTTGCTGCAGTGGAAGGCATTTTCTTTTCCGGTTCTTTT
GCGTCGATATTCTGGCTCAAGAAACGAGGACTGATGCCTGGCCTCACATTTTCTAATGAA
CTTATTAGCAGAGATGAGGGTTTACACTGTGATTTTGCTTGCCTGATGTTCAAACACCTG
GTACACAAACCATCGGAGGAGAGAGTAAGAGAAATAATTATCAATGCTGTTCGGATAGAA
CAGGAGTTCCTCACTGAGGCCTTGCCTGTGAAGCTCATTGGGATGAATTGCACTCTAATG
AAGCAATACATTGAGTTTGTGGCAGACAGACTTATGCTGGAACTGGGTTTTAGCAAGGTT
TTCAGAGTAGAGAACCCATTTGACTTTATGGAGAATATTTCACTGGAAGGAAAGACTAAC
TTCTTTGAGAAGAGAGTAGGCGAGTATCAGAGGATGGGAGTGATGTCAAGTCCAACAGAG
AATTCTTTTACCTTGGATGCTGACTTCTAA
|
| Enzyme 37 GenBank Gene ID |
X59618 |
| Enzyme 37 GeneCard ID |
RRM2 |
| Enzyme 37 GenAtlas ID |
RRM2 |
| Enzyme 37 HGNC ID |
HGNC:10452 |
| Enzyme 37 Chromosome Location |
2 |
| Enzyme 37 Locus |
2p25-p24 |
| Enzyme 37 SNPs |
SNPJam Report |
| Enzyme 37 General References |
- Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM: Sequence analysis of the large and small subunits of human ribonucleotide reductase. DNA Seq. 1992;2(4):227-34. [PubMed ]
- Zhou B, Yen Y: Characterization of the human ribonucleotide reductase M2 subunit gene; genomic structure and promoter analyses. Cytogenet Cell Genet. 2001;95(1-2):52-9. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed ]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
5351 |
| Enzyme 38 Name |
Ectonucleotide pyrophosphatase/phosphodiesterase family member 1 |
| Enzyme 38 Synonyms |
- E-NPP 1
- Membrane component chromosome 6 surface marker 1
- Phosphodiesterase I/nucleotide pyrophosphatase 1
- Plasma-cell membrane glycoprotein PC-1
- Alkaline phosphodiesterase I
- Nucleotide pyrophosphatase
- NPPase
|
| Enzyme 38 Gene Name |
ENPP1 |
| Enzyme 38 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
MERDGCAGGGSRGGEGGRAPREGPAGNGRDRGRSHAAEAPGDPQAAASLLAPMDVGEEPL
EKAARARTAKDPNTYKVLSLVLSVCVLTTILGCIFGLKPSCAKEVKSCKGRCFERTFGNC
RCDAACVELGNCCLDYQETCIEPEHIWTCNKFRCGEKRLTRSLCACSDDCKDKGDCCINY
SSVCQGEKSWVEEPCESINEPQCPAGFETPPTLLFSLDGFRAEYLHTWGGLLPVISKLKK
CGTYTKNMRPVYPTKTFPNHYSIVTGLYPESHGIIDNKMYDPKMNASFSLKSKEKFNPEW
YKGEPIWVTAKYQGLKSGTFFWPGSDVEINGIFPDIYKMYNGSVPFEERILAVLQWLQLP
KDERPHFYTLYLEEPDSSGHSYGPVSSEVIKALQRVDGMVGMLMDGLKELNLHRCLNLIL
ISDHGMEQGSCKKYIYLNKYLGDVKNIKVIYGPAARLRPSDVPDKYYSFNYEGIARNLSC
REPNQHFKPYLKHFLPKRLHFAKSDRIEPLTFYLDPQWQLALNPSERKYCGSGFHGSDNV
FSNMQALFVGYGPGFKHGIEADTFENIEVYNLMCDLLNLTPAPNNGTHGSLNHLLKNPVY
TPKHPKEVHPLVQCPFTRNPRDNLGCSCNPSILPIEDFQTQFNLTVAEEKIIKHETLPYG
RPRVLQKENTICLLSQHQFMSGYSQDILMPLWTSYTVDRNDSFSTEDFSNCLYQDFRIPL
SPVHKCSFYKNNTKVSYGFLSPPQLNKNSSGIYSEALLTTNIVPMYQSFQVIWRYFHDTL
LRKYAEERNGVNVVSGPVFDFDYDGRCDSLENLRQKRRVIRNQEILIPTHFFIVLTSCKD
TSQTPLHCENLDTLAFILPHRTDNSESCVHGKHDSSWVEELLMLHRARITDVEHITGLSF
YQQRKEPVSDILKLKTHLPTFSQED
|
| Enzyme 38 Number of Residues |
925 |
| Enzyme 38 Molecular Weight |
104923.6 |
| Enzyme 38 Theoretical pI |
7.14 |
| Enzyme 38 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- ion binding
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- pattern binding
- polysaccharide binding
- receptor activity
- scavenger receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- immune response
- immune system process
- metabolic process
|
| Component |
| — |
|
| Enzyme 38 General Function |
Involved in catalytic activity |
| Enzyme 38 Specific Function |
Involved primarily in ATP hydrolysis at the plasma membrane. Plays a role in regulating pyrophosphate levels, and functions in bone mineralization and soft tissue calcification. In vitro, has a broad specificity, hydrolyzing other nucleoside 5' triphosphates such as GTP, CTP, TTP and UTP to their corresponding monophosphates with release of pyrophosphate and diadenosine polyphosphates, and also 3',5'-cAMP to AMP. May also be involved in the regulation of the availability of nucleotide sugars in the endoplasmic reticulum and Golgi, and the regulation of purinergic signaling. Appears to modulate insulin sensitivity |
| Enzyme 38 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760 )
- Pantothenate and CoA Biosynthesis (map00770 )
- Purine Metabolism (map00230 )
- Riboflavin Metabolism (map00740 )
- Starch and Sucrose Metabolism (map00500 )
|
| Enzyme 38 Reactions |
- a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
170650661 |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
P22413 |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
ENPP1_HUMAN |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>2778 bp
ATGGAGCGCGACGGCTGCGCGGGGGGCGGGAGCCGCGGCGGCGAGGGCGGGCGCGCTCCC
CGGGAGGGCCCGGCGGGGAACGGCCGCGATCGGGGCCGCAGCCACGCTGCCGAGGCGCCC
GGGGACCCGCAGGCGGCCGCGTCCTTGCTGGCCCCTATGGACGTGGGGGAGGAGCCGCTG
GAGAAGGCGGCGCGCGCCCGCACTGCCAAGGACCCCAACACCTATAAAGTACTCTCGCTG
GTATTGTCAGTATGTGTGTTAACAACAATACTTGGTTGTATATTTGGGTTGAAACCAAGC
TGTGCCAAAGAAGTTAAAAGTTGCAAAGGTCGCTGTTTCGAGAGAACATTTGGGAACTGT
CGCTGTGATGCTGCCTGTGTTGAGCTTGGAAACTGCTGTTTAGATTACCAGGAGACGTGC
ATAGAACCAGAACATATATGGACTTGCAACAAATTCAGGTGTGGTGAGAAAAGGTTGACC
AGAAGCCTCTGTGCCTGTTCAGATGACTGCAAGGACAAGGGCGACTGCTGCATCAACTAC
AGTTCTGTGTGTCAAGGTGAGAAAAGTTGGGTAGAAGAACCATGTGAGAGCATTAATGAG
CCACAGTGCCCAGCAGGGTTTGAAACGCCTCCTACCCTCTTATTTTCTTTGGATGGATTC
AGGGCAGAATATTTACACACTTGGGGTGGACTTCTTCCTGTTATTAGCAAACTAAAAAAA
TGTGGAACATATACTAAAAACATGAGACCGGTATATCCAACAAAAACTTTCCCCAATCAC
TACAGCATTGTCACCGGATTGTATCCAGAATCTCATGGCATAATCGACAATAAAATGTAT
GATCCCAAAATGAATGCTTCCTTTTCACTTAAAAGTAAAGAGAAATTTAATCCTGAGTGG
TACAAAGGAGAACCAATTTGGGTCACAGCTAAGTATCAAGGCCTCAAGTCTGGCACATTT
TTCTGGCCAGGATCAGATGTGGAAATTAACGGAATTTTCCCAGACATCTATAAAATGTAT
AATGGTTCAGTACCATTTGAAGAAAGGATTTTAGCTGTTCTTCAGTGGCTACAGCTTCCT
AAAGATGAAAGACCACACTTTTACACTCTGTATTTAGAAGAACCAGATTCTTCAGGTCAT
TCATATGGACCAGTCAGCAGTGAAGTCATCAAAGCCTTGCAGAGGGTTGATGGTATGGTT
GGTATGCTGATGGATGGTCTGAAAGAGCTGAACTTGCACAGATGCCTGAACCTCATCCTT
ATTTCAGATCATGGCATGGAACAAGGCAGTTGTAAGAAATACATATATCTGAATAAATAT
TTGGGGGATGTTAAAAATATTAAAGTTATCTATGGACCTGCAGCTCGATTGAGACCCTCT
GATGTCCCAGATAAATACTATTCATTTAACTATGAAGGCATTGCCCGAAATCTTTCTTGC
CGGGAACCAAACCAGCACTTCAAACCTTACCTGAAACATTTCTTACCTAAGCGTTTGCAC
TTTGCTAAGAGTGATAGAATTGAGCCCTTGACATTCTATTTGGACCCTCAGTGGCAACTT
GCATTGAATCCCTCAGAAAGGAAATATTGTGGAAGTGGATTTCATGGCTCTGACAATGTA
TTTTCAAATATGCAAGCCCTCTTTGTTGGCTATGGACCTGGATTCAAGCATGGCATTGAG
GCTGACACCTTTGAAAACATTGAAGTCTATAACTTAATGTGTGATTTACTGAATTTGACA
CCGGCTCCTAATAACGGAACTCATGGAAGTCTTAACCACCTTCTAAAGAATCCTGTTTAT
ACGCCAAAGCATCCCAAAGAAGTGCACCCCCTGGTACAGTGCCCCTTCACAAGAAACCCC
AGAGATAACCTTGGCTGCTCATGTAACCCTTCGATTTTGCCGATTGAGGATTTTCAAACA
CAGTTCAATCTGACTGTGGCAGAAGAGAAGATTATTAAGCATGAAACTTTACCCTATGGA
AGACCTAGAGTTCTCCAGAAGGAAAACACCATCTGTCTTCTTTCCCAGCACCAGTTTATG
AGTGGATACAGCCAAGACATCTTAATGCCCCTTTGGACATCCTATACCGTGGACAGAAAT
GACAGTTTCTCTACGGAAGACTTCTCCAACTGTCTGTACCAGGACTTTAGAATTCCTCTT
AGTCCTGTCCATAAATGTTCATTTTATAAAAATAACACCAAAGTGAGTTACGGGTTCCTC
TCCCCACCACAACTAAATAAAAATTCAAGTGGAATATATTCTGAAGCTTTGCTTACTACA
AATATAGTGCCAATGTACCAGAGTTTTCAAGTTATATGGCGCTACTTTCATGACACCCTA
CTGCGAAAGTATGCTGAAGAAAGAAATGGTGTCAATGTCGTCAGTGGTCCTGTGTTTGAC
TTTGATTATGATGGACGTTGTGATTCCTTAGAGAATCTGAGGCAAAAAAGAAGAGTCATC
CGTAACCAAGAAATTTTGATTCCAACTCACTTCTTTATTGTGCTAACAAGCTGTAAAGAT
ACATCTCAGACGCCTTTGCACTGTGAAAACCTAGACACCTTAGCTTTCATTTTGCCTCAC
AGGACTGATAACAGCGAGAGCTGTGTGCATGGGAAGCATGACTCCTCATGGGTTGAAGAA
TTGTTAATGTTACACAGAGCACGGATCACAGATGTTGAGCACATCACTGGACTCAGCTTC
TATCAACAAAGAAAAGAGCCAGTTTCAGACATTTTAAAGTTGAAAACACATTTGCCAACC
TTTAGCCAAGAAGACTGA
|
| Enzyme 38 GenBank Gene ID |
NM_006208.2 |
| Enzyme 38 GeneCard ID |
ENPP1 |
| Enzyme 38 GenAtlas ID |
ENPP1 |
| Enzyme 38 HGNC ID |
HGNC:3356 |
| Enzyme 38 Chromosome Location |
6 |
| Enzyme 38 Locus |
6q22-q23 |
| Enzyme 38 SNPs |
SNPJam Report |
| Enzyme 38 General References |
- Buckley MF, Loveland KA, McKinstry WJ, Garson OM, Goding JW: Plasma cell membrane glycoprotein PC-1. cDNA cloning of the human molecule, amino acid sequence, and chromosomal location. J Biol Chem. 1990 Oct 15;265(29):17506-11. [PubMed ]
- Funakoshi I, Kato H, Horie K, Yano T, Hori Y, Kobayashi H, Inoue T, Suzuki H, Fukui S, Tsukahara M, et al.: Molecular cloning of cDNAs for human fibroblast nucleotide pyrophosphatase. Arch Biochem Biophys. 1992 May 15;295(1):180-7. [PubMed ]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Pizzuti A, Frittitta L, Argiolas A, Baratta R, Goldfine ID, Bozzali M, Ercolino T, Scarlato G, Iacoviello L, Vigneri R, Tassi V, Trischitta V: A polymorphism (K121Q) of the human glycoprotein PC-1 gene coding region is strongly associated with insulin resistance. Diabetes. 1999 Sep;48(9):1881-4. [PubMed ]
- Belli SI, Goding JW: Biochemical characterization of human PC-1, an enzyme possessing alkaline phosphodiesterase I and nucleotide pyrophosphatase activities. Eur J Biochem. 1994 Dec 1;226(2):433-43. [PubMed ]
- Belli SI, Mercuri FA, Sali A, Goding JW: Autophosphorylation of PC-1 (alkaline phosphodiesterase I/nucleotide pyrophosphatase) and analysis of the active site. Eur J Biochem. 1995 Mar 15;228(3):669-76. [PubMed ]
- Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed ]
- Bello V, Goding JW, Greengrass V, Sali A, Dubljevic V, Lenoir C, Trugnan G, Maurice M: Characterization of a di-leucine-based signal in the cytoplasmic tail of the nucleotide-pyrophosphatase NPP1 that mediates basolateral targeting but not endocytosis. Mol Biol Cell. 2001 Oct;12(10):3004-15. [PubMed ]
- Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed ]
- Nakamura I, Ikegawa S, Okawa A, Okuda S, Koshizuka Y, Kawaguchi H, Nakamura K, Koyama T, Goto S, Toguchida J, Matsushita M, Ochi T, Takaoka K, Nakamura Y: Association of the human NPPS gene with ossification of the posterior longitudinal ligament of the spine (OPLL). Hum Genet. 1999 Jun;104(6):492-7. [PubMed ]
- Rutsch F, Ruf N, Vaingankar S, Toliat MR, Suk A, Hohne W, Schauer G, Lehmann M, Roscioli T, Schnabel D, Epplen JT, Knisely A, Superti-Furga A, McGill J, Filippone M, Sinaiko AR, Vallance H, Hinrichs B, Smith W, Ferre M, Terkeltaub R, Nurnberg P: Mutations in ENPP1 are associated with 'idiopathic' infantile arterial calcification. Nat Genet. 2003 Aug;34(4):379-81. [PubMed ]
- Cheng KS, Chen MR, Ruf N, Lin SP, Rutsch F: Generalized arterial calcification of infancy: different clinical courses in two affected siblings. Am J Med Genet A. 2005 Jul 15;136(2):210-3. [PubMed ]
- Bacci S, Ludovico O, Prudente S, Zhang YY, Di Paola R, Mangiacotti D, Rauseo A, Nolan D, Duffy J, Fini G, Salvemini L, Amico C, Vigna C, Pellegrini F, Menzaghi C, Doria A, Trischitta V: The K121Q polymorphism of the ENPP1/PC-1 gene is associated with insulin resistance/atherogenic phenotypes, including earlier onset of type 2 diabetes and myocardial infarction. Diabetes. 2005 Oct;54(10):3021-5. [PubMed ]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
5354 |
| Enzyme 39 Name |
Peroxisomal sarcosine oxidase |
| Enzyme 39 Synonyms |
- PSO
- L-pipecolate oxidase
- L-pipecolic acid oxidase
|
| Enzyme 39 Gene Name |
PIPOX |
| Enzyme 39 Protein Sequence |
>Peroxisomal sarcosine oxidase
MAAQKDLWDAIVIGAGIQGCFTAYHLAKHRKRILLLEQFFLPHSRGSSHGQSRIIRKAYL
EDFYTRMMHECYQIWAQLEHEAGTQLHRQTGLLLLGMKENQELKTIQANLSRQRVEHQCL
SSEELKQRFPNIRLPRGEVGLLDNSGGVIYAYKALRALQDAIRQLGGIVRDGEKVVEINP
GLLVTVKTTSRSYQAKSLVITAGPWTNQLLRPLGIEMPLQTLRINVCYWREMVPGSYGVS
QAFPCFLWLGLCPHHIYGLPTGEYPGLMKVSYHHGNHADPEERDCPTARTDIGDVQILSS
FVRDHLPDLKPEPAVIESCMYTNTPDEQFILDRHPKYDNIVIGAGFSGHGFKLAPVVGKI
LYELSMKLTPSYDLAPFRISRFPSLGKAHL
|
| Enzyme 39 Number of Residues |
390 |
| Enzyme 39 Molecular Weight |
44065.5 |
| Enzyme 39 Theoretical pI |
8.54 |
| Enzyme 39 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH group of donors
- oxidoreductase activity, acting on the CH-NH group of donors, oxygen as acceptor
- sarcosine oxidase activity
|
| Process |
- cellular aromatic compound metabolic process
- cellular metabolic process
- folic acid and derivative metabolic process
- metabolic process
- oxidation reduction
- tetrahydrofolate metabolic process
|
| Component |
| — |
|
| Enzyme 39 General Function |
Involved in oxidoreductase activity |
| Enzyme 39 Specific Function |
Metabolizes sarcosine, L-pipecolic acid and L-proline |
| Enzyme 39 Pathways |
|
| Enzyme 39 Reactions |
- L-pipecolate + O2 = 2,3,4,5-tetrahydropyridine-2-carboxylate + H2O2 [RN:R02204]
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
7157903 |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q9P0Z9 |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
SOX_HUMAN |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1173 bp
ATGGCGGCTCAGAAAGATCTCTGGGACGCCATTGTGATTGGGGCGGGGATCCAGGGCTGC
TTCACTGCATACCACCTCGCCAAACACAGGAAGAGGATCCTCCTGCTGGAGCAGTTCTTT
CTACCACACTCCCGAGGAAGCTCCCATGGACAAAGCCGGATAATCCGAAAGGCGTACCTG
GAAGACTTTTACACCCGGATGATGCATGAGTGCTATCAGATATGGGCCCAGCTGGAGCAC
GAGGCTGGAACCCAATTGCACAGGCAGACTGGATTACTGCTGCTGGGAATGAAAGAGAAT
CAAGAATTAAAGACAATCCAGGCCAATCTGTCGAGGCAGAGGGTAGAACACCAGTGTCTT
TCATCTGAGGAACTGAAGCAACGTTTCCCAAATATTCGGTTGCCCAGGGGAGAAGTGGGG
CTCTTGGACAATTCCGGAGGAGTTATCTATGCATATAAGGCCCTCAGAGCCCTGCAGGAT
GCAATTCGACAGCTAGGAGGCATAGTGCGTGACGGAGAGAAGGTGGTGGAGATAAACCCA
GGGCTACTGGTCACGGTGAAAACCACCTCCAGGAGCTACCAAGCTAAGAGCTTGGTCATC
ACAGCAGGTCCTTGGACCAACCAGCTCCTCCGTCCCCTGGGCATTGAGATGCCTCTCCAG
ACCCTGCGGATCAACGTGTGTTACTGGCGAGAGATGGTTCCTGGGAGCTATGGTGTGTCC
CAGGCCTTTCCGTGCTTCCTGTGGCTGGGCTTGTGTCCCCACCACATCTACGGACTGCCC
ACAGGAGAGTACCCAGGGCTGATGAAGGTCAGCTATCACCACGGCAACCACGCAGACCCT
GAGGAGCGGGACTGCCCCACAGCACGCACAGACATCGGAGACGTCCAGATCCTGAGCAGC
TTTGTCAGAGATCACTTACCTGATCTGAAGCCCGAGCCTGCTGTCATTGAGAGCTGCATG
TACACGAATACCCCTGATGAGCAGTTCATTCTCGATCGCCACCCAAAGTATGACAACATT
GTCATTGGTGCTGGATTCTCTGGGCACGGGTTCAAGCTGGCCCCTGTGGTGGGGAAGATC
CTGTATGAATTAAGCATGAAATTAACACCATCTTATGACTTGGCACCTTTTCGAATCAGC
CGTTTCCCAAGCCTGGCCAAAGCCCACCTGTGA
|
| Enzyme 39 GenBank Gene ID |
AF134593 |
| Enzyme 39 GeneCard ID |
PIPOX |
| Enzyme 39 GenAtlas ID |
PIPOX |
| Enzyme 39 HGNC ID |
HGNC:17804 |
| Enzyme 39 Chromosome Location |
1 |
| Enzyme 39 Locus |
17q11.2 |
| Enzyme 39 SNPs |
SNPJam Report |
| Enzyme 39 General References |
- IJlst L, de Kromme I, Oostheim W, Wanders RJ: Molecular cloning and expression of human L-pipecolate oxidase. Biochem Biophys Res Commun. 2000 Apr 21;270(3):1101-5. [PubMed ]
- Dodt G, Kim DG, Reimann SA, Reuber BE, McCabe K, Gould SJ, Mihalik SJ: L-Pipecolic acid oxidase, a human enzyme essential for the degradation of L-pipecolic acid, is most similar to the monomeric sarcosine oxidases. Biochem J. 2000 Feb 1;345 Pt 3:487-94. [PubMed ]
- Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
5355 |
| Enzyme 40 Name |
Peroxisomal N(1)-acetyl-spermine/spermidine oxidase |
| Enzyme 40 Synonyms |
- Polyamine oxidase
|
| Enzyme 40 Gene Name |
PAOX |
| Enzyme 40 Protein Sequence |
>Peroxisomal N(1)-acetyl-spermine/spermidine oxidase
MESTGSVGEAPGGPRVLVVGGGIAGLGAAQRLCGHSAFPHLRVLEATARAGGRIRSERCF
GGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLVETGGHVGLPSVSYASSGT
SVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKEIGQHVARLCGHSAFPHLR
VLEATARAGGRIRSERCFGGVVEVGAHWIHGPSRGNPVFQLAAEYGLLGEKELSQENQLV
ETGGHVGLPSVSYASSGASVSLQLVAEMATLFYGLIDQTREFLHAAETPVPSVGEYLKKE
IGQHVAGWTEDEETRKLKLAVLNSFFNLECCVSGTHSMDLVALAPFGEYTVLPGLDCTFS
KGYQGLTNCMMAALPEDTVVFEKPVKTIHWNGSFQEAAFPGETFPVSVECEDGDRFPAHH
VIVTVPLGFLREHLDTFFDPPLPAEKAEAIRKIGFGTNNKIFLEFEEPFWEPDCQLIQLV
WEDTSPLEDAAPELQDAWFRKLIGFVVLPAFASVHVLCGFIAGLESEFMETLSDEEVLLC
LTQVLRRVTGNPRLPAPKSVLRSRWHSAPYTRGSYSYVAVGSTGGDLDLLAQPLPADGAG
AQLQILFAGEATHRTFYSTTHGALLSGWREADRLLSLWAPQVQQPRPRL
|
| Enzyme 40 Number of Residues |
649 |
| Enzyme 40 Molecular Weight |
70289.3 |
| Enzyme 40 Theoretical pI |
5.27 |
| Enzyme 40 GO Classification |
Not Available |
| Enzyme 40 General Function |
Amino acid transport and metabolism |
| Enzyme 40 Specific Function |
Flavoenzyme which catalyzes the oxidation of N(1)- acetylspermine to spermidine and is thus involved in the polyamine back-conversion. Can also oxidize N(1)-acetylspermidine to putrescine. Substrate specificity:N(1)-acetylspermine = N(1)- acetylspermidine > N(1),N(12)-diacylspermine >> spermine. Does not oxidize spermidine. Plays an important role in the regulation of polyamine intracellular concentration and has the potential to act as a determinant of cellular sensitivity to the antitumor polyamine analogs |
| Enzyme 40 Pathways |
Not Available |
| Enzyme 40 Reactions |
- (1) N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2 [RN:R09074]
- (2) N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2 [RN:R03899]
|
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
45439842 |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
Q6QHF9 |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
PAOX_HUMAN |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>1950 bp
ATGGAGTCGACCGGCAGCGTCGGGGAGGCCCCGGGCGGACCCCGGGTGCTGGTGGTGGGC
GGCGGCATCGCGGGGCTGGGCGCGGCGCAGAGGCTCTGCGGCCACTCCGCCTTCCCGCAC
CTACGGGTCCTGGAGGCCACGGCCCGTGCCGGGGGCCGCATCCGCTCGGAGCGCTGCTTC
GGTGGCGTGGTGGAGGTGGGCGCGCACTGGATCCATGGGCCCTCCCGGGGTAACCCCGTC
TTCCAGCTGGCTGCTGAGTACGGGCTGCTGGGGGAGAAGGAGCTGTCCCAGGAGAACCAG
CTGGTGGAGACCGGGGGTCACGTGGGCCTGCCCTCCGTGAGCTACGCCAGCTCCGGGACC
AGCGTGAGCCTCCAGCTGGTGGCGGAGATGGCGACTCTGTTCTACGGCCTGATAGACCAG
ACCCGGGAGTTCCTGCACGCTGCAGAGACCCCGGTGCCCAGCGTCGGGGAGTACCTCAAG
AAGGAGATTGGCCAGCACGTGGCGAGGCTCTGCGGCCACTCCGCCTTCCCACACCTGCGG
GTCCTGGAGGCCACGGCCCGCGCCGGGGGCCGCATCCGCTCGGAGCGCTGCTTCGGTGGC
GTGGTGGAGGTGGGCGCGCACTGGATCCATGGGCCCTCCCGGGGTAACCCCGTCTTCCAG
CTGGCTGCTGAGTACGGGCTGCTGGGGGAGAAGGAGCTGTCCCAGGAGAACCAGCTGGTG
GAGACCGGGGGTCACGTGGGCCTGCCCTCCGTGAGCTACGCCAGCTCCGGAGCCAGCGTG
AGCCTCCAGCTGGTGGCGGAGATGGCGACTCTGTTCTACGGCCTGATAGACCAGACCCGG
GAGTTCCTGCACGCTGCAGAGACCCCGGTGCCCAGCGTCGGGGAGTACCTCAAGAAGGAG
ATTGGCCAGCACGTGGCCGGCTGGACAGAGGATGAGGAGACCAGGAAGCTGAAGCTGGCC
GTCCTGAACTCCTTCTTCAACCTGGAATGCTGTGTGAGCGGCACCCACAGCATGGACCTG
GTGGCCCTGGCACCCTTTGGGGAGTATACCGTGCTGCCGGGGCTGGACTGCACCTTTTCT
AAGGGCTATCAAGGACTCACAAACTGCATGATGGCCGCCCTGCCGGAGGACACTGTAGTT
TTTGAGAAGCCTGTGAAGACCATCCACTGGAACGGGTCCTTCCAGGAGGCAGCCTTTCCC
GGGGAGACCTTTCCAGTGTCGGTAGAGTGTGAGGATGGAGACCGGTTCCCGGCGCACCAT
GTCATCGTCACCGTGCCCTTAGGTTTTCTTAGGGAACATTTGGACACCTTCTTTGACCCT
CCCCTGCCGGCTGAGAAGGCAGAAGCAATCAGGAAGATAGGCTTTGGGACCAACAACAAA
ATCTTCCTGGAGTTTGAGGAGCCCTTCTGGGAGCCAGACTGCCAGCTGATCCAGCTGGTG
TGGGAGGACACGTCGCCCCTGGAGGATGCTGCCCCTGAGCTACAGGACGCCTGGTTCCGG
AAGCTCATTGGCTTTGTGGTCCTGCCTGCCTTTGCGTCTGTCCACGTTCTCTGTGGGTTC
ATTGCCGGACTTGAGTCTGAGTTCATGGAGACTCTGTCGGATGAAGAAGTACTTCTGTGT
CTCACCCAAGTGCTCCGGAGAGTGACAGGAAACCCACGGCTCCCCGCGCCCAAGAGCGTC
CTGCGGTCTCGCTGGCACAGCGCCCCGTACACTAGGGGGTCCTACAGCTACGTGGCCGTG
GGCAGTACTGGGGGCGACCTGGACCTGCTGGCTCAGCCCCTCCCTGCAGACGGCGCCGGC
GCCCAGCTCCAGATCCTGTTTGCGGGGGAAGCCACACATCGCACGTTTTACTCCACGACG
CACGGGGCTCTGCTGTCGGGATGGAGGGAGGCCGACCGCCTCCTCAGTCTGTGGGCCCCG
CAGGTGCAGCAGCCCAGGCCGAGGCTCTAG
|
| Enzyme 40 GenBank Gene ID |
AY541520 |
| Enzyme 40 GeneCard ID |
PAOX |
| Enzyme 40 GenAtlas ID |
PAOX |
| Enzyme 40 HGNC ID |
HGNC:20837 |
| Enzyme 40 Chromosome Location |
1 |
| Enzyme 40 Locus |
10q26.3 |
| Enzyme 40 SNPs |
SNPJam Report |
| Enzyme 40 General References |
- Wu T, Yankovskaya V, McIntire WS: Cloning, sequencing, and heterologous expression of the murine peroxisomal flavoprotein, N1-acetylated polyamine oxidase. J Biol Chem. 2003 Jun 6;278(23):20514-25. Epub 2003 Mar 26. [PubMed ]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Vujcic S, Liang P, Diegelman P, Kramer DL, Porter CW: Genomic identification and biochemical characterization of the mammalian polyamine oxidase involved in polyamine back-conversion. Biochem J. 2003 Feb 15;370(Pt 1):19-28. [PubMed ]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
5358 |
| Enzyme 41 Name |
Aldehyde oxidase |
| Enzyme 41 Synonyms |
Not Available |
| Enzyme 41 Gene Name |
AOX1 |
| Enzyme 41 Protein Sequence |
>Aldehyde oxidase
MDRASELLFYVNGRKVIEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISRYN
PITKRIRHHPANACLIPICSLYGAAVTTVEGIGSTHTRIHPVQERIAKCHGTQCGFCTPG
MVMSIYTLLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDACKTFCKTSGCCQSKENGVCC
LDQGINGLPEFEEGSKTSPKLFAEEEFLPLDPTQELIFPPELMIMAEKQSQRTRVFGSER
MMWFSPVTLKELLEFKFKYPQAPVIMGNTSVGPEVKFKGVFHPVIISPDRIEELSVVNHA
YNGLTLGAGLSLAQVKDILADVVQKLPEEKTQMYHALLKHLGTLAGSQIRNMASLGGHII
SRHPDSDLNPILAVGNCTLNLLSKEGKRQIPLNEQFLSKCPNADLKPQEILVSVNIPYSR
KWEFVSAFRQAQRQENALAIVNSGMRVFFGEGDGIIRELCISYGGVGPATICAKNSCQKL
IGRHWNEQMLDIACRLILNEVSLLGSAPGGKVEFKRTLIISFLFKFYLEVSQILKKMDPV
HYPSLADKYESALEDLHSKHHCSTLKYQNIGPKQHPEDPIGHPIMHLSGVKHATGEAIYC
DDMPLVDQELFLTFVTSSRAHAKIVSIDLSEALSMPGVVDIMTAEHLSDVNSFCFFTEAE
KFLATDKVFCVGQLVCAVLADSEVQAKRAAKRVKIVYQDLEPLILTIEESIQHNSSFKPE
RKLEYGNVDEAFKVVDQILEGEIHMGGQEHFYMETQSMLVVPKGEDQEMDVYVSTQFPKY
IQDIVASTLKLPANKVMCHVRRVGGAFGGKVLKTGIIAAVTAFAANKHGRAVRCVLERGE
DMLITGGRHPYLGKYKAGFMNDGRILALDMEHYSNAGASLDESLFVIEMGLLKMDNAYKF
PNLRCRGWACRTNLPSNTAFRGFGFPQAALITESCITEVAAKCGLSPEKVRIINMYKEID
QTPYKQEINAKNLIQCWRECMAMSSYSLRKVAVEKFNAENYWKKKGLAMVPLKFPVGLGS
RAAGQAAALVHIYLDGSVLVTHGGIEMGQGVHTKMIQVVSRELRMPMSNVHLRGTSTETV
PNANISGGSVVADLNGLAVKDACQTLLKRLEPIISKNPKGTWKDWAQTAFDESINLSAVG
YFRGYESDMNWEKGEGQPFEYFVYGAACSEVEIDCLTGDHKNIRTDIVMDVGCSINPAID
IGQIEGAFIQGMGLYTIEELNYSPQGILHTRGPDQYKIPAICDMPTELHIALLPPSQNSN
TLYSSKGLGESGVFLGCSVFFAIHDAVSAARQERGLHGPLTLNSPLTPEKIRMACEDKFT
KMIPRDEPGSYVPWNVPI
|
| Enzyme 41 Number of Residues |
1338 |
| Enzyme 41 Molecular Weight |
147916.7 |
| Enzyme 41 Theoretical pI |
7.17 |
| Enzyme 41 GO Classification |
| Function |
- FAD or FADH2 binding
- NAD or NADH binding
- adenyl nucleotide binding
- binding
- catalytic activity
- cation binding
- electron carrier activity
- ion binding
- iron ion binding
- iron-sulfur cluster binding
- metal cluster binding
- metal ion binding
- nucleoside binding
- nucleotide binding
- oxidoreductase activity
- purine nucleoside binding
- transition metal ion binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 41 General Function |
Involved in oxidoreductase activity |
| Enzyme 41 Specific Function |
An aldehyde + H(2)O + O(2) = a carboxylic acid + H(2)O(2) |
| Enzyme 41 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760 )
- Tryptophan Metabolism (map00380 )
- Tyrosine Metabolism (map00350 )
- Valine, Leucine and Isoleucine Degradation (map00280 )
- Vitamin B6 Metabolism (map00750 )
|
| Enzyme 41 Reactions |
- an aldehyde + H2O + O2 = a carboxylic acid + H2O2 [RN:R00635]
|
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
71773480 |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
Q06278 |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
ADO_HUMAN |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>4017 bp
ATGGACCGGGCGTCCGAGCTGCTCTTCTACGTGAACGGCCGCAAGGTGATAGAAAAAAAT
GTCGATCCTGAAACAATGCTGTTGCCTTATTTGAGGAAGAAGCTTCGACTCACAGGAACT
AAGTATGGCTGTGGAGGAGGAGGCTGTGGTGCTTGTACAGTGATGATATCACGATACAAC
CCCATCACCAAGAGGATAAGGCATCACCCAGCCAATGCCTGTCTGATTCCCATCTGTTCT
CTGTATGGTGCTGCCGTCACCACAGTAGAAGGCATAGGAAGCACCCACACCAGAATTCAT
CCTGTTCAGGAGAGGATTGCCAAGTGTCATGGCACCCAGTGTGGCTTCTGCACACCTGGG
ATGGTGATGTCCATCTACACGCTGCTCAGGAACCACCCAGAGCCCACTCTGGATCAGTTA
ACTGATGCCCTTGGTGGTAACCTGTGCCGTTGCACTGGATACAGGCCCATAATTGATGCA
TGCAAGACTTTCTGTAAAACTTCGGGCTGCTGTCAAAGTAAAGAAAATGGGGTTTGCTGT
TTGGATCAAGGAATCAATGGATTGCCAGAATTTGAGGAAGGAAGTAAGACAAGTCCAAAA
CTCTTCGCAGAAGAGGAGTTTCTGCCATTGGATCCAACCCAGGAACTGATATTTCCTCCT
GAGCTAATGATAATGGCTGAGAAACAGTCGCAAAGGACCAGGGTGTTTGGCAGTGAGAGA
ATGATGTGGTTTTCCCCCGTGACCCTGAAGGAACTGCTGGAATTTAAATTCAAGTATCCC
CAGGCTCCTGTTATCATGGGAAACACCTCTGTGGGGCCTGAAGTGAAATTTAAAGGCGTC
TTTCACCCAGTTATAATTTCTCCTGATAGAATTGAAGAACTGAGTGTTGTAAACCATGCA
TATAATGGACTCACCCTTGGTGCTGGTCTCAGCCTAGCCCAGGTGAAGGACATTTTGGCT
GATGTAGTCCAGAAGCTTCCAGAGGAGAAGACACAGATGTACCATGCTCTCCTGAAGCAT
TTGGGAACTCTGGCTGGGTCCCAGATCAGGAACATGGCTTCTTTAGGGGGACACATCATT
AGCAGGCATCCAGATTCAGATCTGAATCCCATCCTGGCTGTGGGTAACTGTACCCTCAAC
TTGCTATCAAAAGAAGGAAAACGACAGATTCCTTTAAATGAGCAATTCCTCAGCAAGTGC
CCTAATGCAGATCTTAAGCCTCAAGAAATCTTGGTCTCAGTGAACATCCCCTACTCAAGG
AAGTGGGAATTTGTGTCAGCCTTCCGACAAGCCCAGCGACAGGAGAATGCGCTAGCGATA
GTCAATTCAGGAATGAGAGTCTTTTTTGGAGAAGGGGATGGCATTATTAGAGAGTTATGC
ATCTCATATGGAGGCGTTGGTCCAGCCACCATCTGTGCCAAGAATTCCTGCCAGAAACTC
ATTGGAAGGCACTGGAACGAACAGATGCTGGATATAGCCTGCAGGCTTATTCTGAATGAA
GTCTCCCTTTTGGGCTCGGCGCCAGGTGGGAAAGTGGAGTTCAAGAGGACTCTCATCATC
AGCTTCCTCTTCAAGTTCTACCTGGAAGTGTCACAGATTTTGAAAAAGATGGATCCAGTT
CACTATCCTAGCCTTGCAGACAAGTATGAAAGTGCTTTAGAAGATCTTCATTCCAAACAT
CACTGCAGTACATTAAAGTACCAGAATATAGGCCCAAAGCAGCATCCTGAAGACCCAATT
GGCCACCCCATCATGCATCTGTCTGGTGTGAAGCATGCCACGGGGGAGGCCATCTACTGT
GATGACATGCCTCTGGTGGACCAGGAACTTTTCTTGACTTTTGTGACTAGTTCAAGAGCT
CATGCTAAGATTGTGTCTATTGATCTGTCAGAAGCTCTCAGCATGCCCGGTGTGGTGGAC
ATCATGACAGCAGAACATCTTAGTGACGTCAACTCCTTCTGCTTTTTTACTGAAGCTGAG
AAATTTCTGGCGACAGATAAGGTGTTCTGTGTGGGTCAGCTTGTCTGTGCTGTGCTTGCC
GATTCTGAGGTTCAGGCAAAGCGAGCTGCTAAGCGAGTGAAGATTGTCTATCAAGACTTG
GAGCCGCTGATACTAACAATTGAGGAAAGTATACAACACAACTCCTCCTTCAAGCCAGAA
AGGAAACTGGAATATGGAAATGTTGACGAAGCATTTAAAGTGGTTGATCAAATTCTTGAA
GGTGAAATACATATGGGAGGTCAAGAACATTTTTATATGGAAACCCAAAGCATGCTTGTC
GTTCCCAAGGGAGAGGATCAAGAAATGGATGTCTACGTGTCCACACAGTTTCCCAAATAT
ATACAGGACATTGTTGCCTCAACCTTGAAGCTCCCAGCTAACAAGGTCATGTGCCATGTA
AGGCGTGTTGGTGGAGCGTTTGGAGGGAAGGTGTTAAAAACCGGAATCATTGCAGCCGTC
ACTGCATTTGCCGCAAACAAACATGGCCGTGCAGTTCGCTGTGTTCTGGAACGAGGAGAA
GACATGTTAATAACTGGAGGCCGCCATCCTTACCTTGGAAAGTACAAAGCTGGATTCATG
AACGATGGCAGAATCTTGGCCCTGGACATGGAGCATTACAGCAATGCAGGCGCCTCCTTG
GATGAATCATTATTCGTGATAGAAATGGGACTTCTGAAAATGGACAATGCTTACAAGTTT
CCCAATCTCCGCTGCCGGGGTTGGGCATGCAGAACCAACCTTCCATCCAACACAGCTTTT
CGTGGGTTTGGCTTTCCTCAGGCAGCGCTGATCACCGAATCTTGTATCACGGAAGTTGCA
GCCAAATGTGGACTATCCCCTGAGAAGGTGCGAATCATAAACATGTACAAGGAAATTGAT
CAAACACCCTACAAACAAGAGATCAATGCCAAGAACCTAATCCAGTGTTGGAGAGAATGT
ATGGCCATGTCTTCCTACTCCTTGAGGAAAGTTGCTGTGGAAAAGTTCAATGCAGAGAAT
TATTGGAAGAAGAAAGGACTGGCCATGGTCCCCCTGAAGTTTCCTGTTGGCCTTGGCTCA
CGTGCTGCTGGTCAGGCTGCTGCCTTGGTTCACATTTATCTTGATGGCTCTGTGCTGGTC
ACTCACGGTGGAATTGAAATGGGGCAGGGGGTCCACACTAAAATGATTCAGGTGGTCAGC
CGTGAATTAAGAATGCCAATGTCGAATGTCCACCTGCGTGGAACAAGCACAGAAACTGTC
CCTAATGCAAATATCTCTGGAGGTTCTGTGGTGGCAGATCTCAACGGTTTGGCAGTAAAG
GATGCCTGTCAAACTCTTCTAAAACGCCTCGAACCCATCATCAGCAAGAATCCTAAAGGA
ACTTGGAAAGACTGGGCACAGACTGCTTTTGATGAAAGCATTAACCTTTCAGCTGTTGGA
TACTTCAGAGGTTATGAGTCAGACATGAACTGGGAGAAAGGCGAAGGCCAGCCCTTCGAA
TACTTTGTTTATGGAGCTGCCTGTTCCGAGGTTGAAATAGACTGCCTGACGGGGGATCAT
AAGAACATCAGAACAGACATTGTCATGGATGTTGGCTGCAGTATAAATCCAGCCATTGAC
ATAGGCCAGATTGAAGGTGCATTTATTCAAGGCATGGGACTTTATACAATAGAGGAACTG
AATTATTCTCCCCAGGGCATTCTGCACACTCGTGGTCCAGACCAATATAAAATCCCTGCC
ATCTGTGACATGCCCACGGAGTTGCACATTGCTTTGTTGCCTCCTTCTCAAAACTCAAAT
ACTCTTTATTCATCTAAGGGTCTGGGAGAGTCGGGGGTGTTCCTGGGGTGTTCCGTGTTT
TTCGCTATCCATGACGCAGTGAGTGCAGCACGACAGGAGAGAGGCCTGCATGGACCCTTG
ACCCTTAATAGTCCACTGACCCCGGAGAAGATTAGGATGGCCTGTGAAGACAAGTTCACA
AAAATGATTCCGAGAGATGAACCTGGATCCTACGTTCCTTGGAATGTACCCATCTGA
|
| Enzyme 41 GenBank Gene ID |
NM_001159.3 |
| Enzyme 41 GeneCard ID |
AOX1 |
| Enzyme 41 GenAtlas ID |
AOX1 |
| Enzyme 41 HGNC ID |
HGNC:553 |
| Enzyme 41 Chromosome Location |
2 |
| Enzyme 41 Locus |
2q33 |
| Enzyme 41 SNPs |
SNPJam Report |
| Enzyme 41 General References |
- Wright RM, Vaitaitis GM, Wilson CM, Repine TB, Terada LS, Repine JE: cDNA cloning, characterization, and tissue-specific expression of human xanthine dehydrogenase/xanthine oxidase. Proc Natl Acad Sci U S A. 1993 Nov 15;90(22):10690-4. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
5367 |
| Enzyme 42 Name |
Lathosterol oxidase |
| Enzyme 42 Synonyms |
- C-5 sterol desaturase
- Delta(7)-sterol 5-desaturase
- Lathosterol 5-desaturase
- Sterol-C5-desaturase
|
| Enzyme 42 Gene Name |
SC5DL |
| Enzyme 42 Protein Sequence |
>Lathosterol oxidase
MDLVLRVADYYFFTPYVYPATWPEDDIFRQAISLLIVTNVGAYILYFFCATLSYYFVFDH
ALMKHPQFLKNQVRREIKFTVQALPWISILTVALFLLEIRGYSKLHDDLGEFPYGLFELV
VSIISFLFFTDMFIYWIHRGLHHRLVYKRLHKPHHIWKIPTPFASHAFHPIDGFLQSLPY
HIYPFIFPLHKVVYLSLYILVNIWTISIHDGDFRVPQILQPFINGSAHHTDHHMFFDYNY
GQYFTLWDRIGGSFKNPSSFEGKGPLSYVKEMTEGKRSSHSGNGCKNEKLFNGEFTKTE
|
| Enzyme 42 Number of Residues |
299 |
| Enzyme 42 Molecular Weight |
35300.6 |
| Enzyme 42 Theoretical pI |
8.24 |
| Enzyme 42 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- transition metal ion binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- organelle
|
|
| Enzyme 42 General Function |
Involved in iron ion binding |
| Enzyme 42 Specific Function |
Catalyzes a dehydrogenation to introduce C5-6 double bond into lathosterol |
| Enzyme 42 Pathways |
Not Available |
| Enzyme 42 Reactions |
- 5alpha-cholest-7-en-3beta-ol + NAD(P)H + H+ + O2 = cholesta-5,7-dien-3beta-ol + NAD(P)+ + 2 H2O [RN:R03310 R07215]
|
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
- 32-52
79-99
117-137
186-206
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
3721882 |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
O75845 |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
SC5D_HUMAN |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>900 bp
ATGGATCTTGTACTCCGTGTTGCAGATTACTATTTTTTTACACCATACGTGTATCCAGCC
ACATGGCCAGAAGATGACATCTTCCGACAAGCTATTAGTCTTCTGATTGTAACAAATGTT
GGTGCTTACATCCTTTATTTCTTCTGTGCAACACTGAGCTATTATTTTGTCTTCGATCAT
GCATTAATGAAACATCCACAATTTTTAAAGAATCAAGTCCGTCGAGAGATTAAGTTTACT
GTCCAGGCATTGCCATGGATAAGTATTCTTACTGTTGCACTGTTCTTGCTGGAGATAAGA
GGTTACAGCAAATTACATGATGACCTAGGAGAGTTTCCATATGGATTGTTTGAACTTGTC
GTTAGTATAATATCTTTCCTCTTTTTCACTGACATGTTCATCTACTGGATTCACAGAGGC
CTTCATCATAGACTGGTATATAAGCGCCTACATAAACCTCACCATATTTGGAAGATTCCT
ACTCCATTTGCAAGTCATGCTTTTCACCCTATTGATGGCTTTCTTCAGAGTCTACCTTAC
CATATATACCCTTTTATCTTTCCATTACACAAGGTGGTTTATTTAAGTCTGTACATCTTG
GTTAATATCTGGACAATTTCCATTCATGACGGTGATTTTCGTGTCCCCCAAATCTTACAG
CCATTTATTAATGGCTCAGCTCATCATACAGACCACCATATGTTCTTTGACTATAATTAT
GGACAATATTTCACTTTGTGGGATAGGATTGGCGGCTCATTCAAAAATCCTTCATCCTTT
GAGGGGAAGGGACCGCTCAGTTATGTGAAGGAGATGACAGAGGGAAAGCGCAGCAGCCCT
TCAGGAAATGGCTGTAAGAATGAAAAATTATTCAATGGAGAGTTTACAAAGACTGAATAG
|
| Enzyme 42 GenBank Gene ID |
AB016247 |
| Enzyme 42 GeneCard ID |
SC5DL |
| Enzyme 42 GenAtlas ID |
SC5DL |
| Enzyme 42 HGNC ID |
HGNC:10547 |
| Enzyme 42 Chromosome Location |
1 |
| Enzyme 42 Locus |
11q23.3 |
| Enzyme 42 SNPs |
SNPJam Report |
| Enzyme 42 General References |
- Matsushima M, Inazawa J, Takahashi E, Suzumori K, Nakamura Y: Molecular cloning and mapping of a human cDNA (SC5DL) encoding a protein homologous to fungal sterol-C5-desaturase. Cytogenet Cell Genet. 1996;74(4):252-4. [PubMed ]
- Husselstein T, Schaller H, Gachotte D, Benveniste P: Delta7-sterol-C5-desaturase: molecular characterization and functional expression of wild-type and mutant alleles. Plant Mol Biol. 1999 Mar;39(5):891-906. [PubMed ]
- Nishi S, Nishino H, Ishibashi T: cDNA cloning of the mammalian sterol C5-desaturase and the expression in yeast mutant. Biochim Biophys Acta. 2000 Jan 31;1490(1-2):106-8. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Brunetti-Pierri N, Corso G, Rossi M, Ferrari P, Balli F, Rivasi F, Annunziata I, Ballabio A, Russo AD, Andria G, Parenti G: Lathosterolosis, a novel multiple-malformation/mental retardation syndrome due to deficiency of 3beta-hydroxysteroid-delta5-desaturase. Am J Hum Genet. 2002 Oct;71(4):952-8. Epub 2002 Aug 20. [PubMed ]
- Krakowiak PA, Wassif CA, Kratz L, Cozma D, Kovarova M, Harris G, Grinberg A, Yang Y, Hunter AG, Tsokos M, Kelley RI, Porter FD: Lathosterolosis: an inborn error of human and murine cholesterol synthesis due to lathosterol 5-desaturase deficiency. Hum Mol Genet. 2003 Jul 1;12(13):1631-41. [PubMed ]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
5375 |
| Enzyme 43 Name |
Dimethylaniline monooxygenase [N-oxide-forming] 5 |
| Enzyme 43 Synonyms |
- Dimethylaniline oxidase 5
- Hepatic flavin-containing monooxygenase 5
- FMO 5
|
| Enzyme 43 Gene Name |
FMO5 |
| Enzyme 43 Protein Sequence |
>Dimethylaniline monooxygenase [N-oxide-forming] 5
MTKKRIAVIGGGVSGLSSIKCCVEEGLEPVCFERTDDIGGLWRFQENPEEGRASIYKSVI
INTSKEMMCFSDYPIPDHYPNFMHNAQVLEYFRMYAKEFDLLKYIRFKTTVCSVKKQPDF
ATSGQWEVVTESEGKKEMNVFDGVMVCTGHHTNAHLPLESFPGIEKFKGQYFHSRDYKNP
EGFTGKRVIIIGIGNSGGDLAVEISQTAKQVFLSTRRGAWILNRVGDYGYPADVLFSSRL
THFIWKICGQSLANKYLEKKINQRFDHEMFGLKPKHRALSQHPTLNDDLPNRIISGLVKV
KGNVKEFTETAAIFEDGSREDDIDAVIFATGYSFDFPFLEDSVKVVKNKISLYKKVFPPN
LERPTLAIIGLIQPLGAIMPISELQGRWATQVFKGLKTLPSQSEMMAEISKAQEEIDKRY
VESQRHTIQGDYIDTMEELADLVGVRPNLLSLAFTDPKLALHLLLGPCTPIHYRVQGPGK
WDGARKAILTTDDRIRKPLMTRVVERSSSMTSTMTIGKFMLALAFFAIIIAYF
|
| Enzyme 43 Number of Residues |
533 |
| Enzyme 43 Molecular Weight |
60220.0 |
| Enzyme 43 Theoretical pI |
8.36 |
| Enzyme 43 GO Classification |
| Function |
- FAD or FADH2 binding
- NADP or NADPH binding
- adenyl nucleotide binding
- binding
- catalytic activity
- flavin-containing monooxygenase activity
- monooxygenase activity
- nucleoside binding
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- cell part
- intrinsic to endoplasmic reticulum membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 43 General Function |
Involved in flavin-containing monooxygenase activity |
| Enzyme 43 Specific Function |
In contrast with other forms of FMO it does not seem to be a drug-metabolizing enzyme |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
- N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
|
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
189054435 |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P49326 |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
FMO5_HUMAN |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>1602 bp
ATGACTAAGAAAAGAATTGCTGTGATTGGGGGAGGAGTGAGCGGGCTCTCTTCCATCAAG
TGCTGCGTAGAAGAAGGCTTGGAACCTGTCTGCTTTGAAAGGACTGATGACATCGGAGGG
CTCTGGAGGTTCCAGGAAAATCCTGAAGAAGGAAGGGCCAGTATTTACAAATCAGTGATC
ATCAATACTTCTAAAGAGATGATGTGCTTCAGTGACTATCCAATCCCAGATCATTATCCC
AACTTCATGCATAATGCCCAGGTCCTGGAGTATTTCAGGATGTATGCCAAAGAATTTGAC
CTTCTAAAGTATATTCGATTTAAGACCACTGTGTGCAGTGTGAAGAAGCAGCCTGATTTT
GCCACTTCAGGCCAATGGGAAGTGGTCACTGAATCTGAAGGGAAAAAGGAGATGAATGTC
TTTGATGGAGTCATGGTTTGCACTGGCCATCACACCAATGCTCATCTACCTCTGGAAAGC
TTCCCTGGAATTGAGAAGTTCAAAGGGCAGTACTTCCACAGTCGAGACTATAAGAACCCA
GAGGGATTCACTGGAAAGAGAGTCATTATAATTGGCATTGGGAATTCTGGAGGGGATCTG
GCTGTAGAGATTAGCCAAACAGCCAAGCAGGTTTTCCTCAGCACCAGGAGAGGGGCTTGG
ATCCTGAATCGTGTAGGGGACTACGGATATCCTGCTGATGTGTTGTTCTCTTCTCGACTT
ACACATTTTATATGGAAGATCTGTGGCCAATCATTAGCAAACAAATATTTGGAAAAAAAG
ATAAACCAAAGGTTTGACCATGAAATGTTTGGCCTGAAGCCTAAACACAGAGCTCTGAGT
CAGCATCCAACCTTAAATGATGACCTGCCAAATCGTATCATTTCTGGCTTGGTGAAAGTG
AAAGGAAATGTGAAGGAATTCACGGAGACAGCTGCCATATTTGAGGATGGCTCCAGGGAG
GATGACATTGATGCTGTTATCTTTGCCACAGGCTATAGCTTTGACTTTCCATTTCTGGAA
GATTCCGTCAAAGTGGTCAAAAACAAGATATCCCTGTATAAAAAGGTCTTCCCTCCTAAC
CTGGAAAGGCCAACTCTTGCAATCATAGGCTTGATTCAGCCCTTAGGAGCCATTATGCCC
ATTTCAGAGCTCCAAGGACGCTGGGCCACTCAGGTATTTAAAGGTCTAAAGACATTGCCC
TCACAGAGTGAAATGATGGCAGAAATATCTAAAGCTCAAGAGGAAATTGACAAAAGGTAT
GTGGAGAGCCAACGCCATACCATTCAGGGAGACTACATAGATACCATGGAAGAGCTTGCT
GATTTGGTGGGGGTCAGGCCCAATCTGCTGTCTCTGGCCTTCACTGACCCCAAGCTGGCA
TTACACTTATTACTGGGACCCTGCACTCCAATCCACTATCGTGTACAGGGCCCTGGAAAG
TGGGATGGGGCTCGAAAAGCTATCCTCACCACAGATGATCGCATCAGGAAGCCTCTGATG
ACAAGAGTAGTTGAAAGGAGTAGTTCTATGACTTCAACAATGACAATAGGCAAGTTTATG
CTAGCTCTTGCCTTCTTTGCTATAATTATAGCTTACTTCTAG
|
| Enzyme 43 GenBank Gene ID |
AK314647 |
| Enzyme 43 GeneCard ID |
FMO5 |
| Enzyme 43 GenAtlas ID |
FMO5 |
| Enzyme 43 HGNC ID |
HGNC:3773 |
| Enzyme 43 Chromosome Location |
1 |
| Enzyme 43 Locus |
1q21.1 |
| Enzyme 43 SNPs |
SNPJam Report |
| Enzyme 43 General References |
- Overby LH, Buckpitt AR, Lawton MP, Atta-Asafo-Adjei E, Schulze J, Philpot RM: Characterization of flavin-containing monooxygenase 5 (FMO5) cloned from human and guinea pig: evidence that the unique catalytic properties of FMO5 are not confined to the rabbit ortholog. Arch Biochem Biophys. 1995 Feb 20;317(1):275-84. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed ]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
5383 |
| Enzyme 44 Name |
Heme oxygenase 2 |
| Enzyme 44 Synonyms |
- HO-2
|
| Enzyme 44 Gene Name |
HMOX2 |
| Enzyme 44 Protein Sequence |
>Heme oxygenase 2
MSAEVETSEGVDESEKKNSGALEKENQMRMADLSELLKEGTKEAHDRAENTQFVKDFLKG
NIKKELFKLATTALYFTYSALEEEMERNKDHPAFAPLYFPMELHRKEALTKDMEYFFGEN
WEEQVQCPKAAQKYVERIHYIGQNEPELLVAHAYTRYMGDLSGGQVLKKVAQRALKLPST
GEGTQFYLFENVDNAQQFKQLYRARMNALDLNMKTKERIVEEANKAFEYNMQIFNELDQA
GSTLARETLEDGFPVHDGKGDMRKCPFYAAEQDKGALEGSSCPFRTAMAVLRKPSLQFIL
AAGVALAAGLLAWYYM
|
| Enzyme 44 Number of Residues |
316 |
| Enzyme 44 Molecular Weight |
36032.6 |
| Enzyme 44 Theoretical pI |
5.09 |
| Enzyme 44 GO Classification |
| Function |
- catalytic activity
- heme oxygenase (decyclizing) activity
- heme oxygenase (decyclizing) activity
- heme oxygenase (decyclizing) activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
|
| Process |
- heme metabolic process
- heme oxidation
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 44 General Function |
Involved in heme oxygenase (decyclizing) activity |
| Enzyme 44 Specific Function |
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter |
| Enzyme 44 Pathways |
|
| Enzyme 44 Reactions |
- heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O [RN:R00311]
|
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
187761307 |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
P30519 |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
HMOX2_HUMAN |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>951 bp
ATGTCAGCGGAAGTGGAAACCTCAGAGGGGGTAGACGAGTCAGAAAAAAAGAACTCTGGG
GCCCTAGAAAAGGAGAACCAAATGAGAATGGCTGACCTCTCGGAGCTCCTGAAGGAAGGG
ACCAAGGAAGCACACGACCGGGCAGAAAACACCCAGTTTGTCAAGGACTTCTTGAAAGGC
AACATTAAGAAGGAGCTGTTTAAGCTGGCCACCACGGCACTTTACTTCACATACTCAGCC
CTCGAGGAGGAAATGGAGCGCAACAAGGACCATCCAGCCTTTGCCCCTTTGTACTTCCCC
ATGGAGCTGCACCGGAAGGAGGCGCTGACCAAGGACATGGAGTATTTCTTTGGTGAAAAC
TGGGAGGAGCAGGTGCAGTGCCCCAAGGCTGCCCAGAAGTACGTGGAGCGGATCCACTAC
ATAGGGCAGAACGAGCCGGAGCTACTGGTGGCCCATGCATACACCCGCTACATGGGGGAT
CTCTCGGGGGGCCAGGTGCTGAAGAAGGTGGCCCAGCGAGCACTGAAACTCCCCAGCACA
GGGGAAGGGACCCAGTTCTACCTGTTTGAGAATGTGGACAATGCCCAGCAGTTCAAGCAG
CTCTACCGGGCCAGGATGAACGCCCTGGACCTGAACATGAAGACCAAAGAGAGGATCGTG
GAGGAGGCCAACAAGGCTTTTGAGTATAACATGCAGATATTCAATGAACTGGACCAGGCC
GGCTCCACACTGGCCAGAGAGACCTTGGAGGATGGGTTCCCTGTACACGATGGGAAAGGA
GACATGCGTAAATGCCCTTTCTACGCTGCTGAACAAGACAAAGGTGCCCTGGAGGGCAGC
AGCTGTCCCTTCCGAACAGCTATGGCTGTGCTGAGGAAGCCCAGCCTCCAGTTCATCCTG
GCCGCTGGTGTGGCCCTAGCTGCTGGACTCTTGGCCTGGTACTACATGTGA
|
| Enzyme 44 GenBank Gene ID |
NM_001127204.1 |
| Enzyme 44 GeneCard ID |
HMOX2 |
| Enzyme 44 GenAtlas ID |
HMOX2 |
| Enzyme 44 HGNC ID |
HGNC:5014 |
| Enzyme 44 Chromosome Location |
1 |
| Enzyme 44 Locus |
16p13.3 |
| Enzyme 44 SNPs |
SNPJam Report |
| Enzyme 44 General References |
- Ishikawa K, Takeuchi N, Takahashi S, Matera KM, Sato M, Shibahara S, Rousseau DL, Ikeda-Saito M, Yoshida T: Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2. J Biol Chem. 1995 Mar 17;270(11):6345-50. [PubMed ]
- McCoubrey WK Jr, Ewing JF, Maines MD: Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal. Arch Biochem Biophys. 1992 May 15;295(1):13-20. [PubMed ]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr: Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. J Biol Chem. 2007 Dec 28;282(52):37624-31. Epub 2007 Oct 26. [PubMed ]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
5388 |
| Enzyme 45 Name |
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial |
| Enzyme 45 Synonyms |
- P5C dehydrogenase
- Aldehyde dehydrogenase family 4 member A1
|
| Enzyme 45 Gene Name |
ALDH4A1 |
| Enzyme 45 Protein Sequence |
>Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
MLLPAPALRRALLSRPWTGAGLRWKHTSSLKVANEPVLAFTQGSPERDALQKALKDLKGR
MEAIPCVVGDEEVWTSDVQYQVSPFNHGHKVAKFCYADKSLLNKAIEAALAARKEWDLKP
IADRAQIFLKAADMLSGPRRAEILAKTMVGQGKTVIQAEIDAAAELIDFFRFNAKYAVEL
EGQQPISVPPSTNSTVYRGLEGFVAAISPFNFTAIGGNLAGAPALMGNVVLWKPSDTAML
ASYAVYRILREAGLPPNIIQFVPADGPLFGDTVTSSEHLCGINFTGSVPTFKHLWKQVAQ
NLDRFHTFPRLAGECGGKNFHFVHRSADVESVVSGTLRSAFEYGGQKCSACSRLYVPHSL
WPQIKGRLLEEHSRIKVGDPAEDFGTFFSAVIDAKSFARIKKWLEHARSSPSLTILAGGK
CDDSVGYFVEPCIVESKDPQEPIMKEEIFGPVLSVYVYPDDKYKETLQLVDSTTSYGLTG
AVFSQDKDVVQEATKVLRNAAGNFYINDKSTGSIVGQQPFGGARASGTNDKPGGPHYILR
WTSPQVIKETHKPLGDWSYAYMQ
|
| Enzyme 45 Number of Residues |
563 |
| Enzyme 45 Molecular Weight |
61718.9 |
| Enzyme 45 Theoretical pI |
8.20 |
| Enzyme 45 GO Classification |
| Function |
- 1-pyrroline-5-carboxylate dehydrogenase activity
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH group of donors
- oxidoreductase activity, acting on the CH-NH group of donors, NAD or NADP as acceptor
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- metabolic process
- oxidation reduction
- proline biosynthetic process
- proline metabolic process
|
| Component |
- cell part
- cytoplasmic part
- intracellular part
- mitochondrial matrix
- mitochondrial part
|
|
| Enzyme 45 General Function |
Involved in oxidoreductase activity |
| Enzyme 45 Specific Function |
Irreversible conversion of delta-1-pyrroline-5- carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes |
| Enzyme 45 Pathways |
|
| Enzyme 45 Reactions |
- (S)-1-pyrroline-5-carboxylate + NAD(P)+ + 2 H2O = L-glutamate + NAD(P)H + H+ [RN:R00707 R00708]
|
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
62896531 |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
P30038 |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
AL4A1_HUMAN |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>1692 bp
ATGCTGCTGCCGGCGCCCGCGCTCCGCCGCGCCCTGCTGTCCCGCCCCTGGACCGGGGCC
GGCCTGCGGTGGAAGCACACCTCCTCCCTGAAGGTGGCCAACGAGCCCGTCTTAGCCTTC
ACGCAGGGCAGCCCTGAGCGAGATGCCCTGCAAAAGGCCTTGAAGGACCTGAAGGGCCGG
ATGGAAGCCATCCCATGCGTGGTGGGGGATGAGGAGGTGTGGACGTCGGACGTGCAGTAC
CAAGTGTCGCCTTTTAACCATGGACATAAGGTGGCCAAGTTCTGTTATGCAGACAAGAGC
CTGCTCAACAAAGCCATTGAGGCTGCCCTGGCTGCCCGGAAAGAGTGGGACCTGAAGCCT
ATTGCAGACCGGGCCCAGATCTTCCTGAAGGCGGCAGACATGCTGAGTGGGCCGCGCAGG
GCTGAGATCCTCGCCAAGACCATGGTGGGACAGGGTAAGACCGTGATCCAAGCGGAGATT
GACGCTGCAGCGGAACTCATCGACTTCTTCCGGTTCAATGCCAAGTATGCGGTGGAGCTG
GAGGGGCAGCAGCCCATCAGCGTGCCCCCGAGCACCAACAGCACGGTGTACCGGGGTCTG
GAGGGCTTCGTGGCGGCCATCTCGCCCTTTAACTTCACTGCAATCGGCGGCAACCTGGCG
GGGGCACCGGCCCTGATAGGCAACGTGGTCCTATGGAAGCCCAGTGACACTGCCATGCTG
GCCAGCTATGCTGTCTACCGCATCCTTCGGGAGGCTGGCCTGCCCCCCAACATCATCCAG
TTTGTGCCAGCTGATGGGCCCCTATTTGGGGACACTGTCACCAGCTCAGAGCACCTCTGT
GGCATCAACTTCACAGGCAGTGTGCCCACCTTCAAACACCTGTGGAAGCAGGTGGCCCAG
AACCTGGACCGGTTCCACACCTTCCCACGCCTGGCTGGAGAGTGCGGCGGAAAGAACTTC
CACTTCGTGCACCGCTCGGCCGACGTGGAGAGCGTGGTGAGCGGGACCCTCCGCTCAGCC
TTCGAGTACGGTGGCCAGAAGTGTTCCGCCTGCTCGCGTCTCTACGTGCCGCACTCGCTG
TGGCCGCAGATCAAAGGGCGGCTGCTGGAGGAGCACAGTCGGATCAGAGTGGGCGACCCT
GCAGAGGATTTTGGGACCTTCTTCTCTGCAGTGATTGATGCCAAGTCCTTTGCCCGTATC
AAGAAGTGGCTGGAGCACGCACGCTCCTCACCCAGCCTCACCATCCTGGCCGGGGGCAAG
TGTGATGACTCCGTGGGCTACTTTGTGGAGCCCTGCATCGTGGAGAGCAAGGACCCTCAG
GAGCCCATCATGAAGGAGGAGATCTTCGGGCCTGTACTGTCTGTGTACGTCTACCCGGAT
GACAAGTACAAGGAGACGCTGCAGCTGGTTGACAGCACCACCAGCTATGGCCTCACGGGG
GCAGTGTTCTCCCAGGATAAGGACGTCGTGCAGGAGGCCACAAAGGTGCTGAGGAATGCT
GCCGGCAACTTCTACATCAACGACAAGTCCACTGGCTCGATAGTGGGCCAGCAGCCCTTT
GGGGGGGCCCGAGCCTCTGGAACCAATGACAAGCCAGGGGGCCCACACTACATCCTGCGC
TGGACGTCGCCGCAGGTCATCAAGGAGACACATAAGCCCCTGGGGGACTGGAGCTACGCG
TACATGCAGTGA
|
| Enzyme 45 GenBank Gene ID |
AK222486 |
| Enzyme 45 GeneCard ID |
ALDH4A1 |
| Enzyme 45 GenAtlas ID |
ALDH4A1 |
| Enzyme 45 HGNC ID |
HGNC:406 |
| Enzyme 45 Chromosome Location |
1 |
| Enzyme 45 Locus |
1p36 |
| Enzyme 45 SNPs |
SNPJam Report |
| Enzyme 45 General References |
- Hu CA, Lin WW, Valle D: Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase. J Biol Chem. 1996 Apr 19;271(16):9795-800. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Hempel J, Eckey R, Berie D, Romovacek H, Agarwal DP, Goedde HW: Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme. Comp Biochem Physiol B. 1992 Aug;102(4):791-93. [PubMed ]
- Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed ]
- Agarwal DP, Eckey R, Hempel J, Goedde HW: Human liver high Km aldehyde dehydrogenase (ALDH4): properties and structural relationship to the glutamic gamma-semialdehyde dehydrogenase. Adv Exp Med Biol. 1993;328:191-7. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Geraghty MT, Vaughn D, Nicholson AJ, Lin WW, Jimenez-Sanchez G, Obie C, Flynn MP, Valle D, Hu CA: Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia. Hum Mol Genet. 1998 Sep;7(9):1411-5. [PubMed ]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
5393 |
| Enzyme 46 Name |
Amine oxidase [flavin-containing] B |
| Enzyme 46 Synonyms |
- Monoamine oxidase type B
- MAO-B
|
| Enzyme 46 Gene Name |
MAOB |
| Enzyme 46 Protein Sequence |
>Amine oxidase [flavin-containing] B
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSY
VGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWR
TMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEV
SALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQ
TRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVY
YKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEER
LKKLCELYAKVLGSLEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDR
IYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTT
FLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
|
| Enzyme 46 Number of Residues |
520 |
| Enzyme 46 Molecular Weight |
58762.5 |
| Enzyme 46 Theoretical pI |
7.55 |
| Enzyme 46 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 46 General Function |
Involved in oxidoreductase activity |
| Enzyme 46 Specific Function |
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOB preferentially degrades benzylamine and phenylethylamine |
| Enzyme 46 Pathways |
|
| Enzyme 46 Reactions |
- RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853]
|
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
Not Available |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
P27338 |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
AOFB_HUMAN |
| Enzyme 46 PDB ID |
2BK3 |
| Enzyme 46 PDB File |
Show |
| Enzyme 46 3D Structure |
|
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>1560 bp
ATGAGCAACAAATGCGACGTGGTCGTGGTGGGGGGCGGCATCTCAGGTATGGCAGCAGCC
AAACTTCTGCATGACTCTGGACTGAATGTGGTTGTTCTGGAAGCCCGGGACCGTGTGGGA
GGCAGGACTTACACTCTTAGGAACCAAAAGGTTAAATATGTGGACCTTGGAGGATCCTAT
GTTGGACCAACCCAGAATCGTATCTTGAGATTAGCCAAGGAGCTAGGATTGGAGACCTAC
AAAGTGAATGAGGTTGAGCGTCTGATCCACCATGTAAAGGGCAAATCATACCCCTTCAGG
GGGCCATTCCCACCTGTATGGAATCCAATTACCTACTTAGATCATAACAACTTTTGGAGG
ACAATGGATGACATGGGGCGAGAGATTCCGAGTGATGCCCCATGGAAGGCTCCCCTTGCA
GAAGAGTGGGACAACATGACAATGAAGGAGCTACTGGACAAGCTCTGCTGGACTGAATCT
GCAAAGCAGCTTGCCACTCTCTTTGTGAACCTGTGTGTCACTGCAGAGACCCATGAGGTC
TCTGCTCTCTGGTTCCTGTGGTATGTGAAGCAGTGTGGAGGCACAACAAGAATCATCTCG
ACAACAAATGGAGGACAGGAGAGGAAATTTGTGGGCGGATCTGGTCAAGTGAGTGAGCGG
ATAATGGACCTCCTTGGAGACCGAGTGAAGCTGGAGAGGCCTGTGATCTACATTGACCAG
ACAAGAGAAAATGTCCTTGTGGAGACCCTAAACCATGAGATGTATGAGGCTAAATATGTG
ATTAGTGCTATTCCTCCTACTCTGGGCATGAAGATTCACTTCAATCCCCCTCTGCCAATG
ATGAGAAACCAGATGATCACTCGTGTGCCTTTGGGTTCAGTCATCAAGTGTATAGTTTAT
TATAAAGAGCCTTTCTGGAGGAAAAAGGATTACTGTGGAACCATGATTATTGATGGAGAA
GAAGCTCCAGTTGCCTACACGTTGGATGATACCAAACCTGAAGGCAACTATGCTGCCATA
ATGGGATTTATCCTGGCCCACAAAGCCAGAAAACTGGCACGTCTTACCAAAGAGGAAAGG
TTGAAGAAACTTTGTGAACTCTATGCCAAGGTTCTGGGTTCCCTAGAAGCTCTGGAGCCA
GTGCATTATGAAGAAAAGAACTGGTGTGAGGAGCAGTACTCTGGGGGCTGCTACACAACT
TATTTCCCCCCTGGGATCCTGACTCAATATGGAAGGGTTCTACGCCAGCCAGTGGACAGG
ATTTACTTTGCAGGCACCGAGACTGCCACACACTGGAGCGGCTACATGGAGGGGGCTGTA
GAGGCCGGGGAGAGAGCAGCCCGAGAGATCCTGCATGCCATGGGGAAGATTCCAGAGGAT
GAAATCTGGCAGTCAGAACCAGAGTCTGTGGATGTCCCTGCACAGCCCATCACCACCACC
TTTTTGGAGAGACATTTGCCCTCCGTGCCAGGCCTGCTCAGGCTGATTGGATTGACCACC
ATCTTTTCAGCAACGGCTCTTGGCTTCCTGGCCCACAAAAGGGGGCTACTTGTGAGAGTC
|
| Enzyme 46 GenBank Gene ID |
S62734 |
| Enzyme 46 GeneCard ID |
MAOB |
| Enzyme 46 GenAtlas ID |
MAOB |
| Enzyme 46 HGNC ID |
HGNC:6834 |
| Enzyme 46 Chromosome Location |
Not Available |
| Enzyme 46 Locus |
Not Available |
| Enzyme 46 SNPs |
SNPJam Report |
| Enzyme 46 General References |
- Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [PubMed ]
- Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed ]
- Chen K, Wu HF, Shih JC: The deduced amino acid sequences of human platelet and frontal cortex monoamine oxidase B are identical. J Neurochem. 1993 Jul;61(1):187-90. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed ]
- Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed ]
- Newton-Vinson P, Hubalek F, Edmondson DE: High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr Purif. 2000 Nov;20(2):334-45. [PubMed ]
- Cesura AM, Gottowik J, Lahm HW, Lang G, Imhof R, Malherbe P, Rothlisberger U, Da Prada M: Investigation on the structure of the active site of monoamine oxidase-B by affinity labeling with the selective inhibitor lazabemide and by site-directed mutagenesis. Eur J Biochem. 1996 Mar 15;236(3):996-1002. [PubMed ]
- Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed ]
- Binda C, Newton-Vinson P, Hubalek F, Edmondson DE, Mattevi A: Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol. 2002 Jan;9(1):22-6. [PubMed ]
- Binda C, Li M, Hubalek F, Restelli N, Edmondson DE, Mattevi A: Insights into the mode of inhibition of human mitochondrial monoamine oxidase B from high-resolution crystal structures. Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9750-5. Epub 2003 Aug 11. [PubMed ]
- Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A: Crystal structures of monoamine oxidase B in complex with four inhibitors of the N-propargylaminoindan class. J Med Chem. 2004 Mar 25;47(7):1767-74. [PubMed ]
- Hubalek F, Binda C, Khalil A, Li M, Mattevi A, Castagnoli N, Edmondson DE: Demonstration of isoleucine 199 as a structural determinant for the selective inhibition of human monoamine oxidase B by specific reversible inhibitors. J Biol Chem. 2005 Apr 22;280(16):15761-6. Epub 2005 Feb 14. [PubMed ]
- Binda C, Hubalek F, Li M, Herzig Y, Sterling J, Edmondson DE, Mattevi A: Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis. J Med Chem. 2005 Dec 29;48(26):8148-54. [PubMed ]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
5396 |
| Enzyme 47 Name |
Peroxisomal acyl-coenzyme A oxidase 2 |
| Enzyme 47 Synonyms |
- 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA 24-hydroxylase
- 3-alpha,7-alpha,12-alpha-trihydroxy-5-beta-cholestanoyl-CoA oxidase
- Trihydroxycoprostanoyl-CoA oxidase
- THCA-CoA oxidase
- THCCox
|
| Enzyme 47 Gene Name |
ACOX2 |
| Enzyme 47 Protein Sequence |
>Peroxisomal acyl-coenzyme A oxidase 2
MGSPVHRVSLGDTWSRQMHPDIESERYMQSFDVERLTNILDGGAQNTALRRKVESIIHSY
PEFSCKDNYFMTQNERYKAAMRRAFHIRLIARRLGWLEDGRELGYAYRALSGDVALNIHR
VFVRALRSLGSEEQIAKWDPLCKNIQIIATYAQTELGHGTYLQGLETEATYDAATQEFVI
HSPTLTATKWWPGDLGRSATHALVQAQLICSGARRGMHAFIVPIRSLQDHTPLPGIIIGD
IGPKMDFDQTDNGFLQLNHVRVPRENMLSRFAQVLPDGTYVKLGTAQSNYLPMVVVRVEL
LSGEILPILQKACVIAMRYSVIRRQSRLRPSDPEAKVLDYQTQQQKLFPQLAISYAFHFL
AVSLLEFFQHSYTAILNQDFSFLPELHALSTGMKAMMSEFCTQGAEMCRRACGGHGYSKL
SGLPSLVTKLSASCTYEGENTVLYLQVARFLVKSYLQTQMSPGSTPQRSLSPSVAYLTAP
DLARCPAQRAADFLCPELYTTAWAHVAVRLIKDSVQHLQTLTQSGADQHEAWNQTTVIHL
QAAKVHCYYVTVKGFTEALEKLENEPAIQQVLKRLCDLHAIHGILTNSGDFLHDAFLSGA
QVDMARTAYLDLLRLIRKDAILLTDAFDFTDQCLNSALGCYDGNVYERLFQWAQKSPTNT
QENPAYEEYIRPLLQSWRSKL
|
| Enzyme 47 Number of Residues |
681 |
| Enzyme 47 Molecular Weight |
76826.1 |
| Enzyme 47 Theoretical pI |
7.59 |
| Enzyme 47 GO Classification |
| Function |
- FAD or FADH2 binding
- acyl-CoA dehydrogenase activity
- acyl-CoA oxidase activity
- adenyl nucleotide binding
- binding
- catalytic activity
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
- purine nucleoside binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid beta-oxidation
- fatty acid catabolic process
- fatty acid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- microbody
- organelle
- peroxisome
|
|
| Enzyme 47 General Function |
Involved in acyl-CoA dehydrogenase activity |
| Enzyme 47 Specific Function |
Oxidizes the CoA esters of the bile acid intermediates di- and tri-hydroxycholestanoic acids |
| Enzyme 47 Pathways |
Not Available |
| Enzyme 47 Reactions |
- (25R)-3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-26-oyl-CoA + H2O + acceptor = (24R,25R)-3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestan-26- oyl-CoA + reduced acceptor [RN:R07374]
|
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
1780991 |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
Q99424 |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
ACOX2_HUMAN |
| Enzyme 47 PDB ID |
Not Available |
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>2046 bp
ATGGGCAGCCCAGTGCACCGAGTGTCATTGGGGGATACCTGGAGCAGGCAAATGCACCCC
GACATAGAGAGCGAGAGGTATATGCAGTCCTTTGACGTGGAACGGCTCACCAACATCCTT
GATGGAGGTGCCCAGAACACTGCACTCCGCAGGAAAGTTGAGAGCATCATCCACAGTTAC
CCGGAGTTTAGCTGTAAGGACAATTATTTCATGACCCAGAATGAGCGTTATAAGGCTGCC
ATGCGGAGGGCATTCCACATCCGGTTGATAGCTCGGCGCCTGGGTTGGTTAGAAGATGGT
CGTGAATTAGGCTACGCTTACAGAGCCCTTTCTGGAGACGTGGCCTTAAATATACACAGA
GTCTTCGTGAGAGCCCTCAGGAGCCTGGGCTCAGAGGAGCAGATTGCCAAATGGGACCCA
CTCTGCAAAAACATCCAGATCATCGCAACGTATGCACAGACAGAGTTGGGACATGGGACA
TATCTTCAGGGCCTGGAGACTGAAGCCACCTATGACGCAGCCACCCAGGAGTTTGTGATA
CACAGCCCCACGCTGACTGCCACCAAATGGTGGCCTGGAGACTTGGGACGGTCAGCCACC
CATGCCCTGGTCCAGGCCCAGCTGATCTGCTCAGGAGCCAGGCGGGGCATGCACGCTTTT
ATTGTGCCAATCCGGAGTCTTCAGGACCACACCCCACTGCCAGGAATCATCATTGGGGAC
ATCGGACCCAAGATGGACTTTGATCAAACAGACAATGGCTTCCTGCAGCTGAACCATGTG
CGGGTCCCCAGGGAGAACATGCTGAGTCGCTTTGCACAGGTCTTGCCAGATGGCACCTAC
GTCAAACTCGGTACAGCACAGAGCAACTACCTTCCCATGGTGGTGGTGCGGGTGGAGCTG
CTGTCAGGGGAGATCCTCCCTATACTGCAGAAGGCCTGTGTCATCGCCATGCGCTACTCG
GTCATCCGCCGCCAATCCCGGCTCCGGCCCAGTGACCCAGAGGCAAAGGTCCTGGACTAC
CAGACACAACAGCAGAAACTCTTTCCTCAGCTGGCCATCAGTTATGCCTTCCATTTCCTG
GCAGTCAGCCTCTTGGAGTTCTTCCAGCACTCCTACACTGCCATTCTGAACCAAGACTTC
AGCTTCCTGCCTGAGCTCCACGCGCTGAGCACGGGCATGAAGGCCATGATGTCAGAATTC
TGCACCCAGGGAGCTGAGATGTGCCGCAGGGCCTGTGGCGGACATGGCTACTCAAAGCTG
AGTGGCCTGCCATCACTGGTCACCAAATTGTCGGCCTCCTGCACCTACGAGGGTGAGAAC
ACAGTGCTCTACCTGCAGGTGGCCAGGTTCCTGGTGAAGAGCTACCTGCAGACTCAGATG
TCCCCTGGCTCCACGCCACAGAGATCTCTCTCTCCATCTGTCGCATATCTCACCGCACCT
GACCTGGCCAGGTGTCCAGCCCAGAGGGCAGCCGACTTCCTCTGCCCGGAGCTCTACACC
ACGGCCTGGGCACATGTGGCAGTAAGGCTCATAAAGGACTCAGTGCAGCATTTACAGACC
CTGACGCAATCCGGAGCTGACCAGCACGAGGCTTGGAACCAGACCACTGTCATACACCTC
CAGGCTGCTAAGGTGCACTGCTACTATGTCACTGTGAAGGGTTTTACAGAAGCTCTGGAG
AAACTAGAAAATGAACCAGCGATTCAGCAGGTGCTCAAGCGCCTCTGTGACCTCCATGCC
ATACATGGAATCTTGACTAACTCGGGTGACTTTCTCCATGACGCCTTCCTGTCTGGTGCC
CAAGTGGACATGGCAAGAACAGCCTACCTGGACCTGCTCCGCCTGATCCGGAAGGATGCC
ATCCTGTTAACTGATGCTTTTGACTTCACCGATCAGTGTTTAAATTCAGCCCTTGGCTGT
TATGATGGAAACGTCTACGAACGCCTGTTCCAGTGGGCTCAGAAGTCACCAACCAATACT
CAGGAGAACCCTGCCTATGAGGAATATATAAGACCACTTTTACAAAGTTGGAGATCCAAG
CTATGA
|
| Enzyme 47 GenBank Gene ID |
X95190 |
| Enzyme 47 GeneCard ID |
ACOX2 |
| Enzyme 47 GenAtlas ID |
ACOX2 |
| Enzyme 47 HGNC ID |
HGNC:120 |
| Enzyme 47 Chromosome Location |
3 |
| Enzyme 47 Locus |
3p14.3 |
| Enzyme 47 SNPs |
SNPJam Report |
| Enzyme 47 General References |
- Baumgart E, Vanhooren JC, Fransen M, Marynen P, Puype M, Vandekerckhove J, Leunissen JA, Fahimi HD, Mannaerts GP, van Veldhoven PP: Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome. Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13748-53. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
|
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
5397 |
| Enzyme 48 Name |
Dimethylaniline monooxygenase [N-oxide-forming] 4 |
| Enzyme 48 Synonyms |
- Dimethylaniline oxidase 4
- Hepatic flavin-containing monooxygenase 4
- FMO 4
|
| Enzyme 48 Gene Name |
FMO4 |
| Enzyme 48 Protein Sequence |
>Dimethylaniline monooxygenase [N-oxide-forming] 4
MAKKVAVIGAGVSGLSSIKCCVDEDLEPTCFERSDDIGGLWKFTESSKDGMTRVYKSLVT
NVCKEMSCYSDFPFHEDYPNFMNHEKFWDYLQEFAEHFDLLKYIQFKTTVCSITKRPDFS
ETGQWDVVTETEGKQNRAVFDAVMVCTGHFLNPHLPLEAFPGIHKFKGQILHSQEYKIPE
GFQGKRVLVIGLGNTGGDIAVELSRTAAQVLLSTRTGTWVLGRSSDWGYPYNMMVTRRCC
SFIAQVLPSRFLNWIQERKLNKRFNHEDYGLSITKGKKAKFIVNDELPNCILCGAITMKT
SVIEFTETSAVFEDGTVEENIDVVIFTTGYTFSFPFFEEPLKSLCTKKIFLYKQVFPLNL
ERATLAIIGLIGLKGSILSGTELQARWVTRVFKGLCKIPPSQKLMMEATEKEQLIKRGVF
KDTSKDKFDYIAYMDDIAACIGTKPSIPLLFLKDPRLAWEVFFGPCTPYQYRLMGPGKWD
GARNAILTQWDRTLKPLKTRIVPDSSKPASMSHYLKAWGAPVLLASLLLICKSSLFLKLV
RDKLQDRMSPYLVSLWRG
|
| Enzyme 48 Number of Residues |
558 |
| Enzyme 48 Molecular Weight |
63342.1 |
| Enzyme 48 Theoretical pI |
8.59 |
| Enzyme 48 GO Classification |
| Function |
- FAD or FADH2 binding
- NADP or NADPH binding
- adenyl nucleotide binding
- binding
- catalytic activity
- flavin-containing monooxygenase activity
- monooxygenase activity
- nucleoside binding
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- cell part
- intrinsic to endoplasmic reticulum membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 48 General Function |
Involved in flavin-containing monooxygenase activity |
| Enzyme 48 Specific Function |
This protein is involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides |
| Enzyme 48 Pathways |
Not Available |
| Enzyme 48 Reactions |
- N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
|
| Enzyme 48 Pfam Domain Function |
|
| Enzyme 48 Signals |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
4753758 |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
P31512 |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
FMO4_HUMAN |
| Enzyme 48 PDB ID |
Not Available |
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>1677 bp
ATGGCCAAGAAAGTTGCAGTGATTGGAGCTGGTGTGAGTGGCCTCTCCTCCATCAAATGC
TGTGTGGATGAGGACCTGGAGCCCACCTGCTTTGAGAGAAGTGATGACATTGGGGGATTA
TGGAAGTTTACTGAATCTTCCAAAGATGGGATGACCAGGGTCTATAAGTCATTAGTGACA
AATGTCTGTAAGGAAATGTCATGTTACAGTGACTTCCCTTTCCACGAAGATTATCCTAAT
TTCATGAACCATGAAAAATTTTGGGACTATCTCCAAGAATTTGCTGAGCACTTTGACCTC
CTGAAATACATTCAGTTTAAGACCACTGTGTGCAGCATAACGAAGCGTCCAGACTTCTCC
GAAACTGGTCAGTGGGATGTTGTCACAGAGACAGAGGGCAAGCAAAATAGAGCTGTCTTT
GATGCTGTTATGGTTTGCACTGGACATTTCCTGAATCCCCATTTACCTTTGGAAGCCTTT
CCTGGAATTCATAAGTTTAAAGGTCAGATCCTGCATAGTCAAGAGTACAAGATCCCAGAA
GGCTTTCAGGGCAAACGCGTCTTGGTGATTGGTCTTGGGAACACTGGAGGAGACATTGCT
GTGGAACTCAGTCGAACGGCAGCTCAGGTACTTCTCAGTACTAGAACTGGTACCTGGGTT
CTTGGGCGCTCTTCAGATTGGGGCTATCCTTATAATATGATGGTTACAAGAAGATGCTGT
AGTTTTATTGCACAAGTTCTGCCTTCACGTTTTCTAAACTGGATTCAAGAAAGGAAGTTG
AATAAGAGATTTAATCATGAGGATTATGGATTAAGTATTACCAAAGGGAAAAAAGCAAAA
TTCATTGTGAATGATGAGCTGCCAAACTGTATCCTCTGTGGGGCAATCACTATGAAAACC
AGCGTGATTGAATTTACAGAAACCTCTGCTGTCTTTGAAGATGGGACAGTGGAAGAAAAC
ATTGATGTTGTGATCTTCACTACAGGATATACATTTTCTTTTCCATTTTTTGAAGAACCT
CTTAAAAGCCTCTGTACAAAGAAGATATTTCTATACAAGCAAGTCTTTCCCTTAAACCTA
GAGAGAGCGACATTAGCCATCATCGGCCTTATCGGCCTTAAAGGATCCATCTTATCAGGC
ACAGAGCTCCAAGCACGATGGGTCACAAGAGTATTCAAAGGACTCTGTAAGATACCTCCA
TCCCAAAAATTGATGATGGAGGCTACTGAAAAGGAACAGCTCATTAAAAGGGGAGTGTTT
AAAGACACCAGCAAAGACAAATTTGACTACATTGCCTACATGGATGATATCGCTGCCTGC
ATAGGCACAAAGCCCAGCATCCCACTTCTGTTCCTCAAGGATCCCAGACTAGCTTGGGAA
GTTTTCTTTGGACCATGTACTCCTTATCAGTACCGCCTCATGGGCCCTGGAAAATGGGAT
GGAGCCAGAAATGCCATCCTGACCCAGTGGGACAGAACATTGAAACCTTTAAAAACTCGA
ATTGTCCCTGATTCCTCCAAGCCTGCCTCCATGTCACATTATTTAAAAGCCTGGGGGGCA
CCTGTCCTACTTGCCTCTCTTCTACTTATCTGTAAATCTTCACTTTTCTTGAAATTGGTG
AGAGATAAACTACAGGACAGAATGTCCCCTTACCTAGTAAGTCTTTGGCGAGGATGA
|
| Enzyme 48 GenBank Gene ID |
AL031274 |
| Enzyme 48 GeneCard ID |
FMO4 |
| Enzyme 48 GenAtlas ID |
FMO4 |
| Enzyme 48 HGNC ID |
HGNC:3772 |
| Enzyme 48 Chromosome Location |
1 |
| Enzyme 48 Locus |
1q24.3 |
| Enzyme 48 SNPs |
SNPJam Report |
| Enzyme 48 General References |
- Dolphin CT, Shephard EA, Povey S, Smith RL, Phillips IR: Cloning, primary sequence and chromosomal localization of human FMO2, a new member of the flavin-containing mono-oxygenase family. Biochem J. 1992 Oct 1;287 ( Pt 1):261-7. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed ]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
5399 |
| Enzyme 49 Name |
Ectonucleotide pyrophosphatase/phosphodiesterase family member 2 |
| Enzyme 49 Synonyms |
- E-NPP 2
- Autotaxin
- Extracellular lysophospholipase D
- LysoPLD
|
| Enzyme 49 Gene Name |
ENPP2 |
| Enzyme 49 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 2
MARRSSFQSCQIISLFTFAVGVNICLGFTAHRIKRAEGWEEGPPTVLSDSPWTNISGSCK
GRCFELQEAGPPDCRCDNLCKSYTSCCHDFDELCLKTARGWECTKDRCGEVRNEENACHC
SEDCLARGDCCTNYQVVCKGESHWVDDDCEEIKAAECPAGFVRPPLIIFSVDGFRASYMK
KGSKVMPNIEKLRSCGTHSPYMRPVYPTKTFPNLYTLATGLYPESHGIVGNSMYDPVFDA
TFHLRGREKFNHRWWGGQPLWITATKQGVKAGTFFWSVVIPHERRILTILQWLTLPDHER
PSVYAFYSEQPDFSGHKYGPFGPEMTNPLREIDKIVGQLMDGLKQLKLHRCVNVIFVGDH
GMEDVTCDRTEFLSNYLTNVDDITLVPGTLGRIRSKFSNNAKYDPKAIIANLTCKKPDQH
FKPYLKQHLPKRLHYANNRRIEDIHLLVERRWHVARKPLDVYKKPSGKCFFQGDHGFDNK
VNSMQTVFVGYGSTFKYKTKVPPFENIELYNVMCDLLGLKPAPNNGTHGSLNHLLRTNTF
RPTMPEEVTRPNYPGIMYLQSDFDLGCTCDDKVEPKNKLDELNKRLHTKGSTEERHLLYG
RPAVLYRTRYDILYHTDFESGYSEIFLMPLWTSYTVSKQAEVSSVPDHLTSCVRPDVRVS
PSFSQNCLAYKNDKQMSYGFLFPPYLSSSPEAKYDAFLVTNMVPMYPAFKRVWNYFQRVL
VKKYASERNGVNVISGPIFDYDYDGLHDTEDKIKQYVEGSSIPVPTHYYSIITSCLDFTQ
PADKCDGPLSVSSFILPHRPDNEESCNSSEDESKWVEELMKMHTARVRDIEHLTSLDFFR
KTSRSYPEILTLKTYLHTYESEI
|
| Enzyme 49 Number of Residues |
863 |
| Enzyme 49 Molecular Weight |
98992.8 |
| Enzyme 49 Theoretical pI |
7.39 |
| Enzyme 49 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- ion binding
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- pattern binding
- polysaccharide binding
- receptor activity
- scavenger receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- immune response
- immune system process
- metabolic process
|
| Component |
| — |
|
| Enzyme 49 General Function |
Involved in catalytic activity |
| Enzyme 49 Specific Function |
Hydrolyzes lysophospholipids to produce lysophosphatidic acid (LPA) in extracellular fluids. Major substrate is lysophosphatidylcholine. Also can act on sphingosylphosphphorylcholine producing sphingosine-1-phosphate, a modulator of cell motility. Can hydrolyze, in vitro, bis-pNPP, to some extent pNP-TMP, and barely ATP. Involved in several motility- related processes such as angiogenesis and neurite outgrowth. Acts as an angiogenic factor by stimulating migration of smooth muscle cells and microtubule formation. Stimulates migration of melanoma cells, probably via a pertussis toxin-sensitive G protein. May have a role in induction of parturition. Possible involvement in cell proliferation and adipose tissue development. Tumor cell motility-stimulating factor |
| Enzyme 49 Pathways |
Not Available |
| Enzyme 49 Reactions |
- 1-alkyl-sn-glycero-3-phosphoethanolamine + H2O = 1-alkyl-sn-glycerol 3-phosphate + ethanolamine [RN:R04362]
|
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
91823602 |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q13822 |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
ENPP2_HUMAN |
| Enzyme 49 PDB ID |
Not Available |
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>2592 bp
ATGGCAAGGAGGAGCTCGTTCCAGTCGTGTCAGATAATATCCCTGTTCACTTTTGCCGTT
GGAGTCAATATCTGCTTAGGATTCACTGCACATCGAATTAAGAGAGCAGAAGGATGGGAG
GAAGGTCCTCCTACAGTGCTATCAGACTCCCCCTGGACCAACATCTCCGGATCTTGCAAG
GGCAGGTGCTTTGAACTTCAAGAGGCTGGACCTCCTGATTGTCGCTGTGACAACTTGTGT
AAGAGCTATACCAGTTGCTGCCATGACTTTGATGAGCTGTGTTTGAAGACAGCCCGTGGC
TGGGAGTGTACTAAGGACAGATGTGGAGAAGTCAGAAATGAAGAAAATGCCTGTCACTGC
TCAGAGGACTGCTTGGCCAGGGGAGACTGCTGTACCAATTACCAAGTGGTTTGCAAAGGA
GAGTCGCATTGGGTTGATGATGACTGTGAGGAAATAAAGGCCGCAGAATGCCCTGCAGGG
TTTGTTCGCCCTCCATTAATCATCTTCTCCGTGGATGGCTTCCGTGCATCATACATGAAG
AAAGGCAGCAAAGTCATGCCTAATATTGAAAAACTAAGGTCTTGTGGCACACACTCTCCC
TACATGAGGCCGGTGTACCCAACTAAAACCTTTCCTAACTTATACACTTTGGCCACTGGG
CTATATCCAGAATCACATGGAATTGTTGGCAATTCAATGTATGATCCTGTATTTGATGCC
ACTTTTCATCTGCGAGGGCGAGAGAAATTTAATCATAGATGGTGGGGAGGTCAACCGCTA
TGGATTACAGCCACCAAGCAAGGGGTGAAAGCTGGAACATTCTTTTGGTCTGTTGTCATC
CCTCACGAGCGGAGAATATTAACCATATTGCAGTGGCTCACCCTGCCAGATCATGAGAGG
CCTTCGGTCTATGCCTTCTATTCTGAGCAACCTGATTTCTCTGGACACAAATATGGCCCT
TTCGGCCCTGAGATGACAAATCCTCTGAGGGAAATCGACAAAATTGTGGGGCAATTAATG
GATGGACTGAAACAACTAAAACTGCATCGGTGTGTCAACGTCATCTTTGTCGGAGACCAT
GGAATGGAAGATGTCACATGTGATAGAACTGAGTTCTTGAGTAATTACCTAACTAATGTG
GATGATATTACTTTAGTGCCTGGAACTCTAGGAAGAATTCGATCCAAATTTAGCAACAAT
GCTAAATATGACCCCAAAGCCATTATTGCCAATCTCACGTGTAAAAAACCAGATCAGCAC
TTTAAGCCTTACTTGAAACAGCACCTTCCCAAACGTTTGCACTATGCCAACAACAGAAGA
ATTGAGGATATCCATTTATTGGTGGAACGCAGATGGCATGTTGCAAGGAAACCTTTGGAT
GTTTATAAGAAACCATCAGGAAAATGCTTTTTCCAGGGAGACCACGGATTTGATAACAAG
GTCAACAGCATGCAGACTGTTTTTGTAGGTTATGGCTCAACATTTAAGTACAAGACTAAA
GTGCCTCCATTTGAAAACATTGAACTTTACAATGTTATGTGTGATCTCCTGGGATTGAAG
CCAGCTCCTAATAATGGGACCCATGGAAGTTTGAATCATCTCCTGCGCACTAATACCTTC
AGGCCAACCATGCCAGAGGAAGTTACCAGACCCAATTATCCAGGGATTATGTACCTTCAG
TCTGATTTTGACCTGGGCTGCACTTGTGATGATAAGGTAGAGCCAAAGAACAAGTTGGAT
GAACTCAACAAACGGCTTCATACAAAAGGGTCTACAGAAGAGAGACACCTCCTCTATGGG
CGACCTGCAGTGCTTTATCGGACTAGATATGATATCTTATATCACACTGACTTTGAAAGT
GGTTATAGTGAAATATTCCTAATGCCACTCTGGACATCATATACTGTTTCCAAACAGGCT
GAGGTTTCCAGCGTTCCTGACCATCTGACCAGTTGCGTCCGGCCTGATGTCCGTGTTTCT
CCGAGTTTCAGTCAGAACTGTTTGGCCTACAAAAATGATAAGCAGATGTCCTACGGATTC
CTCTTTCCTCCTTATCTGAGCTCTTCACCAGAGGCTAAATATGATGCATTCCTTGTAACC
AATATGGTTCCAATGTATCCTGCTTTCAAACGGGTCTGGAATTATTTCCAAAGGGTATTG
GTGAAGAAATATGCTTCGGAAAGAAATGGAGTTAACGTGATAAGTGGACCAATCTTCGAC
TATGACTATGATGGCTTACATGACACAGAAGACAAAATAAAACAGTACGTGGAAGGCAGT
TCCATTCCTGTTCCAACTCACTACTACAGCATCATCACCAGCTGTCTGGATTTCACTCAG
CCTGCCGACAAGTGTGACGGCCCTCTCTCTGTGTCCTCCTTCATCCTGCCTCACCGGCCT
GACAACGAGGAGAGCTGCAATAGCTCAGAGGACGAATCAAAATGGGTAGAAGAACTCATG
AAGATGCACACAGCTAGGGTGCGTGACATTGAACATCTCACCAGCCTGGACTTCTTCCGA
AAGACCAGCCGCAGCTACCCAGAAATCCTGACACTCAAGACATACCTGCATACATATGAG
AGCGAGATTTAA
|
| Enzyme 49 GenBank Gene ID |
NM_001040092.1 |
| Enzyme 49 GeneCard ID |
ENPP2 |
| Enzyme 49 GenAtlas ID |
ENPP2 |
| Enzyme 49 HGNC ID |
HGNC:3357 |
| Enzyme 49 Chromosome Location |
8 |
| Enzyme 49 Locus |
8q24.1 |
| Enzyme 49 SNPs |
SNPJam Report |
| Enzyme 49 General References |
- Murata J, Lee HY, Clair T, Krutzsch HC, Arestad AA, Sobel ME, Liotta LA, Stracke ML: cDNA cloning of the human tumor motility-stimulating protein, autotaxin, reveals a homology with phosphodiesterases. J Biol Chem. 1994 Dec 2;269(48):30479-84. [PubMed ]
- Kawagoe H, Soma O, Goji J, Nishimura N, Narita M, Inazawa J, Nakamura H, Sano K: Molecular cloning and chromosomal assignment of the human brain-type phosphodiesterase I/nucleotide pyrophosphatase gene (PDNP2). Genomics. 1995 Nov 20;30(2):380-4. [PubMed ]
- Lee HY, Murata J, Clair T, Polymeropoulos MH, Torres R, Manrow RE, Liotta LA, Stracke ML: Cloning, chromosomal localization, and tissue expression of autotaxin from human teratocarcinoma cells. Biochem Biophys Res Commun. 1996 Jan 26;218(3):714-9. [PubMed ]
- van Meeteren LA, Ruurs P, Christodoulou E, Goding JW, Takakusa H, Kikuchi K, Perrakis A, Nagano T, Moolenaar WH: Inhibition of autotaxin by lysophosphatidic acid and sphingosine 1-phosphate. J Biol Chem. 2005 Jun 3;280(22):21155-61. Epub 2005 Mar 15. [PubMed ]
- Giganti A, Rodriguez M, Fould B, Moulharat N, Coge F, Chomarat P, Galizzi JP, Valet P, Saulnier-Blache JS, Boutin JA, Ferry G: Murine and human autotaxin alpha, beta, and gamma isoforms: gene organization, tissue distribution, and biochemical characterization. J Biol Chem. 2008 Mar 21;283(12):7776-89. Epub 2008 Jan 6. [PubMed ]
- Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Tokumura A, Majima E, Kariya Y, Tominaga K, Kogure K, Yasuda K, Fukuzawa K: Identification of human plasma lysophospholipase D, a lysophosphatidic acid-producing enzyme, as autotaxin, a multifunctional phosphodiesterase. J Biol Chem. 2002 Oct 18;277(42):39436-42. Epub 2002 Aug 9. [PubMed ]
- Stracke ML, Krutzsch HC, Unsworth EJ, Arestad A, Cioce V, Schiffmann E, Liotta LA: Identification, purification, and partial sequence analysis of autotaxin, a novel motility-stimulating protein. J Biol Chem. 1992 Feb 5;267(4):2524-9. [PubMed ]
- Nam SW, Clair T, Kim YS, McMarlin A, Schiffmann E, Liotta LA, Stracke ML: Autotaxin (NPP-2), a metastasis-enhancing motogen, is an angiogenic factor. Cancer Res. 2001 Sep 15;61(18):6938-44. [PubMed ]
- Boucher J, Quilliot D, Praderes JP, Simon MF, Gres S, Guigne C, Prevot D, Ferry G, Boutin JA, Carpene C, Valet P, Saulnier-Blache JS: Potential involvement of adipocyte insulin resistance in obesity-associated up-regulation of adipocyte lysophospholipase D/autotaxin expression. Diabetologia. 2005 Mar;48(3):569-77. Epub 2005 Feb 8. [PubMed ]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
5401 |
| Enzyme 50 Name |
Amine oxidase [flavin-containing] A |
| Enzyme 50 Synonyms |
- Monoamine oxidase type A
- MAO-A
|
| Enzyme 50 Gene Name |
MAOA |
| Enzyme 50 Protein Sequence |
>Amine oxidase [flavin-containing] A
MENQEKASIAGHMFDVVVIGGGISGLSAAKLLTEYGVSVLVLEARDRVGGRTYTIRNEHV
DYVDVGGAYVGPTQNRILRLSKELGIETYKVNVSERLVQYVKGKTYPFRGAFPPVWNPIA
YLDYNNLWRTIDNMGKEIPTDAPWEAQHADKWDKMTMKELIDKICWTKTARRFAYLFVNI
NVTSEPHEVSALWFLWYVKQCGGTTRIFSVTNGGQERKFVGGSGQVSERIMDLLGDQVKL
NHPVTHVDQSSDNIIIETLNHEHYECKYVINAIPPTLTAKIHFRPELPAERNQLIQRLPM
GAVIKCMMYYKEAFWKKKDYCGCMIIEDEDAPISITLDDTKPDGSLPAIMGFILARKADR
LAKLHKEIRKKKICELYAKVLGSQEALHPVHYEEKNWCEEQYSGGCYTAYFPPGIMTQYG
RVIRQPVGRIFFAGTETATKWSGYMEGAVEAGERAAREVLNGLGKVTEKDIWVQEPESKD
VPAVEITHTFWERNLPSVSGLLKIIGFSTSVTALGFVLYKYKLLPRS
|
| Enzyme 50 Number of Residues |
527 |
| Enzyme 50 Molecular Weight |
59681.3 |
| Enzyme 50 Theoretical pI |
7.96 |
| Enzyme 50 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 50 General Function |
Involved in oxidoreductase activity |
| Enzyme 50 Specific Function |
Catalyzes the oxidative deamination of biogenic and xenobiotic amines and has important functions in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. MAOA preferentially oxidizes biogenic amines such as 5-hydroxytryptamine (5-HT), norepinephrine and epinephrine |
| Enzyme 50 Pathways |
|
| Enzyme 50 Reactions |
- RCH2NHR' + H2O + O2 = RCHO + R'NH2 + H2O2 [RN:R01853]
|
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
187355 |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
P21397 |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
AOFA_HUMAN |
| Enzyme 50 PDB ID |
1O5W |
| Enzyme 50 PDB File |
Show |
| Enzyme 50 3D Structure |
|
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>1584 bp
ATGGAGAATCAAGAGAAGGCGAGTATCGCGGGCCACATGTTCGACGTAGTCGTGATCGGA
GGTGGCATTTCAGGACTATCTGCTGCCAAACTCTTGACTGAATATGGCGTTAGTGTTTTG
GTTTTAGAAGCTCGGGACAGGGTTGGAGGAAGAACATATACTATAAGGAATGAGCATGTT
GATTACGTAGATGTTGGTGGAGCTTATGTGGGACCAACCCAAAACAGAATCTTACGCTTG
TCTAAGGAGCTGGGCATAGAGACTTACAAAGTGAATGTCAGTGAGCGTCTCGTTCAATAT
GTCAAGGGGAAAACATATCCATTTCGGGGCGCCTTTCCACCAGTATGGAATCCCATTGCA
TATTTGGATTACAATAATCTGTGGAGGACAATAGATAACATGGGGAAGGAGATTCCAACT
GATGCACCCTGGGAGGCTCAACATGCTGACAAATGGGACAAAATGACCATGAAAGAGCTC
ATTGACAAAATCTGCTGGACAAAGACTGCTAGGCGGTTTGCTTATCTTTTTGTGAATATC
AATGTGACCTCTGAGCCTCACGAAGTGTCTGCCCTGTGGTTCTTGTGGTATGTGAAGCAG
TGCGGGGGCACCACTCGGATATTCTCTGTCACCAATGGTGGCCAGGAACGGAAGTTTGTA
GGTGGATCTGGTCAAGTGAGCGAACGGATAATGGACCTCCTCGGAGACCAAGTGAAGCTG
AACCATCCTGTCACTCACGTTGACCAGTCAAGTGACAACATCATCATAGAGACGCTGAAC
CATGAACATTATGAGTGCAAATACGTAATTAATGCGATCCCTCCGACCTTGACTGCCAAG
ATTCACTTCAGACCAGAGCTTCCAGCAGAGAGAAACCAGTTAATTCAGCGTCTTCCAATG
GGAGCTGTCATTAAGTGCATGATGTATTACAAGGAGGCCTTCTGGAAGAAGAAGGATTAC
TGTGGCTGCATGATCATTGAAGATGAAGATGCTCCAATTTCAATAACCTTGGATGACACC
AAGCCAGATGGGTCACTGCCTGCCATCATGGGCTTCATTCTTGCCCGGAAAGCTGATCGA
CTTGCTAAGCTACATAAGGAAATAAGGAAGAAGAAAATCTGTGAGCTCTATGCCAAAGTG
CTGGGATCCCAAGAAGCTTTACATCCAGTGCATTATGAAGAGAAGAACTGGTGTGAGGAG
CAGTACTCTGGGGGCTGCTACACGGCCTACTTCCCTCCTGGGATCATGACTCAATATGGA
AGGGTGATTCGTCAACCCGTGGGCAGGATTTTCTTTGCGGGCACAGAGACTGCCACAAAG
TGGAGCGGCTACATGGAAGGGGCAGTTGAGGCTGGAGAACGAGCAGCTAGGGAGGTCTTA
AATGGTCTCGGGAAGGTGACCGAGAAAGACATCTGGGTACAAGAACCTGAATCAAAGGAC
GTTCCAGCGGTAGAAATCACCCACACCTTCTGGGAAAGGAACCTGCCCTCTGTTTCTGGC
CTGCTGAAGATCATTGGATTTTCCACATCAGTAACTGCCCTGGGGTTTGTGCTGTACAAA
TACAAGCTCCTGCCACGGTCTTGA
|
| Enzyme 50 GenBank Gene ID |
M69226 |
| Enzyme 50 GeneCard ID |
MAOA |
| Enzyme 50 GenAtlas ID |
MAOA |
| Enzyme 50 HGNC ID |
HGNC:6833 |
| Enzyme 50 Chromosome Location |
Not Available |
| Enzyme 50 Locus |
Not Available |
| Enzyme 50 SNPs |
SNPJam Report |
| Enzyme 50 General References |
- Hsu YP, Weyler W, Chen S, Sims KB, Rinehart WB, Utterback MC, Powell JF, Breakefield XO: Structural features of human monoamine oxidase A elucidated from cDNA and peptide sequences. J Neurochem. 1988 Oct;51(4):1321-4. [PubMed ]
- Bach AW, Lan NC, Johnson DL, Abell CW, Bembenek ME, Kwan SW, Seeburg PH, Shih JC: cDNA cloning of human liver monoamine oxidase A and B: molecular basis of differences in enzymatic properties. Proc Natl Acad Sci U S A. 1988 Jul;85(13):4934-8. [PubMed ]
- Chen ZY, Hotamisligil GS, Huang JK, Wen L, Ezzeddine D, Aydin-Muderrisoglu N, Powell JF, Huang RH, Breakefield XO, Craig I, et al.: Structure of the human gene for monoamine oxidase type A. Nucleic Acids Res. 1991 Aug 25;19(16):4537-41. [PubMed ]
- Grimsby J, Chen K, Wang LJ, Lan NC, Shih JC: Human monoamine oxidase A and B genes exhibit identical exon-intron organization. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3637-41. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Zhu QS, Grimsby J, Chen K, Shih JC: Promoter organization and activity of human monoamine oxidase (MAO) A and B genes. J Neurosci. 1992 Nov;12(11):4437-46. [PubMed ]
- Denney RM: The promoter of the human monoamine oxidase A gene. Prog Brain Res. 1995;106:57-66. [PubMed ]
- Denney RM, Sharma A, Dave SK, Waguespack A: A new look at the promoter of the human monoamine oxidase A gene: mapping transcription initiation sites and capacity to drive luciferase expression. J Neurochem. 1994 Sep;63(3):843-56. [PubMed ]
- Chen SA, Weyler W: Partial amino acid sequence analysis of human placenta monoamine oxidase A and bovine liver monoamine oxidase B. Biochem Biophys Res Commun. 1988 Oct 14;156(1):445-50. [PubMed ]
- Weyler W: Monoamine oxidase A from human placenta and monoamine oxidase B from bovine liver both have one FAD per subunit. Biochem J. 1989 Jun 15;260(3):725-9. [PubMed ]
- Li M, Hubalek F, Newton-Vinson P, Edmondson DE: High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif. 2002 Feb;24(1):152-62. [PubMed ]
- Wu HF, Chen K, Shih JC: Site-directed mutagenesis of monoamine oxidase A and B: role of cysteines. Mol Pharmacol. 1993 Jun;43(6):888-93. [PubMed ]
- De Colibus L, Li M, Binda C, Lustig A, Edmondson DE, Mattevi A: Three-dimensional structure of human monoamine oxidase A (MAO A): relation to the structures of rat MAO A and human MAO B. Proc Natl Acad Sci U S A. 2005 Sep 6;102(36):12684-9. Epub 2005 Aug 29. [PubMed ]
- Brunner HG, Nelen M, Breakefield XO, Ropers HH, van Oost BA: Abnormal behavior associated with a point mutation in the structural gene for monoamine oxidase A. Science. 1993 Oct 22;262(5133):578-80. [PubMed ]
- Son SY, Ma J, Kondou Y, Yoshimura M, Yamashita E, Tsukihara T: Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors. Proc Natl Acad Sci U S A. 2008 Apr 15;105(15):5739-44. Epub 2008 Apr 7. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
5403 |
| Enzyme 51 Name |
Dimethylaniline monooxygenase [N-oxide-forming] 3 |
| Enzyme 51 Synonyms |
- Dimethylaniline oxidase 3
- FMO II
- FMO form 2
- Hepatic flavin-containing monooxygenase 3
- FMO 3
|
| Enzyme 51 Gene Name |
FMO3 |
| Enzyme 51 Protein Sequence |
>Dimethylaniline monooxygenase [N-oxide-forming] 3
MGKKVAIIGAGVSGLASIRSCLEEGLEPTCFEKSNDIGGLWKFSDHAEEGRASIYKSVFS
NSSKEMMCFPDFPFPDDFPNFMHNSKIQEYIIAFAKEKNLLKYIQFKTFVSSVNKHPDFA
TTGQWDVTTERDGKKESAVFDAVMVCSGHHVYPNLPKESFPGLNHFKGKCFHSRDYKEPG
VFNGKRVLVVGLGNSGCDIATELSRTAEQVMISSRSGSWVMSRVWDNGYPWDMLLVTRFG
TFLKNNLPTAISDWLYVKQMNARFKHENYGLMPLNGVLRKEPVFNDELPASILCGIVSVK
PNVKEFTETSAIFEDGTIFEGIDCVIFATGYSFAYPFLDESIIKSRNNEIILFKGVFPPL
LEKSTIAVIGFVQSLGAAIPTVDLQSRWAAQVIKGTCTLPSMEDMMNDINEKMEKKRKWF
GKSETIQTDYIVYMDELSSFIGAKPNIPWLFLTDPKLAMEVYFGPCSPYQFRLVGPGQWP
GARNAILTQWDRSLKPMQTRVVGRLQKPCFFFHWLKLFAIPILLIAVFLVLT
|
| Enzyme 51 Number of Residues |
532 |
| Enzyme 51 Molecular Weight |
60033.0 |
| Enzyme 51 Theoretical pI |
7.87 |
| Enzyme 51 GO Classification |
| Function |
- FAD or FADH2 binding
- NADP or NADPH binding
- adenyl nucleotide binding
- binding
- catalytic activity
- flavin-containing monooxygenase activity
- monooxygenase activity
- nucleoside binding
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NADH or NADPH as one donor, and incorporation of one atom of oxygen
- purine nucleoside binding
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- cell part
- intrinsic to endoplasmic reticulum membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 51 General Function |
Involved in flavin-containing monooxygenase activity |
| Enzyme 51 Specific Function |
Involved in the oxidative metabolism of a variety of xenobiotics such as drugs and pesticides. It N-oxygenates primary aliphatic alkylamines as well as secondary and tertiary amines. Plays an important role in the metabolism of trimethylamine (TMA), via the production of TMA N-oxide (TMAO). Is also able to perform S-oxidation when acting on sulfide compounds |
| Enzyme 51 Pathways |
Not Available |
| Enzyme 51 Reactions |
- N,N-dimethylaniline + NADPH + H+ + O2 = N,N-dimethylaniline N-oxide + NADP+ + H2O [RN:R03344]
|
| Enzyme 51 Pfam Domain Function |
|
| Enzyme 51 Signals |
|
| Enzyme 51 Transmembrane Regions |
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
189053761 |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
P31513 |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
FMO3_HUMAN |
| Enzyme 51 PDB ID |
Not Available |
| Enzyme 51 Cellular Location |
Not Available |
| Enzyme 51 Gene Sequence |
>1599 bp
ATGGGGAAGAAAGTGGCCATCATTGGAGCTGGTGTGAGTGGCTTGGCCTCCATCAGGAGC
TGTCTGGAAGAGGGGCTGGAGCCCACCTGCTTTGAGAAGAGCAATGACATTGGGGGCCTG
TGGAAATTTTCAGACCATGCAGAGGAGGGCAGGGCTAGCATTTACAAATCAGTCTTTTCC
AACTCTTCCAAAGAGATGATGTGTTTCCCAGACTTCCCATTTCCCGATGACTTCCCCAAC
TTTATGCACAACAGCAAGATCCAGGAATATATCATTGCATTTGCCAAAGAAAAGAACCTC
CTGAAGTACATACAATTTAAGACATTTGTATCCAGTGTAAATAAACATCCTGATTTTGCA
ACTACTGGCCAGTGGGATGTTACCACTGAAAGGGATGGTAAAAAAGAATCGGCTGTCTTT
GATGCTGTAATGGTTTGTTCCGGACATCATGTGTATCCCAACCTACCAAAAGAGTCCTTT
CCAGGACTAAACCACTTTAAAGGCAAATGCTTCCACAGCAGGGACTATAAAGAACCAGGT
GTATTCAATGGAAAGCGTGTCCTGGTGGTTGGCCTGGGGAATTCGGGCTGTGATATTGCC
ACAGAACTCAGCCGCACAGCAGAACAGGTCATGATCAGTTCCAGAAGTGGCTCCTGGGTG
ATGAGCCGGGTCTGGGACAATGGTTATCCTTGGGACATGCTGCTCGTCACTCGATTTGGA
ACCTTCCTCAAGAACAATTTACCGACAGCCATCTCTGACTGGTTGTACGTGAAGCAGATG
AATGCAAGATTCAAGCATGAAAACTATGGCTTGATGCCTTTAAATGGAGTCCTGAGGAAA
GAGCCTGTATTTAACGATGAGCTCCCAGCAAGCATTCTGTGTGGCATTGTGTCCGTAAAG
CCTAACGTGAAGGAATTCACAGAGACCTCGGCCATTTTTGAGGATGGGACCATATTTGAG
GGCATTGACTGTGTAATCTTTGCAACAGGGTATAGTTTTGCCTACCCCTTCCTTGATGAG
TCTATCATCAAAAGCAGAAACAATGAGATCATTTTATTTAAAGGAGTATTTCCTCCTCTA
CTTGAGAAGTCAACCATAGCAGTGATTGGCTTTGTCCAGTCCCTTGGGGCTGCCATTCCC
ACAGTTGACCTCCAGTCCCGCTGGGCAGCACAAGTAATAAAGGGAACTTGTACTTTGCCT
TCTATGGAAGACATGATGAATGATATTAATGAGAAAATGGAGAAAAAGCGCAAATGGTTT
GGCAAAAGCGAGACCATACAGACAGATTACATTGTTTATATGGATGAACTCTCCTCCTTC
ATTGGGGCAAAGCCCAACATCCCATGGCTGTTTCTCACAGATCCCAAATTGGCCATGGAA
GTTTATTTTGGCCCTTGTAGTCCCTACCAGTTTAGGCTGGTGGGCCCAGGGCAGTGGCCA
GGAGCCAGAAATGCCATACTGACCCAGTGGGACCGGTCGTTGAAACCCATGCAGACACGA
GTGGTCGGGAGACTTCAGAAGCCTTGCTTCTTTTTCCATTGGCTGAAGCTCTTTGCAATT
CCTATTCTGTTAATCGCTGTTTTCCTTGTGTTGACCTAA
|
| Enzyme 51 GenBank Gene ID |
AK313197 |
| Enzyme 51 GeneCard ID |
FMO3 |
| Enzyme 51 GenAtlas ID |
FMO3 |
| Enzyme 51 HGNC ID |
HGNC:3771 |
| Enzyme 51 Chromosome Location |
1 |
| Enzyme 51 Locus |
1q24.3 |
| Enzyme 51 SNPs |
SNPJam Report |
| Enzyme 51 General References |
- Lomri N, Gu Q, Cashman JR: Molecular cloning of the flavin-containing monooxygenase (form II) cDNA from adult human liver. Proc Natl Acad Sci U S A. 1992 Mar 1;89(5):1685-9. [PubMed ]
- Dolphin CT, Cullingford TE, Shephard EA, Smith RL, Phillips IR: Differential developmental and tissue-specific regulation of expression of the genes encoding three members of the flavin-containing monooxygenase family of man, FMO1, FMO3 and FM04. Eur J Biochem. 1996 Feb 1;235(3):683-9. [PubMed ]
- Dolphin CT, Riley JH, Smith RL, Shephard EA, Phillips IR: Structural organization of the human flavin-containing monooxygenase 3 gene (FMO3), the favored candidate for fish-odor syndrome, determined directly from genomic DNA. Genomics. 1997 Dec 1;46(2):260-7. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Treacy EP, Akerman BR, Chow LM, Youil R, Bibeau C, Lin J, Bruce AG, Knight M, Danks DM, Cashman JR, Forrest SM: Mutations of the flavin-containing monooxygenase gene (FMO3) cause trimethylaminuria, a defect in detoxication. Hum Mol Genet. 1998 May;7(5):839-45. [PubMed ]
- Akerman BR, Forrest S, Chow L, Youil R, Knight M, Treacy EP: Two novel mutations of the FMO3 gene in a proband with trimethylaminuria. Hum Mutat. 1999;13(5):376-9. [PubMed ]
- Akerman BR, Lemass H, Chow LM, Lambert DM, Greenberg C, Bibeau C, Mamer OA, Treacy EP: Trimethylaminuria is caused by mutations of the FMO3 gene in a North American cohort. Mol Genet Metab. 1999 Sep;68(1):24-31. [PubMed ]
- Dolphin CT, Janmohamed A, Smith RL, Shephard EA, Phillips IR: Compound heterozygosity for missense mutations in the flavin-containing monooxygenase 3 (FM03) gene in patients with fish-odour syndrome. Pharmacogenetics. 2000 Dec;10(9):799-807. [PubMed ]
- Furnes B, Feng J, Sommer SS, Schlenk D: Identification of novel variants of the flavin-containing monooxygenase gene family in African Americans. Drug Metab Dispos. 2003 Feb;31(2):187-93. [PubMed ]
- Fujieda M, Yamazaki H, Togashi M, Saito T, Kamataki T: Two novel single nucleotide polymorphisms (SNPs) of the FMO3 gene in Japanese. Drug Metab Pharmacokinet. 2003;18(5):333-5. [PubMed ]
- Zhang J, Tran Q, Lattard V, Cashman JR: Deleterious mutations in the flavin-containing monooxygenase 3 (FMO3) gene causing trimethylaminuria. Pharmacogenetics. 2003 Aug;13(8):495-500. [PubMed ]
- Yeung CK, Adman ET, Rettie AE: Functional characterization of genetic variants of human FMO3 associated with trimethylaminuria. Arch Biochem Biophys. 2007 Aug 15;464(2):251-9. Epub 2007 May 2. [PubMed ]
- Koukouritaki SB, Poch MT, Henderson MC, Siddens LK, Krueger SK, VanDyke JE, Williams DE, Pajewski NM, Wang T, Hines RN: Identification and functional analysis of common human flavin-containing monooxygenase 3 genetic variants. J Pharmacol Exp Ther. 2007 Jan;320(1):266-73. Epub 2006 Oct 18. [PubMed ]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
5413 |
| Enzyme 52 Name |
Xanthine dehydrogenase/oxidase |
| Enzyme 52 Synonyms |
- Xanthine dehydrogenase
- XD
- Xanthine oxidase
- XO
- Xanthine oxidoreductase
|
| Enzyme 52 Gene Name |
XDH |
| Enzyme 52 Protein Sequence |
>Xanthine dehydrogenase/oxidase
MTADKLVFFVNGRKVVEKNADPETTLLAYLRRKLGLSGTKLGCGEGGCGACTVMLSKYDR
LQNKIVHFSANACLAPICSLHHVAVTTVEGIGSTKTRLHPVQERIAKSHGSQCGFCTPGI
VMSMYTLLRNQPEPTMEEIENAFQGNLCRCTGYRPILQGFRTFARDGGCCGGDGNNPNCC
MNQKKDHSVSLSPSLFKPEEFTPLDPTQEPIFPPELLRLKDTPRKQLRFEGERVTWIQAS
TLKELLDLKAQHPDAKLVVGNTEIGIEMKFKNMLFPMIVCPAWIPELNSVEHGPDGISFG
AACPLSIVEKTLVDAVAKLPAQKTEVFRGVLEQLRWFAGKQVKSVASVGGNIITASPISD
LNPVFMASGAKLTLVSRGTRRTVQMDHTFFPGYRKTLLSPEEILLSIEIPYSREGEYFSA
FKQASRREDDIAKVTSGMRVLFKPGTTEVQELALCYGGMANRTISALKTTQRQLSKLWKE
ELLQDVCAGLAEELHLPPDAPGGMVDFRCTLTLSFFFKFYLTVLQKLGQENLEDKCGKLD
PTFASATLLFQKDPPADVQLFQEVPKGQSEEDMVGRPLPHLAADMQASGEAVYCDDIPRY
ENELSLRLVTSTRAHAKIKSIDTSEAKKVPGFVCFISADDVPGSNITGICNDETVFAKDK
VTCVGHIIGAVVADTPEHTQRAAQGVKITYEELPAIITIEDAIKNNSFYGPELKIEKGDL
KKGFSEADNVVSGEIYIGGQEHFYLETHCTIAVPKGEAGEMELFVSTQNTMKTQSFVAKM
LGVPANRIVVRVKRMGGGFGGKETRSTVVSTAVALAAYKTGRPVRCMLDRDEDMLITGGR
HPFLARYKVGFMKTGTVVALEVDHFSNVGNTQDLSQSIMERALFHMDNCYKIPNIRGTGR
LCKTNLPSNTAFRGFGGPQGMLIAECWMSEVAVTCGMPAEEVRRKNLYKEGDLTHFNQKL
EGFTLPRCWEECLASSQYHARKSEVDKFNKENCWKKRGLCIIPTKFGISFTVPFLNQAGA
LLHVYTDGSVLLTHGGTEMGQGLHTKMVQVASRALKIPTSKIYISETSTNTVPNTSPTAA
SVSADLNGQAVYAACQTILKRLEPYKKKNPSGSWEDWVTAAYMDTVSLSATGFYRTPNLG
YSFETNSGNPFHYFSYGVACSEVEIDCLTGDHKNLRTDIVMDVGSSLNPAIDIGQVEGAF
VQGLGLFTLEELHYSPEGSLHTRGPSTYKIPAFGSIPIEFRVSLLRDCPNKKAIYASKAV
GEPPLFLAASIFFAIKDAIRAARAQHTGNNVKELFRLDSPATPEKIRNACVDKFTTLCVT
GVPENCKPWSVRV
|
| Enzyme 52 Number of Residues |
1333 |
| Enzyme 52 Molecular Weight |
146423.0 |
| Enzyme 52 Theoretical pI |
7.70 |
| Enzyme 52 GO Classification |
| Function |
- FAD or FADH2 binding
- adenyl nucleotide binding
- binding
- catalytic activity
- cation binding
- electron carrier activity
- ion binding
- iron ion binding
- iron-sulfur cluster binding
- metal cluster binding
- metal ion binding
- molybdenum ion binding
- nucleoside binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH or CH2 groups
- oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor
- oxidoreductase activity, acting on CH or CH2 groups, oxygen as acceptor
- purine nucleoside binding
- transition metal ion binding
- xanthine dehydrogenase activity
- xanthine oxidase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 52 General Function |
Involved in oxidoreductase activity |
| Enzyme 52 Specific Function |
Key enzyme in purine degradation. Catalyzes the oxidation of hypoxanthine to xanthine. Catalyzes the oxidation of xanthine to uric acid. Contributes to the generation of reactive oxygen species. Has also low oxidase activity towards aldehydes (in vitro) |
| Enzyme 52 Pathways |
|
| Enzyme 52 Reactions |
- xanthine + H2O + O2 = urate + H2O2 [RN:R02107]
|
| Enzyme 52 Pfam Domain Function |
|
| Enzyme 52 Signals |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
Not Available |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
P47989 |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
XDH_HUMAN |
| Enzyme 52 PDB ID |
1V97 |
| Enzyme 52 PDB File |
Show |
| Enzyme 52 3D Structure |
|
| Enzyme 52 Cellular Location |
Not Available |
| Enzyme 52 Gene Sequence |
>4002 bp
ATGACAGCAGACAAATTGGTTTTCTTTGTGAATGGCAGAAAGGTGGTGGAGAAAAATGCA
GATCCAGAGACAACCCTTTTGGCCTACCTGAGAAGAAAGTTGGGGCTGAGTGGAACCAAG
CTCGGCTGTGGAGAGGGGGGCTGCGGGGCTTGCACAGTGATGCTCTCCAAGTATGATCGT
CTGCAGAACAAGATCGTCCACTTTTCTGCCAATGCCTGCCTGGCCCCCATCTGCTCCTTG
CACCATGTTGCAGTGACAACTGTGGAAGGAATAGGAAGCACCAAGACGAGGCTGCATCCT
GTGCAGGAGAGAATTGCCAAAAGCCACGGCTCCCAGTGCGGGTTCTGCACCCCTGGCATC
GTCATGAGTATGTACACACTGCTCCGGAATCAGCCCGAGCCCACCATGGAGGAGATTGAG
AATGCCTTCCAAGGAAATCTGTGCCGCTGCACAGGCTACAGACCCATCCTCCAGGGCTTC
CGGACCTTTGCCAGGGATGGTGGATGCTGTGGAGGAGATGGGAATAATCCAAATTGCTGC
ATGAACCAGAAGAAAGACCACTCAGTCAGCCTCTCGCCATCTTTATTCAAACCAGAGGAG
TTCACGCCCCTGGATCCAACCCAGGAGCCCATTTTTCCCCCAGAGTTGCTGAGGCTGAAA
GACACTCCTCGGAAGCAGCTGCGATTTGAAGGGGAGCGTGTGACGTGGATACAGGCCTCA
ACCCTCAAGGAGCTGCTGGACCTCAAGGCTCAGCACCCTGACGCCAAGCTGGTCGTGGGG
AACACGGAGATTGGCATTGAGATGAAGTTCAAGAATATGCTGTTTCCTATGATTGTCTGC
CCAGCCTGGATCCCTGAGCTGAATTCGGTAGAACATGGACCCGACGGTATCTCCTTTGGA
GCTGCTTGCCCCCTGAGCATTGTGGAAAAAACCCTGGTGGATGCTGTTGCTAAGCTTCCT
GCCCAAAAGACAGAGGTGTTCAGAGGGGTCCTGGAGCAGCTGCGCTGGTTTGCTGGGAAG
CAAGTCAAGTCTGTGGCGTCCGTTGGAGGGAACATCATCACTGCCAGCCCCATCTCCGAC
CTCAACCCCGTGTTCATGGCCAGTGGGGCCAAGCTGACACTTGTGTCCAGAGGCACCAGG
AGAACTGTCCAGATGGACCACACCTTCTTCCCTGGCTACAGAAAGACCCTGCTGAGCCCG
GAGGAGATACTGCTCTCCATAGAGATCCCCTACAGCAGGGAGGGGGAGTATTTCTCAGCA
TTCAAGCAGGCCTCCCGGAGAGAAGATGACATTGCCAAGGTAACCAGTGGCATGAGAGTT
TTATTCAAGCCAGGAACCACAGAGGTACAGGAGCTGGCCCTTTGCTATGGTGGAATGGCC
AACAGAACCATCTCAGCCCTCAAGACCACTCAGAGGCAGCTTTCCAAGCTCTGGAAGGAG
GAGCTGCTGCAGGACGTGTGTGCAGGACTGGCAGAGGAGCTGCATCTGCCTCCCGATGCC
CCTGGTGGCATGGTGGACTTCCGGTGCACCCTCACCCTCAGCTTCTTCTTCAAGTTCTAC
CTGACAGTCCTTCAGAAGCTGGGCCAAGAGAACCTGGAAGACAAGTGTGGTAAACTGGAC
CCCACTTTCGCCAGTGCAACTTTACTGTTTCAGAAAGACCCCCCAGCCGATGTCCAGCTC
TTCCAAGAGGTGCCCAAGGGTCAGTCTGAGGAGGACATGGTGGGCCGGCCCCTGCCCCAC
CTGGCAGCGGACATGCAGGCCTCTGGTGAGGCCGTGTACTGTGACGACATTCCTCGCTAC
GAGAATGAGCTGTCTCTCCGGCTGGTCACCAGCACCCGGGCCCACGCCAAGATCAAGTCC
ATAGATACATCAGAAGCTAAGAAGGTTCCAGGGTTTGTTTGTTTCATTTCCGCTGATGAT
GTTCCTGGGAGTAACATAACTGGAATTTGTAATGATGAGACAGTCTTTGCGAAGGATAAG
GTTACTTGTGTTGGGCATATCATTGGTGCTGTGGTTGCTGACACCCCGGAACACACACAG
AGAGCTGCCCAAGGGGTGAAAATCACCTATGAAGAACTACCAGCCATTATCACAATTGAG
GATGCTATAAAGAACAACTCCTTTTATGGACCTGAGCTGAAGATCGAGAAAGGGGACCTA
AAGAAGGGGTTTTCCGAAGCAGATAATGTTGTGTCAGGGGAGATATACATCGGTGGCCAA
GAGCACTTCTACCTGGAGACTCACTGCACCATTGCTGTTCCAAAAGGCGAGGCAGGGGAG
ATGGAGCTCTTTGTGTCTACACAGAACACCATGAAGACCCAGAGCTTTGTTGCAAAAATG
TTGGGGGTTCCAGCAAACCGGATTGTGGTTCGAGTGAAGAGAATGGGAGGAGGCTTTGGA
GGCAAGGAGACCCGGAGCACTGTGGTGTCCACGGCAGTGGCCCTGGCTGCATATAAGACC
GGCCGCCCTGTGCGATGCATGCTGGACCGTGATGAGGACATGCTGATAACTGGTGGCAGA
CATCCCTTCCTGGCCAGATACAAGGTTGGCTTCATGAAGACTGGGACAGTTGTGGCTCTT
GAGGTGGACCACTTCAGCAATGTGGGGAACACCCAGGATCTCTCTCAGAGTATTATGGAA
CGAGCTTTATTCCACATGGACAACTGCTATAAAATCCCCAACATCCGGGGCACTGGGCGG
CTGTGCAAAACCAACCTTCCCTCCAACACGGCCTTCCGGGGCTTTGGGGGGCCCCAGGGG
ATGCTCATTGCCGAGTGCTGGATGAGTGAAGTTGCAGTGACCTGTGGGATGCCTGCAGAG
GAGGTGCGGAGAAAAAACCTGTACAAAGAAGGGGACCTGACACACTTCAACCAGAAGCTT
GAGGGTTTCACCTTGCCCAGATGCTGGGAAGAATGCCTAGCAAGCTCTCAGTATCATGCT
CGGAAGAGTGAGGTTGACAAGTTCAACAAGGAGAATTGTTGGAAAAAGAGAGGATTGTGC
ATAATTCCCACCAAGTTTGGAATAAGCTTCACAGTTCCTTTTCTGAATCAGGCAGGAGCC
CTACTTCATGTGTACACAGATGGCTCTGTGCTGCTGACCCACGGGGGGACTGAGATGGGC
CAAGGCCTTCATACCAAAATGGTCCAGGTGGCCAGTAGAGCTCTGAAAATCCCCACCTCT
AAGATTTATATCAGCGAGACAAGCACTAACACTGTGCCCAACACCTCTCCCACGGCTGCC
TCTGTCAGCGCTGACCTCAATGGACAGGCCGTCTATGCGGCTTGTCAGACCATCTTGAAA
AGGCTGGAACCCTACAAGAAGAAGAATCCCAGTGGCTCCTGGGAAGACTGGGTCACAGCT
GCCTACATGGACACAGTGAGCTTGTCTGCCACTGGGTTTTATAGAACACCCAATCTGGGC
TACAGCTTTGAGACTAACTCAGGGAACCCCTTCCACTACTTCAGCTATGGGGTGGCTTGC
TCTGAAGTAGAAATCGACTGCCTAACAGGAGATCATAAGAACCTCCGCACAGATATTGTC
ATGGATGTTGGCTCCAGTCTAAACCCTGCCATTGATATTGGACAGGTGGAAGGGGCATTT
GTCCAGGGCCTTGGCCTCTTCACCCTAGAGGAGCTACACTATTCCCCCGAGGGGAGCCTG
CACACCCGTGGCCCTAGCACCTACAAGATCCCGGCATTTGGCAGCATCCCCATTGAGTTC
AGGGTGTCCCTGCTCCGCGACTGCCCCAACAAGAAGGCCATCTATGCATCGAAGGCTGTT
GGAGAGCCGCCCCTCTTCCTGGCTGCTTCTATCTTCTTTGCCATCAAAGATGCCATCCGT
GCAGCTCGAGCTCAGCACACAGGTAATAACGTGAAGGAACTCTTCCGGCTAGACAGCCCT
GCCACCCCGGAGAAGATCCGCAATGCCTGCGTGGACAAGTTCACCACCCTGTGTGTCACT
GGTGTCCCAGAAAACTGCAAACCCTGGTCTGTGAGGGTCTAA
|
| Enzyme 52 GenBank Gene ID |
D11456 |
| Enzyme 52 GeneCard ID |
XDH |
| Enzyme 52 GenAtlas ID |
XDH |
| Enzyme 52 HGNC ID |
HGNC:12805 |
| Enzyme 52 Chromosome Location |
2 |
| Enzyme 52 Locus |
2p23.1 |
| Enzyme 52 SNPs |
SNPJam Report |
| Enzyme 52 General References |
- Ichida K, Amaya Y, Noda K, Minoshima S, Hosoya T, Sakai O, Shimizu N, Nishino T: Cloning of the cDNA encoding human xanthine dehydrogenase (oxidase): structural analysis of the protein and chromosomal location of the gene. Gene. 1993 Nov 15;133(2):279-84. [PubMed ]
- Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1994 Mar 15;199(2):998-1004. [PubMed ]
- Xu P, Huecksteadt TP, Harrison R, Hoidal JR: Molecular cloning, tissue expression of human xanthine dehydrogenase. Biochem Biophys Res Commun. 1995 Oct 4;215(1):429. [PubMed ]
- Saksela M, Raivio KO: Cloning and expression in vitro of human xanthine dehydrogenase/oxidase. Biochem J. 1996 Apr 1;315 ( Pt 1):235-9. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Ichida K, Amaya Y, Kamatani N, Nishino T, Hosoya T, Sakai O: Identification of two mutations in human xanthine dehydrogenase gene responsible for classical type I xanthinuria. J Clin Invest. 1997 May 15;99(10):2391-7. [PubMed ]
- Levartovsky D, Lagziel A, Sperling O, Liberman U, Yaron M, Hosoya T, Ichida K, Peretz H: XDH gene mutation is the underlying cause of classical xanthinuria: a second report. Kidney Int. 2000 Jun;57(6):2215-20. [PubMed ]
- Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed ]
- Yamaguchi Y, Matsumura T, Ichida K, Okamoto K, Nishino T: Human xanthine oxidase changes its substrate specificity to aldehyde oxidase type upon mutation of amino acid residues in the active site: roles of active site residues in binding and activation of purine substrate. J Biochem. 2007 Apr;141(4):513-24. Epub 2007 Feb 14. [PubMed ]
- Sakamoto N, Yamamoto T, Moriwaki Y, Teranishi T, Toyoda M, Onishi Y, Kuroda S, Sakaguchi K, Fujisawa T, Maeda M, Hada T: Identification of a new point mutation in the human xanthine dehydrogenase gene responsible for a case of classical type I xanthinuria. Hum Genet. 2001 Apr;108(4):279-83. [PubMed ]
- Gok F, Ichida K, Topaloglu R: Mutational analysis of the xanthine dehydrogenase gene in a Turkish family with autosomal recessive classical xanthinuria. Nephrol Dial Transplant. 2003 Nov;18(11):2278-83. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
5426 |
| Enzyme 53 Name |
Ectonucleotide pyrophosphatase/phosphodiesterase family member 3 |
| Enzyme 53 Synonyms |
- E-NPP 3
- Phosphodiesterase I beta
- PD-Ibeta
- Phosphodiesterase I/nucleotide pyrophosphatase 3
- CD203c antigen
- Alkaline phosphodiesterase I
- Nucleotide pyrophosphatase
- NPPase
|
| Enzyme 53 Gene Name |
ENPP3 |
| Enzyme 53 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
MESTLTLATEQPVKKNTLKKYKIACIVLLALLVIMSLGLGLGLGLRKLEKQGSCRKKCFD
ASFRGLENCRCDVACKDRGDCCWDFEDTCVESTRIWMCNKFRCGETRLEASLCSCSDDCL
QRKDCCADYKSVCQGETSWLEENCDTAQQSQCPEGFDLPPVILFSMDGFRAEYLYTWDTL
MPNINKLKTCGIHSKYMRAMYPTKTFPNHYTIVTGLYPESHGIIDNNMYDVNLNKNFSLS
SKEQNNPAWWHGQPMWLTAMYQGLKAATYFWPGSEVAINGSFPSIYMPYNGSVPFEERIS
TLLKWLDLPKAERPRFYTMYFEEPDSSGHAGGPVSARVIKALQVVDHAFGMLMEGLKQRN
LHNCVNIILLADHGMDQTYCNKMEYMTDYFPRINFFYMYEGPAPRIRAHNIPHDFFSFNS
EEIVRNLSCRKPDQHFKPYLTPDLPKRLHYAKNVRIDKVHLFVDQQWLAVRSKSNTNCGG
GNHGYNNEFRSMEAIFLAHGPSFKEKTEVEPFENIEVYNLMCDLLRIQPAPNNGTHGSLN
HLLKVPFYEPSHAEEVSKFSVCGFANPLPTESLDCFCPHLQNSTQLEQVNQMLNLTQEEI
TATVKVNLPFGRPRVLQKNVDHCLLYHREYVSGFGKAMRMPMWSSYTVPQLGDTSPLPPT
VPDCLRADVRVPPSESQKCSFYLADKNITHGFLYPPASNRTSDSQYDALITSNLVPMYEE
FRKMWDYFHSVLLIKHATERNGVNVVSGPIFDYNYDGHFDAPDEITKHLANTDVPIPTHY
FVVLTSCKNKSHTPENCPGWLDVLPFIIPHRPTNVESCPEGKPEALWVEERFTAHIARVR
DVELLTGLDFYQDKVQPVSEILQLKTYLPTFETTI
|
| Enzyme 53 Number of Residues |
875 |
| Enzyme 53 Molecular Weight |
100123.5 |
| Enzyme 53 Theoretical pI |
6.55 |
| Enzyme 53 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- ion binding
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- pattern binding
- polysaccharide binding
- receptor activity
- scavenger receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- immune response
- immune system process
- metabolic process
|
| Component |
| — |
|
| Enzyme 53 General Function |
Involved in catalytic activity |
| Enzyme 53 Specific Function |
Cleaves a variety of phosphodiester and phosphosulfate bonds including deoxynucleotides, nucleotide sugars, and NAD |
| Enzyme 53 Pathways |
- Nicotinate and Nicotinamide Metabolism (map00760 )
- Pantothenate and CoA Biosynthesis (map00770 )
- Purine Metabolism (map00230 )
- Riboflavin Metabolism (map00740 )
- Starch and Sucrose Metabolism (map00500 )
|
| Enzyme 53 Reactions |
- a dinucleotide + H2O = 2 mononucleotides [RN:R00056]
|
| Enzyme 53 Pfam Domain Function |
|
| Enzyme 53 Signals |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
2465540 |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
O14638 |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
ENPP3_HUMAN |
| Enzyme 53 PDB ID |
Not Available |
| Enzyme 53 Cellular Location |
Not Available |
| Enzyme 53 Gene Sequence |
>2628 bp
ATGGAATCTACGTTGACTTTAGCAACGGAACAACCTGTTAAGAAGAACACTCTTAAGAAA
TATAAAATAGCTTGCATTGTTCTTCTTGCTTTGCTGGTGATCATGTCACTTGGATTAGGC
CTGGGGCTTGGACTCAGGAAACTGGAAAAGCAAGGCAGCTGCAGGAAGAAGTGCTTTGAT
GCATCATTTAGAGGACTGGAGAACTGCCGGTGTGATGTGGCATGTAAAGACCGAGGTGAT
TGCTGCTGGGATTTTGAAGACACCTGTGTGGAATCAACTCGAATATGGATGTGCAATAAA
TTTCGTTGTGGAGAGACCAGATTAGAGGCCAGCCTTTGCTCTTGTTCAGATGACTGTTTG
CAGAAGAAAGATTGCTGTGCTGACTATAAGAGTGTTTGCCAAGGAGAAACCTCATGGCTG
GAAGAAAACTGTGACACAGCCCAGCAGTCTCAGTGCCCAGAAGGGTTTGACCTGCCACCA
GTTATCTTGTTTTCTATGGATGGATTTAGAGCTGAATATTTATACACATGGGATACTTTA
ATGCCAAATATCAATAAACTGAAAACATGTGGAATTCATTCAAAATACATGAGAGCTATG
TATCCTACCAAAACCTTCCCAAATCATTACACCATTGTCACGGGCTTGTATCCAGAGTCA
CATGGCATCATTGACAATAATATGTATGATGTAAATCTCAACAAGAATTTTTCACTTTCT
TCAAAGGAACAAAATAATCCAGCCTGGTGGCATGGGCAACCAATGTGGCTGACAGCAATG
TATCAAGGTTTAAAAGCCGCTACCTACTTTTGGCCCGGATCAGAAGTGGCTATAAATGGC
TCCTTTCCTTCCATATACATGCCTTACAACGGAAGTGTCCCATTTGAAGAGAGGATTTCT
ACACTGTTAAAATGGCTGGACCTGCCCAAAGCTGAAAGACCCAGGTTTTATACCATGTAT
TTTGAAGAACCTGATTCCTCTGGACATGCAGGTGGACCAGTCAGTGCCAGAGTAATTAAA
GCCTTACAGGTAGTAGATCATGCTTTTGGGATGTTGATGGAAGGCCTGAAGCAGCGGAAT
TTGCACAACTGTGTCAATATCATCCTTCTGGCTGACCATGGAATGGACCAGACTTATTGT
AACAAGATGGAATACATGACTGATTATTTTCCCAGAATAAACTTCTTCTACATGTACGAA
GGGCCTGCCCCCCGCATCCGAGCTCATAATATACCTCATGACTTTTTTAGTTTTAATTCT
GAGGAAATTGTTAGAAACCTCAGTTGCCGAAAACCTGATCAGCATTTCAAGCCCTATTTG
ACTCCTGATTTGCCAAAGCGACTGCACTATGCCAAGAACGTCAGAATCGACAAAGTTCAT
CTCTTTGTGGATCAACAGTGGCTGGCTGTTAGGAGTAAATCAAATACAAATTGTGGAGGA
GGCAACCATGGTTATAACAATGAGTTTAGGAGCATGGAGGCTATCTTTCTGGCACATGGA
CCCAGTTTTAAAGAGAAGACTGAAGTTGAACCATTTGAAAATATTGAAGTCTATAACCTA
ATGTGTGATCTTCTACGCATTCAACCAGCACCAAACAATGGAACCCATGGTAGTTTAAAC
CATCTTCTGAAGGTGCCTTTTTATGAGCCATCCCATGCAGAGGAGGTGTCAAAGTTTTCT
GTTTGTGGCTTTGCTAATCCATTGCCCACAGAGTCTCTTGACTGTTTCTGCCCTCACCTA
CAAAATAGTACTCAGCTGGAACAAGTGAATCAGATGCTAAATCTCACCCAAGAAGAAATA
ACAGCAACAGTGAAAGTAAATTTGCCATTTGGGAGGCCTAGGGTACTGCAGAAGAACGTG
GACCACTGTCTCCTTTACCACAGGGAATATGTCAGTGGATTTGGAAAAGCTATGAGGATG
CCCATGTGGAGTTCATACACAGTCCCCCAGTTGGGAGACACATCGCCTCTGCCTCCCACT
GTCCCAGACTGTCTGCGGGCTGATGTCAGGGTTCCTCCTTCTGAGAGCCAAAAATGTTCC
TTCTATTTAGCAGACAAGAATATCACCCACGGCTTCCTCTATCCTCCTGCCAGCAATAGA
ACATCAGATAGCCAATATGATGCTTTAATTACTAGCAATTTGGTACCTATGTATGAAGAA
TTCAGAAAAATGTGGGACTACTTCCACAGTGTTCTTCTTATAAAACATGCCACAGAAAGA
AATGGAGTAAATGTGGTTAGTGGACCAATATTTGATTATAATTATGATGGCCATTTTGAT
GCTCCAGATGAAATTACCAAACATTTAGCCAACACTGATGTTCCCATCCCAACACACTAC
TTTGTGGTGCTGACCAGTTGTAAAAACAAGAGCCACACACCGGAAAACTGCCCTGGGTGG
CTGGATGTCCTACCCTTTATCATCCCTCACCGACCTACCAACGTGGAGAGCTGTCCTGAA
GGTAAACCAGAAGCTCTTTGGGTTGAAGAAAGATTTACAGCTCACATTGCCCGGGTCCGT
GATGTAGAACTTCTCACTGGGCTTGACTTCTATCAGGATAAAGTGCAGCCTGTCTCTGAA
ATTTTGCAACTAAAGACATATTTACCAACATTTGAAACCACTATTTAA
|
| Enzyme 53 GenBank Gene ID |
AF005632 |
| Enzyme 53 GeneCard ID |
ENPP3 |
| Enzyme 53 GenAtlas ID |
ENPP3 |
| Enzyme 53 HGNC ID |
HGNC:3358 |
| Enzyme 53 Chromosome Location |
6 |
| Enzyme 53 Locus |
6q22 |
| Enzyme 53 SNPs |
SNPJam Report |
| Enzyme 53 General References |
- Jin-Hua P, Goding JW, Nakamura H, Sano K: Molecular cloning and chromosomal localization of PD-Ibeta (PDNP3), a new member of the human phosphodiesterase I genes. Genomics. 1997 Oct 15;45(2):412-5. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
- Buhring HJ, Seiffert M, Giesert C, Marxer A, Kanz L, Valent P, Sano K: The basophil activation marker defined by antibody 97A6 is identical to the ectonucleotide pyrophosphatase/phosphodiesterase 3. Blood. 2001 May 15;97(10):3303-5. [PubMed ]
- Yano Y, Hayashi Y, Sano K, Nagano H, Nakaji M, Seo Y, Ninomiya T, Yoon S, Yokozaki H, Kasuga M: Expression and localization of ecto-nucleotide pyrophosphatase/phosphodiesterase I-1 (E-NPP1/PC-1) and -3 (E-NPP3/CD203c/PD-Ibeta/B10/gp130(RB13-6)) in inflammatory and neoplastic bile duct diseases. Cancer Lett. 2004 Apr 30;207(2):139-47. [PubMed ]
- Buhring HJ, Streble A, Valent P: The basophil-specific ectoenzyme E-NPP3 (CD203c) as a marker for cell activation and allergy diagnosis. Int Arch Allergy Immunol. 2004 Apr;133(4):317-29. Epub 2004 Mar 17. [PubMed ]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
5430 |
| Enzyme 54 Name |
Heme oxygenase 1 |
| Enzyme 54 Synonyms |
- HO-1
|
| Enzyme 54 Gene Name |
HMOX1 |
| Enzyme 54 Protein Sequence |
>Heme oxygenase 1
MERPQPDSMPQDLSEALKEATKEVHTQAENAEFMRNFQKGQVTRDGFKLVMASLYHIYVA
LEEEIERNKESPVFAPVYFPEELHRKAALEQDLAFWYGPRWQEVIPYTPAMQRYVKRLHE
VGRTEPELLVAHAYTRYLGDLSGGQVLKKIAQKALDLPSSGEGLAFFTFPNIASATKFKQ
LYRSRMNSLEMTPAVRQRVIEEAKTAFLLNIQLFEELQELLTHDTKDQSPSRAPGLRQRA
SNKVQDSAPVETPRGKPPLNTRSQAPLLRWVLTLSFLVATVAVGLYAM
|
| Enzyme 54 Number of Residues |
288 |
| Enzyme 54 Molecular Weight |
32818.3 |
| Enzyme 54 Theoretical pI |
8.68 |
| Enzyme 54 GO Classification |
| Function |
- catalytic activity
- heme oxygenase (decyclizing) activity
- heme oxygenase (decyclizing) activity
- heme oxygenase (decyclizing) activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
|
| Process |
- heme metabolic process
- heme oxidation
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 54 General Function |
Involved in heme oxygenase (decyclizing) activity |
| Enzyme 54 Specific Function |
Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed |
| Enzyme 54 Pathways |
|
| Enzyme 54 Reactions |
- heme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O [RN:R00311]
|
| Enzyme 54 Pfam Domain Function |
|
| Enzyme 54 Signals |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
35173 |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
P09601 |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
HMOX1_HUMAN |
| Enzyme 54 PDB ID |
1T5P |
| Enzyme 54 PDB File |
Show |
| Enzyme 54 3D Structure |
|
| Enzyme 54 Cellular Location |
Not Available |
| Enzyme 54 Gene Sequence |
>867 bp
ATGGAGCGTCCGCAACCCGACAGCATGCCCCAGGATTTGTCAGAGGCCCTGAAGGAGGCC
ACCAAGGAGGTGCACACCCAGGCAGAGAATGCTGAGTTCATGAGGAACTTTCAGAAGGGC
CAGGTGACCCGAGACGGCTTCAAGCTGGTGATGGCCTCCCTGTACCACATCTATGTGGCC
CTGGAGGAGGAGATTGAGCGCAACAAGGAGAGCCCAGTCTTCGCCCCTGTCTACTTCCCA
GAAGAGCTGCACCGCAAGGCTGCCCTGGAGCAGGACCTGGCCTTCTGGTACGGGCCCCGC
TGGCAGGAGGTCATCCCCTACACACCAGCCATGCAGCGCTATGTGAAGCGGCTCCACGAG
GTGGGGCGCACAGAGCCCGAGCTGCTGGTGGCCCACGCCTACACCCGCTACCTGGGTGAC
CTGTCTGGGGGCCAGGTGCTCAAAAAGATTGCCCAGAAAGCCCTGGACCTGCCCAGCTCT
GGCGAGGGCCTGGCCTTCTTCACCTTCCCCAACATTGCCAGTGCCACCAAGTTCAAGCAG
CTCTACCGCTCCCGCATGAACTCCCTGGAGATGACTCCCGCAGTCAGGCAGAGGGTGATA
GAAGAGGCCAAGACTGCGTTCCTGCTCAACATCCAGCTCTTTGAGGAGTTGCAGGAGCTG
CTGACCCATGACACCAAGGACCAGAGCCCCTCACGGGCACCAGGGCTTCGCCAGCGGGCC
AGCAACAAAGTGCAAGATTCTGCCCCCGTGGAGACTCCCAGAGGGAAGCCCCCACTCAAC
ACCCGCTCCCAGGCTCCGCTTCTCCGATGGGTCCTTACACTCAGCTTTCTGGTGGCGACA
GTTGCTGTAGGGCTTTATGCCATGTGA
|
| Enzyme 54 GenBank Gene ID |
X06985 |
| Enzyme 54 GeneCard ID |
HMOX1 |
| Enzyme 54 GenAtlas ID |
HMOX1 |
| Enzyme 54 HGNC ID |
HGNC:5013 |
| Enzyme 54 Chromosome Location |
2 |
| Enzyme 54 Locus |
22q12|22q13.1 |
| Enzyme 54 SNPs |
SNPJam Report |
| Enzyme 54 General References |
- Yoshida T, Biro P, Cohen T, Muller RM, Shibahara S: Human heme oxygenase cDNA and induction of its mRNA by hemin. Eur J Biochem. 1988 Feb 1;171(3):457-61. [PubMed ]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed ]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
- Keyse SM, Tyrrell RM: Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite. Proc Natl Acad Sci U S A. 1989 Jan;86(1):99-103. [PubMed ]
- Shibahara S, Sato M, Muller RM, Yoshida T: Structural organization of the human heme oxygenase gene and the function of its promoter. Eur J Biochem. 1989 Feb 15;179(3):557-63. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Schuller DJ, Wilks A, Ortiz de Montellano PR, Poulos TL: Crystal structure of human heme oxygenase-1. Nat Struct Biol. 1999 Sep;6(9):860-7. [PubMed ]
|
| Enzyme 54 Metabolite References |
Not Available |
|
Enzyme 55
[top]
|
| Enzyme 55 ID |
5431 |
| Enzyme 55 Name |
Retinal dehydrogenase 1 |
| Enzyme 55 Synonyms |
- RALDH 1
- RalDH1
- ALDH-E1
- ALHDII
- Aldehyde dehydrogenase family 1 member A1
- Aldehyde dehydrogenase, cytosolic
|
| Enzyme 55 Gene Name |
ALDH1A1 |
| Enzyme 55 Protein Sequence |
>Retinal dehydrogenase 1
MSSSGTPDLPVLLTDLKIQYTKIFINNEWHDSVSGKKFPVFNPATEEELCQVEEGDKEDV
DKAVKAARQAFQIGSPWRTMDASERGRLLYKLADLIERDRLLLATMESMNGGKLYSNAYL
NDLAGCIKTLRYCAGWADKIQGRTIPIDGNFFTYTRHEPIGVCGQIIPWNFPLVMLIWKI
GPALSCGNTVVVKPAEQTPLTALHVASLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDID
KVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPCIVLADADLDNAVEFAHHGVFYHQG
QCCIAASRIFVEESIYDEFVRRSVERAKKYILGNPLTPGVTQGPQIDKEQYDKILDLIES
GKKEGAKLECGGGPWGNKGYFVQPTVFSNVTDEMRIAKEEIFGPVQQIMKFKSLDDVIKR
ANNTFYGLSAGVFTKDIDKAITISSALQAGTVWVNCYGVVSAQCPFGGFKMSGNGRELGE
YGFHEYTEVKTVTVKISQKNS
|
| Enzyme 55 Number of Residues |
501 |
| Enzyme 55 Molecular Weight |
54861.4 |
| Enzyme 55 Theoretical pI |
6.71 |
| Enzyme 55 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 55 General Function |
Involved in oxidoreductase activity |
| Enzyme 55 Specific Function |
Binds free retinal and cellular retinol-binding protein- bound retinal. Can convert/oxidize retinaldehyde to retinoic acid |
| Enzyme 55 Pathways |
|
| Enzyme 55 Reactions |
- retinal + NAD+ + H2O = retinoate + NADH + 2 H+ [RN:R02123]
|
| Enzyme 55 Pfam Domain Function |
|
| Enzyme 55 Signals |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
2183299 |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
P00352 |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
AL1A1_HUMAN |
| Enzyme 55 PDB ID |
1BXS |
| Enzyme 55 PDB File |
Show |
| Enzyme 55 3D Structure |
|
| Enzyme 55 Cellular Location |
Not Available |
| Enzyme 55 Gene Sequence |
>1506 bp
ATGTCATCCTCAGGCACGCCAGACTTACCTGTCCTACTCACCGATTTGAAGATTCAATAT
ACTAAGATCTTCATAAACAATGAATGGCATGATTCAGTGAGTGGCAAGAAATTTCCTGTC
TTTAATCCTGCAACTGAGGAGGAGCTCTGCCAGGTAGAAGAAGGAGATAAGGAGGATGTT
GACAAGGCAGTGAAGGCCGCAAGACAGGCTTTTCAGATTGGATCTCCGTGGCGTACTATG
GATGCTTCCGAGAGGGGGCGACTATTATACAAGTTGGCTGATTTAATCGAAAGAGATCGT
CTGCTGCTGGCGACAATGGAGTCAATGAATGGTGGAAAACTCTATTCCAATGCATATCTG
AGTGATTTAGCAGGCTGCATCAAAACATTGCGCTACTGTGCAGGTTGGGCTGACAAGATC
CAGGGCCGTACAATACCAATTGATGGAAATTTTTTTACATATACAAGACATGAACCTATT
GGTGTATGTGGCCAAATCATTCCTTGGAATTTCCCGTTGGTTATGCTCATTTGGAAGATA
GGGCCTGCACTGAGCTGTGGAAACACAGTGGTTGTCAAACCAGCAGAGCAAACTCCTCTC
ACTGCTCTCCACGTGGCATCTTTAATAAAAGAGGCAGGGTTTCCTCCTGGAGTAGTGAAT
ATTGTTCCTGGTTATGGGCCTACAGCAGGGGCAGCCATTTCTTCTCACATGGATATAGAC
AAAGTAGCCTTCACAGGATCAACAGAGGTTGGCAAGTTGATCAAAGAAGCTGCCGGGAAA
AGCAATCTGAAGAGGGTGACCCTGGAGCTTGGAGGAAAGAGCCCTTGCATTGTGTTAGCT
GATGCCGACTTGGACAATGCTGTTGAATTTGCACACCATGGGGTATTCTACCACCAGGGC
CAGTGTTGTATAGCCGCATCCAGGATTTTTGTGGAAGAATCAATTTATGATGAGTTTGTT
CGAAGGAGTGTTGAGCGGGCTAAGAAGTATATCCTTGGAAATCCTCTGACCCCAGGAGTC
ACTCAAGGCCCTCAGATTGACAAGGAACAATATGATAAAATACTTGACCTCATTGAGAGT
GGGAAGAAAGAAGGGGCCAAACTGGAATGTGGAGGAGGCCCGTGGGGGAATAAAGGCTAC
TTTGTCCAGCCCACAGTGTTCTCTAATGTTACAGATGAGATGCGCATTGCCAAAGAGGAG
ATTTTTGGACCAGTGCAGCAAATCATGAAGTTTAAATCTTTAGATGACGTGATCAAAAGA
GCAAACAATACTTTCTATGGCTTATCAGCAGGAGTGTTTACCAAAGACATTGATAAAGCC
ATAACAATCTCCTCTGCTCTGCAGGCAGGAACAGTGTGGGTGAATTGCTATGGCGTGGTA
AGTGCCCAGTGCCCCTTTGGCGGATTCAAGATGTCTGGAAATGGAAGAGAACTGGGAGAG
TACGGTTTCCATGAATATACAGAGGTCAAAACAGTCACAGTGAAAATCTCTCAGAAGAAC
TCATAA
|
| Enzyme 55 GenBank Gene ID |
AF003341 |
| Enzyme 55 GeneCard ID |
ALDH1A1 |
| Enzyme 55 GenAtlas ID |
ALDH1A1 |
| Enzyme 55 HGNC ID |
HGNC:402 |
| Enzyme 55 Chromosome Location |
9 |
| Enzyme 55 Locus |
9q21.13 |
| Enzyme 55 SNPs |
SNPJam Report |
| Enzyme 55 General References |
- Hsu LC, Chang WC, Yoshida A: Genomic structure of the human cytosolic aldehyde dehydrogenase gene. Genomics. 1989 Nov;5(4):857-65. [PubMed ]
- Zheng CF, Wang TT, Weiner H: Cloning and expression of the full-length cDNAS encoding human liver class 1 and class 2 aldehyde dehydrogenase. Alcohol Clin Exp Res. 1993 Aug;17(4):828-31. [PubMed ]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Yoshida A, Hsu LC, Yanagawa Y: Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal response, retinal oxidation and implication in testicular feminization. Adv Exp Med Biol. 1993;328:37-44. [PubMed ]
- Hempel J, von Bahr-Lindstrom H, Jornvall H: Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme. Eur J Biochem. 1984 May 15;141(1):21-35. [PubMed ]
- Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed ]
- Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed ]
- Abriola DP, Fields R, Stein S, MacKerell AD Jr, Pietruszko R: Active site of human liver aldehyde dehydrogenase. Biochemistry. 1987 Sep 8;26(18):5679-84. [PubMed ]
- Agarwal DP, Cohn P, Goedde HW, Hempel J: Aldehyde dehydrogenase from human erythrocytes: structural relationship to the liver cytosolic isozyme. Enzyme. 1989;42(1):47-52. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 55 Metabolite References |
Not Available |
|
Enzyme 56
[top]
|
| Enzyme 56 ID |
5435 |
| Enzyme 56 Name |
Dimethylglycine dehydrogenase, mitochondrial |
| Enzyme 56 Synonyms |
- ME2GLYDH
|
| Enzyme 56 Gene Name |
DMGDH |
| Enzyme 56 Protein Sequence |
>Dimethylglycine dehydrogenase, mitochondrial
MLRPGAQLLRGLLLRSCPLQGSPGRPRSVCGREGEEKPPLSAETQWKDRAETVIIGGGCV
GVSLAYHLAKAGMKDVVLLEKSELTAGSTWHAAGLTTYFHPGINLKKIHYDSIKLYEKLE
EETGQVVGFHQPGSIRLATTPVRVDEFKYQMTRTGWHATEQYLIEPEKIQEMFPLLNMNK
VLAGLYNPGDGHIDPYSLTMALAAGARKCGALLKYPAPVTSLKARSDGTWDVETPQGSMR
ANRIVNAAGFWAREVGKMIGLEHPLIPVQHQYVVTSTISEVKALKRELPVLRDLEGSYYL
RQERDGLLFGPYESQEKMKVQDSWVTNGVPPGFGKELFESDLDRIMEHIKAAMEMVPVLK
KADIINVVNGPITYSPDILPMVGPHQGVRNYWVAIGFGYGIIHAGGVGKYLSDWILHGEP
PFDLIELDPNRYGKWTTTQYTEAKARESYGFNNIVGYPKEERFAGRPTQRVSGLYQRLES
KCSMGFHAGWEQPHWFYKPGQDTQYRPSFRRTNWFEPVGSEYKQVMQRVAVTDLSPFGKF
NIKGQDSIRLLDHLFANVIPKVGFTNISHMLTPKGRVYAELTVSHQSPGEFLLITGSGSE
LHDLRWIEEEAVKGGYDVEIKNITDELGVLGVAGPQARKVLQKLTSEDLSDDVFKFLQTK
SLKVSNIPVTAIRISYTGELGWELYHRREDSVALYDAIMNAGQEEGIDNFGTYAMNALRL
EKAFRAWGLEMNCDTNPLEAGLEYFVKLNKPADFIGKQALKQIKAKGLKRRLVCLTLATD
DVDPEGNESIWYNGKVVGNTTSGSYSYSIQKSLAFAYVPVQLSEVGQQVEVELLGKNYPA
VIIQEPLVLTEPTRNRLQKKGGKDKT
|
| Enzyme 56 Number of Residues |
866 |
| Enzyme 56 Molecular Weight |
96810.1 |
| Enzyme 56 Theoretical pI |
7.69 |
| Enzyme 56 GO Classification |
| Function |
- aminomethyltransferase activity
- catalytic activity
- methyltransferase activity
- oxidoreductase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glycine catabolic process
- glycine metabolic process
- metabolic process
- serine family amino acid metabolic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 56 General Function |
Involved in oxidoreductase activity |
| Enzyme 56 Specific Function |
N,N-dimethylglycine + acceptor + H(2)O = sarcosine + formaldehyde + reduced acceptor |
| Enzyme 56 Pathways |
- Glycine, Serine and Threonine Metabolism (map00260 )
|
| Enzyme 56 Reactions |
- N,N-dimethylglycine + acceptor + H2O = sarcosine + formaldehyde + reduced acceptor [RN:R01565]
|
| Enzyme 56 Pfam Domain Function |
|
| Enzyme 56 Signals |
|
| Enzyme 56 Transmembrane Regions |
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
24797151 |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
Q9UI17 |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
M2GD_HUMAN |
| Enzyme 56 PDB ID |
Not Available |
| Enzyme 56 Cellular Location |
Not Available |
| Enzyme 56 Gene Sequence |
>2601 bp
ATGCTCCGTCCCGGCGCGCAGCTGCTGCGGGGCCTCCTGCTGCGGAGCTGCCCGCTGCAG
GGCTCCCCCGGGCGCCCGCGCTCTGTCTGCGGCCGGGAAGGAGAGGAAAAACCACCCTTA
TCTGCAGAAACACAATGGAAAGACAGAGCAGAAACAGTGATAATTGGAGGTGGCTGTGTT
GGTGTGAGTCTGGCTTATCACCTGGCCAAAGCAGGGATGAAAGATGTGGTCCTGCTGGAG
AAATCAGAGCTCACGGCTGGATCTACCTGGCACGCAGCAGGTTTAACAACTTACTTTCAT
CCTGGAATAAACTTGAAGAAAATACATTATGATAGCATCAAACTTTATGAGAAACTGGAA
GAAGAAACTGGTCAGGTGGTGGGATTCCATCAGCCAGGTAGTATCAGACTTGCTACCACC
CCTGTAAGGGTAGATGAATTTAAATATCAAATGACTCGGACTGGCTGGCATGCAACAGAA
CAGTATCTCATTGAACCTGAAAAAATTCAAGAGATGTTCCCTTTACTCAACATGAATAAG
GTTTTAGCTGGATTGTATAATCCTGGAGATGGTCACATTGATCCTTATTCTCTAACTATG
GCACTGGCTGCTGGGGCTAGGAAATGTGGTGCCCTTTTAAAATATCCTGCACCAGTAACT
TCTCTGAAAGCCAGGTCAGATGGAACATGGGACGTTGAAACACCACAGGGGTCTATGAGA
GCAAATAGAATTGTGAATGCTGCAGGATTTTGGGCTCGTGAAGTAGGTAAAATGATTGGA
CTAGAACATCCTCTCATTCCGGTTCAACATCAATATGTTGTTACATCGACTATATCTGAA
GTGAAAGCTTTGAAACGAGAACTGCCTGTGCTCCGTGACCTGGAAGGATCATATTATCTC
CGACAGGAAAGGGATGGGCTTTTGTTTGGTCCATATGAAAGTCAAGAGAAAATGAAAGTT
CAGGACTCCTGGGTCACCAATGGAGTTCCTCCAGGTTTTGGAAAGGAACTCTTTGAGTCT
GATCTAGATCGAATCATGGAACACATCAAAGCTGCCATGGAAATGGTTCCTGTCTTGAAA
AAGGCTGACATCATCAATGTTGTCAATGGTCCTATCACGTATTCTCCTGACATTCTGCCT
ATGGTGGGGCCCCATCAGGGGGTCAGAAACTACTGGGTGGCTATAGGCTTTGGATATGGC
ATAATCCACGCTGGTGGGGTAGGGAAATATCTCAGTGACTGGATCCTGCATGGAGAACCT
CCTTTTGATCTGATAGAATTGGATCCTAATCGCTATGGCAAATGGACAACAACCCAGTAC
ACTGAGGCCAAAGCAAGAGAATCATATGGATTCAACAATATTGTTGGTTATCCTAAAGAA
GAACGGTTTGCTGGGAGGCCGACTCAACGAGTCAGTGGGCTCTATCAAAGGCTGGAGTCT
AAGTGTTCCATGGGGTTCCATGCTGGCTGGGAGCAGCCGCACTGGTTCTACAAACCAGGC
CAGGACACTCAGTACAGGCCAAGTTTTCGCCGCACAAACTGGTTTGAGCCTGTGGGCTCG
GAGTATAAACAGGTTATGCAAAGAGTAGCGGTAACTGACCTATCACCATTTGGCAAGTTT
AACATCAAAGGCCAAGATTCCATTAGACTACTGGACCATCTCTTTGCAAATGTCATTCCA
AAGGTGGGTTTTACAAATATAAGTCACATGTTAACACCCAAGGGTCGAGTGTATGCTGAG
CTGACTGTTTCTCACCAATCTCCTGGGGAGTTTCTTTTAATTACTGGCTCTGGATCAGAA
CTTCATGATCTTAGATGGATTGAAGAAGAAGCAGTCAAAGGTGGATATGATGTTGAAATT
AAAAACATAACTGATGAGCTTGGAGTTCTTGGAGTTGCTGGGCCACAGGCAAGAAAGGTC
CTTCAGAAACTGACCTCTGAAGATCTTAGTGATGATGTTTTCAAGTTTCTTCAAACCAAG
TCCTTAAAGGTTTCCAACATTCCTGTCACTGCTATTAGGATATCTTATACTGGTGAGCTG
GGTTGGGAGCTGTATCACAGAAGAGAAGATTCTGTGGCGCTGTATGACGCTATCATGAAT
GCAGGCCAGGAGGAGGGAATCGACAATTTTGGAACCTATGCCATGAATGCCTTACGCCTG
GAGAAAGCCTTCAGAGCCTGGGGGTTAGAGATGAACTGTGATACAAATCCTTTGGAAGCT
GGACTGGAATATTTTGTGAAGTTAAATAAGCCAGCAGACTTCATAGGAAAGCAAGCACTG
AAACAGATTAAAGCCAAGGGGCTGAAACGAAGACTGGTCTGCCTCACCTTGGCAACGGAT
GATGTTGATCCAGAGGGAAATGAAAGCATCTGGTACAATGGCAAGGTGGTTGGCAACACG
ACATCTGGAAGCTATAGCTACAGCATCCAGAAGAGTCTGGCTTTCGCATATGTCCCTGTA
CAACTAAGTGAAGTGGGACAGCAAGTGGAAGTTGAACTATTAGGCAAAAATTACCCAGCA
GTCATCATACAAGAACCTTTGGTATTGACCGAACCAACCAGAAACCGGCTTCAGAAAAAA
GGTGGAAAGGACAAAACTTGA
|
| Enzyme 56 GenBank Gene ID |
NM_013391.2 |
| Enzyme 56 GeneCard ID |
DMGDH |
| Enzyme 56 GenAtlas ID |
DMGDH |
| Enzyme 56 HGNC ID |
HGNC:24475 |
| Enzyme 56 Chromosome Location |
5 |
| Enzyme 56 Locus |
5q14.1 |
| Enzyme 56 SNPs |
SNPJam Report |
| Enzyme 56 General References |
- Binzak BA, Vockley JG, Jenkins RB, Vockley J: Structure and analysis of the human dimethylglycine dehydrogenase gene. Mol Genet Metab. 2000 Mar;69(3):181-7. [PubMed ]
- Binzak BA, Wevers RA, Moolenaar SH, Lee YM, Hwu WL, Poggi-Bach J, Engelke UF, Hoard HM, Vockley JG, Vockley J: Cloning of dimethylglycine dehydrogenase and a new human inborn error of metabolism, dimethylglycine dehydrogenase deficiency. Am J Hum Genet. 2001 Apr;68(4):839-47. Epub 2001 Feb 28. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed ]
- Moolenaar SH, Poggi-Bach J, Engelke UF, Corstiaensen JM, Heerschap A, de Jong JG, Binzak BA, Vockley J, Wevers RA: Defect in dimethylglycine dehydrogenase, a new inborn error of metabolism: NMR spectroscopy study. Clin Chem. 1999 Apr;45(4):459-64. [PubMed ]
|
| Enzyme 56 Metabolite References |
Not Available |
|
Enzyme 57
[top]
|
| Enzyme 57 ID |
5437 |
| Enzyme 57 Name |
Retinal dehydrogenase 2 |
| Enzyme 57 Synonyms |
- RALDH 2
- RalDH2
- Aldehyde dehydrogenase family 1 member A2
- Retinaldehyde-specific dehydrogenase type 2
- RALDH(II)
|
| Enzyme 57 Gene Name |
ALDH1A2 |
| Enzyme 57 Protein Sequence |
>Retinal dehydrogenase 2
MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTKIFINNEWQNSESGRVFPVYNP
ATGEQVCEVQEADKADIDKAVQAARLAFSLGSVWRRMDASERGRLLDKLADLVERDRAVL
ATMESLNGGKPFLQAFYVDLQGVIKTFRYYAGWADKIHGMTIPVDGDYFTFTRHEPIGVC
GQIIPWNFPLLMFAWKIAPALCCGNTVVIKPAEQTPLSALYMGALIKEAGFPPGVINILP
GYGPTAGAAIASHIGIDKIAFTGSTEVGKLIQEAAGRSNLKRVTLELGGKSPNIIFADAD
LDYAVEQAHQGVFFNQGQCCTAGSRIFVEESIYEEFVRRSVERAKRRVVGSPFDPTTEQG
PQIDKKQYNKILELIQSGVAEGAKLECGGKGLGRKGFFIEPTVFSNVTDDMRIAKEEIFG
PVQEILRFKTMDEVIERANNSDFGLVAAVFTNDINKALTVSSAMQAGTVWINCYNALNAQ
SPFGGFKMSGNGREMGEFGLREYSEVKTVTVKIPQKNS
|
| Enzyme 57 Number of Residues |
518 |
| Enzyme 57 Molecular Weight |
56723.5 |
| Enzyme 57 Theoretical pI |
5.84 |
| Enzyme 57 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 57 General Function |
Involved in oxidoreductase activity |
| Enzyme 57 Specific Function |
Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently |
| Enzyme 57 Pathways |
|
| Enzyme 57 Reactions |
- retinal + NAD+ + H2O = retinoate + NADH + 2 H+ [RN:R02123]
|
| Enzyme 57 Pfam Domain Function |
|
| Enzyme 57 Signals |
|
| Enzyme 57 Transmembrane Regions |
|
| Enzyme 57 Essentiality |
Not Available |
| Enzyme 57 GenBank ID Protein |
3970842 |
| Enzyme 57 UniProtKB/Swiss-Prot ID |
O94788 |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
AL1A2_HUMAN |
| Enzyme 57 PDB ID |
1BI9 |
| Enzyme 57 PDB File |
Show |
| Enzyme 57 3D Structure |
|
| Enzyme 57 Cellular Location |
Not Available |
| Enzyme 57 Gene Sequence |
>1557 bp
ATGACTTCCAGCAAGATAGAGATGCCCGGCGAGGTGAAGGCCGACCCCGCCGCCCTCATG
GCGTCGCTGCACCTCCTGCCGTCGCCCACGCCCAATCTCGAAATTAAGTACACCAAGATC
TTTATAAACAACGAGTGGCAGAACTCAGAGAGTGGGAGAGTGTTCCCTGTCTATAATCCA
GCCACAGGAGAACAGGTGTGTGAAGTTCAAGAAGCAGACAAGGCAGATATAGACAAAGCA
GTGCAGGCAGCCCGCCTGGCTTTCTCTCTTGGTTCAGTGTGGAGAAGGATGGATGCTTCA
GAAAGGGGACGTCTGTTGGATAAGCTTGCAGACTTGGTGGAACGGGACAGGGCAGTTCTT
GCAACCATGGAATCCCTAAATGGTGGCAAACCATTCCTGCAAGCTTTTTATGTGGATTTG
CAGGGCGTCATCAAAACCTTTCGATATTACGCAGGCTGGGCTGATAAAATTCATGGGATG
ACCATTCCTGTAGATGGAGACTATTTTACCTTTACAAGACATGAACCCATTGGAGTGTGT
GGACAGATCATCCCATGGAACTTCCCCCTGCTGATGTTTGCCTGGAAAATAGCTCCAGCT
TTGTGCTGTGGCAATACAGTAGTTATTAAGCCAGCAGAGCAAACACCACTCAGTGCACTC
TACATGGGAGCCCTCATCAAGGAGGCTGGCTTTCCTCCCGGGGTCATCAATATTTTGCCA
GGATATGGGCCAACGGCTGGGGCAGCAATAGCTTCTCACATTGGCATAGACAAGATTGCA
TTCACAGGGTCTACTGAGGTTGGAAAGCTTATCCAAGAAGCAGCTGGAAGAAGTAATTTG
AAGAGAGTAACTCTGGAACTTGGAGGCAAAAGTCCTAATATTATTTTTGCTGATGCTGAC
TTGGACTATGCTGTGGAGCAGGCCCACCAGGGTGTGTTCTTCAATCAAGGTCAGTGCTGC
ACTGCAGGCTCTCGCATCTTCGTGGAGGAGTCCATCTATGAGGAGTTTGTGAGAAGAAGC
GTGGAGCGGGCCAAGAGGCGCATAGTGGGGAGTCCCTTTGACCCCACCACTGAGCAGGGT
CCCCAGATTGATAAGAAACAGTACAACAAGATCTTGGAACTCATCCAGAGTGGTGTGGCT
GAGGGCGCCAAGCTGGAATGTGGAGGCAAAGGACTGGGCCGAAAGGGGTTTTTCATTGAG
CCCACAGTGTTTTCCAACGTCACTGATGATATGCGGATTGCCAAGGAGGAGATCTTTGGC
CCTGTTCAGGAAATTTTGAGATTTAAGACGATGGATGAAGTTATCGAAAGAGCCAATAAC
TCAGACTTTGGACTCGTAGCAGCTGTCTTTACTAATGACATCAACAAGGCCCTCACAGTG
TCTTCTGCAATGCAAGCTGGGACTGTTTGGATCAATTGTTACAATGCCTTAAATGCCCAG
AGCCCCTTTGGGGGATTCAAGATGTCTGGAAATGGGAGAGAAATGGGAGAATTTGGCTTG
CGGGAGTACTCAGAAGTTAAGACGGTGACAGTAAAGATCCCCCAGAAGAACTCCTAA
|
| Enzyme 57 GenBank Gene ID |
AB015226 |
| Enzyme 57 GeneCard ID |
ALDH1A2 |
| Enzyme 57 GenAtlas ID |
ALDH1A2 |
| Enzyme 57 HGNC ID |
HGNC:15472 |
| Enzyme 57 Chromosome Location |
1 |
| Enzyme 57 Locus |
15q21.3 |
| Enzyme 57 SNPs |
SNPJam Report |
| Enzyme 57 General References |
- Ono Y, Fukuhara N, Yoshie O: TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3. Mol Cell Biol. 1998 Dec;18(12):6939-50. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
|
| Enzyme 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
5438 |
| Enzyme 58 Name |
D-amino-acid oxidase |
| Enzyme 58 Synonyms |
- DAAO
- DAMOX
- DAO
|
| Enzyme 58 Gene Name |
DAO |
| Enzyme 58 Protein Sequence |
>D-amino-acid oxidase
MRVVVIGAGVIGLSTALCIHERYHSVLQPLDIKVYADRFTPLTTTDVAAGLWQPYLSDPN
NPQEADWSQQTFDYLLSHVHSPNAENLGLFLISGYNLFHEAIPDPSWKDTVLGFRKLTPR
ELDMFPDYGYGWFHTSLILEGKNYLQWLTERLTERGVKFFQRKVESFEEVAREGADVIVN
CTGVWAGALQRDPLLQPGRGQIMKVDAPWMKHFILTHDPERGIYNSPYIIPGTQTVTLGG
IFQLGNWSELNNIQDHNTIWEGCCRLEPTLKNARIIGERTGFRPVRPQIRLEREQLRTGP
SNTEVIHNYGHGGYGLTIHWGCALEAAKLFGRILEEKKLSRMPPSHL
|
| Enzyme 58 Number of Residues |
347 |
| Enzyme 58 Molecular Weight |
39473.7 |
| Enzyme 58 Theoretical pI |
6.84 |
| Enzyme 58 GO Classification |
| Function |
- D-amino-acid oxidase activity
- binding
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-NH2 group of donors
- oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 58 General Function |
Involved in D-amino-acid oxidase activity |
| Enzyme 58 Specific Function |
Regulates the level of the neuromodulator D-serine in the brain. Has high activity towards D-DOPA and contributes to dopamine synthesis. Could act as a detoxifying agent which removes D-amino acids accumulated during aging. Acts on a variety of D- amino acids with a preference for those having small hydrophobic side chains followed by those bearing polar, aromatic, and basic groups. Does not act on acidic amino acids |
| Enzyme 58 Pathways |
- Arginine and Proline Metabolism (map00330 )
- D-Arginine and D-ornithine Metabolism (map00472 )
- Glycine, Serine and Threonine Metabolism (map00260 )
|
| Enzyme 58 Reactions |
- a D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2 [RN:R01340]
|
| Enzyme 58 Pfam Domain Function |
|
| Enzyme 58 Signals |
|
| Enzyme 58 Transmembrane Regions |
|
| Enzyme 58 Essentiality |
Not Available |
| Enzyme 58 GenBank ID Protein |
30446 |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
P14920 |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
OXDA_HUMAN |
| Enzyme 58 PDB ID |
Not Available |
| Enzyme 58 Cellular Location |
Not Available |
| Enzyme 58 Gene Sequence |
>1044 bp
ATGCGTGTGGTGGTGATTGGAGCAGGAGTCATCGGGCTGTCCACCGCCCTCTGCATCCAT
GAGCGCTACCACTCAGTCCTGCAGCCACTGCACATAAAGGTCTACGCGGACCGCTTCACC
CCACTCACCACCACCGACGTGGCTGCCGGCCTCTGGCAGCCCTACCTTTCTGACCCCAAC
AACCCACAGGAGGCGGACTGGAGCCAACAGACCTTTGACTATCTCCTGAGCCATGTCCAT
TCTCCCAACGCTGAAAACCTGGGCCTGTTCCTAATCTCGGGCTACAACCTCTTCCATGAA
GCCATTCCGGACCCTTCCTGGAAGGACACAGTTCTGGGATTTCGGAAGCTGACCCCCAGA
GAGCTGGATATGTTCCCAGATTACGGCTATGGCTGGTTCCACACAAGCCTAATTCTGGAG
GGAAAGAACTATCTACAGTGGCTGACTGAAAGGTTAACTGAGAGGGGAGTGAAGTTCTTC
CAGCGGAAAGTGGAGTCTTTTGAGGAGGTGGCAAGAGAAGGCGCAGACGTGATTGTCAAC
TGCACTGGGGTATGGGCTGGGGCGCTACAACGAGACCCCCTGCTGCAGCCAGGCCGGGGG
CAGATCATGAAGGTGGACGCCCCTTGGATGAAGCACTTCATTCTCACCCATGACCCAGAG
AGAGGCATCTACAATTCCCCGTACATCATCCCAGGGACCCAGACAGTTACTCTTGGAGGC
ATCTTCCAGTTGGGAAACTGGAGTGAACTAAACAATATCCAGGACCACAACACCATTTGG
GAAGGCTGCTGCAGACTGGAGCCCACACTGAAGAATGCAAGAATTATTGGTGAAGCAACT
GGCTTCCGGCCAGTACGCCCCCAGATTCGGCTAGAAAGAGAACAGCTTCGCACTGGACCT
TCAAACACAGAGGTCATCCACAACTATGGCCATGGAGGCTACGGGCTCACCATCCACTGG
GGATGTGCCCTGGAGGCAGCCAAGCTCTTTGGGAGAATCCTGGAAGAAAAGAAATTGTCC
AGAATGCCACCATCCCACCTCTGA
|
| Enzyme 58 GenBank Gene ID |
X13227 |
| Enzyme 58 GeneCard ID |
DAO |
| Enzyme 58 GenAtlas ID |
DAO |
| Enzyme 58 HGNC ID |
HGNC:2671 |
| Enzyme 58 Chromosome Location |
1 |
| Enzyme 58 Locus |
12q24 |
| Enzyme 58 SNPs |
SNPJam Report |
| Enzyme 58 General References |
- Momoi K, Fukui K, Watanabe F, Miyake Y: Molecular cloning and sequence analysis of cDNA encoding human kidney D-amino acid oxidase. FEBS Lett. 1988 Sep 26;238(1):180-4. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Fukui K, Miyake Y: Molecular cloning and chromosomal localization of a human gene encoding D-amino-acid oxidase. J Biol Chem. 1992 Sep 15;267(26):18631-8. [PubMed ]
- Kawazoe T, Tsuge H, Pilone MS, Fukui K: Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring. Protein Sci. 2006 Dec;15(12):2708-17. Epub 2006 Nov 6. [PubMed ]
- Kawazoe T, Tsuge H, Imagawa T, Aki K, Kuramitsu S, Fukui K: Structural basis of D-DOPA oxidation by D-amino acid oxidase: alternative pathway for dopamine biosynthesis. Biochem Biophys Res Commun. 2007 Apr 6;355(2):385-91. Epub 2007 Feb 8. [PubMed ]
- Sparey T, Abeywickrema P, Almond S, Brandon N, Byrne N, Campbell A, Hutson PH, Jacobson M, Jones B, Munshi S, Pascarella D, Pike A, Prasad GS, Sachs N, Sakatis M, Sardana V, Venkatraman S, Young MB: The discovery of fused pyrrole carboxylic acids as novel, potent D-amino acid oxidase (DAO) inhibitors. Bioorg Med Chem Lett. 2008 Jun 1;18(11):3386-91. Epub 2008 Apr 13. [PubMed ]
|
| Enzyme 58 Metabolite References |
Not Available |
|
Enzyme 59
[top]
|
| Enzyme 59 ID |
5443 |
| Enzyme 59 Name |
Glucosamine-6-phosphate isomerase 1 |
| Enzyme 59 Synonyms |
- Glucosamine-6-phosphate deaminase 1
- GNPDA 1
- GlcN6P deaminase 1
- Oscillin
|
| Enzyme 59 Gene Name |
GNPDA1 |
| Enzyme 59 Protein Sequence |
>Glucosamine-6-phosphate isomerase 1
MKLIILEHYSQASEWAAKYIRNRIIQFNPGPEKYFTLGLPTGSTPLGCYKKLIEYYKNGD
LSFKYVKTFNMDEYVGLPRDHPESYHSFMWNNFFKHIDIHPENTHILDGNAVDLQAECDA
FEEKIKAAGGIELFVGGIGPDGHIAFNEPGSSLVSRTRVKTLAMDTILANARFFDGELTK
VPTMALTVGVGTVMDAREVMILITGAHKAFALYKAIEEGVNHMWTVSAFQQHPRTVFVCD
EDATLELKVKTVKYFKGLMLVHNKLVDPLYSIKEKETEKSQSSKKPYSD
|
| Enzyme 59 Number of Residues |
289 |
| Enzyme 59 Molecular Weight |
32668.3 |
| Enzyme 59 Theoretical pI |
6.91 |
| Enzyme 59 GO Classification |
| Function |
- catalytic activity
- glucosamine-6-phosphate deaminase activity
- intramolecular oxidoreductase activity
- intramolecular oxidoreductase activity, interconverting aldoses and ketoses
- isomerase activity
|
| Process |
- N-acetylglucosamine metabolic process
- alcohol metabolic process
- amino sugar metabolic process
- carbohydrate metabolic process
- glucosamine metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 59 General Function |
Involved in carbohydrate metabolic process |
| Enzyme 59 Specific Function |
Seems to trigger calcium oscillations in mammalian eggs. These oscillations serve as the essential trigger for egg activation and early development of the embryo |
| Enzyme 59 Pathways |
|
| Enzyme 59 Reactions |
- D-glucosamine 6-phosphate + H2O = D-fructose 6-phosphate + NH3 [RN:R00765]
|
| Enzyme 59 Pfam Domain Function |
|
| Enzyme 59 Signals |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
Not Available |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
P46926 |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
GNPI1_HUMAN |
| Enzyme 59 PDB ID |
1NE7 |
| Enzyme 59 PDB File |
Show |
| Enzyme 59 3D Structure |
|
| Enzyme 59 Cellular Location |
Not Available |
| Enzyme 59 Gene Sequence |
>870 bp
ATGAAGCTCATCATCCTGGAGCACTATTCTCAGGCGAGCGAGTGGGCGGCTAAATACATC
AGGAACCGTATCATCCAGTTTAACCCAGGGCCAGAGAAGTACTTCACCCTGGGGCTCCCC
ACTGGGAGTACCCCACTTGGCTGCTACAAGAAGCTGATTGAATACTATAAGAATGGGGAC
CTGTCCTTTAAATATGTGAAGACCTTCAACATGGATGAGTACGTGGGCCTTCCTCGAGAC
CACCCGGAGAGTTACCACTCCTTCATGTGGAACAACTTCTTCAAGCACATTGACATCCAC
CCAGAAAACACCCACATTCTGGATGGGAATGCAGTCGACCTACAGGCAGAATGTGATGCC
TTTGAAGAGAAGATCAAGGCTGCAGGTGGGATCGAGCTATTTGTTGGAGGCATCGGCCCT
GATGGACACATTGCCTTCAACGAGCCAGGCTCCAGTCTGGTGTCCAGGACCCGTGTGAAG
ACGCTGGCCATGGATACCATCCTGGCCAATGCTAGGTTCTTCGATGGAGAACTCACCAAG
GTGCCCACCATGGCCTTGACGGTGGGGGTGGGCACTGTCATGGATGCTAGAGAGGTGATG
ATCCTTATCACAGGTGCTCACAAGGCATTTGCTCTGTACAAGGCCATCGAGGAGGGAGTG
AACCACATGTGGACCGTGTCTGCCTTCCAGCAGCATCCCCGCACCGTGTTTGTGTGTGAC
GAGGATGCCACCTTGGAGCTGAAAGTGAAGACTGTCAAGTATTTCAAAGGTTTAATGCTT
GTTCATAACAAGTTGGTGGACCCCTTGTACAGTATCAAAGAGAAAGAAACTGAGAAAAGC
CAATCTTCGAAGAAACCATACAGCGATTAG
|
| Enzyme 59 GenBank Gene ID |
AF048826 |
| Enzyme 59 GeneCard ID |
GNPDA1 |
| Enzyme 59 GenAtlas ID |
GNPDA1 |
| Enzyme 59 HGNC ID |
HGNC:4417 |
| Enzyme 59 Chromosome Location |
5 |
| Enzyme 59 Locus |
5q21 |
| Enzyme 59 SNPs |
SNPJam Report |
| Enzyme 59 General References |
- Wolosker H, Kline D, Bian Y, Blackshaw S, Cameron AM, Fralich TJ, Schnaar RL, Snyder SH: Molecularly cloned mammalian glucosamine-6-phosphate deaminase localizes to transporting epithelium and lacks oscillin activity. FASEB J. 1998 Jan;12(1):91-9. [PubMed ]
- Shevchenko V, Hogben M, Ekong R, Parrington J, Lai FA: The human glucosamine-6-phosphate deaminase gene: cDNA cloning and expression, genomic organization and chromosomal localization. Gene. 1998 Aug 17;216(1):31-8. [PubMed ]
- Nomura N, Nagase T, Miyajima N, Sazuka T, Tanaka A, Sato S, Seki N, Kawarabayasi Y, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1994;1(5):223-9. [PubMed ]
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Arreola R, Valderrama B, Morante ML, Horjales E: Two mammalian glucosamine-6-phosphate deaminases: a structural and genetic study. FEBS Lett. 2003 Sep 11;551(1-3):63-70. [PubMed ]
|
| Enzyme 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
5453 |
| Enzyme 60 Name |
Pancreatic triacylglycerol lipase |
| Enzyme 60 Synonyms |
- PL
- Pancreatic lipase
|
| Enzyme 60 Gene Name |
PNLIP |
| Enzyme 60 Protein Sequence |
>Pancreatic triacylglycerol lipase
MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTN
ENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCIC
VDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGR
RTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGH
LDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGF
PCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFARWRYKVS
VTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWY
NNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC
|
| Enzyme 60 Number of Residues |
465 |
| Enzyme 60 Molecular Weight |
51156.5 |
| Enzyme 60 Theoretical pI |
6.72 |
| Enzyme 60 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 60 General Function |
Involved in catalytic activity |
| Enzyme 60 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 60 Pathways |
|
| Enzyme 60 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 60 Pfam Domain Function |
|
| Enzyme 60 Signals |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
Not Available |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
P16233 |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
LIPP_HUMAN |
| Enzyme 60 PDB ID |
1N8S |
| Enzyme 60 PDB File |
Show |
| Enzyme 60 3D Structure |
|
| Enzyme 60 Cellular Location |
Not Available |
| Enzyme 60 Gene Sequence |
>1398 bp
ATGCTGCCACTTTGGACTCTTTCACTGCTGCTGGGAGCAGTAGCAGGAAAAGAAGTTTGC
TACGAAAGACTCGGCTGCTTCAGTGATGACTCCCCATGGTCAGGAATTACGGAAAGACCC
CTCCATATATTGCCTTGGTCTCCAAAAGATGTCAACACCCGCTTCCTCCTATATACTAAT
GAGAACCCAAACAACTTTCAAGAAGTTGCCGCAGATTCATCAAGCATCAGTGGCTCCAAT
TTCAAAACAAATAGAAAAACTCGCTTTATTATTCATGGATTCATAGACAAGGGAGAAGAA
AACTGGCTGGCCAATGTGTGCAAGAATCTGTTCAAGGTGGAAAGTGTGAACTGTATCTGT
GTGGACTGGAAAGGTGGCTCCCGAACTGGATACACACAAGCCTCGCAGAACATCAGGATC
GTGGGAGCAGAAGTGGCATATTTTGTTGAATTTCTTCAGTCGGCGTTCGGTTACTCACCT
TCCAACGTGCATGTCATTGGCCACAGCCTGGGTGCCCACGCTGCTGGGGAGGCTGGAAGG
AGAACCAATGGGACCATTGGACGCATCACAGGGTTGGACCCAGCAGAACCTTGCTTTCAG
GGCACACCTGAATTAGTCCGATTGGACCCCAGCGATGCCAAATTTGTGGATGTAATTCAC
ACGGATGGTGCCCCCATAGTCCCCAATTTGGGGTTTGGAATGAGCCAAGTCGTGGGCCAC
CTAGATTTCTTTCCAAATGGAGGAGTGGAAATGCCTGGATGTAAAAAGAACATTCTCTCT
CAGATTGTGGACATAGACGGAATCTGGGAAGGGACTCGAGACTTTGCGGCCTGTAATCAC
TTAAGAAGCTACAAATATTACACTGATAGCATCGTCAACCCTGATGGCTTTGCTGGATTC
CCCTGTGCCTCTTACAACGTCTTCACTGCAAACAAGTGTTTCCCTTGTCCAAGTGGAGGC
TGCCCACAGATGGGTCACTATGCTGATAGATATCCTGGGAAAACAAATGATGTGGGCCAG
AAATTTTATCTAGACACTGGTGATGCCAGTAATTTTGCACGTTGGAGGTATAAGGTATCT
GTCACACTGTCTGGAAAAAAGGTTACAGGACACATACTAGTTTCTTTGTTCGGAAATAAA
GGAAACTCTAAGCAGTATGAAATTTTCAAGGGCACTCTCAAACCAGATAGTACTCATTCC
AATGAATTTGACTCAGATGTGGATGTTGGGGACTTGCAGATGGTTAAATTTATTTGGTAT
AACAATGTGATCAACCCAACTTTACCTAGAGTGGGAGCATCCAAGATTATAGTGGAGACA
AATGTTGGAAAACAGTTCAACTTCTGTAGTCCAGAAACCGTCAGGGAGGAAGTTCTGCTC
ACCCTCACACCGTGTTAG
|
| Enzyme 60 GenBank Gene ID |
J05125 |
| Enzyme 60 GeneCard ID |
PNLIP |
| Enzyme 60 GenAtlas ID |
PNLIP |
| Enzyme 60 HGNC ID |
HGNC:9155 |
| Enzyme 60 Chromosome Location |
1 |
| Enzyme 60 Locus |
10q26.1 |
| Enzyme 60 SNPs |
SNPJam Report |
| Enzyme 60 General References |
- Lowe ME, Rosenblum JL, Strauss AW: Cloning and characterization of human pancreatic lipase cDNA. J Biol Chem. 1989 Nov 25;264(33):20042-8. [PubMed ]
- Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed ]
- Sims HF, Jennens ML, Lowe ME: The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family. Gene. 1993 Sep 15;131(2):281-5. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Winkler FK, D'Arcy A, Hunziker W: Structure of human pancreatic lipase. Nature. 1990 Feb 22;343(6260):771-4. [PubMed ]
- van Tilbeurgh H, Sarda L, Verger R, Cambillau C: Structure of the pancreatic lipase-procolipase complex. Nature. 1992 Sep 10;359(6391):159-62. [PubMed ]
- van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C: Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 1993 Apr 29;362(6423):814-20. [PubMed ]
- Carriere F, Thirstrup K, Boel E, Verger R, Thim L: Structure-function relationships in naturally occurring mutants of pancreatic lipase. Protein Eng. 1994 Apr;7(4):563-9. [PubMed ]
|
| Enzyme 60 Metabolite References |
Not Available |
|
Enzyme 61
[top]
|
| Enzyme 61 ID |
5454 |
| Enzyme 61 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1 |
| Enzyme 61 Synonyms |
- PLC-154
- Phosphoinositide phospholipase C-beta-1
- Phospholipase C-I
- PLC-I
- Phospholipase C-beta-1
- PLC-beta-1
|
| Enzyme 61 Gene Name |
PLCB1 |
| Enzyme 61 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-1
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKE
TELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLV
AFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSA
DRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYL
TVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLS
GEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCV
ELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQ
QAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKK
KLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEM
SNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPK
GTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDK
HFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQG
NAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNER
NQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKK
EADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQS
VLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYL
RRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLR
QEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKI
TEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKP
KLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSS
EELGGDIPGKEFDTPL
|
| Enzyme 61 Number of Residues |
1216 |
| Enzyme 61 Molecular Weight |
138565.8 |
| Enzyme 61 Theoretical pI |
6.12 |
| Enzyme 61 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid catabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 61 General Function |
Involved in calcium ion binding |
| Enzyme 61 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes |
| Enzyme 61 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 61 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 61 Pfam Domain Function |
|
| Enzyme 61 Signals |
|
| Enzyme 61 Transmembrane Regions |
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
12083581 |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
Q9NQ66 |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
PLCB1_HUMAN |
| Enzyme 61 PDB ID |
Not Available |
| Enzyme 61 Cellular Location |
Not Available |
| Enzyme 61 Gene Sequence |
>3651 bp
ATGGCCGGGGCTCAACCCGGAGTGCACGCCTTGCAACTCAAGCCCGTGTGCGTGTCCGAC
AGCCTCAAGAAGGGCACCAAATTCGTCAAGTGGGATGATGACTCAACTATTGTTACTCCA
ATTATTTTGAGGACTGACCCTCAGGGATTTTTCTTTTACTGGACAGATCAAAACAAGGAG
ACAGAGCTACTGGATCTCAGCCTTGTCAAAGATGCCAGATGTGGGAGACACGCCAAAGCT
CCCAAGGACCCCAAATTACGTGAACTTTTGGATGTGGGGAACATCGGGCGCCTGGAGCAG
CGCATGATCACAGTGGTGTATGGGCCTGACCTCGTGAACATCTCCCATTTGAATCTCGTG
GCTTTCCAAGAAGAAGTGGCCAAGGAATGGACAAATGAGGTTTTCAGTTTGGCAACAAAC
CTGCTGGCCCAAAACATGTCCAGGGATGCATTTCTGGAAAAAGCCTATACTAAACTTAAG
CTGCAAGTCACTCCAGAAGGGCGTATTCCTCTCAAAAACATATATCGCTTGTTTTCAGCA
GATCGGAAGCGAGTTGAAACTGCTTTAGAGGCTTGTAGTCTTCCATCTTCAAGGAATGAT
TCAATACCTCAAGAAGATTTCACTCCAGAAGTGTACAGAGTTTTCCTCAACAACCTTTGC
CCTCGACCTGAAATTGATAACATCTTTTCAGAATTTGGTGCAAAAAGCAAACCATATCTT
ACCGTTGATCAGATGATGGATTTTATCAACCTTAAGCAGCGAGATCCTCGGCTTAATGAA
ATACTTTATCCACCTCTAAAACAAGAGCAAGTCCAAGTATTGATTGAGAAGTATGAACCC
AACAACAGCCTCGCCAGAAAAGGACAAATATCAGTGGATGGGTTCATGCGCTATCTGAGT
GGAGAAGAAAACGGAGTCGTTTCACCTGAGAAACTGGATTTGAATGAAGACATGTCTCAG
CCCCTTTCTCACTATTTCATTAATTCCTCGCACAACACCTACCTCACAGCTGGCCAACTG
GCTGGAAACTCCTCTGTTGAGATGTATCGCCAAGTGCTCCTGTCTGGTTGTCGCTGTGTG
GAGCTGGACTGCTGGAAGGGACGGACTGCAGAAGAGGAACCTGTCATCACCCATGGCTTC
ACCATGACAACTGAAATATCTTTCAAGGAAGTGATAGAAGCAATTGCGGAGTGTGCATTT
AAGACTTCACCTTTTCCAATTCTCCTTTCGTTTGAGAACCATGTGGATTCCCCAAAGCAG
CAAGCCAAGATGGCGGAGTACTGCCGACTGATCTTTGGGGATGCCCTTCTCATGGAGCCC
CTGGAAAAATATCCACTGGAATCTGGAGTTCCTCTTCCAAGCCCTATGGATTTAATGTAT
AAAATTTTGGTGAAAAATAAGAAGAAATCACACAAGTCATCAGAAGGAAGCGGCAAAAAG
AAGCTCTCAGAACAAGCCTCCAACACCTACAGTGACTCCTCCAGCATGTTCGAGCCCTCA
TCCCCAGGAGCCGGAGAAGCTGATACGGAAAGTGACGACGACGATGATGATGATGACTGT
AAAAAATCTTCAATGGATGAGGGGACTGCTGGAAGTGAGGCTATGGCCACAGAAGAAATG
TCTAATCTGGTGAACTATATTCAGCCAGTCAAGTTTGAGTCATTTGAAATTTCAAAAAAA
AGAAATAAAAGTTTTGAAATGTCTTCCTTCGTGGAAACCAAAGGACTTGAACAACTCACC
AAGTCTCCAGTGGAATTTGTAGAATATAACAAAATGCAGCTTAGCAGGATATATCCAAAA
GGAACACGTGTGGATTCATCCAACTATATGCCTCAGCTCTTCTGGAATGCAGGTTGTCAG
ATGGTGGCACTTAATTTCCAGACAATGGACCTGGCTATGCAAATAAATATGGGGATGTAT
GAATACAACGGGAAGAGTGGCTACAGATTGAAGCCAGAGTTCATGAGGAGGCCTGACAAG
CATTTTGATCCATTTACTGAAGGCATCGTAGATGGGATAGTGGCAAACACTTTGTCTGTT
AAGATTATTTCAGGTCAGTTTCTTTCTGATAAGAAAGTTGGGACTTACGTGGAAGTAGAT
ATGTTTGGTTTGCCTGTGGATACAAGGAGGAAGGCATTTAAGACCAAAACATCCCAAGGA
AATGCTGTGAATCCTGTCTGGGAAGAAGAACCTATTGTGTTCAAAAAGGTGGTTCTTCCT
ACTCTGGCCTGTTTGAGAATAGCAGTTTATGAAGAAGGAGGTAAATTCATTGGCCACCGT
ATCTTGCCAGTGCAAGCCATTCGGCCAGGCTATCACTATATCTGTCTAAGGAATGAAAGG
AACCAGCCTCTGACGCTGCCTGCTGTCTTTGTCTACATAGAAGTGAAAGACTATGTGCCA
GACACATATGCAGATGTCATCGAAGCTTTATCAAACCCAATCCGATATGTGAACCTGATG
GAACAGAGAGCTAAGCAATTGGCTGCTTTGACACTGGAAGATGAAGAAGAAGTAAAGAAA
GAGGCTGATCCTGGAGAAACACCATCAGAGGCTCCAAGTGAAGCGAGAACGACTCCAGCA
GAAAATGGGGTGAATCACACTACAACCCTGACACCCAAGCCACCCTCCCAGGCTCTCCAC
AGCCAGCCAGCTCCAGGTTCTGTAAAGGCACCTGCCAAAACAGAAGATCTTATTCAGAGT
GTCTTAACAGAAGTGGAAGCACAGACCATCGAAGAACTAAAGCAACAGAAATCGTTTGTG
AAACTTCAAAAGAAACACTACAAAGAAATGAAAGACCTGGTTAAGAGACACCACAAGAAA
ACCACTGACCTTATCAAAGAACACACTACCAAGTATAATGAAATTCAGAATGACTACTTG
AGAAGGAGAGCCGCTTTGGAAAAGTCCGCCAAAAAGGACAGTAAGAAAAAATCGGAACCC
AGCAGCCCTGATCATGGTTCATCAACGATTGAGCAAGACCTCGCTGCTCTGGATGCTGAA
ATGACCCAAAAGTTAATAGACTTGAAGGACAAACAACAGCAGCAGCTGCTTAATCTTCGG
CAAGAACAGTATTATAGTGAAAAATACCAGAAGCGAGAACATATTAAACTGCTTATTCAA
AAGTTGACGGATGTCGCAGAAGAGTGTCAGAACAATCAGTTAAAGAAGCTCAAAGAAATC
TGTGAGAAAGAAAAGAAAGAATTAAAGAAGAAAATGGATAAAAAGAGGCAGGAGAAGATA
ACAGAAGCTAAATCCAAAGACAAAAGTCAGATGGAAGAGGAGAAGACAGAGATGATCCGG
TCATATATCCAGGAAGTGGTGCAGTATATCAAGAGGCTAGAAGAAGCGCAAAGTAAACGG
CAAGAAAAACTCGTAGAGAAACACAAGGAAATACGTCAGCAGATCCTGGATGAAAAGCCC
AAGCTGCAGGTGGAGCTGGAGCAAGAATACCAAGACAAATTCAAAAGACTGCCCCTCGAG
ATTTTGGAATTCGTGCAGGAAGCCATGAAAGGAAAGATCAGTGAAGACAGCAATCACGGT
TCTGCCCCTCTCTCCCTGTCCTCAGACCCTGGAAAAGTGAACCACAAGACTCCCTCCAGT
GAGGAGCTGGGAGGAGACATCCCAGGAAAAGAATTTGATACTCCTCTGTGA
|
| Enzyme 61 GenBank Gene ID |
NM_015192.2 |
| Enzyme 61 GeneCard ID |
PLCB1 |
| Enzyme 61 GenAtlas ID |
PLCB1 |
| Enzyme 61 HGNC ID |
HGNC:15917 |
| Enzyme 61 Chromosome Location |
2 |
| Enzyme 61 Locus |
20p12 |
| Enzyme 61 SNPs |
SNPJam Report |
| Enzyme 61 General References |
- Caricasole A, Sala C, Roncarati R, Formenti E, Terstappen GC: Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1). Biochim Biophys Acta. 2000 Dec 15;1517(1):63-72. [PubMed ]
- Peruzzi D, Calabrese G, Faenza I, Manzoli L, Matteucci A, Gianfrancesco F, Billi AM, Stuppia L, Palka G, Cocco L: Identification and chromosomal localisation by fluorescence in situ hybridisation of human gene of phosphoinositide-specific phospholipase C beta(1). Biochim Biophys Acta. 2000 Apr 12;1484(2-3):175-82. [PubMed ]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed ]
- Nakajima D, Okazaki N, Yamakawa H, Kikuno R, Ohara O, Nagase T: Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones. DNA Res. 2002 Jun 30;9(3):99-106. [PubMed ]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Tabellini G, Bortul R, Santi S, Riccio M, Baldini G, Cappellini A, Billi AM, Berezney R, Ruggeri A, Cocco L, Martelli AM: Diacylglycerol kinase-theta is localized in the speckle domains of the nucleus. Exp Cell Res. 2003 Jul 1;287(1):143-54. [PubMed ]
- Kim SC, Sprung R, Chen Y, Xu Y, Ball H, Pei J, Cheng T, Kho Y, Xiao H, Xiao L, Grishin NV, White M, Yang XJ, Zhao Y: Substrate and functional diversity of lysine acetylation revealed by a proteomics survey. Mol Cell. 2006 Aug;23(4):607-18. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 61 Metabolite References |
Not Available |
|
Enzyme 62
[top]
|
| Enzyme 62 ID |
5455 |
| Enzyme 62 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4 |
| Enzyme 62 Synonyms |
- Phosphoinositide phospholipase C-beta-4
- Phospholipase C-beta-4
- PLC-beta-4
|
| Enzyme 62 Gene Name |
PLCB4 |
| Enzyme 62 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-4
MAKPYEFNWQKEVPSFLQEGAVFDRYEEESFVFEPNCLFKVDEFGFFLTWRSEGKEGQVL
ECSLINSIRSGAIPKDPKILAALEAVGKSENDLEGRIVCVCSGTDLVNISFTYMVAENPE
VTKQWVEGLRSIIHNFRANNVSPMTCLKKHWMKLAFMTNTNGKIPVRSITRTFASGKTEK
VIFQALKELGLPSGKNDEIEPTAFSYEKFYELTQKICPRTDIEDLFKKINGDKTDYLTVD
QLVSFLNEHQRDPRLNEILFPFYDAKRAMQIIEMYEPDEDLKKKGLISSDGFCRYLMSDE
NAPVFLDRLELYQEMDHPLAHYFISSSHNTYLTGRQFGGKSSVEMYRQVLLAGCRCVELD
CWDGKGEDQEPIITHGKAMCTDILFKDVIQAIKETAFVTSEYPVILSFENHCSKYQQYKM
SKYCEDLFGDLLLKQALESHPLEPGRALPSPNDLKRKILIKNKRLKPEVEKKQLEALRSM
MEAGESASPANILEDDNEEEIESADQEEEAHPEFKFGNELSADDLGHKEAVANSVKKGLV
TVEDEQAWMASYKYVGATTNIHPYLSTMINYAQPVKFQGFHVAEERNIHYNMSSFNESVG
LGYLKTHAIEFVNYNKRQMSRIYPKGGRVDSSNYMPQIFWNAGCQMVSLNYQTPDLAMQL
NQGKFEYNGSCGYLLKPDFMRRPDRTFDPFSETPVDGVIAATCSVQVISGQFLSDKKIGT
YVEVDMYGLPTDTIRKEFRTRMVMNNGLNPVYNEESFVFRKVILPDLAVLRIAVYDDNNK
LIGQRILPLDGLQAGYRHISLRNEGNKPLSLPTIFCNIVLKTYVPDGFGDIVDALSDPKK
FLSITEKRADQMRAMGIETSDIADVPSDTSKNDKKGKANTAKANVTPQSSSELRPTTTAA
LASGVEAKKGIELIPQVRIEDLKQMKAYLKHLKKQQKELNSLKKKHAKEHSTMQKLHCTQ
VDKIVAQYDKEKSTHEKILEKAMKKKGGSNCLEMKKETEIKIQTLTSDHKSKVKEIVAQH
TKEWSEMINTHSAEEQEIRDLHLSQQCELLKKLLINAHEQQTQQLKLSHDRESKEMRAHQ
AKISMENSKAISQDKSIKNKAERERRVRELNSSNTKKFLEERKRLAMKQSKEMDQLKKVQ
LEHLEFLEKQNEQAKEMQQMVKLEAEMDRRPATVV
|
| Enzyme 62 Number of Residues |
1175 |
| Enzyme 62 Molecular Weight |
134462.6 |
| Enzyme 62 Theoretical pI |
6.90 |
| Enzyme 62 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 62 General Function |
Involved in calcium ion binding |
| Enzyme 62 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This form has a role in retina signal transduction |
| Enzyme 62 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 62 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 62 Pfam Domain Function |
|
| Enzyme 62 Signals |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
57284038 |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
Q15147 |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
PLCB4_HUMAN |
| Enzyme 62 PDB ID |
Not Available |
| Enzyme 62 Cellular Location |
Not Available |
| Enzyme 62 Gene Sequence |
>3528 bp
ATGGCCAAACCTTATGAATTTAACTGGCAGAAGGAAGTTCCCTCCTTTTTGCAAGAAGGA
GCAGTTTTTGACAGATACGAGGAGGAATCCTTTGTGTTTGAACCCAACTGCCTCTTCAAA
GTGGATGAGTTTGGCTTCTTTCTGACATGGAGAAGTGAAGGCAAGGAAGGACAGGTGCTA
GAATGCTCCCTCATCAACAGTATTCGGTCGGGAGCCATACCAAAGGATCCCAAAATCTTG
GCTGCTCTTGAAGCTGTTGGAAAATCAGAAAATGATCTGGAAGGGCGGATAGTTTGTGTC
TGCAGTGGCACAGATCTAGTGAACATTAGTTTTACCTACATGGTGGCTGAAAATCCAGAA
GTAACTAAGCAATGGGTAGAAGGCCTGAGATCAATCATACACAACTTCAGGGCCAACAAC
GTCAGTCCAATGACATGCCTCAAGAAACACTGGATGAAATTGGCATTTATGACCAACACA
AATGGTAAAATTCCAGTTAGGAGTATTACTAGAACATTTGCATCGGGAAAAACAGAAAAG
GTGATCTTTCAAGCACTCAAGGAGTTAGGTCTTCCCAGTGGAAAGAATGATGAAATTGAG
CCCACAGCATTTTCTTATGAAAAGTTCTATGAACTGACACAAAAGATTTGTCCTCGGACA
GATATAGAAGATCTTTTCAAAAAAATCAATGGAGACAAAACTGATTATTTAACGGTAGAC
CAATTAGTGAGCTTTCTAAATGAACATCAACGAGATCCTCGATTGAATGAAATTTTATTT
CCATTTTATGATGCCAAAAGGGCAATGCAGATCATTGAGATGTATGAACCTGATGAAGAT
TTGAAGAAAAAAGGCCTTATATCAAGTGATGGGTTTTGCAGATATCTGATGTCAGATGAA
AACGCCCCAGTCTTCCTAGATCGTTTAGAACTTTACCAAGAAATGGACCATCCTCTGGCT
CACTACTTCATCAGTTCTTCCCATAACACTTATCTCACTGGCAGACAGTTCGGCGGGAAG
TCTTCGGTAGAAATGTACAGACAGGTTCTCCTGGCTGGTTGCAGATGTGTTGAACTTGAC
TGCTGGGATGGAAAAGGTGAAGACCAAGAACCAATAATAACTCATGGAAAAGCAATGTGT
ACAGATATCCTTTTTAAGGATGTAATTCAAGCCATCAAGGAAACTGCATTTGTCACATCA
GAATATCCTGTAATTCTCTCCTTTGAAAATCACTGCAGCAAATATCAACAGTACAAGATG
TCCAAATATTGCGAAGATCTATTTGGGGATCTCCTGTTGAAACAAGCACTTGAATCACAT
CCACTTGAACCAGGCAGGGCTTTGCCATCCCCCAATGACCTCAAAAGAAAAATACTCATA
AAAAACAAGCGGCTGAAACCTGAAGTTGAAAAAAAACAGCTGGAAGCTTTGAGAAGCATG
ATGGAAGCTGGAGAATCTGCCTCCCCAGCAAACATCTTAGAGGACGATAATGAAGAGGAG
ATCGAAAGTGCTGACCAAGAGGAGGAAGCTCACCCCGAATTCAAATTTGGAAATGAACTT
TCTGCTGATGACTTGGGTCACAAGGAAGCTGTTGCAAATAGCGTCAAGAAGGGCCTGGTC
ACTGTAGAAGATGAGCAGGCGTGGATGGCATCTTATAAATATGTAGGTGCTACCACTAAT
ATCCATCCATATTTGTCCACAATGATCAACTACGCCCAGCCTGTAAAGTTTCAAGGTTTC
CATGTGGCAGAAGAACGCAATATTCATTATAACATGTCTTCTTTTAATGAATCAGTCGGT
CTTGGCTACTTGAAGACACATGCAATTGAATTTGTCAATTATAACAAACGGCAAATGAGT
CGCATTTACCCCAAGGGAGGCCGAGTCGATTCCAGTAATTACATGCCTCAGATTTTCTGG
AACGCTGGCTGCCAGATGGTTTCACTGAACTATCAAACCCCAGATTTAGCGATGCAATTG
AATCAGGGAAAATTTGAGTATAATGGATCGTGCGGGTACCTTCTCAAACCAGATTTCATG
AGGCGGCCTGATCGAACATTTGACCCCTTCTCTGAAACTCCTGTTGATGGTGTTATTGCA
GCCACTTGCTCAGTGCAGGTTATATCAGGTCAATTCTTATCAGATAAGAAAATTGGCACC
TACGTAGAGGTGGATATGTATGGGTTGCCCACTGACACCATACGTAAGGAATTCCGAACT
CGCATGGTTATGAATAATGGACTCAATCCAGTTTACAATGAAGAGTCATTTGTATTTCGG
AAGGTGATCCTGCCGGACCTGGCTGTCTTGAGAATAGCTGTGTATGATGATAACAACAAG
CTGATTGGCCAGAGGATCCTCCCGCTTGATGGCCTCCAAGCCGGATATCGACACATTTCC
CTTCGAAATGAGGGAAATAAACCATTATCACTACCAACAATTTTCTGCAATATTGTTCTT
AAAACATATGTGCCTGATGGATTTGGAGATATCGTGGATGCTTTATCAGATCCAAAGAAA
TTTCTCTCAATTACAGAAAAGAGAGCAGACCAAATGAGAGCTATGGGCATTGAAACTAGT
GACATAGCCGACGTGCCCAGTGACACTTCCAAAAATGACAAGAAAGGAAAGGCCAACACC
GCCAAAGCAAATGTGACCCCTCAGAGTAGCTCTGAGCTCAGACCAACCACCACGGCTGCC
CTGGCCTCTGGTGTGGAAGCCAAGAAAGGTATTGAACTTATCCCTCAAGTAAGGATAGAA
GACTTAAAGCAGATGAAGGCTTACTTGAAGCATTTAAAGAAACAGCAGAAGGAGCTAAAT
TCTTTAAAGAAGAAACATGCAAAGGAACACAGTACCATGCAGAAGTTACACTGCACGCAA
GTTGACAAAATTGTGGCACAGTATGACAAAGAGAAGTCGACTCATGAGAAAATCCTAGAG
AAGGCAATGAAGAAGAAGGGGGGAAGTAATTGTCTCGAAATGAAAAAAGAAACAGAAATC
AAAATTCAGACGCTGACATCAGATCACAAATCTAAGGTCAAAGAGATTGTAGCACAGCAC
ACAAAGGAATGGTCAGAAATGATCAATACCCACAGTGCTGAGGAGCAAGAAATCCGAGAC
CTGCACCTCAGCCAGCAGTGTGAGCTGCTGAAAAAGCTACTCATCAATGCCCACGAGCAG
CAAACCCAGCAGCTGAAACTGTCCCATGACAGGGAAAGCAAGGAAATGCGAGCACACCAG
GCTAAGATTTCTATGGAAAATAGCAAAGCCATCAGCCAAGATAAATCTATCAAGAATAAA
GCAGAACGGGAAAGGCGAGTCAGGGAGTTAAACAGCAGCAACACTAAAAAGTTTCTGGAA
GAAAGAAAGAGACTTGCCATGAAGCAGTCCAAAGAAATGGATCAGTTGAAAAAAGTCCAG
CTTGAACATCTAGAATTCCTAGAGAAACAGAATGAGCAGGCGAAGGAGATGCAGCAGATG
GTGAAATTGGAAGCCGAGATGGACCGCAGACCAGCAACAGTAGTATGA
|
| Enzyme 62 GenBank Gene ID |
AL023805 |
| Enzyme 62 GeneCard ID |
PLCB4 |
| Enzyme 62 GenAtlas ID |
PLCB4 |
| Enzyme 62 HGNC ID |
HGNC:9059 |
| Enzyme 62 Chromosome Location |
2 |
| Enzyme 62 Locus |
20p12 |
| Enzyme 62 SNPs |
SNPJam Report |
| Enzyme 62 General References |
- Alvarez RA, Ghalayini AJ, Xu P, Hardcastle A, Bhattacharya S, Rao PN, Pettenati MJ, Anderson RE, Baehr W: cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4). Genomics. 1995 Sep 1;29(1):53-61. [PubMed ]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed ]
|
| Enzyme 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
5456 |
| Enzyme 63 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2 |
| Enzyme 63 Synonyms |
- Phosphoinositide phospholipase C-beta-2
- Phospholipase C-beta-2
- PLC-beta-2
|
| Enzyme 63 Gene Name |
PLCB2 |
| Enzyme 63 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-2
MSLLNPVLLPPKVKAYLSQGERFIKWDDETTVASPVILRVDPKGYYLYWTYQSKEMEFLD
ITSIRDTRFGKFAKMPKSQKLRDVFNMDFPDNSFLLKTLTVVSGPDMVDLTFHNFVSYKE
NVGKAWAEDVLALVKHPLTANASRSTFLDKILVKLKMQLNSEGKIPVKNFFQMFPADRKR
VEAALSACHLPKGKNDAINPEDFPEPVYKSFLMSLCPRPEIDEIFTSYHAKAKPYMTKEH
LTKFINQKQRDSRLNSLLFPPARPDQVQGLIDKYEPSGINAQRGQLSPEGMVWFLCGPEN
SVLAQDKLLLHHDMTQPLNHYFINSSHNTYLTAGQFSGLSSAEMYRQVLLSGCRCVELDC
WKGKPPDEEPIITHGFTMTTDIFFKEAIEAIAESAFKTSPYPIILSFENHVDSPRQQAKM
AEYCRTIFGDMLLTEPLEKFPLKPGVPLPSPEDLRGKILIKNKKNQFSGPTSSSKDTGGE
AEGSSPPSAPAGEGTVWAGEEGTELEEEEVEEEEEEESGNLDEEEIKKMQSDEGTAGLEV
TAYEEMSSLVNYIQPTKFVSFEFSAQKNRSYVISSFTELKAYDLLSKASVQFVDYNKRQM
SRIYPKGTRMDSSNYMPQMFWNAGCQMVALNFQTMDLPMQQNMAVFEFNGQSGYLLKHEF
MRRPDKQFNPFSVDRIDVVVATTLSITVISGQFLSERSVRTYVEVELFGLPGDPKRRYRT
KLSPSTNSINPVWKEEPFVFEKILMPELASLRVAVMEEGNKFLGHRIIPINALNSGYHHL
CLHSESNMPLTMPALFIFLEMKDYIPGAWADLTVALANPIKFFSAHDTKSVKLKEAMGGL
PEKPFPLASPVASQVNGALAPTSNGSPAARAGAREEAMKEAAEPRTASLEELRELKGVVK
LQRRHEKELRELERRGARRWEELLQRGAAQLAELGPPGVGGVGACKLGPGKGSRKKRSLP
REESAGAAPGEGPEGVDGRVRELKDRLELELLRQGEEQYECVLKRKEQHVAEQISKMMEL
AREKQAAELKALKETSENDTKEMKKKLETKRLERIQGMTKVTTDKMAQERLKREINNSHI
QEVVQVIKQMTENLERHQEKLEEKQAACLEQIREMEKQFQKEALAEYEARMKGLEAEVKE
SVRACLRTCFPSEAKDKPERACECPPELCEQDPLIAKADAQESRL
|
| Enzyme 63 Number of Residues |
1185 |
| Enzyme 63 Molecular Weight |
134023.2 |
| Enzyme 63 Theoretical pI |
6.21 |
| Enzyme 63 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid catabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 63 General Function |
Involved in calcium ion binding |
| Enzyme 63 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes |
| Enzyme 63 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 63 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 63 Pfam Domain Function |
|
| Enzyme 63 Signals |
|
| Enzyme 63 Transmembrane Regions |
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
95147333 |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
Q00722 |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
PLCB2_HUMAN |
| Enzyme 63 PDB ID |
Not Available |
| Enzyme 63 Cellular Location |
Not Available |
| Enzyme 63 Gene Sequence |
>3558 bp
ATGTCTCTGCTCAACCCTGTCCTGCTGCCCCCCAAGGTGAAGGCCTATCTGAGCCAAGGG
GAGCGCTTCATCAAATGGGATGATGAAACTACAGTTGCCTCTCCAGTTATCCTCCGTGTG
GATCCTAAGGGCTACTACTTATACTGGACGTATCAAAGTAAGGAGATGGAGTTTCTGGAT
ATCACCAGCATCCGGGATACTCGCTTTGGGAAGTTTGCCAAGATGCCCAAGAGCCAGAAG
CTCCGGGACGTCTTCAACATGGACTTTCCTGATAACAGTTTCCTGCTGAAGACACTCACG
GTGGTGTCCGGCCCGGACATGGTGGACCTCACCTTCCACAACTTCGTCTCCTACAAGGAG
AACGTGGGCAAGGCCTGGGCTGAGGACGTACTGGCCCTAGTCAAACATCCGCTGACGGCC
AACGCCTCCCGCAGCACCTTCCTGGACAAGATCCTTGTGAAGCTCAAGATGCAGCTCAAC
TCTGAAGGGAAGATTCCGGTGAAGAACTTTTTCCAGATGTTTCCTGCTGACCGCAAGCGG
GTGGAAGCTGCTCTCAGTGCCTGCCACCTCCCCAAAGGCAAAAATGACGCCATCAATCCT
GAGGACTTCCCAGAACCTGTCTACAAGAGTTTCCTCATGAGCCTCTGTCCTCGGCCAGAA
ATAGATGAGATCTTCACTTCTTACCATGCTAAGGCCAAACCCTACATGACGAAGGAGCAC
CTGACCAAATTCATCAACCAGAAACAGCGGGACTCCCGGCTTAACTCCCTGCTGTTCCCG
CCAGCACGGCCTGACCAGGTGCAGGGCCTCATCGACAAGTATGAGCCCAGTGGCATCAAT
GCACAGAGGGGCCAGCTGTCACCTGAAGGCATGGTCTGGTTTCTCTGTGGGCCAGAGAAC
AGCGTGCTGGCCCAGGACAAGCTGCTGCTCCACCACGACATGACGCAGCCACTCAATCAT
TACTTCATCAACTCGTCCCACAACACCTACCTGACAGCCGGCCAGTTCTCAGGCCTCTCC
TCGGCTGAGATGTACCGCCAGGTGCTGCTCTCTGGCTGCCGTTGCGTGGAGCTAGACTGC
TGGAAGGGGAAACCCCCTGACGAGGAGCCCATTATCACCCATGGCTTCACCATGACCACA
GACATCTTCTTCAAAGAAGCAATTGAGGCTATTGCAGAAAGCGCCTTTAAGACCTCCCCC
TATCCCATCATCCTGTCGTTTGAGAACCATGTGGACTCACCCCGCCAGCAGGCTAAGATG
GCTGAGTATTGCCGGACGATCTTTGGGGATATGCTGCTCACAGAGCCCCTGGAAAAGTTC
CCACTAAAACCAGGTGTCCCCCTGCCCAGCCCTGAGGATCTCAGGGGCAAGATCCTCATC
AAGAACAAGAAGAACCAGTTTTCTGGCCCCACCTCCTCCAGTAAGGATACTGGTGGGGAG
GCTGAGGGCAGCAGCCCACCCAGTGCCCCTGCAGGTGAGGGCACAGTGTGGGCTGGCGAG
GAAGGGACTGAGCTGGAGGAGGAGGAGGTGGAAGAGGAAGAGGAGGAGGAGTCAGGAAAC
CTGGATGAAGAAGAGATTAAGAAGATGCAGTCGGATGAGGGCACAGCGGGCCTGGAAGTG
ACGGCTTATGAGGAGATGTCCAGCCTAGTCAATTACATCCAGCCCACCAAGTTCGTCTCC
TTTGAGTTCTCTGCCCAAAAGAACCGAAGTTATGTCATCTCGTCCTTCACAGAGCTCAAG
GCATATGACCTGCTCTCCAAGGCCTCGGTGCAGTTTGTGGACTACAACAAGCGCCAGATG
AGCCGCATTTACCCCAAGGGAACCCGCATGGACTCCTCCAACTACATGCCCCAGATGTTC
TGGAATGCTGGATGCCAGATGGTTGCCCTCAACTTCCAGACGATGGACTTGCCCATGCAG
CAGAACATGGCAGTATTTGAGTTCAACGGGCAGAGCGGCTACCTCCTCAAGCATGAGTTC
ATGCGCCGGCCGGACAAGCAGTTCAACCCCTTCTCAGTGGACCGCATCGACGTGGTGGTG
GCCACCACCCTTTCCATTACGGTGATCTCTGGGCAGTTCCTGTCAGAACGCAGCGTGCGC
ACCTATGTAGAAGTGGAGCTGTTTGGCCTTCCTGGGGACCCCAAGAGGCGCTATCGAACT
AAGCTGTCACCCAGTACTAACTCCATCAATCCTGTCTGGAAGGAGGAGCCCTTTGTCTTT
GAGAAGATCTTGATGCCTGAGCTGGCCTCCCTCAGAGTGGCTGTGATGGAGGAAGGCAAC
AAGTTTCTTGGACACCGCATCATCCCCATCAATGCCCTAAATTCTGGGTACCACCACCTG
TGCCTGCACAGTGAGAGCAACATGCCCCTCACCATGCCTGCGCTCTTCATCTTCCTGGAG
ATGAAGGACTACATACCTGGTGCTTGGGCAGATCTCACTGTGGCCCTCGCCAACCCCATT
AAGTTCTTCAGTGCCCATGACACGAAGTCTGTGAAGCTCAAGGAGGCCATGGGAGGTCTG
CCTGAGAAGCCCTTCCCACTGGCGAGTCCAGTTGCCAGCCAGGTCAATGGGGCGTTGGCC
CCAACGAGCAATGGGTCACCAGCAGCCAGGGCCGGGGCCAGGGAAGAGGCTATGAAAGAA
GCTGCGGAGCCGCGGACCGCCAGCCTGGAGGAGCTCCGGGAGCTAAAGGGCGTGGTGAAG
CTGCAGCGGCGGCACGAGAAGGAGCTGCGAGAGTTGGAGCGGCGCGGAGCGCGGCGCTGG
GAGGAGCTGCTGCAGCGGGGCGCGGCGCAGCTGGCGGAGCTCGGGCCACCGGGCGTGGGG
GGCGTCGGGGCCTGCAAGCTCGGTCCCGGCAAGGGCTCTCGCAAGAAGAGGAGCCTGCCC
CGCGAGGAGAGCGCCGGAGCCGCGCCGGGCGAGGGCCCTGAGGGCGTGGACGGGCGCGTG
CGGGAGCTGAAAGACAGGCTGGAGCTGGAGCTGCTGCGGCAGGGCGAGGAGCAGTACGAG
TGCGTTCTGAAGCGCAAGGAGCAGCACGTGGCCGAGCAAATCTCCAAAATGATGGAGCTG
GCCAGAGAGAAACAGGCGGCAGAGCTGAAGGCCCTGAAGGAGACGTCGGAGAACGACACC
AAAGAGATGAAGAAAAAGCTGGAGACAAAGAGACTGGAGCGGATCCAGGGCATGACCAAA
GTCACCACAGACAAGATGGCCCAGGAGAGGTTGAAGAGAGAGATTAACAACTCCCACATC
CAGGAAGTAGTGCAGGTGATCAAGCAGATGACGGAGAACTTGGAGAGGCACCAGGAGAAG
CTGGAGGAGAAGCAGGCGGCTTGCCTGGAACAGATACGGGAGATGGAAAAGCAGTTCCAG
AAGGAGGCGCTGGCAGAGTACGAGGCCAGGATGAAGGGTCTGGAGGCAGAGGTGAAGGAG
TCGGTGAGGGCCTGCCTCAGGACCTGCTTTCCCTCCGAGGCCAAGGACAAGCCTGAGAGG
GCCTGCGAGTGCCCCCCAGAGCTGTGTGAGCAGGACCCACTCATAGCAAAGGCAGATGCC
CAGGAGAGCCGCCTCTGA
|
| Enzyme 63 GenBank Gene ID |
NM_004573.2 |
| Enzyme 63 GeneCard ID |
PLCB2 |
| Enzyme 63 GenAtlas ID |
PLCB2 |
| Enzyme 63 HGNC ID |
HGNC:9055 |
| Enzyme 63 Chromosome Location |
1 |
| Enzyme 63 Locus |
15q15 |
| Enzyme 63 SNPs |
SNPJam Report |
| Enzyme 63 General References |
- Park D, Jhon DY, Kriz R, Knopf J, Rhee SG: Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2. J Biol Chem. 1992 Aug 15;267(23):16048-55. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed ]
- Jezyk MR, Snyder JT, Gershberg S, Worthylake DK, Harden TK, Sondek J: Crystal structure of Rac1 bound to its effector phospholipase C-beta2. Nat Struct Mol Biol. 2006 Dec;13(12):1135-40. Epub 2006 Nov 19. [PubMed ]
|
| Enzyme 63 Metabolite References |
Not Available |
|
Enzyme 64
[top]
|
| Enzyme 64 ID |
5458 |
| Enzyme 64 Name |
Hepatic triacylglycerol lipase |
| Enzyme 64 Synonyms |
- HL
- Hepatic lipase
- Lipase member C
|
| Enzyme 64 Gene Name |
LIPC |
| Enzyme 64 Protein Sequence |
>Hepatic triacylglycerol lipase
MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ
GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLV
DWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSS
IGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGH
YDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY
PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQLKIQF
INQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKW
ENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQ
EKIFVKCEIKSKTSKRKIR
|
| Enzyme 64 Number of Residues |
499 |
| Enzyme 64 Molecular Weight |
55880.1 |
| Enzyme 64 Theoretical pI |
9.37 |
| Enzyme 64 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 64 General Function |
Involved in catalytic activity |
| Enzyme 64 Specific Function |
Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin |
| Enzyme 64 Pathways |
|
| Enzyme 64 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 64 Pfam Domain Function |
|
| Enzyme 64 Signals |
|
| Enzyme 64 Transmembrane Regions |
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
194097335 |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
P11150 |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
LIPC_HUMAN |
| Enzyme 64 PDB ID |
Not Available |
| Enzyme 64 Cellular Location |
Not Available |
| Enzyme 64 Gene Sequence |
>1500 bp
ATGGACACAAGTCCCCTGTGTTTCTCCATTCTGTTGGTTTTATGCATCTTTATCCAATCA
AGTGCCCTTGGACAAAGCCTGAAACCAGAGCCATTTGGAAGAAGAGCTCAAGCTGTTGAA
ACAAACAAAACGCTGCATGAGATGAAGACCAGATTCCTGCTCTTTGGAGAAACCAATCAG
GGCTGTCAGATTCGAATCAATCATCCGGACACGTTACAGGAGTGCGGCTTCAACTCCTCC
CTGCCTCTGGTGATGATAATCCACGGGTGGTCGGTGGACGGCGTGCTAGAAAACTGGATC
TGGCAGATGGTGGCCGCGCTGAAGTCTCAGCCGGCCCAGCCAGTGAACGTGGGGCTGGTG
GACTGGATCACCCTGGCCCACGACCACTACACCATCGCCGTCCGCAACACCCGCCTTGTG
GGCAAGGAGGTCGCGGCTCTTCTCCGGTGGCTGGAGGAATCTGTGCAACTCTCTCGAAGC
CATGTTCACCTAATTGGGTACAGCCTGGGTGCACACGTGTCAGGATTTGCCGGCAGTTCC
ATCGGTGGAACGCACAAGATTGGGAGAATCACAGGGCTGGATGCCGCGGGACCTTTGTTT
GAGGGAAGTGCCCCCAGCAATCGTCTTTCTCCAGATGATGCCAATTTTGTGGATGCCATT
CATACCTTTACCCGGGAGCACATGGGCCTGAGCGTGGGCATCAAACAGCCCATAGGACAC
TATGACTTCTATCCCAACGGGGGCTCCTTCCAGCCTGGCTGCCACTTCCTAGAGCTCTAC
AGACATATTGCCCAGCACGGCTTCAATGCCATCACCCAGACCATAAAATGCTCCCACGAG
CGATCGGTGCACCTTTTCATCGACTCCTTGCTGCACGCCGGCACGCAGAGCATGGCCTAC
CCGTGTGGTGACATGAACAGCTTCAGCCAGGGCCTGTGCCTGAGCTGCAAGAAGGGCCGC
TGCAACACGCTGGGCTACCACGTCCGCCAGGAGCCGCGGAGCAAGAGCAAGAGGCTCTTC
CTCGTAACGCGAGCCCAGTCCCCCTTCAAAGTTTATCATTACCAGTTCAAGATCCAGTTC
ATCAACCAAACTGAGACACCAATACAAACAACTTTTACCATGTCACTACTCGGAACAAAA
GAGAAAATGCAGAAAATTCCCATCACTCTGGGCAAAGGAATTGCTAGTAATAAAACGTAT
TCCTTTCTTATCACGCTGGATGTGGATATCGGCGAGCTGATCATGATCAAGTTCAAGTGG
GAAAACAGTGCAGTGTGGGCCAATGTCTGGGACACGGTCCAGACCATCATCCCATGGAGC
ACAGGGCCGCGCCACTCAGGCCTCGTTCTGAAGACGATCAGAGTCAAAGCAGGAGAAACC
CAGCAAAGAATGACATTTTGTTCAGAAAACACAGATGACCTACTACTTCGCCCAACCCAG
GAAAAAATCTTCGTGAAATGTGAAATAAAGTCTAAAACATCAAAGCGAAAGATCAGATGA
|
| Enzyme 64 GenBank Gene ID |
NM_000236.2 |
| Enzyme 64 GeneCard ID |
LIPC |
| Enzyme 64 GenAtlas ID |
LIPC |
| Enzyme 64 HGNC ID |
HGNC:6619 |
| Enzyme 64 Chromosome Location |
1 |
| Enzyme 64 Locus |
15q21-q23 |
| Enzyme 64 SNPs |
SNPJam Report |
| Enzyme 64 General References |
- Martin GA, Busch SJ, Meredith GD, Cardin AD, Blankenship DT, Mao SJ, Rechtin AE, Woods CW, Racke MM, Schafer MP, et al.: Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase. J Biol Chem. 1988 Aug 5;263(22):10907-14. [PubMed ]
- Stahnke G, Sprengel R, Augustin J, Will H: Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line. Differentiation. 1987;35(1):45-52. [PubMed ]
- Datta S, Luo CC, Li WH, VanTuinen P, Ledbetter DH, Brown MA, Chen SH, Liu SW, Chan L: Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase. J Biol Chem. 1988 Jan 25;263(3):1107-10. [PubMed ]
- Cai SJ, Wong DM, Chen SH, Chan L: Structure of the human hepatic triglyceride lipase gene. Biochemistry. 1989 Nov 14;28(23):8966-71. [PubMed ]
- Ameis D, Stahnke G, Kobayashi J, McLean J, Lee G, Buscher M, Schotz MC, Will H: Isolation and characterization of the human hepatic lipase gene. J Biol Chem. 1990 Apr 25;265(12):6552-5. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Tiebel O, Gehrisch S, Pietzsch J, Gromeier S, Jaross W: 18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3. Mutations in brief no. 181. Online. Hum Mutat. 1998;12(3):216. [PubMed ]
- Takagi A, Ikeda Y, Mori A, Ashida Y, Yamamoto A: Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene. Mol Cell Probes. 1996 Aug;10(4):313-4. [PubMed ]
- Todorova B, Kubaszek A, Pihlajamaki J, Lindstrom J, Eriksson J, Valle TT, Hamalainen H, Ilanne-Parikka P, Keinanen-Kiukaanniemi S, Tuomilehto J, Uusitupa M, Laakso M: The G-250A promoter polymorphism of the hepatic lipase gene predicts the conversion from impaired glucose tolerance to type 2 diabetes mellitus: the Finnish Diabetes Prevention Study. J Clin Endocrinol Metab. 2004 May;89(5):2019-23. [PubMed ]
- Grarup N, Andreasen CH, Andersen MK, Albrechtsen A, Sandbaek A, Lauritzen T, Borch-Johnsen K, Jorgensen T, Schmitz O, Hansen T, Pedersen O: The -250G>A promoter variant in hepatic lipase associates with elevated fasting serum high-density lipoprotein cholesterol modulated by interaction with physical activity in a study of 16,156 Danish subjects. J Clin Endocrinol Metab. 2008 Jun;93(6):2294-9. Epub 2008 Mar 25. [PubMed ]
- Hegele RA, Tu L, Connelly PW: Human hepatic lipase mutations and polymorphisms. Hum Mutat. 1992;1(4):320-4. [PubMed ]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed ]
|
| Enzyme 64 Metabolite References |
Not Available |
|
Enzyme 65
[top]
|
| Enzyme 65 ID |
5459 |
| Enzyme 65 Name |
Lysosomal acid lipase/cholesteryl ester hydrolase |
| Enzyme 65 Synonyms |
- Acid cholesteryl ester hydrolase
- LAL
- Cholesteryl esterase
- Lipase A
- Sterol esterase
|
| Enzyme 65 Gene Name |
LIPA |
| Enzyme 65 Protein Sequence |
>Lysosomal acid lipase/cholesteryl ester hydrolase
MKMRFLGLVVCLVLWTLHSEGSGGKLTAVDPETNMNVSEIISYWGFPSEEYLVETEDGYI
LCLNRIPHGRKNHSDKGPKPVVFLQHGLLADSSNWVTNLANSSLGFILADAGFDVWMGNS
RGNTWSRKHKTLSVSQDEFWAFSYDEMAKYDLPASINFILNKTGQEQVYYVGHSQGTTIG
FIAFSQIPELAKRIKMFFALGPVASVAFCTSPMAKLGRLPDHLIKDLFGDKEFLPQSAFL
KWLGTHVCTHVILKELCGNLCFLLCGFNERNLNMSRVDVYTTHSPAGTSVQNMLHWSQAV
KFQKFQAFDWGSSAKNYFHYNQSYPPTYNVKDMLVPTAVWSGGHDWLADVYDVNILLTQI
TNLVFHESIPEWEHLDFIWGLDAPWRLYNKIINLMRKYQ
|
| Enzyme 65 Number of Residues |
399 |
| Enzyme 65 Molecular Weight |
45418.7 |
| Enzyme 65 Theoretical pI |
6.91 |
| Enzyme 65 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 65 General Function |
Involved in lipid metabolic process |
| Enzyme 65 Specific Function |
Crucial for the intracellular hydrolysis of cholesteryl esters and triglycerides that have been internalized via receptor- mediated endocytosis of lipoprotein particles. Important in mediating the effect of LDL (low density lipoprotein) uptake on suppression of hydroxymethylglutaryl-CoA reductase and activation of endogenous cellular cholesteryl ester formation |
| Enzyme 65 Pathways |
|
| Enzyme 65 Reactions |
- a steryl ester + H2O = a sterol + a fatty acid [RN:R02115]
|
| Enzyme 65 Pfam Domain Function |
|
| Enzyme 65 Signals |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
62897079 |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
P38571 |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
LICH_HUMAN |
| Enzyme 65 PDB ID |
Not Available |
| Enzyme 65 Cellular Location |
Not Available |
| Enzyme 65 Gene Sequence |
>1200 bp
ATGAAAATGCGGTTCTTGGGGTTGGTGGTCTGTTTGGTTCTCTGGACCCTGCATTCTGAG
GGGTCTGGAGGGAAACTGACAGCTGTGGATCCTGAAACAAACATGAATGTGAGTGAAATT
ATCTCTTACTGGGGATTCCCTAGTGAGGAATACCTAGTTGAGACAGAAGATGGATATATT
CTGTGCCTTAACCGAATTCCTCATGGGAGGAAGAACCATTCTGACAAAGGTCCCAAACCA
GTTGTCTTCCTGCAACATGGCTTGCTGGCAGATTCTAGTAACTGGGTCACAAACCTTGCC
AACAGCAGCCTGGGCTTCATTCTTGCTGATGCTGGTTTTGACGTGTGGATGGGCAACAGC
AGAGGAAATACCTGGTCTCGGAAACATAAGACACTCTCAGTTTCTCAGGATGAATTCTGG
GCTTTCAGTTATGATGAGATGGCAAAATATGACCTACCAGCTTCCATTAACTTCATTCTG
AATAAAACTGGCCAAGAACAAGTGTATTATGTGGGTCATTCTCAAGGCACCACTATAGGT
TTTATAGCATTTTCACAGATCCCTGAGCTGGCTAAAAGGATTAAAATGTTTTTTGCCCTG
GGTCCTGTGGCTTCCGTCGCCTTCTGTACTAGCCCTATGGCCAAATTAGGACGATTACCA
GATCATCTCATTAAGGACTTATTTGGAGACAAAGAATTTCTTCCCCAGAGTGCGTTTTTG
AAGTGGCTGGGTACCCACGTTTGCACTCATGTCATACTGAAGGAGCTCTGTGGAAATCTC
TGTTTTCTTCTGTGTGGATTTAATGAGAGAAATTTAAATATGTCTAGAGTGGATGTATAT
ACAACACATTCTCCTGCTGGAACTTCTGTGCAAAACATGTTACACTGGAGCCAGGCTGTT
AAATTCCAAAAGTTTCAAGCCTTTGACTGGGGAAGCAGTGCCAAGAATTATTTTCATTAC
AACCAGAGTTATCCTCCCACATACAATGTGAAGGACATGCTTGTGCCGACTGCAGTCTGG
AGCGGGGGTCACGACTGGCTTGCAGATGTCTACGACGTCAATATCTTACTGACTCAGATC
ACCAACTTGGTGTTCCATGAGAGCATTCCGGAATGGGAGCATCTTGACTTCATTTGGGGC
CTGGATGCCCCTTGGAGGCTTTATAATAAAATTATTAATCTAATGAGGAGATATCAGTGA
|
| Enzyme 65 GenBank Gene ID |
AK222760 |
| Enzyme 65 GeneCard ID |
LIPA |
| Enzyme 65 GenAtlas ID |
LIPA |
| Enzyme 65 HGNC ID |
HGNC:6617 |
| Enzyme 65 Chromosome Location |
1 |
| Enzyme 65 Locus |
10q23.2-q23.3 |
| Enzyme 65 SNPs |
SNPJam Report |
| Enzyme 65 General References |
- Anderson RA, Sando GN: Cloning and expression of cDNA encoding human lysosomal acid lipase/cholesteryl ester hydrolase. Similarities to gastric and lingual lipases. J Biol Chem. 1991 Nov 25;266(33):22479-84. [PubMed ]
- Ameis D, Merkel M, Eckerskorn C, Greten H: Purification, characterization and molecular cloning of human hepatic lysosomal acid lipase. Eur J Biochem. 1994 Feb 1;219(3):905-14. [PubMed ]
- Du H, Witte DP, Grabowski GA: Tissue and cellular specific expression of murine lysosomal acid lipase mRNA and protein. J Lipid Res. 1996 May;37(5):937-49. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
- Anderson RA, Byrum RS, Coates PM, Sando GN: Mutations at the lysosomal acid cholesteryl ester hydrolase gene locus in Wolman disease. Proc Natl Acad Sci U S A. 1994 Mar 29;91(7):2718-22. [PubMed ]
- Ries S, Buchler C, Schindler G, Aslanidis C, Ameis D, Gasche C, Jung N, Schambach A, Fehringer P, Vanier MT, Belli DC, Greten H, Schmitz G: Different missense mutations in histidine-108 of lysosomal acid lipase cause cholesteryl ester storage disease in unrelated compound heterozygous and hemizygous individuals. Hum Mutat. 1998;12(1):44-51. [PubMed ]
|
| Enzyme 65 Metabolite References |
Not Available |
|
Enzyme 66
[top]
|
| Enzyme 66 ID |
5460 |
| Enzyme 66 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3 |
| Enzyme 66 Synonyms |
- Phosphoinositide phospholipase C-beta-3
- Phospholipase C-beta-3
- PLC-beta-3
|
| Enzyme 66 Gene Name |
PLCB3 |
| Enzyme 66 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta-3
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNME
VDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNF
MAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFS
ADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPY
LTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYL
GGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRC
VELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAK
QQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDS
AGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGD
EGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPV
KFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYM
PQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIV
DGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEP
FDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLI
YTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQL
GSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGH
KALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVED
TKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQF
KRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLE
EAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLG
DGPLVACASNGHAPGSSGHLSGADSESQEENTQL
|
| Enzyme 66 Number of Residues |
1234 |
| Enzyme 66 Molecular Weight |
138797.7 |
| Enzyme 66 Theoretical pI |
5.66 |
| Enzyme 66 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid catabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 66 General Function |
Involved in calcium ion binding |
| Enzyme 66 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes |
| Enzyme 66 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 66 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 66 Pfam Domain Function |
|
| Enzyme 66 Signals |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
148745659 |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
Q01970 |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
PLCB3_HUMAN |
| Enzyme 66 PDB ID |
Not Available |
| Enzyme 66 Cellular Location |
Not Available |
| Enzyme 66 Gene Sequence |
>3705 bp
ATGGCGGGCGCCCAGCCCGGCGTCCACGCGCTGCAGTTGGAGCCGCCCACCGTGGTGGAG
ACCCTGCGGCGCGGGAGTAAGTTCATCAAATGGGACGAGGAGACCTCCAGTCGGAACCTG
GTGACCCTGCGTGTGGACCCCAATGGCTTCTTCTTGTACTGGACGGGCCCCAACATGGAG
GTGGACACACTGGACATCAGTTCCATCAGGGACACACGGACAGGCCGGTACGCCCGCCTG
CCCAAGGACCCCAAGATCCGGGAAGTTCTGGGCTTTGGGGGTCCCGATGCCCGGCTGGAG
GAGAAGCTGATGACGGTGGTGTCTGGGCCAGACCCGGTGAACACAGTGTTCTTGAACTTC
ATGGCCGTGCAGGATGACACAGCCAAGGTCTGGTCTGAGGAGCTATTCAAGCTGGCTATG
AACATCCTGGCTCAGAACGCCTCCCGGAACACCTTCCTGCGCAAAGCATACACGAAGCTG
AAGCTGCAGGTGAACCAGGATGGTCGGATCCCCGTCAAGAACATCCTGAAGATGTTCTCA
GCAGACAAGAAGCGGGTGGAGACTGCGCTGGAATCCTGTGGCCTCAAATTCAACCGGAGT
GAGTCCATCCGGCCTGATGAGTTTTCCTTGGAAATCTTTGAGCGGTTCCTGAACAAGCTG
TGTCTGCGGCCGGACATTGACAAGATCCTGCTGGAGATAGGCGCCAAGGGCAAGCCATAC
CTGACGCTGGAGCAGCTCATGGACTTCATCAACCAGAAGCAACGCGACCCGAGACTCAAC
GAAGTGCTGTACCCGCCCCTGCGGCCCTCCCAGGCCCGGCTGCTCATCGAAAAGTATGAG
CCCAACCAGCAGTTTCTGGAGCGAGACCAGATGTCCATGGAGGGCTTTAGCCGCTACCTG
GGAGGCGAGGAGAATGGCATCCTGCCCCTGGAAGCCCTGGATCTGAGCACGGACATGACC
CAGCCACTGAGTGCCTACTTCATCAACTCCTCGCATAACACCTATCTCACTGCGGGGCAG
CTGGCTGGGACCTCGTCGGTGGAGATGTACCGCCAGGCACTACTATGGGGCTGCCGCTGC
GTGGAGCTGGACGTGTGGAAGGGACGGCCGCCTGAGGAGGAACCCTTCATTACCCACGGC
TTCACCATGACCACAGAGGTGCCTCTGCGCGACGTGCTGGAGGCCATTGCCGAGACTGCC
TTCAAGACCTCGCCCTACCCCGTCATCCTCTCCTTCGAGAACCATGTGGACTCGGCAAAG
CAACAGGCAAAGATGGCTGAGTACTGCCGCTCCATCTTTGGAGACGCGCTACTCATCGAG
CCTCTGGACAAGTACCCGCTGGCCCCAGGCGTTCCCCTGCCCAGCCCCCAGGACCTGATG
GGCCGTATCCTGGTGAAGAACAAGAAGCGGCACCGACCCAGCGCAGGTGGCCCAGACAGC
GCCGGGCGCAAGCGGCCCCTGGAGCAGAGCAATTCTGCCCTGAGCGAGAGCTCCGCGGCC
ACCGAGCCCTCCTCCCCGCAGCTGGGGTCTCCCAGCTCTGACAGCTGCCCAGGCCTGAGC
AATGGGGAGGAGGTAGGGCTTGAGAAGCCCAGCCTGGAGCCTCAGAAGTCTCTGGGTGAC
GAGGGCCTGAACCGAGGCCCCTATGTTCTTGGACCTGCTGACCGTGAGGATGAGGAGGAA
GATGAGGAAGAGGAGGAACAGACAGACCCCAAAAAGCCAACTACAGATGAGGGCACAGCC
AGCAGCGAGGTGAATGCCACTGAGGAGATGTCCACGCTTGTCAACTACATCGAACCTGTC
AAGTTCAAGTCCTTTGAGGCTGCTCGAAAGAGGAACAAATGCTTCGAGATGTCGTCCTTT
GTGGAGACCAAGGCCATGGAGCAACTGACCAAGAGCCCCATGGAGTTTGTGGAATACAAC
AAGCAGCAGCTCAGCCGCATCTACCCCAAGGGCACCCGCGTGGACTCCTCCAACTACATG
CCCCAGCTCTTCTGGAACGTAGGGTGCCAGCTTGTTGCGCTCAACTTCCAGACCCTCGAT
GTGGCGATGCAGCTCAACGCGGGCGTTTTTGAGTACAACGGGCGCAGCGGGTACCTGCTC
AAGCCGGAGTTCATGCGGCGGCCGGACAAGTCCTTCGACCCCTTCACTGAGGTCATCGTG
GATGGCATCGTGGCCAATGCCTTGCGGGTCAAGGTGATCTCAGGGCAGTTCCTGTCCGAC
AGGAAGGTGGGCATCTACGTGGAGGTGGACATGTTTGGCCTCCCTGTTGATACGCGGCGC
AAGTACCGCACCCGGACCTCTCAGGGGAACTCGTTCAACCCCGTGTGGGACGAAGAGCCC
TTCGACTTCCCCAAGGTGGTGCTGCCCACGCTGGCTTCACTTCGCATTGCAGCCTTTGAG
GAGGGGGGTAAATTCGTAGGGCACCGGATCCTGCCTGTCTCTGCCATCCGCTCCGGATAC
CACTACGTCTGCCTGCGGAACGAGGCCAACCAACCGCTGTGCCTGCCGGCCCTGCTCATC
TACACCGAAGCCTCGGACTACATTCCTGACGACCACCAGGACTATGCGGAGGCCCTGATC
AACCCCATTAAGCACGTCAGCCTGATGGACCAGAGGGCCCGGCAGCTGGCCGCCCTCATT
GGGGAGAGTGAGGCTCAGGCTGGCCAAGAGACGTGCCAGGACACCCAGTCTCAGCAGCTG
GGGTCTCAGCCGTCCTCAAACCCCACCCCCAGCCCACTGGATGCCTCCCCCCGCCGGCCC
CCTGGCCCCACCACCTCCCCTGCCAGCACCTCCCTCAGCAGCCCAGGGCAGCGTGATGAT
CTCATCGCCAGCATCCTCTCAGAGGTGGCCCCCACCCCGCTGGATGAGCTCCGAGGTCAC
AAGGCTCTGGTCAAGCTCCGGAGCCGGCAAGAGCGAGACCTGCGGGAGCTGCGCAAGAAG
CATCAGCGGAAGGCAGTCACCCTCACCCGCCGCCTGCTGGATGGCCTGGCTCAGGCACAG
GCTGAGGGCAGGTGCCGGCTGCGGCCAGGTGCCCTAGGTGGGGCCGCTGATGTGGAGGAC
ACGAAGGAGGGGGAGGACGAGGCAAAGCGGTATCAGGAGTTCCAGAACAGACAGGTGCAG
AGCCTGCTGGAGCTGCGGGAGGCCCAGGTGGACGCAGAGGCCCAGCGGAGGCTGGAACAC
CTGAGACAGGCTCTGCAGCGGCTCAGGGAGGTCGTCCTTGATGCAAACACAACTCAGTTC
AAGAGGCTGAAAGAGATGAACGAGAGGGAGAAGAAGGAGCTGCAGAAGATCCTGGACAGA
AAGCGCCATAACAGCATCTCGGAGGCCAAGATGAGGGACAAGCATAAGAAGGAGGCGGAA
CTGACGGAGATTAACCGTCGGCACATCACTGAGTCAGTCAACTCCATCCGTCGGCTGGAG
GAGGCCCAGAAGCAGCGGCATGACCGTCTTGTGGCTGGGCAGCAGCAGGTCCTGCAACAG
CTGGCAGAAGAGGAGCCCAAGCTGCTGGCCCAGCTGGCCCAGGAGTGTCAGGAGCAGCGG
GCGAGGCTCCCCCAGGAGATCCGCCGGAGCCTGCTGGGCGAGATGCCAGAGGGGCTGGGG
GACGGGCCTCTGGTGGCCTGTGCCAGCAACGGTCACGCACCCGGGAGCAGCGGGCACCTG
TCGGGCGCTGACTCGGAGAGCCAGGAGGAGAACACGCAGCTCTGA
|
| Enzyme 66 GenBank Gene ID |
BC142681 |
| Enzyme 66 GeneCard ID |
PLCB3 |
| Enzyme 66 GenAtlas ID |
PLCB3 |
| Enzyme 66 HGNC ID |
HGNC:9056 |
| Enzyme 66 Chromosome Location |
1 |
| Enzyme 66 Locus |
11q13 |
| Enzyme 66 SNPs |
SNPJam Report |
| Enzyme 66 General References |
- Mazuruk K, Schoen TJ, Chader GJ, Rodriguez IR: Structural organization and expression of the human phosphatidylinositol-specific phospholipase C beta-3 gene. Biochem Biophys Res Commun. 1995 Jul 6;212(1):190-5. [PubMed ]
- Lagercrantz J, Carson E, Phelan C, Grimmond S, Rosen A, Dare E, Nordenskjold M, Hayward NK, Larsson C, Weber G: Genomic organization and complete cDNA sequence of the human phosphoinositide-specific phospholipase C beta 3 gene (PLCB3). Genomics. 1995 Apr 10;26(3):467-72. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Carozzi AJ, Kriz RW, Webster C, Parker PJ: Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily. Eur J Biochem. 1992 Dec 1;210(2):521-9. [PubMed ]
- Oh YS, Jo NW, Choi JW, Kim HS, Seo SW, Kang KO, Hwang JI, Heo K, Kim SH, Kim YH, Kim IH, Kim JH, Banno Y, Ryu SH, Suh PG: NHERF2 specifically interacts with LPA2 receptor and defines the specificity and efficiency of receptor-mediated phospholipase C-beta3 activation. Mol Cell Biol. 2004 Jun;24(11):5069-79. [PubMed ]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
|
| Enzyme 66 Metabolite References |
Not Available |
|
Enzyme 67
[top]
|
| Enzyme 67 ID |
5461 |
| Enzyme 67 Name |
Pancreatic lipase-related protein 1 |
| Enzyme 67 Synonyms |
- PL-RP1
|
| Enzyme 67 Gene Name |
PNLIPRP1 |
| Enzyme 67 Protein Sequence |
>Pancreatic lipase-related protein 1
MLIFWTITLFLLGAAKGKEVCYEDLGCFSDTEPWGGTAIRPLKILPWSPEKIGTRFLLYT
NENPNNFQILLLSDPSTIEASNFQMDRKTRFIIHGFIDKGDESWVTDMCKKLFEVEEVNC
ICVDWKKGSQATYTQAANNVRVVGAQVAQMLDILLTEYSYPPSKVHLIGHSLGAHVAGEA
GSKTPGLSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPLIPFLGFGTNQQMG
HLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRDFVACNHLRSYKYYLESILNPDGFAA
YPCTSYKSFESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNFARWRYGV
SITLSGRTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLW
NNNVINPTLPKVGATKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC
|
| Enzyme 67 Number of Residues |
467 |
| Enzyme 67 Molecular Weight |
51847.4 |
| Enzyme 67 Theoretical pI |
5.47 |
| Enzyme 67 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 67 General Function |
Involved in catalytic activity |
| Enzyme 67 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 67 Pathways |
|
| Enzyme 67 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 67 Pfam Domain Function |
|
| Enzyme 67 Signals |
|
| Enzyme 67 Transmembrane Regions |
|
| Enzyme 67 Essentiality |
Not Available |
| Enzyme 67 GenBank ID Protein |
5453920 |
| Enzyme 67 UniProtKB/Swiss-Prot ID |
P54315 |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
LIPR1_HUMAN |
| Enzyme 67 PDB ID |
Not Available |
| Enzyme 67 Cellular Location |
Not Available |
| Enzyme 67 Gene Sequence |
>1404 bp
ATGCTGATCTTCTGGACAATCACACTTTTCCTGCTGGGAGCAGCCAAAGGAAAAGAAGTT
TGCTATGAGGACCTCGGGTGCTTTTCTGACACTGAGCCCTGGGGCGGGACAGCAATCAGG
CCCCTGAAAATTCTCCCCTGGAGCCCTGAGAAGATCGGCACCCGCTTCCTGCTGTACACC
AATGAAAACCCAAACAACTTTCAAATTCTCCTCCTCTCTGATCCATCAACAATTGAGGCA
TCAAATTTTCAAATGGACAGAAAGACCCGGTTCATCATCCATGGCTTCATAGACAAAGGA
GATGAGAGCTGGGTGACAGACATGTGCAAGAAACTGTTCGAGGTGGAGGAGGTGAACTGC
ATCTGCGTGGACTGGAAGAAGGGCTCCCAAGCCACCTACACACAGGCTGCCAACAACGTG
CGAGTGGTGGGCGCCCAGGTGGCCCAGATGCTCGACATCCTCTTGACAGAGTATAGCTAC
CCCCCTTCCAAAGTTCACCTCATTGGCCACAGCCTGGGAGCCCACGTGGCTGGAGAGGCA
GGAAGCAAGACTCCAGGCCTGAGCAGGATTACAGGGTTGGATCCTGTAGAAGCAAGTTTC
GAGAGTACTCCTGAAGAGGTGCGACTTGATCCCTCTGATGCTGACTTTGTTGATGTGATT
CACACGGATGCAGCTCCCCTGATCCCATTCTTGGGTTTTGGAACGAACCAACAGATGGGT
CATCTTGACTTCTTCCCCAATGGAGGAGAGAGCATGCCGGGATGCAAGAAGAATGCCCTG
TCTCAGATCGTGGATCTAGATGGCATCTGGGCGGGAACCCGGGACTTTGTGGCTTGCAAT
CACCTAAGAAGCTACAAGTATTACTTGGAAAGCATCCTCAATCCCGATGGGTTTGCTGCA
TATCCCTGCACTTCCTACAAGTCCTTTGAGTCTGACAAGTGCTTCCCGTGTCCAGATCAA
GGATGCCCACAGATGGGTCACTATGCTGATAAATTTGCTGGCAGGACAAGTGAAGAGCAG
CAGAAATTCTTCTTGAACACAGGAGAGGCTAGCAATTTCGCTCGCTGGAGATATGGGGTT
TCCATCACACTGTCTGGAAGAACAGCCACTGGTCAGATCAAAGTTGCTTTGTTTGGAAAT
AAGGGAAACACTCACCAGTACAGCATCTTCAGGGGGATTCTCAAACCAGGCTCAACCCAT
TCCTATGAGTTTGATGCAAAGCTGGATGTTGGAACAATTGAGAAAGTCAAGTTTCTTTGG
AATAACAATGTGATAAATCCAACCCTCCCCAAAGTGGGTGCCACCAAGATCACTGTGCAA
AAGGGAGAAGAGAAGACAGTGTACAACTTCTGTAGCGAAGACACAGTGCGGGAAGACACG
CTGCTCACCCTCACGCCCTGCTAA
|
| Enzyme 67 GenBank Gene ID |
NM_006229.2 |
| Enzyme 67 GeneCard ID |
PNLIPRP1 |
| Enzyme 67 GenAtlas ID |
PNLIPRP1 |
| Enzyme 67 HGNC ID |
HGNC:9156 |
| Enzyme 67 Chromosome Location |
1 |
| Enzyme 67 Locus |
10q25.3 |
| Enzyme 67 SNPs |
SNPJam Report |
| Enzyme 67 General References |
- Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
5462 |
| Enzyme 68 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2 |
| Enzyme 68 Synonyms |
- Phosphoinositide phospholipase C-gamma-2
- Phospholipase C-IV
- PLC-IV
- Phospholipase C-gamma-2
- PLC-gamma-2
|
| Enzyme 68 Gene Name |
PLCG2 |
| Enzyme 68 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase gamma-2
MSTTVNVDSLAEYEKSQIKRALELGTVMTVFSFRKSTPERRTVQVIMETRQVAWSKTADK
IEGFLDIMEIKEIRPGKNSKDFERAKAVRQKEDCCFTILYGTQFVLSTLSLAADSKEDAV
NWLSGLKILHQEAMNASTPTIIESWLRKQIYSVDQTRRNSISLRELKTILPLINFKVSSA
KFLKDKFVEIGAHKDELSFEQFHLFYKKLMFEQQKSILDEFKKDSSVFILGNTDRPDASA
VYLHDFQRFLIHEQQEHWAQDLNKVRERMTKFIDDTMRETAEPFLFVDEFLTYLFSRENS
IWDEKYDAVDMQDMNNPLSHYWISSSHNTYLTGDQLRSESSPEAYIRCLRMGCRCIELDC
WDGPDGKPVIYHGWTRTTKIKFDDVVQAIKDHAFVTSSFPVILSIEEHCSVEQQRHMAKA
FKEVFGDLLLTKPTEASADQLPSPSQLREKIIIKHKKLGPRGDVDVNMEDKKDEHKQQGE
LYMWDSIDQKWTRHYCAIADAKLSFSDDIEQTMEEEVPQDIPPTELHFGEKWFHKKVEKR
TSAEKLLQEYCMETGGKDGTFLVRESETFPNDYTLSFWRSGRVQHCRIRSTMEGGTLKYY
LTDNLTFSSIYALIQHYRETHLRCAEFELRLTDPVPNPNPHESKPWYYDSLSRGEAEDML
MRIPRDGAFLIRKREGSDSYAITFRARGKVKHCRINRDGRHFVLGTSAYFESLVELVSYY
EKHSLYRKMRLRYPVTPELLERYNMERDINSLYDVSRMYVDPSEINPSMPQRTVKALYDY
KAKRSDELSFCRGALIHNVSKEPGGWWKGDYGTRIQQYFPSNYVEDISTADFEELEKQII
EDNPLGSLCRGILDLNTYNVVKAPQGKNQKSFVFILEPKQQGDPPVEFATDRVEELFEWF
QSIREITWKIDTKENNMKYWEKNQSIAIELSDLVVYCKPTSKTKDNLENPDFREIRSFVE
TKADSIIRQKPVDLLKYNQKGLTRVYPKGQRVDSSNYDPFRLWLCGSQMVALNFQTADKY
MQMNHALFSLNGRTGYVLQPESMRTEKYDPMPPESQRKILMTLTVKVLGARHLPKLGRSI
ACPFVEVEICGAEYDNNKFKTTVVNDNGLSPIWAPTQEKVTFEIYDPNLAFLRFVVYEED
MFSDPNFLAHATYPIKAVKSGFRSVPLKNGYSEDIELASLLVFCEMRPVLESEEELYSSC
RQLRRRQEELNNQLFLYDTHQNLRNANRDALVKEFSVNENQLQLYQEKCNKRLREKRVSN
SKFYS
|
| Enzyme 68 Number of Residues |
1265 |
| Enzyme 68 Molecular Weight |
147868.7 |
| Enzyme 68 Theoretical pI |
6.60 |
| Enzyme 68 GO Classification |
| Function |
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- molecular transducer activity
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
- protein binding
- signal transducer activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 68 General Function |
Involved in phosphoinositide phospholipase C activity |
| Enzyme 68 Specific Function |
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. It is a crucial enzyme in transmembrane signaling |
| Enzyme 68 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 68 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 68 Pfam Domain Function |
|
| Enzyme 68 Signals |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
117320537 |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
P16885 |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
PLCG2_HUMAN |
| Enzyme 68 PDB ID |
Not Available |
| Enzyme 68 Cellular Location |
Not Available |
| Enzyme 68 Gene Sequence |
>3798 bp
ATGTCCACCACGGTCAATGTAGATTCCCTTGCGGAATATGAGAAGAGCCAGATCAAGAGA
GCCCTGGAGCTGGGGACGGTGATGACTGTGTTCAGCTTCCGCAAGTCCACCCCCGAGCGG
AGAACCGTCCAGGTGATCATGGAGACGCGGCAGGTGGCCTGGAGCAAGACCGCCGACAAG
ATCGAGGGCTTCTTGGATATCATGGAAATAAAAGAAATCCGCCCAGGGAAGAACTCCAAA
GATTTCGAGCGAGCAAAAGCAGTTCGCCAGAAAGAAGACTGCTGCTTCACCATCCTATAT
GGCACTCAGTTCGTCCTCAGCACGCTCAGCTTGGCAGCTGACTCTAAAGAGGATGCAGTT
AACTGGCTCTCTGGCTTGAAAATCTTACACCAGGAAGCGATGAATGCGTCCACGCCCACC
ATTATCGAGAGTTGGCTGAGAAAGCAGATATATTCTGTGGATCAAACCAGAAGAAACAGC
ATCAGTCTCCGAGAGTTGAAGACCATCTTGCCCCTGATCAACTTTAAAGTGAGCAGTGCC
AAGTTCCTTAAAGATAAGTTTGTGGAAATAGGAGCACACAAAGATGAGCTCAGCTTTGAA
CAGTTCCATCTCTTCTATAAAAAACTTATGTTTGAACAGCAAAAATCGATTCTCGATGAA
TTCAAAAAGGATTCGTCCGTGTTCATCCTGGGGAACACTGACAGGCCGGATGCCTCTGCT
GTTTACCTGCATGACTTCCAGAGGTTTCTCATACATGAACAGCAGGAGCATTGGGCTCAG
GATCTGAACAAAGTCCGTGAGCGGATGACAAAGTTCATTGATGACACCATGCGTGAAACT
GCTGAGCCTTTCTTGTTTGTGGATGAGTTCCTCACGTACCTGTTTTCACGAGAAAACAGC
ATCTGGGATGAGAAGTATGACGCGGTGGACATGCAGGACATGAACAACCCCCTGTCTCAT
TACTGGATCTCCTCGTCACATAACACGTACCTTACAGGTGACCAGCTGCGGAGCGAGTCG
TCCCCAGAAGCTTACATCCGCTGCCTGCGCATGGGCTGTCGCTGCATTGAACTGGACTGC
TGGGACGGGCCCGATGGGAAGCCGGTCATCTACCATGGCTGGACGCGGACTACCAAGATC
AAGTTTGACGACGTCGTGCAGGCCATCAAAGACCACGCCTTTGTTACCTCGAGCTTCCCA
GTGATCCTGTCCATCGAGGAGCACTGCAGCGTGGAGCAACAGCGTCACATGGCCAAGGCC
TTCAAGGAAGTATTTGGCGACCTGCTGTTGACGAAGCCCACGGAGGCCAGTGCTGACCAG
CTGCCCTCGCCCAGCCAGCTGCGGGAGAAGATCATCATCAAGCATAAGAAGCTGGGCCCC
CGAGGCGATGTGGATGTCAACATGGAGGACAAGAAGGACGAACACAAGCAACAGGGGGAG
CTGTACATGTGGGATTCCATTGACCAGAAATGGACTCGGCACTACTGCGCCATTGCCGAT
GCCAAGCTGTCCTTCAGTGATGACATTGAACAGACTATGGAGGAGGAAGTGCCCCAGGAT
ATACCCCCTACAGAACTACATTTTGGGGAGAAATGGTTCCACAAGAAGGTGGAGAAGAGG
ACGAGTGCCGAGAAGTTGCTGCAGGAATACTGCATGGAGACGGGGGGCAAGGATGGCACC
TTCCTGGTTCGGGAGAGCGAGACCTTCCCCAATGACTACACCCTGTCCTTCTGGCGGTCA
GGCCGGGTCCAGCACTGCCGGATCCGCTCCACCATGGAGGGCGGGACCCTGAAATACTAC
TTGACTGACAACCTCACCTTCAGCAGCATCTATGCCCTCATCCAGCACTACCGCGAGACG
CACCTGCGCTGCGCCGAGTTCGAGCTGCGGCTCACGGACCCTGTGCCCAACCCCAACCCC
CACGAGTCCAAGCCGTGGTACTATGACAGCCTGAGCCGCGGAGAGGCAGAGGACATGCTG
ATGAGGATTCCCCGGGACGGGGCCTTCCTGATCCGGAAGCGAGAGGGGAGCGACTCCTAT
GCCATCACCTTCAGGGCTAGGGGCAAGGTAAAGCATTGTCGCATCAACCGGGACGGCCGG
CACTTTGTGCTGGGGACCTCCGCCTATTTTGAGAGTCTGGTGGAGCTCGTCAGTTACTAC
GAGAAGCATTCACTCTACCGAAAGATGAGACTGCGCTACCCCGTGACCCCCGAGCTCCTG
GAGCGCTACAATATGGAAAGAGATATAAACTCCCTCTACGACGTCAGCAGAATGTATGTG
GATCCCAGTGAAATCAATCCGTCCATGCCTCAGAGAACCGTGAAAGCTCTGTATGACTAC
AAAGCCAAGCGAAGCGATGAGCTGAGCTTCTGCCGTGGTGCCCTCATCCACAATGTCTCC
AAGGAGCCCGGGGGCTGGTGGAAAGGAGACTATGGAACCAGGATCCAGCAGTACTTCCCA
TCCAACTACGTCGAGGACATCTCAACTGCAGACTTCGAGGAGCTAGAAAAGCAGATTATT
GAAGACAATCCCTTAGGGTCTCTTTGCAGAGGAATATTGGACCTCAATACCTATAACGTC
GTGAAAGCCCCTCAGGGAAAAAACCAGAAGTCCTTTGTCTTCATCCTGGAGCCCAAGCAG
CAGGGCGATCCTCCGGTGGAGTTTGCCACAGACAGGGTGGAGGAGCTCTTTGAGTGGTTT
CAGAGCATCCGAGAGATCACCTGGAAGATTGACACCAAGGAGAACAACATGAAGTACTGG
GAGAAGAACCAGTCCATCGCCATCGAGCTCTCTGACCTGGTTGTCTACTGCAAACCAACC
AGCAAAACCAAGGACAACTTAGAAAATCCTGACTTCCGAGAAATCCGCTCCTTTGTGGAG
ACGAAGGCTGACAGCATCATCAGACAGAAGCCCGTCGACCTCCTGAAGTACAATCAAAAG
GGCCTGACCCGCGTCTACCCAAAGGGACAAAGAGTTGACTCTTCAAACTACGACCCCTTC
CGCCTCTGGCTGTGCGGTTCTCAGATGGTGGCACTCAATTTCCAGACGGCAGATAAGTAC
ATGCAGATGAATCACGCATTGTTTTCTCTCAATGGGCGCACGGGCTACGTTCTGCAGCCT
GAGAGCATGAGGACAGAGAAATATGACCCGATGCCACCCGAGTCCCAGAGGAAGATCCTG
ATGACGCTGACAGTCAAGGTTCTCGGTGCTCGCCATCTCCCCAAACTTGGACGAAGTATT
GCCTGTCCCTTTGTAGAAGTGGAGATCTGTGGAGCCGAGTATGACAACAACAAGTTCAAG
ACGACGGTTGTGAATGATAATGGCCTCAGCCCTATCTGGGCTCCAACACAGGAGAAGGTG
ACATTTGAAATTTATGACCCAAACCTGGCATTTCTGCGCTTTGTGGTTTATGAAGAAGAT
ATGTTCAGCGATCCCAACTTTCTTGCTCATGCCACTTACCCCATTAAAGCAGTCAAATCA
GGATTCAGGTCCGTTCCTCTGAAGAATGGGTACAGCGAGGACATAGAGCTGGCTTCCCTC
CTGGTTTTCTGTGAGATGCGGCCAGTCCTGGAGAGCGAAGAGGAACTTTACTCCTCCTGT
CGCCAGCTGAGGAGGCGGCAAGAAGAACTGAACAACCAGCTCTTTCTGTATGACACACAC
CAGAACTTGCGCAATGCCAACCGGGATGCCCTGGTTAAAGAGTTCAGTGTTAATGAGAAC
CAGCTCCAGCTGTACCAGGAGAAATGCAACAAGAGGTTAAGAGAGAAGAGAGTCAGCAAC
AGCAAGTTTTACTCATAG
|
| Enzyme 68 GenBank Gene ID |
NM_002661.2 |
| Enzyme 68 GeneCard ID |
PLCG2 |
| Enzyme 68 GenAtlas ID |
PLCG2 |
| Enzyme 68 HGNC ID |
HGNC:9066 |
| Enzyme 68 Chromosome Location |
1 |
| Enzyme 68 Locus |
16q24.1 |
| Enzyme 68 SNPs |
SNPJam Report |
| Enzyme 68 General References |
- Ohta S, Matsui A, Nazawa Y, Kagawa Y: Complete cDNA encoding a putative phospholipase C from transformed human lymphocytes. FEBS Lett. 1988 Dec 19;242(1):31-5. [PubMed ]
- Kemmer D, Podowski RM, Arenillas D, Lim J, Hodges E, Roth P, Sonnhammer EL, Hoog C, Wasserman WW: NovelFam3000--uncharacterized human protein domains conserved across model organisms. BMC Genomics. 2006 Mar 13;7:48. [PubMed ]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Ozdener F, Dangelmaier C, Ashby B, Kunapuli SP, Daniel JL: Activation of phospholipase Cgamma2 by tyrosine phosphorylation. Mol Pharmacol. 2002 Sep;62(3):672-9. [PubMed ]
- Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed ]
|
| Enzyme 68 Metabolite References |
Not Available |
|
Enzyme 69
[top]
|
| Enzyme 69 ID |
5463 |
| Enzyme 69 Name |
Lipid phosphate phosphohydrolase 2 |
| Enzyme 69 Synonyms |
- PAP2-gamma
- PAP2-G
- Phosphatidate phosphohydrolase type 2c
- Phosphatidic acid phosphatase 2c
- PAP-2c
- PAP2c
|
| Enzyme 69 Gene Name |
PPAP2C |
| Enzyme 69 Protein Sequence |
>Lipid phosphate phosphohydrolase 2
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGV
TITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMI
GRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLA
LYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTV
CYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
|
| Enzyme 69 Number of Residues |
288 |
| Enzyme 69 Molecular Weight |
32573.4 |
| Enzyme 69 Theoretical pI |
8.44 |
| Enzyme 69 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 69 General Function |
Involved in catalytic activity |
| Enzyme 69 Specific Function |
Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P |
| Enzyme 69 Pathways |
|
| Enzyme 69 Reactions |
- a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
|
| Enzyme 69 Pfam Domain Function |
|
| Enzyme 69 Signals |
|
| Enzyme 69 Transmembrane Regions |
- 5-25
52-72
88-108
163-183
197-217
227-247
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
4505977 |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
O43688 |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
LPP2_HUMAN |
| Enzyme 69 PDB ID |
Not Available |
| Enzyme 69 Cellular Location |
Not Available |
| Enzyme 69 Gene Sequence |
>867 bp
ATGCAGCGGAGGTGGGTCTTCGTGCTGCTCGACGTGCTGTGCTTACTGGTCGCCTCCCTG
CCCTTCGCTATCCTGACGCTGGTGAACGCCCCGTACAAGCGAGGATTTTACTGCGGGGAT
GACTCCATCCGGTACCCCTACCGTCCAGATACCATCACCCACGGGCTCATGGCTGGGGTC
ACCATCACGGCCACCGTCATCCTTGTCTCGGCCGGGGAAGCCTACCTGGTGTACACAGAC
CGGCTCTATTCTCGCTCGGACTTCAACAACTACGTGGCTGCTGTATACAAGGTGCTGGGG
ACCTTCCTGTTTGGGGCTGCCGTGAGCCAGTCTCTGACAGACCTGGCCAAGTACATGATT
GGGCGTCTGAGGCCCAACTTCCTAGCCGTCTGCGACCCCGACTGGAGCCGGGTCAACTGC
TCGGTCTATGTGCAGCTGGAGAAGGTGTGCAGGGGAAACCCTGCTGATGTCACCGAGGCC
AGGTTGTCTTTCTACTCGGGACACTCTTCCTTTGGGATGTACTGCATGGTGTTCTTGGCG
CTGTATGTGCAGGCACGACTCTGTTGGAAGTGGGCACGGCTGCTGCGACCCACAGTCCAG
TTCTTCCTGGTGGCCTTTGCCCTCTACGTGGGCTACACCCGCGTGTCTGATTACAAACAC
CACTGGAGCGATGTCCTTGTTGGCCTCCTGCAGGGGGCACTGGTGGCTGCCCTCACTGTC
TGCTACATCTCAGACTTCTTCAAAGCCCGACCCCCACAGCACTGTCTGAAGGAGGAGGAG
CTGGAACGGAAGCCCAGCCTGTCACTGACGTTGACCCTGGGCGAGGCTGACCACAACCAC
TATGGATACCCGCACTCCTCCTCCTGA
|
| Enzyme 69 GenBank Gene ID |
NM_003712.2 |
| Enzyme 69 GeneCard ID |
PPAP2C |
| Enzyme 69 GenAtlas ID |
PPAP2C |
| Enzyme 69 HGNC ID |
HGNC:9230 |
| Enzyme 69 Chromosome Location |
1 |
| Enzyme 69 Locus |
19p13 |
| Enzyme 69 SNPs |
SNPJam Report |
| Enzyme 69 General References |
- Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed ]
- Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed ]
- Hooks SB, Ragan SP, Lynch KR: Identification of a novel human phosphatidic acid phosphatase type 2 isoform. FEBS Lett. 1998 May 8;427(2):188-92. [PubMed ]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 69 Metabolite References |
Not Available |
|
Enzyme 70
[top]
|
| Enzyme 70 ID |
5464 |
| Enzyme 70 Name |
Patatin-like phospholipase domain-containing protein 3 |
| Enzyme 70 Synonyms |
- Acylglycerol O-acyltransferase
- Adiponutrin
- Calcium-independent phospholipase A2-epsilon
- iPLA2-epsilon
|
| Enzyme 70 Gene Name |
PNPLA3 |
| Enzyme 70 Protein Sequence |
>Patatin-like phospholipase domain-containing protein 3
MYDAERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGI
PLEQTLQVLSDLVRKARSRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTR
VSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGVSDNVPFIDAKT
TITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLR
GYLDAFRFLEEKGICNRPQPGLKSSSEGMDPEVAMPSWANMSLDSSPESAALAVRLEGDE
LLDHLRLSILPWDESILDTLSPRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTL
PVESAIAIVQRLVTWLPDMPDDVLWLQWVTSQVFTRVLMCLLPASRSQMPVSSQQASPCT
PEQDWPCWTPCSPKGCPAETKAEATPRSILRSSLNFFLGNKVPAGAEGLSTFPSFSLEKS
L
|
| Enzyme 70 Number of Residues |
481 |
| Enzyme 70 Molecular Weight |
52864.6 |
| Enzyme 70 Theoretical pI |
6.68 |
| Enzyme 70 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 70 General Function |
Involved in metabolic process |
| Enzyme 70 Specific Function |
Multifunctional enzyme which has both triacylglycerol lipase and acylglycerol O-acyltransferase activities |
| Enzyme 70 Pathways |
|
| Enzyme 70 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 70 Pfam Domain Function |
|
| Enzyme 70 Signals |
|
| Enzyme 70 Transmembrane Regions |
|
| Enzyme 70 Essentiality |
Not Available |
| Enzyme 70 GenBank ID Protein |
17059636 |
| Enzyme 70 UniProtKB/Swiss-Prot ID |
Q9NST1 |
| Enzyme 70 UniProtKB/Swiss-Prot Entry Name |
PLPL3_HUMAN |
| Enzyme 70 PDB ID |
Not Available |
| Enzyme 70 Cellular Location |
Not Available |
| Enzyme 70 Gene Sequence |
>1446 bp
ATGTACGACGCAGAGCGCGGCTGGAGCTTGTCCTTCGCGGGCTGCGGCTTCCTGGGCTTC
TACCACGTCGGGGCGACCCGCTGCCTGAGCGAGCACGCCCCGCACCTCCTCCGCGACGCG
CGCATGTTGTTCGGCGCTTCGGCCGGGGCGTTGCACTGCGTCGGCGTCCTCTCCGGTATC
CCGCTGGAGCAGACTCTGCAGGTCCTCTCAGATCTTGTGCGGAAGGCCAGGAGTCGGAAC
ATTGGCATCTTCCATCCATCCTTCAACTTAAGCAAGTTCCTCCGACAGGGTCTCTGCAAA
TGCCTCCCGGCCAATGTCCACCAGCTCATCTCCGGCAAAATAGGCATCTCTCTTACCAGA
GTGTCTGATGGGGAAAACGTTCTGGTGTCTGACTTTCGGTCCAAAGACGAAGTCGTGGAT
GCCTTGGTATGTTCCTGCTTCATCCCCTTCTACAGTGGCCTTATCCCTCCTTCCTTCAGA
GGCGTGCGATATGTGGATGGAGGAGTGAGTGACAACGTACCCTTCATTGATGCCAAAACA
ACCATCACCGTGTCCCCCTTCTATGGGGAGTACGACATCTGCCCTAAAGTCAAGTCCACG
AACTTTCTTCATGTGGACATCACCAAGCTCAGTCTACGCCTCTGCACAGGGAACCTCTAC
CTTCTCTCGAGAGCTTTTGTCCCCCCGGATCTCAAGGTGCTGGGAGAGATATGCCTTCGA
GGATATTTGGATGCATTCAGGTTCTTGGAAGAGAAGGGCATCTGCAACAGGCCCCAGCCA
GGCCTGAAGTCATCCTCAGAAGGGATGGATCCTGAGGTCGCCATGCCCAGCTGGGCAAAC
ATGAGTCTGGATTCTTCCCCGGAGTCGGCTGCCTTGGCTGTGAGGCTGGAGGGAGATGAG
CTGCTAGACCACCTGCGTCTCAGCATCCTGCCCTGGGATGAGAGCATCCTGGACACCCTC
TCGCCCAGGCTCGCTACAGCACTGAGTGAAGAAATGAAAGACAAAGGTGGATACATGAGC
AAGATTTGCAACTTGCTACCCATTAGGATAATGTCTTATGTAATGCTGCCCTGTACCCTG
CCTGTGGAATCTGCCATTGCGATTGTCCAGAGACTGGTGACATGGCTTCCAGATATGCCC
GACGATGTCCTGTGGTTGCAGTGGGTGACCTCACAGGTGTTCACTCGAGTGCTGATGTGT
CTGCTCCCCGCCTCCAGGTCCCAAATGCCAGTGAGCAGCCAACAGGCCTCCCCATGCACA
CCTGAGCAGGACTGGCCCTGCTGGACTCCCTGCTCCCCCAAGGGCTGTCCAGCAGAGACC
AAAGCAGAGGCCACCCCGCGGTCCATCCTCAGGTCCAGCCTGAACTTCTTCTTGGGCAAT
AAAGTACCTGCTGGTGCTGAGGGGCTCTCCACCTTTCCCAGTTTTTCACTAGAGAAGAGT
CTGTGA
|
| Enzyme 70 GenBank Gene ID |
AL138578 |
| Enzyme 70 GeneCard ID |
PNPLA3 |
| Enzyme 70 GenAtlas ID |
PNPLA3 |
| Enzyme 70 HGNC ID |
HGNC:18590 |
| Enzyme 70 Chromosome Location |
2 |
| Enzyme 70 Locus |
22q13.31 |
| Enzyme 70 SNPs |
SNPJam Report |
| Enzyme 70 General References |
- Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I: Reevaluating human gene annotation: a second-generation analysis of chromosome 22. Genome Res. 2003 Jan;13(1):27-36. [PubMed ]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed ]
- Liu YM, Moldes M, Bastard JP, Bruckert E, Viguerie N, Hainque B, Basdevant A, Langin D, Pairault J, Clement K: Adiponutrin: A new gene regulated by energy balance in human adipose tissue. J Clin Endocrinol Metab. 2004 Jun;89(6):2684-9. [PubMed ]
- Johansson LE, Lindblad U, Larsson CA, Rastam L, Ridderstrale M: Polymorphisms in the adiponutrin gene are associated with increased insulin secretion and obesity. Eur J Endocrinol. 2008 Nov;159(5):577-83. Epub 2008 Aug 26. [PubMed ]
- Romeo S, Kozlitina J, Xing C, Pertsemlidis A, Cox D, Pennacchio LA, Boerwinkle E, Cohen JC, Hobbs HH: Genetic variation in PNPLA3 confers susceptibility to nonalcoholic fatty liver disease. Nat Genet. 2008 Dec;40(12):1461-5. Epub 2008 Sep 25. [PubMed ]
- Kotronen A, Johansson LE, Johansson LM, Roos C, Westerbacka J, Hamsten A, Bergholm R, Arkkila P, Arola J, Kiviluoto T, Fisher RM, Ehrenborg E, Orho-Melander M, Ridderstrale M, Groop L, Yki-Jarvinen H: A common variant in PNPLA3, which encodes adiponutrin, is associated with liver fat content in humans. Diabetologia. 2009 Jun;52(6):1056-60. Epub 2009 Feb 18. [PubMed ]
- He S, McPhaul C, Li JZ, Garuti R, Kinch L, Grishin NV, Cohen JC, Hobbs HH: A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis. J Biol Chem. 2010 Feb 26;285(9):6706-15. Epub 2009 Dec 23. [PubMed ]
- Sookoian S, Castano GO, Burgueno AL, Gianotti TF, Rosselli MS, Pirola CJ: A nonsynonymous gene variant in the adiponutrin gene is associated with nonalcoholic fatty liver disease severity. J Lipid Res. 2009 Oct;50(10):2111-6. [PubMed ]
|
| Enzyme 70 Metabolite References |
Not Available |
|
Enzyme 71
[top]
|
| Enzyme 71 ID |
5468 |
| Enzyme 71 Name |
Gastric triacylglycerol lipase |
| Enzyme 71 Synonyms |
- GL
- Gastric lipase
|
| Enzyme 71 Gene Name |
LIPF |
| Enzyme 71 Protein Sequence |
>Gastric triacylglycerol lipase
MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILE
VNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRG
NTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFI
AFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQF
LATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKS
GKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPN
LIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK
|
| Enzyme 71 Number of Residues |
398 |
| Enzyme 71 Molecular Weight |
45237.4 |
| Enzyme 71 Theoretical pI |
7.37 |
| Enzyme 71 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 71 General Function |
Involved in lipid metabolic process |
| Enzyme 71 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 71 Pathways |
|
| Enzyme 71 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 71 Pfam Domain Function |
|
| Enzyme 71 Signals |
|
| Enzyme 71 Transmembrane Regions |
|
| Enzyme 71 Essentiality |
Not Available |
| Enzyme 71 GenBank ID Protein |
758063 |
| Enzyme 71 UniProtKB/Swiss-Prot ID |
P07098 |
| Enzyme 71 UniProtKB/Swiss-Prot Entry Name |
LIPG_HUMAN |
| Enzyme 71 PDB ID |
1HLG |
| Enzyme 71 PDB File |
Show |
| Enzyme 71 3D Structure |
|
| Enzyme 71 Cellular Location |
Not Available |
| Enzyme 71 Gene Sequence |
>1197 bp
ATGTGGCTGCTTTTAACAATGGCAAGTTTGATATCTGTACTGGGGACTACACATGGTTTG
TTTGGAAAATTACATCCTGGAAGCCCTGAAGTGACTATGAACATTAGTCAGATGATTACT
TATTGGGGATACCCAAATGAAGAATATGAAGTTGTGACTGAAGATGGTTATATTCTTGAA
GTCAATAGAATTCCTTATGGGAAGAAAAATTCAGGGAATACAGGCCAGAGACCTGTTGTG
TTTTTGCAGCATGGTTTGCTTGCATCAGCCACAAACTGGATTTCCAACCTGCCGAACAAC
AGCCTTGCCTTCATTCTGGCAGATGCTGGTTATGATGTGTGGCTGGGCAACAGCAGAGGA
AACACCTGGGCCAGAAGAAACTTGTACTATTCACCAGATTCAGTTGAATTCTGGGCTTTC
AGCTTTGATGAAATGGCTAAATATGACCTTCCAGCCACAATCGACTTCATTGTAAAGAAA
ACTGGACAGAAGCAGCTACACTATGTTGGCCATTCCCAGGGCACCACCATTGGTTTTATT
GCCTTTTCCACCAATCCCAGCCTGGCTAAAAGAATCAAAACCTTCTATGCTCTAGCTCCT
GTTGCCACTGTGAAGTATACAAAAAGCCTTATAAACAAACTTAGATTTGTTCCTCAATCC
CTCTTCAAGTTTATATTTGGTGACAAAATATTCTACCCACACAACTTCTTTGATCAATTT
CTTGCTACTGAAGTGTGCTCCCGTGAGATGCTGAATCTCCTTTGCAGCAATGCCTTATTT
ATAATTTGTGGATTTGACAGTAAGAACTTTAACACGAGTCGCTTGGATGTGTATCTATCA
CATAATCCAGCAGGAACTTCTGTTCAAAACATGTTCCATTGGACCCAGGCTGTTAAGTCT
GGGAAATTCCAAGCTTATGACTGGGGAAGCCCAGTTCAGAATAGGATGCACTATGATCAG
TCCCAACCTCCCTACTACAATGTGACAGCCATGAATGTACCAATTGCAGTGTGGAACGGT
GGCAAGGACCTGTTGGCTGACCCCCAAGATGTTGGCCTTTTGCTTCCAAAACTCCCCAAT
CTTATTTACCACAAGGAGATTCCTTTTTACAATCACTTGGACTTTATCTGGGCAATGGAT
GCCCCTCAAGAAGTTTACAATGACATTGTTTCTATGATATCAGAAGATAAAAAGTAG
|
| Enzyme 71 GenBank Gene ID |
X05997 |
| Enzyme 71 GeneCard ID |
LIPF |
| Enzyme 71 GenAtlas ID |
LIPF |
| Enzyme 71 HGNC ID |
HGNC:6622 |
| Enzyme 71 Chromosome Location |
1 |
| Enzyme 71 Locus |
10q23.31 |
| Enzyme 71 SNPs |
SNPJam Report |
| Enzyme 71 General References |
- Bodmer MW, Angal S, Yarranton GT, Harris TJ, Lyons A, King DJ, Pieroni G, Riviere C, Verger R, Lowe PA: Molecular cloning of a human gastric lipase and expression of the enzyme in yeast. Biochim Biophys Acta. 1987 Aug 25;909(3):237-44. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Bernback S, Blackberg L: Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity. Eur J Biochem. 1989 Jul 1;182(3):495-9. [PubMed ]
- Roussel A, Canaan S, Egloff MP, Riviere M, Dupuis L, Verger R, Cambillau C: Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J Biol Chem. 1999 Jun 11;274(24):16995-7002. [PubMed ]
|
| Enzyme 71 Metabolite References |
Not Available |
|
Enzyme 72
[top]
|
| Enzyme 72 ID |
5469 |
| Enzyme 72 Name |
Lipid phosphate phosphohydrolase 1 |
| Enzyme 72 Synonyms |
- PAP2-alpha
- Phosphatidate phosphohydrolase type 2a
- Phosphatidic acid phosphatase 2a
- PAP-2a
- PAP2a
|
| Enzyme 72 Gene Name |
PPAP2A |
| Enzyme 72 Protein Sequence |
>Lipid phosphate phosphohydrolase 1
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLG
GIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAK
YSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCML
FVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAI
LVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
|
| Enzyme 72 Number of Residues |
284 |
| Enzyme 72 Molecular Weight |
32155.7 |
| Enzyme 72 Theoretical pI |
8.06 |
| Enzyme 72 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 72 General Function |
Involved in catalytic activity |
| Enzyme 72 Specific Function |
Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma |
| Enzyme 72 Pathways |
|
| Enzyme 72 Reactions |
- a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
|
| Enzyme 72 Pfam Domain Function |
|
| Enzyme 72 Signals |
|
| Enzyme 72 Transmembrane Regions |
- 7-27
54-74
95-115
165-185
200-220
230-250
|
| Enzyme 72 Essentiality |
Not Available |
| Enzyme 72 GenBank ID Protein |
2467298 |
| Enzyme 72 UniProtKB/Swiss-Prot ID |
O14494 |
| Enzyme 72 UniProtKB/Swiss-Prot Entry Name |
LPP1_HUMAN |
| Enzyme 72 PDB ID |
Not Available |
| Enzyme 72 Cellular Location |
Not Available |
| Enzyme 72 Gene Sequence |
>855 bp
ATGTTCGACAAGACGCGGCTGCCGTACGTGGCCCTCGATGTGCTCTGCGTGTTGCTGGCT
GGATTGCCTTTTGCAATTCTTACTTCAAGGCATACCCCCTTCCAACGAGGAGTATTCTGT
AATGATGAGTCCATCAAGTACCCTTACAAAGAAGACACCATACCTTATGCGTTATTAGGT
GGAATAATCATTCCATTCAGTATTATCGTTATTATTCTTGGAGAAACCCTGTCTGTTTAC
TGTAACCTTTTGCACTCAAATTCCTTTATCAGGAATAACTACATAGCCACTATTTACAAA
GCCATTGGAACCTTTTTATTTGGTGCAGCTGCTAGTCAGTCCCTGACTGACATTGCCAAG
TATTCAATAGGCAGACTGCGGCCTCACTTCTTGGATGTTTGTGATCCAGATTGGTCAAAA
ATCAACTGCAGCGATGGTTACATTGAATACTACATATGTCGAGGGAATGCAGAAAGAGTT
AAGGAAGGCAGGTTGTCCTTCTATTCAGGCCACTCTTCGTTTTCCATGTACTGCATGCTG
TTTGTGGCACTTTATCTTCAAGCCAGGATGAAGGGAGACTGGGCAAGACTCTTACGCCCC
ACACTGCAATTTGGTCTTGTTGCCGTATCCATTTATGTGGGCCTTTCTCGAGTTTCTGAT
TATAAACACCACTGGAGCGATGTGTTGACTGGACTCATTCAGGGAGCTCTGGTTGCAATA
TTAGTTGCTGTATATGTATCGGATTTCTTCAAAGAAAGAACTTCTTTTAAAGAAAGAAAA
GAGGAGGACTCTCATACAACTCTGCATGAAACACCAACAACTGGGAATCACTATCCGAGC
AATCACCAGCCTTGA
|
| Enzyme 72 GenBank Gene ID |
AB000888 |
| Enzyme 72 GeneCard ID |
PPAP2A |
| Enzyme 72 GenAtlas ID |
PPAP2A |
| Enzyme 72 HGNC ID |
HGNC:9228 |
| Enzyme 72 Chromosome Location |
5 |
| Enzyme 72 Locus |
5q11 |
| Enzyme 72 SNPs |
SNPJam Report |
| Enzyme 72 General References |
- Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed ]
- Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed ]
- Ulrix W, Swinnen JV, Heyns W, Verhoeven G: Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. J Biol Chem. 1998 Feb 20;273(8):4660-5. [PubMed ]
- Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Smyth SS, Sciorra VA, Sigal YJ, Pamuklar Z, Wang Z, Xu Y, Prestwich GD, Morris AJ: Lipid phosphate phosphatases regulate lysophosphatidic acid production and signaling in platelets: studies using chemical inhibitors of lipid phosphate phosphatase activity. J Biol Chem. 2003 Oct 31;278(44):43214-23. Epub 2003 Aug 8. [PubMed ]
|
| Enzyme 72 Metabolite References |
Not Available |
|
Enzyme 73
[top]
|
| Enzyme 73 ID |
5471 |
| Enzyme 73 Name |
Endothelial lipase |
| Enzyme 73 Synonyms |
- Endothelial cell-derived lipase
- EDL
- EL
|
| Enzyme 73 Gene Name |
LIPG |
| Enzyme 73 Protein Sequence |
>Endothelial lipase
MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPE
HEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVV
VDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGN
FVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHID
IYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDS
NRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKN
MGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGAS
QSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWF
RKCRDGWRMKNETSPTVELP
|
| Enzyme 73 Number of Residues |
500 |
| Enzyme 73 Molecular Weight |
56794.3 |
| Enzyme 73 Theoretical pI |
8.00 |
| Enzyme 73 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipoprotein lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 73 General Function |
Involved in catalytic activity |
| Enzyme 73 Specific Function |
Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin |
| Enzyme 73 Pathways |
|
| Enzyme 73 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 73 Pfam Domain Function |
|
| Enzyme 73 Signals |
|
| Enzyme 73 Transmembrane Regions |
|
| Enzyme 73 Essentiality |
Not Available |
| Enzyme 73 GenBank ID Protein |
4836419 |
| Enzyme 73 UniProtKB/Swiss-Prot ID |
Q9Y5X9 |
| Enzyme 73 UniProtKB/Swiss-Prot Entry Name |
LIPE_HUMAN |
| Enzyme 73 PDB ID |
Not Available |
| Enzyme 73 Cellular Location |
Not Available |
| Enzyme 73 Gene Sequence |
>1503 bp
ATGAGCAACTCCGTTCCTCTGCTCTGTTTCTGGAGCCTCTGCTATTGCTTTGCTGCGGGG
AGCCCCGTACCTTTTGGTCCAGAGGGACGGCTGGAAGATAAGCTCCACAAACCCAAAGCT
ACACAGACTGAGGTCAAACCATCTGTGAGGTTTAACCTCCGCACCTCCAAGGACCCAGAG
CATGAAGGATGCTACCTCTCCGTCGGCCACAGCCAGCCCTTAGAAGACTGCAGTTTCAAC
ATGACAGCTAAAACCTTTTTCATCATTCACGGATGGACGATGAGCGGTATCTTTGAAAAC
TGGCTGCACAAACTCGTGTCAGCCCTGCACACAAGAGAGAAAGACGCCAATGTAGTTGTG
GTTGACTGGCTCCCCCTGGCCCACCAGCTTTACACGGATGCGGTCAATAATACCAGGGTG
GTGGGACACAGCATTGCCAGGATGCTCGACTGGCTGCAGGAGAAGGACGATTTTTCTCTC
GGGAATGTCCACTTGATCGGCTACAGCCTCGGAGCGCACGTGGCCGGGTATGCAGGCAAC
TTCGTGAAAGGAACGGTGGGCCGAATCACAGGTTTGGATCCTGCCGGGCCCATGTTTGAA
GGGGCCGACATCCACAAGAGGCTCTCTCCGGACGATGCAGATTTTGTGGATGTCCTCCAC
ACCTACACGCGTTCCTTCGGCTTGAGCATTGGTATTCAGATGCCTGTGGGCCACATTGAC
ATCTACCCCAATGGGGGTGACTTCCAGCCAGGCTGTGGACTCAACGATGTCTTGGGATCA
ATTGCATATGGAACAATCACAGAGGTGGTAAAATGTGAGCATGAGCGAGCCGTCCACCTC
TTTGTTGACTCTCTGGTGAATCAGGACAAGCCGAGTTTTGCCTTCCAGTGCACTGACTCC
AATCGCTTCAAAAAGGGGATCTGTCTGAGCTGCCGCAAGAACCGTTGTAATAGCATTGGC
TACAATGCCAAGAAAATGAGGAACAAGAGGAACAGCAAAATGTACCTAAAAACCCGGGCA
GGCATGCCTTTCAGAGTTTACCATTATCAGATGAAAATCCATGTCTTCAGTTACAAGAAC
ATGGGAGAAATTGAGCCCACCTTTTACGTCACCCTTTATGGCACTAATGCAGATTCCCAG
ACTCTGCCACTGGAAATAGTGGAGCGGATCGAGCAGAATGCCACCAACACCTTCCTGGTC
TACACCGAGGAGGACTTGGGAGACCTCTTGAAGATCCAGCTCACCTGGGAGGGGGCCTCT
CAGTCTTGGTACAACCTGTGGAAGGAGTTTCGCAGCTACCTGTCTCAACCCCGCAACCCC
GGACGGGAGCTGAATATCAGGCGCATCCGGGTGAAGTCTGGGGAAACCCAGCGGAAACTG
ACATTTTGTACAGAAGACCCTGAGAACACCAGCATATCCCCAGGCCGGGAGCTCTGGTTT
CGCAAGTGTCGGGATGGCTGGAGGATGAAAAACGAAACCAGTCCCACTGTGGAGCTTCCC
TGA
|
| Enzyme 73 GenBank Gene ID |
AF118767 |
| Enzyme 73 GeneCard ID |
LIPG |
| Enzyme 73 GenAtlas ID |
LIPG |
| Enzyme 73 HGNC ID |
HGNC:6623 |
| Enzyme 73 Chromosome Location |
1 |
| Enzyme 73 Locus |
18q21.1 |
| Enzyme 73 SNPs |
SNPJam Report |
| Enzyme 73 General References |
- Hirata K, Dichek HL, Cioffi JA, Choi SY, Leeper NJ, Quintana L, Kronmal GS, Cooper AD, Quertermous T: Cloning of a unique lipase from endothelial cells extends the lipase gene family. J Biol Chem. 1999 May 14;274(20):14170-5. [PubMed ]
- Jaye M, Lynch KJ, Krawiec J, Marchadier D, Maugeais C, Doan K, South V, Amin D, Perrone M, Rader DJ: A novel endothelial-derived lipase that modulates HDL metabolism. Nat Genet. 1999 Apr;21(4):424-8. [PubMed ]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- McCoy MG, Sun GS, Marchadier D, Maugeais C, Glick JM, Rader DJ: Characterization of the lipolytic activity of endothelial lipase. J Lipid Res. 2002 Jun;43(6):921-9. [PubMed ]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed ]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed ]
|
| Enzyme 73 Metabolite References |
Not Available |
|
Enzyme 74
[top]
|
| Enzyme 74 ID |
5473 |
| Enzyme 74 Name |
Bile salt-activated lipase |
| Enzyme 74 Synonyms |
- BAL
- Bile salt-stimulated lipase
- BSSL
- Bucelipase
- Carboxyl ester lipase
- Cholesterol esterase
- Pancreatic lysophospholipase
- Sterol esterase
|
| Enzyme 74 Gene Name |
CEL |
| Enzyme 74 Protein Sequence |
>Bile salt-activated lipase
MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTK
ALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPV
MIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPG
NYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQS
GVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYP
MLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVT
EEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIA
LAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTV
SKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLR
YWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSG
APPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVP
PTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDS
GAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF
|
| Enzyme 74 Number of Residues |
753 |
| Enzyme 74 Molecular Weight |
79320.9 |
| Enzyme 74 Theoretical pI |
4.94 |
| Enzyme 74 GO Classification |
Not Available |
| Enzyme 74 General Function |
Lipid transport and metabolism |
| Enzyme 74 Specific Function |
Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides |
| Enzyme 74 Pathways |
|
| Enzyme 74 Reactions |
- a steryl ester + H2O = a sterol + a fatty acid [RN:R02115]
|
| Enzyme 74 Pfam Domain Function |
|
| Enzyme 74 Signals |
|
| Enzyme 74 Transmembrane Regions |
|
| Enzyme 74 Essentiality |
Not Available |
| Enzyme 74 GenBank ID Protein |
148536848 |
| Enzyme 74 UniProtKB/Swiss-Prot ID |
P19835 |
| Enzyme 74 UniProtKB/Swiss-Prot Entry Name |
CEL_HUMAN |
| Enzyme 74 PDB ID |
1F6W |
| Enzyme 74 PDB File |
Show |
| Enzyme 74 3D Structure |
|
| Enzyme 74 Cellular Location |
Not Available |
| Enzyme 74 Gene Sequence |
>2271 bp
ATGCTCACCATGGGGCGCCTGCAACTGGTTGTGTTGGGCCTCACCTGCTGCTGGGCAGTG
GCGAGTGCCGCGAAGCTGGGCGCCGTGTACACAGAAGGTGGGTTCGTGGAAGGCGTCAAT
AAGAAGCTCGGCCTCCTGGGTGACTCTGTGGACATCTTCAAGGGCATCCCCTTCGCAGCT
CCCACCAAGGCCCTGGAAAATCCTCAGCCACATCCTGGCTGGCAAGGGACCCTGAAGGCC
AAGAACTTCAAGAAGAGATGCCTGCAGGCCACCATCACCCAGGACAGCACCTACGGGGAT
GAAGACTGCCTGTACCTCAACATTTGGGTGCCCCAGGGCAGGAAGCAAGTCTCCCGGGAC
CTGCCCGTTATGATCTGGATCTATGGAGGCGCCTTCCTCATGGGGTCCGGCCATGGGGCC
AACTTCCTCAACAACTACCTGTATGACGGCGAGGAGATCGCCACACGCGGAAACGTCATC
GTGGTCACCTTCAACTACCGTGTCGGCCCCCTTGGGTTCCTCAGCACTGGGGACGCCAAT
CTGCCAGGTAACTATGGCCTTCGGGATCAGCACATGGCCATTGCTTGGGTGAAGAGGAAT
ATCGCGGCCTTCGGGGGGGACCCCAACAACATCACGCTCTTCGGGGAGTCTGCTGGAGGT
GCCAGCGTCTCTCTGCAGACCCTCTCCCCCTACAACAAGGGCCTCATCCGGCGAGCCATC
AGCCAGAGCGGCGTGGCCCTGAGTCCCTGGGTCATCCAGAAAAACCCACTCTTCTGGGCC
AAAAAGGTGGCTGAGAAGGTGGGTTGCCCTGTGGGTGATGCCGCCAGGATGGCCCAGTGT
CTGAAGGTTACTGATCCCCGAGCCCTGACGCTGGCCTATAAGGTGCCGCTGGCAGGCCTG
GAGTACCCCATGCTGCACTATGTGGGCTTCGTCCCTGTCATTGATGGAGACTTCATCCCC
GCTGACCCGATCAACCTGTACGCCAACGCCGCCGACATCGACTATATAGCAGGCACCAAC
AACATGGACGGCCACATCTTCGCCAGCATCGACATGCCTGCCATCAACAAGGGCAACAAG
AAAGTCACGGAGGAGGACTTCTACAAGCTGGTCAGTGAGTTCACAATCACCAAGGGGCTC
AGAGGCGCCAAGACGACCTTTGATGTCTACACCGAGTCCTGGGCCCAGGACCCATCCCAG
GAGAATAAGAAGAAGACTGTGGTGGACTTTGAGACCGATGTCCTCTTCCTGGTGCCCACC
GAGATTGCCCTAGCCCAGCACAGAGCCAATGCCAAGAGTGCCAAGACCTACGCCTACCTG
TTTTCCCATCCCTCTCGGATGCCCGTCTACCCCAAATGGGTGGGGGCCGACCATGCAGAT
GACATTCAGTACGTTTTCGGGAAGCCCTTCGCCACCCCCACGGGCTACCGGCCCCAAGAC
AGGACAGTCTCTAAGGCCATGATCGCCTACTGGACCAACTTTGCCAAAACAGGGGACCCC
AACATGGGCGACTCGGCTGTGCCCACACACTGGGAACCCTACACTACGGAAAACAGCGGC
TACCTGGAGATCACCAAGAAGATGGGCAGCAGCTCCATGAAGCGGAGCCTGAGAACCAAC
TTCCTGCGCTACTGGACCCTCACCTATCTGGCGCTGCCCACAGTGACCGACCAGGAGGCC
ACCCCTGTGCCCCCCACAGGGGACTCCGAGGCCACTCCCGTGCCCCCCACGGGTGACTCC
GAGACCGCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGT
GACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCC
ACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTG
CCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCC
CCCGTGCCGCCCACGGGTGACTCCGGCGCCCCCCCCGTGCCGCCCACGGGTGACGCCGGG
CCCCCCCCCGTGCCGCCCACGGGTGACTCCGGCGCCCCCCCCGTGCCGCCCACGGGTGAC
TCCGGGGCCCCCCCCGTGACCCCCACGGGTGACTCCGAGACCGCCCCCGTGCCGCCCACG
GGTGACTCCGGGGCCCCCCCTGTGCCCCCCACGGGTGACTCTGAGGCTGCCCCTGTGCCC
CCCACAGATGACTCCAAGGAAGCTCAGATGCCTGCAGTCATTAGGTTTTAG
|
| Enzyme 74 GenBank Gene ID |
Not Available |
| Enzyme 74 GeneCard ID |
CEL |
| Enzyme 74 GenAtlas ID |
CEL |
| Enzyme 74 HGNC ID |
HGNC:1848 |
| Enzyme 74 Chromosome Location |
9 |
| Enzyme 74 Locus |
9q34.3 |
| Enzyme 74 SNPs |
SNPJam Report |
| Enzyme 74 General References |
- Nilsson J, Blackberg L, Carlsson P, Enerback S, Hernell O, Bjursell G: cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur J Biochem. 1990 Sep 11;192(2):543-50. [PubMed ]
- Hui DY, Kissel JA: Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. FEBS Lett. 1990 Dec 10;276(1-2):131-4. [PubMed ]
- Baba T, Downs D, Jackson KW, Tang J, Wang CS: Structure of human milk bile salt activated lipase. Biochemistry. 1991 Jan 15;30(2):500-10. [PubMed ]
- Lidberg U, Nilsson J, Stromberg K, Stenman G, Sahlin P, Enerback S, Bjursell G: Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. Genomics. 1992 Jul;13(3):630-40. [PubMed ]
- Roudani S, Miralles F, Margotat A, Escribano MJ, Lombardo D: Bile salt-dependent lipase transcripts in human fetal tissues. Biochim Biophys Acta. 1995 Oct 17;1264(1):141-50. [PubMed ]
- Madeyski K, Lidberg U, Bjursell G, Nilsson J: Structure and organization of the human carboxyl ester lipase locus. Mamm Genome. 1998 Apr;9(4):334-8. [PubMed ]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
- Hui DY, Hayakawa K, Oizumi J: Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase). Biochem J. 1993 Apr 1;291 ( Pt 1):65-9. [PubMed ]
- Christie DL, Cleverly DR, O'Connor CJ: Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. FEBS Lett. 1991 Jan 28;278(2):190-4. [PubMed ]
- Wang CS, Dashti A, Jackson KW, Yeh JC, Cummings RD, Tang J: Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. Biochemistry. 1995 Aug 22;34(33):10639-44. [PubMed ]
- Mechref Y, Chen P, Novotny MV: Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk. Glycobiology. 1999 Mar;9(3):227-34. [PubMed ]
- Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC: Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 2000 Sep;9(9):1783-90. [PubMed ]
- Raeder H, Johansson S, Holm PI, Haldorsen IS, Mas E, Sbarra V, Nermoen I, Eide SA, Grevle L, Bjorkhaug L, Sagen JV, Aksnes L, Sovik O, Lombardo D, Molven A, Njolstad PR: Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction. Nat Genet. 2006 Jan;38(1):54-62. Epub 2005 Dec 20. [PubMed ]
|
| Enzyme 74 Metabolite References |
Not Available |
|
Enzyme 75
[top]
|
| Enzyme 75 ID |
5474 |
| Enzyme 75 Name |
Lipid phosphate phosphohydrolase 3 |
| Enzyme 75 Synonyms |
- PAP2-beta
- Phosphatidate phosphohydrolase type 2b
- Phosphatidic acid phosphatase 2b
- PAP-2b
- PAP2b
- Vascular endothelial growth factor and type I collagen-inducible protein
- VCIP
|
| Enzyme 75 Gene Name |
PPAP2B |
| Enzyme 75 Protein Sequence |
>Lipid phosphate phosphohydrolase 3
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
|
| Enzyme 75 Number of Residues |
311 |
| Enzyme 75 Molecular Weight |
35115.6 |
| Enzyme 75 Theoretical pI |
9.40 |
| Enzyme 75 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 75 General Function |
Involved in catalytic activity |
| Enzyme 75 Specific Function |
Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is LPA = PA > C-1-P > S-1-P. May be involved in cell adhesion and in cell-cell interactions |
| Enzyme 75 Pathways |
|
| Enzyme 75 Reactions |
- a 1,2-diacylglycerol 3-phosphate + H2O = a 1,2-diacyl-sn-glycerol + phosphate [RN:R02239]
|
| Enzyme 75 Pfam Domain Function |
|
| Enzyme 75 Signals |
|
| Enzyme 75 Transmembrane Regions |
- 34-54
86-106
123-143
194-214
228-248
258-278
|
| Enzyme 75 Essentiality |
Not Available |
| Enzyme 75 GenBank ID Protein |
Not Available |
| Enzyme 75 UniProtKB/Swiss-Prot ID |
O14495 |
| Enzyme 75 UniProtKB/Swiss-Prot Entry Name |
LPP3_HUMAN |
| Enzyme 75 PDB ID |
Not Available |
| Enzyme 75 Cellular Location |
Not Available |
| Enzyme 75 Gene Sequence |
>936 bp
ATGCAAAACTACAAGTACGACAAAGCGATCGTCCCGGAGAGCAAGAACGGCGGCAGCCCG
GCGCTCAACAACAACCCGAGGAGGAGCGGCAGCAAGCGGGTGCTGCTCATCTGCCTCGAC
CTCTTCTGCCTCTTCATGGCGGGCCTCCCCTTCCTCATCATCGAGACAAGCACCATCAAG
CCTTACCACCGAGGGTTTTACTGCAATGATGAGAGCATCAAGTACCCACTGAAAACTGGT
GAGACAATAAATGACGCTGTGCTCTGTGCCGTGGGGATCGTCATTGCCATCCTCGCGATC
ATCACGGGGGAATTCTACCGGATCTATTACCTGAAGAAGTCGCGGTCGACGATTCAGAAC
CCCTACGTGGCAGCACTCTATAAGCAAGTGGGCTGCTTCCTCTTTGGCTGTGCCATCAGC
CAGTCTTTCACAGACATTGCCAAAGTGTCCATAGGGCGCCTGCGTCCTCACTTCTTGAGT
GTCTGCAACCCTGATTTCAGCCAGATCAACTGCTCTGAAGGCTACATTCAGAACTACAGA
TGCAGAGGTGATGACAGCAAAGTCCAGGAAGCCAGGAAGTCCTTCTTCTCTGGCCATGCC
TCCTTCTCCATGTACACTATGCTGTATTTGGTGCTATACCTGCAGGCCCGCTTCACTTGG
CGAGGAGCCCGCCTGCTCCGGCCCCTCCTGCAGTTCACCTTGATCATGATGGCCTTCTAC
ACGGGACTGTCTCGCGTATCAGACCACAAGCACCATCCCAGTGATGTTCTGGCAGGATTT
GCTCAAGGAGCCCTGGTGGCCTGCTGCATAGTTTTCTTCGTGTCTGACCTCTTCAAGACT
AAGACGACGCTCTCCCTGCCTGCCCCTGCTATCCGGAAGGAAATCCTTTCACCTGTGGAC
ATTATTGACAGGAACAATCACCACAACATGATGTAG
|
| Enzyme 75 GenBank Gene ID |
AB000889 |
| Enzyme 75 GeneCard ID |
PPAP2B |
| Enzyme 75 GenAtlas ID |
PPAP2B |
| Enzyme 75 HGNC ID |
HGNC:9229 |
| Enzyme 75 Chromosome Location |
1 |
| Enzyme 75 Locus |
1pter-p22.1 |
| Enzyme 75 SNPs |
SNPJam Report |
| Enzyme 75 General References |
- Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed ]
- Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed ]
- Humtsoe JO, Feng S, Thakker GD, Yang J, Hong J, Wary KK: Regulation of cell-cell interactions by phosphatidic acid phosphatase 2b/VCIP. EMBO J. 2003 Apr 1;22(7):1539-54. [PubMed ]
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, Ricafrente JY, Wentland MA, Lennon G, Gibbs RA: Large-scale concatenation cDNA sequencing. Genome Res. 1997 Apr;7(4):353-8. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Burnett C, Makridou P, Hewlett L, Howard K: Lipid phosphate phosphatases dimerise, but this interaction is not required for in vivo activity. BMC Biochem. 2004 Jan 16;5:2. [PubMed ]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
|
| Enzyme 75 Metabolite References |
Not Available |
|
Enzyme 76
[top]
|
| Enzyme 76 ID |
5477 |
| Enzyme 76 Name |
Pancreatic lipase-related protein 2 |
| Enzyme 76 Synonyms |
- PL-RP2
|
| Enzyme 76 Gene Name |
PNLIPRP2 |
| Enzyme 76 Protein Sequence |
>Pancreatic lipase-related protein 2
MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYT
NENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNC
ICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEA
GRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKV
GHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFL
GYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYK
VSVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKF
LWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPC
|
| Enzyme 76 Number of Residues |
469 |
| Enzyme 76 Molecular Weight |
51946.3 |
| Enzyme 76 Theoretical pI |
5.11 |
| Enzyme 76 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 76 General Function |
Involved in catalytic activity |
| Enzyme 76 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 76 Pathways |
|
| Enzyme 76 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 76 Pfam Domain Function |
|
| Enzyme 76 Signals |
|
| Enzyme 76 Transmembrane Regions |
|
| Enzyme 76 Essentiality |
Not Available |
| Enzyme 76 GenBank ID Protein |
Not Available |
| Enzyme 76 UniProtKB/Swiss-Prot ID |
P54317 |
| Enzyme 76 UniProtKB/Swiss-Prot Entry Name |
LIPR2_HUMAN |
| Enzyme 76 PDB ID |
Not Available |
| Enzyme 76 Cellular Location |
Not Available |
| Enzyme 76 Gene Sequence |
>1410 bp
ATGCTGCCCCCTTGGACCCTCGGCCTTCTCCTGCTGGCCACAGTCAGAGGAAAAGAGGTC
TGCTACGGACAACTTGGCTGCTTTTCTGATGAAAAACCATGGGCAGGAACCCTTCAGCGA
CCTGTAAAATTACTTCCCTGGTCCCCCGAGGACATTGACACCCGCTTTCTTCTGTACACA
AATGAAAATCCAAACAACTTCCAACTAATCACTGGCACGGAACCAGACACCATTGAGGCT
TCAAACTTCCAACTGGACCGCAAGACACGCTTCATCATCCATGGCTTCTTAGACAAGGCG
GAGGACAGCTGGCCATCGGACATGTGCAAGAAAATGTTTGAAGTGGAGAAGGTGAACTGC
ATCTGTGTGGACTGGAGGCACGGGTCCCGGGCAATGTACACCCAAGCCGTGCAAAACATT
CGGGTTGTTGGGGCGGAGACAGCTTTCTTAATACAAGCACTGTCGACGCAGCTAGGGTAC
AGCCTTGAGGACGTGCATGTCATCGGCCACAGCCTGGGCGCGCACACGGCCGCGGAGGCG
GGCAGGAGGCTGGGGGGCCGCGTGGGCAGGATCACAGGGCTGGATCCAGCAGGGCCGTGC
TTCCAGGATGAACCTGAGGAGGTTCGGTTGGATCCATCTGACGCCGTGTTTGTGGATGTG
ATTCACACAGATTCTTCTCCCATAGTTCCTTCCCTAGGTTTCGGAATGAGCCAAAAGGTG
GGCCATCTGGATTTCTTTCCAAATGGAGGAAAGGAAATGCCCGGATGTAAGAAAAATGTC
CTTTCAACCATTACTGATATTGATGGAATATGGGAAGGAATTGGTGGCTTTGTGTCTTGC
AATCACCTAAGAAGCTTCGAGTATTACTCAAGCAGCGTCCTCAACCCTGATGGCTTCCTG
GGCTATCCCTGTGCCTCCTACGATGAGTTTCAGGAGAGTAAGTGTTTCCCTTGTCCAGCT
GAAGGATGCCCCAAAATGGGGCACTATGCTGACCAATTTAAGGGGAAAACAAGTGCTGTG
GAACAAACCTTTTTCCTGAACACAGGAGAGAGTGGTAACTTTACTAGTTGGAGATATAAG
GTATCAGTCACACTTTCTGGAAAAGAGAAAGTGAATGGGTACATCAGGATTGCTTTGTAT
GGAAGTAATGAAAACTCGAAACAATATGAGATTTTCAAAGGATCCCTCAAACCAGATGCA
AGTCACACGTGTGCTATTGATGTGGATTTTAATGTTGGAAAAATACAGAAAGTTAAATTC
CTCTGGAACAAACGTGGGATAAATCTATCTGAGCCCAAACTGGGGGCTTCCCAAATCACA
GTGCAAAGTGGTGAAGATGGGACTGAGTATAATTTTTGTAGCAGCGACACTGTGGAAGAA
AACGTCTTGCAATCTCTTTACCCTTGTTAA
|
| Enzyme 76 GenBank Gene ID |
M93284 |
| Enzyme 76 GeneCard ID |
PNLIPRP2 |
| Enzyme 76 GenAtlas ID |
PNLIPRP2 |
| Enzyme 76 HGNC ID |
HGNC:9157 |
| Enzyme 76 Chromosome Location |
1 |
| Enzyme 76 Locus |
10q25.3 |
| Enzyme 76 SNPs |
SNPJam Report |
| Enzyme 76 General References |
- Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Eydoux C, Spinelli S, Davis TL, Walker JR, Seitova A, Dhe-Paganon S, De Caro A, Cambillau C, Carriere F: Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation. Biochemistry. 2008 Sep 9;47(36):9553-64. Epub 2008 Aug 15. [PubMed ]
|
| Enzyme 76 Metabolite References |
Not Available |
|
Enzyme 77
[top]
|
| Enzyme 77 ID |
5481 |
| Enzyme 77 Name |
Succinate-semialdehyde dehydrogenase, mitochondrial |
| Enzyme 77 Synonyms |
- Aldehyde dehydrogenase family 5 member A1
- NAD(+)-dependent succinic semialdehyde dehydrogenase
|
| Enzyme 77 Gene Name |
ALDH5A1 |
| Enzyme 77 Protein Sequence |
>Succinate-semialdehyde dehydrogenase, mitochondrial
MATCIWLRSCGARRLGSTFPGCRLRPRAGGLVPASGPAPGPAQLRCYAGRLAGLSAALLR
TDSFVGGRWLPAAATFPVQDPASGAALGMVADCGVREARAAVRAAYEAFCRWREVSAKER
SSLLRKWYNLMIQNKDDLARIITAESGKPLKEAHGEILYSAFFLEWFSEEARRVYGDIIH
TPAKDRRALVLKQPIGVAAVITPWNFPSAMITRKVGAALAAGCTVVVKPAEDTPFSALAL
AELASQAGIPSGVYNVIPCSRKNAKEVGEAICTDPLVSKISFTGSTTTGKILLHHAANSV
KRVSMELGGLAPFIVFDSANVDQAVAGAMASKFRNTGQTCVCSNQFLVQRGIHDAFVKAF
AEAMKKNLRVGNGFEEGTTQGPLINEKAVEKVEKQVNDAVSKGATVVTGGKRHQLGKNFF
EPTLLCNVTQDMLCTHEETFGPLAPVIKFDTEEEAIAIANAADVGLAGYFYSQDPAQIWR
VAEQLEVGMVGVNEGLISSVECPFGGVKQSGLGREGSKYGIDEYLELKYVCYGGL
|
| Enzyme 77 Number of Residues |
535 |
| Enzyme 77 Molecular Weight |
57214.2 |
| Enzyme 77 Theoretical pI |
8.37 |
| Enzyme 77 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 77 General Function |
Involved in oxidoreductase activity |
| Enzyme 77 Specific Function |
Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) |
| Enzyme 77 Pathways |
|
| Enzyme 77 Reactions |
- succinate semialdehyde + NAD+ + H2O = succinate + NADH + 2 H+ [RN:R00713]
|
| Enzyme 77 Pfam Domain Function |
|
| Enzyme 77 Signals |
|
| Enzyme 77 Transmembrane Regions |
|
| Enzyme 77 Essentiality |
Not Available |
| Enzyme 77 GenBank ID Protein |
3766467 |
| Enzyme 77 UniProtKB/Swiss-Prot ID |
P51649 |
| Enzyme 77 UniProtKB/Swiss-Prot Entry Name |
SSDH_HUMAN |
| Enzyme 77 PDB ID |
Not Available |
| Enzyme 77 Cellular Location |
Not Available |
| Enzyme 77 Gene Sequence |
>1608 bp
ATGGCGACCTGCATTTGGCTGCGGAGCTGTGGGGCCCGGCGCCTCGGGTCGACGTTTCCA
GGCTGCCGCCTCCGCCCCCGCGCCGGCGGCCTGGTCCCTGCCTCCGGGCCTGCGCCCGGC
CCGGCCCAGCTCCGCTGCTACGCTGGGCGCCTGGCGGGCCTCTCTGCGGCGCTGCTGCGC
ACCGACAGCTTCGTGGGCGGCCGCTGGCTCCCGGCCGCCGCCACCTTCCCCGTGCAAGAC
CCGGCCAGCGGCGCCGCTCTGGGCATGGTAGCCGACTGCGGGGTGCGAGAGGCCCGCGCC
GCCGTGCGCGCTGCCTACGAGGCTTTCTGCCGCTGGAGGGAGGTCTCCGCCAAGGAGAGG
AGTTCATTACTTCGGAAGTGGTACAATTTAATGATACAAAATAAGGATGACCTTGCCAGA
ATAATCACAGCTGAAAGTGGAAAGCCACTGAAGGAGGCACATGGAGAAATTCTCTATTCC
GCCTTTTTCCTAGAGTGGTTCTCTGAGGAAGCCCGCCGTGTTTACGGAGACATTATCCAC
ACCCCGGCAAAGGACAGGCGGGCCCTGGTCCTCAAGCAGCCCATAGGCGTGGCTGCAGTC
ATCACCCCGTGGAATTTCCCCAGTGCCATGATCACCCGGAAGGTGGGGGCCGCCCTGGCA
GCCGGCTGTACTGTCGTGGTGAAGCCTGCCGAAGACACGCCCTTCTCCGCCCTGGCCCTG
GCTGAGCTTGCAAGCCAGGCTGGGATTCCTTCAGGTGTATACAATGTTATTCCCTGTTCT
CGAAAGAATGCCAAGGAAGTAGGGGAGGCAATTTGTACTGATCCTCTGGTGTCCAAAATT
TCCTTTACTGGTTCAACAACTACAGGAAAGATCCTGTTGCACCACGCAGCAAACTCTGTG
AAAAGGGTCTCTATGGAGCTGGGCGGCCTTGCTCCATTTATAGTATTTGACAGTGCCAAC
GTGGACCAGGCTGTAGCAGGGGCCATGGCATCTAAATTTAGGAACACTGGACAGACTTGT
GTTTGCTCAAACCAATTCTTGGTGCAAAGGGGCATCCATGATGCCTTTGTAAAAGCATTC
GCCGAGGCCATGAAGAAGAACCTGCGCGTAGGTAATGGATTTGAGGAAGGAACTACTCAG
GGCCCATTAATTAATGAAAAAGCGGTAGAAAAGGTGGAGAAACAGGTGAATGATGCCGTT
TCTAAAGGTGCCACCGTTGTGACAGGTGGAAAACGACACCAACTTGGAAAAAATTTCTTT
GAGCCTACCCTGCTGTGCAATGTCACCCAGGACATGCTGTGCACTCATGAAGAGACTTTC
GGGCCTCTGGCACCAGTTATCAAGTTCGATACAGAGGAGGAGGCTATAGCAATCGCTAAC
GCAGCTGATGTTGGGTTAGCAGGTTATTTTTACTCTCAAGACCCAGCCCAGATCTGGAGA
GTGGCAGAGCAGCTGGAAGTGGGCATGGTTGGCGTCAACGAAGGATTAATTTCCTCTGTG
GAGTGCCCTTTTGGTGGAGTGAAGCAGTCCGGCCTTGGGCGAGAGGGGTCCAAGTATGGC
ATTGATGAGTATCTGGAACTCAAGTATGTGTGTTACGGGGGCTTGTAG
|
| Enzyme 77 GenBank Gene ID |
Y11192 |
| Enzyme 77 GeneCard ID |
ALDH5A1 |
| Enzyme 77 GenAtlas ID |
ALDH5A1 |
| Enzyme 77 HGNC ID |
HGNC:408 |
| Enzyme 77 Chromosome Location |
6 |
| Enzyme 77 Locus |
6p22.2-p22.3 |
| Enzyme 77 SNPs |
SNPJam Report |
| Enzyme 77 General References |
- Chambliss KL, Hinson DD, Trettel F, Malaspina P, Novelletto A, Jakobs C, Gibson KM: Two exon-skipping mutations as the molecular basis of succinic semialdehyde dehydrogenase deficiency (4-hydroxybutyric aciduria). Am J Hum Genet. 1998 Aug;63(2):399-408. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Chambliss KL, Caudle DL, Hinson DD, Moomaw CR, Slaughter CA, Jakobs C, Gibson KM: Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression. J Biol Chem. 1995 Jan 6;270(1):461-7. [PubMed ]
- Trettel F, Malaspina P, Jodice C, Novelletto A, Slaughter CA, Caudle DL, Hinson DD, Chambliss KL, Gibson KM: Human succinic semialdehyde dehydrogenase. Molecular cloning and chromosomal localization. Adv Exp Med Biol. 1997;414:253-60. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Kim YG, Lee S, Kwon OS, Park SY, Lee SJ, Park BJ, Kim KJ: Redox-switch modulation of human SSADH by dynamic catalytic loop. EMBO J. 2009 Apr 8;28(7):959-68. Epub 2009 Mar 19. [PubMed ]
- Hogema BM, Akaboshi S, Taylor M, Salomons GS, Jakobs C, Schutgens RB, Wilcken B, Worthington S, Maropoulos G, Grompe M, Gibson KM: Prenatal diagnosis of succinic semialdehyde dehydrogenase deficiency: increased accuracy employing DNA, enzyme, and metabolite analyses. Mol Genet Metab. 2001 Mar;72(3):218-22. [PubMed ]
- Aoshima T, Kajita M, Sekido Y, Ishiguro Y, Tsuge I, Kimura M, Yamaguchi S, Watanabe K, Shimokata K, Niwa T: Mutation analysis in a patient with succinic semialdehyde dehydrogenase deficiency: a compound heterozygote with 103-121del and 1460T > A of the ALDH5A1 gene. Hum Hered. 2002;53(1):42-4. [PubMed ]
- Akaboshi S, Hogema BM, Novelletto A, Malaspina P, Salomons GS, Maropoulos GD, Jakobs C, Grompe M, Gibson KM: Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency. Hum Mutat. 2003 Dec;22(6):442-50. [PubMed ]
|
| Enzyme 77 Metabolite References |
Not Available |
|
Enzyme 78
[top]
|
| Enzyme 78 ID |
5483 |
| Enzyme 78 Name |
Coproporphyrinogen-III oxidase, mitochondrial |
| Enzyme 78 Synonyms |
- COX
- Coprogen oxidase
- Coproporphyrinogenase
|
| Enzyme 78 Gene Name |
CPOX |
| Enzyme 78 Protein Sequence |
>Coproporphyrinogen-III oxidase, mitochondrial
MALQLGRLSSGPCWLVARGGCGGPRAWSQCGGGGLRAWSQRSAAGRVCRPPGPAGTEQSR
GLGHGSTSRGGPWVGTGLAAALAGLVGLATAAFGHVQRAEMLPKTSGTRATSLGRPEEEE
DELAHRCSSFMAPPVTDLGELRRRPGDMKTKMELLILETQAQVCQALAQVDGGANFSVDR
WERKEGGGGISCVLQDGCVFEKAGVSISVVHGNLSEEAAKQMRSRGKVLKTKDGKLPFCA
MGVSSVIHPKNPHAPTIHFNYRYFEVEEADGNKQWWFGGGCDLTPTYLNQEDAVHFHRTL
KEACDQHGPDLYPKFKKWCDDYFFIAHRGERRGIGGIFFDDLDSPSKEEVFRFVQSCARA
VVPSYIPLVKKHCDDSFTPQEKLWQQLRRGRYVEFNLLYDRGTKFGLFTPGSRIESILMS
LPLTARWEYMHSPSENSKEAEILEVLRHPRDWVR
|
| Enzyme 78 Number of Residues |
454 |
| Enzyme 78 Molecular Weight |
50151.6 |
| Enzyme 78 Theoretical pI |
8.33 |
| Enzyme 78 GO Classification |
| Function |
- catalytic activity
- coproporphyrinogen oxidase activity
- oxidoreductase activity
- oxidoreductase activity, acting on the CH-CH group of donors
- oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor
|
| Process |
- metabolic process
- nitrogen compound metabolic process
- oxidation reduction
- porphyrin biosynthetic process
- porphyrin metabolic process
- tetrapyrrole metabolic process
|
| Component |
| — |
|
| Enzyme 78 General Function |
Involved in coproporphyrinogen oxidase activity |
| Enzyme 78 Specific Function |
Key enzyme in heme biosynthesis. Catalyzes the oxidative decarboxylation of propionic acid side chains of rings A and B of coproporphyrinogen III |
| Enzyme 78 Pathways |
|
| Enzyme 78 Reactions |
- coproporphyrinogen III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O [RN:R03220]
|
| Enzyme 78 Pfam Domain Function |
|
| Enzyme 78 Signals |
|
| Enzyme 78 Transmembrane Regions |
|
| Enzyme 78 Essentiality |
Not Available |
| Enzyme 78 GenBank ID Protein |
Not Available |
| Enzyme 78 UniProtKB/Swiss-Prot ID |
P36551 |
| Enzyme 78 UniProtKB/Swiss-Prot Entry Name |
HEM6_HUMAN |
| Enzyme 78 PDB ID |
Not Available |
| Enzyme 78 Cellular Location |
Not Available |
| Enzyme 78 Gene Sequence |
>1365 bp
ATGGCCTTGCAGCTGGGCAGGCTGAGCTCGGGCCCCTGCTGGCTCGTGGCGCGGGGCGGC
TGCGGAGGGCCCCGCGCCTGGTCCCAGTGCGGCGGCGGAGGGCTCCGAGCCTGGTCCCAG
CGCAGCGCAGCCGGACGCGTCTGCCGGCCCCCTGGCCCGGCTGGCACGGAGCAGAGCCGC
GGGCTGGGGCACGGCTCGACGTCGAGAGGCGGCCCCTGGGTGGGGACAGGGCTGGCCGCG
GCGCTGGCGGGGTTGGTGGGGCTGGCCACCGCCGCCTTCGGGCATGTGCAGCGGGCGGAG
ATGTTGCCTAAGACCTCGGGGACGCGGGCCACTTCGCTGGGGAGGCCGGAGGAGGAGGAG
GATGAGCTGGCCCACCGCTGCAGCAGCTTCATGGCCCCGCCTGTGACCGACCTGGGCGAG
CTGCGAAGGAGGCCGGGCGACATGAAGACCAAGATGGAGCTGCTGATTCTGGAGACCCAG
GCCCAGGTGTGCCAGGCTCTGGCACAGGTAGACGGGGGCGCCAACTTTTCTGTGGACCGG
TGGGAGAGGAAGGAAGGAGGTGGCGGCATCAGCTGTGTACTTCAAGATGGGTGTGTTTTC
GAAAAGGCTGGGGTGAGCATTTCTGTTGTTCATGGAAATCTTTCAGAGGAAGCTGCAAAA
CAAATGAGAAGCAGAGGAAAAGTTCTGAAGACTAAAGATGGTAAATTGCCATTTTGTGCT
ATGGGCGTGAGCTCTGTTATCCACCCCAAGAATCCTCATGCTCCTACTATCCATTTCAAC
TACAGATACTTTGAAGTAGAAGAAGCTGATGGCAACAAGCAGTGGTGGTTTGGTGGTGGA
TGTGACCTCACTCCAACATACTTGAATCAAGAAGACGCTGTCCATTTTCACAGAACTCTG
AAGGAGGCTTGTGACCAGCATGGTCCAGATCTCTACCCCAAATTTAAAAAATGGTGTGAT
GATTACTTCTTTATAGCCCATCGTGGAGAACGGCGGGGCATTGGTGGTATCTTTTTTGAT
GATCTTGACTCTCCGTCCAAGGAGGAGGTGTTTCGCTTTGTACAGAGCTGTGCCAGGGCT
GTAGTTCCTTCTTACATTCCCCTTGTGAAAAAGCACTGTGATGACTCATTCACCCCCCAG
GAGAAGCTGTGGCAGCAGCTCAGAAGAGGACGGTATGTAGAATTTAATCTGCTGTATGAT
CGGGGCACAAAGTTTGGCCTCTTCACTCCAGGATCCAGAATTGAAAGTATCTTGATGTCT
TTACCTCTAACTGCCCGATGGGAGTACATGCATTCACCCTCAGAGAATTCCAAAGAAGCT
GAAATTCTGGAAGTTCTACGCCATCCAAGGGACTGGGTGCGTTGA
|
| Enzyme 78 GenBank Gene ID |
AK290140 |
| Enzyme 78 GeneCard ID |
CPOX |
| Enzyme 78 GenAtlas ID |
CPOX |
| Enzyme 78 HGNC ID |
HGNC:2321 |
| Enzyme 78 Chromosome Location |
3 |
| Enzyme 78 Locus |
3q12 |
| Enzyme 78 SNPs |
SNPJam Report |
| Enzyme 78 General References |
- Delfau-Larue MH, Martasek P, Grandchamp B: Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping. Hum Mol Genet. 1994 Aug;3(8):1325-30. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Taketani S, Kohno H, Furukawa T, Yoshinaga T, Tokunaga R: Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase. Biochim Biophys Acta. 1994 Jan 4;1183(3):547-9. [PubMed ]
- Martasek P, Camadro JM, Delfau-Larue MH, Dumas JB, Montagne JJ, de Verneuil H, Labbe P, Grandchamp B: Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase. Proc Natl Acad Sci U S A. 1994 Apr 12;91(8):3024-8. [PubMed ]
- Susa S, Daimon M, Ono H, Li S, Yoshida T, Kato T: The long, but not the short, presequence of human coproporphyrinogen oxidase is essential for its import and sorting to mitochondria. Tohoku J Exp Med. 2003 May;200(1):39-45. [PubMed ]
- Lee DS, Flachsova E, Bodnarova M, Demeler B, Martasek P, Raman CS: Structural basis of hereditary coproporphyria. Proc Natl Acad Sci U S A. 2005 Oct 4;102(40):14232-7. Epub 2005 Sep 21. [PubMed ]
- Martasek P, Nordmann Y, Grandchamp B: Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms. Hum Mol Genet. 1994 Mar;3(3):477-80. [PubMed ]
- Fujita H, Kondo M, Taketani S, Nomura N, Furuyama K, Akagi R, Nagai T, Terajima M, Galbraith RA, Sassa S: Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria. Hum Mol Genet. 1994 Oct;3(10):1807-10. [PubMed ]
- Lamoril J, Martasek P, Deybach JC, Da Silva V, Grandchamp B, Nordmann Y: A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria. Hum Mol Genet. 1995 Feb;4(2):275-8. [PubMed ]
- Daimon M, Gojyou E, Sugawara M, Yamatani K, Tominaga M, Sasaki H: A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria. Hum Genet. 1997 Feb;99(2):199-201. [PubMed ]
- Lamoril J, Deybach JC, Puy H, Grandchamp B, Nordmann Y: Three novel mutations in the coproporphyrinogen oxidase gene. Hum Mutat. 1997;9(1):78-80. [PubMed ]
- Schreiber WE, Zhang X, Senz J, Jamani A: Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene. Hum Mutat. 1997;10(3):196-200. [PubMed ]
- Rosipal R, Lamoril J, Puy H, Da Silva V, Gouya L, De Rooij FW, Te Velde K, Nordmann Y, Martasek P, Deybach JC: Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update. Hum Mutat. 1999;13(1):44-53. [PubMed ]
- Wiman A, Floderus Y, Harper P: Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria. J Hum Genet. 2002;47(8):407-12. [PubMed ]
- To-Figueras J, Badenas C, Enriquez MT, Segura S, Alvarez C, Mila M, Lecha M, Herrero C: Biochemical and genetic characterization of four cases of hereditary coproporphyria in Spain. Mol Genet Metab. 2005 Jun;85(2):160-3. Epub 2005 Feb 25. [PubMed ]
- Akagi R, Inoue R, Muranaka S, Tahara T, Taketani S, Anderson KE, Phillips JD, Sassa S: Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient. Br J Haematol. 2006 Jan;132(2):237-43. [PubMed ]
|
| Enzyme 78 Metabolite References |
Not Available |
|
Enzyme 79
[top]
|
| Enzyme 79 ID |
5484 |
| Enzyme 79 Name |
Peptidyl-glycine alpha-amidating monooxygenase |
| Enzyme 79 Synonyms |
- PAM
- Peptidylglycine alpha-hydroxylating monooxygenase
- PHM
- Peptidyl-alpha-hydroxyglycine alpha-amidating lyase
- Peptidylamidoglycolate lyase
- PAL
|
| Enzyme 79 Gene Name |
PAM |
| Enzyme 79 Protein Sequence |
>Peptidyl-glycine alpha-amidating monooxygenase
MAGRVPSLLVLLVFPSSCLAFRSPLSVFKRFKETTRPFSNECLGTTRPVVPIDSSDFALD
IRMPGVTPKQSDTYFCMSMRIPVDEEAFVIDFKPRASMDTVHHMLLFGCNMPSSTGSYWF
CDEGTCTDKANILYAWARNAPPTRLPKGVGFRVGGETGSKYFVLQVHYGDISAFRDNNKD
CSGVSLHLTRLPQPLIAGMYLMMSVDTVIPAGEKVVNSDISCHYKNYPMHVFAYRVHTHH
LGKVVSGYRVRNGQWTLIGRQSPQLPQAFYPVGHPVDVSFGDLLAARCVFTGEGRTEATH
IGGTSSDEMCNLYIMYYMEAKHAVSFMTCTQNVAPDMFRTIPPEANIPIPVKSDMVMMHE
HHKETEYKDKIPLLQQPKREEEEVLDQGDFYSLLSKLLGEREDVVHVHKYNPTEKAESES
DLVAEIANVVQKKDLGRSDAREGAEHERGNAILVRDRIHKFHRLVSTLRPPESRVFSLQQ
PPPGEGTWEPEHTGDFHMEEALDWPGVYLLPGQVSGVALDPKNNLVIFHRGDHVWDGNSF
DSKFVYQQIGLGPIEEDTILVIDPNNAAVLQSSGKNLFYLPHGLSIDKDGNYWVTDVALH
QVFKLDPNNKEGPVLILGRSMQPGSDQNHFCQPTDVAVDPGTGAIYVSDGYCNSRIVQFS
PSGKFITQWGEESSGSSPLPGQFTVPHSLALVPLLGQLCVADRENGRIQCFKTDTKEFVR
EIKHSSFGRNVFAISYIPGLLFAVNGKPHFGDQEPVQGFVMNFSNGEIIDIFKPVRKHFD
MPHDIVASEDGTVYIGDAHTNTVWKFTLTEKLEHRSVKKAGIEVQEIKEAEAVVETKMEN
KPTSSELQKMQEKQKLIKEPGSGVPVVLITTLLVIPVVVLLAIAIFIRWKKSRAFGDSEH
KLETSSGRVLGRFRGKGSGGLNLGNFFASRKGYSRKGFDRLSTEGSDQEKEDDGSESEEE
YSAPLPALAPSSS
|
| Enzyme 79 Number of Residues |
973 |
| Enzyme 79 Molecular Weight |
108331.3 |
| Enzyme 79 Theoretical pI |
6.39 |
| Enzyme 79 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- copper ion binding
- ion binding
- metal ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
- peptidylglycine monooxygenase activity
- transition metal ion binding
|
| Process |
- cellular metabolic process
- cellular process
- metabolic process
- oxidation reduction
- peptide metabolic process
|
| Component |
|
|
| Enzyme 79 General Function |
Involved in monooxygenase activity |
| Enzyme 79 Specific Function |
Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity |
| Enzyme 79 Pathways |
Not Available |
| Enzyme 79 Reactions |
- peptidylamidoglycolate = peptidyl amide + glyoxylate [RN:R03874]
|
| Enzyme 79 Pfam Domain Function |
|
| Enzyme 79 Signals |
|
| Enzyme 79 Transmembrane Regions |
|
| Enzyme 79 Essentiality |
Not Available |
| Enzyme 79 GenBank ID Protein |
24430388 |
| Enzyme 79 UniProtKB/Swiss-Prot ID |
P19021 |
| Enzyme 79 UniProtKB/Swiss-Prot Entry Name |
AMD_HUMAN |
| Enzyme 79 PDB ID |
1SDW |
| Enzyme 79 PDB File |
Show |
| Enzyme 79 3D Structure |
|
| Enzyme 79 Cellular Location |
Not Available |
| Enzyme 79 Gene Sequence |
>2922 bp
ATGGCTGGCCGCGTCCCTAGCCTGCTAGTTCTCCTTGTTTTTCCAAGCAGCTGTTTGGCT
TTCCGAAGCCCACTTTCTGTCTTTAAGAGGTTTAAAGAAACTACCAGACCATTTTCCAAT
GAATGTCTTGGTACCACCAGACCCGTAGTTCCTATTGATTCATCAGATTTTGCATTGGAT
ATTCGCATGCCTGGGGTTACACCTAAACAGTCCGATACATACTTCTGCATGTCTATGCGA
ATACCAGTGGATGAGGAAGCCTTCGTGATTGACTTCAAGCCTCGAGCCAGCATGGATACT
GTCCATCACATGTTACTTTTTGGATGCAATATGCCTTCATCCACTGGAAGTTACTGGTTT
TGTGATGAAGGAACCTGTACAGATAAAGCCAATATTCTGTATGCCTGGGCGAGAAATGCT
CCCCCTACCCGGCTCCCCAAAGGTGTTGGATTCAGAGTTGGAGGAGAGACTGGAAGTAAA
TACTTTGTACTACAGGTACACTATGGGGATATTAGTGCTTTTAGAGATAATAACAAGGAC
TGTTCTGGTGTGTCCTTACACCTCACACGTCTGCCACAGCCTTTAATTGCTGGCATGTAC
CTTATGATGTCTGTTGACACTGTTATCCCAGCAGGAGAAAAAGTGGTGAATTCTGACATT
TCATGCCATTATAAAAATTATCCAATGCATGTCTTTGCCTATAGAGTTCACACTCACCAT
TTAGGTAAGGTAGTAAGTGGATACAGAGTAAGAAATGGACAGTGGACACTGATTGGACGG
CAGAGCCCTCAGCTGCCACAGGCTTTCTACCCTGTGGGGCATCCAGTTGATGTAAGTTTT
GGTGACCTACTGGCTGCAAGATGTGTATTCACTGGTGAAGGAAGGACAGAAGCCACACAC
ATTGGTGGCACGTCTAGTGATGAAATGTGCAACTTATACATTATGTATTACATGGAAGCC
AAGCATGCAGTTTCTTTCATGACCTGTACCCAGAATGTAGCTCCAGATATGTTCAGAACC
ATACCACCAGAGGCCAACATTCCAATTCCCGTGAAGTCTGATATGGTTATGATGCATGAA
CATCATAAAGAAACAGAATATAAAGATAAGATTCCTTTACTACAGCAGCCAAAACGAGAA
GAAGAAGAAGTGTTAGACCAGGGTGATTTCTATTCACTACTTTCCAAGCTGCTAGGAGAA
AGGGAAGATGTTGTTCATGTGCACAAATATAATCCTACAGAAAAGGCAGAATCAGAGTCA
GACCTGGTAGCTGAGATTGCAAATGTAGTCCAAAAAAAGGATCTTGGTCGATCTGATGCC
AGAGAGGGTGCAGAACATGAGAGGGGTAATGCTATTCTTGTCAGAGACAGAATTCACAAA
TTCCACAGACTAGTATCTACCTTGAGGCCACCAGAGAGCAGAGTTTTCTCATTACAGCAG
CCCCCACCTGGTGAAGGCACCTGGGAACCAGAACACACAGGAGATTTCCACATGGAAGAG
GCACTGGATTGGCCTGGAGTATACTTGTTACCAGGCCAGGTTTCTGGGGTGGCTCTAGAC
CCTAAGAATAACCTGGTGATTTTCCACAGAGGTGACCATGTCTGGGATGGAAACTCGTTT
GACAGCAAGTTTGTTTACCAGCAAATAGGACTCGGACCAATTGAAGAAGACACTATTCTT
GTCATAGATCCAAATAATGCTGCAGTACTCCAGTCCAGTGGAAAAAATCTGTTTTACTTG
CCACATGGCTTGAGTATAGATAAAGATGGGAATTATTGGGTCACAGACGTGGCTCTCCAT
CAGGTGTTCAAACTGGATCCAAACAATAAAGAAGGCCCTGTATTAATCCTGGGAAGGAGC
ATGCAACCAGGCAGTGACCAGAATCACTTCTGTCAACCCACTGATGTGGCTGTGGATCCA
GGCACTGGAGCCATTTATGTATCAGATGGTTACTGCAACAGCAGGATTGTGCAGTTTTCA
CCAAGTGGAAAGTTCATCACACAGTGGGGAGAAGAGTCTTCAGGGAGCAGTCCTCTGCCA
GGCCAGTTCACTGTTCCTCACAGCTTGGCTCTTGTGCCTCTTTTGGGCCAATTATGTGTG
GCAGACCGGGAAAATGGTCGGATCCAGTGTTTTAAAACTGACACCAAAGAATTTGTGAGA
GAGATTAAGCATTCATCATTTGGAAGAAATGTATTTGCAATTTCATATATACCAGGCTTG
CTCTTTGCAGTGAATGGGAAGCCTCATTTTGGGGACCAAGAACCTGTACAAGGATTTGTG
ATGAACTTTTCCAATGGGGAAATTATCGACATCTTCAAGCCAGTGCGCAAGCACTTTGAT
ATGCCTCATGATATTGTTGCATCTGAAGATGGGACTGTGTACATTGGAGATGCTCATACC
AACACCGTGTGGAAGTTCACCTTGACTGAGAAATTGGAACATCGATCAGTTAAAAAGGCT
GGCATTGAGGTCCAGGAAATCAAAGAAGCCGAGGCAGTTGTTGAAACCAAAATGGAGAAC
AAACCCACCTCCTCAGAATTGCAGAAGATGCAAGAGAAACAGAAACTGATCAAAGAGCCA
GGCTCGGGAGTGCCTGTTGTTCTCATTACAACCCTTCTGGTTATTCCGGTGGTTGTCCTG
CTGGCCATTGCCATATTTATTCGGTGGAAAAAATCAAGGGCCTTTGGAGATTCTGAACAC
AAACTCGAGACGAGTTCAGGAAGAGTACTGGGAAGATTTAGAGGAAAGGGAAGTGGAGGC
TTAAACCTTGGTAATTTCTTTGCAAGCCGTAAGGGCTACAGTCGAAAAGGGTTTGACCGG
CTTAGCACTGAGGGCAGTGACCAAGAGAAAGAGGATGATGGAAGTGAATCAGAAGAGGAG
TATTCAGCACCTCTGCCTGCGCTCGCACCTTCCTCCTCCTGA
|
| Enzyme 79 GenBank Gene ID |
AB095007 |
| Enzyme 79 GeneCard ID |
PAM |
| Enzyme 79 GenAtlas ID |
PAM |
| Enzyme 79 HGNC ID |
HGNC:8596 |
| Enzyme 79 Chromosome Location |
5 |
| Enzyme 79 Locus |
5q14-q21 |
| Enzyme 79 SNPs |
SNPJam Report |
| Enzyme 79 General References |
- Glauder J, Ragg H, Rauch J, Engels JW: Human peptidylglycine alpha-amidating monooxygenase: cDNA, cloning and functional expression of a truncated form in COS cells. Biochem Biophys Res Commun. 1990 Jun 15;169(2):551-8. [PubMed ]
- Tateishi K, Arakawa F, Misumi Y, Treston AM, Vos M, Matsuoka Y: Isolation and functional expression of human pancreatic peptidylglycine alpha-amidating monooxygenase. Biochem Biophys Res Commun. 1994 Nov 30;205(1):282-90. [PubMed ]
- Satani M, Takahashi K, Sakamoto H, Harada S, Kaida Y, Noguchi M: Expression and characterization of human bifunctional peptidylglycine alpha-amidating monooxygenase. Protein Expr Purif. 2003 Apr;28(2):293-302. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Yun HY, Keutmann HT, Eipper BA: Alternative splicing governs sulfation of tyrosine or oligosaccharide on peptidylglycine alpha-amidating monooxygenase. J Biol Chem. 1994 Apr 8;269(14):10946-55. [PubMed ]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed ]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed ]
|
| Enzyme 79 Metabolite References |
Not Available |
|
Enzyme 80
[top]
|
| Enzyme 80 ID |
5485 |
| Enzyme 80 Name |
Dopamine beta-hydroxylase |
| Enzyme 80 Synonyms |
- Dopamine beta-monooxygenase
- Soluble dopamine beta-hydroxylase
|
| Enzyme 80 Gene Name |
DBH |
| Enzyme 80 Protein Sequence |
>Dopamine beta-hydroxylase
MPALSRWASLPGPSMREAAFMYSTAVAIFLVILVAALQGSAPRESPLPYHIPLDPEGSLE
LSWNVSYTQEAIHFQLLVRRLKAGVLFGMSDRGELENADLVVLWTDGDTAYFADAWSDQK
GQIHLDPQQDYQLLQVQRTPEGLTLLFKRPFGTCDPKDYLIEDGTVHLVYGILEEPFRSL
EAINGSGLQMGLQRVQLLKPNIPEPELPSDACTMEVQAPNIQIPSQETTYWCYIKELPKG
FSRHHIIKYEPIVTKGNEALVHHMEVFQCAPEMDSVPHFSGPCDSKMKPDRLNYCRHVLA
AWALGAKAFYYPEEAGLAFGGPGSSRYLRLEVHYHNPLVIEGRNDSSGIRLYYTAKLRRF
NAGIMELGLVYTPVMAIPPRETAFILTGYCTDKCTQLALPPSGIHIFASQLHTHLTGRKV
VTVLVRDGREWEIVNQDNHYSPHFQEIRMLKKVVSVHPGDVLITSCTYNTEDRELATVGG
FGILEEMCVNYVHYYPQTQLELCKSAVDAGFLQKYFHLINRFNNEDVCTCPQASVSQQFT
SVPWNSFNRDVLKALYSFAPISMHCNKSSAVRFQGEWNLQPLPKVISTLEEPTPQCPTSQ
GRSPAGPTVVSIGGGKG
|
| Enzyme 80 Number of Residues |
617 |
| Enzyme 80 Molecular Weight |
69064.4 |
| Enzyme 80 Theoretical pI |
6.39 |
| Enzyme 80 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- copper ion binding
- dopamine beta-monooxygenase activity
- ion binding
- metal ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen
- transition metal ion binding
|
| Process |
- catecholamine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular amino acid metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- cellular process
- histidine catabolic process
- histidine family amino acid metabolic process
- histidine metabolic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 80 General Function |
Involved in monooxygenase activity |
| Enzyme 80 Specific Function |
Conversion of dopamine to noradrenaline |
| Enzyme 80 Pathways |
|
| Enzyme 80 Reactions |
- 3,4-dihydroxyphenethylamine + ascorbate + O2 = noradrenaline + dehydroascorbate + H2O [RN:R02535]
|
| Enzyme 80 Pfam Domain Function |
|
| Enzyme 80 Signals |
|
| Enzyme 80 Transmembrane Regions |
|
| Enzyme 80 Essentiality |
Not Available |
| Enzyme 80 GenBank ID Protein |
123230459 |
| Enzyme 80 UniProtKB/Swiss-Prot ID |
P09172 |
| Enzyme 80 UniProtKB/Swiss-Prot Entry Name |
DOPO_HUMAN |
| Enzyme 80 PDB ID |
Not Available |
| Enzyme 80 Cellular Location |
Not Available |
| Enzyme 80 Gene Sequence |
>1854 bp
ATGCCCGCCCTCAGTCGCTGGGCCAGCCTGCCCGGCCCCAGCATGCGGGAGGCAGCCTTC
ATGTACAGCACAGCAGTGGCCATCTTCCTGGTCATCCTGGTGGCCGCACTGCAGGGCTCG
GCTCCCCGTGAGAGCCCCCTCCCCTATCACATCCCCCTGGACCCGGAGGGGTCCCTGGAG
CTCTCATGGAATGTCAGCTACACCCAGGAGGCCATCCATTTCCAGCTCCTGGTGCGGAGG
CTCAAGGCTGGCGTCCTGTTTGGGATGTCCGACCGTGGCGAGCTTGAGAACGCAGATCTC
GTGGTGCTCTGGACCGATGGGGACACTGCCTATTTTGCGGACGCCTGGAGTGACCAGAAG
GGGCAGATCCACCTGGATCCCCAGCAGGACTACCAGCTGCTGCAGGTGCAGAGGACCCCA
GAAGGCCTGACCCTGCTTTTCAAGAGGCCCTTTGGCACCTGCGACCCCAAGGATTACCTC
ATTGAAGACGGCACTGTCCACTTGGTCTACGGGATCCTGGAGGAGCCGTTCCGGTCACTG
GAGGCCATCAACGGCTCGGGCCTGCAGATGGGGCTGCAGAGGGTGCAGCTCCTGAAGCCC
AATATCCCCGAACCGGAGTTGCCCTCAGACGCGTGCACCATGGAGGTCCAAGCTCCCAAT
ATCCAGATCCCCAGCCAGGAGACCACGTACTGGTGCTACATTAAGGAGCTTCCAAAGGGC
TTCTCTCGGCACCACATTATCAAGTACGAGCCCATCGTCACCAAGGGCAATGAGGCCCTT
GTCCACCACATGGAAGTCTTCCAGTGCGCCCCCGAGATGGACAGCGTCCCCCACTTCAGC
GGGCCCTGCGACTCCAAGATGAAACCCGACCGCCTCAACTACTGCCGCCACGTGCTGGCC
GCCTGGGCCCTGGGTGCCAAGGCATTTTACTACCCAGAGGAAGCCGGCCTTGCCTTCGGG
GGTCCAGGGTCCTCCAGATATCTCCGCCTGGAAGTTCACTACCACAACCCACTGGTGATA
GAAGGACGAAACGACTCCTCAGGCATCCGCTTGTACTACACAGCCAAGCTGCGGCGCTTC
AACGCGGGGATCATGGAGCTGGGACTGGTGTACACGCCAGTGATGGCCATTCCACCACGG
GAGACCGCCTTCATCCTCACTGGCTACTGCACGGACAAGTGCACCCAGCTGGCACTGCCT
CCCTCCGGGATCCACATCTTCGCCTCTCAGCTCCACACACACCTGACTGGGAGAAAGGTG
GTCACAGTGCTGGTCCGGGACGGCCGGGAGTGGGAGATCGTGAACCAGGACAATCACTAC
AGCCCTCACTTCCAGGAGATCCGCATGTTGAAGAAGGTCGTGTCGGTCCATCCGGGAGAT
GTGCTCATCACCTCCTGCACGTACAACACAGAAGACCGGGAGCTGGCCACAGTGGGGGGC
TTCGGGATCCTGGAGGAGATGTGTGTCAACTACGTGCACTACTACCCCCAGACGCAGCTG
GAGCTCTGCAAGAGCGCTGTGGACGCCGGCTTCCTGCAGAAGTACTTCCACCTCATCAAC
AGGTTCAACAACGAGGATGTCTGCACCTGCCCTCAGGCGTCCGTGTCTCAGCAGTTCACC
TCTGTTCCCTGGAACTCCTTCAACCGCGACGTACTGAAGGCCCTGTACAGCTTCGCGCCC
ATCTCCATGCACTGCAACAAGTCCTCAGCCGTCCGCTTCCAGGGTGAATGGAACCTGCAG
CCCCTGCCCAAGGTCATCTCCACACTGGAAGAGCCCACCCCACAGTGCCCCACCAGCCAG
GGCCGAAGCCCTGCTGGCCCCACCGTTGTCAGCATTGGTGGGGGCAAAGGCTGA
|
| Enzyme 80 GenBank Gene ID |
AL365494 |
| Enzyme 80 GeneCard ID |
DBH |
| Enzyme 80 GenAtlas ID |
DBH |
| Enzyme 80 HGNC ID |
HGNC:2689 |
| Enzyme 80 Chromosome Location |
9 |
| Enzyme 80 Locus |
9q34 |
| Enzyme 80 SNPs |
SNPJam Report |
| Enzyme 80 General References |
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
- Lamouroux A, Vigny A, Faucon Biguet N, Darmon MC, Franck R, Henry JP, Mallet J: The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme. EMBO J. 1987 Dec 20;6(13):3931-7. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Kobayashi K, Kurosawa Y, Fujita K, Nagatsu T: Human dopamine beta-hydroxylase gene: two mRNA types having different 3'-terminal regions are produced through alternative polyadenylation. Nucleic Acids Res. 1989 Feb 11;17(3):1089-102. [PubMed ]
- Li B, Tsing S, Kosaka AH, Nguyen B, Osen EG, Bach C, Chan H, Barnett J: Expression of human dopamine beta-hydroxylase in Drosophila Schneider 2 cells. Biochem J. 1996 Jan 1;313 ( Pt 1):57-64. [PubMed ]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed ]
- Williams HJ, Bray N, Murphy KC, Cardno AG, Jones LA, Owen MJ: No evidence for allelic association between schizophrenia and a functional variant of the human dopamine beta-hydroxylase gene (DBH). Am J Med Genet. 1999 Oct 15;88(5):557-9. [PubMed ]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]
- Halushka MK, Fan JB, Bentley K, Hsie L, Shen N, Weder A, Cooper R, Lipshutz R, Chakravarti A: Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis. Nat Genet. 1999 Jul;22(3):239-47. [PubMed ]
- Kim CH, Zabetian CP, Cubells JF, Cho S, Biaggioni I, Cohen BM, Robertson D, Kim KS: Mutations in the dopamine beta-hydroxylase gene are associated with human norepinephrine deficiency. Am J Med Genet. 2002 Mar 1;108(2):140-7. [PubMed ]
|
| Enzyme 80 Metabolite References |
Not Available |
|
Enzyme 81
[top]
|
| Enzyme 81 ID |
5496 |
| Enzyme 81 Name |
Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating |
| Enzyme 81 Synonyms |
- Protein H105e3
|
| Enzyme 81 Gene Name |
NSDHL |
| Enzyme 81 Protein Sequence |
>Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
MEPAVSEPMRDQVARTHLTEDTPKVNADIEKVNQNQAKRCTVIGGSGFLGQHMVEQLLAR
GYAVNVFDIQQGFDNPQVRFFLGDLCSRQDLYPALKGVNTVFHCASPPPSSNNKELFYRV
NYIGTKNVIETCKEAGVQKLILTSSASVIFEGVDIKNGTEDLPYAMKPIDYYTETKILQE
RAVLGANDPEKNFLTTAIRPHGIFGPRDPQLVPILIEAARNGKMKFVIGNGKNLVDFTFV
ENVVHGHILAAEQLSRDSTLGGKAFHITNDEPIPFWTFLSRILTGLNYEAPKYHIPYWVA
YYLALLLSLLVMVISPVIQLQPTFTPMRVALAGTFHYYSCERAKKAMGYQPLVTMDDAME
RTVQSFRHLRRVK
|
| Enzyme 81 Number of Residues |
373 |
| Enzyme 81 Molecular Weight |
41900.0 |
| Enzyme 81 Theoretical pI |
8.20 |
| Enzyme 81 GO Classification |
| Function |
- 3-beta-hydroxy-delta5-steroid dehydrogenase activity
- binding
- catalytic activity
- oxidoreductase activity
- steroid dehydrogenase activity
- steroid dehydrogenase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
- steroid biosynthetic process
- steroid metabolic process
|
| Component |
| — |
|
| Enzyme 81 General Function |
Involved in 3-beta-hydroxy-delta5-steroid dehydrogenase activity |
| Enzyme 81 Specific Function |
3-beta-hydroxy-4-beta-methyl-5-alpha-cholest- 7-ene-4-alpha-carboxylate + NAD(P)(+) = 4-alpha-methyl-5-alpha- cholest-7-en-3-one + CO(2) + NAD(P)H |
| Enzyme 81 Pathways |
Not Available |
| Enzyme 81 Reactions |
- 3beta-hydroxy-4beta-methyl-5alpha-cholest-7-ene-4alpha-carboxylate + NAD(P)+ = 4alpha-methyl-5alpha-cholest-7-en-3-one + CO2 + NAD(P)H [RN:R04483 R07149]
|
| Enzyme 81 Pfam Domain Function |
|
| Enzyme 81 Signals |
|
| Enzyme 81 Transmembrane Regions |
|
| Enzyme 81 Essentiality |
Not Available |
| Enzyme 81 GenBank ID Protein |
Not Available |
| Enzyme 81 UniProtKB/Swiss-Prot ID |
Q15738 |
| Enzyme 81 UniProtKB/Swiss-Prot Entry Name |
NSDHL_HUMAN |
| Enzyme 81 PDB ID |
Not Available |
| Enzyme 81 Cellular Location |
Not Available |
| Enzyme 81 Gene Sequence |
>1122 bp
ATGGAACCAGCAGTTAGCGAGCCAATGAGAGACCAAGTCGCACGGACTCATTTGACAGAG
GACACTCCCAAAGTGAATGCTGACATAGAAAAGGTTAACCAGAATCAGGCCAAGAGATGC
ACAGTGATCGGTGGCTCTGGATTCCTGGGGCAGCACATGGTGGAGCAGTTGCTGGCAAGA
GGATATGCTGTCAATGTATTTGATATCCAGCAAGGGTTTGATAATCCCCAGGTGCGGTTC
TTTCTGGGTGACCTCTGCAGCCGACAGGATCTGTACCCAGCTCTGAAAGGTGTAAACACA
GTTTTCCACTGTGCGTCACCCCCACCATCCAGTAACAACAAGGAGCTCTTTTATAGAGTG
AATTACATTGGCACCAAGAATGTCATTGAAACTTGCAAAGAGGCTGGGGTTCAGAAACTC
ATTTTAACCAGCAGTGCCAGTGTCATCTTTGAGGGCGTCGATATCAAGAATGGAACTGAA
GACCTTCCCTATGCCATGAAACCCATTGACTACTACACAGAGACTAAGATCTTACAGGAG
AGGGCAGTTCTGGGCGCCAACGATCCTGAGAAGAATTTCTTAACCACAGCCATCCGCCCT
CATGGCATTTTCGGCCCAAGGGACCCGCAGTTGGTACCCATCCTCATCGAGGCAGCCAGG
AACGGCAAGATGAAGTTCGTGATTGGAAATGGGAAGAACTTGGTGGACTTCACCTTTGTG
GAGAACGTGGTCCATGGACACATCCTGGCGGCAGAGCAGCTCTCCCGAGACTCGACACTG
GGTGGGAAGGCATTTCACATCACCAATGATGAGCCCATCCCTTTCTGGACATTCCTGTCT
CGCATCCTGACAGGCCTCAATTATGAGGCCCCCAAGTACCACATCCCCTACTGGGTGGCC
TACTACCTGGCCCTCCTGCTATCCCTGCTGGTGATGGTGATCAGTCCTGTCATCCAGCTG
CAGCCCACCTTCACACCCATGCGGGTCGCACTGGCTGGCACATTCCACTACTACAGCTGC
GAGAGAGCCAAAAAGGCCATGGGCTACCAGCCACTAGTGACCATGGATGATGCTATGGAG
AGGACCGTGCAGAGCTTTCGCCACCTGCGGAGGGTCAAGTGA
|
| Enzyme 81 GenBank Gene ID |
U47105 |
| Enzyme 81 GeneCard ID |
NSDHL |
| Enzyme 81 GenAtlas ID |
NSDHL |
| Enzyme 81 HGNC ID |
HGNC:13398 |
| Enzyme 81 Chromosome Location |
Not Available |
| Enzyme 81 Locus |
Not Available |
| Enzyme 81 SNPs |
SNPJam Report |
| Enzyme 81 General References |
- Mallon AM, Platzer M, Bate R, Gloeckner G, Botcherby MR, Nordsiek G, Strivens MA, Kioschis P, Dangel A, Cunningham D, Straw RN, Weston P, Gilbert M, Fernando S, Goodall K, Hunter G, Greystrong JS, Clarke D, Kimberley C, Goerdes M, Blechschmidt K, Rump A, Hinzmann B, Mundy CR, Miller W, Poustka A, Herman GE, Rhodes M, Denny P, Rosenthal A, Brown SD: Comparative genome sequence analysis of the Bpa/Str region in mouse and Man. Genome Res. 2000 Jun;10(6):758-75. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Levin ML, Chatterjee A, Pragliola A, Worley KC, Wehnert M, Zhuchenko O, Smith RF, Lee CC, Herman GE: A comparative transcription map of the murine bare patches (Bpa) and striated (Str) critical regions and human Xq28. Genome Res. 1996 Jun;6(6):465-77. [PubMed ]
- Konig A, Happle R, Bornholdt D, Engel H, Grzeschik KH: Mutations in the NSDHL gene, encoding a 3beta-hydroxysteroid dehydrogenase, cause CHILD syndrome. Am J Med Genet. 2000 Feb 14;90(4):339-46. [PubMed ]
|
| Enzyme 81 Metabolite References |
Not Available |
|
Enzyme 82
[top]
|
| Enzyme 82 ID |
5497 |
| Enzyme 82 Name |
Lanosterol 14-alpha demethylase |
| Enzyme 82 Synonyms |
- LDM
- CYPLI
- Cytochrome P450 51A1
- Cytochrome P450-14DM
- Cytochrome P45014DM
- Cytochrome P450LI
- Sterol 14-alpha demethylase
|
| Enzyme 82 Gene Name |
CYP51A1 |
| Enzyme 82 Protein Sequence |
>Lanosterol 14-alpha demethylase
MLLLGLLQAGGSVLGQAMEKVTGGNLLSMLLIACAFTLSLVYLIRLAAGHLVQLPAGVKS
PPYIFSPIPFLGHAIAFGKSPIEFLENAYEKYGPVFSFTMVGKTFTYLLGSDAAALLFNS
KNEDLNAEDVYSRLTTPVFGKGVAYDVPNPVFLEQKKMLKSGLNIAHFKQHVSIIEKETK
EYFESWGESGEKNVFEALSELIILTASHCLHGKEIRSQLNEKVAQLYADLDGGFSHAAWL
LPGWLPLPSFRRRDRAHREIKDIFYKAIQKRRQSQEKIDDILQTLLDATYKDGRPLTDDE
VAGMLIGLLLAGQHTSSTTSAWMGFFLARDKTLQKKCYLEQKTVCGENLPPLTYDQLKDL
NLLDRCIKETLRLRPPIMIMMRMARTPQTVAGYTIPPGHQVCVSPTVNQRLKDSWVERLD
FNPDRYLQDNPASGEKFAYVPFGAGRHRCIGENFAYVQIKTIWSTMLRLYEFDLIDGYFP
TVNYTTMIHTPENPVIRYKRRSK
|
| Enzyme 82 Number of Residues |
503 |
| Enzyme 82 Molecular Weight |
56805.3 |
| Enzyme 82 Theoretical pI |
8.72 |
| Enzyme 82 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- electron carrier activity
- heme binding
- ion binding
- iron ion binding
- metal ion binding
- monooxygenase activity
- oxidoreductase activity
- transition metal ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 82 General Function |
Involved in monooxygenase activity |
| Enzyme 82 Specific Function |
Catalyzes C14-demethylation of lanosterol; it transforms lanosterol into 4,4'-dimethyl cholesta-8,14,24-triene-3-beta-ol |
| Enzyme 82 Pathways |
Not Available |
| Enzyme 82 Reactions |
- obtusifoliol + 3 O2 + 3 NADPH + 3 H+ = 4alpha-methyl-5alpha-ergosta-8,14,24(28)-trien-3beta-ol + formate + 3 NADP+ + 4 H2O [RN:R05731]
|
| Enzyme 82 Pfam Domain Function |
|
| Enzyme 82 Signals |
|
| Enzyme 82 Transmembrane Regions |
|
| Enzyme 82 Essentiality |
Not Available |
| Enzyme 82 GenBank ID Protein |
4503243 |
| Enzyme 82 UniProtKB/Swiss-Prot ID |
Q16850 |
| Enzyme 82 UniProtKB/Swiss-Prot Entry Name |
CP51A_HUMAN |
| Enzyme 82 PDB ID |
Not Available |
| Enzyme 82 Cellular Location |
Not Available |
| Enzyme 82 Gene Sequence |
>1530 bp
ATGGCGGCGGCGGCTGGGATGCTGCTGCTGGGCTTGCTGCAGGCGGGTGGGTCGGTGCTG
GGCCAGGCGATGGAGAAGGTGACAGGCGGCAACCTCTTGTCCATGCTGCTGATCGCCTGC
GCCTTCACCCTCAGCCTGGTCTACCTGATCCGTCTGGCCGCCGGCCACCTGGTCCAGCTG
CCCGCAGGGGTGAAAAGTCCTCCATACATTTTCTCCCCAATTCCATTCCTTGGGCATGCC
ATAGCATTTGGGAAAAGTCCAATTGAATTTCTAGAAAATGCATATGAGAAGTATGGACCT
GTATTTAGTTTTACCATGGTAGGCAAGACATTTACTTACCTTCTGGGGAGTGATGCTGCT
GCACTGCTTTTTAATAGTAAAAATGAAGACCTGAATGCAGAAGATGTCTACAGTCGCCTG
ACAACACCTGTGTTTGGGAAGGGAGTTGCATACGATGTGCCTAATCCAGTTTTCTTGGAG
CAGAAGAAAATGTTAAAAAGTGGCCTTAACATAGCCCACTTTAAACAGCATGTTTCTATA
ATTGAAAAAGAAACAAAGGAATACTTTGAGAGTTGGGGAGAAAGTGGAGAAAAAAATGTG
TTTGAAGCTCTTTCTGAGCTCATAATTTTAACAGCTAGCCATTGTTTGCATGGAAAGGAA
ATCAGAAGTCAACTCAATGAAAAGGTAGCACAGCTGTATGCAGATTTGGATGGAGGTTTC
AGCCATGCAGCCTGGCTCTTACCAGGTTGGCTGCCTTTGCCTAGTTTCAGACGCAGGGAC
AGAGCTCATCGGGAAATCAAGGATATTTTCTATAAGGCAATCCAGAAACGCAGACAGTCT
CAAGAAAAAATTGATGACATTCTCCAAACTTTACTAGATGCTACATACAAGGATGGGCGT
CCTTTGACTGATGATGAAGTAGCAGGGATGCTTATTGGATTACTCTTGGCAGGGCAGCAT
ACATCCTCAACTACTAGTGCTTGGATGGGCTTCTTTTTGGCCAGAGACAAAACACTTCAA
AAAAAATGTTATTTAGAACAGAAAACAGTCTGTGGAGAGAATCTGCCTCCTTTAACTTAT
GACCAGCTCAAGGATCTAAATTTACTTGATCGCTGTATAAAAGAAACATTAAGACTTAGA
CCTCCTATAATGATCATGATGAGAATGGCCAGAACTCCTCAGACTGTGGCAGGGTATACC
ATTCCTCCAGGACATCAGGTGTGTGTTTCTCCCACTGTCAATCAAAGACTTAAAGACTCA
TGGGTAGAACGCCTGGACTTTAATCCTGATCGCTACTTACAGGATAACCCAGCATCAGGG
GAAAAGTTTGCCTATGTGCCATTTGGAGCTGGGCGTCATCGTTGTATTGGGGAAAATTTT
GCCTATGTTCAAATTAAGACAATTTGGTCCACTATGCTTCGTTTATATGAATTTGATCTC
ATTGATGGATACTTTCCCACTGTGAATTATACAACTATGATTCACACCCCTGAAAACCCA
GTTATCCGTTACAAACGAAGATCAAAATGA
|
| Enzyme 82 GenBank Gene ID |
NM_000786 |
| Enzyme 82 GeneCard ID |
CYP51A1 |
| Enzyme 82 GenAtlas ID |
CYP51A1 |
| Enzyme 82 HGNC ID |
HGNC:2649 |
| Enzyme 82 Chromosome Location |
7 |
| Enzyme 82 Locus |
7q21.2 |
| Enzyme 82 SNPs |
SNPJam Report |
| Enzyme 82 General References |
- Stromstedt M, Rozman D, Waterman MR: The ubiquitously expressed human CYP51 encodes lanosterol 14 alpha-demethylase, a cytochrome P450 whose expression is regulated by oxysterols. Arch Biochem Biophys. 1996 May 1;329(1):73-81. [PubMed ]
- Aoyama Y, Noshiro M, Gotoh O, Imaoka S, Funae Y, Kurosawa N, Horiuchi T, Yoshida Y: Sterol 14-demethylase P450 (P45014DM*) is one of the most ancient and conserved P450 species. J Biochem. 1996 May;119(5):926-33. [PubMed ]
- Rozman D, Stromstedt M, Waterman MR: The three human cytochrome P450 lanosterol 14 alpha-demethylase (CYP51) genes reside on chromosomes 3, 7, and 13: structure of the two retrotransposed pseudogenes, association with a line-1 element, and evolution of the human CYP51 family. Arch Biochem Biophys. 1996 Sep 15;333(2):466-74. [PubMed ]
- Rozman D, Stromstedt M, Tsui LC, Scherer SW, Waterman MR: Structure and mapping of the human lanosterol 14alpha-demethylase gene (CYP51) encoding the cytochrome P450 involved in cholesterol biosynthesis; comparison of exon/intron organization with other mammalian and fungal CYP genes. Genomics. 1996 Dec 15;38(3):371-81. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed ]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 82 Metabolite References |
Not Available |
|
Enzyme 83
[top]
|
| Enzyme 83 ID |
5505 |
| Enzyme 83 Name |
Tyrosine 3-monooxygenase |
| Enzyme 83 Synonyms |
- Tyrosine 3-hydroxylase
- TH
|
| Enzyme 83 Gene Name |
TH |
| Enzyme 83 Protein Sequence |
>Tyrosine 3-monooxygenase
MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTP
RSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPR
ATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVR
QVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEI
AFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNI
PQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCC
HELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTLYWFTVEFGLCKQNGEVKAYG
AGLLSSYGELLHCLSEEPEIRAFDPEAAAVQPYQDQTYQSVYFVSESFSDAKDKLRSYAS
RIQRPFSVKFDPYTLAIDVLDSPQAVRRSLEGVQDELDTLAHALSAIG
|
| Enzyme 83 Number of Residues |
528 |
| Enzyme 83 Molecular Weight |
58599.5 |
| Enzyme 83 Theoretical pI |
6.25 |
| Enzyme 83 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
- transition metal ion binding
- tyrosine 3-monooxygenase activity
|
| Process |
- aromatic amino acid family metabolic process
- catecholamine biosynthetic process
- catecholamine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid derivative metabolic process
- cellular amino acid metabolic process
- cellular biogenic amine metabolic process
- cellular metabolic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 83 General Function |
Involved in monooxygenase activity |
| Enzyme 83 Specific Function |
Plays an important role in the physiology of adrenergic neurons |
| Enzyme 83 Pathways |
|
| Enzyme 83 Reactions |
- L-tyrosine + tetrahydrobiopterin + O2 = 3,4-dihydroxy-L-phenylalanine + 4a-hydroxytetrahydrobiopterin [RN:R07212]
|
| Enzyme 83 Pfam Domain Function |
|
| Enzyme 83 Signals |
|
| Enzyme 83 Transmembrane Regions |
|
| Enzyme 83 Essentiality |
Not Available |
| Enzyme 83 GenBank ID Protein |
339681 |
| Enzyme 83 UniProtKB/Swiss-Prot ID |
P07101 |
| Enzyme 83 UniProtKB/Swiss-Prot Entry Name |
TY3H_HUMAN |
| Enzyme 83 PDB ID |
1TOH |
| Enzyme 83 PDB File |
Show |
| Enzyme 83 3D Structure |
|
| Enzyme 83 Cellular Location |
Not Available |
| Enzyme 83 Gene Sequence |
>1587 bp
ATGCCCACCCCCGACGCCACCACGCCACAGGCCAAGGGCTTCCGCAGGGCCGTGTCTGAG
CTGGACGCCAAGCAGGCAGAGGCCATCATGGTAAGAGGGCAGGGCGCCCCGGGGCCCAGC
CTCACAGGCTCTCCGTGGCCTGGAACTGCAGCCCCAGCTGCATCCTACACCCCCACCCCA
AGGTCCCCGCGGTTCATTGGGCGCAGGCAGAGCCTCATCGAGGACGCCCGCAAGGAGCGG
GAGGCGGCGGTGGCAGCAGCGGCCGCTGCAGTCCCCTCGGAGCCCGGGGACCCCCTGGAG
GCTGTGGCCTTTGAGGAGAAGGAGGGGAAGGCCGTGCTAAACCTGCTCTTCTCCCCGAGG
GCCACCAAGCCCTCGGCGCTGTCCCGAGCTGTGAAGGTGTTTGAGACGTTTGAAGCCAAA
ATCCACCATCTAGAGACCCGGCCCGCCCAGAGGCCGCGAGCTGGGGGCCCCCACCTGGAG
TACTTCGTGCGCCTCGAGGTGCGCCGAGGGGACCTGGCCGCCCTGCTCAGTGGTGTGCGC
CAGGTGTCAGAGGACGTGCGCAGCCCCGCGGGGCCCAAGGTCCCCTGGTTCCCAAGAAAA
GTGTCAGAGCTGGACAAGTGTCATCACCTGGTCACCAAGTTCGACCCTGACCTGGACTTG
GACCACCCGGGCTTCTCGGACCAGGTGTACCGCCAGCGCAGGAAGCTGATTGCTGAGATC
GCCTTCCAGTACAGGCACGGCGACCCGATTCCCCGTGTGGAGTACACCGCCGAGGAGATT
GCCACCTGGAAGGAGGTCTACACCACGCTGAAGGGCCTCTACGCCACGCACGCCTGCGGG
GAGCACCTGGAGGCCTTTGCTTTGCTGGAGCGCTTCAGCGGCTACCGGGAAGACAATATC
CCCCAGCTGGAGGACGTCTCCCGCTTCCTGAAGGAGCGCACGGGCTTCCAGCTGCGGCCT
GTGGCCGGCCTGCTGTCCGCCCGGGACTTCCTGGCCAGCCTGGCCTTCCGCGTGTTCCAG
TGCACCCAGTATATCCGCCACGCGTCCTCGCCCATGCACTCCCCTGAGCCGGACTGCTGC
CACGAGCTGCTGGGGCACGTGCCCATGCTGGCCGACCGCACCTTCGCGCAGTTCTCGCAG
GACATTGGCCTGGCGTCCCTGGGGGCCTCGGATGAGGAAATTGAGAAGCTGTCCACGCTG
TCATGGTTCACGGTGGAGTTCGGGCTGTGTAAGCAGAACGGGGAGGTGAAGGCCTATGGT
GCCGGGCTGCTGTCCTCCTACGGGGAGCTCCTGCACTGCCTGTCTGAGGAGCCTGAGATT
CGGGCCTTCGACCCTGAGGCTGCGGCCGTGCAGCCCTACCAAGACCAGACGTACCAGTCA
GTCTACTTCGTGTCTGAGAGCTTCAGTGACGCCAAGGACAAGCTCAGGAGCTATGCCTCA
CGCATCCAGCGCCCCTTCTCCGTGAAGTTCGACCCGTACACGCTGGCCATCGACGTGCTG
GACAGCCCCCAGGCCGTGCGGCGCTCCCTGGAGGGTGTCCAGGATGAGCTGGACACCCTT
GCCCATGCGCTGAGTGCCATTGGCTAG
|
| Enzyme 83 GenBank Gene ID |
M17589 |
| Enzyme 83 GeneCard ID |
TH |
| Enzyme 83 GenAtlas ID |
TH |
| Enzyme 83 HGNC ID |
HGNC:11782 |
| Enzyme 83 Chromosome Location |
1 |
| Enzyme 83 Locus |
11p15.5 |
| Enzyme 83 SNPs |
SNPJam Report |
| Enzyme 83 General References |
- Kaneda N, Kobayashi K, Ichinose H, Kishi F, Nakazawa A, Kurosawa Y, Fujita K, Nagatsu T: Isolation of a novel cDNA clone for human tyrosine hydroxylase: alternative RNA splicing produces four kinds of mRNA from a single gene. Biochem Biophys Res Commun. 1987 Aug 14;146(3):971-5. [PubMed ]
- Grima B, Lamouroux A, Boni C, Julien JF, Javoy-Agid F, Mallet J: A single human gene encoding multiple tyrosine hydroxylases with different predicted functional characteristics. Nature. 1987 Apr 16-22;326(6114):707-11. [PubMed ]
- Kobayashi K, Kaneda N, Ichinose H, Kishi F, Nakazawa A, Kurosawa Y, Fujita K, Nagatsu T: Isolation of a full-length cDNA clone encoding human tyrosine hydroxylase type 3. Nucleic Acids Res. 1987 Aug 25;15(16):6733. [PubMed ]
- Kobayashi K, Kaneda N, Ichinose H, Kishi F, Nakazawa A, Kurosawa Y, Fujita K, Nagatsu T: Structure of the human tyrosine hydroxylase gene: alternative splicing from a single gene accounts for generation of four mRNA types. J Biochem (Tokyo). 1988 Jun;103(6):907-12. [PubMed ]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Le Bourdelles B, Boularand S, Boni C, Horellou P, Dumas S, Grima B, Mallet J: Analysis of the 5' region of the human tyrosine hydroxylase gene: combinatorial patterns of exon splicing generate multiple regulated tyrosine hydroxylase isoforms. J Neurochem. 1988 Mar;50(3):988-91. [PubMed ]
- Ginns EI, Rehavi M, Martin BM, Weller M, O'Malley KL, LaMarca ME, McAllister CG, Paul SM: Expression of human tyrosine hydroxylase cDNA in invertebrate cells using a baculovirus vector. J Biol Chem. 1988 May 25;263(15):7406-10. [PubMed ]
- Ludecke B, Dworniczak B, Bartholome K: A point mutation in the tyrosine hydroxylase gene associated with Segawa's syndrome. Hum Genet. 1995 Jan;95(1):123-5. [PubMed ]
- Ludecke B, Bartholome K: Frequent sequence variant in the human tyrosine hydroxylase gene. Hum Genet. 1995 Jun;95(6):716. [PubMed ]
- Knappskog PM, Flatmark T, Mallet J, Ludecke B, Bartholome K: Recessively inherited L-DOPA-responsive dystonia caused by a point mutation (Q381K) in the tyrosine hydroxylase gene. Hum Mol Genet. 1995 Jul;4(7):1209-12. [PubMed ]
- Ludecke B, Knappskog PM, Clayton PT, Surtees RA, Clelland JD, Heales SJ, Brand MP, Bartholome K, Flatmark T: Recessively inherited L-DOPA-responsive parkinsonism in infancy caused by a point mutation (L205P) in the tyrosine hydroxylase gene. Hum Mol Genet. 1996 Jul;5(7):1023-8. [PubMed ]
- Kunugi H, Kawada Y, Hattori M, Ueki A, Otsuka M, Nanko S: Association study of structural mutations of the tyrosine hydroxylase gene with schizophrenia and Parkinson's disease. Am J Med Genet. 1998 Mar 28;81(2):131-3. [PubMed ]
- Ishiguro H, Arinami T, Saito T, Akazawa S, Enomoto M, Mitushio H, Fujishiro H, Tada K, Akimoto Y, Mifune H, Shiozuka S, Hamaguchi H, Toru M, Shibuya H: Systematic search for variations in the tyrosine hydroxylase gene and their associations with schizophrenia, affective disorders, and alcoholism. Am J Med Genet. 1998 Sep 7;81(5):388-96. [PubMed ]
- van den Heuvel LP, Luiten B, Smeitink JA, de Rijk-van Andel JF, Hyland K, Steenbergen-Spanjers GC, Janssen RJ, Wevers RA: A common point mutation in the tyrosine hydroxylase gene in autosomal recessive L-DOPA-responsive dystonia in the Dutch population. Hum Genet. 1998 Jun;102(6):644-6. [PubMed ]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]
- Swaans RJ, Rondot P, Renier WO, Van Den Heuvel LP, Steenbergen-Spanjers GC, Wevers RA: Four novel mutations in the tyrosine hydroxylase gene in patients with infantile parkinsonism. Ann Hum Genet. 2000 Jan;64(Pt 1):25-31. [PubMed ]
|
| Enzyme 83 Metabolite References |
Not Available |
|
Enzyme 84
[top]
|
| Enzyme 84 ID |
5508 |
| Enzyme 84 Name |
Thyroid peroxidase |
| Enzyme 84 Synonyms |
- TPO
|
| Enzyme 84 Gene Name |
TPO |
| Enzyme 84 Protein Sequence |
>Thyroid peroxidase
MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQR
NLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALS
EDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPV
YEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHD
IAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGD
QGALFGNLSTANPRQQMNGLTSFLDASTVYGSSPALERQLRNWTSAEGLLRVHARLRDSG
RAYLPFVPPRAPAACAPEPGIPGETRGPCFLAGDGRASEVPSLTALHTLWLREHNRLAAA
LKALNAHWSADAVYQEARKVVGALHQIITLRDYIPRILGPEAFQQYVGPYEGYDSTANPT
VSNVFSTAAFRFGHATIHPLVRRLDASFQEHPDLPGLWLHQAFFSPWTLLRGGGLDPLIR
GLLARPAKLQVQDQLMNEELTERLFVLSNSSTLDLASINLQRGRDHGLPGYNEWREFCGL
PRLETPADLSTAIASRSVADKILDLYKHPDNIDVWLGGLAENFLPRARTGPLFACLIGKQ
MKALRDGDWFWWENSHVFTDAQRRELEKHSLSRVICDNTGLTRVPMDAFQVGKFPEDFES
CDSITGMNLEAWRETFPQDDKCGFPESVENGDFVHCEESGRRVLVYSCRHGYELQGREQL
TCTQEGWDFQPPLCKDVNECADGAHPPCHASARCRNTKGGFQCLCADPYELGDDGRTCVD
SGRLPRVTWISMSLAALLIGGFAGLTSTVICRWTRTGTKSTLPISETGGGTPELRCGKHQ
AVGTSPQRAAAQDSEQESAGMEGRDTHRLPRAL
|
| Enzyme 84 Number of Residues |
933 |
| Enzyme 84 Molecular Weight |
102961.6 |
| Enzyme 84 Theoretical pI |
6.75 |
| Enzyme 84 GO Classification |
| Function |
- antioxidant activity
- binding
- calcium ion binding
- cation binding
- heme binding
- ion binding
- iron ion binding
- metal ion binding
- peroxidase activity
- transition metal ion binding
|
| Process |
- metabolic process
- oxidation reduction
- response to oxidative stress
- response to stimulus
- response to stress
|
| Component |
| — |
|
| Enzyme 84 General Function |
Involved in calcium ion binding |
| Enzyme 84 Specific Function |
Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4) |
| Enzyme 84 Pathways |
|
| Enzyme 84 Reactions |
- 2 iodide + H2O2 + 2 H+ = diiodine + 2 H2O [RN:R02810]
|
| Enzyme 84 Pfam Domain Function |
|
| Enzyme 84 Signals |
|
| Enzyme 84 Transmembrane Regions |
|
| Enzyme 84 Essentiality |
Not Available |
| Enzyme 84 GenBank ID Protein |
339867 |
| Enzyme 84 UniProtKB/Swiss-Prot ID |
P07202 |
| Enzyme 84 UniProtKB/Swiss-Prot Entry Name |
PERT_HUMAN |
| Enzyme 84 PDB ID |
Not Available |
| Enzyme 84 Cellular Location |
Not Available |
| Enzyme 84 Gene Sequence |
>2802 bp
ATGAGAGCGCTCGCTGTGCTGTCTGTCACGCTGGTTATGGCCTGCACAGAAGCCTTCTTC
CCCTTCATCTCGAGAGGGAAAGAACTCCTTTGGGGAAAGCCTGAGGAGTCTCGTGTCTCT
AGCGTCTTGGAGGAAAGCAAGCGCCTGGTGGACACCGCCATGTACGCCACGATGCAGAGA
AACCTCAAGAAAAGAGGAATCCTTTCTCCAGCTCAGCTTCTGTCTTTTTCCAAACTTCCT
GAGCCAACAAGCGGAGTGATTGCCCGAGCAGCAGAGATAATGGAAACATCAATACAAGCG
ATGAAAAGAAAAGTCAACCTGAAAACTCAACAATCACAGCATCCAACGGATGCTTTATCA
GAAGATCTGCTGAGCATCATTGCAAACATGTCTGGATGTCTCCCTTACATGCTGCCCCCA
AAATGCCCAAACACTTGCCTGGCGAACAAATACAGGCCCATCACAGGAGCTTGCAACAAC
AGAGACCACCCCAGATGGGGCGCCTCCAACACGGCCCTGGCACGATGGCTCCCTCCAGTC
TATGAGGACGGCTTCAGTCAGCCCCGAGGCTGGAACCCCGGCTTCTTGTACAACGGGTTC
CCACTGCCCCCGGTCCGGGAGGTGACAAGACATGTCATTCAAGTTTCAAATGAGGTTGTC
ACAGATGATGACCGCTATTCTGACCTCCTGATGGCATGGGGACAATACATCGACCACGAC
ATCGCGTTCACACCACAGAGCACCAGCAAAGCTGCCTTCGGGGGAGGGGCTGACTGCCAG
ATGACTTGTGAGAACCAAAACCCATGTTTTCCCATACAACTCCCGGAGGAGGCCCGGCCG
GCCGCGGGCACCGCCTGTCTGCCCTTCTACCGCTCTTCGGCCGCCTGCGGCACCGGGGAC
CAAGGCGCGCTCTTTGGGAACCTGTCCACGGCCAACCCGCGGCAGCAGATGAACGGGTTG
ACCTCGTTCCTGGACGCGTCCACCGTGTATGGCAGCTCCCCGGCCCTAGAGAGGCAGCTG
CGGAACTGGACCAGTGCCGAAGGGCTGCTCCGCGTCCACGCGCGCCTCCGGGACTCCGGC
CGCGCCTACCTGCCCTTCGTGCCGCCACGGCGGCCTGCGGCCTGTGCGCCCGAGCCCGGC
ATCCCCGGAGAGACCCGCGGGCCCTGCTTCCTGGCCGGAGACGGCCGCGCCAGCGAGGTC
CCCTCCCTGACGGCACTGCACACGCTGTGGCTGCGCGAGCACAACCGCCTGGCCGCGGCG
CTCAAGGCCCTCAATGCGCACTGGAGCGCGGACGCCGTGTACCAGGAGGCGCGCAAGGTC
GTGGGCGCTCTGCACCAGATCATCACCCTGAGGGATTACATCCCCAGGATCCTGGGACCC
GAGGCCTTCCAGCAGTACGTGGGTCCCTATGAAGGCTATGACTCCACCGCCAACCCCACT
GTGTCCAACGTGTTCTCCACAGCCGCCTTCCGCTTCGGCCATGCCACGATCCACCCGCTG
GTGAGGAGGCTGGACGCCAGCTTCCAGGAGCACCCCGACCTGCCCGGGCTGTGGCTGCAC
CAGGCTTTCTTCAGCCCATGGACATTACTCCGTGGAGGTGGTTTGGACCCACTAATACGA
GGCCTTCTTGCAAGACCAGCCAAACTGCAGGTGCAGGATCAGCTGATGAACGAGGAGCTG
ACGGAAAGGCTCTTTGTGCTGTCCAATTCCAGCACCTTGGATCTGGCGTCCATCAACCTG
CAGAGGGGCCGGGACCACGGGCTGCCAGGTTACAATGAGTGGAGGGAGTTCTGCGGCCTG
CCTCGCCTGGAGACCCCCGCTGACCTGAGCACAGCCATCGCCAGCAGGAGCGTGGCCGAC
AAGATCCTGGACTTGTACAAGCATCCTGACAACATCGATGTCTGGCTGGGAGGCTTAGCT
GAAAACTTCCTCCCCAGGGCTCGGACAGGGCCCCTGTTTGCCTGTCTCATTGGGAAGCAG
ATGAAGGCTCTGCGGGATGGTGACTGGTTTTGGTGGGAGAACAGCCACGTCTTCACGGAT
GCACAGAGGCGTGAGCTGGAGAAGCACTCCCTGTCTCGGGTCATCTGTGACAACACTGGC
CTCACCAGGGTGCCCATGGATGCCTTCCAAGTCGGCAAATTCCCTGAAGACTTTGAGTCT
TGTGACAGCATCCCTGGCATGAACCTGGAGGCCTGGAGGGAAACCTTTCCTCAAGACGAC
AAGTGTGGCTTCCCAGAGAGCGTGGAGAATGGGGACTTTGTGCACTGTGAGGAGTCTGGG
AGGCGCGTGCTGGTGTATTCCTGCCGGCACGGGTATGAGCTCCAAGGCCGGGAGCAGCTC
ACTTGCACCCAGGAAGGATGGGATTTCCAGCCTCCCCTCTGCAAAGATGTGAACGAGTGT
GCAGACGGTGCCCACCCCCCCTGCCACGCCTCTGCGAGGTGCAGAAACACCAAAGGCGGC
TTCCAGTGTCTCTGCGCGGACCCCTACGAGTTAGGAGACGATGGGAGAACCTGCGTAGAC
TCCGGGAGGCTCCCTCGGGCGACTTGGATCTCCATGTCGCTGGCTGCTCTGCTGATCGGA
GGCTTCGCAGGTCTCACCTCGACGGTGATTTGCAGGTGGACACGCACTGGCACTAAATCC
ACACTGCCCATCTCGGAGACAGGCGGAGGAACTCCCGAGCTGAGATGCGGAAAGCACCAG
GCCGTAGGGACCTCACCGCAGCGGGCCGCAGCTCAGGACTCGGAGCAGGAGAGTGCTGGG
ATGGAAGGCCGGGATACTCACAGGCTGCCGAGAGCCCTCTGA
|
| Enzyme 84 GenBank Gene ID |
J02969 |
| Enzyme 84 GeneCard ID |
TPO |
| Enzyme 84 GenAtlas ID |
TPO |
| Enzyme 84 HGNC ID |
HGNC:12015 |
| Enzyme 84 Chromosome Location |
2 |
| Enzyme 84 Locus |
2p25 |
| Enzyme 84 SNPs |
SNPJam Report |
| Enzyme 84 General References |
- Kimura S, Kotani T, McBride OW, Umeki K, Hirai K, Nakayama T, Ohtaki S: Human thyroid peroxidase: complete cDNA and protein sequence, chromosome mapping, and identification of two alternately spliced mRNAs. Proc Natl Acad Sci U S A. 1987 Aug;84(16):5555-9. [PubMed ]
- Libert F, Ruel J, Ludgate M, Swillens S, Alexander N, Vassart G, Dinsart C: Complete nucleotide sequence of the human thyroperoxidase-microsomal antigen cDNA. Nucleic Acids Res. 1987 Aug 25;15(16):6735. [PubMed ]
- Kimura S, Hong YS, Kotani T, Ohtaki S, Kikkawa F: Structure of the human thyroid peroxidase gene: comparison and relationship to the human myeloperoxidase gene. Biochemistry. 1989 May 16;28(10):4481-9. [PubMed ]
- Barnett PS, Banga JP, Watkins J, Huang GC, Gluckman DR, Page MJ, McGregor AM: Nucleotide sequence of the alternatively spliced human thyroid peroxidase cDNA, TPO-2. Nucleic Acids Res. 1990 Feb 11;18(3):670. [PubMed ]
- Ferrand M, Le Fourn V, Franc JL: Increasing diversity of human thyroperoxidase generated by alternative splicing. Characterized by molecular cloning of new transcripts with single- and multispliced mRNAs. J Biol Chem. 2003 Feb 7;278(6):3793-800. Epub 2002 Nov 25. [PubMed ]
- Seto P, Hirayu H, Magnusson RP, Gestautas J, Portmann L, DeGroot LJ, Rapoport B: Isolation of a complementary DNA clone for thyroid microsomal antigen. Homology with the gene for thyroid peroxidase. J Clin Invest. 1987 Oct;80(4):1205-8. [PubMed ]
- Zanelli E, Henry M, Charvet B, Malthiery Y: Evidence for an alternate splicing in the thyroperoxidase messenger from patients with Graves' disease. Biochem Biophys Res Commun. 1990 Jul 31;170(2):735-41. [PubMed ]
- Wang D, De Deken X, Milenkovic M, Song Y, Pirson I, Dumont JE, Miot F: Identification of a novel partner of duox: EFP1, a thioredoxin-related protein. J Biol Chem. 2005 Jan 28;280(4):3096-103. Epub 2004 Nov 22. [PubMed ]
- Bikker H, Vulsma T, Baas F, de Vijlder JJ: Identification of five novel inactivating mutations in the human thyroid peroxidase gene by denaturing gradient gel electrophoresis. Hum Mutat. 1995;6(1):9-16. [PubMed ]
- Bikker H, Baas F, De Vijlder JJ: Molecular analysis of mutated thyroid peroxidase detected in patients with total iodide organification defects. J Clin Endocrinol Metab. 1997 Feb;82(2):649-53. [PubMed ]
- Santos CL, Bikker H, Rego KG, Nascimento AC, Tambascia M, De Vijlder JJ, Medeiros-Neto G: A novel mutation in the TPO gene in goitrous hypothyroid patients with iodide organification defect. Clin Endocrinol (Oxf). 1999 Aug;51(2):165-72. [PubMed ]
- Pannain S, Weiss RE, Jackson CE, Dian D, Beck JC, Sheffield VC, Cox N, Refetoff S: Two different mutations in the thyroid peroxidase gene of a large inbred Amish kindred: power and limits of homozygosity mapping. J Clin Endocrinol Metab. 1999 Mar;84(3):1061-71. [PubMed ]
- Kotani T, Umeki K, Yamamoto I, Maesaka H, Tachibana K, Ohtaki S: A novel mutation in the human thyroid peroxidase gene resulting in a total iodide organification defect. J Endocrinol. 1999 Feb;160(2):267-73. [PubMed ]
- Bakker B, Bikker H, Vulsma T, de Randamie JS, Wiedijk BM, De Vijlder JJ: Two decades of screening for congenital hypothyroidism in The Netherlands: TPO gene mutations in total iodide organification defects (an update). J Clin Endocrinol Metab. 2000 Oct;85(10):3708-12. [PubMed ]
- Ambrugger P, Stoeva I, Biebermann H, Torresani T, Leitner C, Gruters A: Novel mutations of the thyroid peroxidase gene in patients with permanent congenital hypothyroidism. Eur J Endocrinol. 2001 Jul;145(1):19-24. [PubMed ]
- Umeki K, Kotani T, Kawano J, Suganuma T, Yamamoto I, Aratake Y, Furujo M, Ichiba Y: Two novel missense mutations in the thyroid peroxidase gene, R665W and G771R, result in a localization defect and cause congenital hypothyroidism. Eur J Endocrinol. 2002 Apr;146(4):491-8. [PubMed ]
- Niu DM, Hwang B, Chu YK, Liao CJ, Wang PL, Lin CY: High prevalence of a novel mutation (2268 insT) of the thyroid peroxidase gene in Taiwanese patients with total iodide organification defect, and evidence for a founder effect. J Clin Endocrinol Metab. 2002 Sep;87(9):4208-12. [PubMed ]
- Wu JY, Shu SG, Yang CF, Lee CC, Tsai FJ: Mutation analysis of thyroid peroxidase gene in Chinese patients with total iodide organification defect: identification of five novel mutations. J Endocrinol. 2002 Mar;172(3):627-35. [PubMed ]
- Calaciura F, Miscio G, Coco A, Leonardi D, Cisternino C, Regalbuto C, Bozzali M, Maiorana R, Ranieri A, Carta A, Buscema M, Trischitta V, Sava L, Tassi V: Genetics of specific phenotypes of congenital hypothyroidism: a population-based approach. Thyroid. 2002 Nov;12(11):945-51. [PubMed ]
- Kotani T, Umeki K, Kawano J, Suganuma T, Hishinuma A, Ieiri T, Harada S: Partial iodide organification defect caused by a novel mutation of the thyroid peroxidase gene in three siblings. Clin Endocrinol (Oxf). 2003 Aug;59(2):198-206. [PubMed ]
- Rivolta CM, Esperante SA, Gruneiro-Papendieck L, Chiesa A, Moya CM, Domene S, Varela V, Targovnik HM: Five novel inactivating mutations in the thyroid peroxidase gene responsible for congenital goiter and iodide organification defect. Hum Mutat. 2003 Sep;22(3):259. [PubMed ]
- Fugazzola L, Cerutti N, Mannavola D, Vannucchi G, Fallini C, Persani L, Beck-Peccoz P: Monoallelic expression of mutant thyroid peroxidase allele causing total iodide organification defect. J Clin Endocrinol Metab. 2003 Jul;88(7):3264-71. [PubMed ]
- Tajima T, Tsubaki J, Fujieda K: Two novel mutations in the thyroid peroxidase gene with goitrous hypothyroidism. Endocr J. 2005 Oct;52(5):643-5. [PubMed ]
- Pfarr N, Borck G, Turk A, Napiontek U, Keilmann A, Muller-Forell W, Kopp P, Pohlenz J: Goitrous congenital hypothyroidism and hearing impairment associated with mutations in the TPO and SLC26A4/PDS genes. J Clin Endocrinol Metab. 2006 Jul;91(7):2678-81. Epub 2006 May 9. [PubMed ]
|
| Enzyme 84 Metabolite References |
Not Available |
|
Enzyme 85
[top]
|
| Enzyme 85 ID |
5511 |
| Enzyme 85 Name |
Lactoperoxidase |
| Enzyme 85 Synonyms |
- LPO
- Salivary peroxidase
- SPO
|
| Enzyme 85 Gene Name |
LPO |
| Enzyme 85 Protein Sequence |
>Lactoperoxidase
MRVLLHLPALLASLILLQAAASTTRAQTTRTSAISDTVSQAKVQVNKAFLDSRTRLKTAM
SSETPTSRQLSEYLKHAKGRTRTAIRNGQVWEESLKRLRQKASLTNVTDPSLDLTSLSLE
VGCGAPAPVVRCDPCSPYRTITGDCNNRRKPALGAANRALARWLPAEYEDGLSLPFGWTP
GKTRNGFPLPLAREVSNKIVGYLNEEGVLDQNRSLLFMQWGQIVDHDLDFAPDTELGSSE
YSKAQCDEYCIQGDNCFPIMFPPNDPKAGTQGKCMPFFRAGFVCPTPPYKSLAREQINAL
TSFLDASFVYSSEPSLASRLRNLSSPLGLMAVNQEVSDHGLPYLPYDSKKPSPCEFINTT
ARVPCFLAGDSRASEHILLATSHTLFLREHNRLARELKRLNPQWDGEKLYQEARKILGAF
VQIITFRDYLPILLGDHMQKWIPPYQGYSESVDPRISNVFTFAFRFGHLEVPSSMFRLDE
NYQPWGPEPELPLHTLFFNTWRMVKDGGIDPLVRGLLAKKSKLMKQNKMMTGELRNKLFQ
PTHRIHGFDLAAINTQRCRDHGQPGYNSWRAFCDLSQPQTLEELNTVLKSKMLAKKLLGL
YGTPDNIDIWIGAIAEPLVERGRVGPLLACLLGKQFQQIRDGDRFWWENPGVFTNEQKDS
LQKMSFSRLVCDNTRITKVPRDPFWANSYPYDFVDCSAIDKLDLSPWASVKN
|
| Enzyme 85 Number of Residues |
712 |
| Enzyme 85 Molecular Weight |
80287.1 |
| Enzyme 85 Theoretical pI |
8.76 |
| Enzyme 85 GO Classification |
| Function |
- antioxidant activity
- binding
- cation binding
- heme binding
- ion binding
- iron ion binding
- metal ion binding
- peroxidase activity
- transition metal ion binding
|
| Process |
- metabolic process
- oxidation reduction
- response to oxidative stress
- response to stimulus
- response to stress
|
| Component |
| — |
|
| Enzyme 85 General Function |
Involved in peroxidase activity |
| Enzyme 85 Specific Function |
May contribute to airway host defense against infection |
| Enzyme 85 Pathways |
- Arachidonic acid metabolism (map00590 )
- Methane metabolism (map00680 )
- Phenylalanine Metabolism (map00360 )
- Stilbene, coumarine and lignin biosynthesis (map00940 )
|
| Enzyme 85 Reactions |
- donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
|
| Enzyme 85 Pfam Domain Function |
|
| Enzyme 85 Signals |
|
| Enzyme 85 Transmembrane Regions |
|
| Enzyme 85 Essentiality |
Not Available |
| Enzyme 85 GenBank ID Protein |
Not Available |
| Enzyme 85 UniProtKB/Swiss-Prot ID |
P22079 |
| Enzyme 85 UniProtKB/Swiss-Prot Entry Name |
PERL_HUMAN |
| Enzyme 85 PDB ID |
Not Available |
| Enzyme 85 Cellular Location |
Not Available |
| Enzyme 85 Gene Sequence |
>2139 bp
ATGAGGGTCCTTCTCCATCTCCCAGCCCTCCTGGCTTCCCTCATCTTGCTTCAGGCTGCA
GCATCTACCACAAGAGCGCAGACTACCAGAACCTCTGCCATCTCCGATACTGTGAGTCAG
GCCAAGGTCCAAGTCAACAAGGCCTTCCTGGACTCCCGAACCAGGCTGAAGACCGCCATG
AGCTCTGAGACTCCCACCAGCCGACAGCTCTCAGAATACCTCAAGCATGCCAAAGGCCGG
ACGCGCACAGCCATCCGCAATGGACAGGTGTGGGAGGAGTCTTTAAAGAGACTGAGGCAG
AAGGCATCCTTGACCAATGTCACAGATCCCAGCCTGGACTTGACTTCACTGTCTCTGGAG
GTGGGCTGTGGTGCTCCTGCTCCCGTGGTGAGATGCGACCCGTGCAGCCCTTACCGCACC
ATTACGGGAGACTGCAATAACAGGAGGAAGCCTGCGCTGGGCGCCGCCAACAGGGCTCTG
GCGCGCTGGCTGCCCGCGGAGTACGAGGACGGGCTCTCCCTGCCCTTCGGCTGGACGCCG
GGGAAGACGCGCAACGGCTTCCCTCTCCCGCTGGCCCGGGAGGTATCTAACAAGATTGTT
GGCTATCTGAATGAGGAGGGTGTTCTGGACCAAAACAGGTCCCTGCTCTTCATGCAGTGG
GGTCAGATTGTGGATCATGACCTGGACTTTGCCCCTGACACCGAGCTGGGGAGTAGCGAG
TACTCCAAAGCCCAGTGTGATGAGTACTGTATCCAGGGAGACAACTGCTTCCCCATCATG
TTCCCACCCAATGACCCCAAGGCGGGGACTCAAGGGAAATGCATGCCTTTCTTCCGAGCT
GGGTTCGTCTGCCCCACTCCACCCTACAAGTCCCTGGCCCGAGAGCAGATCAACGCTCTG
ACCTCCTTCCTGGATGCCAGCTTTGTGTACAGCTCCGAGCCAAGCCTGGCCAGCCGCCTC
CGCAACCTCAGCAGCCCCCTGGGCCTCATGGCTGTCAACCAGGAGGTCTCAGACCATGGA
CTACCCTACCTGCCCTATGACAGCAAGAAGCCAAGCCCCTGTGAGTTCATCAACACCACT
GCCCGTGTGCCCTGCTTCCTGGCAGGAGATTCTCGAGCCTCAGAGCATATTCTGCTGGCC
ACATCCCACACCCTCTTTCTCCGCGAGCATAACCGGCTGGCCAGAGAACTAAAGAGACTC
AACCCTCAGTGGGATGGAGAGAAGCTCTACCAGGAAGCCCGGAAAATCCTGGGAGCCTTC
GTGCAGATTATCACCTTTAGGGACTACCTACCCATTTTGCTAGGTGACCACATGCAGAAG
TGGATACCCCCATATCAAGGCTACAGTGAATCTGTGGATCCCAGAATTTCCAATGTCTTC
ACCTTCGCCTTCCGCTTTGGCCACTTGGAGGTCCCCTCTAGTATGTTCCGCCTGGATGAG
AATTATCAGCCATGGGGGCCAGAACCAGAACTCCCCCTCCACACCCTCTTCTTCAACACT
TGGAGGATGGTCAAAGATGGTGGAATTGATCCTCTGGTGCGGGGCCTGCTGGCCAAGAAA
TCCAAGCTGATGAAACAGAATAAAATGATGACTGGAGAGCTGCGCAACAAGCTTTTCCAG
CCAACTCACAGGATCCATGGCTTTGACCTGGCTGCCATCAACACACAGCGTTGCCGGGAC
CATGGGCAACCTGGGTACAATTCCTGGAGAGCCTTCTGTGACCTCTCACAGCCGCAGACA
CTAGAGGAGTTGAACACAGTGCTGAAGAGCAAGATGCTGGCCAAGAAGTTACTGGGTCTC
TACGGGACCCCTGACAACATCGACATCTGGATAGGGGCCATTGCTGAGCCGCTGGTGGAA
AGGGGTCGGGTGGGGCCTCTCCTGGCCTGCCTCTTGGGCAAGCAGTTCCAGCAGATCCGT
GATGGAGACAGGTTCTGGTGGGAAAACCCTGGGGTCTTCACGAACGAGCAGAAGGACTCT
CTACAGAAAATGTCCTTCTCACGCCTTGTCTGTGACAACACCCGCATCACCAAGGTCCCA
CGGGACCCATTCTGGGCCAACAGCTACCCCTATGACTTCGTGGATTGCTCAGCCATCGAC
AAGCTGGACCTGTCACCCTGGGCCTCAGTGAAGAATTAG
|
| Enzyme 85 GenBank Gene ID |
U39573 |
| Enzyme 85 GeneCard ID |
LPO |
| Enzyme 85 GenAtlas ID |
LPO |
| Enzyme 85 HGNC ID |
HGNC:6678 |
| Enzyme 85 Chromosome Location |
1 |
| Enzyme 85 Locus |
17q23.1 |
| Enzyme 85 SNPs |
SNPJam Report |
| Enzyme 85 General References |
- Kiser C, Caterina CK, Engler JA, Rahemtulla B, Rahemtulla F: Cloning and sequence analysis of the human salivary peroxidase-encoding cDNA. Gene. 1996 Sep 16;173(2):261-4. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Dull TJ, Uyeda C, Strosberg AD, Nedwin G, Seilhamer JJ: Molecular cloning of cDNAs encoding bovine and human lactoperoxidase. DNA Cell Biol. 1990 Sep;9(7):499-509. [PubMed ]
- Wijkstrom-Frei C, El-Chemaly S, Ali-Rachedi R, Gerson C, Cobas MA, Forteza R, Salathe M, Conner GE: Lactoperoxidase and human airway host defense. Am J Respir Cell Mol Biol. 2003 Aug;29(2):206-12. Epub 2003 Mar 6. [PubMed ]
- Ramachandran P, Boontheung P, Xie Y, Sondej M, Wong DT, Loo JA: Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry. J Proteome Res. 2006 Jun;5(6):1493-503. [PubMed ]
- Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed ]
|
| Enzyme 85 Metabolite References |
Not Available |
|
Enzyme 86
[top]
|
| Enzyme 86 ID |
5512 |
| Enzyme 86 Name |
Phenylalanine-4-hydroxylase |
| Enzyme 86 Synonyms |
- PAH
- Phe-4-monooxygenase
|
| Enzyme 86 Gene Name |
PAH |
| Enzyme 86 Protein Sequence |
>Phenylalanine-4-hydroxylase
MSTAVLENPGLGRKLSDFGQETSYIEDNCNQNGAISLIFSLKEEVGALAKVLRLFEENDV
NLTHIESRPSRLKKDEYEFFTHLDKRSLPALTNIIKILRHDIGATVHELSRDKKKDTVPW
FPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYM
EEEKKTWGTVFKTLKSLYKTHACYEYNHIFPLLEKYCGFHEDNIPQLEDVSQFLQTCTGF
RLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFA
QFSQEIGLASLGAPDEYIEKLATIYWFTVEFGLCKQGDSIKAYGAGLLSSFGELQYCLSE
KPKLLPLELEKTAIQNYTVTEFQPLYYVAESFNDAKEKVRNFAATIPRPFSVRYDPYTQR
IEVLDNTQQLKILADSINSEIGILCSALQKIK
|
| Enzyme 86 Number of Residues |
452 |
| Enzyme 86 Molecular Weight |
51861.6 |
| Enzyme 86 Theoretical pI |
6.57 |
| Enzyme 86 GO Classification |
| Function |
- amino acid binding
- binding
- carboxylic acid binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- monooxygenase activity
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced pteridine as one donor, and incorporation of one atom of oxygen
- phenylalanine 4-monooxygenase activity
- transition metal ion binding
|
| Process |
- L-phenylalanine catabolic process
- L-phenylalanine metabolic process
- aromatic amino acid family metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 86 General Function |
Involved in amino acid binding |
| Enzyme 86 Specific Function |
L-phenylalanine + tetrahydrobiopterin + O(2) = L-tyrosine + 4a-hydroxytetrahydrobiopterin |
| Enzyme 86 Pathways |
- Phenylalanine and Tyrosine Metabolism (map00400 )
|
| Enzyme 86 Reactions |
- L-phenylalanine + tetrahydrobiopterin + O2 = L-tyrosine + 4a-hydroxytetrahydrobiopterin [RN:R07211]
|
| Enzyme 86 Pfam Domain Function |
|
| Enzyme 86 Signals |
|
| Enzyme 86 Transmembrane Regions |
|
| Enzyme 86 Essentiality |
Not Available |
| Enzyme 86 GenBank ID Protein |
189937 |
| Enzyme 86 UniProtKB/Swiss-Prot ID |
P00439 |
| Enzyme 86 UniProtKB/Swiss-Prot Entry Name |
PH4H_HUMAN |
| Enzyme 86 PDB ID |
2PHM |
| Enzyme 86 PDB File |
Show |
| Enzyme 86 3D Structure |
|
| Enzyme 86 Cellular Location |
Not Available |
| Enzyme 86 Gene Sequence |
>1359 bp
ATGTCCACTGCGGTCCTGGAAAACCCAGGCTTGGGCAGGAAACTCTCTGACTTTGGACAG
GAAACAAGCTATATTGAAGACAACTGCAATCAAAATGGTGCCATATCACTGATCTTCTCA
CTCAAAGAAGAAGTTGGTGCATTGGCCAAAGTATTGCGCTTATTTGAGGAGAATGATGTA
AACCTGACCCACATTGAATCTAGACCTTCTCGTTTAAAGAAAGATGAGTATGAATTTTTC
ACCCATTTGGATAAACGTAGCCTGCCTGCTCTGACAAACATCATCAAGATCTTGAGGCAT
GACATTGGTGCCACTGTCCATGAGCTTTCACGAGATAAGAAGAAAGACACAGTGCCCTGG
TTCCCAAGAACCATTCAAGAGCTGGACAGATTTGCCAATCAGATTCTCAGCTATGGAGCG
GAACTGGATGCTGACCACCCTGGTTTTAAAGATCCTGTGTACCGTGCAAGACGGAAGCAG
TTTGCTGACATTGCCTACAACTACCGCCATGGGCAGCCCATCCCTCGAGTGGAATACATG
GAGGAAGAAAAGAAAACATGGGGCACAGTGTTCAAGACTCTGAAGTCCTTGTATAAAACC
CATGCTTGCTATGAGTACAATCACATTTTTCCACTTCTTGAAAAGTACTGTGGCTTCCAT
GAAGATAACATTCCCCAGCTGGAAGACGTTTCTCAATTCCTGCAGACTTGCACTGGTTTC
CGCCTCCGACCTGTGGCTGGCCTGCTTTCCTCTCGGGATTTCTTGGGTGGCCTGGCCTTC
CGAGTCTTCCACTGCACACAGTACATCAGACATGGATCCAAGCCCATGTATACCCCCGAA
CCTGACATCTGCCATGAGCTGTTGGGACATGTGCCCTTGTTTTCAGATCGCAGCTTTGCC
CAGTTTTCCCAGGAAATTGGCCTTGCCTCTCTGGGTGCACCTGATGAATACATTGAAAAG
CTCGCCACAATTTACTGGTTTACTGTGGAGTTTGGGCTCTGCAAACAAGGAGACTCCATA
AAGGCATATGGTGCTGGGCTCCTGTCATCCTTTGGTGAATTACAGTACTGCTTATCAGAG
AAGCCAAAGCTTCTCCCCCTGGAGCTGGAGAAGACAGCCATCCAAAATTACACTGTCACG
GAGTTCCAGCCCCTGTATTACGTGGCAGAGAGTTTTAATGATGCCAAGGAGAAAGTAAGG
AACTTTGCTGCCACAATACCTCGGCCCTTCTCAGTTCGCTACGACCCATACACCCAAAGG
ATTGAGGTCTTGGACAATACCCAGCAGCTTAAGATTTTGGCTGATTCCATTAACAGTGAA
ATTGGAATCCTTTGCAGTGCCCTCCAGAAAATAAAGTAA
|
| Enzyme 86 GenBank Gene ID |
K03020 |
| Enzyme 86 GeneCard ID |
PAH |
| Enzyme 86 GenAtlas ID |
PAH |
| Enzyme 86 HGNC ID |
HGNC:8582 |
| Enzyme 86 Chromosome Location |
1 |
| Enzyme 86 Locus |
12q22-q24.2 |
| Enzyme 86 SNPs |
SNPJam Report |
| Enzyme 86 General References |
- Kwok SC, Ledley FD, DiLella AG, Robson KJ, Woo SL: Nucleotide sequence of a full-length complementary DNA clone and amino acid sequence of human phenylalanine hydroxylase. Biochemistry. 1985 Jan 29;24(3):556-61. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Cotton RG, McAdam W, Jennings I, Morgan FJ: A monoclonal antibody to aromatic amino acid hydroxylases. Identification of the epitope. Biochem J. 1988 Oct 1;255(1):193-6. [PubMed ]
- Siltberg-Liberles J, Steen IH, Svebak RM, Martinez A: The phylogeny of the aromatic amino acid hydroxylases revisited by characterizing phenylalanine hydroxylase from Dictyostelium discoideum. Gene. 2008 Dec 31;427(1-2):86-92. Epub 2008 Sep 16. [PubMed ]
- Erlandsen H, Fusetti F, Martinez A, Hough E, Flatmark T, Stevens RC: Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria. Nat Struct Biol. 1997 Dec;4(12):995-1000. [PubMed ]
- Erlandsen H, Flatmark T, Stevens RC, Hough E: Crystallographic analysis of the human phenylalanine hydroxylase catalytic domain with bound catechol inhibitors at 2.0 A resolution. Biochemistry. 1998 Nov 10;37(45):15638-46. [PubMed ]
- Fusetti F, Erlandsen H, Flatmark T, Stevens RC: Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria. J Biol Chem. 1998 Jul 3;273(27):16962-7. [PubMed ]
- Erlandsen H, Bjorgo E, Flatmark T, Stevens RC: Crystal structure and site-specific mutagenesis of pterin-bound human phenylalanine hydroxylase. Biochemistry. 2000 Mar 7;39(9):2208-17. [PubMed ]
- Andersen OA, Flatmark T, Hough E: High resolution crystal structures of the catalytic domain of human phenylalanine hydroxylase in its catalytically active Fe(II) form and binary complex with tetrahydrobiopterin. J Mol Biol. 2001 Nov 23;314(2):279-91. [PubMed ]
- Konecki DS, Lichter-Konecki U: The phenylketonuria locus: current knowledge about alleles and mutations of the phenylalanine hydroxylase gene in various populations. Hum Genet. 1991 Aug;87(4):377-88. [PubMed ]
- Cotton RG: Heterogeneity of phenylketonuria at the clinical, protein and DNA levels. J Inherit Metab Dis. 1990;13(5):739-50. [PubMed ]
- Eisensmith RC, Woo SL: Molecular basis of phenylketonuria and related hyperphenylalaninemias: mutations and polymorphisms in the human phenylalanine hydroxylase gene. Hum Mutat. 1992;1(1):13-23. [PubMed ]
- Hoang L, Byck S, Prevost L, Scriver CR: PAH Mutation Analysis Consortium Database: a database for disease-producing and other allelic variation at the human PAH locus. Nucleic Acids Res. 1996 Jan 1;24(1):127-31. [PubMed ]
- Lichter-Konecki U, Konecki DS, DiLella AG, Brayton K, Marvit J, Hahn TM, Trefz FK, Woo SL: Phenylalanine hydroxylase deficiency caused by a single base substitution in an exon of the human phenylalanine hydroxylase gene. Biochemistry. 1988 Apr 19;27(8):2881-5. [PubMed ]
- Lyonnet S, Caillaud C, Rey F, Berthelon M, Frezal J, Rey J, Munnich A: Molecular genetics of phenylketonuria in Mediterranean countries: a mutation associated with partial phenylalanine hydroxylase deficiency. Am J Hum Genet. 1989 Apr;44(4):511-7. [PubMed ]
- Hofman KJ, Antonarakis SE, Missiou-Tsangaraki S, Boehm CD, Valle D: Phenylketonuria in the Greek population. Haplotype analysis of the phenylalanine hydroxylase gene and identification of a PKU mutation. Mol Biol Med. 1989 Jun;6(3):245-50. [PubMed ]
- Svensson E, Andersson B, Hagenfeldt L: Two mutations within the coding sequence of the phenylalanine hydroxylase gene. Hum Genet. 1990 Aug;85(3):300-4. [PubMed ]
- Dianzani I, Forrest SM, Camaschella C, Saglio G, Ponzone A, Cotton RG: Screening for mutations in the phenylalanine hydroxylase gene from Italian patients with phenylketonuria by using the chemical cleavage method: a new splice mutation. Am J Hum Genet. 1991 Mar;48(3):631-5. [PubMed ]
- Hofman KJ, Steel G, Kazazian HH, Valle D: Phenylketonuria in U.S. blacks: molecular analysis of the phenylalanine hydroxylase gene. Am J Hum Genet. 1991 Apr;48(4):791-8. [PubMed ]
- Okano Y, Wang T, Eisensmith RC, Longhi R, Riva E, Giovannini M, Cerone R, Romano C, Woo SL: Phenylketonuria missense mutations in the Mediterranean. Genomics. 1991 Jan;9(1):96-103. [PubMed ]
- Dworniczak B, Grudda K, Stumper J, Bartholome K, Aulehla-Scholz C, Horst J: Phenylalanine hydroxylase gene: novel missense mutation in exon 7 causing severe phenylketonuria. Genomics. 1991 Jan;9(1):193-9. [PubMed ]
- Konecki DS, Schlotter M, Trefz FK, Lichter-Konecki U: The identification of two mis-sense mutations at the PAH gene locus in a Turkish patient with phenylketonuria. Hum Genet. 1991 Aug;87(4):389-93. [PubMed ]
- Caillaud C, Lyonnet S, Rey F, Melle D, Frebourg T, Berthelon M, Vilarinho L, Vaz Osorio R, Rey J, Munnich A: A 3-base pair in-frame deletion of the phenylalanine hydroxylase gene results in a kinetic variant of phenylketonuria. J Biol Chem. 1991 May 25;266(15):9351-4. [PubMed ]
- Economou-Petersen E, Henriksen KF, Guldberg P, Guttler F: Molecular basis for nonphenylketonuria hyperphenylalaninemia. Genomics. 1992 Sep;14(1):1-5. [PubMed ]
- Lin CH, Hsiao KJ, Tsai TF, Chao HK, Su TS: Identification of a missense phenylketonuria mutation at codon 408 in Chinese. Hum Genet. 1992 Aug;89(6):593-6. [PubMed ]
- Jaruzelska J, Melle D, Matuszak R, Borski K, Munnich A: A new 15 bp deletion in exon 11 of the phenylalanine hydroxylase gene in phenylketonuria. Hum Mol Genet. 1992 Dec;1(9):763-4. [PubMed ]
- Desviat LR, Perez B, Ugarte M: A new PKU mutation associated with haplotype 12. Hum Mol Genet. 1992 Dec;1(9):765-6. [PubMed ]
- Guldberg P, Henriksen KF, Guttler F: Molecular analysis of phenylketonuria in Denmark: 99% of the mutations detected by denaturing gradient gel electrophoresis. Genomics. 1993 Jul;17(1):141-6. [PubMed ]
- Abadie V, Jaruzelska J, Lyonnet S, Millasseau P, Berthelon M, Rey F, Munnich A, Rey J: Illegitimate transcription of the phenylalanine hydroxylase gene in lymphocytes for identification of mutations in phenylketonuria. Hum Mol Genet. 1993 Jan;2(1):31-4. [PubMed ]
- Goebel-Schreiner B, Schreiner R: Identification of a new missense mutation in Japanese phenylketonuric patients. J Inherit Metab Dis. 1993;16(6):950-6. [PubMed ]
- Guldberg P, Henriksen KF, Thony B, Blau N, Guttler F: Molecular heterogeneity of nonphenylketonuria hyperphenylalaninemia in 25 Danish patients. Genomics. 1994 May 15;21(2):453-5. [PubMed ]
- Benit P, Rey F, Melle D, Munnich A, Rey J: Five novel missense mutations of the phenylalanine hydroxylase gene in phenylketonuria. Hum Mutat. 1994;4(3):229-31. [PubMed ]
- Knappskog PM, Eiken HG, Martinez A, Bruland O, Apold J, Flatmark T: PKU mutation (D143G) associated with an apparent high residual enzyme activity: expression of a kinetic variant form of phenylalanine hydroxylase in three different systems. Hum Mutat. 1996;8(3):236-46. [PubMed ]
- Guldberg P, Mallmann R, Henriksen KF, Guttler F: Phenylalanine hydroxylase deficiency in a population in Germany: mutational profile and nine novel mutations. Hum Mutat. 1996;8(3):276-9. [PubMed ]
- Argiolas A, Bosco P, Cali F, Ceratto N, Anello G, Riva E, Biasucci G, Carducci C, Romano V: Two novel PAH gene mutations detected in Italian phenylketonuric patients. Hum Genet. 1997 Feb;99(2):275-8. [PubMed ]
- Byck S, Tyfield L, Carter K, Scriver CR: Prediction of multiple hypermutable codons in the human PAH gene: codon 280 contains recurrent mutations in Quebec and other populations. Hum Mutat. 1997;9(4):316-21. [PubMed ]
- Waters PJ, Parniak MA, Nowacki P, Scriver CR: In vitro expression analysis of mutations in phenylalanine hydroxylase: linking genotype to phenotype and structure to function. Hum Mutat. 1998;11(1):4-17. [PubMed ]
- Bosco P, Cali F, Meli C, Mollica F, Zammarchi E, Cerone R, Vanni C, Palillo L, Greco D, Romano V: Eight new mutations of the phenylalanine hydroxylase gene in Italian patients with hyperphenylalaninemia. Hum Mutat. 1998;11(3):240-3. [PubMed ]
- De Lucca M, Perez B, Desviat LR, Ugarte M: Molecular basis of phenylketonuria in Venezuela: presence of two novel null mutations. Hum Mutat. 1998;11(5):354-9. [PubMed ]
- Mallolas J, Campistol J, Lambruschini N, Vilaseca MA, Cambra FJ, Estivill X, Mila M: Two novel mutations in exon 11 of the PAH gene (V1163del TG and P362T) associated with classic phenylketonuira and mild phenylketonuria. Mutations in brief no. 143. Online. Hum Mutat. 1998;11(6):482. [PubMed ]
- Park YS, Seoung CS, Lee SW, Oh KH, Lee DH, Yim J: Identification of three novel mutations in Korean phenylketonuria patients: R53H, N207D, and Y325X. Hum Mutat. 1998;Suppl 1:S121-2. [PubMed ]
- Michiels L, Francois B, Raus J, Vandevyver C: Identification of seven new mutations in the phenylalanine hydroxylase gene, associated with hyperphenylalaninemia in the Belgian population. Hum Mutat. 1998;Suppl 1:S123-4. [PubMed ]
- Popescu T, Blazkova M, Kozak L, Jebeleanu G, Popescu A: Mutation spectrum and phenylalanine hydroxylase RFLP/VNTR background in 44 Romanian phenylketonuric alleles. Hum Mutat. 1998;12(5):314-9. [PubMed ]
- Waters PJ, Parniak MA, Hewson AS, Scriver CR: Alterations in protein aggregation and degradation due to mild and severe missense mutations (A104D, R157N) in the human phenylalanine hydroxylase gene (PAH). Hum Mutat. 1998;12(5):344-54. [PubMed ]
- Kibayashi M, Nagao M, Chiba S: Mutation analysis of the phenylalanine hydroxylase gene and its clinical implications in two Japanese patients with non-phenylketonuria hyperphenylalaninemia. J Hum Genet. 1998;43(4):231-6. [PubMed ]
- Hennermann JB, Vetter B, Wolf C, Windt E, Buhrdel P, Seidel J, Monch E, Kulozik AE: Phenylketonuria and hyperphenylalaninemia in eastern Germany: a characteristic molecular profile and 15 novel mutations. Hum Mutat. 2000;15(3):254-60. [PubMed ]
- Gjetting T, Petersen M, Guldberg P, Guttler F: Missense mutations in the N-terminal domain of human phenylalanine hydroxylase interfere with binding of regulatory phenylalanine. Am J Hum Genet. 2001 Jun;68(6):1353-60. Epub 2001 Apr 20. [PubMed ]
- Acosta A, Silva W Jr, Carvalho T, Gomes M, Zago M: Mutations of the phenylalanine hydroxylase (PAH) gene in Brazilian patients with phenylketonuria. Hum Mutat. 2001 Feb;17(2):122-30. [PubMed ]
- Yang Y, Drummond-Borg M, Garcia-Heras J: Molecular analysis of phenylketonuria (PKU) in newborns from Texas. Hum Mutat. 2001 Jun;17(6):523. [PubMed ]
- Gjetting T, Romstad A, Haavik J, Knappskog PM, Acosta AX, Silva WA Jr, Zago MA, Guldberg P, Guttler F: A phenylalanine hydroxylase amino acid polymorphism with implications for molecular diagnostics. Mol Genet Metab. 2001 Jul;73(3):280-4. [PubMed ]
|
| Enzyme 86 Metabolite References |
Not Available |
|
Enzyme 87
[top]
|
| Enzyme 87 ID |
5517 |
| Enzyme 87 Name |
Eosinophil peroxidase |
| Enzyme 87 Synonyms |
- EPO
- Eosinophil peroxidase light chain
- Eosinophil peroxidase heavy chain
|
| Enzyme 87 Gene Name |
EPX |
| Enzyme 87 Protein Sequence |
>Eosinophil peroxidase
MHLLPALAGVLATLVLAQPCEGTDPASPGAVETSVLRDCIAEAKLLVDAAYNWTQKSIKQ
RLRSGSASPMDLLSYFKQPVAATRTVVRAADYMHVALGLLEEKLQPQRSGPFNVTDVLTE
PQLRLLSQASGCALRDQAERCSDKYRTITGRCNNKRRPLLGASNQALARWLPAEYEDGLS
LPFGWTPSRRRNGFLLPLVRAVSNQIVRFPNERLTSDRGRALMFMQWGQFIDHDLDFSPE
SPARVAFTAGVDCERTCAQLPPCFPIKIPPNDPRIKNQRDCIPFFRSAPSCPQNKNRVRN
QINALTSFVDASMVYGSEVSLSLRLRNRTNYLGLLAINQRFQDNGRALLPFDNLHDDPCL
LTNRSARIPCFLAGDTRSTETPKLAAMHTLFMREHNRLATELRRLNPRWNGDKLYNEARK
IMGAMVQIITYRDFLPLVLGKARARRTLGHYRGYCSNVDPRVANVFTLAFRFGHTMLQPF
MFRLDSQYRASAPNSHVPLSSAFFASWRIVYEGGIDPILRGLMATPAKLNRQDAMLVDEL
RDRLFRQVRRIGLDLAALNMQRSRDHGLPGYNAWRRFCGLSQPRNLAQLSRVLKNQDLAR
KFLNLYGTPDNIDIWIGAIAEPLLPGARVGPLLACLFENQFRRARDGDRFWWQKRGVFTK
RQRKALSRISLSRIICDNTGITTVSRDIFRANIYPRGFVNCSRIPRLNLSAWRGT
|
| Enzyme 87 Number of Residues |
715 |
| Enzyme 87 Molecular Weight |
81039.5 |
| Enzyme 87 Theoretical pI |
10.81 |
| Enzyme 87 GO Classification |
| Function |
- antioxidant activity
- binding
- cation binding
- heme binding
- ion binding
- iron ion binding
- metal ion binding
- peroxidase activity
- transition metal ion binding
|
| Process |
- metabolic process
- oxidation reduction
- response to oxidative stress
- response to stimulus
- response to stress
|
| Component |
| — |
|
| Enzyme 87 General Function |
Involved in peroxidase activity |
| Enzyme 87 Specific Function |
Mediates tyrosine nitration of secondary granule proteins in mature resting eosinophils. Shows significant inhibitory activity towards Mycobacterium tuberculosis H37Rv by inducing bacterial fragmentation and lysis |
| Enzyme 87 Pathways |
- Arachidonic acid metabolism (map00590 )
- Methane metabolism (map00680 )
- Phenylalanine Metabolism (map00360 )
- Stilbene, coumarine and lignin biosynthesis (map00940 )
|
| Enzyme 87 Reactions |
- donor + H2O2 = oxidized donor + 2 H2O [RN:R03532]
|
| Enzyme 87 Pfam Domain Function |
|
| Enzyme 87 Signals |
|
| Enzyme 87 Transmembrane Regions |
|
| Enzyme 87 Essentiality |
Not Available |
| Enzyme 87 GenBank ID Protein |
66268791 |
| Enzyme 87 UniProtKB/Swiss-Prot ID |
P11678 |
| Enzyme 87 UniProtKB/Swiss-Prot Entry Name |
PERE_HUMAN |
| Enzyme 87 PDB ID |
Not Available |
| Enzyme 87 Cellular Location |
Not Available |
| Enzyme 87 Gene Sequence |
>2148 bp
ATGCATCTGCTCCCAGCCCTGGCAGGGGTCCTGGCCACACTCGTCCTCGCCCAGCCCTGT
GAGGGCACTGACCCAGCCTCCCCTGGGGCAGTGGAGACCTCGGTCCTGCGAGACTGCATA
GCAGAGGCCAAGTTGCTGGTGGATGCTGCCTACAATTGGACCCAGAAGAGCATCAAGCAG
CGGCTTCGCAGCGGTTCAGCCAGCCCCATGGACCTCCTGTCCTACTTCAAACAACCGGTA
GCAGCCACCAGGACAGTTGTTCGGGCCGCAGATTATATGCATGTGGCTTTGGGGCTGCTT
GAAGAGAAGTTACAACCCCAGCGGTCCGGACCCTTCAATGTCACTGATGTGCTAACAGAA
CCACAGCTGCGGCTGCTGTCCCAGGCCAGTGGCTGTGCTCTCCGGGACCAGGCCGAGCGC
TGCAGCGACAAGTACCGCACCATCACTGGACGGTGCAACAACAAGAGGAGACCCTTGCTA
GGGGCCTCCAACCAGGCTCTGGCTCGCTGGCTGCCCGCCGAGTATGAGGATGGGCTGTCG
CTCCCCTTCGGCTGGACCCCCAGCAGGAGGCGCAATGGCTTCCTTCTCCCTCTTGTCCGG
GCTGTCTCCAACCAGATTGTGCGCTTCCCCAATGAGAGACTGACCTCCGACCGTGGCCGA
GCCCTCATGTTCATGCAGTGGGGCCAGTTCATTGACCATGACCTGGACTTCTCCCCGGAG
TCCCCGGCCAGAGTGGCCTTCACTGCAGGCGTTGACTGTGAGAGGACCTGCGCCCAGCTG
CCCCCCTGCTTTCCCATCAAGATCCCACCCAATGACCCCCGCATCAAGAACCAGCGTGAC
TGCATCCCTTTCTTCCGCTCGGCACCCTCATGCCCCCAAAACAAGAACAGAGTCCGCAAC
CAGATCAACGCGCTCACCTCCTTTGTGGACGCCAGCATGGTGTATGGCAGTGAGGTCTCC
CTCTCGCTGCGGCTCCGCAACCGGACCAACTACCTGGGGCTGCTGGCCATCAACCAGCGC
TTTCAAGACAACGGCCGGGCCCTGCTGCCCTTCGACAACCTGCACGATGACCCCTGTCTC
CTCACCAACCGCTCGGCGCGCATCCCCTGCTTCCTGGCAGGTGACACCCGATCAACGGAA
ACCCCCAAACTGGCAGCCATGCACACCCTCTTTATGCGAGAGCACAACCGGCTGGCCACC
GAGCTGAGACGCCTGAATCCCCGGTGGAATGGAGACAAACTGTACAATGAGGCTCGGAAG
ATCATGGGGGCCATGGTCCAGATCATCACCTACCGAGACTTTCTGCCCCTGGTTCTGGGC
AAGGCCCGGGCCAGGAGAACCCTGGGGCACTACAGGGGGTACTGCTCCAATGTGGACCCA
CGGGTGGCCAATGTCTTCACCCTGGCCTTCCGCTTTGGCCACACAATGCTCCAGCCCTTC
ATGTTCCGCTTGGACAGTCAGTACCGGGCCTCCGCACCCAACTCGCATGTCCCACTTAGC
TCTGCCTTCTTTGCCAGCTGGCGGATCGTGTATGAAGGGGGCATCGACCCCATCCTCCGG
GGCCTCATGGCCACCCCTGCCAAGCTGAACCGTCAGGATGCCATGTTAGTGGATGAGCTC
CGGGACCGGCTGTTTCGGCAAGTGAGGAGGATTGGGCTGGACCTGGCAGCTCTCAACATG
CAACGAAGCCGGGACCACGGCCTTCCAGGGTACAATGCTTGGAGGCGCTTCTGTGGGCTC
TCCCAGCCCCGGAATTTGGCACAGCTTAGCCGGGTGCTGAAAAACCAGGACTTGGCAAGG
AAGTTCCTGAATTTGTATGGAACACCTGACAACATTGACATCTGGATTGGGGCCATCGCT
GAGCCTCTTTTGCCGGGGGCTCGAGTGGGGCCTCTTCTGGCTTGTCTGTTCGAGAACCAG
TTCAGAAGAGCCCGAGACGGAGACAGGTTCTGGTGGCAGAAACGAGGTGTTTTCACCAAA
AGACAGCGCAAGGCCCTGAGCAGAATTTCCTTGTCTCGAATTATATGTGACAATACCGGT
ATCACCACGGTTTCAAGGGACATCTTCAGAGCCAACATCTACCCTCGGGGCTTTGTGAAC
TGCAGCCGTATCCCCAGGTTGAACCTATCAGCCTGGCGAGGGACATGA
|
| Enzyme 87 GenBank Gene ID |
DQ054598 |
| Enzyme 87 GeneCard ID |
EPX |
| Enzyme 87 GenAtlas ID |
EPX |
| Enzyme 87 HGNC ID |
HGNC:3423 |
| Enzyme 87 Chromosome Location |
1 |
| Enzyme 87 Locus |
17q23.1 |
| Enzyme 87 SNPs |
SNPJam Report |
| Enzyme 87 General References |
- Sakamaki K, Tomonaga M, Tsukui K, Nagata S: Molecular cloning and characterization of a chromosomal gene for human eosinophil peroxidase. J Biol Chem. 1989 Oct 5;264(28):16828-36. [PubMed ]
- Ten RM, Pease LR, McKean DJ, Bell MP, Gleich GJ: Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family. J Exp Med. 1989 May 1;169(5):1757-69. [PubMed ]
- Oxvig C, Thomsen AR, Overgaard MT, Sorensen ES, Hojrup P, Bjerrum MJ, Gleich GJ, Sottrup-Jensen L: Biochemical evidence for heme linkage through esters with Asp-93 and Glu-241 in human eosinophil peroxidase. The ester with Asp-93 is only partially formed in vivo. J Biol Chem. 1999 Jun 11;274(24):16953-8. [PubMed ]
- Borelli V, Vita F, Shankar S, Soranzo MR, Banfi E, Scialino G, Brochetta C, Zabucchi G: Human eosinophil peroxidase induces surface alteration, killing, and lysis of Mycobacterium tuberculosis. Infect Immun. 2003 Feb;71(2):605-13. [PubMed ]
- Ulrich M, Petre A, Youhnovski N, Promm F, Schirle M, Schumm M, Pero RS, Doyle A, Checkel J, Kita H, Thiyagarajan N, Acharya KR, Schmid-Grendelmeier P, Simon HU, Schwarz H, Tsutsui M, Shimokawa H, Bellon G, Lee JJ, Przybylski M, Doring G: Post-translational tyrosine nitration of eosinophil granule toxins mediated by eosinophil peroxidase. J Biol Chem. 2008 Oct 17;283(42):28629-40. Epub 2008 Aug 11. [PubMed ]
- Romano M, Patriarca P, Melo C, Baralle FE, Dri P: Hereditary eosinophil peroxidase deficiency: immunochemical and spectroscopic studies and evidence for a compound heterozygosity of the defect. Proc Natl Acad Sci U S A. 1994 Dec 20;91(26):12496-500. [PubMed ]
- Nakamura H, Miyagawa K, Ogino K, Endo T, Imai T, Ozasa K, Motohashi Y, Matsuzaki I, Sasahara S, Hatta K, Eboshida A: High contribution contrast between the genes of eosinophil peroxidase and IL-4 receptor alpha-chain in Japanese cedar pollinosis. J Allergy Clin Immunol. 2003 Dec;112(6):1127-31. [PubMed ]
|
| Enzyme 87 Metabolite References |
Not Available |
|
Enzyme 88
[top]
|
| Enzyme 88 ID |
5523 |
| Enzyme 88 Name |
Sucrase-isomaltase, intestinal |
| Enzyme 88 Synonyms |
- Sucrase
- Isomaltase
|
| Enzyme 88 Gene Name |
SI |
| Enzyme 88 Protein Sequence |
>Sucrase-isomaltase, intestinal
MARKKFSGLEISLIVLFVIVTIIAIALIVVLATKTPAVDEISDSTSTPATTRVTTNPSDS
GKCPNVLNDPVNVRINCIPEQFPTEGICAQRGCCWRPWNDSLIPWCFFVDNHGYNVQDMT
TTSIGVEAKLNRIPSPTLFGNDINSVLFTTQNQTPNRFRFKITDPNNRRYEVPHQYVKEF
TGPTVSDTLYDVKVAQNPFSIQVIRKSNGKTLFDTSIGPLVYSDQYLQISARLPSDYIYG
IGEQVHKRFRHDLSWKTWPIFTRDQLPGDNNNNLYGHQTFFMCIEDTSGKSFGVFLMNSN
AMEIFIQPTPIVTYRVTGGILDFYILLGDTPEQVVQQYQQLVGLPAMPAYWNLGFQLSRW
NYKSLDVVKEVVRRNREAGIPFDTQVTDIDYMEDKKDFTYDQVAFNGLPQFVQDLHDHGQ
KYVIILDPAISIGRRANGTTYATYERGNTQHVWINESDGSTPIIGEVWPGLTVYPDFTNP
NCIDWWANECSIFHQEVQYDGLWIDMNEVSSFIQGSTKGCNVNKLNYPPFTPDILDKLMY
SKTICMDAVQNWGKQYDVHSLYGYSMAIATEQAVQKVFPNKRSFILTRSTFAGSGRHAAH
WLGDNTASWEQMEWSITGMLEFSLFGIPLVGADICGFVAETTEELCRRWMQLGAFYPFSR
NHNSDGYEHQDPAFFGQNSLLVKSSRQYLTIRYTLLPFLYTLFYKAHVFGETVARPVLHE
FYEDTNSWIEDTEFLWGPALLITPVLKQGADTVSAYIPDAIWYDYESGAKRPWRKQRVDM
YLPADKIGLHLRGGYIIPIQEPDVTTTASRKNPLGLIVALGENNTAKGDFFWDDGETKDT
IQNGNYILYTFSVSNNTLDIVCTHSSYQEGTTLAFQTVKILGLTDSVTEVRVAENNQPMN
AHSNFTYDASNQVLLIADLKLNLGRNFSVQWNQIFSENERFNCYPDADLATEQKCTQRGC
VWRTGSSLSKAPECYFPRQDNSYSVNSARYSSMGITADLQLNTANARIKLPSDPISTLRV
EVKYHKNDMLQFKIYDPQKKRYEVPVPLNIPTTPISTYEDRLYDVEIKENPFGIQIRRRS
SGRVIWDSWLPGFAFNDQFIQISTRLPSEYIYGFGEVEHTAFKRDLNWNTWGMFTRDQPP
GYKLNSYGFHPYYMALEEEGNAHGVFLLNSNAMDVTFQPTPALTYRTVGGILDFYMFLGP
TPEVATKQYHEVIGHPVMPAYWALGFQLCRYGYANTSEVRELYDAMVAANIPYDVQYTDI
DYMERQLDFTIGEAFQDLPQFVDKIRGEGMRYIIILDPAISGNETKTYPAFERGQQNDVF
VKWPNTNDICWAKVWPDLPNITIDKTLTEDEAVNASRAHVAFPDFFRTSTAEWWAREIVD
FYNEKMKFDGLWIDMNEPSSFVNGTTTNQCRNDELNYPPYFPELTKRTDGLHFRTICMEA
EQILSDGTSVLHYDVHNLYGWSQMKPTHDALQKTTGKRGIVISRSTYPTSGRWGGHWLGD
NYARWDNMDKSIIGMMEFSLFGISYTGADICGFFNNSEYHLCTRWMQLGAFYPYSRNHNI
ANTRRQDPASWNETFAEMSRNILNIRYTLLPYFYTQMHEIHANGGTVIRPLLHEFFDEKP
TWDIFKQFLWGPAFMVTPVLEPYVQTVNAYVPNARWFDYHTGKDIGVRGQFQTFNASYDT
INLHVRGGHILPCQEPAQNTFYSRQKHMKLIVAADDNQMAQGSLFWDDGESIDTYERDLY
LSVQFNLNQTTLTSTILKRGYINKSETRLGSLHVWGKGTTPVNAVTLTYNGNKNSLPFNE
DTTNMILRIDLTTHNVTLEEPIEINWS
|
| Enzyme 88 Number of Residues |
1827 |
| Enzyme 88 Molecular Weight |
209403.4 |
| Enzyme 88 Theoretical pI |
5.35 |
| Enzyme 88 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 88 General Function |
Involved in catalytic activity |
| Enzyme 88 Specific Function |
Plays an important role in the final stage of carbohydrate digestion |
| Enzyme 88 Pathways |
- Starch and Sucrose Metabolism (map00500 )
|
| Enzyme 88 Reactions |
- Hydrolysis of sucrose and maltose by an alpha-D-glucosidase-type action [RN:R00801 R06087] ALL_REAC R00801 R06087(G) > R00802 R06088(G)
|
| Enzyme 88 Pfam Domain Function |
|
| Enzyme 88 Signals |
|
| Enzyme 88 Transmembrane Regions |
|
| Enzyme 88 Essentiality |
Not Available |
| Enzyme 88 GenBank ID Protein |
36645 |
| Enzyme 88 UniProtKB/Swiss-Prot ID |
P14410 |
| Enzyme 88 UniProtKB/Swiss-Prot Entry Name |
SUIS_HUMAN |
| Enzyme 88 PDB ID |
Not Available |
| Enzyme 88 Cellular Location |
Not Available |
| Enzyme 88 Gene Sequence |
>5484 bp
ATGGCAAGAAAGAAATTTAGTGGATTGGAAATCTCTCTGATTGTCCTTTTTGTCATAGTT
ACTATAATAGCTATTGCCTTAATTGTTGTTTTAGCAACTAAGACACCTGCTGTTGATGAA
ATTAGTGATTCTACTTCAACTCCAGCTACTACTCGTGTGACTACAAATCCTTCTGATTCA
GGAAAATGTCCAAATGTGTTAAATGATCCTGTCAATGTGAGAATAAACTGCATTCCAGAA
CAATTCCCAACAGAGGGAATTTGTGCACAGAGAGGCTGCTGCTGGAGGCCGTGGAATGAC
TCTCTTATTCCTTGGTGCTTCTTCGTTGATAATCATGGTTATAACGTTCAAGACATGACA
ACAACAAGTATTGGAGTTGAAGCCAAATTAAACAGGATACCTTCACCTACACTATTTGGA
AATGACATCAACAGTGTTCTCTTCACAACTCAAAATCAGACACCCAATCGTTTCCGGTTC
AAGATTACTGATCCAAATAATAGAAGATATGAAGTTCCTCATCAGTATGTAAAAGAGTTT
ACTGGACCCACAGTTTCTGATACGTTGTATGATGTGAAGGTTGCCCAAAACCCATTTAGC
ATCCAAGTTATTAGGAAAAGCAACGGTAAAACTTTGTTTGACACCAGCATTGGTCCCTTA
GTGTACTCTGACCAGTACTTACAGATCTCAGCCCGTCTTCCAAGTGATTATATTTATGGT
ATTGGAGAACAAGTTCATAAGAGATTTCGTCATGATTTATCCTGGAAAACATGGCCAATT
TTTACTCGAGACCAACTTCCTGGTGATAATAATAATAATTTATACGGCCATCAAACATTC
TTTATGTGTATTGAAGATACATCTGGAAAGTCATTCGGTGTTTTTTTAATGAATAGCAAT
GCAATGGAGATTTTTATCCAGCCTACTCCAATAGTAACATATAGAGTTACCGGTGGCATT
CTGGATTTTTACATCCTTCTAGGAGATACACCAGAACAAGTAGTTCAACAGTATCAACAG
CTTGTTGGACTACCAGCAATGCCAGCATATTGGAATCTTGGATTCCAACTAAGTCGCTGG
AATTATAAGTCACTAGATGTAGTGAAAGAAGTGGTAAGGAGAAACCGGGAAGCTGGCATA
CCATTTGATACACAGGTCACTGATATTGACTACATGGAAGACAAGAAAGACTTTACTTAT
GATCAAGTTGCGTTTAACGGACTCCCTCAATTTGTGCAAGATTTGCATGACCATGGACAG
AAATATGTCATCATCTTGGACCCTGCAATTTCCATAGGTCGACGTGCCAATGGAACAACA
TATGCAACCTATGAGAGGGGAAACACACAACATGTGTGGATAAATGAGTCAGATGGAAGT
ACACCAATTATTGGAGAGGTATGGCCAGGATTAACAGTATACCCTGATTTCACTAATCCA
AACTGCATTGATTGGTGGGCAAATGAATGCAGTATTTTCCATCAAGAAGTGCAATATGAT
GGACTTTGGATTGACATGAATGAAGTTTCCAGCTTTATTCAAGGTTCAACAAAAGGATGT
AATGTAAACAAATTGAATTATCCACCGTTTACTCCTGATATTCTTGACAAACTCATGTAT
TCCAAAACAATTTGCATGGATGCTGTGCAGAACTGGGGTAAACAGTATGATGTTCATAGC
CTCTATGGATACAGCATGGCTATAGCCACAGAGCAAGCTGTACAAAAAGTTTTTCCTAAT
AAGAGAAGCTTCATTCTTACCCGCTCAACATTTGCTGGATCTGGAAGACATGCTGCTCAT
TGGTTAGGAGACAATACTGCTTCATGGGAACAAATGGAATGGTCTATAACTGGAATGCTG
GAGTTCAGTTTGTTTGGAATACCTTTGGTTGGAGCAGACATCTGTGGATTTGTGGCTGAA
ACCACAGAAGAACTTTGCAGAAGATGGATGCAACTTGGGGCATTTTATCCATTTTCCAGA
AACCATAATTCTGACGGATATGAACATCAGGATCCTGCATTTTTTGGGCAGAATTCACTT
TTGGTTAAATCATCAAGGCAGTATTTAACTATTCGCTACACCTTATTACCCTTCCTCTAC
ACTCTGTTTTATAAAGCCCATGTGTTTGGAGAAACAGTAGCAAGACCAGTTCTTCATGAG
TTTTATGAGGATACGAACAGCTGGATTGAGGACACTGAGTTTTTGTGGGGCCCTGCATTA
CTTATTACTCCTGTTCTAAAACAGGGAGCAGATACTGTGAGTGCCTACATCCCTGATGCT
ATTTGGTATGATTATGAATCTGGTGCAAAAAGGCCATGGAGGAAACAACGGGTTGATATG
TATCTTCCAGCAGACAAAATAGGATTACATCTTAGAGGAGGTTATATCATCCCCATTCAA
GAACCAGATGTAACAACAACAGCAAGCCGTAAGAATCCTCTAGGACTTATAGTCGCATTA
GGTGAAAACAACACAGCCAAAGGAGACTTTTTCTGGGATGATGGAGAAACTAAAGATACA
ATACAAAATGGCAACTACATATTATATACATTTTCAGTTTCTAATAACACATTAGATATT
GTGTGCACACATTCATCATATCAGGAAGGAACTACCTTAGCATTTCAGACTGTAAAAATC
CTTGGGTTGACAGACAGTGTTACAGAAGTTAGAGTGGCGGAAAATAATCAACCAATGAAC
GCTCATTCCAATTTCACTTATGATGCTTCTAACCAGGTTCTCCTAATTGCAGATCTCAAA
CTTAATCTTGGAAGAAACTTTAGTGTTCAATGGAATCAAATTTTCTCAGAAAATGAAAGA
TTTAATTGTTATCCAGATGCAGATTTGGCAACTGAACAAAAGTGCACACAACGTGGCTGT
GTATGGAGAACGGGTTCTTCTCTATCCAAAGCACCTGAGTGTTACTTTCCCAGACAAGAT
AACTCTTATTCAGTCAACTCAGCTCGCTATTCATCCATGGGTATAACAGCTGACCTCCAA
CTAAATACTGCAAATGCCAGAATAAAGTTACCTTCTGACCCCATCTCAACTCTTCGTGTG
GAGGTGAAATATCACAAAAATGATATGTTGCAGTTTAAGATTTATGATCCCCAAAAGAAG
AGATATGAAGTACCAGTACCGTTAAACATTCCAACCACCCCAATAAGTACTTATGAAGAC
AGACTTTATGATGTGGAAATCAAGGAAAATCCTTTTGGCATCCAGATTCGACGGAGAAGC
AGTGGAAGAGTCATTTGGGATTCTTGGCTGCCTGGATTTGCTTTTAATGACCAGTTCATT
CAAATATCGACTCGCCTGCCATCAGAATATATATATGGTTTTGGGGAAGTGGAACATACA
GCATTTAAGCGAGATCTGAACTGGAATACTTGGGGAATGTTCACAAGAGACCAACCCCCT
GGTTACAAACTTAATTCCTATGGATTTCATCCCTATTACATGGCTCTGGAAGAGGAGGGC
AATGCTCATGGTGTTTTCTTACTCAACAGCAATGCAATGGATGTTACATTCCAGCCAACT
CCTGCTCTAACTTACCGTACAGTTGGAGGGATCTTGGATTTTTATATGTTTTTGGGCCCA
ACTCCACAAGTTGCAACAAAGCAATACCATGAAGTAATTGGCCATCCAGTCATGCCAGCT
TATTGGGCTTTGGGATTCCAATTATGTCGTTATGGATATGCAAATACTTCAGAGGTTCGG
GAATTATATGACGCTATGGTGGCTGCTAACATCCCCTATGATGTTCAGTACACAGACATT
GACTACATGGAAAGGCAGCTAGACTTTACAATTGGTGAAGCATTCCAGGACCTTCCTCAG
TTTGTTGACAAAATAAGAGGAGAAGGAATGAGATACATTATTATCCTGGATCCAGCAATT
TCAGGAAATGAAACAAAGACTTACCCTGCATTTGAAAGAGGACAGCAGAATGATGTCTTT
GTCAAATGGCCAAACACCAATGACATTTGTTGGGCAAAGGTTTGGCCAGATTTGCCCAAC
ATAACAATAGATAAAACTCTAACGGAAGATGAAGCTGTTAATGCTTCCAGAGCTCATGTA
GCTTTCCCAGATTTCTTCAGGACTTCCACAGCAGAGTGGTGGGCCAGAGAAATTGTGGAC
TTTTACAATGAAAAGATGAAGTTTGATGGTTTGTGGATTGATATGAATGAGCCATCAAGT
TTTGTAAATGGAACAACTACTAATCAATGCAGAAATGACGAACTAAATTATCCACCTTAT
TTCCCAGAACTCACAAAAAGAACTGATGGATTACATTTCAGAACAATTTGCATGGAAGCT
GAGCAGATTCTTAGTGATGGAACATCAGTTTTGCATTACGATGTTCACAATCTCTATGGA
TGGTCACAGATGAAACCTACTCATGATGCATTGCAAAAGACAACTGGAAAAAGAGGGATT
GTAATTTCTCGTTCCACGTATCCTACTAGTGGACGATGGGGAGGACACTGGCTTGGAGAC
AACTATGCACGATGGGACAACATGGACAAATCAATCATTGGTATGATGGAATTTAGTCTG
TTTGGAATATCATATACTGGAGCAGACATCTGTGGTTTTTTCAACAACTCAGAATATCAT
CTCTGTACCCGCTGGATGCAACTTGGAGCATTTTATCCATACTCAAGGAATCACAACATT
GCAAATACTAGAAGACAAGATCCCGCTTCCTGGAATGAAACTTTTGCTGAAATGTCAAGG
AATATTCTAAATATTAGATACACCTTATTGCCCTATTTTTACACACAAATGCATGAAATT
CATGCTAATGGTGGCACTGTTATCCGACCCCTTTTGCATGAGTTCTTTGATGAAAAACCA
ACCTGGGATATATTCAAGCAGTTCTTATGGGGTCCAGCATTTATGGTTACCCCAGTACTG
GAACCTTATGTTCAAACTGTAAATGCCTACGTCCCCAATGCTCGGTGGTTTGACTACCAT
ACAGGCAAAGATATTGGCGTCAGAGGACAATTTCAAACATTTAATGCTTCTTATGACACA
ATAAACCTACATGTCCGTGGTGGTCACATCCTACCATGTCAAGAGCCAGCTCAAAACACA
TTTTACAGTCGACAAAAACACATGAAGCTCATTGTTGCTGCAGATGATAATCAGATGGCA
CAGGGTTCTCTGTTTTGGGATGATGGAGAGAGTATAGACACCTATGAAAGAGACCTATAT
TTATCTGTACAATTTAATTTAAACCAGACCACCTTAACAAGCACTATATTGAAGAGAGGT
TACATAAATAAAAGTGAAACGAGGCTTGGATCCCTTCATGTATGGGGGAAAGGAACTACT
CCTGTCAATGCAGTTACTCTAACGTATAACGGAAATAAAAATTCGCTTCCTTTTAATGAA
GACACTACCAACATGATATTACGTATTGATCTGACCACACACAATGTTACTCTAGAAGAA
CCAATAGAAATCAACTGGTCATGA
|
| Enzyme 88 GenBank Gene ID |
X63597 |
| Enzyme 88 GeneCard ID |
SI |
| Enzyme 88 GenAtlas ID |
SI |
| Enzyme 88 HGNC ID |
HGNC:10856 |
| Enzyme 88 Chromosome Location |
3 |
| Enzyme 88 Locus |
3q25.2-q26.2 |
| Enzyme 88 SNPs |
SNPJam Report |
| Enzyme 88 General References |
- Chantret I, Lacasa M, Chevalier G, Ruf J, Islam I, Mantei N, Edwards Y, Swallow D, Rousset M: Sequence of the complete cDNA and the 5' structure of the human sucrase-isomaltase gene. Possible homology with a yeast glucoamylase. Biochem J. 1992 Aug 1;285 ( Pt 3):915-23. [PubMed ]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Green F, Edwards Y, Hauri HP, Povey S, Ho MW, Pinto M, Swallow D: Isolation of a cDNA probe for a human jejunal brush-border hydrolase, sucrase-isomaltase, and assignment of the gene locus to chromosome 3. Gene. 1987;57(1):101-10. [PubMed ]
- Gorvel JP, Ferrero A, Chambraud L, Rigal A, Bonicel J, Maroux S: Expression of sucrase-isomaltase and dipeptidylpeptidase IV in human small intestine and colon. Gastroenterology. 1991 Sep;101(3):618-25. [PubMed ]
- Ouwendijk J, Moolenaar CE, Peters WJ, Hollenberg CP, Ginsel LA, Fransen JA, Naim HY: Congenital sucrase-isomaltase deficiency. Identification of a glutamine to proline substitution that leads to a transport block of sucrase-isomaltase in a pre-Golgi compartment. J Clin Invest. 1996 Feb 1;97(3):633-41. [PubMed ]
- Jacob R, Zimmer KP, Schmitz J, Naim HY: Congenital sucrase-isomaltase deficiency arising from cleavage and secretion of a mutant form of the enzyme. J Clin Invest. 2000 Jul;106(2):281-7. [PubMed ]
- Spodsberg N, Jacob R, Alfalah M, Zimmer KP, Naim HY: Molecular basis of aberrant apical protein transport in an intestinal enzyme disorder. J Biol Chem. 2001 Jun 29;276(26):23506-10. Epub 2001 May 4. [PubMed ]
- Ritz V, Alfalah M, Zimmer KP, Schmitz J, Jacob R, Naim HY: Congenital sucrase-isomaltase deficiency because of an accumulation of the mutant enzyme in the endoplasmic reticulum. Gastroenterology. 2003 Dec;125(6):1678-85. [PubMed ]
- Sander P, Alfalah M, Keiser M, Korponay-Szabo I, Kovacs JB, Leeb T, Naim HY: Novel mutations in the human sucrase-isomaltase gene (SI) that cause congenital carbohydrate malabsorption. Hum Mutat. 2006 Jan;27(1):119. [PubMed ]
|
| Enzyme 88 Metabolite References |
Not Available |
|
Enzyme 89
[top]
|
| Enzyme 89 ID |
5526 |
| Enzyme 89 Name |
4-trimethylaminobutyraldehyde dehydrogenase |
| Enzyme 89 Synonyms |
- TMABADH
- Aldehyde dehydrogenase E3 isozyme
- Aldehyde dehydrogenase family 9 member A1
- Gamma-aminobutyraldehyde dehydrogenase
- R-aminobutyraldehyde dehydrogenase
|
| Enzyme 89 Gene Name |
ALDH9A1 |
| Enzyme 89 Protein Sequence |
>4-trimethylaminobutyraldehyde dehydrogenase
MSTGTFVVSQPLNYRGGARVEPADASGTEKAFEPATGRVIATFTCSGEKEVNLAVQNAKA
AFKIWSQKSGMERCRILLEAARIIREREDEIATMECINNGKSIFEARLDIDISWQCLEYY
AGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIASWKSAPALACGNAMVFK
PSPFTPVSALLLAEIYSEAGVPPGLFNVVQGGAATGQFLCQHPDVAKVSFTGSVPTGMKI
MEMSAKGIKPVTLELGGKSPLIIFSDCDMNNAVKGALMANFLTQGQVCCNGTRVFVQKEI
LDKFTEEVVKQTQRIKIGDPLLEDTRMGPLINRPHLERVLGFVKVAKEQGAKVLCGGDIY
VPEDPKLKDGYYMRPCVLTNCRDDMTCVKEEIFGPVMSILSFDTEAEVLERANDTTFGLA
AGVFTRDIQRAHRVVAELQAGTCFINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQL
KTVCVEMGDVESAF
|
| Enzyme 89 Number of Residues |
494 |
| Enzyme 89 Molecular Weight |
53801.5 |
| Enzyme 89 Theoretical pI |
5.61 |
| Enzyme 89 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 89 General Function |
Involved in oxidoreductase activity |
| Enzyme 89 Specific Function |
Converts gamma-trimethylaminobutyraldehyde into gamma- butyrobetaine. Catalyzes the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction |
| Enzyme 89 Pathways |
|
| Enzyme 89 Reactions |
- 4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+ [RN:R03283]
|
| Enzyme 89 Pfam Domain Function |
|
| Enzyme 89 Signals |
|
| Enzyme 89 Transmembrane Regions |
|
| Enzyme 89 Essentiality |
Not Available |
| Enzyme 89 GenBank ID Protein |
7248636 |
| Enzyme 89 UniProtKB/Swiss-Prot ID |
P49189 |
| Enzyme 89 UniProtKB/Swiss-Prot Entry Name |
AL9A1_HUMAN |
| Enzyme 89 PDB ID |
Not Available |
| Enzyme 89 Cellular Location |
Not Available |
| Enzyme 89 Gene Sequence |
>1485 bp
ATGAGCACTGGCACCTTCGTCGTGTCGCAGCCGCTCAATTACCGCGGCGGGGCCCGCGTG
GAGCCGGCGGACGCCTCCGGTACCGAGAAAGCTTTCGAGCCAGCAACCGGCCGAGTGATA
GCTACTTTCACATGTTCAGGAGAAAAGGAAGTAAATTTGGCTGTTCAAAATGCAAAGGCT
GCTTTTAAAATATGGAGTCAAAAATCTGGCATGGAGCGTTGCCGAATCCTTTTGGAGGCT
GCCAGGATAATAAGGGAACGGGAGGATGAAATTGCTACTATGGAGTGCATCAACAATGGC
AAGTCCATCTTTGAGGCCCGCTTGGACATTGACATTTCCTGGCAGTGCCTGGAGTATTAT
GCGGGCTTGGCTGCATCCATGGCTGGTGAACACATCCAGCTCCCAGGTGGATCGTTTGGT
TATACCAGAAGAGAACCACTTGGGGTATGTGTGGGAATAGGAGCATGGAACTACCCCTTT
CAGATTGCCTCTTGGAAGTCGGCTCCAGCATTAGCCTGTGGTAATGCCATGGTCTTTAAA
CCTTCTCCCTTTACACCTGTTTCTGCATTGCTACTGGCTGAAATCTACAGTGAGGCTGGT
GTACCTCCTGGGCTCTTCAATGTGGTGCAGGGAGGGGCTGCCACAGGCCAGTTTCTGTGT
CAGCATCCCGATGTGGCCAAAGTCTCCTTCACTGGAAGTGTGCCCACTGGCATGAAGATC
ATGGAGATGTCAGCTAAAGGAATCAAACCTGTTACCTTGGAACTTGGAGGCAAATCTCCA
CTCATCATCTTCTCAGACTGTGATATGAACAATGCTGTAAAGGGGGCGCTGATGGCCAAC
TTCCTCACACAAGGCCAGGTTTGCTGTAATGGCACAAGAGTATTTGTGCAGAAAGAAATT
CTTGATAAATTTACAGAGGAAGTGGTGAAACAGACCCAAAGGATTAAAATTGGAGATCCC
CTTCTGGAAGATACAAGGATGGGTCCACTCATCAACCGACCACACCTGGAGCGAGTCCTT
GGGTTTGTCAAAGTGGCAAAGGAGCAGGGTGCTAAAGTGTTATGTGGTGGAGATATATAT
GTACCTGAAGATCCCAAATTAAAGGATGGATATTACATGAGACCTTGTGTATTAACTAAT
TGCAGAGACGACATGACCTGTGTGAAGGAAGAGATCTTTGGGCCTGTTATGTCCATTTTA
TCATTTGACACTGAAGCTGAGGTTCTAGAAAGAGCCAATGATACCACTTTTGGACTAGCA
GCTGGCGTCTTTACCAGGGACATCCAACGGGCTCATAGAGTGGTAGCTGAGCTTCAGGCT
GGGACGTGCTTCATTAACAACTATAACGTCAGCCCAGTGGAGTTGCCCTTTGGTGGATAT
AAGAAGTCAGGATTTGGCAGAGAGAACGGCCGTGTGACAATCGAATATTATTCACAGCTG
AAGACTGTGTGTGTGGAGATGGGTGATGTGGAATCTGCTTTTTGA
|
| Enzyme 89 GenBank Gene ID |
AF172093 |
| Enzyme 89 GeneCard ID |
ALDH9A1 |
| Enzyme 89 GenAtlas ID |
ALDH9A1 |
| Enzyme 89 HGNC ID |
HGNC:412 |
| Enzyme 89 Chromosome Location |
1 |
| Enzyme 89 Locus |
1q23.1 |
| Enzyme 89 SNPs |
SNPJam Report |
| Enzyme 89 General References |
- Lin SW, Chen JC, Hsu LC, Hsieh CL, Yoshida A: Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression. Genomics. 1996 Jun 15;34(3):376-80. [PubMed ]
- Vaz FM, Fouchier SW, Ofman R, Sommer M, Wanders RJ: Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis. J Biol Chem. 2000 Mar 10;275(10):7390-4. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Kikonyogo A, Pietruszko R: Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution. Biochem J. 1996 May 15;316 ( Pt 1):317-24. [PubMed ]
- Kurys G, Shah PC, Kikonygo A, Reed D, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde. Eur J Biochem. 1993 Dec 1;218(2):311-20. [PubMed ]
- Kurys G, Ambroziak W, Pietruszko R: Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde. J Biol Chem. 1989 Mar 15;264(8):4715-21. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 89 Metabolite References |
Not Available |
|
Enzyme 90
[top]
|
| Enzyme 90 ID |
5528 |
| Enzyme 90 Name |
Alpha-aminoadipic semialdehyde dehydrogenase |
| Enzyme 90 Synonyms |
- Alpha-AASA dehydrogenase
- Aldehyde dehydrogenase family 7 member A1
- Antiquitin-1
- Betaine aldehyde dehydrogenase
- Delta1-piperideine-6-carboxylate dehydrogenase
- P6c dehydrogenase
|
| Enzyme 90 Gene Name |
ALDH7A1 |
| Enzyme 90 Protein Sequence |
>Alpha-aminoadipic semialdehyde dehydrogenase
MWRLPRALCVHAAKTSKLSGPWSRPAAFMSTLLINQPQYAWLKELGLREENEGVYNGSWG
GRGEVITTYCPANNEPIARVRQASVADYEETVKKAREAWKIWADIPAPKRGEIVRQIGDA
LREKIQVLGSLVSLEMGKILVEGVGEVQEYVDICDYAVGLSRMIGGPILPSERSGHALIE
QWNPVGLVGIITAFNFPVAVYGWNNAIAMICGNVCLWKGAPTTSLISVAVTKIIAKVLED
NKLPGAICSLTCGGADIGTAMAKDERVNLLSFTGSTQVGKQVGLMVQERFGRSLLELGGN
NAIIAFEDADLSLVVPSALFAAVGTAGQRCTTARRLFIHESIHDEVVNRLKKAYAQIRVG
NPWDPNVLYGPLHTKQAVSMFLGAVEEAKKEGGTVVYGGKVMDRPGNYVEPTIVTGLGHD
ASIAHTETFAPILYVFKFKNEEEVFAWNNEVKQGLSSSIFTKDLGRIFRWLGPKGSDCGI
VNVNIPTSGAEIGGAFGGEKHTGGGRESGSDAWKQYMRRSTCTINYSKDLPLAQGIKFQ
|
| Enzyme 90 Number of Residues |
539 |
| Enzyme 90 Molecular Weight |
58486.7 |
| Enzyme 90 Theoretical pI |
8.09 |
| Enzyme 90 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 90 General Function |
Involved in oxidoreductase activity |
| Enzyme 90 Specific Function |
Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism |
| Enzyme 90 Pathways |
|
| Enzyme 90 Reactions |
- L-2-aminoadipate 6-semialdehyde + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H + H+ [RN:R03102 R03103]
|
| Enzyme 90 Pfam Domain Function |
|
| Enzyme 90 Signals |
|
| Enzyme 90 Transmembrane Regions |
|
| Enzyme 90 Essentiality |
Not Available |
| Enzyme 90 GenBank ID Protein |
188035924 |
| Enzyme 90 UniProtKB/Swiss-Prot ID |
P49419 |
| Enzyme 90 UniProtKB/Swiss-Prot Entry Name |
AL7A1_HUMAN |
| Enzyme 90 PDB ID |
Not Available |
| Enzyme 90 Cellular Location |
Not Available |
| Enzyme 90 Gene Sequence |
>1620 bp
ATGTGGCGCCTTCCTCGCGCGCTGTGTGTGCACGCTGCAAAGACCAGCAAGCTCTCTGGA
CCTTGGAGCAGGCCTGCCGCCTTCATGTCCACTCTCCTCATCAATCAGCCCCAGTATGCG
TGGCTGAAAGAGCTGGGGCTCCGCGAGGAAAACGAGGGCGTGTATAATGGAAGCTGGGGA
GGCCGGGGAGAGGTTATTACGACCTATTGCCCTGCTAACAACGAGCCAATAGCAAGAGTC
CGACAGGCCAGTGTGGCAGACTATGAAGAAACTGTAAAGAAAGCAAGAGAAGCATGGAAA
ATCTGGGCAGATATTCCTGCTCCAAAACGAGGAGAAATAGTAAGACAGATTGGCGATGCC
TTGCGGGAGAAGATCCAAGTACTAGGAAGCTTGGTGTCTTTGGAGATGGGGAAAATCTTA
GTGGAAGGTGTGGGTGAAGTTCAGGAGTATGTGGATATCTGTGACTATGCTGTTGGTTTA
TCAAGGATGATTGGAGGACCTATCTTGCCTTCTGAAAGATCTGGCCATGCACTGATTGAG
CAGTGGAATCCCGTAGGCCTGGTTGGAATCATCACGGCATTCAATTTCCCTGTGGCAGTG
TATGGTTGGAACAACGCCATCGCCATGATCTGTGGAAATGTCTGCCTCTGGAAAGGAGCT
CCAACCACTTCCCTCATTAGTGTGGCTGTCACAAAGATAATAGCCAAGGTTCTGGAGGAC
AACAAGCTGCCTGGTGCAATTTGTTCCTTGACTTGTGGTGGAGCAGATATTGGCACAGCA
ATGGCCAAAGATGAACGAGTGAACCTGCTGTCCTTCACTGGGAGCACTCAGGTGGGAAAA
CAGGTGGGCCTGATGGTGCAGGAGAGGTTTGGGAGAAGTCTGTTGGAACTTGGAGGAAAC
AATGCCATTATTGCCTTTGAAGATGCAGACCTCAGCTTAGTTGTTCCATCAGCTCTCTTC
GCTGCTGTGGGAACAGCTGGCCAGAGGTGTACCACTGCGAGGCGACTGTTTATACATGAA
AGCATCCATGATGAGGTTGTAAACAGACTTAAAAAGGCCTATGCACAGATCCGAGTTGGG
AACCCATGGGACCCTAATGTTCTCTATGGGCCACTCCACACCAAGCAGGCAGTGAGCATG
TTTCTTGGAGCAGTGGAAGAAGCAAAGAAAGAAGGTGGCACAGTGGTCTATGGGGGCAAG
GTTATGGATCGCCCTGGAAATTATGTAGAACCGACAATTGTGACAGGTCTTGGCCACGAT
GCGTCCATTGCACACACAGAGACTTTTGCTCCGATTCTCTATGTCTTTAAATTCAAGAAT
GAAGAAGAGGTCTTTGCATGGAATAATGAAGTAAAACAGGGACTTTCAAGTAGCATCTTT
ACCAAAGATCTGGGCAGAATCTTTCGCTGGCTTGGACCTAAAGGATCAGACTGTGGCATT
GTAAATGTCAACATTCCAACAAGTGGGGCTGAGATTGGAGGTGCCTTTGGAGGAGAAAAG
CACACTGGTGGTGGCAGGGAGTCTGGCAGTGATGCCTGGAAACAGTACATGAGAAGGTCT
ACTTGTACTATCAACTACAGTAAAGACCTTCCTCTGGCCCAAGGAATCAAGTTTCAGTAA
|
| Enzyme 90 GenBank Gene ID |
NM_001182.3 |
| Enzyme 90 GeneCard ID |
ALDH7A1 |
| Enzyme 90 GenAtlas ID |
ALDH7A1 |
| Enzyme 90 HGNC ID |
HGNC:877 |
| Enzyme 90 Chromosome Location |
5 |
| Enzyme 90 Locus |
5q31 |
| Enzyme 90 SNPs |
SNPJam Report |
| Enzyme 90 General References |
- Lee P, Kuhl W, Gelbart T, Kamimura T, West C, Beutler E: Homology between a human protein and a protein of the green garden pea. Genomics. 1994 May 15;21(2):371-8. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Skvorak AB, Robertson NG, Yin Y, Weremowicz S, Her H, Bieber FR, Beisel KW, Lynch ED, Beier DR, Morton CC: An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1). Genomics. 1997 Dec 1;46(2):191-9. [PubMed ]
- Brocker C, Lassen N, Estey T, Pappa A, Cantore M, Orlova VV, Chavakis T, Kavanagh KL, Oppermann U, Vasiliou V: Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress. J Biol Chem. 2010 Jun 11;285(24):18452-63. Epub 2010 Mar 5. [PubMed ]
- Mills PB, Struys E, Jakobs C, Plecko B, Baxter P, Baumgartner M, Willemsen MA, Omran H, Tacke U, Uhlenberg B, Weschke B, Clayton PT: Mutations in antiquitin in individuals with pyridoxine-dependent seizures. Nat Med. 2006 Mar;12(3):307-9. Epub 2006 Feb 19. [PubMed ]
|
| Enzyme 90 Metabolite References |
Not Available |
|
Enzyme 91
[top]
|
| Enzyme 91 ID |
5529 |
| Enzyme 91 Name |
Aldehyde dehydrogenase family 1 member A3 |
| Enzyme 91 Synonyms |
- Aldehyde dehydrogenase 6
- Retinaldehyde dehydrogenase 3
- RALDH-3
- RalDH3
|
| Enzyme 91 Gene Name |
ALDH1A3 |
| Enzyme 91 Protein Sequence |
>Aldehyde dehydrogenase family 1 member A3
MATANGAVENGQPDRKPPALPRPIRNLEVKFTKIFINNEWHESKSGKKFATCNPSTREQI
CEVEEGDKPDVDKAVEAAQVAFQRGSPWRRLDALSRGRLLHQLADLVERDRATLAALETM
DTGKPFLHAFFIDLEGCIRTLRYFAGWADKIQGKTIPTDDNVVCFTRHEPIGVCGAITPW
NFPLLMLVWKLAPALCCGNTMVLKPAEQTPLTALYLGSLIKEAGFPPGVVNIVPGFGPTV
GAAISSHPQINKIAFTGSTEVGKLVKEAASRSNLKRVTLELGGKNPCIVCADADLDLAVE
CAHQGVFFNQGQCCTAASRVFVEEQVYSEFVRRSVEYAKKRPVGDPFDVKTEQGPQIDQK
QFDKILELIESGKKEGAKLECGGSAMEDKGLFIKPTVFSEVTDNMRIAKEEIFGPVQPIL
KFKSIEEVIKRANSTDYGLTAAVFTKNLDKALKLASALESGTVWINCYNALYAQAPFGGF
KMSGNGRELGEYALAEYTEVKTVTIKLGDKNP
|
| Enzyme 91 Number of Residues |
512 |
| Enzyme 91 Molecular Weight |
56108.0 |
| Enzyme 91 Theoretical pI |
7.29 |
| Enzyme 91 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 91 General Function |
Involved in oxidoreductase activity |
| Enzyme 91 Specific Function |
Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Seems to be the key enzyme in the formation of an RA gradient along the dorso-ventral axis during the early eye development and also in the development of the olfactory system |
| Enzyme 91 Pathways |
|
| Enzyme 91 Reactions |
- an aldehyde + NAD(P)+ + H2O = an acid + NAD(P)H + H+ [RN:R00538 R00634]
|
| Enzyme 91 Pfam Domain Function |
|
| Enzyme 91 Signals |
|
| Enzyme 91 Transmembrane Regions |
|
| Enzyme 91 Essentiality |
Not Available |
| Enzyme 91 GenBank ID Protein |
46621670 |
| Enzyme 91 UniProtKB/Swiss-Prot ID |
P47895 |
| Enzyme 91 UniProtKB/Swiss-Prot Entry Name |
AL1A3_HUMAN |
| Enzyme 91 PDB ID |
Not Available |
| Enzyme 91 Cellular Location |
Not Available |
| Enzyme 91 Gene Sequence |
>1539 bp
ATGGCCACCGCTAACGGGGCCGTGGAAAACGGGCAGCCGGACAGGAAGCCGCCGGCCCTG
CCGCGCCCCATCCGCAACCTGGAGGTCAAGTTCACCAAGATATTTATCAACAATGAATGG
CACGAATCCAAGAGTGGGAAAAAGTTTGCTACATGTAACCCTTCAACTCGGGAGCAAATA
TGTGAAGTGGAAGAAGGAGATAAGCCCGACGTGGACAAGGCTGTGGAGGCTGCACAGGTT
GCCTTCCAGAGGGGCTCGCCATGGCGCCGGCTGGATGCCCTGAGTCGTGGGCGGCTGCTG
CACCAGCTGGCTGACCTGGTGGAGAGGGACCGCGCCACCTTGGCCGCCCTGGAGACGATG
GATACAGGGAAGCCATTTCTTCATGCTTTTTTCATCGACCTGGAGGGCTGTATTAGAACC
CTCAGATACTTTGCAGGGTGGGCAGACAAAATCCAGGGCAAGACCATCCCCACAGATGAC
AACGTCGTGTGCTTCACCAGGCATGAGCCCATTGGTGTCTGTGGGGCCATCACTCCATGG
AACTTCCCCCTGCTGATGCTGGTGTGGAAGCTGGCACCCGCCCTCTGCTGTGGGAACACC
ATGGTCCTGAAGCCTGCGGAGCAGACACCTCTCACCGCCCTTTATCTCGGCTCTCTGATC
AAAGAGGCCGGGTTCCCTCCAGGAGTGGTGAACATTGTGCCAGGATTCGGGCCCACAGTG
GGAGCAGCAATTTCTTCTCACCCTCAGATCAACAAGATCGCCTTCACCGGCTCCACAGAG
GTTGGAAAACTGGTTAAAGAAGCTGCGTCCCGGAGCAATCTGAAGCGGGTGACGCTGGAG
CTGGGGGGGAAGAACCCCTGCATCGTGTGTGCGGACGCTGACTTGGACTTGGCAGTGGAG
TGTGCCCATCAGGGAGTGTTCTTCAACCAAGGCCAGTGTTGCACGGCAGCCTCCAGGGTG
TTCGTGGAGGAGCAGGTCTACTCTGAGTTTGTCAGGCGGAGCGTGGAGTATGCCAAGAAA
CGGCCCGTGGGAGACCCCTTCGATGTCAAAACAGAACAGGGGCCTCAGATTGATCAAAAG
CAGTTCGACAAAATCTTAGAGCTGATCGAGAGTGGGAAGAAGGAAGGGGCCAAGCTGGAA
TGCGGGGGCTCAGCCATGGAAGACAAGGGGCTCTTCATCAAACCCACTGTCTTCTCAGAA
GTCACAGACAACATGCGGATTGCCAAAGAGGAGATTTTCGGGCCAGTGCAACCAATACTG
AAGTTCAAAAGTATCGAAGAAGTGATAAAAAGAGCGAATAGCACCGACTATGGACTCACA
GCAGCCGTGTTCACAAAAAATCTCGACAAAGCCCTGAAGTTGGCTTCTGCCTTAGAGTCT
GGAACGGTCTGGATCAACTGCTACAACGCCCTCTATGCACAGGCTCCATTTGGTGGCTTT
AAAATGTCAGGAAATGGCAGAGAACTAGGTGAATACGCTTTGGCCGAATACACAGAAGTG
AAAACTGTCACCATCAAACTTGGCGACAAGAACCCCTGA
|
| Enzyme 91 GenBank Gene ID |
BC069274 |
| Enzyme 91 GeneCard ID |
ALDH1A3 |
| Enzyme 91 GenAtlas ID |
ALDH1A3 |
| Enzyme 91 HGNC ID |
HGNC:409 |
| Enzyme 91 Chromosome Location |
1 |
| Enzyme 91 Locus |
15q26.3 |
| Enzyme 91 SNPs |
SNPJam Report |
| Enzyme 91 General References |
- Hsu LC, Chang WC, Hiraoka L, Hsieh CL: Molecular cloning, genomic organization, and chromosomal localization of an additional human aldehyde dehydrogenase gene, ALDH6. Genomics. 1994 Nov 15;24(2):333-41. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
|
| Enzyme 91 Metabolite References |
Not Available |
|
Enzyme 92
[top]
|
| Enzyme 92 ID |
5530 |
| Enzyme 92 Name |
Aldehyde dehydrogenase, mitochondrial |
| Enzyme 92 Synonyms |
- ALDH class 2
- ALDH-E2
- ALDHI
|
| Enzyme 92 Gene Name |
ALDH2 |
| Enzyme 92 Protein Sequence |
>Aldehyde dehydrogenase, mitochondrial
MLRAAARFGPRLGRRLLSAAATQAVPAPNQQPEVFCNQIFINNEWHDAVSRKTFPTVNPS
TGEVICQVAEGDKEDVDKAVKAARAAFQLGSPWRRMDASHRGRLLNRLADLIERDRTYLA
ALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGVCG
QIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIVPG
FGPTAGAAIASHEDVDKVAFTGSTEIGRVIQVAAGSSNLKRVTLELGGKSPNIIMSDADM
DWAVEQAHFALFFNQGQCCCAGSRTFVQEDIYDEFVERSVARAKSRVVGNPFDSKTEQGP
QVDETQFKKILGYINTGKQEGAKLLCGGGIAADRGYFIQPTVFGDVQDGMTIAKEEIFGP
VMQILKFKTIEEVVGRANNSTYGLAAAVFTKDLDKANYLSQALQAGTVWVNCYDVFGAQS
PFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
|
| Enzyme 92 Number of Residues |
517 |
| Enzyme 92 Molecular Weight |
56380.9 |
| Enzyme 92 Theoretical pI |
7.05 |
| Enzyme 92 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 92 General Function |
Involved in oxidoreductase activity |
| Enzyme 92 Specific Function |
An aldehyde + NAD(+) + H(2)O = an acid + NADH |
| Enzyme 92 Pathways |
|
| Enzyme 92 Reactions |
- an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
|
| Enzyme 92 Pfam Domain Function |
|
| Enzyme 92 Signals |
|
| Enzyme 92 Transmembrane Regions |
|
| Enzyme 92 Essentiality |
Not Available |
| Enzyme 92 GenBank ID Protein |
28606 |
| Enzyme 92 UniProtKB/Swiss-Prot ID |
P05091 |
| Enzyme 92 UniProtKB/Swiss-Prot Entry Name |
ALDH2_HUMAN |
| Enzyme 92 PDB ID |
1OF7 |
| Enzyme 92 PDB File |
Show |
| Enzyme 92 3D Structure |
|
| Enzyme 92 Cellular Location |
Not Available |
| Enzyme 92 Gene Sequence |
>1551 bp
ATGTTGCGCGCTGCCGCCGCTCGGGCCCCGCCTGGCCGCCGCCTCTTGTCAGCCGCCGCC
ACCCAGGCCGTGCCTGCCCCCAACCAGCAGCCCGAGGTCTTCTGCAACCAGATTTTCATA
AACAATGAATGGCACGATGCCGTCAGCAGGAAAACATTCCCCACCGTCAATCCGTCCACT
GGAGAGGTCATCTGTCAGGTAGCTGAAGGGGACAAGGAAGATGTGGACAAGGCACGTGAA
GGCCGCCCGGGCGCCTTCCAGCTGGGCTCACCTTGGCGCCGCATGGACGCATCACACAGC
GGCCGGCTGCTGAACCGCCTGGCCGATCTGATCGAGCGGGACCGGACCTACCTGGCGGCC
TTGGAGACCCTGGACAATGGCAAGCCCTATGTCATCTCCTACCTGGTGGATTTGGACATG
GTCCTCAAATGTCTCCGGTATTATGCCGGCTGGGCTGATAAGTACCACGGGAAAACCATC
CCCATTGACGGAGACTTCTTCAGCTACACACGCCATGAACCTGTGGGGGTGTGCGGGCAG
ATCATTCCGTGGAATTTCCCGCTCCTGATGCAAGCATGGAAGCTGGGCCCAGCCTTGGCA
ACTGGAAACGTGGTTGTGATGAAGGTAGCTGAGCAGACACCCCTCACCGCCCTCTATGTG
GCCAACCTGATCAAGGAGGCTGGCTTTCCCCCTGGTGTGGTCAACATTGTGCCTGGATTT
GGCCCCACGGCTGGGGCCGCCATTGCCTCCCATGAGGATGTGGACAAAGTGGCATTCACA
GGCTCCACTGAGATTGGCCGCGTAATCCAGGTTGCTGCTGGGAGCAGCAACCTCAAGAGA
GTGACCTTGGAGCTGGGGGGGAAGAGCCCCAACATCATCATGTCAGATGCCGATATGGAT
TGGGCCGTGGAACAGGCCCACTTCGCCCTGTTCTTCAACCAGGGCCAGTGCTGCTGTGCC
GGCTCCCGGACCTTCGTGCAGGAGGACATCTATGATGAGTTTGTGGTGCGGAGCGTTGCC
CGGGCCAAGTCTCGGGTGGTCGGGAACCCCTTTGATAGCAAGACCGAGCAGGGGCCGCAG
GTGGATGAAACTCAGTTTAAGAAGATCCTCGGCTACATCAACACGGGGAAGCAAGAGGGG
GCGAAGCTGCTGTGTGGTGGGGGCATTGCTGCTGACCGTGGTTACTTCATCCAGCCCACT
GTGTTTGGAGATGTGCAGGATGGCATGACCATCGCCAAGGAGGAGATCTTCGGGCCAGTG
ATGCAGATCCTGAAGTTCAAGACCATAGAGGAGGTTGTTGGGAGAGCCAACAATTCCACG
TACGGGCTGGCCGCAGCTGTCTTCACAAAGGATTTGGACAAGGCCAATTACCTGTCCCAG
GCCCTCCAGGCGGGCACTGTGTGGGTCAACTGCTATGATGTGTTTGGAGCCCAGTCACCC
TTTGGTGGCTACAAGATGTCGGGGAGTGGCCGGGAGTTGGGCGAGTACGGGCTGCAGGCA
TACACTGAAGTGAAAACTGTCACAGTCAAAGTGCCTCAGAAGAACTCATAA
|
| Enzyme 92 GenBank Gene ID |
X05409 |
| Enzyme 92 GeneCard ID |
ALDH2 |
| Enzyme 92 GenAtlas ID |
ALDH2 |
| Enzyme 92 HGNC ID |
HGNC:404 |
| Enzyme 92 Chromosome Location |
1 |
| Enzyme 92 Locus |
12q24.2 |
| Enzyme 92 SNPs |
SNPJam Report |
| Enzyme 92 General References |
- Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Evidence for a signal peptide at the amino-terminal end of human mitochondrial aldehyde dehydrogenase. FEBS Lett. 1987 May 11;215(2):233-6. [PubMed ]
- Braun T, Bober E, Singh S, Agarwal DP, Goedde HW: Isolation and sequence analysis of a full length cDNA clone coding for human mitochondrial aldehyde dehydrogenase. Nucleic Acids Res. 1987 Apr 10;15(7):3179. [PubMed ]
- Hsu LC, Bendel RE, Yoshida A: Genomic structure of the human mitochondrial aldehyde dehydrogenase gene. Genomics. 1988 Jan;2(1):57-65. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Hempel J, Kaiser R, Jornvall H: Mitochondrial aldehyde dehydrogenase from human liver. Primary structure, differences in relation to the cytosolic enzyme, and functional correlations. Eur J Biochem. 1985 Nov 15;153(1):13-28. [PubMed ]
- Hsu LC, Tani K, Fujiyoshi T, Kurachi K, Yoshida A: Cloning of cDNAs for human aldehyde dehydrogenases 1 and 2. Proc Natl Acad Sci U S A. 1985 Jun;82(11):3771-5. [PubMed ]
- Yoshida A, Ikawa M, Hsu LC, Tani K: Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases. Alcohol. 1985 Jan-Feb;2(1):103-6. [PubMed ]
- Aboulaich N, Vainonen JP, Stralfors P, Vener AV: Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes. Biochem J. 2004 Oct 15;383(Pt 2):237-48. [PubMed ]
- Agarwal DP, Goedde HW: Human aldehyde dehydrogenase isozymes and alcohol sensitivity. Isozymes Curr Top Biol Med Res. 1987;16:21-48. [PubMed ]
- Hempel J, Hoog JO, Jornvall H: Mitochondrial aldehyde dehydrogenase. Homology of putative targeting sequence to that of carbamyl phosphate synthetase I revealed by correlation of cDNA and protein data. FEBS Lett. 1987 Sep 28;222(1):95-8. [PubMed ]
- Ni L, Zhou J, Hurley TD, Weiner H: Human liver mitochondrial aldehyde dehydrogenase: three-dimensional structure and the restoration of solubility and activity of chimeric forms. Protein Sci. 1999 Dec;8(12):2784-90. [PubMed ]
- Yoshida A, Huang IY, Ikawa M: Molecular abnormality of an inactive aldehyde dehydrogenase variant commonly found in Orientals. Proc Natl Acad Sci U S A. 1984 Jan;81(1):258-61. [PubMed ]
- Novoradovsky A, Tsai SJ, Goldfarb L, Peterson R, Long JC, Goldman D: Mitochondrial aldehyde dehydrogenase polymorphism in Asian and American Indian populations: detection of new ALDH2 alleles. Alcohol Clin Exp Res. 1995 Oct;19(5):1105-10. [PubMed ]
|
| Enzyme 92 Metabolite References |
Not Available |
|
Enzyme 93
[top]
|
| Enzyme 93 ID |
5531 |
| Enzyme 93 Name |
Fatty aldehyde dehydrogenase |
| Enzyme 93 Synonyms |
- Aldehyde dehydrogenase 10
- Aldehyde dehydrogenase family 3 member A2
- Microsomal aldehyde dehydrogenase
|
| Enzyme 93 Gene Name |
ALDH3A2 |
| Enzyme 93 Protein Sequence |
>Fatty aldehyde dehydrogenase
MELEVRRVRQAFLSGRSRPLRFRLQQLEALRRMVQEREKDILTAIAADLCKSEFNVYSQE
VITVLGEIDFMLENLPEWVTAKPVKKNVLTMLDEAYIQPQPLGVVLIIGAWNYPFVLTIQ
PLIGAIAAGNAVIIKPSELSENTAKILAKLLPQYLDQDLYIVINGGVEETTELLKQRFDH
IFYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDKDCDLDIVCRRITWGKYMNCGQT
CIAPDYILCEASLQNQIVWKIKETVKEFYGENIKESPDYERIINLRHFKRILSLLEGQKI
AFGGETDEATRYIAPTVLTDVDPKTKVMQEEIFGPILPIVPVKNVDEAINFINEREKPLA
LYVFSHNHKLIKRMIDETSSGGVTGNDVIMHFTLNSFPFGGVGSSGMGAYHGKHSFDTFS
HQRPCLLKSLKREGANKLRYPPNSQSKVDWGKFFLLKRFNKEKLGLLLLTFLGIVAAVLV
KAEYY
|
| Enzyme 93 Number of Residues |
485 |
| Enzyme 93 Molecular Weight |
54847.4 |
| Enzyme 93 Theoretical pI |
7.99 |
| Enzyme 93 GO Classification |
| Function |
- aldehyde dehydrogenase [NAD(P)+] activity
- catalytic activity
- oxidoreductase activity
- oxidoreductase activity, acting on the aldehyde or oxo group of donors
- oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
|
| Process |
- cellular aldehyde metabolic process
- cellular metabolic process
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 93 General Function |
Involved in oxidoreductase activity |
| Enzyme 93 Specific Function |
Catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length |
| Enzyme 93 Pathways |
|
| Enzyme 93 Reactions |
- an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
|
| Enzyme 93 Pfam Domain Function |
|
| Enzyme 93 Signals |
|
| Enzyme 93 Transmembrane Regions |
|
| Enzyme 93 Essentiality |
Not Available |
| Enzyme 93 GenBank ID Protein |
Not Available |
| Enzyme 93 UniProtKB/Swiss-Prot ID |
P51648 |
| Enzyme 93 UniProtKB/Swiss-Prot Entry Name |
AL3A2_HUMAN |
| Enzyme 93 PDB ID |
Not Available |
| Enzyme 93 Cellular Location |
Not Available |
| Enzyme 93 Gene Sequence |
>1458 bp
ATGGAGCTCGAAGTCCGGCGGGTCCGACAGGCGTTCCTGTCCGGCCGGTCGCGACCTCTG
CGGTTTCGGCTGCAGCAGCTGGAGGCCCTGCGGAGGATGGTGCAGGAGCGCGAGAAGGAT
ATCCTGACGGCCATCGCCGCCGACCTGTGCAAGAGTGAATTCAATGTGTACAGTCAGGAA
GTCATTACTGTCCTTGGGGAAATTGATTTTATGCTTGAGAATCTTCCTGAATGGGTTACT
GCTAAACCAGTTAAGAAGAACGTGCTCACCATGCTGGATGAGGCCTATATTCAGCCACAG
CCTCTGGGAGTGGTGCTGATAATCGGAGCTTGGAATTACCCCTTCGTTCTCACCATTCAG
CCACTGATAGGAGCCATCGCTGCAGGAAATGCTGTGATTATAAAGCCTTCTGAACTGAGT
GAAAATACAGCCAAGATCTTGGCAAAGCTTCTCCCTCAGTATTTAGACCAGGATCTCTAT
ATTGTTATTAATGGTGGTGTTGAGGAAACCACGGAGCTCCTGAAGCAGCGATTTGACCAC
ATTTTCTATACGGGAAACACTGCGGTTGGCAAAATTGTCATGGAAGCTGCTGCCAAGCAT
CTGACCCCTGTGACTCTTGAACTGGGAGGGAAAAGTCCATGTTATATTGATAAAGATTGT
GACCTGGACATTGTTTGCAGACGCATAACCTGGGGAAAATACATGAATTGTGGCCAAACC
TGCATTGCACCCGACTATATTCTCTGTGAAGCATCCCTCCAAAATCAAATTGTATGGAAG
ATTAAGGAAACAGTGAAGGAATTTTATGGAGAAAATATAAAAGAGTCTCCTGATTATGAA
AGGATCATCAATCTTCGTCATTTTAAGAGGATACTAAGTTTGCTTGAAGGACAAAAGATA
GCTTTTGGTGGGGAGACTGATGAGGCCACACGCTACATAGCCCCAACAGTACTTACCGAT
GTTGATCCTAAAACCAAGGTGATGCAAGAAGAAATTTTTGGACCAATTCTTCCAATAGTG
CCTGTGAAAAATGTAGATGAGGCCATAAATTTCATAAATGAACGTGAAAAGCCTCTGGCT
CTTTATGTATTTTCGCATAACCATAAGCTCATCAAACGGATGATTGATGAGACATCCAGT
GGAGGTGTCACAGGCAATGACGTCATTATGCACTTCACGCTCAACTCTTTCCCATTTGGA
GGAGTGGGTTCCAGTGGGATGGGAGCTTATCACGGAAAACATAGTTTTGATACTTTTTCT
CATCAGCGTCCCTGTTTATTAAAAAGTTTAAAGAGAGAAGGTGCTAACAAACTCAGATAT
CCTCCCAACAGCCAGTCAAAGGTGGATTGGGGGAAATTTTTTCTCTTGAAACGGTTCAAC
AAAGAAAAACTCGGTCTCCTGTTGCTCACTTTCCTGGGTATTGTAGCCGCTGTGCTTGTC
AAGGCAGAATATTACTGA
|
| Enzyme 93 GenBank Gene ID |
L47162 |
| Enzyme 93 GeneCard ID |
ALDH3A2 |
| Enzyme 93 GenAtlas ID |
ALDH3A2 |
| Enzyme 93 HGNC ID |
HGNC:403 |
| Enzyme 93 Chromosome Location |
1 |
| Enzyme 93 Locus |
17p11.2 |
| Enzyme 93 SNPs |
SNPJam Report |
| Enzyme 93 General References |
- De Laurenzi V, Rogers GR, Hamrock DJ, Marekov LN, Steinert PM, Compton JG, Markova N, Rizzo WB: Sjogren-Larsson syndrome is caused by mutations in the fatty aldehyde dehydrogenase gene. Nat Genet. 1996 Jan;12(1):52-7. [PubMed ]
- Rogers GR, Markova NG, De Laurenzi V, Rizzo WB, Compton JG: Genomic organization and expression of the human fatty aldehyde dehydrogenase gene (FALDH). Genomics. 1997 Jan 15;39(2):127-35. [PubMed ]
- Chang C, Yoshida A: Human fatty aldehyde dehydrogenase gene (ALDH10): organization and tissue-dependent expression. Genomics. 1997 Feb 15;40(1):80-5. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Sillen A, Jagell S, Wadelius C: A missense mutation in the FALDH gene identified in Sjogren-Larsson syndrome patients originating from the northern part of Sweden. Hum Genet. 1997 Aug;100(2):201-3. [PubMed ]
- Sillen A, Anton-Lamprecht I, Braun-Quentin C, Kraus CS, Sayli BS, Ayuso C, Jagell S, Kuster W, Wadelius C: Spectrum of mutations and sequence variants in the FALDH gene in patients with Sjogren-Larsson syndrome. Hum Mutat. 1998;12(6):377-84. [PubMed ]
- Rizzo WB, Carney G, Lin Z: The molecular basis of Sjogren-Larsson syndrome: mutation analysis of the fatty aldehyde dehydrogenase gene. Am J Hum Genet. 1999 Dec;65(6):1547-60. [PubMed ]
- Aoki N, Suzuki H, Ito K, Ito M: A novel point mutation of the FALDH gene in a Japanese family with Sjogren-Larsson syndrome. J Invest Dermatol. 2000 May;114(5):1065-6. [PubMed ]
|
| Enzyme 93 Metabolite References |
Not Available |
|
Enzyme 94
[top]
|
| Enzyme 94 ID |
5532 |
| Enzyme 94 Name |
Aldehyde dehydrogenase X, mitochondrial |
| Enzyme 94 Synonyms |
- Aldehyde dehydrogenase 5
- Aldehyde dehydrogenase family 1 member B1
|
| Enzyme 94 Gene Name |
ALDH1B1 |
| Enzyme 94 Protein Sequence |
>Aldehyde dehydrogenase X, mitochondrial
MLRFLAPRLLSLQGRTARYSSAAALPSPILNPDIPYNQLFINNEWQDAVSKKTFPTVNPT
TGEVIGHVAEGDRADVDRAVKAAREAFRLGSPWRRMDASERGRLLNLLADLVERDRVYLA
SLETLDNGKPFQESYALDLDEVIKVYRYFAGWADKWHGKTIPMDGQHFCFTRHEPVGVCG
QIIPWNFPLVMQGWKLAPALATGNTVVMKVAEQTPLSALYLASLIKEAGFPPGVVNIITG
YGPTAGAAIAQHMDVDKVAFTGSTEVGHLIQKAAGDSNLKRVTLELGGKSPSIVLADADM
EHAVEQCHEALFFNMGQCCCAGSRTFVEESIYNEFLERTVEKAKQRKVGNPFELDTQQGP
QVDKEQFERVLGYIQLGQKEGAKLLCGGERFGERGFFIKPTVFGGVQDDMRIAKEEIFGP
VQPLFKFKKIEEVVERANNTRYGLAAAVFTRDLDKAMYFTQALQAGTVWVNTYNIVTCHT
PFGGFKESGNGRELGEDGLKAYTEVKTVTIKVPQKNS
|
| Enzyme 94 Number of Residues |
517 |
| Enzyme 94 Molecular Weight |
57238.0 |
| Enzyme 94 Theoretical pI |
6.79 |
| Enzyme 94 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 94 General Function |
Involved in oxidoreductase activity |
| Enzyme 94 Specific Function |
ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation |
| Enzyme 94 Pathways |
|
| Enzyme 94 Reactions |
- an aldehyde + NAD+ + H2O = an acid + NADH + H+ [RN:R00538]
|
| Enzyme 94 Pfam Domain Function |
|
| Enzyme 94 Signals |
|
| Enzyme 94 Transmembrane Regions |
|
| Enzyme 94 Essentiality |
Not Available |
| Enzyme 94 GenBank ID Protein |
Not Available |
| Enzyme 94 UniProtKB/Swiss-Prot ID |
P30837 |
| Enzyme 94 UniProtKB/Swiss-Prot Entry Name |
AL1B1_HUMAN |
| Enzyme 94 PDB ID |
Not Available |
| Enzyme 94 Cellular Location |
Not Available |
| Enzyme 94 Gene Sequence |
>1554 bp
ATGCTGCGCTTCCTGGCACCCCGGCTGCTTAGCCTCCAGGGCAGGACCGCCCGCTACTCC
TCGGCAGCAGCCCTCCCAAGCCCCATTCTGAACCCAGACATCCCCTACAACCAGCTGTTC
ATCAACAATGAATGGCAAGATGCAGTCAGCAAGAAGACCTTCCCGACGGTCAACCCTACC
ACCGGGGAGGTCATCGGGCACGTGGCTGAAGGTGACCGGGCTGATGTGGATCGGGCCGTG
AAAGCAGCCCGGGAAGCCTTCCGCCTGGGGTCCCCATGGCGCCGGATGGATGCCTCTGAG
CGGGGCCGGCTGCTGAACCTCCTGGCAGACCTAGTGGAGCGGGATCGAGTCTACTTGGCC
TCACTCGAGACCTTGGACAATGGGAAGCCTTTCCAAGAGTCTTACGCCTTGGACTTGGAT
GAGGTCATCAAGGTGTATCGGTACTTTGCTGGCTGGGCTGACAAGTGGCATGGCAAGACC
ATCCCCATGGATGGCCAGCATTTCTGCTTCACCCGGCATGAGCCCGTTGGTGTCTGTGGC
CAGATCATCCCGTGGAACTTCCCCTTGGTCATGCAGGGTTGGAAACTTGCCCCGGCACTC
GCCACAGGCAACACTGTGGTTATGAAGGTGGCAGAGCAGACCCCCCTCTCTGCCCTGTAT
TTGGCCTCCCTCATCAAGGAGGCAGGCTTTCCCCCTGGGGTGGTGAACATCATCACGGGG
TATGGCCCAACAGCAGGTGCGGCCATCGCCCAGCACATGGATGTTGACAAAGTTGCCTTC
ACCGGTTCCACCGAGGTGGGCCACCTGATCCAGAAAGCAGCTGGCGATTCCAACCTCAAG
AGAGTCACCCTGGAGCTGGGTGGTAAGAGCCCCAGCATCGTGCTGGCCGATGCTGACATG
GAGCATGCCGTGGAGCAGTGCCACGAAGCCCTGTTCTTCAACATGGGCCAGTGCTGCTGT
GCTGGCTCCCGGACCTTCGTGGAAGAATCCATCTACAATGAGTTTCTCGAGAGAACCGTG
GAGAAAGCAAAGCAGAGGAAAGTGGGGAACCCCTTTGAGCTGGACACCCAGCAGGGGCCT
CAGGTGGACAAGGAGCAGTTTGAACGAGTCCTAGGCTACATCCAGCTTGGCCAGAAGGAG
GGCGCAAAACTCCTCTGTGGCGGAGAGCGTTTCGGGGAGCGTGGTTTCTTCATCAAGCCT
ACTGTCTTTGGTGGCGTGCAGGATGACATGAGAATTGCCAAAGAGGAGATCTTTGGGCCT
GTGCAGCCCCTGTTCAAGTTCAAGAAGATTGAGGAGGTGGTTGAGAGGGCCAACAACACC
AGGTATGGCCTGGCTGCGGCTGTGTTCACCCGGGATCTGGACAAGGCCATGTACTTCACC
CAGGCACTCCAGGCCGGGACCGTGTGGGTAAACACCTACAACATCGTCACCTGCCACACG
CCATTTGGAGGGTTTAAGGAATCTGGAAACGGGAGGGAGCTGGGTGAGGATGGGCTTAAG
GCCTACACAGAGGTAAAGACGGTCACCATCAAGGTTCCTCAGAAGAACTCGTAG
|
| Enzyme 94 GenBank Gene ID |
BT007418 |
| Enzyme 94 GeneCard ID |
ALDH1B1 |
| Enzyme 94 GenAtlas ID |
ALDH1B1 |
| Enzyme 94 HGNC ID |
HGNC:407 |
| Enzyme 94 Chromosome Location |
9 |
| Enzyme 94 Locus |
9p11.1 |
| Enzyme 94 SNPs |
SNPJam Report |
| Enzyme 94 General References |
- Hsu LC, Chang WC: Cloning and characterization of a new functional human aldehyde dehydrogenase gene. J Biol Chem. 1991 Jul 5;266(19):12257-65. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Sherman D, Dave V, Hsu LC, Peters TJ, Yoshida A: Diverse polymorphism within a short coding region of the human aldehyde dehydrogenase-5 (ALDH5) gene. Hum Genet. 1993 Nov;92(5):477-80. [PubMed ]
|
| Enzyme 94 Metabolite References |
Not Available |
|
Enzyme 95
[top]
|
| Enzyme 95 ID |
5533 |
| Enzyme 95 Name |
Arginase-1 |
| Enzyme 95 Synonyms |
- Liver-type arginase
- Type I arginase
|
| Enzyme 95 Gene Name |
ARG1 |
| Enzyme 95 Protein Sequence |
>Arginase-1
MSAKSRTIGIIGAPFSKGQPRGGVEEGPTVLRKAGLLEKLKEQECDVKDYGDLPFADIPN
DSPFQIVKNPRSVGKASEQLAGKVAEVKKNGRISLVLGGDHSLAIGSISGHARVHPDLGV
IWVDAHTDINTPLTTTSGNLHGQPVSFLLKELKGKIPDVPGFSWVTPCISAKDIVYIGLR
DVDPGEHYILKTLGIKYFSMTEVDRLGIGKVMEETLSYLLGRKKRPIHLSFDVDGLDPSF
TPATGTPVVGGLTYREGLYITEEIYKTGLLSGLDIMEVNPSLGKTPEEVTRTVNTAVAIT
LACFGLAREGNHKPIDYLNPPK
|
| Enzyme 95 Number of Residues |
322 |
| Enzyme 95 Molecular Weight |
34734.7 |
| Enzyme 95 Theoretical pI |
7.25 |
| Enzyme 95 GO Classification |
| Function |
- arginase activity
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
- ion binding
- metal ion binding
|
| Process |
- arginine metabolic process
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 95 General Function |
Involved in arginase activity |
| Enzyme 95 Specific Function |
L-arginine + H(2)O = L-ornithine + urea |
| Enzyme 95 Pathways |
- Arginine and Proline Metabolism (map00330 )
|
| Enzyme 95 Reactions |
- L-arginine + H2O = L-ornithine + urea [RN:R00551]
|
| Enzyme 95 Pfam Domain Function |
|
| Enzyme 95 Signals |
|
| Enzyme 95 Transmembrane Regions |
|
| Enzyme 95 Essentiality |
Not Available |
| Enzyme 95 GenBank ID Protein |
178995 |
| Enzyme 95 UniProtKB/Swiss-Prot ID |
P05089 |
| Enzyme 95 UniProtKB/Swiss-Prot Entry Name |
ARGI1_HUMAN |
| Enzyme 95 PDB ID |
Not Available |
| Enzyme 95 Cellular Location |
Not Available |
| Enzyme 95 Gene Sequence |
>969 bp
ATGAGCGCCAAGTCCAGAACCATAGGGATTATTGGAGCTCCTTTCTCAAAGGGACAGCCA
CGAGGAGGGGTGGAAGAAGGCCCTACAGTATTGAGAAAGGCTGGTCTGCTTGAGAAACTT
AAAGAACAAGAGTGTGATGTGAAGGATTATGGGGACCTGCCCTTTGCTGACATCCCTAAT
GACAGTCCCTTTCAAATTGTGAAGAATCCAAGGTCTGTGGGAAAAGCAAGCGAGCAGCTG
GCTGGCAAGGTGGCACAAGTCAAGAAGAACGGAAGAATCAGCCTGGTGCTGGGCGGAGAC
CACAGTTTGGCAATTGGAAGCATCTCTGGCCATGCCAGGGTCCACCCTGATCTTGGAGTC
ATCTGGGTGGATGCTCACACTGATATCAACACTCCACTGACAACCACAAGTGGAAACTTG
CATGGACAACCTGTATCTTTCCTCCTGAAGGAACTAAAAGGAAAGATTCCCGATGTGCCA
GGATTCTCCTGGGTGACTCCCTGTATATCTGCCAAGGATATTGTGTATATTGGCTTGAGA
GACGTGGACCCTGGGGAACACTACATTTTGAAAACTCTAGGCATTAAATACTTTTCAATG
ACTGAAGTGGACAGACTAGGAATTGGCAAGGTGATGGAAGAAACACTCAGCTATCTACTA
GGAAGAAAGAAAAGGCCAATTCATCTAAGTTTTGATGTTGACGGACTGGACCCATCTTTC
ACACCAGCTACTGGCACACCAGTCGTGGGAGGTCTGACATACAGAGAAGGTCTCTACATC
ACAGAAGAAATCTACAAAACAGGGCTACTCTCAGGATTAGATATAATGGAAGTGAACCCA
TCCCTGGGGAAGACACCAGAAGAAGTAACTCGAACAGTGAACACAGCAGTTGCAATAACC
TTGGCTTGTTTCGGACTTGCTCGGGAGGGTAATCACAAGCCTATTGACTACCTTAACCCA
CCTAAGTAA
|
| Enzyme 95 GenBank Gene ID |
M14502 |
| Enzyme 95 GeneCard ID |
ARG1 |
| Enzyme 95 GenAtlas ID |
ARG1 |
| Enzyme 95 HGNC ID |
HGNC:663 |
| Enzyme 95 Chromosome Location |
6 |
| Enzyme 95 Locus |
6q23 |
| Enzyme 95 SNPs |
SNPJam Report |
| Enzyme 95 General References |
- Haraguchi Y, Takiguchi M, Amaya Y, Kawamoto S, Matsuda I, Mori M: Molecular cloning and nucleotide sequence of cDNA for human liver arginase. Proc Natl Acad Sci U S A. 1987 Jan;84(2):412-5. [PubMed ]
- Takiguchi M, Haraguchi Y, Mori M: Human liver-type arginase gene: structure of the gene and analysis of the promoter region. Nucleic Acids Res. 1988 Sep 26;16(18):8789-802. [PubMed ]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Ikemoto M, Tabata M, Miyake T, Kono T, Mori M, Totani M, Murachi T: Expression of human liver arginase in Escherichia coli. Purification and properties of the product. Biochem J. 1990 Sep 15;270(3):697-703. [PubMed ]
- Di Costanzo L, Sabio G, Mora A, Rodriguez PC, Ochoa AC, Centeno F, Christianson DW: Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response. Proc Natl Acad Sci U S A. 2005 Sep 13;102(37):13058-63. Epub 2005 Sep 2. [PubMed ]
- Di Costanzo L, Moulin M, Haertlein M, Meilleur F, Christianson DW: Expression, purification, assay, and crystal structure of perdeuterated human arginase I. Arch Biochem Biophys. 2007 Sep 1;465(1):82-9. Epub 2007 May 21. [PubMed ]
- Di Costanzo L, Pique ME, Christianson DW: Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster. J Am Chem Soc. 2007 May 23;129(20):6388-9. Epub 2007 May 1. [PubMed ]
- Zakharian TY, Di Costanzo L, Christianson DW: Synthesis of (2S)-2-amino-7,8-epoxyoctanoic acid and structure of its metal-bridging complex with human arginase I. Org Biomol Chem. 2008 Sep 21;6(18):3240-3. Epub 2008 Aug 6. [PubMed ]
- Uchino T, Haraguchi Y, Aparicio JM, Mizutani N, Higashikawa M, Naitoh H, Mori M, Matsuda I: Three novel mutations in the liver-type arginase gene in three unrelated Japanese patients with argininemia. Am J Hum Genet. 1992 Dec;51(6):1406-12. [PubMed ]
- Grody WW, Klein D, Dodson AE, Kern RM, Wissmann PB, Goodman BK, Bassand P, Marescau B, Kang SS, Leonard JV, et al.: Molecular genetic study of human arginase deficiency. Am J Hum Genet. 1992 Jun;50(6):1281-90. [PubMed ]
- Uchino T, Snyderman SE, Lambert M, Qureshi IA, Shapira SK, Sansaricq C, Smit LM, Jakobs C, Matsuda I: Molecular basis of phenotypic variation in patients with argininemia. Hum Genet. 1995 Sep;96(3):255-60. [PubMed ]
|
| Enzyme 95 Metabolite References |
Not Available |
|
Enzyme 96
[top]
|
| Enzyme 96 ID |
5545 |
| Enzyme 96 Name |
Lipoprotein lipase |
| Enzyme 96 Synonyms |
- LPL
|
| Enzyme 96 Gene Name |
LPL |
| Enzyme 96 Protein Sequence |
>Lipoprotein lipase
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGV
AESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEH
YPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRIT
GLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQ
PGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKG
LCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQ
AFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDW
WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
|
| Enzyme 96 Number of Residues |
475 |
| Enzyme 96 Molecular Weight |
53162.1 |
| Enzyme 96 Theoretical pI |
8.26 |
| Enzyme 96 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipoprotein lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 96 General Function |
Involved in catalytic activity |
| Enzyme 96 Specific Function |
The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium |
| Enzyme 96 Pathways |
|
| Enzyme 96 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 96 Pfam Domain Function |
|
| Enzyme 96 Signals |
|
| Enzyme 96 Transmembrane Regions |
|
| Enzyme 96 Essentiality |
Not Available |
| Enzyme 96 GenBank ID Protein |
189065397 |
| Enzyme 96 UniProtKB/Swiss-Prot ID |
P06858 |
| Enzyme 96 UniProtKB/Swiss-Prot Entry Name |
LIPL_HUMAN |
| Enzyme 96 PDB ID |
Not Available |
| Enzyme 96 Cellular Location |
Not Available |
| Enzyme 96 Gene Sequence |
>1428 bp
ATGGAGAGCAAAGCCCTGCTCGTGCTGACTCTGGCCGTGTGGCTCCAGAGTCTGACCGCC
TCCCGCGGAGGGGTGGCCGCCGCCGACCAAAGAAGAGATTTTATCGACATCGAAAGTAAA
TTTGCCCTAAGGACCCCTGAAGACACAGCTGAGGACACTTGCCACCTCATTCCCGGAGTA
GCAGAGTCCGTGGCTACCTGTCATTTCAATCACAGCAGCAAAACCTTCATGGTGATCCAT
GGCTGGACGGTAACAGGAATGTATGAGAGTTGGGTGCCAAAACTTGTGGCCGCCCTGTAC
AAGAGAGAACCAGACTCCAATGTCATTGTGGTGGACTGGCTGTCACGGGCTCAGGAGCAT
TACCCAGTGTCCGCGGGCTACACCAAACTGGTGGGACAGGATGTGGCCCGGTTTATCAAC
TGGATGGAGGAGGAGTTTAACTACCCTCTGGACAATGTCCATCTCTTGGGATACAGCCTT
GGAGCCCATGCTGCTGGCATTGCAGGAAGTCTGACCAATAAGAAAGTCAACAGAATTACT
GGCCTCGATCCAGCTGGACCTAACTTTGAGTATGCAGAAGCCCCGAGTCGTCTTTCTCCT
GATGATGCAGATTTTGTAGACGTCTTACACACATTCACCAGAGGGTCCCCTGGTCGAAGC
ATTGGAATCCAGAAACCAGTTGGGCATGTTGACATTTACCCGAATGGAGGTACTTTTCAG
CCAGGATGTAACATTGGAGAAGCTATCCGCGTGATTGCAGAGAGAGGACTTGGAGATGTG
GACCAGCTAGTGAAGTGCTCCCACGAGCGCTCCATTCATCTCTTCATCGACTCTCTGTTG
AATGAAGAAAATCCAAGTAAGGCCTACAGGTGCAGTTCCAAGGAAGCCTTTGAGAAAGGG
CTCTGCTTGAGTTGTAGAAAGAACCGCTGCAACAATCTGGGCTATGAGATCAATAAAGTC
AGAGCCAAAAGAAGCAGCAAAATGTACCTGAAGACTCGTTCTCAGATGCCCTACAAAGTC
TTCCATTACCAAGTAAAGATTCATTTTTCTGGGACTGAGAGTGAAACCCATACCAATCAG
GCCTTTGAGATTTCTCTGTATGGCACCGTGGCCGAGAGTGAGAACATCCCATTCACTCTG
CCTGAAGTTTCCACAAATAAGACCTACTCCTTCCTAATTTACACAGAGGTAGATATTGGA
GAACTACTCATGTTGAAGCTCAAATGGAAGAGTGATTCATACTTTAGCTGGTCAGACTGG
TGGAGCAGTCCCGGCTTCGCCATTCAGAAGATCAGAGTAAAAGCAGGAGAGACTCAGAAA
AAGGTGATCTTCTGTTCTAGGGAGAAAGTGTCTCATTTGCAGAAAGGAAAGGCACCTGCG
GTATTTGTGAAATGCCATGACAAGTCTCTGAATAAGAAGTCAGGCTGA
|
| Enzyme 96 GenBank Gene ID |
AK312311 |
| Enzyme 96 GeneCard ID |
LPL |
| Enzyme 96 GenAtlas ID |
LPL |
| Enzyme 96 HGNC ID |
HGNC:6677 |
| Enzyme 96 Chromosome Location |
8 |
| Enzyme 96 Locus |
8p22 |
| Enzyme 96 SNPs |
SNPJam Report |
| Enzyme 96 General References |
- Wion KL, Kirchgessner TG, Lusis AJ, Schotz MC, Lawn RM: Human lipoprotein lipase complementary DNA sequence. Science. 1987 Mar 27;235(4796):1638-41. [PubMed ]
- Gotoda T, Senda M, Gamou T, Furuichi Y, Oka K: Nucleotide sequence of human cDNA coding for a lipoprotein lipase (LPL) cloned from placental cDNA library. Nucleic Acids Res. 1989 Mar 25;17(6):2351. [PubMed ]
- Takagi A, Ikeda Y, Yamamoto A: DNA sequence of lipoprotein lipase cDNA cloned from human monocytic leukemia THP-1 cells. Nucleic Acids Res. 1990 Nov 11;18(21):6436. [PubMed ]
- Chuat JC, Raisonnier A, Etienne J, Galibert F: The lipoprotein lipase-encoding human gene: sequence from intron-6 to intron-9 and presence in intron-7 of a 40-million-year-old Alu sequence. Gene. 1992 Jan 15;110(2):257-61. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Enerback S, Ohlsson BG, Samuelsson L, Bjursell G: Characterization of the human lipoprotein lipase (LPL) promoter: evidence of two cis-regulatory regions, LP-alpha and LP-beta, of importance for the differentiation-linked induction of the LPL gene during adipogenesis. Mol Cell Biol. 1992 Oct;12(10):4622-33. [PubMed ]
- Zechner R: Rapid and simple isolation procedure for lipoprotein lipase from human milk. Biochim Biophys Acta. 1990 May 1;1044(1):20-5. [PubMed ]
- Lutz EP, Merkel M, Kako Y, Melford K, Radner H, Breslow JL, Bensadoun A, Goldberg IJ: Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues. J Clin Invest. 2001 May;107(9):1183-92. [PubMed ]
- Gin P, Beigneux AP, Davies B, Young MF, Ryan RO, Bensadoun A, Fong LG, Young SG: Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution. Biochim Biophys Acta. 2007 Dec;1771(12):1464-8. Epub 2007 Oct 22. [PubMed ]
- Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed ]
- van Tilbeurgh H, Roussel A, Lalouel JM, Cambillau C: Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis. J Biol Chem. 1994 Feb 11;269(6):4626-33. [PubMed ]
- Hata A, Emi M, Luc G, Basdevant A, Gambert P, Iverius PH, Lalouel JM: Compound heterozygote for lipoprotein lipase deficiency: Ser----Thr244 and transition in 3' splice site of intron 2 (AG----AA) in the lipoprotein lipase gene. Am J Hum Genet. 1990 Oct;47(4):721-6. [PubMed ]
- Emi M, Wilson DE, Iverius PH, Wu L, Hata A, Hegele R, Williams RR, Lalouel JM: Missense mutation (Gly----Glu188) of human lipoprotein lipase imparting functional deficiency. J Biol Chem. 1990 Apr 5;265(10):5910-6. [PubMed ]
- Monsalve MV, Henderson H, Roederer G, Julien P, Deeb S, Kastelein JJ, Peritz L, Devlin R, Bruin T, Murthy MR, et al.: A missense mutation at codon 188 of the human lipoprotein lipase gene is a frequent cause of lipoprotein lipase deficiency in persons of different ancestries. J Clin Invest. 1990 Sep;86(3):728-34. [PubMed ]
- Beg OU, Meng MS, Skarlatos SI, Previato L, Brunzell JD, Brewer HB Jr, Fojo SS: Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity. Proc Natl Acad Sci U S A. 1990 May;87(9):3474-8. [PubMed ]
- Dichek HL, Fojo SS, Beg OU, Skarlatos SI, Brunzell JD, Cutler GB Jr, Brewer HB Jr: Identification of two separate allelic mutations in the lipoprotein lipase gene of a patient with the familial hyperchylomicronemia syndrome. J Biol Chem. 1991 Jan 5;266(1):473-7. [PubMed ]
- Faustinella F, Chang A, Van Biervliet JP, Rosseneu M, Vinaimont N, Smith LC, Chen SH, Chan L: Catalytic triad residue mutation (Asp156----Gly) causing familial lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation (Ser447----Ter) in a Turkish family. J Biol Chem. 1991 Aug 5;266(22):14418-24. [PubMed ]
- Ameis D, Kobayashi J, Davis RC, Ben-Zeev O, Malloy MJ, Kane JP, Lee G, Wong H, Havel RJ, Schotz MC: Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene. J Clin Invest. 1991 Apr;87(4):1165-70. [PubMed ]
- Henderson HE, Ma Y, Hassan MF, Monsalve MV, Marais AD, Winkler F, Gubernator K, Peterson J, Brunzell JD, Hayden MR: Amino acid substitution (Ile194----Thr) in exon 5 of the lipoprotein lipase gene causes lipoprotein lipase deficiency in three unrelated probands. Support for a multicentric origin. J Clin Invest. 1991 Jun;87(6):2005-11. [PubMed ]
- Gotoda T, Yamada N, Kawamura M, Kozaki K, Mori N, Ishibashi S, Shimano H, Takaku F, Yazaki Y, Furuichi Y, et al.: Heterogeneous mutations in the human lipoprotein lipase gene in patients with familial lipoprotein lipase deficiency. J Clin Invest. 1991 Dec;88(6):1856-64. [PubMed ]
- Ma Y, Henderson HE, Murthy V, Roederer G, Monsalve MV, Clarke LA, Normand T, Julien P, Gagne C, Lambert M, et al.: A mutation in the human lipoprotein lipase gene as the most common cause of familial chylomicronemia in French Canadians. N Engl J Med. 1991 Jun 20;324(25):1761-6. [PubMed ]
- Ishimura-Oka K, Faustinella F, Kihara S, Smith LC, Oka K, Chan L: A missense mutation (Trp86----Arg) in exon 3 of the lipoprotein lipase gene: a cause of familial chylomicronemia. Am J Hum Genet. 1992 Jun;50(6):1275-80. [PubMed ]
- Bruin T, Kastelein JJ, Van Diermen DE, Ma Y, Henderson HE, Stuyt PM, Stalenhoef AF, Sturk A, Brunzell JD, Hayden MR: A missense mutation Pro157 Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity. Eur J Biochem. 1992 Sep 1;208(2):267-72. [PubMed ]
- Ma Y, Wilson BI, Bijvoet S, Henderson HE, Cramb E, Roederer G, Ven Murthy MR, Julien P, Bakker HD, Kastelein JJ, et al.: A missense mutation (Asp250----Asn) in exon 6 of the human lipoprotein lipase gene causes chylomicronemia in patients of different ancestries. Genomics. 1992 Jul;13(3):649-53. [PubMed ]
- Ma YH, Bruin T, Tuzgol S, Wilson BI, Roederer G, Liu MS, Davignon J, Kastelein JJ, Brunzell JD, Hayden MR: Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis. J Biol Chem. 1992 Jan 25;267(3):1918-23. [PubMed ]
- Emmerich J, Beg OU, Peterson J, Previato L, Brunzell JD, Brewer HB Jr, Santamarina-Fojo S: Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241. J Biol Chem. 1992 Feb 25;267(6):4161-5. [PubMed ]
- Hata A, Ridinger DN, Sutherland SD, Emi M, Kwong LK, Shuhua J, Lubbers A, Guy-Grand B, Basdevant A, Iverius PH, et al.: Missense mutations in exon 5 of the human lipoprotein lipase gene. Inactivation correlates with loss of dimerization. J Biol Chem. 1992 Oct 5;267(28):20132-9. [PubMed ]
- Ishimura-Oka K, Semenkovich CF, Faustinella F, Goldberg IJ, Shachter N, Smith LC, Coleman T, Hide WA, Brown WV, Oka K, et al.: A missense (Asp250----Asn) mutation in the lipoprotein lipase gene in two unrelated families with familial lipoprotein lipase deficiency. J Lipid Res. 1992 May;33(5):745-54. [PubMed ]
- Reina M, Brunzell JD, Deeb SS: Molecular basis of familial chylomicronemia: mutations in the lipoprotein lipase and apolipoprotein C-II genes. J Lipid Res. 1992 Dec;33(12):1823-32. [PubMed ]
- Kobayashi J, Sasaki N, Tashiro J, Inadera H, Saito Y, Yoshida S: A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase gene in a case with type I hyperlipidemia. Biochem Biophys Res Commun. 1993 Mar 31;191(3):1046-54. [PubMed ]
- Haubenwallner S, Horl G, Shachter NS, Presta E, Fried SK, Hofler G, Kostner GM, Breslow JL, Zechner R: A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia). Genomics. 1993 Nov;18(2):392-6. [PubMed ]
- Ma Y, Liu MS, Ginzinger D, Frohlich J, Brunzell JD, Hayden MR: Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172-->Cys mutation in the lipoprotein lipase gene. J Clin Invest. 1993 May;91(5):1953-8. [PubMed ]
- Wilson DE, Hata A, Kwong LK, Lingam A, Shuhua J, Ridinger DN, Yeager C, Kaltenborn KC, Iverius PH, Lalouel JM: Mutations in exon 3 of the lipoprotein lipase gene segregating in a family with hypertriglyceridemia, pancreatitis, and non-insulin-dependent diabetes. J Clin Invest. 1993 Jul;92(1):203-11. [PubMed ]
- Bruin T, Tuzgol S, van Diermen DE, Hoogerbrugge-van der Linden N, Brunzell JD, Hayden MR, Kastelein JJ: Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase. J Lipid Res. 1993 Dec;34(12):2109-19. [PubMed ]
- Pepe G, Chimienti G, Resta F, Di Perna V, Tarricone C, Lovecchio M, Colacicco AM, Capurso A: A new Italian case of lipoprotein lipase deficiency: a Leu365- > Val change resulting in loss of enzyme activity. Biochem Biophys Res Commun. 1994 Mar 15;199(2):570-6. [PubMed ]
- Kobayashi J, Inadera H, Fujita Y, Talley G, Morisaki N, Yoshida S, Saito Y, Fojo SS, Brewer HB Jr: A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion. Biochem Biophys Res Commun. 1994 Nov 30;205(1):506-15. [PubMed ]
- Ma Y, Liu MS, Chitayat D, Bruin T, Beisiegel U, Benlian P, Foubert L, De Gennes JL, Funke H, Forsythe I, et al.: Recurrent missense mutations at the first and second base of codon Arg243 in human lipoprotein lipase in patients of different ancestries. Hum Mutat. 1994;3(1):52-8. [PubMed ]
- Bruin T, Tuzgol S, Mulder WJ, van den Ende AE, Jansen H, Hayden MR, Kastelein JJ: A compound heterozygote for lipoprotein lipase deficiency, Val69-->Leu and Gly188-->Glu: correlation between in vitro LPL activity and clinical expression. J Lipid Res. 1994 Mar;35(3):438-45. [PubMed ]
- Ma Y, Ooi TC, Liu MS, Zhang H, McPherson R, Edwards AL, Forsythe IJ, Frohlich J, Brunzell JD, Hayden MR: High frequency of mutations in the human lipoprotein lipase gene in pregnancy-induced chylomicronemia: possible association with apolipoprotein E2 isoform. J Lipid Res. 1994 Jun;35(6):1066-75. [PubMed ]
- Previato L, Guardamagna O, Dugi KA, Ronan R, Talley GD, Santamarina-Fojo S, Brewer HB Jr: A novel missense mutation in the C-terminal domain of lipoprotein lipase (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia. J Lipid Res. 1994 Sep;35(9):1552-60. [PubMed ]
- Reymer PW, Gagne E, Groenemeyer BE, Zhang H, Forsyth I, Jansen H, Seidell JC, Kromhout D, Lie KE, Kastelein J, et al.: A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL cholesterol levels in premature atherosclerosis. Nat Genet. 1995 May;10(1):28-34. [PubMed ]
- Henderson HE, Hassan F, Marais D, Hayden MR: A new mutation destroying disulphide bridging in the C-terminal domain of lipoprotein lipase. Biochem Biophys Res Commun. 1996 Oct 3;227(1):189-94. [PubMed ]
- de Bruin TW, Mailly F, van Barlingen HH, Fisher R, Castro Cabezas M, Talmud P, Dallinga-Thie GM, Humphries SE: Lipoprotein lipase gene mutations D9N and N291S in four pedigrees with familial combined hyperlipidaemia. Eur J Clin Invest. 1996 Aug;26(8):631-9. [PubMed ]
- Wiebusch H, Funke H, Bruin T, Bucher H, von Eckardstein A, Kastelein JJ, Assmann G: Compound heterozygosity for a known (D250N) and a novel (E410K) missense mutation in the C-terminal domain of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):381-3. [PubMed ]
- Wiebusch H, Funke H, Santer R, Richter W, Assmann G: A novel missense (E163G) mutation in the catalytic subunit of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):392. [PubMed ]
- Rouis M, Lohse P, Dugi KA, Lohse P, Beg OU, Ronan R, Talley GD, Brunzell JD, Santamarina-Fojo S: Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His). J Lipid Res. 1996 Mar;37(3):651-61. [PubMed ]
- Benlian P, De Gennes JL, Foubert L, Zhang H, Gagne SE, Hayden M: Premature atherosclerosis in patients with familial chylomicronemia caused by mutations in the lipoprotein lipase gene. N Engl J Med. 1996 Sep 19;335(12):848-54. [PubMed ]
- Foubert L, Bruin T, De Gennes JL, Ehrenborg E, Furioli J, Kastelein J, Benlian P, Hayden M: A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in Moroccans of Berber ancestry. Hum Mutat. 1997;10(3):179-85. [PubMed ]
- Mailly F, Palmen J, Muller DP, Gibbs T, Lloyd J, Brunzell J, Durrington P, Mitropoulos K, Betteridge J, Watts G, Lithell H, Angelico F, Humphries SE, Talmud PJ: Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene mutations identified in 20 patients from the UK, Sweden, and Italy. Hum Mutat. 1997;10(6):465-73. [PubMed ]
- Foubert L, De Gennes JL, Lagarde JP, Ehrenborg E, Raisonnier A, Girardet JP, Hayden MR, Benlian P: Assessment of French patients with LPL deficiency for French Canadian mutations. J Med Genet. 1997 Aug;34(8):672-5. [PubMed ]
- Henderson HE, Bijvoet SM, Mannens MA, Bruin T, Erkelens DW, Hayden MR, Kastelein JJ: Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de novo event. Am J Med Genet. 1998 Jul 24;78(4):313-6. [PubMed ]
- Henderson H, Leisegang F, Hassan F, Hayden M, Marais D: A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis. Clin Chim Acta. 1998 Jan 12;269(1):1-12. [PubMed ]
- Evans D, Wendt D, Ahle S, Guerra A, Beisiegel U: Compound heterozygosity for a new (S259G) and a previously described (G188E) mutation in lipoprotein lipase (LpL) as a cause of chylomicronemia. Mutations in brief no. 183. Online. Hum Mutat. 1998;12(3):217. [PubMed ]
- Zhang Q, Liu Y, Liu BW, Fan P, Cavanna J, Galton DJ: Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects. Mol Genet Metab. 1998 Jul;64(3):177-83. [PubMed ]
- Nickerson DA, Taylor SL, Weiss KM, Clark AG, Hutchinson RG, Stengard J, Salomaa V, Vartiainen E, Boerwinkle E, Sing CF: DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase gene. Nat Genet. 1998 Jul;19(3):233-40. [PubMed ]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]
- Takagi A, Ikeda Y, Takeda E, Yamamoto A: A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a Japanese patient with familial LPL deficiency. Biochim Biophys Acta. 2000 Nov 15;1502(3):433-46. [PubMed ]
- Ikeda Y, Goji K, Takagi A: A compound heterozygote for a novel missense mutation (G105R) in exon 3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in a Japanese infant with hyperchylomicronaemia. Clin Sci (Lond). 2000 Dec;99(6):569-78. [PubMed ]
- Hoffmann MM, Jacob S, Luft D, Schmulling RM, Rett K, Marz W, Haring HU, Matthaei S: Type I hyperlipoproteinemia due to a novel loss of function mutation of lipoprotein lipase, Cys(239)-->Trp, associated with recurrent severe pancreatitis. J Clin Endocrinol Metab. 2000 Dec;85(12):4795-8. [PubMed ]
- Holzl B, Kraft HG, Wiebusch H, Sandhofer A, Patsch J, Sandhofer F, Paulweber B: Two novel mutations in the lipoprotein lipase gene in a family with marked hypertriglyceridemia in heterozygous carriers. Potential interaction with the polymorphic marker D1S104 on chromosome 1q21-q23. J Lipid Res. 2000 May;41(5):734-41. [PubMed ]
- Ikeda Y, Takagi A, Nakata Y, Sera Y, Hyoudou S, Hamamoto K, Nishi Y, Yamamoto A: Novel compound heterozygous mutations for lipoprotein lipase deficiency. A G-to-T transversion at the first position of exon 5 causing G154V missense mutation and a 5' splice site mutation of intron 8. J Lipid Res. 2001 Jul;42(7):1072-81. [PubMed ]
- Chan LY, Lam CW, Mak YT, Tomlinson B, Tsang MW, Baum L, Masarei JR, Pang CP: Genotype-phenotype studies of six novel LPL mutations in Chinese patients with hypertriglyceridemia. Hum Mutat. 2002 Sep;20(3):232-3. [PubMed ]
- Saika Y, Sakai N, Takahashi M, Maruyama T, Kihara S, Ouchi N, Ishigami M, Hiraoka H, Nakamura T, Yamashita S, Matsuzawa Y: Novel LPL mutation (L303F) found in a patient associated with coronary artery disease and severe systemic atherosclerosis. Eur J Clin Invest. 2003 Mar;33(3):216-22. [PubMed ]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed ]
- Abifadel M, Jambart S, Allard D, Rabes JP, Varret M, Derre A, Chouery E, Salem N, Junien C, Aydenian H, Boileau C: Identification of the first Lebanese mutation in the LPL gene and description of a rapid detection method. Clin Genet. 2004 Feb;65(2):158-61. [PubMed ]
- Kavazarakis E, Stabouli S, Gourgiotis D, Roumeliotou K, Traeger-Synodinos J, Bossios A, Fretzayas A, Kanavakis E: Severe hypertriglyceridaemia in a Greek infant: a clinical, biochemical and genetic study. Eur J Pediatr. 2004 Aug;163(8):462-6. Epub 2004 Jun 5. [PubMed ]
- Maruyama T, Yamashita S, Matsuzawa Y, Bujo H, Takahashi K, Saito Y, Ishibashi S, Ohashi K, Shionoiri F, Gotoda T, Yamada N, Kita T: Mutations in Japanese subjects with primary hyperlipidemia--results from the Research Committee of the Ministry of Health and Welfare of Japan since 1996--. J Atheroscler Thromb. 2004;11(3):131-45. [PubMed ]
- Santer R, Gokcay G, Demirkol M, Gal A, Lukacs Z: Hyperchylomicronaemia due to lipoprotein lipase deficiency as a cause of false-positive newborn screening for biotinidase deficiency. J Inherit Metab Dis. 2005;28(2):137-40. [PubMed ]
|
| Enzyme 96 Metabolite References |
Not Available |
|
Enzyme 97
[top]
|
| Enzyme 97 ID |
5548 |
| Enzyme 97 Name |
Acyl-CoA desaturase |
| Enzyme 97 Synonyms |
- Delta(9)-desaturase
- Fatty acid desaturase
- Stearoyl-CoA desaturase
|
| Enzyme 97 Gene Name |
SCD |
| Enzyme 97 Protein Sequence |
>Acyl-CoA desaturase
MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYK
DKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAH
RLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFS
HVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGE
TFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNY
HHSFPYDYSASEYRWHINFTTFFIDCMAALGLAYDRKKVSKAAILARIKRTGDGNYKSG
|
| Enzyme 97 Number of Residues |
359 |
| Enzyme 97 Molecular Weight |
41522.3 |
| Enzyme 97 Theoretical pI |
9.28 |
| Enzyme 97 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- ion binding
- iron ion binding
- metal ion binding
- oxidoreductase activity
- oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen
- oxidoreductase activity, acting on paired donors, with oxidation of a pair of donors resulting in the reduction of molecular oxygen to two molecules of water
- stearoyl-CoA 9-desaturase activity
- transition metal ion binding
|
| Process |
- carboxylic acid metabolic process
- cellular metabolic process
- fatty acid biosynthetic process
- fatty acid metabolic process
- lipid metabolic process
- metabolic process
- monocarboxylic acid metabolic process
- organic acid metabolic process
- oxidation reduction
- oxoacid metabolic process
- primary metabolic process
|
| Component |
- cell part
- endoplasmic reticulum
- intracellular membrane-bounded organelle
- membrane
- membrane-bounded organelle
- organelle
|
|
| Enzyme 97 General Function |
Involved in oxidoreductase activity |
| Enzyme 97 Specific Function |
Terminal component of the liver microsomal stearyl-CoA desaturase system, that utilizes O(2) and electrons from reduced cytochrome b5 to catalyze the insertion of a double bond into a spectrum of fatty acyl-CoA substrates including palmitoyl-CoA and stearoyl-CoA |
| Enzyme 97 Pathways |
Not Available |
| Enzyme 97 Reactions |
- stearoyl-CoA + 2 ferrocytochrome b5 + O2 + 2 H+ = oleoyl-CoA + 2 ferricytochrome b5 + 2 H2O [RN:R02222]
|
| Enzyme 97 Pfam Domain Function |
|
| Enzyme 97 Signals |
|
| Enzyme 97 Transmembrane Regions |
- 76-96
98-118
223-243
315-335
|
| Enzyme 97 Essentiality |
Not Available |
| Enzyme 97 GenBank ID Protein |
7415721 |
| Enzyme 97 UniProtKB/Swiss-Prot ID |
O00767 |
| Enzyme 97 UniProtKB/Swiss-Prot Entry Name |
ACOD_HUMAN |
| Enzyme 97 PDB ID |
Not Available |
| Enzyme 97 Cellular Location |
Not Available |
| Enzyme 97 Gene Sequence |
>1080 bp
ATGCCGGCCCACTTGCTGCAGGACGATATCTCTAGCTCCTATACCACCACCACCACCATT
ACAGCGCCTCCCTCCAGGGTCCTGCAGAATGGAGGAGATAAGTTGGAGACGATGCCCCTC
TACTTGGAAGACGACATTCGCCCTGATATAAAAGATGATATATATGACCCCACCTACAAG
GATAAGGAAGGCCCAAGCCCCAAGGTTGAATATGTCTGGAGAAACATCATCCTTATGTCT
CTGCTACACTTGGGAGCCCTGTATGGGATCACTTTGATTCCTACCTGCAAGTTCTACACC
TGGCTTTGGGGGGTATTCTACTATTTTGTCAGTGCCCTGGGCATAACAGCAGGAGCTCAT
CGTCTGTGGAGCCACCGCTCTTACAAAGCTCGGCTGCCCCTACGGCTCTTTCTGATCATT
GCCAACACAATGGCATTCCAGAATGATGTCTATGAATGGGCTCGTGACCACCGTGCCCAC
CACAAGTTTTCAGAAACACATGCTGATCCTCATAATTCCCGACGTGGCTTTTTCTTCTCT
CACGTGGGTTGGCTGCTTGTGCGCAAACACCCAGCTGTCAAAGAGAAGGGGAGTACGCTA
GACTTGTCTGACCTAGAAGCTGAGAAACTGGTGATGTTCCAGAGGAGGTACTACAAACCT
GGCTTGCTGCTGATGTGCTTCATCCTGCCCACGCTTGTGCCCTGGTATTTCTGGGGTGAA
ACTTTTCAAAACAGTGTGTTCGTTGCCACTTTCTTGCGATATGCTGTGGTGCTTAATGCC
ACCTGGCTGGTGAACAGTGCTGCCCACCTCTTCGGATATCGTCCTTATGACAAGAACATT
AGCCCCCGGGAGAATATCCTGGTTTCACTTGGAGCTGTGGGTGAGGGCTTCCACAACTAC
CACCACTCCTTTCCCTATGACTACTCTGCCAGTGAGTACCGCTGGCACATCAACTTCACC
ACATTCTTCATTGATTGCATGGCCGCCCTCGGTCTGGCCTATGACCGGAAGAAAGTCTCC
AAGGCCGCCATCTTGGCCAGGATTAAAAGAACCGGAGATGGAAACTACAAGAGTGGCTGA
|
| Enzyme 97 GenBank Gene ID |
AB032261 |
| Enzyme 97 GeneCard ID |
SCD |
| Enzyme 97 GenAtlas ID |
SCD |
| Enzyme 97 HGNC ID |
HGNC:10571 |
| Enzyme 97 Chromosome Location |
1 |
| Enzyme 97 Locus |
10q24.31 |
| Enzyme 97 SNPs |
SNPJam Report |
| Enzyme 97 General References |
- Zhang L, Ge L, Parimoo S, Stenn K, Prouty SM: Human stearoyl-CoA desaturase: alternative transcripts generated from a single gene by usage of tandem polyadenylation sites. Biochem J. 1999 May 15;340 ( Pt 1):255-64. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Zhang L, Ge L, Tran T, Stenn K, Prouty SM: Isolation and characterization of the human stearoyl-CoA desaturase gene promoter: requirement of a conserved CCAAT cis-element. Biochem J. 2001 Jul 1;357(Pt 1):183-93. [PubMed ]
- Xu G, Shin SB, Jaffrey SR: Global profiling of protease cleavage sites by chemoselective labeling of protein N-termini. Proc Natl Acad Sci U S A. 2009 Nov 17;106(46):19310-5. Epub 2009 Nov 5. [PubMed ]
- Li J, Ding SF, Habib NA, Fermor BF, Wood CB, Gilmour RS: Partial characterization of a cDNA for human stearoyl-CoA desaturase and changes in its mRNA expression in some normal and malignant tissues. Int J Cancer. 1994 May 1;57(3):348-52. [PubMed ]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed ]
|
| Enzyme 97 Metabolite References |
Not Available |
|
Enzyme 98
[top]
|
| Enzyme 98 ID |
5549 |
| Enzyme 98 Name |
Monoglyceride lipase |
| Enzyme 98 Synonyms |
- MGL
- HU-K5
- Lysophospholipase homolog
- Lysophospholipase-like
|
| Enzyme 98 Gene Name |
MGLL |
| Enzyme 98 Protein Sequence |
>Monoglyceride lipase
MPEESSPRRTPQSIPYQDLPHLVNADGQYLFCRYWKPTGTPKALIFVSHGAGEHSGRYEE
LARMLMGLDLLVFAHDHVGHGQSEGERMVVSDFHVFVRDVLQHVDSMQKDYPGLPVFLLG
HSMGGAIAILTAAERPGHFAGMVLISPLVLANPESATTFKVLAAKVLNLVLPNLSLGPID
SSVLSRNKTEVDIYNSDPLICRAGLKVCFGIQLLNAVSRVERALPKLTVPFLLLQGSADR
LCDSKGAYLLMELAKSQDKTLKIYEGAYHVLHKELPEVTNSVFHEINMWVSQRTATAGTA
SPP
|
| Enzyme 98 Number of Residues |
303 |
| Enzyme 98 Molecular Weight |
33261.1 |
| Enzyme 98 Theoretical pI |
7.00 |
| Enzyme 98 GO Classification |
Not Available |
| Enzyme 98 General Function |
Lipid transport and metabolism |
| Enzyme 98 Specific Function |
Converts monoacylglycerides to free fatty acids and glycerol. Hydrolyzes 2-arachidonoylglycerol, a putative endocannabinoid |
| Enzyme 98 Pathways |
|
| Enzyme 98 Reactions |
- Hydrolyses glycerol monoesters of long-chain fatty acids ALL_REAC (other) R01351 R01352 REFERENCE 1 [PMID:6776896] AUTHORS Mentlein R, Heiland S, Heymann E. TITLE Simultaneous purification and comparative characterization of six serine hydrolases from rat liver microsomes. JOURNAL Arch. Biochem. Biophys. 200 (1980) 547-59. ORGANISM Rattus norvegicus [GN:rno] REFERENCE 2 [PMID:5916497] AUTHORS Pope JL, McPherson JC, Tidwell HC. TITLE A study of a monoglyceride-hydrolyzing enzyme of intestinal mucosa. JOURNAL J. Biol. Chem. 241 (1966) 2306-10. ORGANISM Rattus norvegicus [GN:rno]
|
| Enzyme 98 Pfam Domain Function |
|
| Enzyme 98 Signals |
|
| Enzyme 98 Transmembrane Regions |
|
| Enzyme 98 Essentiality |
Not Available |
| Enzyme 98 GenBank ID Protein |
14594904 |
| Enzyme 98 UniProtKB/Swiss-Prot ID |
Q99685 |
| Enzyme 98 UniProtKB/Swiss-Prot Entry Name |
MGLL_HUMAN |
| Enzyme 98 PDB ID |
Not Available |
| Enzyme 98 Cellular Location |
Not Available |
| Enzyme 98 Gene Sequence |
>912 bp
ATGCCAGAGGAAAGTTCCCCCAGGCGGACCCCGCAGAGCATTCCCTACCAGGACCTCCCT
CACCTGGTCAATGCAGACGGACAGTACCTCTTCTGCAGGTACTGGAAACCCACAGGCACA
CCCAAGGCCCTCATCTTTGTGTCCCATGGAGCCGGAGAGCACAGTGGCCGCTATGAAGAG
CTGGCTCGGATGCTGATGGGGCTGGACCTGCTGGTGTTCGCCCACGACCATGTTGGCCAC
GGACAGAGCGAAGGGGAGAGGATGGTAGTGTCTGACTTCCACGTTTTCGTCAGGGATGTG
TTGCAGCATGTGGATTCCATGCAGAAAGACTACCCTGGGCTTCCTGTCTTCCTTCTGGGC
CACTCCATGGGAGGCGCCATCGCCATCCTCACGGCCGCAGAGAGGCCGGGCCACTTCGCC
GGCATGGTACTCATTTCGCCTCTGGTTCTTGCCAATCCTGAATCTGCAACAACTTTCAAG
GTCCTTGCTGCGAAAGTGCTCAACCTTGTGCTGCCAAACTTGTCCCTCGGGCCCATCGAC
TCCAGCGTGCTCTCTCGGAATAAGACAGAGGTCGACATTTATAACTCAGACCCCCTGATC
TGCCGGGCAGGGCTGAAGGTGTGCTTCGGCATCCAACTGCTGAATGCCGTCTCACGGGTG
GAGCGCGCCCTCCCCAAGCTGACTGTGCCCTTCCTGCTGCTCCAGGGCTCTGCCGATCGC
CTATGTGACAGCAAAGGGGCCTACCTGCTCATGGAGTTAGCCAAGAGCCAGGACAAGACT
CTCAAGATTTATGAAGGTGCCTACCATGTTCTCCACAAGGAGCTTCCTGAAGTCACCAAC
TCCGTCTTCCATGAAATAAACATGTGGGTCTCTCAAAGGACAGCCACGGCAGGAACTGCG
TCCCCACCCTGA
|
| Enzyme 98 GenBank Gene ID |
AJ270950 |
| Enzyme 98 GeneCard ID |
MGLL |
| Enzyme 98 GenAtlas ID |
MGLL |
| Enzyme 98 HGNC ID |
HGNC:17038 |
| Enzyme 98 Chromosome Location |
3 |
| Enzyme 98 Locus |
3q21.3 |
| Enzyme 98 SNPs |
SNPJam Report |
| Enzyme 98 General References |
- Wall EM, Cao J, Chen N, Buller RM, Upton C: A novel poxvirus gene and its human homolog are similar to an E. coli lysophospholipase. Virus Res. 1997 Dec;52(2):157-67. [PubMed ]
- Karlsson M, Reue K, Xia YR, Lusis AJ, Langin D, Tornqvist H, Holm C: Exon-intron organization and chromosomal localization of the mouse monoglyceride lipase gene. Gene. 2001 Jul 11;272(1-2):11-8. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
|
| Enzyme 98 Metabolite References |
Not Available |
|
Enzyme 99
[top]
|
| Enzyme 99 ID |
5550 |
| Enzyme 99 Name |
Galactocerebrosidase |
| Enzyme 99 Synonyms |
- GALCERase
- Galactocerebroside beta-galactosidase
- Galactosylceramidase
- Galactosylceramide beta-galactosidase
|
| Enzyme 99 Gene Name |
GALC |
| Enzyme 99 Protein Sequence |
>Galactocerebrosidase
MAEWLLSASWQRRAKAMTAAAGSAGRAAVPLLLCALLAPGGAYVLDDSDGLGREFDGIGA
VSGGGATSRLLVNYPEPYRSQILDYLFKPNFGASLHILKVEIGGDGQTTDGTEPSHMHYA
LDENYFRGYEWWLMKEAKKRNPNITLIGLPWSFPGWLGKGFDWPYVNLQLTAYYVVTWIV
GAKRYHDLDIDYIGIWNERSYNANYIKILRKMLNYQGLQRVKIIASDNLWESISASMLLD
AELFKVVDVIGAHYPGTHSAKDAKLTGKKLWSSEDFSTLNSDMGAGCWGRILNQNYINGY
MTSTIAWNLVASYYEQLPYGRCGLMTAQEPWSGHYVVESPVWVSAHTTQFTQPGWYYLKT
VGHLEKGGSYVALTDGLGNLTIIIETMSHKHSKCIRPFLPYFNVSQQFATFVLKGSFSEI
PELQVWYTKLGKTSERFLFKQLDSLWLLDSDGSFTLSLHEDELFTLTTLTTGRKGSYPLP
PKSQPFPSTYKDDFNVDYPFFSEAPNFADQTGVFEYFTNIEDPGEHHFTLRQVLNQRPIT
WAADASNTISIIGDYNWTNLTIKCDVYIETPDTGGVFIAGRVNKGGILIRSARGIFFWIF
ANGSYRVTGDLAGWIIYALGRVEVTAKKWYTLTLTIKGHFASGMLNDKSLWTDIPVNFPK
NGWAAIGTHSFEFAQFDNFLVEATR
|
| Enzyme 99 Number of Residues |
685 |
| Enzyme 99 Molecular Weight |
77032.8 |
| Enzyme 99 Theoretical pI |
6.62 |
| Enzyme 99 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- galactosylceramidase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- ion binding
|
| Process |
- carbohydrate metabolic process
- cellular lipid metabolic process
- galactosylceramide catabolic process
- galactosylceramide metabolic process
- glycolipid metabolic process
- glycosylceramide metabolic process
- lipid metabolic process
- membrane lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 99 General Function |
Involved in galactosylceramidase activity |
| Enzyme 99 Specific Function |
Hydrolyzes the galactose ester bonds of galactosylceramide, galactosylsphingosine, lactosylceramide, and monogalactosyldiglyceride. Enzyme with very low activity responsible for the lysosomal catabolism of galactosylceramide, a major lipid in myelin, kidney and epithelial cells of small intestine and colon |
| Enzyme 99 Pathways |
|
| Enzyme 99 Reactions |
- D-galactosyl-N-acylsphingosine + H2O = D-galactose + N-acylsphingosine [RN:R03617]
|
| Enzyme 99 Pfam Domain Function |
|
| Enzyme 99 Signals |
|
| Enzyme 99 Transmembrane Regions |
|
| Enzyme 99 Essentiality |
Not Available |
| Enzyme 99 GenBank ID Protein |
83281450 |
| Enzyme 99 UniProtKB/Swiss-Prot ID |
P54803 |
| Enzyme 99 UniProtKB/Swiss-Prot Entry Name |
GALC_HUMAN |
| Enzyme 99 PDB ID |
Not Available |
| Enzyme 99 Cellular Location |
Not Available |
| Enzyme 99 Gene Sequence |
>2058 bp
ATGGCTGAGTGGCTACTCTCGGCTTCCTGGCAACGCCGAGCGAAAGCTATGACTGCGGCC
GCGGGTTCGGCGGGCCGCGCCGCGGTGCCCTTGCTGCTGTGTGCGCTGCTGGCGCCCGGC
GGCGCGTACGTGCTCGACGACTCCGACGGGCTGGGCCGGGAGTTCGACGGCATCGGCGCG
GTCAGCGGCGGCGGGGCAACCTCCCGACTTCTAGTAAATTACCCAGAGCCCTATCGTTCT
CAGATATTGGATTATCTCTTTAAGCCGAATTTTGGTGCCTCTTTGCATATTTTAAAAGTG
GAAATAGGTGGTGATGGGCAGACAACAGACGGCACTGAGCCCTCCCACATGCATTATGCA
CTAGATGAGAATTATTTCCGAGGATACGAGTGGTGGTTGATGAAAGAAGCTAAGAAGAGG
AATCCCAATATTACACTCATTGGGTTGCCATGGTCATTCCCTGGATGGCTGGGAAAAGGT
TTCGACTGGCCTTATGTCAATCTTCAGCTGACTGCCTATTATGTCGTGACCTGGATTGTG
GGCGCCAAGCGTTACCATGATTTGGACATTGATTATATTGGAATTTGGAATGAGAGGTCA
TATAATGCCAATTATATTAAGATATTAAGAAAAATGCTGAATTATCAAGGTCTCCAGCGA
GTGAAAATCATAGCAAGTGATAATCTCTGGGAGTCCATCTCTGCATCCATGCTCCTTGAT
GCCGAACTCTTCAAGGTGGTTGATGTTATAGGGGCTCATTATCCTGGAACCCATTCAGCA
AAAGATGCAAAGTTGACTGGGAAGAAGCTTTGGTCTTCTGAAGACTTTAGCACTTTAAAT
AGTGACATGGGTGCAGGCTGCTGGGGTCGCATTTTAAATCAGAATTATATCAATGGCTAT
ATGACTTCCACAATCGCATGGAATTTAGTGGCTAGTTACTATGAACAGTTGCCTTATGGG
AGATGCGGGTTGATGACGGCCCAGGAGCCATGGAGTGGGCACTACGTGGTAGAATCTCCT
GTCTGGGTATCAGCTCATACCACTCAGTTTACTCAACCTGGCTGGTATTACCTGAAGACA
GTTGGCCATTTAGAGAAAGGAGGAAGCTACGTAGCTCTGACTGATGGCTTAGGGAACCTC
ACCATCATCATTGAAACCATGAGTCATAAACATTCTAAGTGCATACGGCCATTTCTTCCT
TATTTCAATGTGTCACAACAATTTGCCACCTTTGTTCTTAAGGGATCTTTTAGTGAAATA
CCAGAGCTACAGGTATGGTATACCAAACTTGGAAAAACATCCGAAAGATTTCTTTTTAAG
CAGCTGGATTCTCTATGGCTCCTTGACAGCGATGGCAGTTTCACACTGAGCCTGCATGAA
GATGAGCTGTTCACACTCACCACTCTCACCACTGGTCGCAAAGGCAGCTACCCGCTTCCT
CCAAAATCCCAGCCCTTCCCAAGTACCTATAAGGATGATTTCAATGTTGATTACCCATTT
TTTAGTGAAGCTCCAAACTTTGCTGATCAAACTGGTGTATTTGAATATTTTACAAATATT
GAAGACCCTGGCGAGCATCACTTCACGCTACGCCAAGTTCTCAACCAGAGACCCATTACG
TGGGCTGCCGATGCATCCAACACAATCAGTATTATAGGAGACTACAACTGGACCAATCTG
ACTATAAAGTGTGATGTATACATAGAGACCCCTGACACAGGAGGTGTGTTCATTGCAGGA
AGAGTAAATAAAGGTGGTATTTTGATTAGAAGTGCCAGAGGAATTTTCTTCTGGATTTTT
GCAAATGGATCTTACAGGGTTACAGGTGATTTAGCTGGATGGATTATATATGCTTTAGGA
CGTGTTGAAGTTACAGCAAAAAAATGGTATACACTCACGTTAACTATTAAGGGTCATTTC
ACCTCTGGCATGCTGAATGACAAGTCTCTGTGGACAGACATCCCTGTGAATTTTCCAAAG
AATGGCTGGGCTGCAATTGGAACTCACTCCTTTGAATTTGCACAGTTTGACAACTTTCTT
GTGGAAGCCACACGCTAA
|
| Enzyme 99 GenBank Gene ID |
NM_000153.2 |
| Enzyme 99 GeneCard ID |
GALC |
| Enzyme 99 GenAtlas ID |
GALC |
| Enzyme 99 HGNC ID |
HGNC:4115 |
| Enzyme 99 Chromosome Location |
1 |
| Enzyme 99 Locus |
14q31 |
| Enzyme 99 SNPs |
SNPJam Report |
| Enzyme 99 General References |
- Luzi P, Rafi MA, Wenger DA: Structure and organization of the human galactocerebrosidase (GALC) gene. Genomics. 1995 Mar 20;26(2):407-9. [PubMed ]
- Sakai N, Fukushima H, Inui K, Fu L, Nishigaki T, Yanagihara I, Tatsumi N, Ozono K, Okada S: Human galactocerebrosidase gene: promoter analysis of the 5'-flanking region and structural organization. Biochim Biophys Acta. 1998 Jan 7;1395(1):62-7. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed ]
- Chen YQ, Rafi MA, de Gala G, Wenger DA: Cloning and expression of cDNA encoding human galactocerebrosidase, the enzyme deficient in globoid cell leukodystrophy. Hum Mol Genet. 1993 Nov;2(11):1841-5. [PubMed ]
- Sakai N, Inui K, Fujii N, Fukushima H, Nishimoto J, Yanagihara I, Isegawa Y, Iwamatsu A, Okada S: Krabbe disease: isolation and characterization of a full-length cDNA for human galactocerebrosidase. Biochem Biophys Res Commun. 1994 Jan 28;198(2):485-91. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Chen YQ, Wenger DA: Galactocerebrosidase from human urine: purification and partial characterization. Biochim Biophys Acta. 1993 Sep 29;1170(1):53-61. [PubMed ]
- Wenger DA, Rafi MA, Luzi P: Molecular genetics of Krabbe disease (globoid cell leukodystrophy): diagnostic and clinical implications. Hum Mutat. 1997;10(4):268-79. [PubMed ]
- Wenger DA, Rafi MA, Luzi P, Datto J, Costantino-Ceccarini E: Krabbe disease: genetic aspects and progress toward therapy. Mol Genet Metab. 2000 May;70(1):1-9. [PubMed ]
- Rafi MA, Luzi P, Chen YQ, Wenger DA: A large deletion together with a point mutation in the GALC gene is a common mutant allele in patients with infantile Krabbe disease. Hum Mol Genet. 1995 Aug;4(8):1285-9. [PubMed ]
- Tatsumi N, Inui K, Sakai N, Fukushima H, Nishimoto J, Yanagihara I, Nishigaki T, Tsukamoto H, Fu L, Taniike M, et al.: Molecular defects in Krabbe disease. Hum Mol Genet. 1995 Oct;4(10):1865-8. [PubMed ]
- De Gasperi R, Gama Sosa MA, Sartorato EL, Battistini S, MacFarlane H, Gusella JF, Krivit W, Kolodny EH: Molecular heterogeneity of late-onset forms of globoid-cell leukodystrophy. Am J Hum Genet. 1996 Dec;59(6):1233-42. [PubMed ]
- Rafi MA, Luzi P, Zlotogora J, Wenger DA: Two different mutations are responsible for Krabbe disease in the Druze and Moslem Arab populations in Israel. Hum Genet. 1996 Mar;97(3):304-8. [PubMed ]
- Furuya H, Kukita Y, Nagano S, Sakai Y, Yamashita Y, Fukuyama H, Inatomi Y, Saito Y, Koike R, Tsuji S, Fukumaki Y, Hayashi K, Kobayashi T: Adult onset globoid cell leukodystrophy (Krabbe disease): analysis of galactosylceramidase cDNA from four Japanese patients. Hum Genet. 1997 Sep;100(3-4):450-6. [PubMed ]
- De Gasperi R, Gama Sosa MA, Sartorato E, Battistini S, Raghavan S, Kolodny EH: Molecular basis of late-life globoid cell leukodystrophy. Hum Mutat. 1999;14(3):256-62. [PubMed ]
- Fu L, Inui K, Nishigaki T, Tatsumi N, Tsukamoto H, Kokubu C, Muramatsu T, Okada S: Molecular heterogeneity of Krabbe disease. J Inherit Metab Dis. 1999 Apr;22(2):155-62. [PubMed ]
|
| Enzyme 99 Metabolite References |
Not Available |
|
Enzyme 100
[top]
|
| Enzyme 100 ID |
5551 |
| Enzyme 100 Name |
Arylsulfatase D |
| Enzyme 100 Synonyms |
- ASD
|
| Enzyme 100 Gene Name |
ARSD |
| Enzyme 100 Protein Sequence |
>Arylsulfatase D
MRSAARRGRAAPAARDSLPVLLFLCLLLKTCEPKTANAFKPNILLIMADDLGTGDLGCYG
NNTLRTPNIDQLAEEGVRLTQHLAAAPLCTPSRAAFLTGRHSFRSGMDASNGYRALQWNA
GSGGLPENETTFARILQQHGYATGLIGKWHQGVNCASRGDHCHHPLNHGFDYFYGMPFTL
TNDCDPGRPPEVDAALRAQLWGYTQFLALGILTLAAGQTCGFFSVSARAVTGMAGVGCLF
FISWYSSFGFVRRWNCILMRNHDVTEQPMVLEKTASLMLKEAVSYIERHKHGPFLLFLSL
LHVHIPLVTTSAFLGKSQHGLYGDNVEEMDWLIGKVLNAIEDNGLKNSTFTYFTSDHGGH
LEARDGHSQLGGWNGIYKGGKGMGGWEGGIRVPGIFHWPGVLPAGRVIGEPTSLMDVFPT
VVQLVGGEVPQDRVIDGHSLVPLLQGAEARSAHEFLFHYCGQHLHAARWHQKDSGSVWKV
HYTTPQFHPEGAGACYGRGVCPCSGEGVTHHRPPLLFDLSRDPSEARPLTPDSEPLYHAV
IARVGAAVSEHRQTLSPVPQQFSMSNILWKPWLQPCCGHFPFCSCHEDGDGTP
|
| Enzyme 100 Number of Residues |
593 |
| Enzyme 100 Molecular Weight |
64859.3 |
| Enzyme 100 Theoretical pI |
7.24 |
| Enzyme 100 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- sulfuric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 100 General Function |
Involved in catalytic activity |
| Enzyme 100 Specific Function |
Not Available |
| Enzyme 100 Pathways |
Not Available |
| Enzyme 100 Reactions |
Not Available |
| Enzyme 100 Pfam Domain Function |
|
| Enzyme 100 Signals |
|
| Enzyme 100 Transmembrane Regions |
|
| Enzyme 100 Essentiality |
Not Available |
| Enzyme 100 GenBank ID Protein |
791002 |
| Enzyme 100 UniProtKB/Swiss-Prot ID |
P51689 |
| Enzyme 100 UniProtKB/Swiss-Prot Entry Name |
ARSD_HUMAN |
| Enzyme 100 PDB ID |
Not Available |
| Enzyme 100 Cellular Location |
Not Available |
| Enzyme 100 Gene Sequence |
>1782 bp
ATGCGATCCGCCGCGCGGAGGGGACGCGCCGCGCCCGCCGCCAGGGACTCTTTGCCGGTG
CTACTGTTTTTATGCTTGCTTCTGAAGACGTGTGAACCTAAAACTGCAAATGCCTTTAAA
CCAAATATCCTACTGATCATGGCGGATGATCTAGGCACTGGGGATCTCGGTTGCTACGGG
AACAATACACTGAGAACGCCGAATATTGACCAGCTTGCAGAGGAAGGTGTGAGGCTCACT
CAGCACCTGGCGGCCGCCCCGCTCTGCACCCCAAGCCGAGCTGCATTCCTCACAGGGAGA
CATTCCTTCAGATCAGGCATGGACGCCAGCAATGGATACCGGGCCCTTCAGTGGAACGCA
GGCTCAGGTGGACTCCCTGAGAACGAAACCACTTTTGCAAGAATCTTGCAGCAGCATGGC
TATGCAACCGGCCTCATAGGAAAATGGCACCAGGGTGTGAATTGTGCATCCCGCGGGGAT
CACTGCCACCACCCCCTGAACCACGGATTTGACTATTTCTACGGCATGCCCTTCACGCTC
ACAAACGACTGTGACCCAGGCAGGCCCCCCGAAGTGGACGCCGCCCTGAGGGCGCAGCTC
TGGGGTTACACCCAGTTCCTGGCGCTGGGGATTCTCACCCTGGCTGCCGGCCAGACCTGC
GGTTTCTTCTCTGTCTCCGCGAGAGCAGTCACCGGCATGGCCGGCGTGGGCTGCCTGTTT
TTCATCTCTTGGTACTCCTCCTTCGGGTTTGTGCGACGCTGGAACTGTATCCTGATGAGA
AACCATGACGTCACGGAGCAACCCATGGTTCTGGAGAAAACAGCGAGTCTTATGCTAAAG
GAAGCTGTTTCCTATATTGAAAGACACAAGCATGGGCCATTTCTCCTCTTCCTTTCTTTG
CTGCATGTGCACATTCCCCTTGTGACCACGAGTGCATTCCTGGGGAAAAGTCAGCATGGC
TTATATGGTGATAATGTGGAGGAGATGGACTGGCTCATAGGTAAGGTTCTTAATGCCATC
GAAGACAATGGTTTAAAGAACTCAACATTCACGTATTTCACCTCTGACCATGGAGGACAT
TTAGAGGCAAGAGATGGACACAGCCAGTTAGGGGGATGGAACGGAATTTACAAAGGTGGG
AAGGGCATGGGAGGATGGGAAGGTGGGATCCGAGTGCCCGGGATCTTCCACTGGCCGGGG
GTGCTCCCGGCCGGCCGAGTGATTGGAGAGCCCACGAGCCTGATGGACGTGTTCCCTACT
GTGGTCCAGCTGGTGGGTGGCGAGGTGCCCCAGGACAGGGTGATTGATGGCCACAGCCTG
GTACCCTTGCTGCAGGGAGCTGAGGCACGCTCGGCACATGAGTTCCTGTTTCATTACTGT
GGGCAGCATCTTCACGCAGCACGCTGGCACCAGAAGGACAGTGGAAGCGTCTGGAAGGTT
CATTACACGACCCCGCAGTTCCACCCCGAGGAGCGGGGCCTGCTAACGGCCGAGGCGTCT
GCCCATGCTGAATGGGGAGGCGTGACCCATCACAGACCCCCTTTGCTCTTTGACCTCTCC
AGGGACCCCTCCGAGGCACGGCCCCTGACCCCCGACTCCGAGCCCCTGTACCACGCCGTG
ATAGCAAGGGTAGGTGCCGCGGTGTCGGAGCATCGGCAGACCCTGAGTCCTGTGCCCCAG
CAGTTTTCCATGAGCAACATCCTGTGGAAGCCGTGGCTGCAGCCGTGCTGCGGACATTTC
CCGTTCTGTTCATGCCACGAGGATGGGGATGGCACCCCCTGA
|
| Enzyme 100 GenBank Gene ID |
X83572 |
| Enzyme 100 GeneCard ID |
ARSD |
| Enzyme 100 GenAtlas ID |
ARSD |
| Enzyme 100 HGNC ID |
HGNC:717 |
| Enzyme 100 Chromosome Location |
Not Available |
| Enzyme 100 Locus |
Not Available |
| Enzyme 100 SNPs |
SNPJam Report |
| Enzyme 100 General References |
- Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed ]
- Urbitsch P, Salzer MJ, Hirschmann P, Vogt PH: Arylsulfatase D gene in Xp22.3 encodes two protein isoforms. DNA Cell Biol. 2000 Dec;19(12):765-73. [PubMed ]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
|
| Enzyme 100 Metabolite References |
Not Available |
|
Enzyme 101
[top]
|
| Enzyme 101 ID |
5552 |
| Enzyme 101 Name |
Sialidase-2 |
| Enzyme 101 Synonyms |
- Cytosolic sialidase
- N-acetyl-alpha-neuraminidase 2
|
| Enzyme 101 Gene Name |
NEU2 |
| Enzyme 101 Protein Sequence |
>Sialidase-2
MASLPVLQKESVFQSGAHAYRIPALLYLPGQQSLLAFAEQRASKKDEHAELIVLRRGDYD
APTHQVQWQAQEVVAQARLDGHRSMNPCPLYDAQTGTLFLFFIAIPGQVTEQQQLQTRAN
VTRLCQVTSTDHGRTWSSPRDLTDAAIGPAYREWSTFAVGPGHCLQLHDRARSLVVPAYA
YRKLHPIQRPIPSAFCFLSHDHGRTWARGHFVAQDTLECQVAEVETGEQRVVTLNARSHL
RARVQAQSTNDGLDFQESQLVKKLVEPPPQGCQGSVISFPSPRSGPGSPAQWLLYTHPTH
SWQRADLGAYLNPRPPAPEAWSEPVLLAKGSCAYSDLQSMGTGPDGSPLFGCLYEANDYE
EIVFLMFTLKQAFPAEYLPQ
|
| Enzyme 101 Number of Residues |
380 |
| Enzyme 101 Molecular Weight |
42253.3 |
| Enzyme 101 Theoretical pI |
6.87 |
| Enzyme 101 GO Classification |
Not Available |
| Enzyme 101 General Function |
Involved in exo-alpha-sialidase activity |
| Enzyme 101 Specific Function |
Hydrolyzes sialylated compounds |
| Enzyme 101 Pathways |
|
| Enzyme 101 Reactions |
- Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates ALL_REAC (other) R03491 R04018 R04634 R04650 R05115 R05117 R05996(G) R05998(G) R05999(G) R06012(G) R06147(G) R06253(G) INHIBITOR 2-Deoxy-2,3-dehydro-N-acetylneuraminic acid [CPD:C04580]
|
| Enzyme 101 Pfam Domain Function |
Not Available |
| Enzyme 101 Signals |
|
| Enzyme 101 Transmembrane Regions |
|
| Enzyme 101 Essentiality |
Not Available |
| Enzyme 101 GenBank ID Protein |
46575656 |
| Enzyme 101 UniProtKB/Swiss-Prot ID |
Q9Y3R4 |
| Enzyme 101 UniProtKB/Swiss-Prot Entry Name |
NEUR2_HUMAN |
| Enzyme 101 PDB ID |
1VCU |
| Enzyme 101 PDB File |
Show |
| Enzyme 101 3D Structure |
|
| Enzyme 101 Cellular Location |
Not Available |
| Enzyme 101 Gene Sequence |
>1143 bp
ATGGCGTCCCTTCCTGTCCTGCAGAAGGAGAGCGTGTTCCAGTCGGGAGCCCATGCCTAC
AGAATCCCTGCCCTGCTCTACCTGCCTGGGCAGCAGTCCCTGCTGGCCTTCGCGGAACAG
CGGGCAAGCAAGAAGGATGAGCACGCAGAGCTGATTGTCCTGCGCAGAGGAGACTACGAC
GCACCCACCCACCAGGTTCAGTGGCAAGCTCAGGAGGTGGTGGCCCAGGCCCGGCTGGAT
GGCCACCGGTCCATGAACCCATGCCCCTTGTATGACGCGCAGACGGGGACCCTCTTCCTC
TTCTTCATTGCCATCCCTGGGCAAGTCACGGAGCAACAGCAGCTGCAGACCAGGGCCAAT
GTGACGCGGCTGTGCCAAGTCACCAGCACTGACCACGGGAGGACCTGGAGCTCCCCCAGA
GACCTCACTGATGCGGCCATCGGCCCAGCCTACCGGGAGTGGTCCACCTTTGCAGTGGGC
CCGGGGCATTGTTTGCAGCTTCACGACAGGGCCCGGAGCCTGGTGGTGCCCGCCTACGCC
TACCGGAAACTTCACCCCATCCAAAGGCCGATCCCCTCTGCCTTCTGCTTCCTCAGCCAT
GACCATGGGCGCACGTGGGCGCGAGGGCACTTTGTGGCCCAGGACACCCTGGAGTGCCAG
GTGGCCGAAGTCGAGACTGGGGAGCAGAGGGTGGTGACCCTCAACGCGAGAAGCCACCTC
CGAGCCAGGGTCCAGGCCCAGAGCACCAATGACGGGCTTGATTTCCAGGAGTCTCAGCTG
GTGAAGAAGCTGGTGGAGCCGCCGCCCCAGGGCTGCCAGGGGAGCGTCATCAGCTTCCCC
AGCCCCCGCTCGGGGCCTGGCTCCCCAGCCCAGTGGCTGCTCTACACTCACCCCACACAC
TCCTGGCAGAGGGCCGACCTGGGTGCCTACCTCAACCCGCGACCTCCAGCCCCTGAGGCC
TGGTCAGAGCCGGTACTGCTGGCCAAGGGCAGCTGTGCCTACTCAGACCTCCAGAGCATG
GGCACCGGCCCTGATGGGTCCCCCTTGTTTGGGTGTCTGTACGAAGCCAATGATTACGAG
GAGATTGTCTTTCTCATGTTCACCCTGAAGCAAGCCTTCCCAGCTGAGTACCTGCCTCAG
TGA
|
| Enzyme 101 GenBank Gene ID |
BC069151 |
| Enzyme 101 GeneCard ID |
NEU2 |
| Enzyme 101 GenAtlas ID |
NEU2 |
| Enzyme 101 HGNC ID |
HGNC:7759 |
| Enzyme 101 Chromosome Location |
2 |
| Enzyme 101 Locus |
2q37 |
| Enzyme 101 SNPs |
SNPJam Report |
| Enzyme 101 General References |
- Monti E, Preti A, Rossi E, Ballabio A, Borsani G: Cloning and characterization of NEU2, a human gene homologous to rodent soluble sialidases. Genomics. 1999 Apr 1;57(1):137-43. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Chavas LM, Tringali C, Fusi P, Venerando B, Tettamanti G, Kato R, Monti E, Wakatsuki S: Crystal structure of the human cytosolic sialidase Neu2. Evidence for the dynamic nature of substrate recognition. J Biol Chem. 2005 Jan 7;280(1):469-75. Epub 2004 Oct 22. [PubMed ]
- Li CY, Yu Q, Ye ZQ, Sun Y, He Q, Li XM, Zhang W, Luo J, Gu X, Zheng X, Wei L: A nonsynonymous SNP in human cytosolic sialidase in a small Asian population results in reduced enzyme activity: potential link with severe adverse reactions to oseltamivir. Cell Res. 2007 Apr;17(4):357-62. [PubMed ]
|
| Enzyme 101 Metabolite References |
Not Available |
|
Enzyme 102
[top]
|
| Enzyme 102 ID |
5556 |
| Enzyme 102 Name |
Arylsulfatase A |
| Enzyme 102 Synonyms |
- ASA
- Cerebroside-sulfatase
- Arylsulfatase A component B
- Arylsulfatase A component C
|
| Enzyme 102 Gene Name |
ARSA |
| Enzyme 102 Protein Sequence |
>Arylsulfatase A
MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFT
DFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGM
AGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIP
LLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAE
RSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRC
GKGTTYEGGVREPALAFWPGHIAPGVTHELASSLDLLPTLAALAGAPLPNVTLDGFDLSP
LLLGTGKSPRQSLFFYPSYPDEVRGVFAVRTGKYKAHFFTQGSAHSDTTADPACHASSSL
TAHEPPLLYDLSKDPGENYNLLGGVAGATPEVLQALKQLQLLKAQLDAAVTFGPSQVARG
EDPALQICCHPGCTPRPACCHCPDPHA
|
| Enzyme 102 Number of Residues |
507 |
| Enzyme 102 Molecular Weight |
53587.6 |
| Enzyme 102 Theoretical pI |
6.01 |
| Enzyme 102 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- sulfuric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 102 General Function |
Involved in catalytic activity |
| Enzyme 102 Specific Function |
Hydrolyzes cerebroside sulfate |
| Enzyme 102 Pathways |
|
| Enzyme 102 Reactions |
- a cerebroside 3-sulfate + H2O = a cerebroside + sulfate [RN:R04856 R06280]
|
| Enzyme 102 Pfam Domain Function |
|
| Enzyme 102 Signals |
|
| Enzyme 102 Transmembrane Regions |
|
| Enzyme 102 Essentiality |
Not Available |
| Enzyme 102 GenBank ID Protein |
28858 |
| Enzyme 102 UniProtKB/Swiss-Prot ID |
P15289 |
| Enzyme 102 UniProtKB/Swiss-Prot Entry Name |
ARSA_HUMAN |
| Enzyme 102 PDB ID |
1E2S |
| Enzyme 102 PDB File |
Show |
| Enzyme 102 3D Structure |
|
| Enzyme 102 Cellular Location |
Not Available |
| Enzyme 102 Gene Sequence |
>1524 bp
ATGGGGGCACCGCGGTCCCTCCTCCTGGCCCTGGCTGCTGGCCTGGCCGTTGCCCGTCCG
CCCAACATCGTGCTGATCTTTGCCGACGACCTCGGCTATGGGGACCTGGGCTGCTATGGG
CACCCCAGCTCTACCACTCCCAACCTGGACCAGCTGGCGGCGGGAGGGCTGCGGTTCACA
GACTTCTACGTGCCTGTGTCTCTGTGCACACCCTCTAGGGCCGCCCTCCTGACCGGCCGG
CTCCCGGTTCGGATGGGCATGTACCCTGGCGTCCTGGTGCCCAGCTCCCGGGGGGGCCTG
CCCCTGGAGGAGGTGACCGTGGCCGAAGTCCTGGCTGCCCGAGGCTACCTCACAGGAATG
GCCGGCAAGTGGCACCTTGGGGTGGGGCCTGAGGGGGCCTTCCTGCCCCCCCATCAGGGC
TTCCATCGATTTCTAGGCATCCCGTACTCCCACGACCAGGGCCCCTGCCAGAACCTGACC
TGCTTCCCGCCGGCCACTCCTTGCGACGGTGGCTGTGACCAGGGCCTGGTCCCCATCCCA
CTGTTGGCCAACCTGTCCGTGGAGGCGCAGCCCCCCTGGCTGCCCGGACTAGAGGCCCGC
TACATGGCTTTCGCCCATGACCTCATGGCCGACGCCCAGCGCCAGGATCGCCCCTTCTTC
CTGTACTATGCCTCTCACCACACCCACTACCCTCAGTTCAGTGGGCAGAGCTTTGCAGAG
CGTTCAGGCCGCGGGCCATTTGGGGACTCCCTGATGGAGCTGGATGCAGCTGTGGGGACC
CTGATGACAGCCATAGGGGACCTGGGGCTGCTTGAAGAGACGCTGGTCATCTTCACTGCA
GACAATGGACCTGAGACCATGCGTATGTCCCGAGGCGGCTGCTCCGGTCTCTTGCGGTGT
GGAAAGGGAACGACCTACGAGGGCGGTGTCCGAGAGCCTGCCTTGGCCTTCTGGCCAGGT
CATATCGCTCCCGGCGTGACCCACGAGCTGGCCAGCTCCCTGGACCTGCTGCCTACCCTG
GCAGCCCTGGCTGGGGCCCCACTGCCCAATGTCACCTTGGATGGCTTTGACCTCAGCCCC
CTGCTGCTGGGCACAGGCAAGAGCCCTCGGCAGTCTCTCTTCTTCTACCCGTCCTACCCA
GACGAGGTCCGTGGGGTTTTTGCTGTGCGGACTGGAAAGTACAAGGCTCACTTCTTCACC
CAGGGCTCTGCCCACAGTGATACCACTGCAGACCCTGCCTGCCACGCCTCCAGCTCTCTG
ACTGCTCATGAGCCCCCGCTGCTCTATGACCTGTCCAAGGACCCTGGTGAGAACTACAAC
CTGCTGGGGGGTGTGGCCGGGGCCACCCCAGAGGTGCTGCAAGCCCTGAAACAGCTTCAG
CTGCTCAAGGCCCAGTTAGACGCAGCTGTGACCTTCGGCCCCAGCCAGGTGGCCCGGGGC
GAGGACCCCGCCCTGCAGATCTGCTGTCATCCTGGCTGCACCCCCCGCCCAGCTTGCTGC
CATTGCCCAGATCCCCATGCCTGA
|
| Enzyme 102 GenBank Gene ID |
X52151 |
| Enzyme 102 GeneCard ID |
ARSA |
| Enzyme 102 GenAtlas ID |
ARSA |
| Enzyme 102 HGNC ID |
HGNC:713 |
| Enzyme 102 Chromosome Location |
2 |
| Enzyme 102 Locus |
22q13.31-qter|22q13.33 |
| Enzyme 102 SNPs |
SNPJam Report |
| Enzyme 102 General References |
- Stein C, Gieselmann V, Kreysing J, Schmidt B, Pohlmann R, Waheed A, Meyer HE, O'Brien JS, von Figura K: Cloning and expression of human arylsulfatase A. J Biol Chem. 1989 Jan 15;264(2):1252-9. [PubMed ]
- Kreysing J, von Figura K, Gieselmann V: Structure of the arylsulfatase A gene. Eur J Biochem. 1990 Aug 17;191(3):627-31. [PubMed ]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Fujii T, Kobayashi T, Honke K, Gasa S, Ishikawa M, Shimizu T, Makita A: Proteolytic processing of human lysosomal arylsulfatase A. Biochim Biophys Acta. 1992 Jul 13;1122(1):93-8. [PubMed ]
- Schmidt B, Selmer T, Ingendoh A, von Figura K: A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 1995 Jul 28;82(2):271-8. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
- Lukatela G, Krauss N, Theis K, Selmer T, Gieselmann V, von Figura K, Saenger W: Crystal structure of human arylsulfatase A: the aldehyde function and the metal ion at the active site suggest a novel mechanism for sulfate ester hydrolysis. Biochemistry. 1998 Mar 17;37(11):3654-64. [PubMed ]
- von Bulow R, Schmidt B, Dierks T, von Figura K, Uson I: Crystal structure of an enzyme-substrate complex provides insight into the interaction between human arylsulfatase A and its substrates during catalysis. J Mol Biol. 2001 Jan 12;305(2):269-77. [PubMed ]
- Chruszcz M, Laidler P, Monkiewicz M, Ortlund E, Lebioda L, Lewinski K: Crystal structure of a covalent intermediate of endogenous human arylsulfatase A. J Inorg Biochem. 2003 Aug 1;96(2-3):386-92. [PubMed ]
- Roeser D, Preusser-Kunze A, Schmidt B, Gasow K, Wittmann JG, Dierks T, von Figura K, Rudolph MG: A general binding mechanism for all human sulfatases by the formylglycine-generating enzyme. Proc Natl Acad Sci U S A. 2006 Jan 3;103(1):81-6. Epub 2005 Dec 20. [PubMed ]
- Gieselmann V, Zlotogora J, Harris A, Wenger DA, Morris CP: Molecular genetics of metachromatic leukodystrophy. Hum Mutat. 1994;4(4):233-42. [PubMed ]
- Gieselmann V, Polten A, Kreysing J, von Figura K: Arylsulfatase A pseudodeficiency: loss of a polyadenylylation signal and N-glycosylation site. Proc Natl Acad Sci U S A. 1989 Dec;86(23):9436-40. [PubMed ]
- Kondo R, Wakamatsu N, Yoshino H, Fukuhara N, Miyatake T, Tsuji S: Identification of a mutation in the arylsulfatase A gene of a patient with adult-type metachromatic leukodystrophy. Am J Hum Genet. 1991 May;48(5):971-8. [PubMed ]
- Gieselmann V, Fluharty AL, Tonnesen T, Von Figura K: Mutations in the arylsulfatase A pseudodeficiency allele causing metachromatic leukodystrophy. Am J Hum Genet. 1991 Aug;49(2):407-13. [PubMed ]
- Polten A, Fluharty AL, Fluharty CB, Kappler J, von Figura K, Gieselmann V: Molecular basis of different forms of metachromatic leukodystrophy. N Engl J Med. 1991 Jan 3;324(1):18-22. [PubMed ]
- Kappler J, von Figura K, Gieselmann V: Late-onset metachromatic leukodystrophy: molecular pathology in two siblings. Ann Neurol. 1992 Mar;31(3):256-61. [PubMed ]
- Kreysing J, Bohne W, Bosenberg C, Marchesini S, Turpin JC, Baumann N, von Figura K, Gieselmann V: High residual arylsulfatase A (ARSA) activity in a patient with late-infantile metachromatic leukodystrophy. Am J Hum Genet. 1993 Aug;53(2):339-46. [PubMed ]
- Hasegawa Y, Kawame H, Eto Y: Mutations in the arylsulfatase A gene of Japanese patients with metachromatic leukodystrophy. DNA Cell Biol. 1993 Jul-Aug;12(6):493-8. [PubMed ]
- Barth ML, Fensom A, Harris A: Prevalence of common mutations in the arylsulphatase A gene in metachromatic leukodystrophy patients diagnosed in Britain. Hum Genet. 1993 Mar;91(1):73-7. [PubMed ]
- Honke K, Kobayashi T, Fujii T, Gasa S, Xu M, Takamaru Y, Kondo R, Tsuji S, Makita A: An adult-type metachromatic leukodystrophy caused by substitution of serine for glycine-122 in arylsulfatase A. Hum Genet. 1993 Nov;92(5):451-6. [PubMed ]
- Barth ML, Fensom A, Harris A: Missense mutations in the arylsulphatase A genes of metachromatic leukodystrophy patients. Hum Mol Genet. 1993 Dec;2(12):2117-21. [PubMed ]
- Harvey JS, Nelson PV, Carey WF, Robertson EF, Morris CP: An arylsulfatase A (ARSA) missense mutation (T274M) causing late-infantile metachromatic leukodystrophy. Hum Mutat. 1993;2(4):261-7. [PubMed ]
- Hasegawa Y, Kawame H, Ida H, Ohashi T, Eto Y: Single exon mutation in arylsulfatase A gene has two effects: loss of enzyme activity and aberrant splicing. Hum Genet. 1994 Apr;93(4):415-20. [PubMed ]
- Heinisch U, Zlotogora J, Kafert S, Gieselmann V: Multiple mutations are responsible for the high frequency of metachromatic leukodystrophy in a small geographic area. Am J Hum Genet. 1995 Jan;56(1):51-7. [PubMed ]
- Kafert S, Heinisch U, Zlotogora J, Gieselmann V: A missense mutation P136L in the arylsulfatase A gene causes instability and loss of activity of the mutant enzyme. Hum Genet. 1995 Feb;95(2):201-4. [PubMed ]
- Barth ML, Fensom A, Harris A: Identification of seven novel mutations associated with metachromatic leukodystrophy. Hum Mutat. 1995;6(2):170-6. [PubMed ]
- Tsuda T, Hasegawa Y, Eto Y: Two novel mutations in a Japanese patient with the late-infantile form of metachromatic leukodystrophy. Brain Dev. 1996 Sep-Oct;18(5):400-3. [PubMed ]
- Hess B, Kafert S, Heinisch U, Wenger DA, Zlotogora J, Gieselmann V: Characterization of two arylsulfatase A missense mutations D335V and T274M causing late infantile metachromatic leukodystrophy. Hum Mutat. 1996;7(4):311-7. [PubMed ]
- Regis S, Filocamo M, Stroppiano M, Corsolini F, Gatti R: A T > C transition causing a Leu > Pro substitution in a conserved region of the arylsulfatase A gene in a late infantile metachromatic leukodystrophy patient. Clin Genet. 1997 Jul;52(1):65-7. [PubMed ]
- Draghia R, Letourneur F, Drugan C, Manicom J, Blanchot C, Kahn A, Poenaru L, Caillaud C: Metachromatic leukodystrophy: identification of the first deletion in exon 1 and of nine novel point mutations in the arylsulfatase A gene. Hum Mutat. 1997;9(3):234-42. [PubMed ]
- Regis S, Filocamo M, Stroppiano M, Corsolini F, Caroli F, Gatti R: A 9-bp deletion (2320del9) on the background of the arylsulfatase A pseudodeficiency allele in a metachromatic leukodystrophy patient and in a patient with nonprogressive neurological symptoms. Hum Genet. 1998 Jan;102(1):50-3. [PubMed ]
- Gomez-Lira M, Perusi C, Mottes M, Pignatti PF, Manfredi M, Rizzuto N, Salviati A: Molecular genetic characterization of two metachromatic leukodystrophy patients who carry the T799G mutation and show different phenotypes; description of a novel null-type mutation. Hum Genet. 1998 Apr;102(4):459-63. [PubMed ]
- Ricketts MH, Poretz RD, Manowitz P: The R496H mutation of arylsulfatase A does not cause metachromatic leukodystrophy. Hum Mutat. 1998;12(4):238-9. [PubMed ]
- Coulter-Mackie MB, Gagnier L: Two novel mutations in the arylsulfatase A gene associated with juvenile (R390Q) and adult onset (H397Y) metachromatic leukodystrophy. Hum Mutat. 1998;Suppl 1:S254-6. [PubMed ]
- Kurosawa K, Ida H, Eto Y: Prevalence of arylsulphatase A mutations in 11 Japanese patients with metachromatic leukodystrophy: identification of two novel mutations. J Inherit Metab Dis. 1998 Oct;21(7):781-2. [PubMed ]
- Berger J, Gmach M, Mayr U, Molzer B, Bernheimer H: Coincidence of two novel arylsulfatase A alleles and mutation 459+1G>A within a family with metachromatic leukodystrophy: molecular basis of phenotypic heterogeneity. Hum Mutat. 1999;13(1):61-8. [PubMed ]
- Marcao A, Amaral O, Pinto E, Pinto R, Sa Miranda MC: Metachromatic leucodystrophy in Portugal-finding of four new molecular lesions: C300F, P425T, g.1190-1191insC, and g.2408delC. Mutations in brief no. 232. Online. Hum Mutat. 1999;13(4):337-8. [PubMed ]
- Gort L, Coll MJ, Chabas A: Identification of 12 novel mutations and two new polymorphisms in the arylsulfatase A gene: haplotype and genotype-phenotype correlation studies in Spanish metachromatic leukodystrophy patients. Hum Mutat. 1999;14(3):240-8. [PubMed ]
- Halsall DJ, Halligan EP, Elsey TS, Cox TM: Metachromatic leucodystrophy: a newly identified mutation in arylsulphatase A, D281Y, found as a compound heterozygote with I179L in an adult onset case. Hum Mutat. 1999 Nov;14(5):447. [PubMed ]
- Qu Y, Shapira E, Desnick RJ: Metachromatic leukodystrophy: subtype genotype/phenotype correlations and identification of novel missense mutations (P148L and P191T) causing the juvenile-onset disease. Mol Genet Metab. 1999 Jul;67(3):206-12. [PubMed ]
- Hermann S, Schestag F, Polten A, Kafert S, Penzien J, Zlotogora J, Baumann N, Gieselmann V: Characterization of four arylsulfatase A missense mutations G86D, Y201C, D255H, and E312D causing metachromatic leukodystrophy. Am J Med Genet. 2000 Mar 6;91(1):68-73. [PubMed ]
- Felice KJ, Gomez Lira M, Natowicz M, Grunnet ML, Tsongalis GJ, Sima AA, Kaplan RF: Adult-onset MLD: a gene mutation with isolated polyneuropathy. Neurology. 2000 Oct 10;55(7):1036-9. [PubMed ]
- Arbour LT, Silver K, Hechtman P, Treacy EP, Coulter-Mackie MB: Variable onset of metachromatic leukodystrophy in a Vietnamese family. Pediatr Neurol. 2000 Aug;23(2):173-6. [PubMed ]
- Comabella M, Waye JS, Raguer N, Eng B, Dominguez C, Navarro C, Borras C, Krivit W, Montalban X: Late-onset metachromatic leukodystrophy clinically presenting as isolated peripheral neuropathy: compound heterozygosity for the IVS2+1G-->A mutation and a newly identified missense mutation (Thr408Ile) in a Spanish family. Ann Neurol. 2001 Jul;50(1):108-12. [PubMed ]
- Regis S, Corsolini F, Stroppiano M, Cusano R, Filocamo M: Contribution of arylsulfatase A mutations located on the same allele to enzyme activity reduction and metachromatic leukodystrophy severity. Hum Genet. 2002 Apr;110(4):351-5. Epub 2002 Mar 8. [PubMed ]
- Marcao A, Simonis H, Schestag F, Sa Miranda MC, Gieselmann V: Biochemical characterization of two (C300F, P425T) arylsulfatase a missense mutations. Am J Med Genet A. 2003 Jan 30;116A(3):238-42. [PubMed ]
- Marcao A, Azevedo JE, Gieselmann V, Sa Miranda MC: Oligomerization capacity of two arylsulfatase A mutants: C300F and P425T. Biochem Biophys Res Commun. 2003 Jun 20;306(1):293-7. [PubMed ]
- Eng B, Nakamura LN, O'Reilly N, Schokman N, Nowaczyk MM, Krivit W, Waye JS: Identification of nine novel arylsulfatase a (ARSA) gene mutations in patients with metachromatic leukodystrophy (MLD). Hum Mutat. 2003 Nov;22(5):418-9. [PubMed ]
- Olkhovich NV, Takamura N, Pichkur NA, Gorovenko NG, Aoyagi K, Yamashita S: Novel mutations in arylsulfatase A gene in three Ukrainian families with metachromatic leukodystrophy. Mol Genet Metab. 2003 Nov;80(3):360-3. [PubMed ]
- Berna L, Gieselmann V, Poupetova H, Hrebicek M, Elleder M, Ledvinova J: Novel mutations associated with metachromatic leukodystrophy: phenotype and expression studies in nine Czech and Slovak patients. Am J Med Genet A. 2004 Sep 1;129A(3):277-81. [PubMed ]
- Gallo S, Randi D, Bertelli M, Salviati A, Pandolfo M: Late onset MLD with normal nerve conduction associated with two novel missense mutations in the ASA gene. J Neurol Neurosurg Psychiatry. 2004 Apr;75(4):655-7. [PubMed ]
- Marcao AM, Wiest R, Schindler K, Wiesmann U, Weis J, Schroth G, Miranda MC, Sturzenegger M, Gieselmann V: Adult onset metachromatic leukodystrophy without electroclinical peripheral nervous system involvement: a new mutation in the ARSA gene. Arch Neurol. 2005 Feb;62(2):309-13. [PubMed ]
- Grossi S, Regis S, Rosano C, Corsolini F, Uziel G, Sessa M, Di Rocco M, Parenti G, Deodato F, Leuzzi V, Biancheri R, Filocamo M: Molecular analysis of ARSA and PSAP genes in twenty-one Italian patients with metachromatic leukodystrophy: identification and functional characterization of 11 novel ARSA alleles. Hum Mutat. 2008 Nov;29(11):E220-30. [PubMed ]
|
| Enzyme 102 Metabolite References |
Not Available |
|
Enzyme 103
[top]
|
| Enzyme 103 ID |
5557 |
| Enzyme 103 Name |
Arylsulfatase B |
| Enzyme 103 Synonyms |
- ASB
- N-acetylgalactosamine-4-sulfatase
- G4S
|
| Enzyme 103 Gene Name |
ARSB |
| Enzyme 103 Protein Sequence |
>Arylsulfatase B
MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDV
GFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPS
CVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHER
CTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQS
VHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTD
NGGQTLAGGNNWPLRGRKWSLWEGGVRGVGFVASPLLKQKGVKNRELIHISDWLPTLVKL
ARGHTNGTKPLDGFDVWKTISEGSPSPRIELLHNIDPNFVDSSPCPRNSMAPAKDDSSLP
EYSAFNTSVHAAIRHGNWKLLTGYPGCGYWFPPPSQYNVSEIPSSDPPTKTLWLFDIDRD
PEERHDLSREYPHIVTKLLSRLQFYHKHSVPVYFPAQDPRCDPKATGVWGPWM
|
| Enzyme 103 Number of Residues |
533 |
| Enzyme 103 Molecular Weight |
59686.7 |
| Enzyme 103 Theoretical pI |
8.31 |
| Enzyme 103 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- sulfuric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 103 General Function |
Involved in catalytic activity |
| Enzyme 103 Specific Function |
Hydrolysis of the 4-sulfate groups of the N- acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate |
| Enzyme 103 Pathways |
- Glycosaminoglycan degradation (map00531 )
|
| Enzyme 103 Reactions |
- Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate [RN:R07823] ALL_REAC R07823(G)
|
| Enzyme 103 Pfam Domain Function |
|
| Enzyme 103 Signals |
|
| Enzyme 103 Transmembrane Regions |
|
| Enzyme 103 Essentiality |
Not Available |
| Enzyme 103 GenBank ID Protein |
179077 |
| Enzyme 103 UniProtKB/Swiss-Prot ID |
P15848 |
| Enzyme 103 UniProtKB/Swiss-Prot Entry Name |
ARSB_HUMAN |
| Enzyme 103 PDB ID |
1FSU |
| Enzyme 103 PDB File |
Show |
| Enzyme 103 3D Structure |
|
| Enzyme 103 Cellular Location |
Not Available |
| Enzyme 103 Gene Sequence |
>1602 bp
ATGGGTCCGCGCGGCGCGGCGAGCTTGCCCCGAGGCCCCGGACCTCGGCGGCTGCTCCTC
CCCGTCGTCCTCCCGCTGCTGCTGCTGCTGTTGTTGGCGCCGCCGGGCTCGGGCGCCGGG
GCCAGCCGGCCGCCCCACCTGGTCTTCTTGCTGGCAGACGACCTAGGCTGGAACGACGTC
GGCTTCCACGGCTCCCGCATCCGCACGCCGCACCTGGACGCGCTGGCGGCCGGCGGGGTG
CTCCTGGACAACTACTACACGCAGCCGCTGTGCACGCCGTCGCGGAGCCAGCTGCTCACT
GGCCGCTACCAGATCCGTACAGGTTTACAGCACCAAATAATCTGGCCCTGTCAGCCCAGC
TGTGTTCCTCTGGATGAAAAACTCCTGCCCCAGCTCCTAAAAGAAGCAGGTTATACTACC
CATATGGTCGGAAAATGGCACCTGGGAATGTACCGGAAAGAATGCCTTCCAACCCGCCGA
GGATTTGATACCTACTTTGGATATCTCCTGGGTAGTGAAGATTATTATTCCCATGAACGC
TGTACATTAATTGACGCTCTGAATGTCACACGATGTGCTCTTGATTTTCGAGATGGCGAA
GAAGTTGCAACAGGATATAAAAATATGTATTCAACAAACATATTCACCAAAAGGGCTATA
GCCCTCATAACTAACCATCCACCAGAGAAGCCTCTGTTTCTCTACCTTGCTCTCCAGTCT
GTGCATGAGCCCCTTCAGGTCCCTGAGGAATACTTGAAGCCATATGACTTTATCCAAGAC
AAGAACAGGCATCACTATGCAGGAATGGTGTCCCTTATGGATGAAGCAGTAGGAAATGTC
ACTGCAGCTTTAAAAAGCAGTGGGCTCTGGAACAACACGGTGTTCATCTTTTCTACAGAT
AACGGAGGGCAGACTTTGGCAGGGGGTAATAACTGGCCCCTTCGAGGAAGAAAATGGAGC
CTGTGGGAAGGAGGCGTCCGAGGGGTGGGCTTTGTGGCAAGCCCCTTGCTGAAGCAGAAG
GGCGTGAAGAACCGGGAGCTCATCCACATCTCTGACTGGCTGCCAACACTCGTGAAGCTG
GCCAGGGGACACACCAATGGCACAAAGCCTCTGGATGGCTTCGACGTGTGGAAAACCATC
AGTGAAGGAAGCCCATCCCCCAGAATTGAGCTGCTGCATAATATTGACCCAAACTTCGTG
GACTCTTCACCGTGTCCCAGGAACAGCATGGCTCCAGCAAAGGATGACTCTTCTCTTCCA
GAATATTCAGCCTTTAACACATCTGTCCATGCTGCAATTAGACATGGAAATTGGAAACTC
CTCACGGGCTACCCAGGCTGTGGTTACTGGTTCCCTCCACCGTCTCAATACAATGTTTCT
GAGATACCCTCATCAGACCCACCAACCAAGACCCTCTGGCTCTTTGATATTGATCGGGAC
CCTGAAGAAAGACATGACCTGTCCAGAGAATATCCTCACATCGTCACAAAGCTCCTGTCC
CGCCTACAGTTCTACCATAAACACTCAGTCCCCGTGTACTTCCCTGCACAGGACCCCCGC
TGTGATCCCAAGGCCACTGGGGTGTGGGGCCCTTGGATGTAG
|
| Enzyme 103 GenBank Gene ID |
J05225 |
| Enzyme 103 GeneCard ID |
ARSB |
| Enzyme 103 GenAtlas ID |
ARSB |
| Enzyme 103 HGNC ID |
HGNC:714 |
| Enzyme 103 Chromosome Location |
5 |
| Enzyme 103 Locus |
5q11-q13 |
| Enzyme 103 SNPs |
SNPJam Report |
| Enzyme 103 General References |
- Peters C, Schmidt B, Rommerskirch W, Rupp K, Zuhlsdorf M, Vingron M, Meyer HE, Pohlmann R, von Figura K: Phylogenetic conservation of arylsulfatases. cDNA cloning and expression of human arylsulfatase B. J Biol Chem. 1990 Feb 25;265(6):3374-81. [PubMed ]
- Schuchman EH, Jackson CE, Desnick RJ: Human arylsulfatase B: MOPAC cloning, nucleotide sequence of a full-length cDNA, and regions of amino acid identity with arylsulfatases A and C. Genomics. 1990 Jan;6(1):149-58. [PubMed ]
- Modaressi S, Rupp K, von Figura K, Peters C: Structure of the human arylsulfatase B gene. Biol Chem Hoppe Seyler. 1993 May;374(5):327-35. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Litjens T, Morris CP, Gibson GJ, Beckmann KR, Hopwood JJ: Human N-acetylgalactosamine-4-sulphatase: protein maturation and isolation of genomic clones. Biochem Int. 1991 May;24(2):209-15. [PubMed ]
- Kobayashi T, Honke K, Jin T, Gasa S, Miyazaki T, Makita A: Components and proteolytic processing sites of arylsulfatase B from human placenta. Biochim Biophys Acta. 1992 Oct 20;1159(3):243-7. [PubMed ]
- Schmidt B, Selmer T, Ingendoh A, von Figura K: A novel amino acid modification in sulfatases that is defective in multiple sulfatase deficiency. Cell. 1995 Jul 28;82(2):271-8. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
- Bond CS, Clements PR, Ashby SJ, Collyer CA, Harrop SJ, Hopwood JJ, Guss JM: Structure of a human lysosomal sulfatase. Structure. 1997 Feb 15;5(2):277-89. [PubMed ]
- Wicker G, Prill V, Brooks D, Gibson G, Hopwood J, von Figura K, Peters C: Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). An intermediate clinical phenotype caused by substitution of valine for glycine at position 137 of arylsulfatase B. J Biol Chem. 1991 Nov 15;266(32):21386-91. [PubMed ]
- Jin WD, Jackson CE, Desnick RJ, Schuchman EH: Mucopolysaccharidosis type VI: identification of three mutations in the arylsulfatase B gene of patients with the severe and mild phenotypes provides molecular evidence for genetic heterogeneity. Am J Hum Genet. 1992 Apr;50(4):795-800. [PubMed ]
- Isbrandt D, Arlt G, Brooks DA, Hopwood JJ, von Figura K, Peters C: Mucopolysaccharidosis VI (Maroteaux-Lamy syndrome): six unique arylsulfatase B gene alleles causing variable disease phenotypes. Am J Hum Genet. 1994 Mar;54(3):454-63. [PubMed ]
- Voskoboeva E, Isbrandt D, von Figura K, Krasnopolskaya X, Peters C: Four novel mutant alleles of the arylsulfatase B gene in two patients with intermediate form of mucopolysaccharidosis VI (Maroteaux-Lamy syndrome). Hum Genet. 1994 Mar;93(3):259-64. [PubMed ]
- Simonaro CM, Schuchman EH: N-acetylgalactosamine-4-sulfatase: identification of four new mutations within the conserved sulfatase region causing mucopolysaccharidosis type VI. Biochim Biophys Acta. 1995 Dec 12;1272(3):129-32. [PubMed ]
- Litjens T, Brooks DA, Peters C, Gibson GJ, Hopwood JJ: Identification, expression, and biochemical characterization of N-acetylgalactosamine-4-sulfatase mutations and relationship with clinical phenotype in MPS-VI patients. Am J Hum Genet. 1996 Jun;58(6):1127-34. [PubMed ]
- Villani GR, Balzano N, Di Natale P: Two novel mutations of the arylsulfatase B gene in two Italian patients with severe form of mucopolysaccharidosis. Mutations in brief no. 127. Online. Hum Mutat. 1998;11(5):410. [PubMed ]
- Wang DG, Fan JB, Siao CJ, Berno A, Young P, Sapolsky R, Ghandour G, Perkins N, Winchester E, Spencer J, Kruglyak L, Stein L, Hsie L, Topaloglou T, Hubbell E, Robinson E, Mittmann M, Morris MS, Shen N, Kilburn D, Rioux J, Nusbaum C, Rozen S, Hudson TJ, Lipshutz R, Chee M, Lander ES: Large-scale identification, mapping, and genotyping of single-nucleotide polymorphisms in the human genome. Science. 1998 May 15;280(5366):1077-82. [PubMed ]
- Villani GR, Balzano N, Vitale D, Saviano M, Pavone V, Di Natale P: Maroteaux-lamy syndrome: five novel mutations and their structural localization. Biochim Biophys Acta. 1999 Feb 24;1453(2):185-92. [PubMed ]
- Wu JY, Yang CF, Lee CC, Chang JG, Tsai FJ: A novel mutation (Q239R) identified in a Taiwan Chinese patient with type VI mucopolysaccharidosis (Maroteaux-Lamy syndrome). Hum Mutat. 2000 Apr;15(4):389-90. [PubMed ]
- Yang CF, Wu JY, Lin SP, Tsai FJ: Mucopolysaccharidosis type VI: Report of two Taiwanese patients and identification of one novel mutation. J Formos Med Assoc. 2001 Dec;100(12):820-3. [PubMed ]
- Karageorgos L, Harmatz P, Simon J, Pollard A, Clements PR, Brooks DA, Hopwood JJ: Mutational analysis of mucopolysaccharidosis type VI patients undergoing a trial of enzyme replacement therapy. Hum Mutat. 2004 Mar;23(3):229-33. [PubMed ]
|
| Enzyme 103 Metabolite References |
Not Available |
|
Enzyme 104
[top]
|
| Enzyme 104 ID |
5558 |
| Enzyme 104 Name |
Sialidase-4 |
| Enzyme 104 Synonyms |
- N-acetyl-alpha-neuraminidase 4
|
| Enzyme 104 Gene Name |
NEU4 |
| Enzyme 104 Protein Sequence |
>Sialidase-4
MGVPRTPSRTVLFERERTGLTYRVPSLLPVPPGPTLLAFVEQRLSPDDSHAHRLVLRRGT
LAGGSVRWGALHVLGTAALAEHRSMNPCPVHDAGTGTVFLFFIAVLGHTPEAVQIATGRN
AARLCCVASRDAGLSWGSARDLTEEAIGGAVQDWATFAVGPGHGVQLPSGRLLVPAYTYR
VDRRECFGKICRTSPHSFAFYSDDHGRTWRCGGLVPNLRSGECQLAAVDGGQAGSFLYCN
ARSPLGSRVQALSTDEGTSFLPAERVASLPETAWGCQGSIVGFPAPAPNRPRDDSWSVGP
GSPLQPPLLGPGVHEPPEEAAVDPRGGQVPGGPFSRLQPRGDGPRQPGPRPGVSGDVGSW
TLALPMPFAAPPQSPTWLLYSHPVGRRARLHMGIRLSQSPLDPRSWTEPWVIYEGPSGYS
DLASIGPAPEGGLVFACLYESGARTSYDEISFCTFSLREVLENVPASPKPPNLGDKPRGC
CWPS
|
| Enzyme 104 Number of Residues |
484 |
| Enzyme 104 Molecular Weight |
51571.9 |
| Enzyme 104 Theoretical pI |
7.84 |
| Enzyme 104 GO Classification |
Not Available |
| Enzyme 104 General Function |
Involved in exo-alpha-sialidase activity |
| Enzyme 104 Specific Function |
May function in lysosomal catabolism of sialylated glycoconjugates. Has sialidase activity towards synthetic substrates, such as 2'-(4-methylumbelliferyl)-alpha-D-N- acetylneuraminic acid (4-MU-NANA or 4MU-NeuAc). Has a broad substrate specificity being active on glycoproteins, oligosaccharides and sialylated glycolipids |
| Enzyme 104 Pathways |
|
| Enzyme 104 Reactions |
- Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates ALL_REAC (other) R03491 R04018 R04634 R04650 R05115 R05117 R05996(G) R05998(G) R05999(G) R06012(G) R06147(G) R06253(G) INHIBITOR 2-Deoxy-2,3-dehydro-N-acetylneuraminic acid [CPD:C04580]
|
| Enzyme 104 Pfam Domain Function |
Not Available |
| Enzyme 104 Signals |
|
| Enzyme 104 Transmembrane Regions |
|
| Enzyme 104 Essentiality |
Not Available |
| Enzyme 104 GenBank ID Protein |
262527265 |
| Enzyme 104 UniProtKB/Swiss-Prot ID |
Q8WWR8 |
| Enzyme 104 UniProtKB/Swiss-Prot Entry Name |
NEUR4_HUMAN |
| Enzyme 104 PDB ID |
Not Available |
| Enzyme 104 Cellular Location |
Not Available |
| Enzyme 104 Gene Sequence |
>1455 bp
ATGGGGGTCCCTCGTACCCCTTCACGGACAGTGCTCTTCGAGCGGGAGAGGACGGGCCTG
ACCTACCGCGTGCCCTCGCTGCTCCCCGTGCCCCCCGGGCCCACCCTGCTGGCCTTTGTG
GAGCAGCGGCTCAGCCCTGACGACTCCCACGCCCACCGCCTGGTGCTGAGGAGGGGCACG
CTGGCCGGGGGCTCCGTGCGGTGGGGTGCCCTGCACGTGCTGGGGACAGCAGCCCTGGCG
GAGCACCGGTCCATGAACCCCTGCCCTGTGCACGATGCTGGCACGGGCACCGTCTTCCTC
TTCTTCATCGCGGTGCTGGGCCACACGCCTGAGGCCGTGCAGATCGCCACGGGAAGGAAC
GCCGCGCGCCTCTGCTGTGTGGCCAGCCGTGACGCCGGCCTCTCGTGGGGCAGCGCCCGG
GACCTCACCGAGGAGGCCATCGGTGGTGCCGTGCAGGACTGGGCCACATTCGCTGTGGGT
CCCGGCCACGGCGTGCAGCTGCCCTCAGGCCGCCTGCTGGTACCCGCCTACACCTACCGC
GTGGACCGCCGAGAGTGTTTTGGCAAGATCTGCCGGACCAGCCCTCACTCCTTCGCCTTC
TACAGCGATGACCACGGCCGCACCTGGCGCTGTGGAGGCCTCGTGCCCAACCTGCGCTCA
GGCGAGTGCCAGCTGGCGGCGGTGGACGGTGGGCAGGCCGGCAGCTTCCTCTACTGCAAT
GCCCGGAGCCCACTGGGCAGCCGTGTGCAGGCGCTCAGCACTGACGAGGGCACCTCCTTC
CTGCCCGCAGAGCGCGTGGCTTCCCTGCCCGAGACTGCCTGGGGCTGCCAGGGCAGCATC
GTGGGCTTCCCAGCCCCCGCCCCCAACAGGCCACGGGATGACAGTTGGTCAGTGGGCCCC
GGGAGTCCCCTCCAGCCTCCACTCCTCGGTCCTGGAGTCCACGAACCCCCAGAGGAGGCT
GCTGTAGACCCCCGTGGAGGCCAGGTGCCTGGTGGGCCCTTCAGCCGTCTGCAGCCTCGG
GGGGATGGCCCCAGGCAGCCTGGCCCCAGGCCTGGGGTCAGTGGGGATGTGGGGTCCTGG
ACCCTGGCACTCCCCATGCCCTTTGCTGCCCCGCCCCAGAGCCCCACGTGGCTGCTGTAC
TCCCACCCAGTGGGGCGCAGGGCTCGGCTACACATGGGTATCCGCCTGAGCCAGTCCCCG
CTGGACCCGCGCAGCTGGACAGAGCCCTGGGTGATCTACGAGGGCCCCAGCGGCTACTCC
GACCTGGCGTCCATCGGGCCGGCTCCTGAGGGGGGCCTGGTTTTTGCCTGCCTGTACGAG
AGCGGGGCCAGGACCTCCTATGATGAGATTTCCTTTTGTACATTCTCCCTGCGTGAGGTC
CTGGAGAACGTGCCCGCCAGCCCCAAGCCGCCCAACCTTGGGGACAAGCCTCGGGGGTGC
TGCTGGCCCTCCTGA
|
| Enzyme 104 GenBank Gene ID |
NM_001167600.1 |
| Enzyme 104 GeneCard ID |
NEU4 |
| Enzyme 104 GenAtlas ID |
NEU4 |
| Enzyme 104 HGNC ID |
HGNC:21328 |
| Enzyme 104 Chromosome Location |
2 |
| Enzyme 104 Locus |
2q37.3 |
| Enzyme 104 SNPs |
SNPJam Report |
| Enzyme 104 General References |
- Monti E, Bassi MT, Bresciani R, Civini S, Croci GL, Papini N, Riboni M, Zanchetti G, Ballabio A, Preti A, Tettamanti G, Venerando B, Borsani G: Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family. Genomics. 2004 Mar;83(3):445-53. [PubMed ]
- Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J: Large-scale cDNA transfection screening for genes related to cancer development and progression. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15724-9. Epub 2004 Oct 21. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Seyrantepe V, Landry K, Trudel S, Hassan JA, Morales CR, Pshezhetsky AV: Neu4, a novel human lysosomal lumen sialidase, confers normal phenotype to sialidosis and galactosialidosis cells. J Biol Chem. 2004 Aug 27;279(35):37021-9. Epub 2004 Jun 22. [PubMed ]
- Stamatos NM, Liang F, Nan X, Landry K, Cross AS, Wang LX, Pshezhetsky AV: Differential expression of endogenous sialidases of human monocytes during cellular differentiation into macrophages. FEBS J. 2005 May;272(10):2545-56. [PubMed ]
|
| Enzyme 104 Metabolite References |
Not Available |
|
Enzyme 105
[top]
|
| Enzyme 105 ID |
5560 |
| Enzyme 105 Name |
Arylsulfatase E |
| Enzyme 105 Synonyms |
- ASE
|
| Enzyme 105 Gene Name |
ARSE |
| Enzyme 105 Protein Sequence |
>Arylsulfatase E
MLHLHHSCLCFRSWLPAMLAVLLSLAPSASSDISASRPNILLLMADDLGIGDIGCYGNNT
MRTPNIDRLAEDGVKLTQHISAASLCTPSRAAFLTGRYPVRSGMVSSIGYRVLQWTGASG
GLPTNETTFAKILKEKGYATGLIGKWHLGLNCESASDHCHHPLHHGFDHFYGMPFSLMGD
CARWELSEKRVNLEQKLNFLFQVLALVALTLVAGKLTHLIPVSWMPVIWSALSAVLLLAS
SYFVGALIVHADCFLMRNHTITEQPMCFQRTTPLILQEVASFLKRNKHGPFLLFVSFLHV
HIPLITMENFLGKSLHGLYGDNVEEMDWMVGRILDTLDVEGLSNSTLIYFTSDHGGSLEN
QLGNTQYGGWNGIYKGGKGMGGWEGGIRVPGIFRWPGVLPAGRVIGEPTSLMDVFPTVVR
LAGGEVPQDRVIDGQDLLPLLLGTAQHSDHEFLMHYCERFLHAARWHQRDRGTMWKVHFV
TPVFQPEGAGACYGRKVCPCFGEKVVHHDPPLLFDLSRDPSETHILTPASEPVFYQVMER
VQQAVWEHQRTLSPVPLQLDRLGNIWRPWLQPCCGPFPLCWCLREDDPQ
|
| Enzyme 105 Number of Residues |
589 |
| Enzyme 105 Molecular Weight |
65668.4 |
| Enzyme 105 Theoretical pI |
6.96 |
| Enzyme 105 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- sulfuric ester hydrolase activity
|
| Process |
|
| Component |
| — |
|
| Enzyme 105 General Function |
Involved in catalytic activity |
| Enzyme 105 Specific Function |
May be essential for the correct composition of cartilage and bone matrix during development. Has no activity toward steroid sulfates |
| Enzyme 105 Pathways |
Not Available |
| Enzyme 105 Reactions |
Not Available |
| Enzyme 105 Pfam Domain Function |
|
| Enzyme 105 Signals |
|
| Enzyme 105 Transmembrane Regions |
|
| Enzyme 105 Essentiality |
Not Available |
| Enzyme 105 GenBank ID Protein |
62897927 |
| Enzyme 105 UniProtKB/Swiss-Prot ID |
P51690 |
| Enzyme 105 UniProtKB/Swiss-Prot Entry Name |
ARSE_HUMAN |
| Enzyme 105 PDB ID |
Not Available |
| Enzyme 105 Cellular Location |
Not Available |
| Enzyme 105 Gene Sequence |
>1770 bp
ATGTTACATCTGCACCATTCTTGTTTGTGTTTCAGGAGCTGGCTGCCAGCGATGCTCGCT
GTACTGCTAAGTTTGGCACCATCAGCTTCCAGCGACATTTCCGCCTCCCGACCGAACATC
CTTCTTCTGATGGCGGACGACCTTGGCATTGGGGACATTGGCTGCTATGGCAACAACACC
ATGAGGACTCCGAATATTGACCGCCTTGCAGAGGACGGCGTGAAGCTGACCCAACACATC
TCTGCCGCATCTTTGTGCACCCCAAGCAGAGCCGCCTTCCTCACGGGCAGATACCCTGTG
CGATCAGGGATGGTTTCCAGCATTGGTTACCGTGTTCTTCAGTGGACCGGAGCATCTGGA
GGTCTTCCAACAAATGAGACAACTTTTGCAAAAATACTGAAAGAGAAAGGCTATGCCACT
GGACTCATTGGAAAATGGCATCTGGGTCTCAACTGTGAGTCAGCCAGTGATCATTGCCAC
CACCCTCTCCATCACGGCTTTGACCATTTCTACGGAATGCCTTTCTCCTTGATGGGTGAT
TGCGCCCGCTGGGAACTCTCAGAGAAGCGTGTCAACCTGGAACAAAAACTCAACTTCCTC
TTCCAAGTCCTGGCCTTGGTTGCCCTCACACTGGTAGCAGGGAAGCTCACACACCTGATA
CCCGTCTCGTGGATGCCGGTCATCTGGTCAGCCCTTTCGGCCGTCCTCCTCCTCGCAAGC
TCCTATTTTGTGGGTGCTCTGATTGTCCATGCCGATTGCTTTCTGATGAGAAACCACACC
ATCACGGAGCAGCCCATGTGCTTCCAAAGAACGACACCCCTTATTCTGCAGGAGGTTGCG
TCCTTTCTCAAAAGGAATAAGCATGGGCCTTTCCTCCTCTTTGTTTCCTTTCTACACGTT
CACATCCCTCTTATCACTATGGAGAACTTCCTCGGGAAGAGTCTCCACGGGCTGTATGGG
GACAACGTAGAGGAGATGGACTGGATGGTAGGACGGATCCTTGACACTTTGGACGTGGAG
GGTTTGAGCAACAGCACCCTCATTTATTTTACGTCGGATCACGGCGGTTCCCTAGAGAAT
CAACTTGGAAACACCCAGTATGGTGGCTGGAATGGAATTTATAAAGGTGGGAAGGGCATG
GGAGGATGGGAAGGTGGGATCCGCGTGCCCGGGATCTTCCGCTGGCCCGGGGTGCTCCCG
GCCGGCCGAGTGATTGGCGAGCCCACGAGTCTGATGGACGTGTTCCCCACCGTGGTCCGG
CTGGCGGGCAGCGAGGTGCCCCAGGACAGAGTGATTGACGGCCAAGACCTTCTGCCCTTG
CTCCTGGGGACAGCCCAACACTCAGACCACGAGTTCCTGATGCATTATTGTGAGAGGTTT
CTGCACGCAGCCAGGTGGCATCAACGGGACAGAGGAACAATGTGGAAAGTCCACTTTGTG
ACGCCTGTGTTCCAGCCAGAGGGAGCCGGTGCCTGCTATGGAAGAAAGGTCTGCCCGTGC
TTTGGGGAAAAAGTAGTCCACCACGATCCACCTTTGCTCTTTGACCTCTCAAGAGACCCT
TCTGAGACCCACATCCTCACACCAGCCTCAGAGCCCGTGTTCTATCAGGTGATGGAACGA
GTCCAGCAGGCGGTGTGGGAACACCAGCGGACACTCAGCCCAGTTCCTCTGCAGCTGGAC
AGGCTGGGCAATATCTGGAGACCGTGGCTGCAGCCCTGCTGTGGCCCGTTCCCCCTCTGC
TGGTGCCTTAGGGAAGATGACCCACAATAA
|
| Enzyme 105 GenBank Gene ID |
AK223183 |
| Enzyme 105 GeneCard ID |
ARSE |
| Enzyme 105 GenAtlas ID |
ARSE |
| Enzyme 105 HGNC ID |
HGNC:719 |
| Enzyme 105 Chromosome Location |
Not Available |
| Enzyme 105 Locus |
Not Available |
| Enzyme 105 SNPs |
SNPJam Report |
| Enzyme 105 General References |
- Franco B, Meroni G, Parenti G, Levilliers J, Bernard L, Gebbia M, Cox L, Maroteaux P, Sheffield L, Rappold GA, et al.: A cluster of sulfatase genes on Xp22.3: mutations in chondrodysplasia punctata (CDPX) and implications for warfarin embryopathy. Cell. 1995 Apr 7;81(1):15-25. [PubMed ]
- Daniele A, Parenti G, d'Addio M, Andria G, Ballabio A, Meroni G: Biochemical characterization of arylsulfatase E and functional analysis of mutations found in patients with X-linked chondrodysplasia punctata. Am J Hum Genet. 1998 Mar;62(3):562-72. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
- Parenti G, Buttitta P, Meroni G, Franco B, Bernard L, Rizzolo MG, Brunetti-Pierri N, Ballabio A, Andria G: X-linked recessive chondrodysplasia punctata due to a new point mutation of the ARSE gene. Am J Med Genet. 1997 Dec 12;73(2):139-43. [PubMed ]
- Brunetti-Pierri N, Andreucci MV, Tuzzi R, Vega GR, Gray G, McKeown C, Ballabio A, Andria G, Meroni G, Parenti G: X-linked recessive chondrodysplasia punctata: spectrum of arylsulfatase E gene mutations and expanded clinical variability. Am J Med Genet A. 2003 Mar 1;117A(2):164-8. [PubMed ]
|
| Enzyme 105 Metabolite References |
Not Available |
|
Enzyme 106
[top]
|
| Enzyme 106 ID |
5562 |
| Enzyme 106 Name |
Annexin A3 |
| Enzyme 106 Synonyms |
- 35-alpha calcimedin
- Annexin III
- Annexin-3
- Inositol 1,2-cyclic phosphate 2-phosphohydrolase
- Lipocortin III
- Placental anticoagulant protein III
- PAP-III
|
| Enzyme 106 Gene Name |
ANXA3 |
| Enzyme 106 Protein Sequence |
>Annexin A3
MASIWVGHRGTVRDYPDFSPSVDAEAIQKAIRGIGTDEKMLISILTERSNAQRQLIVKEY
QAAYGKELKDDLKGDLSGHFEHLMVALVTPPAVFDAKQLKKSMKGAGTNEDALIEILTTR
TSRQMKDISQAYYTVYKKSLGDDISSETSGDFRKALLTLADGRRDESLKVDEHLAKQDAQ
ILYKAGENRWGTDEDKFTEILCLRSFPQLKLTFDEYRNISQKDIVDSIKGELSGHFEDLL
LAIVNCVRNTPAFLAERLHRALKGIGTDEFTLNRIMVSRSEIDLLDIRTEFKKHYGYSLY
SAIKSDTSGDYEITLLKICGGDD
|
| Enzyme 106 Number of Residues |
323 |
| Enzyme 106 Molecular Weight |
36374.8 |
| Enzyme 106 Theoretical pI |
5.71 |
| Enzyme 106 GO Classification |
| Function |
- binding
- calcium ion binding
- calcium-dependent phospholipid binding
- cation binding
- enzyme inhibitor activity
- enzyme regulator activity
- ion binding
- lipase inhibitor activity
- lipid binding
- metal ion binding
- phospholipase inhibitor activity
- phospholipid binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 106 General Function |
Involved in calcium ion binding |
| Enzyme 106 Specific Function |
Inhibitor of phospholipase A2, also possesses anti- coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate |
| Enzyme 106 Pathways |
Not Available |
| Enzyme 106 Reactions |
Not Available |
| Enzyme 106 Pfam Domain Function |
|
| Enzyme 106 Signals |
|
| Enzyme 106 Transmembrane Regions |
|
| Enzyme 106 Essentiality |
Not Available |
| Enzyme 106 GenBank ID Protein |
Not Available |
| Enzyme 106 UniProtKB/Swiss-Prot ID |
P12429 |
| Enzyme 106 UniProtKB/Swiss-Prot Entry Name |
ANXA3_HUMAN |
| Enzyme 106 PDB ID |
1AII |
| Enzyme 106 PDB File |
Show |
| Enzyme 106 3D Structure |
|
| Enzyme 106 Cellular Location |
Not Available |
| Enzyme 106 Gene Sequence |
>972 bp
ATGGCATCTATCTGGGTTGGACACCGAGGAACAGTAAGAGATTATCCAGACTTTAGCCCA
TCAGTGGATGCTGAAGCTATTCAGAAAGCAATCAGAGGAATTGGAACTGATGAGAAAATG
CTCATCAGCATTCTGACTGAGAGGTCAAATGCACAGCGGCAGCTGATTGTTAAGGAATAT
CAAGCAGCATATGGAAAGGAGCTGAAAGATGACTTGAAGGGTGATCTCTCTGGCCACTTT
GAGCATCTCATGGTGGCCCTAGTGACTCCACCAGCAGTCTTTGATGCAAAGCAGCTAAAG
AAATCCATGAAGGGCGCGGGAACAAACGAAGATGCCTTGATTGAAATCTTAACTACCAGG
ACAAGCAGGCAAATGAAGGATATCTCTCAAGCCTATTATACAGTATACAAGAAGAGTCTT
GGAGATGACATTAGTTCCGAAACATCTGGTGACTTCCGGAAAGCTCTGTTGACTTTGGCA
GATGGCAGAAGAGATGAAAGTCTGAAAGTGGATGAGCATCTGGCCAAACAAGATGCCCAG
ATTCTCTATAAAGCTGGTGAGAACAGATGGGGCACGGATGAAGACAAATTCACTGAGATC
CTGTGTTTAAGGAGCTTTCCTCAATTAAAACTAACATTTGATGAATACAGAAATATCAGC
CAAAAGGACATTGTGGACAGCATAAAAGGAGAATTATCTGGGCATTTTGAAGACTTACTG
TTGGCCATAGTTAATTGTGTGAGGAACACGCCGGCCTTTTTAGCCGAAAGACTGCATCGA
GCCTTGAAGGGTATTGGAACTGATGAGTTTACTCTGAACCGAATAATGGTGTCCAGATCA
GAAATTGACCTTTTGGACATTCGAACAGAGTTCAAGAAGCATTATGGCTATTCCCTATAT
TCAGCAATTAAATCGGATACTTCTGGAGACTATGAAATCACACTCTTAAAAATCTGTGGT
GGAGATGACTGA
|
| Enzyme 106 GenBank Gene ID |
M20560 |
| Enzyme 106 GeneCard ID |
ANXA3 |
| Enzyme 106 GenAtlas ID |
ANXA3 |
| Enzyme 106 HGNC ID |
HGNC:541 |
| Enzyme 106 Chromosome Location |
4 |
| Enzyme 106 Locus |
4q21.21 |
| Enzyme 106 SNPs |
SNPJam Report |
| Enzyme 106 General References |
- Pepinsky RB, Tizard R, Mattaliano RJ, Sinclair LK, Miller GT, Browning JL, Chow EP, Burne C, Huang KS, Pratt D, et al.: Five distinct calcium and phospholipid binding proteins share homology with lipocortin I. J Biol Chem. 1988 Aug 5;263(22):10799-811. [PubMed ]
- Tait JF, Frankenberry DA, Miao CH, Killary AM, Adler DA, Disteche CM: Chromosomal localization of the human annexin III (ANX3) gene. Genomics. 1991 Jun;10(2):441-8. [PubMed ]
- Tait JF, Smith C, Xu L, Cookson BT: Structure and polymorphisms of the human annexin III (ANX3) gene. Genomics. 1993 Oct;18(1):79-86. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed ]
- Ross TS, Tait JF, Majerus PW: Identity of inositol 1,2-cyclic phosphate 2-phosphohydrolase with lipocortin III. Science. 1990 May 4;248(4955):605-7. [PubMed ]
- Tait JF, Sakata M, McMullen BA, Miao CH, Funakoshi T, Hendrickson LE, Fujikawa K: Placental anticoagulant proteins: isolation and comparative characterization four members of the lipocortin family. Biochemistry. 1988 Aug 23;27(17):6268-76. [PubMed ]
- Ernst JD, Hoye E, Blackwood RA, Jaye D: Purification and characterization of an abundant cytosolic protein from human neutrophils that promotes Ca2(+)-dependent aggregation of isolated specific granules. J Clin Invest. 1990 Apr;85(4):1065-71. [PubMed ]
- Favier-Perron B, Lewit-Bentley A, Russo-Marie F: The high-resolution crystal structure of human annexin III shows subtle differences with annexin V. Biochemistry. 1996 Feb 13;35(6):1740-4. [PubMed ]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed ]
|
| Enzyme 106 Metabolite References |
Not Available |
|
Enzyme 107
[top]
|
| Enzyme 107 ID |
5563 |
| Enzyme 107 Name |
6-phosphogluconolactonase |
| Enzyme 107 Synonyms |
- 6PGL
|
| Enzyme 107 Gene Name |
PGLS |
| Enzyme 107 Protein Sequence |
>6-phosphogluconolactonase
MAAPAPGLISVFSSSQELGAALAQLVAQRAACCLAGARARFALGLSGGSLVSMLARELPA
AVAPAGPASLARWTLGFCDERLVPFDHAESTYGLYRTHLLSRLPIPESQVITINPELPVE
EAAEDYAKKLRQAFQGDSIPVFDLLILGVGPDGHTCSLFPDHPLLQEREKIVAPISDSPK
PPPQRVTLTLPVLNAARTVIFVATGEGKAAVLKRILEDQEENPLPAALVQPHTGKLCWFL
DEAAARLLTVPFEKHSTL
|
| Enzyme 107 Number of Residues |
258 |
| Enzyme 107 Molecular Weight |
27546.5 |
| Enzyme 107 Theoretical pI |
5.95 |
| Enzyme 107 GO Classification |
| Function |
- 6-phosphogluconolactonase activity
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- pentose-phosphate shunt
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 107 General Function |
Involved in 6-phosphogluconolactonase activity |
| Enzyme 107 Specific Function |
Hydrolysis of 6-phosphogluconolactone to 6- phosphogluconate |
| Enzyme 107 Pathways |
|
| Enzyme 107 Reactions |
- 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate [RN:R02035]
|
| Enzyme 107 Pfam Domain Function |
Not Available |
| Enzyme 107 Signals |
|
| Enzyme 107 Transmembrane Regions |
|
| Enzyme 107 Essentiality |
Not Available |
| Enzyme 107 GenBank ID Protein |
6912586 |
| Enzyme 107 UniProtKB/Swiss-Prot ID |
O95336 |
| Enzyme 107 UniProtKB/Swiss-Prot Entry Name |
6PGL_HUMAN |
| Enzyme 107 PDB ID |
Not Available |
| Enzyme 107 Cellular Location |
Not Available |
| Enzyme 107 Gene Sequence |
>777 bp
ATGGCCGCGCCGGCCCCGGGCCTCATCTCGGTGTTCTCGAGTTCCCAGGAGCTGGGTGCG
GCGCTAGCGCAGCTGGTGGCCCAGCGCGCAGCATGCTGCCTGGCAGGGGCCCGCGCCCGT
TTCGCGCTCGGCCTGTCGGGCGGGAGCCTCGTCTCGATGCTAGCCCGCGAGCTACCCGCC
GCCGTCGCCCCTGCCGGGCCAGCTAGCTTAGCGCGCTGGACGCTGGGCTTCTGCGACGAG
CGCCTCGTGCCCTTCGATCACGCCGAGAGCACGTACGGCCTCTACCGGACGCATCTTCTC
TCCAGACTGCCGATCCCAGAAAGCCAGGTGATCACCATTAACCCCGAGCTGCCTGTGGAG
GAGGCGGCTGAGGACTACGCCAAGAAGCTGAGACAGGCATTCCAAGGGGACTCCATCCCG
GTTTTCGACCTGCTGATCCTGGGGGTGGGCCCCGATGGTCACACCTGCTCACTCTTCCCA
GACCACCCCCTCCTACAGGAGCGGGAGAAGATTGTGGCTCCCATCAGTGACTCCCCGAAG
CCACCGCCACAGCGTGTGACCCTCACACTACCTGTCCTGAATGCAGCACGAACTGTCATC
TTTGTGGCAACTGGAGAAGGCAAGGCAGCTGTTCTGAAGCGCATTTTGGAGGACCAGGAG
GAAAACCCGCTGCCCGCCGCCCTGGTCCAGCCCCACACCGGGAAACTGTGCTGGTTCTTG
GACGAGGCGGCCGCCCGCCTCCTGACCGTGCCCTTCGAGAAGCATTCCACTTTGTAG
|
| Enzyme 107 GenBank Gene ID |
NM_012088.2 |
| Enzyme 107 GeneCard ID |
PGLS |
| Enzyme 107 GenAtlas ID |
PGLS |
| Enzyme 107 HGNC ID |
HGNC:8903 |
| Enzyme 107 Chromosome Location |
1 |
| Enzyme 107 Locus |
19p13.2 |
| Enzyme 107 SNPs |
SNPJam Report |
| Enzyme 107 General References |
- Collard F, Collet JF, Gerin I, Veiga-da-Cunha M, Van Schaftingen E: Identification of the cDNA encoding human 6-phosphogluconolactonase, the enzyme catalyzing the second step of the pentose phosphate pathway(1). FEBS Lett. 1999 Oct 8;459(2):223-6. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
|
| Enzyme 107 Metabolite References |
Not Available |
|
Enzyme 108
[top]
|
| Enzyme 108 ID |
5565 |
| Enzyme 108 Name |
GDH/6PGL endoplasmic bifunctional protein |
| Enzyme 108 Synonyms |
- Glucose 1-dehydrogenase
- Hexose-6-phosphate dehydrogenase
- 6-phosphogluconolactonase
- 6PGL
|
| Enzyme 108 Gene Name |
H6PD |
| Enzyme 108 Protein Sequence |
>GDH/6PGL endoplasmic bifunctional protein
MWNMLIVAMCLALLGCLQAQELQGHVSIILLGATGDLAKKYLWQGLFQLYLDEAGRGHSF
SFHGAALTAPKQGQELMAKALESLSCPKDMAPSHCAEHKDQFLQLSQYRQLKTAEDYQAL
NKDIEAQLQHAGLREAGRIFYFSVPPFAYEDIARNINSSCRPGPGAWLRVVLEKPFGHDH
FSAQQLATELGTFFQEEEMYRVDHYLGKQAVAQILPFRDQNRKALDGLWNRHHVERVEII
MKETVDAEGRTSFYEEYGVIRDVLQNHLTEVLTLVAMELPHNVSSAEAVLRHKLQVFQAL
RGLQRGSAVVGQYQSYSEQVRRELQKPDSFHSLTPTFAAVLVHIDNLRWEGVPFILMSGK
ALDERVGYARILFKNQACCVQSEKHWAAAQSQCLPRQLVFHIGHGDLGSPAVLVSRNLFR
PSLPSSWKEMEGPPGLRLFGSPLSDYYAYSPVRERDAHSVLLSHIFHGRKNFFITTENLL
ASWNFWTPLLESLAHKAPRLYPGGAENGRLLDFEFSSGRLFFSQQQPEQLVPGPGPAPMP
SDFQVLRAKYRESPLVSAWSEELISKLANDIEATAVRAVRRFGQFHLALSGGSSPVALFQ
QLATAHYGFPWAHTHLWLVDERCVPLSDPESNFQGLQAHLLQHVRIPYYNIHPMPVHLQQ
RLCAEEDQGAQIYAREISALVANSSFDLVLLGMGADGHTASLFPQSPTGLDGEQLVVLTT
SPSQPHRRMSLSLPLINRAKKVAVLVMGRMKREITTLVSRVGHEPKKWPISGVLPHSGQL
VWYMDYDAFLG
|
| Enzyme 108 Number of Residues |
791 |
| Enzyme 108 Molecular Weight |
88892.0 |
| Enzyme 108 Theoretical pI |
7.31 |
| Enzyme 108 GO Classification |
| Function |
- 6-phosphogluconolactonase activity
- NADP or NADPH binding
- binding
- carboxylesterase activity
- catalytic activity
- glucose-6-phosphate dehydrogenase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- nucleotide binding
- oxidoreductase activity
- oxidoreductase activity, acting on CH-OH group of donors
- oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose catabolic process
- glucose metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- oxidation reduction
- pentose-phosphate shunt
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 108 General Function |
Involved in 6-phosphogluconolactonase activity |
| Enzyme 108 Specific Function |
Oxidizes glucose-6-phosphate and glucose, as well as other hexose-6-phosphates |
| Enzyme 108 Pathways |
|
| Enzyme 108 Reactions |
- 6-phospho-D-glucono-1,5-lactone + H2O = 6-phospho-D-gluconate [RN:R02035]
|
| Enzyme 108 Pfam Domain Function |
|
| Enzyme 108 Signals |
|
| Enzyme 108 Transmembrane Regions |
|
| Enzyme 108 Essentiality |
Not Available |
| Enzyme 108 GenBank ID Protein |
4186038 |
| Enzyme 108 UniProtKB/Swiss-Prot ID |
O95479 |
| Enzyme 108 UniProtKB/Swiss-Prot Entry Name |
G6PE_HUMAN |
| Enzyme 108 PDB ID |
Not Available |
| Enzyme 108 Cellular Location |
Not Available |
| Enzyme 108 Gene Sequence |
>2376 bp
ATGTGGAATATGCTCATAGTGGCGATGTGCTTGGCCCTTCTGGGCTGCCTGCAAGCCCAG
GAGCTCCAGGGACATGTCTCCATAATCCTGCTGGGAGCAACTGGGGACCTGGCTAAGAAG
TACTTATGGCAGGGACTGTTCCAGCTGTACCTGGATGAAGCGGGGAGGGGTCACAGTTTT
AGCTTCCATGGAGCTGCTCTGACAGCCCCCAAGCAGGGTCAAGAGCTCATGGCCAAGGCC
CTGGAATCCCTCTCCTGCCCCAAGGACATGGCACCCAGTCACTGTGCAGAGCACAAGGAT
CAGTTCCTGCAGCTGAGCCAGTACCGCCAACTGAAGACGGCCGAGGACTATCAGGCCCTG
AACAAGGACATCGAGGCACAGCTCCAGCACGCAGGCCTCCGGGAGGCTGGCAGGATCTTC
TACTTCTCAGTGCCACCCTTCGCCTATGAAGACATTGCCCGCAACATCAACAGTAGCTGC
CGGCCAGGCCCGGGCGCCTGGCTGCGGGTTGTCCTTGAGAAACCCTTTGGCCATGACCAC
TTCTCAGCCCAGCAGCTGGCCACAGAACTCGGGACCTTTTTCCAGGAGGAGGAGATGTAC
CGGGTGGACCATTACTTAGGCAAGCAGGCTGTGGCGCAGATCCTGCCTTTCCGAGACCAG
AACCGCAAGGCTTTGGACGGCCTCTGGAACCGGCACCATGTGGAGCGGGTGGAGATCATC
ATGAAAGAGACCGTGGATGCTGAAGGCCGCACCAGCTTCTATGAGGAGTACGGTGTCATT
CGCGACGTCCTCCAGAACCATCTGACGGAGGTCCTCACCCTCGTGGCCATGGAGCTGCCC
CACAATGTCAGCAGTGCGGAGGCTGTGCTGCGGCACAAGCTTCAGGTCTTCCAGGCGCTG
CGGGGCCTGCAGAGGGGCAGTGCCGTCGTGGGCCAGTACCAGTCTTACAGTGAGCAGGTG
CGCAGAGAGCTGCAGAAGCCAGACAGCTTCCACAGCCTGACGCCGACCTTCGCAGGTGTC
CTAGTGCACATTGACAACCTTCGCTGGGAGGGCGTGCCTTTCATCCTGATGTCTGGCAAA
GCCTTGGACGAGAGAGTGGGCTACGCTCGGATCTTGTTCAAGAACCAGGCCTGCTGTGTG
CAGAGCGAAAAGCACTGGGCCGCGGCGCAGAGCCAGTGCCTGCCCCGGCAGCTCGTCTTC
CACATCGGCCATGGCGACCTGGGCAGCCCTGCCGTGCTGGTCAGCAGGAACCTGTTCAGG
CCCTCCCTGCCCTCCAGCTGGAAGGAAATGGAGGGACCACCTGGGCTCCGCCTTTTCGGC
AGCCCTCTGTCCGATTACTACGCCTACAGCCCTGTGCGGGAGCGGGACGCCCACTCCGTC
CTCTTATCCCATATCTTCCATGGCCGGAAGAATTTCTTCATCACCACAGAGAACTTGCTG
GCCTCCTGGAACTTCTGGACCCCTCTGCTGGAGAGCCTGGCCCATAAGGCCCCACGCCTC
TACCCTGGAGGAGCTGAGAATGGCCGTCTGTTGGACTTTGAGTTCAGTAGCGGCCGGTTG
TTCTTTTCCCAGCAGCAGCCGGAGCAGCTGGTGCCAGGGCCAGGGCCGGCCCCAATGCCC
AGTGACTTCCAGGTCCTCAGGGCCAAGTACCGAGAGAGCCCGCTGGTCTCCGCCTGGTCC
GAGGAGCTGATCTCTAAGCTGGCTAATGACATCGAGGCCACCGCTGTGCGAGCCGTGCGG
CGCTTTGGCCAGTTCCACCTGGCACTGTCGGGGGGCTCGAGCCCCGTGGCCCTGTTCCAG
CAGCTGGCCACGGCGCACTATGGCTTCCCCTGGGCCCACACGCACCTGTGGCTGGTTGAC
GAGCGCTGCGTCCCACTCTCAGACCCGGAGTCCAACTTCCAGGGCCTGCAGGCCCACCTG
CTGCAGCACGTCCGGATCCCCTACTACAACATCCACCCCATGCCTGTGCACCTGCAGCAG
CGGCTCTGCGCCGAGGAGGACCAGGGCGCCCAGATCTATGCCAGGGAGATCTCAGCCCTG
GTGGCCAACAGCAGCTTCGACCTGGTGCTGCTGGGCATGGGTGCCGACGGGCACACAGCC
TCCCTCTTCCCACAGTCACCCACTGGCCTGGATGGCGAGCAGCTGGTCGTGCTGACCACG
AGCCCCTCCCAGCCACACCGCCGCATGAGCCTTAGCCTGCCTCTCATCAACCGCGCCAAG
AAGGTGGCAGTCCTGGTCATGGGCAGGATGAAGCGTGAGATCACCACGCTGGTGAGCCGG
GTGGGCCATGAGCCCAAGAAGTGGCCCATCTCGGGTGTCCTGCCGCACTCCGGCCAGCTG
GTGTGGTACATGGACTACGACGCCTTCCTGGGATGA
|
| Enzyme 108 GenBank Gene ID |
AJ012590 |
| Enzyme 108 GeneCard ID |
H6PD |
| Enzyme 108 GenAtlas ID |
H6PD |
| Enzyme 108 HGNC ID |
HGNC:4795 |
| Enzyme 108 Chromosome Location |
1 |
| Enzyme 108 Locus |
1p36 |
| Enzyme 108 SNPs |
SNPJam Report |
| Enzyme 108 General References |
- Mason PJ, Stevens D, Diez A, Knight SW, Scopes DA, Vulliamy TJ: Human hexose-6-phosphate dehydrogenase (glucose 1-dehydrogenase) encoded at 1p36: coding sequence and expression. Blood Cells Mol Dis. 1999 Feb;25(1):30-7. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed ]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed ]
- Draper N, Walker EA, Bujalska IJ, Tomlinson JW, Chalder SM, Arlt W, Lavery GG, Bedendo O, Ray DW, Laing I, Malunowicz E, White PC, Hewison M, Mason PJ, Connell JM, Shackleton CH, Stewart PM: Mutations in the genes encoding 11beta-hydroxysteroid dehydrogenase type 1 and hexose-6-phosphate dehydrogenase interact to cause cortisone reductase deficiency. Nat Genet. 2003 Aug;34(4):434-9. [PubMed ]
|
| Enzyme 108 Metabolite References |
Not Available |
|
Enzyme 109
[top]
|
| Enzyme 109 ID |
5566 |
| Enzyme 109 Name |
Trifunctional purine biosynthetic protein adenosine-3 |
| Enzyme 109 Synonyms |
- Phosphoribosylamine--glycine ligase
- Glycinamide ribonucleotide synthetase
- GARS
- Phosphoribosylglycinamide synthetase
- Phosphoribosylformylglycinamidine cyclo-ligase
- AIR synthase
- AIRS
- Phosphoribosyl-aminoimidazole synthetase
- Phosphoribosylglycinamide formyltransferase
- 5'-phosphoribosylglycinamide transformylase
- GAR transformylase
- GART
|
| Enzyme 109 Gene Name |
GART |
| Enzyme 109 Protein Sequence |
>Trifunctional purine biosynthetic protein adenosine-3
MAARVLIIGSGGREHTLAWKLAQSHHVKQVLVAPGNAGTACSEKISNTAISISDHTALAQ
FCKEKKIEFVVVGPEAPLAAGIVGNLRSAGVQCFGPTAEAAQLESSKRFAKEFMDRHGIP
TAQWKAFTKPEEACSFILSADFPALVVKASGLAAGKGVIVAKSKEEACKAVQEIMQEKAF
GAAGETIVIEELLDGEEVSCLCFTDGKTVAPMPPAQDHKRLLEGDGGPNTGGMGAYCPAP
QVSNDLLLKIKDTVLQRTVDGMQQEGTPYTGILYAGIMLTKNGPKVLEFNCRFGDPECQV
ILPLLKSDLYEVIQSTLDGLLCTSLPVWLENHTALTVVMASKGYPGDYTKGVEITGFPEA
QALGLEVFHAGTALKNGKVVTHGGRVLAVTAIRENLISALEEAKKGLAAIKFEGAIYRKD
VGFRAIAFLQQPRSLTYKESGVDIAAGNMLVKKIQPLAKATSRSGCKVDLGGFAGLFDLK
AAGFKDPLLASGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFSC
GKLDLSVTEAVVAGIAKACGKAGCALLGGETAEMPDMYPPGEYDLAGFAVGAMERDQKLP
HLERITEGDVVVGIASSGLHSNGFSLVRKIVAKSSLQYSSPAPDGCGDQTLGDLLLTPTR
IYSHSLLPVLRSGHVKAFAHITGGGLLENIPRVLPEKLGVDLDAQTWRIPRVFSWLQQEG
HLSEEEMARTFNCGVGAVLVVSKEQTEQILRDIQQHKEEAWVIGSVVARAEGSPRVKVKN
LIESMQINGSVLKNGSLTNHFSFEKKKARVAVLISGTGSNLQALIDSTREPNSSAQIDIV
ISNKAAVAGLDKAERAGIPTRVINHKLYKNRVEFDSAIDLVLEEFSIDIVCLAGFMRILS
GPFVQKWNGKMLNIHPSLLPSFKGSNAHEQALETGVTVTGCTVHFVAEDVDAGQIILQEA
VPVKRGDTVATLSERVKLAEHKIFPAALQLVASGTVQLGENGKICWVKEE
|
| Enzyme 109 Number of Residues |
1010 |
| Enzyme 109 Molecular Weight |
107766.3 |
| Enzyme 109 Theoretical pI |
6.68 |
| Enzyme 109 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cyclo-ligase activity
- glycine hydroxymethyltransferase activity
- hydroxymethyl-, formyl- and related transferase activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- methyltransferase activity
- nucleoside binding
- phosphoribosylamine-glycine ligase activity
- phosphoribosylformylglycinamidine cyclo-ligase activity
- phosphoribosylglycinamide formyltransferase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- 'de novo' IMP biosynthetic process
- IMP biosynthetic process
- biosynthetic process
- cellular aromatic compound metabolic process
- cellular metabolic process
- cellular nitrogen compound metabolic process
- metabolic process
- nitrogen compound metabolic process
- nucleobase metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- purine base biosynthetic process
- purine base metabolic process
- purine nucleoside monophosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside monophosphate biosynthetic process
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 109 General Function |
Involved in catalytic activity |
| Enzyme 109 Specific Function |
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide |
| Enzyme 109 Pathways |
|
| Enzyme 109 Reactions |
- ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N1-(5-phospho-D-ribosyl)glycinamide [RN:R04144]
|
| Enzyme 109 Pfam Domain Function |
|
| Enzyme 109 Signals |
|
| Enzyme 109 Transmembrane Regions |
|
| Enzyme 109 Essentiality |
Not Available |
| Enzyme 109 GenBank ID Protein |
31642 |
| Enzyme 109 UniProtKB/Swiss-Prot ID |
P22102 |
| Enzyme 109 UniProtKB/Swiss-Prot Entry Name |
PUR2_HUMAN |
| Enzyme 109 PDB ID |
Not Available |
| Enzyme 109 Cellular Location |
Not Available |
| Enzyme 109 Gene Sequence |
>3033 bp
ATGGCAGCCCGAGTACTTATAATTGGCAGTGGAGGAAGGGAACATACGCTGGCCTGGAAA
CTTGCACAGTCTCATCATGTCAAACAAGTGTTGGTTGCCCCAGGAAACGCAGGCACTGCC
TGCTCTGAAAAGATTTCAAATACCGCCATCTCAATCAGTGACCACACTGCCCTTGCTCAA
TTCTGCAAAGAGAAGAAAATTGAATTTGTAGTTGTTGGACCAGAAGCACCTCTGGCTGCT
GGGATTGTTGGGAACCTGAGGTCTGCAGGAGTGCAATGCTTTGGCCCAACAGCAGAAGCG
GCTCAGTTAGAGTCCAGCAAAAGGTTTGCCAAAGAGTTTATGGACAGACATGGAATCCCA
ACCGCACAATGGAAGGCTTTCACCAAACCTGAAGAAGCCTGCAGCTTCATTTTGAGTGCA
GACTTCCCTGCTTTGGTTGTGAAGGCCAGTGGTCTTGCAGCTGGAAAAGGGGTGATTGTT
GCAAAGAGCAAAGAAGAGGCCTGCAAAGCTGTACAAGAGATCATGCAGGAGAAAGCCTTT
GGGGCAGCTGGAGAAACAATTGTCATTGAAGAACTTCTTGACGGAGAAGAGGTGTCGTGT
CTGTGTTTCACTGATGGCAAGACTGTGGCCCCCATGCCCCCAGCACAGGACCATAAGCGA
TTACTGGAGGGAGATGGTGGCCCTAACACAGGGGGAATGGGAGCCTATTGTCCAGCCCCT
CAGGTTTCTAATGATCTATTACTAAAAATTAAAGATACTGTTCTTCAGAGGACAGTGGAT
GGCATGCAGCAAGAGGGTACTCCATATACAGGTATTCTCTATGCTGGAATAATGCTGACC
AAGAATGGCCCAAAAGTTCTAGAGTTTAATTGCCGTTTTGGTGATCCAGAGTGCCAAGTA
ATCCTCCCACTTCTTAAAAGTGATCTTTATGAAGTGATTCAGTCCACCTTAGATGGACTG
CTCTGCACATCTCTGCCTGTTTGGCTAGAAAACCACACCGCCCTAACTGTTGTCATGGCA
AGTAAAGGTTATCCTGGAGACTACACCAAGGGTGTAGAGATAACAGGGTTTCCTGAGGCT
CAAGCTCTAGGACTGGAGGTGTTCCATGCAGGCACTGCCCTCAAAAATGGCAAAGTAGTA
ACTCATGGGGGTAGAGTTCTTGCAGTCACAGCCATCCGGGAAAATCTCATATCAGCCCTT
GAGGAAGCCAAGAAAGGACTAGCTGCTATAAAGTTTGAGGGAGCAATTTATAGGAAAGAC
GTCGGCTTTCGTGCCATAGCTTTCCTCCAGCAGCCCAGGAGTTTGACTTACAAGGAATCT
GGAGTAGATATCGCAGCTGGAAATATGCTGGTCAAGAAAATTCAGCCTTTAGCAAAAGCC
ACTTCCAGATCAGGCTGTAAAGTTGATCTTGGAGGTTTTGCTGGTCTTTTTGATTTAAAA
GCAGCTGGTTTCAAAGATCCCCTTCTGGCCTCTGGAACAGATGGCGTTGGAACTAAACTA
AAGATTGCCCAGCTATGCAATAAACATGATACCATTGGTCAAGATTTGGTAGCAATGTGT
GTTAATGATATTCTGGCACAAGGAGCAGAGCCCCTCTTCTTCCTTGATTACTTTTCCTGT
GGAAAACTTGACCTCAGTGTAACTGAAGCTGTTGTTGCTGGAATTGCTAAAGCTTGTGGA
AAAGCTGGATGTGCTCTCCTTGGAGGTGAAACAGCAGAAATGCCTGACATGTATCCCCCT
GGAGAGTATGACCTAGCTGGGTTTGCCGTTGGTGCCATGGAGCGAGATCAGAAACTCCCT
CACCTGGAAAGAATCACTGAGGGTGATGTTGTTGTTGGAATAGCTTCATCTGGTCTTCAT
AGCAATGGATTTAGCCTTGTGAGGAAAATCGTTGCAAAATCTTCCCTCCAGTACTCCTCT
CCAGCACCTGATGGTTGTGGTGACCAGACTTTAGGGGACTTACTTCTCACGCCTACCAGA
ATCTACAGCCATTCACTGTTACCTGTCCTACGTTCAGGACATGTCAAAGCCTTTGCCCAT
ATTACTGGTGGAGGATTACTAGAGAACATCCCCAGAGTCCTCCCTGAGAAACTTGGGGTA
GATTTAGATGCCCAGACCTGGAGGATCCCCAGGGTTTTCTCATGGTTGCAGCAGGAAGGA
CACCTCTCTGAGGAAGAGATGGCCAGAACATTTAACTGTGGGGTTGGCGCTGTCCTTGTG
GTATCAAAGGAGCAGACAGAGCAGATTCTGAGGGATATCCAGCAGCACAAGGAAGAAGCC
TGGGTGATTGGCAGTGTGGTTGCACGAGCTGAAGGTTCCCCACGTGTGAAAGTCAAGAAT
CTGATTGAAAGCATGCAAATAAATGGGTCAGTGTTGAAGAATGGCTCCCTGACAAATCAT
TTCTCTTTTGAAAAAAAAAAGGCCAGAGTGGCTGTCTTAATATCTGGAACAGGATCGAAC
CTGCAAGCACTTATAGACAGTACTCGGGAACCAAATAGCTCTGCACAAATTGATATTGTT
ATCTCCAACAAAGCCGCAGTAGCTGGGTTAGATAAAGCGGAAAGAGCTGGTATTCCCACT
AGAGTAATTAATCATAAACTGTATAAAAATCGTGTAGAATTTGACAGTGCAATTGACCTA
GTCCTTGAAGAGTTCTCCATAGACATAGTCTGTCTTGCAGGATTCATGAGAATTCTTTCT
GGCCCCTTTGTCCAAAAGTGGAATGGAAAAATGCTCAATATCCACCCATCCTTGCTCCCT
TCTTTTAAGGGTTCAAATGCCCATGAGCAAGCCCTGGAAACCGGAGTCACAGTTACTGGG
TGCACTGTACACTTTGTAGCTGAAGATGTGGATGCTGGACAGATTATTTTGCAAGAAGCT
GTTCCCGTGAAGAGGGGTGATACTGTCGCAACTCTTTCTGAAAGAGTAAAATTAGCAGAA
CATAAAATATTTCCTGCAGCCCTTCAGCTGGTGGCCAGTGGAACTGTACAGCTTGGAGAA
AATGGCAAGATCTGTTGGGTTAAAGAGGAATGA
|
| Enzyme 109 GenBank Gene ID |
X54199 |
| Enzyme 109 GeneCard ID |
GART |
| Enzyme 109 GenAtlas ID |
GART |
| Enzyme 109 HGNC ID |
HGNC:4163 |
| Enzyme 109 Chromosome Location |
2 |
| Enzyme 109 Locus |
21q22.1|21q22.11 |
| Enzyme 109 SNPs |
SNPJam Report |
| Enzyme 109 General References |
- Aimi J, Qiu H, Williams J, Zalkin H, Dixon JE: De novo purine nucleotide biosynthesis: cloning of human and avian cDNAs encoding the trifunctional glycinamide ribonucleotide synthetase-aminoimidazole ribonucleotide synthetase-glycinamide ribonucleotide transformylase by functional complementation in E. coli. Nucleic Acids Res. 1990 Nov 25;18(22):6665-72. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Kan JL, Moran RG: Intronic polyadenylation in the human glycinamide ribonucleotide formyltransferase gene. Nucleic Acids Res. 1997 Aug 1;25(15):3118-23. [PubMed ]
- Schild D, Brake AJ, Kiefer MC, Young D, Barr PJ: Cloning of three human multifunctional de novo purine biosynthetic genes by functional complementation of yeast mutations. Proc Natl Acad Sci U S A. 1990 Apr;87(8):2916-20. [PubMed ]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Zhang Y, Desharnais J, Greasley SE, Beardsley GP, Boger DL, Wilson IA: Crystal structures of human GAR Tfase at low and high pH and with substrate beta-GAR. Biochemistry. 2002 Dec 3;41(48):14206-15. [PubMed ]
- Zhang Y, Desharnais J, Marsilje TH, Li C, Hedrick MP, Gooljarsingh LT, Tavassoli A, Benkovic SJ, Olson AJ, Boger DL, Wilson IA: Rational design, synthesis, evaluation, and crystal structure of a potent inhibitor of human GAR Tfase: 10-(trifluoroacetyl)-5,10-dideazaacyclic-5,6,7,8-tetrahydrofolic acid. Biochemistry. 2003 May 27;42(20):6043-56. [PubMed ]
- Dahms TE, Sainz G, Giroux EL, Caperelli CA, Smith JL: The apo and ternary complex structures of a chemotherapeutic target: human glycinamide ribonucleotide transformylase. Biochemistry. 2005 Jul 26;44(29):9841-50. [PubMed ]
|
| Enzyme 109 Metabolite References |
Not Available |
|
Enzyme 110
[top]
|
| Enzyme 110 ID |
5569 |
| Enzyme 110 Name |
Sialic acid synthase |
| Enzyme 110 Synonyms |
- N-acetylneuraminate synthase
- N-acetylneuraminate-9-phosphate synthase
- N-acetylneuraminic acid phosphate synthase
- N-acetylneuraminic acid synthase
|
| Enzyme 110 Gene Name |
NANS |
| Enzyme 110 Protein Sequence |
>Sialic acid synthase
MPLELELCPGRWVGGQHPCFIIAEIGQNHQGDLDVAKRMIRMAKECGADCAKFQKSELEF
KFNRKALERPYTSKHSWGKTYGEHKRHLEFSHDQYRELQRYAEEVGIFFTASGMDEMAVE
FLHELNVPFFKVGSGDTNNFPYLEKTAKKGRPMVISSGMQSMDTMKQVYQIVKPLNPNFC
FLQCTSAYPLQPEDVNLRVISEYQKLFPDIPIGYSGHETGIAISVAAVALGAKVLERHIT
LDKTWKGSDHSASLEPGELAELVRSVRLVERALGSPTKQLLPCEMACNEKLGKSVVAKVK
IPEGTILTMDMLTVKVGEPKGYPPEDIFNLVGKKVLVTVEEDDTIMEELVDNHGKKIKS
|
| Enzyme 110 Number of Residues |
359 |
| Enzyme 110 Molecular Weight |
40307.3 |
| Enzyme 110 Theoretical pI |
6.73 |
| Enzyme 110 GO Classification |
| Function |
|
| Process |
- carbohydrate biosynthetic process
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 110 General Function |
Involved in catalytic activity |
| Enzyme 110 Specific Function |
Produces N-acetylneuraminic acid (Neu5Ac) and 2-keto-3- deoxy-D-glycero-D-galacto-nononic acid (KDN). Can also use N- acetylmannosamine 6-phosphate and mannose 6-phosphate as substrates to generate phosphorylated forms of Neu5Ac and KDN, respectively |
| Enzyme 110 Pathways |
|
| Enzyme 110 Reactions |
- phosphoenolpyruvate + N-acyl-D-mannosamine 6-phosphate + H2O = N-acylneuraminate 9-phosphate + phosphate [RN:R02769]
|
| Enzyme 110 Pfam Domain Function |
|
| Enzyme 110 Signals |
|
| Enzyme 110 Transmembrane Regions |
|
| Enzyme 110 Essentiality |
Not Available |
| Enzyme 110 GenBank ID Protein |
8453156 |
| Enzyme 110 UniProtKB/Swiss-Prot ID |
Q9NR45 |
| Enzyme 110 UniProtKB/Swiss-Prot Entry Name |
SIAS_HUMAN |
| Enzyme 110 PDB ID |
Not Available |
| Enzyme 110 Cellular Location |
Not Available |
| Enzyme 110 Gene Sequence |
>1080 bp
ATGCCGCTGGAGCTGGAGCTGTGTCCCGGGCGCTGGGTGGGCGGGCAACACCCGTGCTTC
ATCATTGCCGAGATCGGCCAGAACCACCAGGGCGACCTGGACGTAGCCAAGCGCATGATC
CGCATGGCCAAGGAGTGTGGGGCTGATTGTGCCAAGTTCCAGAAGAGTGAGCTAGAATTC
AAGTTTAATCGGAAAGCCTTGGAGAGGCCATACACCTCGAAGCATTCCTGGGGGAAGACG
TACGGGGAGCACAAACGACATCTGGAGTTCAGCCATGACCAGTACAGGGAGCTGCAGAGG
TACGCCGAGGAGGTTGGGATCTTCTTCACTGCCTCTGGCATGGATGAGATGGCAGTTGAA
TTCCTGCATGAACTGAATGTTCCATTTTTCAAAGTTGGATCTGGAGACACTAATAATTTT
CCTTATCTGGAAAAGACAGCCAAAAAAGGTCGCCCAATGGTGATCTCCAGTGGGATGCAG
TCAATGGACACCATGAAGCAAGTTTATCAGATCGTGAAGCCCCTCAACCCCAACTTCTGC
TTCTTGCAGTGTACCAGCGCATACCCGCTCCAGCCTGAGGACGTCAACCTGCGGGTCATC
TCGGAATATCAGAAGCTCTTTCCTGACATTCCCATAGGGTATTCTGGGCATGAAACAGGC
ATAGCGATATCTGTGGCCGCAGTGGCTCTGGGGGCCAAGGTGTTGGAACGTCACATAACT
TTGGACAAGACCTGGAAGGGGAGTGACCACTCGGCCTCGCTGGAGCCTGGAGAACTGGCC
GAGCTGGTGCGGTCAGTGCGTCTTGTGGAGCGTGCCCTGGGCTCCCCAACCAAGCAGCTG
CTGCCCTGTGAGATGGCCTGCAATGAGAAGCTGGGCAAGTCTGTGGTGGCCAAAGTGAAA
ATTCCGGAAGGCACCATTCTAACAATGGACATGCTCACCGTGAAGGTGGGTGAGCCCAAA
GCCTATCCTCCTGAAGACATCTTTAATCTAGTGGGCAAGAAGGTCCTGGTCACTGTTGAA
GAGGATGACACCATCATGGAAGAATTGGTAGATAATCATGGCAAAAAAATCAAGTCTTAA
|
| Enzyme 110 GenBank Gene ID |
AF257466 |
| Enzyme 110 GeneCard ID |
NANS |
| Enzyme 110 GenAtlas ID |
NANS |
| Enzyme 110 HGNC ID |
HGNC:19237 |
| Enzyme 110 Chromosome Location |
9 |
| Enzyme 110 Locus |
9p24.1-p23 |
| Enzyme 110 SNPs |
SNPJam Report |
| Enzyme 110 General References |
- Lawrence SM, Huddleston KA, Pitts LR, Nguyen N, Lee YC, Vann WF, Coleman TA, Betenbaugh MJ: Cloning and expression of the human N-acetylneuraminic acid phosphate synthase gene with 2-keto-3-deoxy-D-glycero- D-galacto-nononic acid biosynthetic ability. J Biol Chem. 2000 Jun 9;275(23):17869-77. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed ]
- Hamada T, Ito Y, Abe T, Hayashi F, Guntert P, Inoue M, Kigawa T, Terada T, Shirouzu M, Yoshida M, Tanaka A, Sugano S, Yokoyama S, Hirota H: Solution structure of the antifreeze-like domain of human sialic acid synthase. Protein Sci. 2006 May;15(5):1010-6. Epub 2006 Apr 5. [PubMed ]
|
| Enzyme 110 Metabolite References |
Not Available |
|
Enzyme 111
[top]
|
| Enzyme 111 ID |
5578 |
| Enzyme 111 Name |
3'(2'),5'-bisphosphate nucleotidase 1 |
| Enzyme 111 Synonyms |
- Bisphosphate 3'-nucleotidase 1
- PAP-inositol-1,4-phosphatase
- PIP
|
| Enzyme 111 Gene Name |
BPNT1 |
| Enzyme 111 Protein Sequence |
>3'(2'),5'-bisphosphate nucleotidase 1
MASSNTVLMRLVASAYSIAQKAGMIVRRVIAEGDLGIVEKTCATDLQTKADRLAQMSICS
SLARKFPKLTIIGEEDLPSEEVDQELIEDSQWEEILKQPCPSQYSAIKEEDLVVWVDPLD
GTKEYTEGLLDNVTVLIGIAYEGKAIAGVINQPYYNYEAGPDAVLGRTIWGVLGLGAFGF
QLKEVPAGKHIITTTRSHSNKLVTDCVAAMNPDAVLRVGGAGNKIIQLIEGKASAYVFAS
PGCKKWDTCAPEVILHAVGGKLTDIHGNVLQYHKDVKHMNSAGVLATLRNYDYYASRVPE
SIKNALVP
|
| Enzyme 111 Number of Residues |
308 |
| Enzyme 111 Molecular Weight |
33392.0 |
| Enzyme 111 Theoretical pI |
5.41 |
| Enzyme 111 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 111 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 111 Specific Function |
Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Has 1000-fold lower activity towards inositol 1,4-bisphosphate (Ins(1,4)P2) and inositol 1,3,4- trisphosphate (Ins(1,3,4)P3), but does not hydrolyze Ins(1)P, Ins(3,4)P2, Ins(1,3,4,5)P4 or InsP6 |
| Enzyme 111 Pathways |
- Sulfate and Sulfite Metabolism (map00920 )
|
| Enzyme 111 Reactions |
- adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate [RN:R00188]
|
| Enzyme 111 Pfam Domain Function |
|
| Enzyme 111 Signals |
|
| Enzyme 111 Transmembrane Regions |
|
| Enzyme 111 Essentiality |
Not Available |
| Enzyme 111 GenBank ID Protein |
Not Available |
| Enzyme 111 UniProtKB/Swiss-Prot ID |
O95861 |
| Enzyme 111 UniProtKB/Swiss-Prot Entry Name |
BPNT1_HUMAN |
| Enzyme 111 PDB ID |
1JP4 |
| Enzyme 111 PDB File |
Show |
| Enzyme 111 3D Structure |
|
| Enzyme 111 Cellular Location |
Not Available |
| Enzyme 111 Gene Sequence |
>927 bp
ATGGCTTCCAGTAACACTGTGTTGATGCGGTTGGTAGCCTCCGCATATTCTATTGCTCAA
AAGGCAGGAATGATAGTCAGACGTGTTATTGCTGAAGGAGACCTGGGTATTGTGGAGAAG
ACCTGTGCAACAGACCTGCAGACCAAAGCTGACCGATTGGCACAGATGAGCATATGTTCT
TCATTGGCCCGGAAATTCCCCAAACTCACAATTATAGGGGAAGAGGATCTGCCTTCTGAG
GAAGTGGATCAAGAGCTGATTGAAGACAGTCAGTGGGAAGAAATACTGAAGCAACCATGC
CCATCGCAGTACAGTGCTATTAAAGAAGAAGATCTCGTGGTCTGGGTTGATCCTCTGGAT
GGAACCAAGGAATATACCGAAGGTCTTCTTGACAATGTAACAGTTCTTATTGGAATTGCT
TATGAAGGAAAAGCCATAGCAGGAGTTATTAACCAGCCATATTACAACTATGAGGCAGGA
CCAGATGCTGTGTTGGGGAGGACAATCTGGGGAGTTTTAGGTTTAGGCGCCTTTGGGTTT
CAGCTGAAAGAAGTCCCTGCTGGGAAACACATTATCACAACTACTCGATCCCATAGCAAC
AAGTTGGTTACTGACTGTGTTGCTGCTATGAACCCCGATGCTGTGCTGCGAGTAGGAGGA
GCAGGAAATAAGATTATTCAGCTGATTGAAGGCAAAGCCTCTGCTTATGTATTTGCAAGT
CCTGGTTGTAAGAAGTGGGATACTTGTGCTCCAGAAGTTATTTTACATGCTGTGGGAGGC
AAGTTAACCGATATCCATGGGAATGTTCTTCAGTACCACAAGGATGTGAAGCATATGAAC
TCTGCAGGAGTCCTGGCCACACTGAGGAATTATGACTACTATGCAAGCCGAGTTCCAGAA
TCTATTAAAAATGCACTTGTTCCTTAA
|
| Enzyme 111 GenBank Gene ID |
AF125042 |
| Enzyme 111 GeneCard ID |
BPNT1 |
| Enzyme 111 GenAtlas ID |
BPNT1 |
| Enzyme 111 HGNC ID |
HGNC:1096 |
| Enzyme 111 Chromosome Location |
1 |
| Enzyme 111 Locus |
1q41 |
| Enzyme 111 SNPs |
SNPJam Report |
| Enzyme 111 General References |
- Spiegelberg BD, Xiong JP, Smith JJ, Gu RF, York JD: Cloning and characterization of a mammalian lithium-sensitive bisphosphate 3'-nucleotidase inhibited by inositol 1,4-bisphosphate. J Biol Chem. 1999 May 7;274(19):13619-28. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
|
| Enzyme 111 Metabolite References |
Not Available |
|
Enzyme 112
[top]
|
| Enzyme 112 ID |
5593 |
| Enzyme 112 Name |
Uroporphyrinogen-III synthase |
| Enzyme 112 Synonyms |
- UROIIIS
- UROS
- Hydroxymethylbilane hydrolyase [cyclizing]
- Uroporphyrinogen-III cosynthase
|
| Enzyme 112 Gene Name |
UROS |
| Enzyme 112 Protein Sequence |
>Uroporphyrinogen-III synthase
MKVLLLKDAKEDDCGQDPYIRELGLYGLEATLIPVLSFEFLSLPSFSEKLSHPEDYGGLI
FTSPRAVEAAELCLEQNNKTEVWERSLKEKWNAKSVYVVGNATASLVSKIGLDTEGETCG
NAEKLAEYICSRESSALPLLFPCGNLKREILPKALKDKGIAMESITVYQTVAHPGIQGNL
NSYYSQQGVPASITFFSPSGLTYSLKHIQELSGDNIDQIKFAAIGPTTARALAAQGLPVS
CTAESPTPQALATGIRKALQPHGCC
|
| Enzyme 112 Number of Residues |
265 |
| Enzyme 112 Molecular Weight |
28627.4 |
| Enzyme 112 Theoretical pI |
5.16 |
| Enzyme 112 GO Classification |
| Function |
- carbon-oxygen lyase activity
- catalytic activity
- hydro-lyase activity
- lyase activity
- uroporphyrinogen-III synthase activity
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- metabolic process
- tetrapyrrole biosynthetic process
|
| Component |
| — |
|
| Enzyme 112 General Function |
Involved in uroporphyrinogen-III synthase activity |
| Enzyme 112 Specific Function |
Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III, the branch point for the various sub-pathways leading to the wide diversity of porphyrins. Porphyrins act as cofactors for a multitude of enzymes that perform a variety of processes within the cell such as methionine synthesis (vitamin B12) or oxygen transport (heme) |
| Enzyme 112 Pathways |
|
| Enzyme 112 Reactions |
- hydroxymethylbilane = uroporphyrinogen III + H2O [RN:R03165]
|
| Enzyme 112 Pfam Domain Function |
|
| Enzyme 112 Signals |
|
| Enzyme 112 Transmembrane Regions |
|
| Enzyme 112 Essentiality |
Not Available |
| Enzyme 112 GenBank ID Protein |
337463 |
| Enzyme 112 UniProtKB/Swiss-Prot ID |
P10746 |
| Enzyme 112 UniProtKB/Swiss-Prot Entry Name |
HEM4_HUMAN |
| Enzyme 112 PDB ID |
1JR2 |
| Enzyme 112 PDB File |
Show |
| Enzyme 112 3D Structure |
|
| Enzyme 112 Cellular Location |
Not Available |
| Enzyme 112 Gene Sequence |
>798 bp
ATGAAGGTTCTTTTACTGAAGGATGCGAAGGAAGATGACTGTGGCCAGGATCCGTATATC
AGGGAATTAGGATTATATGGACTTGAAGCCACTTTGATCCCTGTTTTATCGTTTGAGTTT
TTGTCTCTTCCCAGTTTCTCTGAGAAGCTTTCTCATCCTGAAGATTACGGGGGACTCATT
TTTACCAGCCCCAGAGCAGTGGAAGCAGCAGAGTTATGTTTGGAGCAAAACAATAAAACT
GAAGTCTGGGAAAGGTCTCTGAAAGAAAAATGGAATGCCAAGTCAGTGTATGTGGTTGGA
AATGCTACTGCTTCTCTAGTGAGTAAAATTGGCCTGGATACAGAAGGAGAAACCTGTGGA
AATGCAGAAAAGCTTGCAGAATATATTTGTTCCAGGGAGTCCTCAGCACTGCCTCTTCTA
TTTCCCTGTGGAAACCTCAAAAGAGAAATCCTGCCAAAAGCGCTCAAGGACAAAGGGATT
GCCATGGAAAGCATAACTGTGTATCAGACAGTTGCACACCCAGGAATCCAAGGGAACCTG
AACAGCTACTATTCCCAGCAGGGGGTTCCAGCCAGCATCACATTTTTTAGTCCCTCTGGC
CTCACATACAGTCTCAAGCACATTCAGGAGTTATCTGGTGACAATATCGATCAAATTAAG
TTTGCAGCCATCGGCCCCACTACGGCTCGCGCGCTGGCCGCCCAGGGCCTTCCTGTAAGC
TGCACTGCAGAGAGCCCCACGCCACAAGCCCTGGCCACTGGCATCAGGAAGGCTCTCCAG
CCCCATGGCTGCTGCTGA
|
| Enzyme 112 GenBank Gene ID |
J03824 |
| Enzyme 112 GeneCard ID |
UROS |
| Enzyme 112 GenAtlas ID |
UROS |
| Enzyme 112 HGNC ID |
HGNC:12592 |
| Enzyme 112 Chromosome Location |
1 |
| Enzyme 112 Locus |
10q25.2-q26.3 |
| Enzyme 112 SNPs |
SNPJam Report |
| Enzyme 112 General References |
- Tsai SF, Bishop DF, Desnick RJ: Human uroporphyrinogen III synthase: molecular cloning, nucleotide sequence, and expression of a full-length cDNA. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7049-53. [PubMed ]
- Aizencang G, Solis C, Bishop DF, Warner C, Desnick RJ: Human uroporphyrinogen-III synthase: genomic organization, alternative promoters, and erythroid-specific expression. Genomics. 2000 Dec 1;70(2):223-31. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Xu W, Astrin KH, Desnick RJ: Molecular basis of congenital erythropoietic porphyria: mutations in the human uroporphyrinogen III synthase gene. Hum Mutat. 1996;7(3):187-92. [PubMed ]
- Mathews MA, Schubert HL, Whitby FG, Alexander KJ, Schadick K, Bergonia HA, Phillips JD, Hill CP: Crystal structure of human uroporphyrinogen III synthase. EMBO J. 2001 Nov 1;20(21):5832-9. [PubMed ]
- Deybach JC, de Verneuil H, Boulechfar S, Grandchamp B, Nordmann Y: Point mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria (Gunther's disease). Blood. 1990 May 1;75(9):1763-5. [PubMed ]
- Boulechfar S, Da Silva V, Deybach JC, Nordmann Y, Grandchamp B, de Verneuil H: Heterogeneity of mutations in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria. Hum Genet. 1992 Jan;88(3):320-4. [PubMed ]
- Warner CA, Yoo HW, Roberts AG, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of exonic mutations in the uroporphyrinogen III synthase gene. J Clin Invest. 1992 Feb;89(2):693-700. [PubMed ]
- Xu W, Warner CA, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of 10 mutations in the uroporphyrinogen III synthase gene. J Clin Invest. 1995 Feb;95(2):905-12. [PubMed ]
- Tanigawa K, Bensidhoum M, Takamura N, Namba H, Yamashita S, de Verneuil H, Ged C: A novel point mutation in congenital erythropoietic porphyria in two members of Japanese family. Hum Genet. 1996 May;97(5):557-60. [PubMed ]
- Takamura N, Hombrados I, Tanigawa K, Namba H, Nagayama Y, de Verneuil H, Yamashita S: Novel point mutation in the uroporphyrinogen III synthase gene causes congenital erythropoietic porphyria of a Japanese family. Am J Med Genet. 1997 Jun 13;70(3):299-302. [PubMed ]
- Tezcan I, Xu W, Gurgey A, Tuncer M, Cetin M, Oner C, Yetgin S, Ersoy F, Aizencang G, Astrin KH, Desnick RJ: Congenital erythropoietic porphyria successfully treated by allogeneic bone marrow transplantation. Blood. 1998 Dec 1;92(11):4053-8. [PubMed ]
- Frank J, Wang X, Lam HM, Aita VM, Jugert FK, Goerz G, Merk HF, Poh-Fitzpatrick MB, Christiano AM: C73R is a hotspot mutation in the uroporphyrinogen III synthase gene in congenital erythropoietic porphyria. Ann Hum Genet. 1998 May;62(Pt 3):225-30. [PubMed ]
- Rogounovitch T, Takamura N, Hombrados I, Morel C, Tanaka T, Kameyoshi Y, Shimizu-Yoshida Y, de Verneuil H, Yamashita S: Congenital erythropoietic porphyria: a novel homozygous mutation in a Japanese patient. J Invest Dermatol. 2000 Dec;115(6):1156. [PubMed ]
- Shady AA, Colby BR, Cunha LF, Astrin KH, Bishop DF, Desnick RJ: Congenital erythropoietic porphyria: identification and expression of eight novel mutations in the uroporphyrinogen III synthase gene. Br J Haematol. 2002 Jun;117(4):980-7. [PubMed ]
- Ged C, Megarbane H, Chouery E, Lalanne M, Megarbane A, de Verneuil H: Congenital erythropoietic porphyria: report of a novel mutation with absence of clinical manifestations in a homozygous mutant sibling. J Invest Dermatol. 2004 Sep;123(3):589-91. [PubMed ]
|
| Enzyme 112 Metabolite References |
Not Available |
|
Enzyme 113
[top]
|
| Enzyme 113 ID |
5594 |
| Enzyme 113 Name |
Porphobilinogen deaminase |
| Enzyme 113 Synonyms |
- PBG-D
- Hydroxymethylbilane synthase
- HMBS
- Pre-uroporphyrinogen synthase
|
| Enzyme 113 Gene Name |
HMBS |
| Enzyme 113 Protein Sequence |
>Porphobilinogen deaminase
MSGNGNAAATAEENSPKMRVIRVGTRKSQLARIQTDSVVATLKASYPGLQFEIIAMSTTG
DKILDTALSKIGEKSLFTKELEHALEKNEVDLVVHSLKDLPTVLPPGFTIGAICKRENPH
DAVVFHPKFVGKTLETLPEKSVVGTSSLRRAAQLQRKFPHLEFRSIRGNLNTRLRKLDEQ
QEFSAIILATAGLQRMGWHNRVGQILHPEECMYAVGQGALGVEVRAKDQDILDLVGVLHD
PETLLRCIAERAFLRHLEGGCSVPVAVHTAMKDGQLYLTGGVWSLDGSDSIQETMQATIH
VPAQHEDGPEDDPQLVGITARNIPRGPQLAAQNLGISLANLLLSKGAKNILDVARQLNDA
H
|
| Enzyme 113 Number of Residues |
361 |
| Enzyme 113 Molecular Weight |
39329.7 |
| Enzyme 113 Theoretical pI |
7.19 |
| Enzyme 113 GO Classification |
| Function |
- catalytic activity
- hydroxymethylbilane synthase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- biosynthetic process
- cellular biosynthetic process
- heterocycle biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- peptidyl-pyrromethane cofactor linkage
- post-translational protein modification
- protein modification process
- protein-cofactor linkage
- tetrapyrrole biosynthetic process
|
| Component |
| — |
|
| Enzyme 113 General Function |
Involved in hydroxymethylbilane synthase activity |
| Enzyme 113 Specific Function |
Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps |
| Enzyme 113 Pathways |
|
| Enzyme 113 Reactions |
- 4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH3 [RN:R00084]
|
| Enzyme 113 Pfam Domain Function |
|
| Enzyme 113 Signals |
|
| Enzyme 113 Transmembrane Regions |
|
| Enzyme 113 Essentiality |
Not Available |
| Enzyme 113 GenBank ID Protein |
158261573 |
| Enzyme 113 UniProtKB/Swiss-Prot ID |
P08397 |
| Enzyme 113 UniProtKB/Swiss-Prot Entry Name |
HEM3_HUMAN |
| Enzyme 113 PDB ID |
Not Available |
| Enzyme 113 Cellular Location |
Not Available |
| Enzyme 113 Gene Sequence |
>1086 bp
ATGTCTGGTAACGGCAATGCGGCTGCAACGGCGGAAGAAAACAGCCCAAAGATGAGAGTG
ATTCGCGTGGGTACCCGCAAGAGCCAGCTTGCTCGCATACAGACGGACAGTGTGGTGGCA
ACATTGAAAGCCTCGTACCCTGGCCTGCAGTTTGAAATCATTGCTATGTCCACCACAGGG
GACAAGATTCTTGATACTGCACTCTCTAAGATTGGAGAGAAAAGCCTGTTTACCAAGGAG
CTTGAACATGCCCTGGAGAAGAATGAAGTGGACCTGGTTGTTCACTCCTTGAAGGACCTG
CCCACTGTGCTTCCTCCTGGCTTCACCATCGGAGCCATCTGCAAGCGGGAAAACCCTCAT
GATGCTGTTGTCTTTCACCCAAAATTTGTTGGGAAGACCCTAGAAACCCTGCCAGAGAAG
AGTGTGGTGGGAACCAGCTCCCTGCGAAGAGCAGCCCAGCTGCAGAGAAAGTTCCCGCAT
CTGGAGTTCAGGAGTATTCGGGGAAACCTCAACACCCGGCTTCGGAAGCTGGACGAGCAG
CAGGAGTTCAGTGCCATCATCCTGGCAACAGCTGGCCTGCAGCGCATGGGCTGGCACAAC
CGGGTGGGGCAGATCCTGCACCCTGAGGAATGCATGTATGCTGTGGGCCAGGGGGCCTTG
GGCGTGGAAGTGCGAGCCAAGGACCAGGACATCTTGGATCTGGTGGGTGTGCTGCACGAT
CCCGAGACTCTGCTTCGCTGCATCGCTGAAAGGGCCTTCCTGAGGCACCTGGAAGGAGGC
TGCAGTGTGCCAGTAGCCGTGCATACAGCTATGAAGGATGGGCAACTGTACCTGACTGGA
GGAGTCTGGAGTCTAGACGGCTCAGATAGCATACAAGAGACCATGCAGGCTACCATCCAT
GTCCCTGCCCAGCATGAAGATGGCCCTGAGGATGACCCACAGTTGGTAGGCATCACTGCT
CGTAACATTCCACGAGGGCCCCAGTTGGCTGCCCAGAACTTGGGCATCAGCCTGGCCAAC
TTGTTGCTGAGCAAAGGAGCCAAAAACATCCTGGATGTTGCACGGCAGCTTAACGATGCC
CATTAA
|
| Enzyme 113 GenBank Gene ID |
AK290275 |
| Enzyme 113 GeneCard ID |
HMBS |
| Enzyme 113 GenAtlas ID |
HMBS |
| Enzyme 113 HGNC ID |
HGNC:4982 |
| Enzyme 113 Chromosome Location |
1 |
| Enzyme 113 Locus |
11q23.3 |
| Enzyme 113 SNPs |
SNPJam Report |
| Enzyme 113 General References |
- Raich N, Romeo PH, Dubart A, Beaupain D, Cohen-Solal M, Goossens M: Molecular cloning and complete primary sequence of human erythrocyte porphobilinogen deaminase. Nucleic Acids Res. 1986 Aug 11;14(15):5955-68. [PubMed ]
- Grandchamp B, De Verneuil H, Beaumont C, Chretien S, Walter O, Nordmann Y: Tissue-specific expression of porphobilinogen deaminase. Two isoenzymes from a single gene. Eur J Biochem. 1987 Jan 2;162(1):105-10. [PubMed ]
- Yoo HW, Warner CA, Chen CH, Desnick RJ: Hydroxymethylbilane synthase: complete genomic sequence and amplifiable polymorphisms in the human gene. Genomics. 1993 Jan;15(1):21-9. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Chretien S, Dubart A, Beaupain D, Raich N, Grandchamp B, Rosa J, Goossens M, Romeo PH: Alternative transcription and splicing of the human porphobilinogen deaminase gene result either in tissue-specific or in housekeeping expression. Proc Natl Acad Sci U S A. 1988 Jan;85(1):6-10. [PubMed ]
- Lannfelt L, Wetterberg L, Lilius L, Thunell S, Jornvall H, Pavlu B, Wielburski A, Gellerfors P: Porphobilinogen deaminase in human erythrocytes: purification of two forms with apparent molecular weights of 40 kDa and 42 kDa. Scand J Clin Lab Invest. 1989 Nov;49(7):677-84. [PubMed ]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed ]
- Gill R, Kolstoe SE, Mohammed F, Al D-Bass A, Mosely JE, Sarwar M, Cooper JB, Wood SP, Shoolingin-Jordan PM: Structure of human porphobilinogen deaminase at 2.8 A: the molecular basis of acute intermittent porphyria. Biochem J. 2009 Apr 28;420(1):17-25. [PubMed ]
- Song G, Li Y, Cheng C, Zhao Y, Gao A, Zhang R, Joachimiak A, Shaw N, Liu ZJ: Structural insight into acute intermittent porphyria. FASEB J. 2009 Feb;23(2):396-404. Epub 2008 Oct 20. [PubMed ]
- Delfau MH, Picat C, de Rooij FW, Hamer K, Bogard M, Wilson JH, Deybach JC, Nordmann Y, Grandchamp B: Two different point G to A mutations in exon 10 of the porphobilinogen deaminase gene are responsible for acute intermittent porphyria. J Clin Invest. 1990 Nov;86(5):1511-6. [PubMed ]
- Delfau MH, Picat C, De Rooij F, Voortman G, Deybach JC, Nordmann Y, Grandchamp B: Molecular heterogeneity of acute intermittent porphyria: identification of four additional mutations resulting in the CRIM-negative subtype of the disease. Am J Hum Genet. 1991 Aug;49(2):421-8. [PubMed ]
- Gu XF, de Rooij F, Voortman G, Te Velde K, Nordmann Y, Grandchamp B: High frequency of mutations in exon 10 of the porphobilinogen deaminase gene in patients with a CRIM-positive subtype of acute intermittent porphyria. Am J Hum Genet. 1992 Sep;51(3):660-5. [PubMed ]
- Mgone CS, Lanyon WG, Moore MR, Connor JM: Detection of seven point mutations in the porphobilinogen deaminase gene in patients with acute intermittent porphyria, by direct sequencing of in vitro amplified cDNA. Hum Genet. 1992 Sep-Oct;90(1-2):12-6. [PubMed ]
- Kauppinen R, Peltonen L, Pihlaja H, Mustajoki P: CRIM-positive mutations of acute intermittent porphyria in Finland. Hum Mutat. 1992;1(5):392-6. [PubMed ]
- Mgone CS, Lanyon WG, Moore MR, Louie GV, Connor JM: Detection of a high mutation frequency in exon 12 of the porphobilinogen deaminase gene in patients with acute intermittent porphyria. Hum Genet. 1993 Dec;92(6):619-22. [PubMed ]
- Llewellyn DH, Whatley S, Elder GH: Acute intermittent porphyria caused by an arginine to histidine substitution (R26H) in the cofactor-binding cleft of porphobilinogen deaminase. Hum Mol Genet. 1993 Aug;2(8):1315-6. [PubMed ]
- Gu XF, de Rooij F, de Baar E, Bruyland M, Lissens W, Nordmann Y, Grandchamp B: Two novel mutations of the porphobilinogen deaminase gene in acute intermittent porphyria. Hum Mol Genet. 1993 Oct;2(10):1735-6. [PubMed ]
- Gu XF, de Rooij F, Voortman G, Te Velde K, Deybach JC, Nordmann Y, Grandchamp B: Detection of eleven mutations causing acute intermittent porphyria using denaturing gradient gel electrophoresis. Hum Genet. 1994 Jan;93(1):47-52. [PubMed ]
- Lundin G, Wedell A, Thunell S, Anvret M: Two new mutations in the porphobilinogen deaminase gene and a screening method using PCR amplification of specific alleles. Hum Genet. 1994 Jan;93(1):59-62. [PubMed ]
- Mgone CS, Lanyon WG, Moore MR, Louie GV, Connor JM: Identification of five novel mutations in the porphobilinogen deaminase gene. Hum Mol Genet. 1994 May;3(5):809-11. [PubMed ]
- Astrin KH, Desnick RJ: Molecular basis of acute intermittent porphyria: mutations and polymorphisms in the human hydroxymethylbilane synthase gene. Hum Mutat. 1994;4(4):243-52. [PubMed ]
- Chen CH, Astrin KH, Lee G, Anderson KE, Desnick RJ: Acute intermittent porphyria: identification and expression of exonic mutations in the hydroxymethylbilane synthase gene. An initiation codon missense mutation in the housekeeping transcript causes "variant acute intermittent porphyria" with normal expression of the erythroid-specific enzyme. J Clin Invest. 1994 Nov;94(5):1927-37. [PubMed ]
- Kauppinen R, Mustajoki S, Pihlaja H, Peltonen L, Mustajoki P: Acute intermittent porphyria in Finland: 19 mutations in the porphobilinogen deaminase gene. Hum Mol Genet. 1995 Feb;4(2):215-22. [PubMed ]
- Lundin G, Hashemi J, Floderus Y, Thunell S, Sagen E, Laegreid A, Wassif W, Peters T, Anvret M: Four mutations in the porphobilinogen deaminase gene in patients with acute intermittent porphyria. J Med Genet. 1995 Dec;32(12):979-81. [PubMed ]
- Puy H, Deybach JC, Lamoril J, Robreau AM, Da Silva V, Gouya L, Grandchamp B, Nordmann Y: Molecular epidemiology and diagnosis of PBG deaminase gene defects in acute intermittent porphyria. Am J Hum Genet. 1997 Jun;60(6):1373-83. [PubMed ]
- Lundin G, Lee JS, Thunell S, Anvret M: Genetic investigation of the porphobilinogen deaminase gene in Swedish acute intermittent porphyria families. Hum Genet. 1997 Jul;100(1):63-6. [PubMed ]
- Mustajoki S, Pihlaja H, Ahola H, Petersen NE, Mustajoki P, Kauppinen R: Three splicing defects, an insertion, and two missense mutations responsible for acute intermittent porphyria. Hum Genet. 1998 May;102(5):541-8. [PubMed ]
- Ong PM, Lanyon WG, Hift RJ, Halkett J, Cramp CE, Moore MR, Connor JM: Identification of two novel mutations in the hydroxymethylbilane synthase gene in three patients from two unrelated families with acute intermittent porphyria. Hum Hered. 1998 Jan-Feb;48(1):24-9. [PubMed ]
- De Siervi A, Rossetti MV, Parera VE, Astrin KH, Aizencang GI, Glass IA, Batlle AM, Desnick RJ: Identification and characterization of hydroxymethylbilane synthase mutations causing acute intermittent porphyria: evidence for an ancestral founder of the common G111R mutation. Am J Med Genet. 1999 Oct 8;86(4):366-75. [PubMed ]
- Whatley SD, Woolf JR, Elder GH: Comparison of complementary and genomic DNA sequencing for the detection of mutations in the HMBS gene in British patients with acute intermittent porphyria: identification of 25 novel mutations. Hum Genet. 1999 Jun;104(6):505-10. [PubMed ]
- De Siervi A, Mendez M, Parera VE, Varela L, Batlle AM, Rossetti MV: Acute intermittent porphyria: characterization of two novel mutations in the porphobilinogen deaminase gene, one amino acid deletion (453-455delAGC) and one splicing aceptor site mutation (IVS8-1G>T). Hum Mutat. 1999 Oct;14(4):355. [PubMed ]
- Gross U, Puy H, Doss M, Robreau AM, Nordmann Y, Doss MO, Deybach JC: New mutations of the hydroxymethylbilane synthase gene in German patients with acute intermittent porphyria. Mol Cell Probes. 1999 Dec;13(6):443-7. [PubMed ]
- Solis C, Lopez-Echaniz I, Sefarty-Graneda D, Astrin KH, Desnick RJ: Identification and expression of mutations in the hydroxymethylbilane synthase gene causing acute intermittent porphyria (AIP). Mol Med. 1999 Oct;5(10):664-71. [PubMed ]
- Ramdall RB, Cunha L, Astrin KH, Katz DR, Anderson KE, Glucksman M, Bottomley SS, Desnick RJ: Acute intermittent porphyria: novel missense mutations in the human hydroxymethylbilane synthase gene. Genet Med. 2000 Sep-Oct;2(5):290-5. [PubMed ]
- Robreau-Fraolini AM, Puy H, Aquaron C, Bogard C, Traore M, Nordmann Y, Aquaron R, Deybach JC: Porphobilinogen deaminase gene in African and Afro-Caribbean ethnic groups: mutations causing acute intermittent porphyria and specific intragenic polymorphisms. Hum Genet. 2000 Aug;107(2):150-9. [PubMed ]
- Schneider-Yin X, Bogard C, Rufenacht UB, Puy H, Nordmann Y, Minder EI, Deybach J: Identification of a prevalent nonsense mutation (W283X) and two novel mutations in the porphobilinogen deaminase gene of Swiss patients with acute intermittent porphyria. Hum Hered. 2000 Jul-Aug;50(4):247-50. [PubMed ]
- De Siervi A, Weiss Cadiz DE, Parera VE, del C Batlle AM, Rossetti MV: Identification and characterization of two novel mutations that produce acute intermittent porphyria: A 3-base deletion (841-843delGGA) and a missense mutation (T35M). Hum Mutat. 2000 Oct;16(4):373. [PubMed ]
- Kauppinen R, von und zu Fraunberg M: Molecular and biochemical studies of acute intermittent porphyria in 196 patients and their families. Clin Chem. 2002 Nov;48(11):1891-900. [PubMed ]
- Floderus Y, Shoolingin-Jordan PM, Harper P: Acute intermittent porphyria in Sweden. Molecular, functional and clinical consequences of some new mutations found in the porphobilinogen deaminase gene. Clin Genet. 2002 Oct;62(4):288-97. [PubMed ]
- Gregor A, Schneider-Yin X, Szlendak U, Wettstein A, Lipniacka A, Rufenacht UB, Minder EI: Molecular study of the hydroxymethylbilane synthase gene (HMBS) among Polish patients with acute intermittent porphyria. Hum Mutat. 2002 Mar;19(3):310. [PubMed ]
- Gouya L, Puy H, Robreau AM, Lyoumi S, Lamoril J, Da Silva V, Grandchamp B, Deybach JC: Modulation of penetrance by the wild-type allele in dominantly inherited erythropoietic protoporphyria and acute hepatic porphyrias. Hum Genet. 2004 Feb;114(3):256-62. Epub 2003 Dec 11. [PubMed ]
- Hessels J, Voortman G, van der Wagen A, van der Elzen C, Scheffer H, Zuijderhoudt FM: Homozygous acute intermittent porphyria in a 7-year-old boy with massive excretions of porphyrins and porphyrin precursors. J Inherit Metab Dis. 2004;27(1):19-27. [PubMed ]
- Schneider-Yin X, Hergersberg M, Schuurmans MM, Gregor A, Minder EI: Mutation hotspots in the human porphobilinogen deaminase gene: recurrent mutations G111R and R173Q occurring at CpG motifs. J Inherit Metab Dis. 2004;27(5):625-31. [PubMed ]
|
| Enzyme 113 Metabolite References |
Not Available |
|
Enzyme 114
[top]
|
| Enzyme 114 ID |
5595 |
| Enzyme 114 Name |
Carbamoyl-phosphate synthase [ammonia], mitochondrial |
| Enzyme 114 Synonyms |
- Carbamoyl-phosphate synthetase I
- CPSase I
|
| Enzyme 114 Gene Name |
CPS1 |
| Enzyme 114 Protein Sequence |
>Carbamoyl-phosphate synthase [ammonia], mitochondrial
MTRILTAFKVVRTLKTGFGFTNVTAHQKWKFSRPGIRLLSVKAQTAHIVLEDGTKMKGYS
FGHPSSVAGEVVFNTGLGGYPEAITDPAYKGQILTMANPIIGNGGAPDTTALDELGLSKY
LESNGIKVSGLLVLDYSKDYNHWLATKSLGQWLQEEKVPAIYGVDTRMLTKIIRDKGTML
GKIEFEGQPVDFVDPNKQNLIAEVSTKDVKVYGKGNPTKVVAVDCGIKNNVIRLLVKRGA
EVHLVPWNHDFTKMEYDGILIAGGPGNPALAEPLIQNVRKILESDRKEPLFGISTGNLIT
GLAAGAKTYKMSMANRGQNQPVLNITNKQAFITAQNHGYALDNTLPAGWKPLFVNVNDQT
NEGIMHESKPFFAVQFHPEVTPGPIDTEYLFDSFFSLIKKGKATTITSVLPKPALVASRV
EVSKVLILGSGGLSIGQAGEFDYSGSQAVKAMKEENVKTVLMNPNIASVQTNEVGLKQAD
TVYFLPITPQFVTEVIKAEQPDGLILGMGGQTALNCGVELFKRGVLKEYGVKVLGTSVES
IMATEDRQLFSDKLNEINEKIAPSFAVESIEDALKAADTIGYPVMIRSAYALGGLGSGIC
PNRETLMDLSTKAFAMTNQILVEKSVTGWKEIEYEVVRDADDNCVTVCNMENVDAMGVHT
GDSVVVAPAQTLSNAEFQMLRRTSINVVRHLGIVGECNIQFALHPTSMEYCIIEVNARLS
RSSALASKATGYPLAFIAAKIALGIPLPEIKNVVSGKTSACFEPSLDYMVTKIPRWDLDR
FHGTSSRIGSSMKSVGEVMAIGRTFEESFQKALRMCHPSIEGFTPRLPMNKEWPSNLDLR
KELSEPSSTRIYAIAKAIDDNMSLDEIEKLTYIDKWFLYKMRDILNMEKTLKGLNSESMT
EETLKRAKEIGFSDKQISKCLGLTEAQTRELRLKKNIHPWVKQIDTLAAEYPSVTNYLYV
TYNGQEHDVNFDDHGMMVLGCGPYHIGSSVEFDWCAVSSIRTLRQLGKKTVVVNCNPETV
STDFDECDKLYFEELSLERILDIYHQEACGGCIISVGGQIPNNLAVPLYKNGVKIMGTSP
LQIDRAEDRSIFSAVLDELKVAQAPWKAVNTLNEALEFAKSVDYPCLLRPSYVLSGSAMN
VVFSEDEMKKFLEEATRVSQEHPVVLTKFVEGAREVEMDAVGKDGRVISHAISEHVEDAG
VHSGDATLMLPTQTISQGAIEKVKDATRKIAKAFAISGPFNVQFLVKGNDVLVIECNLRA
SRSFPFVSKTLGVDFIDVATKVMIGENVDEKHLPTLDHPIIPADYVAIKAPMFSWPRLRD
ADPILRCEMASTGEVACFGEGIHTAFLKAMLSTGFKIPQKGILIGIQQSFRPRFLGVAEQ
LHNEGFKLFATEATSDWLNANNVPATPVAWPSQEGQNPSLSSIRKLIRDGSIDLVINLPN
NNTKFVHDNYVIRRTAVDSGIPLLTNFQVTKLFAEAVQKSRKVDSKSLFHYRQYSAGKAA
|
| Enzyme 114 Number of Residues |
1500 |
| Enzyme 114 Molecular Weight |
164938.1 |
| Enzyme 114 Theoretical pI |
6.71 |
| Enzyme 114 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- carbamoyl-phosphate synthase activity
- catalytic activity
- ligase activity
- ligase activity, forming carbon-nitrogen bonds
- nucleoside binding
- purine nucleoside binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- glutamine family amino acid metabolic process
- glutamine metabolic process
- metabolic process
- nitrogen compound metabolic process
|
| Component |
| — |
|
| Enzyme 114 General Function |
Involved in catalytic activity |
| Enzyme 114 Specific Function |
Involved in the urea cycle of ureotelic animals where the enzyme plays an important role in removing excess ammonia from the cell |
| Enzyme 114 Pathways |
|
| Enzyme 114 Reactions |
- 2 ATP + NH3 + CO2 + H2O = 2 ADP + phosphate + carbamoyl phosphate [RN:R00149]
|
| Enzyme 114 Pfam Domain Function |
|
| Enzyme 114 Signals |
|
| Enzyme 114 Transmembrane Regions |
|
| Enzyme 114 Essentiality |
Not Available |
| Enzyme 114 GenBank ID Protein |
5020420 |
| Enzyme 114 UniProtKB/Swiss-Prot ID |
P31327 |
| Enzyme 114 UniProtKB/Swiss-Prot Entry Name |
CPSM_HUMAN |
| Enzyme 114 PDB ID |
Not Available |
| Enzyme 114 Cellular Location |
Not Available |
| Enzyme 114 Gene Sequence |
>4503 bp
ATGACGAGGATTTTGACAGCTTTCAAAGTGGTGAGGACACTGAAGACTGGTTTTGGCTTT
ACCAATGTGACTGCACACCAAAAATGGAAATTTTCAAGACCTGGCATCAGGCTCCTTTCT
GTCAAGGCACAGACAGCACACATTGTCCTGGAAGATGGAACTAAGATGAAAGGTTACTCC
TTTGGCCATCCATCCTCTGTTGCTGGTGAAGTGGTTTTTAATACTGGCCTGGGAGGGTAC
CCAGAAGCTATTACTGACCCTGCCTACAAAGGACAGATTCTCACAATGGCCAACCCTATT
ATTGGGAATGGTGGAGCTCCTGATACTACTGCTCTGGATGAACTGGGACTTAGCAAATAT
TTGGAGTCTAATGGAATCAAGGTTTCAGGTTTGCTGGTGCTGGATTATAGTAAAGACTAC
AACCACTGGCTGGCTACCAAGAGTTTAGGGCAATGGCTACAGGAAGAAAAGGTTCCTGCA
ATTTATGGAGTGGACACAAGAATGCTGACTAAAATAATTCGGGATAAGGGTACCATGCTT
GGGAAGATTGAATTTGAAGGTCAGCCTGTGGATTTTGTGGATCCAAATAAACAGAATTTG
ATTGCTGAGGTTTCAACCAAGGATGTCAAAGTGTACGGCAAAGGAAACCCCACAAAAGTG
GTAGCTGTAGACTGTGGGATTAAAAACAATGTAATCCGCCTGCTAGTAAAGCGAGGAGCT
GAAGTGCACTTAGTTCCCTGGAACCATGATTTCACCAAGATGGAGTATGATGGGATTTTG
ATCGCGGGAGGACCGGGGAACCCAGCTCTTGCAGAACCACTAATTCAGAATGTCAGAAAG
ATTTTGGAGAGTGATCGCAAGGAGCCATTGTTTGGAATCAGTACAGGAAACTTAATAACA
GGATTGGCTGCTGGTGCCAAAACCTACAAGATGTCCATGGCCAACAGAGGGCAGAATCAG
CCTGTTTTGAATATCACAAACAAACAGGCTTTCATTACTGCTCAGAATCATGGCTATGCC
TTGGACAACACCCTCCCTGCTGGCTGGAAACCACTTTTTGTGAATGTCAACGATCAAACA
AATGAGGGGATTATGCATGAGAGCAAACCCTTCTTCGCTGTGCAGTTCCACCCAGAGGTC
ACCCCGGGGCCAATAGACACTGAGTACCTGTTTGATTCCTTTTTCTCACTGATAAAGAAA
GGAAAAGCTACCACCATTACATCAGTCTTACCGAAGCCAGCACTAGTTGCATCTCGGGTT
GAGGTTTCCAAAGTCCTTATTCTAGGATCAGGAGGTCTGTCCATTGGTCAGGCTGGAGAA
TTTGATTACTCAGGATCTCAAGCTGTAAAAGCCATGAAGGAAGAAAATGTCAAAACTGTT
CTGATGAACCCAAACATTGCATCAGTCCAGACCAATGAGGTGGGCTTAAAGCAAGCGGAT
ACTGTCTACTTTCTTCCCATCACCCCTCAGTTTGTCACAGAGGTCATCAAGGCAGAACAG
CCAGATGGGTTAATTCTGGGCATGGGTGGCCAGACAGCTCTGAACTGTGGAGTGGAACTA
TTCAAGAGAGGTGTGCTCAAGGAATATGGTGTGAAAGTCCTGGGAACTTCAGTTGAGTCC
ATTATGGCTACGGAAGACAGGCAGCTGTTTTCAGATAAACTAAATGAGATCAATGAAAAG
ATTGCTCCAAGTTTTGCAGTGGAATCGATTGAGGATGCACTGAAGGCAGCAGACACCATT
GGCTACCCAGTGATGATCCGTTCCGCCTATGCACTGGGTGGGTTAGGCTCAGGCATCTGT
CCCAACAGAGAGACTTTGATGGACCTCAGCACAAAGGCCTTTGCTATGACCAACCAAATT
CTGGTGGAGAAGTCAGTGACAGGTTGGAAAGAAATAGAATATGAAGTGGTTCGAGATGCT
GATGACAATTGTGTCACTGTCTGTAACATGGAAAATGTTGATGCCATGGGTGTTCACACA
GGTGACTCAGTTGTTGTGGCTCCTGCCCAGACACTCTCCAATGCCGAGTTTCAGATGTTG
AGACGTACTTCAATCAATGTTGTTCGCCACTTGGGCATTGTGGGTGAATGCAACATTCAG
TTTGCCCTTCATCCTACCTCAATGGAATACTGCATCATTGAAGTGAATGCCAGACTGTCC
CGAAGCTCTGCTCTGGCCTCAAAAGCCACTGGCTACCCATTGGCATTCATTGCTGCAAAG
ATTGCCCTAGGAATCCCACTTCCAGAAATTAAGAACGTCGTATCCGGGAAGACATCAGCC
TGTTTTGAACCTAGCCTGGATTACATGGTCACCAAGATTCCCCGCTGGGATCTTGACCGT
TTTCATGGAACATCTAGCCGAATTGGTAGCTCTATGAAAAGTGTAGGAGAGGTCATGGCT
ATTGGTCGTACCTTTGAGGAGAGTTTCCAGAAAGCTTTACGGATGTGCCACCCATCTATA
GAAGGTTTCACTCCCCGTCTCCCAATGAACAAAGAATGGCCATCTAATTTAGATCTTAGA
AAAGAGTTGTCTGAACCAAGCAGCACGCGTATCTATGCCATTGCCAAGGCCATTGATGAC
AACATGTCCCTTGATGAGATTGAGAAGCTCACATACATTGACAAGTGGTTTTTGTATAAG
ATGCGTGATATTTTAAACATGGAAAAGACACTGAAAGGGCTCAACAGTGAGTCCATGACA
GAAGAAACCCTGAAAAGGGCAAAGGAGATTGGGTTCTCAGATAAGCAGATTTCAAAATGC
CTTGGGCTCACTGAGGCCCAGACAAGGGAGCTGAGGTTAAAGAAAAACATCCACCCTTGG
GTTAAACAGATTGATACACTGGCTGCAGAATACCCATCAGTAACAAACTATCTCTATGTT
ACCTACAATGGTCAGGAGCATGATGTCAATTTTGATGACCATGGAATGATGGTGCTAGGC
TGTGGTCCATATCACATTGGCAGCAGTGTGGAATTTGATTGGTGTGCTGTCTCTAGTATC
CGCACACTGCGTCAACTTGGCAAGAAGACGGTGGTGGTGAATTGCAATCCTGAGACTGTG
AGCACAGACTTTGATGAGTGTGACAAACTGTACTTTGAAGAGTTGTCCTTGGAGAGAATC
CTAGACATCTACCATCAGGAGGCATGTGGTGGCTGCATCATATCAGTTGGAGGCCAGATT
CCAAACAACCTGGCAGTTCCTCTATACAAGAATGGTGTCAAGATCATGGGCACAAGCCCC
CTGCAGATCGACAGGGCTGAGGATCGCTCCATCTTCTCAGCTGTCTTGGATGAGCTGAAG
GTGGCTCAGGCACCTTGGAAAGCTGTTAATACTTTGAATGAAGCACTGGAATTTGCAAAG
TCTGTGGACTACCCCTGCTTGTTGAGGCCTTCCTATGTTTTGAGTGGGTCTGCTATGAAT
GTGGTATTCTCTGAGGATGAGATGAAAAAATTCCTAGAAGAGGCGACTAGAGTTTCTCAG
GAGCACCCAGTGGTCCTGACAAAATTTGTTGAAGGGGCCCGAGAAGTAGAAATGGACGCT
GTTGGCAAAGATGGAAGGGTTATCTCTCATGCCATCTCTGAACATGTTGAAGATGCAGGT
GTCCACTCGGGAGATGCCACTCTGATGCTGCCCACACAAACCATCAGCCAAGGGGCCATT
GAAAAGGTGAAGGATGCTACCCGGAAGATTGCAAAGGCTTTTGCCATCTCTGGTCCATTC
AACGTCCAATTTCTTGTCAAAGGAAATGATGTCTTGGTGATTGAGTGTAACTTGAGAGCT
TCTCGATCCTTCCCCTTTGTTTCCAAGACTCTTGGGGTTGACTTCATTGATGTGGCCACC
AAGGTGATGATTGGAGAGAATGTTGATGAGAAACATCTTCCAACATTGGACCATCCCATA
ATTCCTGCTGACTATGTTGCAATTAAGGCTCCCATGTTTTCCTGGCCCCGGTTGAGGGAT
GCTGACCCCATTCTGAGATGTGAGATGGCTTCCACTGGAGAGGTGGCTTGCTTTGGTGAA
GGTATTCATACAGCCTTCCTAAAGGCAATGCTTTCCACAGGATTTAAGATACCCCAGAAA
GGCATCCTGATAGGCATCCAGCAATCATTCCGGCCAAGATTCCTTGGTGTGGCTGAACAA
TTACACAATGAAGGTTTCAAGCTGTTTGCCACGGAAGCCACATCAGACTGGCTCAACGCC
AACAATGTCCCTGCCACCCCAGTGGCATGGCCGTCTCAAGAAGGACAGAATCCCAGCCTC
TCTTCCATCAGAAAATTGATTAGAGATGGCAGCATTGACCTAGTGATTAACCTTCCCAAC
AACAACACTAAATTTGTCCATGATAATTATGTGATTCGGAGGACAGCTGTTGATAGTGGA
ATCCCTCTCCTCACTAATTTTCAGGTGACCAAACTTTTTGCTGAAGCTGTGCAGAAATCT
CGCAAGGTGGACTCCAAGAGTCTTTTCCACTACAGGCAGTACAGTGCTGGAAAAGCAGCA
TAG
|
| Enzyme 114 GenBank Gene ID |
AF154830 |
| Enzyme 114 GeneCard ID |
CPS1 |
| Enzyme 114 GenAtlas ID |
CPS1 |
| Enzyme 114 HGNC ID |
HGNC:2323 |
| Enzyme 114 Chromosome Location |
2 |
| Enzyme 114 Locus |
2q35 |
| Enzyme 114 SNPs |
SNPJam Report |
| Enzyme 114 General References |
- Haraguchi Y, Uchino T, Takiguchi M, Endo F, Mori M, Matsuda I: Cloning and sequence of a cDNA encoding human carbamyl phosphate synthetase I: molecular analysis of hyperammonemia. Gene. 1991 Nov 15;107(2):335-40. [PubMed ]
- Finckh U, Kohlschutter A, Schafer H, Sperhake K, Colombo JP, Gal A: Prenatal diagnosis of carbamoyl phosphate synthetase I deficiency by identification of a missense mutation in CPS1. Hum Mutat. 1998;12(3):206-11. [PubMed ]
- Summar ML, Hall LD, Eeds AM, Hutcheson HB, Kuo AN, Willis AS, Rubio V, Arvin MK, Schofield JP, Dawson EP: Characterization of genomic structure and polymorphisms in the human carbamyl phosphate synthetase I gene. Gene. 2003 Jun 5;311:51-7. [PubMed ]
- Funghini S, Donati MA, Pasquini E, Zammarchi E, Morrone A: Structural organization of the human carbamyl phosphate synthetase I gene (CPS1) and identification of two novel genetic lesions. Hum Mutat. 2003 Oct;22(4):340-1. [PubMed ]
- Haberle J, Schmidt E, Pauli S, Rapp B, Christensen E, Wermuth B, Koch HG: Gene structure of human carbamylphosphate synthetase 1 and novel mutations in patients with neonatal onset. Hum Mutat. 2003 Apr;21(4):444. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed ]
- Aoshima T, Kajita M, Sekido Y, Kikuchi S, Yasuda I, Saheki T, Watanabe K, Shimokata K, Niwa T: Novel mutations (H337R and 238-362del) in the CPS1 gene cause carbamoyl phosphate synthetase I deficiency. Hum Hered. 2001;52(2):99-101. [PubMed ]
- Pearson DL, Dawling S, Walsh WF, Haines JL, Christman BW, Bazyk A, Scott N, Summar ML: Neonatal pulmonary hypertension--urea-cycle intermediates, nitric oxide production, and carbamoyl-phosphate synthetase function. N Engl J Med. 2001 Jun 14;344(24):1832-8. [PubMed ]
- Wakutani Y, Nakayasu H, Takeshima T, Adachi M, Kawataki M, Kihira K, Sawada H, Bonno M, Yamamoto H, Nakashima K: Mutational analysis of carbamoylphosphate synthetase I deficiency in three Japanese patients. J Inherit Metab Dis. 2004;27(6):787-8. [PubMed ]
- Haberle J, Koch HG: Genetic approach to prenatal diagnosis in urea cycle defects. Prenat Diagn. 2004 May;24(5):378-83. [PubMed ]
- Kurokawa K, Yorifuji T, Kawai M, Momoi T, Nagasaka H, Takayanagi M, Kobayashi K, Yoshino M, Kosho T, Adachi M, Otsuka H, Yamamoto S, Murata T, Suenaga A, Ishii T, Terada K, Shimura N, Kiwaki K, Shintaku H, Yamakawa M, Nakabayashi H, Wakutani Y, Nakahata T: Molecular and clinical analyses of Japanese patients with carbamoylphosphate synthetase 1 (CPS1) deficiency. J Hum Genet. 2007;52(4):349-54. Epub 2007 Feb 20. [PubMed ]
- Moonen RM, Reyes I, Cavallaro G, Gonzalez-Luis G, Bakker JA, Villamor E: The T1405N carbamoyl phosphate synthetase polymorphism does not affect plasma arginine concentrations in preterm infants. PLoS One. 2010 May 25;5(5):e10792. [PubMed ]
|
| Enzyme 114 Metabolite References |
Not Available |
|
Enzyme 115
[top]
|
| Enzyme 115 ID |
5597 |
| Enzyme 115 Name |
Type I inositol-1,4,5-trisphosphate 5-phosphatase |
| Enzyme 115 Synonyms |
- 5PTase
|
| Enzyme 115 Gene Name |
INPP5A |
| Enzyme 115 Protein Sequence |
>Type I inositol-1,4,5-trisphosphate 5-phosphatase
MAGKAAAPGTAVLLVTANVGSLFDDPENLQKNWLREFYQVVHTHKPHFMALHCQEFGGKN
YEASMSHVDKFVKELLSSDAMKEYNRARVYLDENYKSQEHFTALGSFYFLHESLKNIYQF
DFKAKKYRKVAGKEIYSDTLESTPMLEKEKFPQDYFPECKWSRKGFIRTRWCIADCAFDL
VNIHLFHDASNLVAWETSPSVYSGIRHKALGYVLDRIIDQRFEKVSYFVFGDFNFRLDSK
SVVETLCTKATMQTVRAADTNEVVKLIFRESDNDRKVMLQLEKKLFDYFNQEVFRDNNGT
ALLEFDKELSVFKDRLYELDISFPPSYPYSEDARQGEQYMNTRCPAWCDRILMSPSAKEL
VLRSESEEKVVTYDHIGPNVCMGDHKPVFLAFRIMPGAGKPHAHVHKCCVVQ
|
| Enzyme 115 Number of Residues |
412 |
| Enzyme 115 Molecular Weight |
47819.2 |
| Enzyme 115 Theoretical pI |
7.04 |
| Enzyme 115 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 115 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 115 Specific Function |
Major isoenzyme hydrolyzing the calcium-mobilizing second messenger Ins(1,4,5)P3, this is a signal-terminating reaction |
| Enzyme 115 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 115 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
|
| Enzyme 115 Pfam Domain Function |
|
| Enzyme 115 Signals |
|
| Enzyme 115 Transmembrane Regions |
|
| Enzyme 115 Essentiality |
Not Available |
| Enzyme 115 GenBank ID Protein |
57209040 |
| Enzyme 115 UniProtKB/Swiss-Prot ID |
Q14642 |
| Enzyme 115 UniProtKB/Swiss-Prot Entry Name |
I5P1_HUMAN |
| Enzyme 115 PDB ID |
Not Available |
| Enzyme 115 Cellular Location |
Not Available |
| Enzyme 115 Gene Sequence |
>1239 bp
ATGGCGGGGAAGGCGGCCGCCCCGGGCACCGCGGTGCTGCTGGTCACGGCCAACGTGGGC
TCGCTCTTCGACGACCCAGAAAACCTGCAGAAGAACTGGCTTCGGGAATTTTACCAGGTC
GTGCACACACACAAGCCGCACTTCATGGCCTTGCACTGTCAGGAGTTTGGAGGGAAGAAC
TACGAGGCCTCCATGTCCCACGTGGACAAGTTCGTCAAAGAACTATTGTCGAGTGATGCG
ATGAAAGAATATAACAGGGCTCGAGTCTACCTGGATGAAAACTACAAATCCCAGGAGCAC
TTCACGGCACTAGGAAGCTTTTATTTTCTTCATGAGTCCTTAAAAAACATCTACCAGTTT
GACTTTAAAGCTAAGAAGTATAGAAAGGTCGCTGGCAAAGAGATCTACTCGGATACCTTA
GAGAGCACGCCCATGCTGGAGAAGGAGAAGTTTCCGCAGGACTACTTCCCCGAGTGCAAA
TGGTCAAGAAAAGGCTTCATCCGGACGAGGTGGTGCATTGCAGACTGTGCCTTTGACTTG
GTGAATATCCATCTTTTCCATGATGCTTCCAATCTGGTCGCCTGGGAAACAAGCCCTTCC
GTGTACTCGGGAATCCGGCACAAGGCACTGGGCTACGTGCTGGACAGAATCATTGATCAG
CGATTCGAGAAGGTTTCCTACTTTGTATTTGGTGATTTCAACTTCCGGCTGGATTCCAAG
TCCGTCGTGGAGACGCTCTGCACAAAAGCCACCATGCAGACGGTCCGGGCCGCCGACACC
AATGAAGTGGTGAAGCTCATATTTCGTGAGTCGGACAACGACCGGAAGGTTATGCTCCAG
TTAGAAAAGAAACTCTTCGACTACTTCAACCAGGAGGTTTTCCGAGACAACAACGGCACC
GCGCTCTTGGAGTTTGACAAGGAGTTGTCTGTCTTTAAGGACAGACTGTATGAACTGGAC
ATCTCGTTCCCTCCCAGCTACCCGTACAGTGAGGACGCCCGCCAGGGTGAGCAGTACATG
AACACCCGGTGCCCAGCCTGGTGTGACCGCATCCTCATGTCCCCGTCTGCCAAGGAGCTG
GTGCTGCGGTCGGAGAGCGAGGAGAAGGTTGTCACCTATGACCACATTGGGCCCAACGTC
TGCATGGGAGACCACAAGCCCGTGTTCCTGGCCTTCCGAATCATGCCCGGGGCAGGTAAA
CCTCATGCCCATGTGCACAAGTGTTGTGTCGTGCAGTGA
|
| Enzyme 115 GenBank Gene ID |
AL356603 |
| Enzyme 115 GeneCard ID |
INPP5A |
| Enzyme 115 GenAtlas ID |
INPP5A |
| Enzyme 115 HGNC ID |
HGNC:6076 |
| Enzyme 115 Chromosome Location |
1 |
| Enzyme 115 Locus |
10q26.3 |
| Enzyme 115 SNPs |
SNPJam Report |
| Enzyme 115 General References |
- De Smedt F, Verjans B, Mailleux P, Erneux C: Cloning and expression of human brain type I inositol 1,4,5-trisphosphate 5-phosphatase. High levels of mRNA in cerebellar Purkinje cells. FEBS Lett. 1994 Jun 20;347(1):69-72. [PubMed ]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Laxminarayan KM, Chan BK, Tetaz T, Bird PI, Mitchell CA: Characterization of a cDNA encoding the 43-kDa membrane-associated inositol-polyphosphate 5-phosphatase. J Biol Chem. 1994 Jun 24;269(25):17305-10. [PubMed ]
|
| Enzyme 115 Metabolite References |
Not Available |
|
Enzyme 116
[top]
|
| Enzyme 116 ID |
5598 |
| Enzyme 116 Name |
Inositol polyphosphate 1-phosphatase |
| Enzyme 116 Synonyms |
- IPP
- IPPase
|
| Enzyme 116 Gene Name |
INPP1 |
| Enzyme 116 Protein Sequence |
>Inositol polyphosphate 1-phosphatase
MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEV
IKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEA
LARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQ
CVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRR
NGSETHTGNTGSEAAFSPSFSAVISTSEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQG
LVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGA
AGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT
|
| Enzyme 116 Number of Residues |
399 |
| Enzyme 116 Molecular Weight |
43997.6 |
| Enzyme 116 Theoretical pI |
4.91 |
| Enzyme 116 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 116 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 116 Specific Function |
1D-myo-inositol 1,4-bisphosphate + H(2)O = 1D- myo-inositol 4-phosphate + phosphate |
| Enzyme 116 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 116 Reactions |
- 1D-myo-inositol 1,4-bisphosphate + H2O = 1D-myo-inositol 4-phosphate + phosphate [RN:R03393]
|
| Enzyme 116 Pfam Domain Function |
|
| Enzyme 116 Signals |
|
| Enzyme 116 Transmembrane Regions |
|
| Enzyme 116 Essentiality |
Not Available |
| Enzyme 116 GenBank ID Protein |
Not Available |
| Enzyme 116 UniProtKB/Swiss-Prot ID |
P49441 |
| Enzyme 116 UniProtKB/Swiss-Prot Entry Name |
INPP_HUMAN |
| Enzyme 116 PDB ID |
Not Available |
| Enzyme 116 Cellular Location |
Not Available |
| Enzyme 116 Gene Sequence |
>1200 bp
ATGTCAGATATCCTCCGGGAGCTGCTCTGTGTCTCTGAGAAGGCTGCTAACATTGCCCGG
GCGTGCAGACAGCAGGAAGCCCTCTTCCAGCTGCTGATCGAAGAAAAGAAAGAGGGAGAA
AAGAACAAGAAGTTTGCAGTTGACTTCAAGACTCTGGCTGATGTACTGGTACAGGAAGTT
ATAAAACAGAATATGGAGAACAAGTTTCCAGGCTTGGAAAAAAATATTTTTGGAGAAGAA
TCCAATGAGTTTACTAATGACTGGGGGGAAAAGATTACCTTGAGGTTGTGTTCAACAGAG
GAAGAAACAGCAGAGCTTCTTAGCAAAGTCCTCAATGGTAACAAGGTAGCATCTGAAGCA
TTAGCCAGGGTTGTTCATCAGGATGTTGCCTTTACTGACCCAACTCTGGATTCCACAGAG
ATCAATGTTCCACAGGACATTTTGGGAATTTGGGTGGACCCCATAGATTCAACTTATCAG
TATATAAAAGGTTCTGCTGACATTAAATCCAACCAGGGAATCTTCCCCTGTGGACTTCAG
TGTGTCACCATTTTAATTGGTGTCTATGACATACAGACAGGGGTTCCCCTGATGGGAGTC
ATCAATCAACCTTTTGTGTCACGAGATCCAAACACCCTCAGGTGGAAAGGACAGTGCTAT
TGGGGCCTTTCTTACATGGGGACCAACATGCATTCACTACAGCTCACCATCTCTAGAAGA
AACGGCAGTGAAACACACACTGGAAACACCGGCTCTGAGGCAGCATTCTCCCCCAGTTTT
TCAGCCGTAATTAGTACAAGTGAAAAGGAGACTATCAAAGCTGCATTGTCACGTGTGTGT
GGAGATCGCATATTTGGGGCAGCTGGGGCTGGTTATAAGAGCCTATGTGTTGTCCAAGGC
CTCGTTGACATTTACATCTTTTCAGAAGATACCACATTCAAATGGGACTCTTGTGCTGCT
CATGCCATACTGCGGGCCATGGGTGGGGGAATAGTAGACTTGAAAGAATGCTTAGAAAGA
AATCCAGAAACAGGGCTTGATTTGCCACAGTTGGTGTACCACGTGGAAAATGAGGGTGCT
GCTGGGGTGGATCGGTGGGCCAACAAGGGAGGACTCATTGCATACAGATCCAGGAAGCGG
CTGGAGACATTCCTGAGCCTCCTGGTCCAAAACCTGGCACCTGCAGAGACGCATACCTAG
|
| Enzyme 116 GenBank Gene ID |
L08488 |
| Enzyme 116 GeneCard ID |
INPP1 |
| Enzyme 116 GenAtlas ID |
INPP1 |
| Enzyme 116 HGNC ID |
HGNC:6071 |
| Enzyme 116 Chromosome Location |
2 |
| Enzyme 116 Locus |
2q32 |
| Enzyme 116 SNPs |
SNPJam Report |
| Enzyme 116 General References |
- York JD, Veile RA, Donis-Keller H, Majerus PW: Cloning, heterologous expression, and chromosomal localization of human inositol polyphosphate 1-phosphatase. Proc Natl Acad Sci U S A. 1993 Jun 15;90(12):5833-7. [PubMed ]
- Lovlie R, Gulbrandsen AK, Molven A, Steen VM: Genomic structure and sequence analysis of a human inositol polyphosphate 1-phosphatase gene (INPP1). Pharmacogenetics. 1999 Aug;9(4):517-28. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
- Steen VM, Lovlie R, Osher Y, Belmaker RH, Berle JO, Gulbrandsen AK: The polymorphic inositol polyphosphate 1-phosphatase gene as a candidate for pharmacogenetic prediction of lithium-responsive manic-depressive illness. Pharmacogenetics. 1998 Jun;8(3):259-68. [PubMed ]
|
| Enzyme 116 Metabolite References |
Not Available |
|
Enzyme 117
[top]
|
| Enzyme 117 ID |
5599 |
| Enzyme 117 Name |
Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A |
| Enzyme 117 Synonyms |
- Inositol polyphosphate 5-phosphatase J
|
| Enzyme 117 Gene Name |
INPP5J |
| Enzyme 117 Protein Sequence |
>Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
MEGQSSRGSRRPGTRAGLGSLPMPQGVAQTGAPSKVDSSFQLPAKKNAALGPSEPRLALA
PVGPRAAMSASSEGPRLALASPRPILAPLCTPEGQKTATAHRSSSLAPTSVGQLVMSASA
GPKPPPATTGSVLAPTSLGLVMPASAGPRSPPVTLGPNLAPTSRDQKQEPPASVGPKPTL
AASGLSLALASEEQPPELPSTPSPVPSPVLSPTQEQALAPASTASGAASVGQTSARKRDA
PAPRPLPASEGHLQPPAQTSGPTGSPPCIQTSPDPRLSPSFRARPEALHSSPEDPVLPRP
PQTLPLDVGQGPSEPGTHSPGLLSPTFRPGAPSGQTVPPPLPKPPRSPSRSPSHSPNRSP
CVPPAPDMALPRLGTQSTGPGRCLSPNLQAQEAPAPVTTSSSTSTLSSSPWSAQPTWKSD
PGFRITVVTWNVGTAMPPDDVTSLLHLGGGDDSDGADMIAIGLQEVNSMLNKRLKDALFT
DQWSELFMDALGPFNFVLVSSVRMQGVILLLFAKYYHLPFLRDVQTDCTRTGLGGYWGNK
GGVSVRLAAFGHMLCFLNCHLPAHMDKAEQRKDNFQTILSLQQFQGPGAQGILDHDLVFW
FGDLNFRIESYDLHFVKFAIDSDQLHQLWEKDQLNMAKNTWPILKGFQEGPLNFAPTFKF
DVGTNKYDTSAKKRKPAWTDRILWKVKAPGGGPSPSGRKSHRLQVTQHSYRSHMEYTVSD
HKPVAAQFLLQFAFRDDMPLVRLEVADEWVRPEQAVVRYRMETVFARSSWDWIGLYRVGF
RHCKDYVAYVWAKHEDVDGNTYQVTFSEESLPKGHGDFILGYYSHNHSILIGITEPFQIS
LPSSELASSSTDSSGTSSEGEDDSTLELLAPKSRSPSPGKSKRHRSRSPGLARFPGLALR
PSSRERRGASRSPSPQSRRLSRVAPDRSSNGSSRGSSEEGPSGLPGPWAFPPAVPRSLGL
LPALRLETVDPGGGGSWGPDREALAPNSLSPSPQGHRGLEEGGLGP
|
| Enzyme 117 Number of Residues |
1006 |
| Enzyme 117 Molecular Weight |
107195.7 |
| Enzyme 117 Theoretical pI |
9.53 |
| Enzyme 117 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 117 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 117 Specific Function |
Inositol 5-phosphatase, which converts inositol 1,4,5- trisphosphate to inositol 1,4-bisphosphate. Also converts phosphatidylinositol 4,5-bisphosphate to phosphatidylinositol 4- phosphate and inositol 1,3,4,5-tetrakisphosphate to inositol 1,3,4-trisphosphate in vitro. May be involved in modulation of the function of inositol and phosphatidylinositol polyphosphate- binding proteins that are present at membranes ruffles |
| Enzyme 117 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 117 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
|
| Enzyme 117 Pfam Domain Function |
|
| Enzyme 117 Signals |
|
| Enzyme 117 Transmembrane Regions |
|
| Enzyme 117 Essentiality |
Not Available |
| Enzyme 117 GenBank ID Protein |
50726960 |
| Enzyme 117 UniProtKB/Swiss-Prot ID |
Q15735 |
| Enzyme 117 UniProtKB/Swiss-Prot Entry Name |
PI5PA_HUMAN |
| Enzyme 117 PDB ID |
Not Available |
| Enzyme 117 Cellular Location |
Not Available |
| Enzyme 117 Gene Sequence |
Not Available |
| Enzyme 117 GenBank Gene ID |
Not Available |
| Enzyme 117 GeneCard ID |
INPP5J |
| Enzyme 117 GenAtlas ID |
INPP5J |
| Enzyme 117 HGNC ID |
HGNC:8956 |
| Enzyme 117 Chromosome Location |
2 |
| Enzyme 117 Locus |
22q12.2 |
| Enzyme 117 SNPs |
SNPJam Report |
| Enzyme 117 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed ]
|
| Enzyme 117 Metabolite References |
Not Available |
|
Enzyme 118
[top]
|
| Enzyme 118 ID |
5600 |
| Enzyme 118 Name |
Inositol polyphosphate 5-phosphatase K |
| Enzyme 118 Synonyms |
- Skeletal muscle and kidney-enriched inositol phosphatase
|
| Enzyme 118 Gene Name |
INPP5K |
| Enzyme 118 Protein Sequence |
>Inositol polyphosphate 5-phosphatase K
MSSRKLSGPKGRRLSIHVVTWNVASAAPPLDLSDLLQLNNRNLNLDIYVIGLQELNSGII
SLLSDAAFNDSWSSFLMDVLSPLSFIKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPT
GLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNCEGRDIPN
ILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYGGLWEKDQLSIAKKHDPLLREFQEGR
LLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQPCAGPDTPIPPASHFSLSLRGY
SSHMTYGISDHKPVSGTFDLELKPLVSAPLIVLMPEDLWTVENDMMVSYSSTSDFPSSPW
DWIGLYKVGLRDVNDYVSYAWVGDSKVSCSDNLNQVYIDISNIPTTEDEFLLCYYSNSLR
SVVGISRPFQIPPGSLREDPLGEAQPQI
|
| Enzyme 118 Number of Residues |
448 |
| Enzyme 118 Molecular Weight |
51089.8 |
| Enzyme 118 Theoretical pI |
6.51 |
| Enzyme 118 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 118 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 118 Specific Function |
Inositol 5-phosphatase which acts on inositol 1,4,5- trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-triphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5- trisphosphate. May negatively regulate assembly of the actin cytoskeleton |
| Enzyme 118 Pathways |
- Inositol Metabolism (map00562 )
- Phosphatidylinositol signaling system (map04070 )
|
| Enzyme 118 Reactions |
- (1) D-myo-inositol 1,4,5-trisphosphate + H2O = myo-inositol 1,4-bisphosphate + phosphate [RN:R03394]
- (2) 1D-myo-inositol 1,3,4,5-tetrakisphosphate + H2O = 1D-myo-inositol 1,3,4-trisphosphate + phosphate [RN:R03430]
|
| Enzyme 118 Pfam Domain Function |
|
| Enzyme 118 Signals |
|
| Enzyme 118 Transmembrane Regions |
|
| Enzyme 118 Essentiality |
Not Available |
| Enzyme 118 GenBank ID Protein |
7209855 |
| Enzyme 118 UniProtKB/Swiss-Prot ID |
Q9BT40 |
| Enzyme 118 UniProtKB/Swiss-Prot Entry Name |
INP5K_HUMAN |
| Enzyme 118 PDB ID |
Not Available |
| Enzyme 118 Cellular Location |
Not Available |
| Enzyme 118 Gene Sequence |
>1347 bp
ATGAGCTCGCGGAAGCTGAGCGGGCCGAAAGGCAGGAGGCTCAGCATACACGTCGTGACT
TGGAACGTGGCTTCGGCAGCGCCCCCTCTAGATCTCAGTGACCTGCTTCAGCTGAACAAC
CGGAACCTCAATCTTGACATATATGTTATTGGTTTGCAGGAATTGAACTCTGGGATCATA
AGCCTCCTTTCCGATGCTGCCTTTAATGACTCGTGGAGCAGTTTCCTCATGGATGTGCTT
TCCCCTCTGAGCTTCATCAAGGTCTCCCATGTCCGTATGCAGGGGATCCTCTTACTGGTC
TTTGCCAAGTATCAGCATTTGCCCTATATCCAGATTCTGTCTACTAAATCCACCCCCACT
GGCCTGTTTGGGTACTGGGGGAACAAAGGTGGAGTCAACATCTGCCTGAAGCTTTATGGC
TACTATGTCAGCATCATCAACTGCCACCTGCCTCCCCACATTTCCAACAATTACCAGCGG
CTGGAGCACTTTGACCGGATCCTGGAGATGCAGAATTGTGAGGGGCGAGACATCCCAAAC
ATCCTGGACCACGACCTCATTATCTGGTTTGGAGACATGAACTTTCGGATCGAGGACTTT
GGGTTGCACTTTGTTCGGGAATCCATTAAAAATCGGTGCTACGGTGGCCTGTGGGAGAAG
GACCAGCTCAGCATTGCCAAGAAACATGACCCGCTGCTCCGGGAGTTCCAGGAGGGCCGC
CTACTCTTCCCGCCCACCTACAAGTTTGATAGGAACTCCAACGACTATGACACCAGTGAG
AAAAAACGCAAGCCTGCATGGACCGATCGCATCCTGTGGAGGCTGAAGCGGCAGCCCTGT
GCTGGCCCCGACACTCCCATACCGCCGGCGTCACACTTCTCCTTGTCTCTGAGGGGCTAC
AGCAGCCACATGACGTACGGCATCAGCGACCACAAGCCTGTCTCCGGCACGTTCGACTTG
GAGCTGAAGCCATTGGTGTCTGCTCCGCTGATCGTCCTGATGCCCGAGGACCTGTGGACC
GTGGAAAATGACATGATGGTCAGCTACTCTTCAACCTCGGACTTCCCCAGCAGCCCGTGG
GACTGGATTGGACTGTACAAGGTGGGGCTGCGGGACGTTAATGACTACGTGTCCTATGCC
TGGGTCGGGGACAGCAAGGTCTCCTGCAGCGACAACCTGAACCAGGTTTACATCGACATC
AGCAATATCCCTACCACTGAAGATGAGTTTCTCCTCTGTTACTACAGAAACAGTCTGCGT
TCTGTGGTGGGGATAAGAAGACCCTTCCAGATCCCGCCTGGCTCCTTGAGGGAGGACCCA
CTGGGTGAAGCACAGCCACAGATCTGA
|
| Enzyme 118 GenBank Gene ID |
AB036829 |
| Enzyme 118 GeneCard ID |
INPP5K |
| Enzyme 118 GenAtlas ID |
INPP5K |
| Enzyme 118 HGNC ID |
HGNC:33882 |
| Enzyme 118 Chromosome Location |
1 |
| Enzyme 118 Locus |
17p13.3 |
| Enzyme 118 SNPs |
SNPJam Report |
| Enzyme 118 General References |
- Ijuin T, Mochizuki Y, Fukami K, Funaki M, Asano T, Takenawa T: Identification and characterization of a novel inositol polyphosphate 5-phosphatase. J Biol Chem. 2000 Apr 14;275(15):10870-5. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Gurung R, Tan A, Ooms LM, McGrath MJ, Huysmans RD, Munday AD, Prescott M, Whisstock JC, Mitchell CA: Identification of a novel domain in two mammalian inositol-polyphosphate 5-phosphatases that mediates membrane ruffle localization. The inositol 5-phosphatase skip localizes to the endoplasmic reticulum and translocates to membrane ruffles following epidermal growth factor stimulation. J Biol Chem. 2003 Mar 28;278(13):11376-85. Epub 2003 Jan 20. [PubMed ]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed ]
|
| Enzyme 118 Metabolite References |
Not Available |
|
Enzyme 119
[top]
|
| Enzyme 119 ID |
5601 |
| Enzyme 119 Name |
Lactase-phlorizin hydrolase |
| Enzyme 119 Synonyms |
- Lactase-glycosylceramidase
- Lactase
- Phlorizin hydrolase
|
| Enzyme 119 Gene Name |
LCT |
| Enzyme 119 Protein Sequence |
>Lactase-phlorizin hydrolase
MELSWHVVFIALLSFSCWGSDWESDRNFISTAGPLTNDLLHNLSGLLGDQSSNFVAGDKD
MYVCHQPLPTFLPEYFSSLHASQITHYKVFLSWAQLLPAGSTQNPDEKTVQCYRRLLKAL
KTARLQPMVILHHQTLPASTLRRTEAFADLFADYATFAFHSFGDLVGIWFTFSDLEEVIK
ELPHQESRASQLQTLSDAHRKAYEIYHESYAFQGGKLSVVLRAEDIPELLLEPPISALAQ
DTVDFLSLDLSYECQNEASLRQKLSKLQTIEPKVKVFIFNLKLPDCPSTMKNPASLLFSL
FEAINKDQVLTIGFDINEFLSCSSSSKKSMSCSLTGSLALQPDQQQDHETTDSSPASAYQ
RVWEAFANQSRAERDAFLQDTFPEGFLWGASTGAFNVEGGWAEGGRGVSIWDPRRPLNTT
EGQATLEVASDSYHKVASDVALLCGLRAQVYKFSISWSRIFPMGHGSSPSLPGVAYYNKL
IDRLQDAGIEPMATLFHWDLPQALQDHGGWQNESVVDAFLDYAAFCFSTFGDRVKLWVTF
HEPWVMSYAGYGTGQHPPGISDPGVASFKVAHLVLKAHARTWHHYNSHHRPQQQGHVGIV
LNSDWAEPLSPERPEDLRASERFLHFMLGWFAHPVFVDGDYPATLRTQIQQMNRQCSHPV
AQLPEFTEAEKQLLKGSADFLGLSHYTSRLISNAPQNTCIPSYDTIGGFSQHVNHVWPQT
SSSWIRVVPWGIRRLLQFVSLEYTRGKVPIYLAGNGMPIGESENLFDDSLRVDYFNQYIN
EVLKAIKEDSVDVRSYIARSLIDGFEGPSGYSQRFGLHHVNFSDSSKSRTPRKSAYFFTS
IIEKNGFLTKGAKRLLPPNTVNLPSKVRAFTFPSEVPSKAKVVWEKFSSQPKFERDLFYH
GTFRDDFLWGVSSSAYQIEGAWDADGKGPSIWDNFTHTPGSNVKDNATGDIACDSYHQLD
ADLNMLRALKVKAYRFSISWSRIFPTGRNSSINSHGVDYYNRLINGLVASNIFPMVTLFH
WDLPQALQDIGGWENPALIDLFDSYADFCFQTFGDRVKFWMTFNEPMYLAWLGYGSGEFP
PGVKDPGWAPYRIAHAVIKAHARVYHTYDEKYRQEQKGVISLSLSTHWAEPKSPGVPRDV
EAADRMLQFSLGWFAHPIFRNGDYPDTMKWKVGNRSELQHLATSRLPSFTEEEKRFIRAT
ADVFCLNTYYSRIVQHKTPRLNPPSYEDDQEMAEEEDPSWPSTAMNRAAPWGTRRLLNWI
KEEYGDIPIYITENGVGLTNPNTEDTDRIFYHKTYINEALKAYRLDGIDLRGYVAWSLMD
NFEWLNGYTVKFGLYHVDFNNTNRPRTARASARYYTEVITNNGMPLAREDEFLYGRFPEG
FIWSAASAAYQIEGAWRADGKGLSIWDTFSHTPLRVENDAIGDVACDSYHKIAEDLVTLQ
NLGVSHYRFSISWSRILPDGTTRYINEAGLNYYVRLIDTLLAASIQPQVTIYHWDLPQTL
QDVGGWENETIVQRFKEYADVLFQRLGDKVKFWITLNEPFVIAYQGYGYGTAAPGVSNRP
GTAPYIVGHNLIKAHAEAWHLYNDVYRASQGGVISITISSDWAEPRDPSNQEDVEAARRY
VQFMGGWFAHPIFKNGDYNEVMKTRIRDRSLAAGLNKSRLPEFTESEKRRINGTYDFFGF
NHYTTVLAYNLNYATAISSFDADRGVASIADRSWPDSGSFWLKMTPFGFRRILNWLKEEY
NDPPIYVTENGVSQREETDLNDTARIYYLRTYINEALKAVQDKVDLRGYTVWSAMDNFEW
ATGFSERFGLHFVNYSDPSLPRIPKASAKFYASVVRCNGFPDPATGPHACLHQPDAGPTI
SPVRQEEVQFLGLMLGTTEAQTALYVLFSLVLLGVCGLAFLSYKYCKRSKQGKTQRSQQE
LSPVSSF
|
| Enzyme 119 Number of Residues |
1927 |
| Enzyme 119 Molecular Weight |
218570.8 |
| Enzyme 119 Theoretical pI |
6.30 |
| Enzyme 119 GO Classification |
| Function |
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- ion binding
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 119 General Function |
Involved in hydrolase activity, hydrolyzing O-glycosyl compounds |
| Enzyme 119 Specific Function |
LPH splits lactose in the small intestine |
| Enzyme 119 Pathways |
|
| Enzyme 119 Reactions |
- lactose + H2O = D-galactose + D-glucose [RN:R01100 R06114]
|
| Enzyme 119 Pfam Domain Function |
|
| Enzyme 119 Signals |
|
| Enzyme 119 Transmembrane Regions |
|
| Enzyme 119 Essentiality |
Not Available |
| Enzyme 119 GenBank ID Protein |
34400 |
| Enzyme 119 UniProtKB/Swiss-Prot ID |
P09848 |
| Enzyme 119 UniProtKB/Swiss-Prot Entry Name |
LPH_HUMAN |
| Enzyme 119 PDB ID |
Not Available |
| Enzyme 119 Cellular Location |
Not Available |
| Enzyme 119 Gene Sequence |
>5784 bp
ATGGAGCTGTCTTGGCATGTAGTCTTTATTGCCCTGCTAAGTTTTTCATGCTGGGGGTCA
GACTGGGAGTCTGATAGAAATTTCATTTCCACCGCTGGTCCTCTAACCAATGACTTGCTG
CACAACCTGAGTGGTCTCCTGGGAGACCAGAGTTCTAACTTTGTAGCAGGGGACAAAGAC
ATGTATGTTTGTCACCAGCCACTGCCCACTTTCCTGCCAGAATACTTCAGCAGTCTCCAT
GCCAGTCAGATCACCCATTATAAGGTATTTCTGTCATGGGCACAGCTCCTCCCAGCAGGA
AGCACCCAGAATCCAGACGAGAAAACAGTGCAGTGCTACCGGCGACTCCTCAAGGCCCTC
AAGACTGCACGGCTTCAGCCCATGGTCATCCTGCACCACCAGACCCTCCCTGCCAGCACC
CTCCGGAGAACCGAAGCCTTTGCTGACCTCTTCGCCGACTATGCCACATTCGCCTTCCAC
TCCTTCGGGGACCTAGTTGGGATCTGGTTCACCTTCAGTGACTTGGAGGAAGTGATCAAG
GAGCTTCCCCACCAGGAATCAAGAGCGTCACAACTCCAGACCCTCAGTGATGCCCACAGA
AAAGCCTATGAGATTTACCACGAAAGCTATGCTTTTCAGGGCGGAAAACTCTCTGTTGTC
CTGCGAGCTGAAGATATCCCGGAGCTCCTGCTAGAACCACCCATATCTGCGCTTGCCCAG
GACACGGTCGATTTCCTCTCTCTTGATTTGTCTTATGAATGCCAAAATGAGGCAAGTCTG
CGGCAGAAGCTGAGTAAATTGCAGACCATTGAGCCAAAAGTGAAAGTTTTCATCTTCAAC
CTAAAACTCCCAGACTGCCCCTCCACCATGAAGAACCCAGCCAGTCTGCTCTTCAGCCTT
TTTGAAGCCATAAATAAAGACCAAGTGCTCACCATTGGGTTTGATATTAATGAGTTTCTG
AGTTGTTCATCAAGTTCCAAGAAAAGCATGTCTTGTTCTCTGACTGGCAGCCTGGCCCTT
CAGCCTGACCAGCAGCAGGACCACGAGACCACGGACTCCTCTCCTGCCTCTGCCTATCAG
AGAGTCTGGGAAGCATTTGCCAATCAGTCCAGAGCGGAAAGGGATGCCTTCCTGCAGGAT
ACTTTCCCTGAAGGCTTCCTCTGGGGTGCCTCCACAGGAGCCTTTAACGTGGAAGGAGGC
TGGGCCGAGGGTGGGAGAGGGGTGAGCATCTGGGATCCACGCAGGCCCCTGAACACCACT
GAGGGCCAAGCGACGCTGGAGGTGGCCAGCGACAGTTACCACAAGGTAGCCTCTGACGTC
GCCCTGCTTTGCGGCCTCCGGGCTCAGGTGTACAAGTTCTCCATCTCCTGGTCCCGGATC
TTCCCCATGGGGCACGGGAGCAGCCCCAGCCTCCCAGGCGTTGCCTACTACAACAAGCTG
ATTGACAGGCTACAGGATGCGGGCATCGAGCCCATGGCCACGCTGTTCCACTGGGACCTG
CCTCAGGCCCTGCAGGATCATGGTGGATGGCAGAATGAGAGCGTGGTGGATGCCTTCCTG
GACTATGCGGCCTTCTGCTTCTCCACATTTGGGGACCGTGTGAAGCTGTGGGTGACCTTC
CATGAGCCGTGGGTGATGAGCTACGCAGGCTATGGCACCGGCCAGCACCCTCCCGGCATC
TCTGACCCAGGAGTGGCCTCTTTTAAGGTGGCTCACTTGGTCCTCAAGGCTCATGCCAGA
ACTTGGCACCACTACAACAGCCATCATCGCCCACAGCAGCAGGGGCACGTGGGCATTGTG
CTGAACTCAGACTGGGCAGAACCCCTGTCTCCAGAGAGGCCTGAGGACCTGAGAGCCTCT
GAGCGCTTCTTGCACTTCATGCTGGGCTGGTTTGCACACCCCGTCTTTGTGGATGGAGAC
TACCCAGCCACCCTGAGGACCCAGATCCAACAGATGAACAGACAGTGCTCCCATCCTGTG
GCTCAACTCCCCGAGTTCACAGAGGCAGAGAAGCAGCTCCTGAAAGGCTCTGCTGATTTT
CTGGGTCTGTCGCATTACACCTCCCGCCTCATCAGCAACGCCCCACAAAACACCTGCATC
CCTAGCTATGATACCATTGGAGGCTTCTCCCAACACGTGAACCATGTGTGGCCCCAGACC
TCATCCTCTTGGATTCGTGTGGTGCCCTGGGGGATAAGGAGGCTGTTGCAGTTTGTATCC
CTGGAATACACAAGAGGAAAAGTTCCAATATACCTTGCCGGGAATGGCATGCCCATAGGG
GAAAGTGAAAATCTCTTTGATGATTCCTTAAGAGTAGACTACTTCAATCAATATATCAAT
GAGGTGCTCAAGGCTATCAAGGAAGACTCTGTGGATGTTCGTTCCTACATTGCTCGTTCC
CTCATTGATGGCTTCGAAGGCCCTTCTGGTTACAGCCAGCGGTTTGGCCTGCACCACGTC
AACTTCAGCGACAGCAGCAAGTCAAGGACTCCCAGGAAATCTGCCTACTTTTTCACTAGC
ATCATAGAAAAGAACGGTTTCCTCACCAAGGGGGCAAAAAGACTGCTACCACCTAATACA
GTAAACCTCCCCTCCAAAGTCAGAGCCTTCACTTTTCCATCTGAGGTGCCCTCCAAGGCT
AAAGTCGTTTGGGAAAAGTTCTCCAGCCAACCCAAGTTCGAAAGAGATTTGTTCTACCAC
GGGACGTTTCGGGATGACTTTCTGTGGGGCGTGTCCTCTTCCGCTTATCAGATTGAAGGC
GCGTGGGATGCCGATGGCAAAGGCCCCAGCATCTGGGATAACTTTACCCACACACCAGGG
AGCAATGTGAAAGACAATGCCACTGGAGACATCGCCTGTGACAGCTATCACCAGCTGGAT
GCCGATCTGAATATGCTCCGAGCTTTGAAGGTGAAGGCCTACCGCTTCTCTATCTCCTGG
TCTCGGATTTTCCCAACTGGGAGAAACAGCTCTATCAACAGTCATGGGGTTGATTATTAC
AACAGGCTGATCAATGGCTTGGTGGCAAGCAACATCTTTCCCATGGTGACATTGTTCCAT
TGGGACCTGCCCCAGGCCCTCCAGGATATCGGAGGCTGGGAGAATCCTGCCTTGATTGAC
TTGTTTGACAGCTACGCAGACTTTTGTTTCCAGACCTTTGGTGATAGAGTCAAGTTTTGG
ATGACTTTTAATGAGCCCATGTACCTGGCATGGCTAGGTTATGGCTCAGGGGAATTTCCC
CCAGGGGTGAAGGACCCAGGCTGGGCACCATATAGGATAGCCCACACCGTCATCAAAGCC
CATGCCAGAGTCTATCACACGTACGATGAGAAATACAGGCAGGAGCAGAAGGGGGTCATC
TCGCTGAGCCTCAGTACACACTGGGCAGAGCCCAAGTCACCAGGGGTCCCCAGAGATGTG
GAAGCCGCTGACCGAATGCTGCAGTTCTCCCTGGGCTGGTTTGCTCACCCCATTTTTAGA
AACGGAGACTATCCTGACACCATGAAGTGGAAAGTGGGGAACAGGAGTGAACTGCAGCAC
TTAGCCACCTCCCGCCTGCCAAGCTTCACTGAGGAAGAGAAGAGGTTCATCAGGGCGACG
GCCGACGTCTTCTGCCTCAACACGTACTACTCCAGAATCGTGCAGCACAAAACACCCAGG
CTAAACCCACCCTCCTACGAAGACGACCAGGAGATGGCTGAGGAGGAGGACCCTTCGTGG
CCTTCCACGGCAATGAACAGAGCTGCGCCCTGGGGGACGCGAAGGCTGCTGAACTGGATC
AAGGAAGAGTATGGTGACATCCCCATTTACATCACCGAAAACGGAGTGGGGCTGACCAAT
CCGAACACGGAGGATACTGATAGGATATTTTACCACAAAACCTACATCAATGAGGCTTTG
AAAGCCTACAGGCTCGATGGTATAGACCTTCGAGGGTATGTCGCCTGGTCTCTGATGGAC
AACTTTGAGTGGCTAAATGGCTACACGGTCAAGTTTGGACTGTACCATGTTGATTTCAAC
AACACGAACAGGCCTCGCACAGCAAGAGCCTCCGCCAGGTACTACACAGAGGTCATTACC
AACAACGGCATGCCACTGGCCAGGGAGGATGAGTTTCTGTACGGACGGTTTCCTGAGGGC
TTCATCTGGAGTGCAGCTTCTGCTGCATATCAGATTGAAGGTGCGTGGAGAGCAGATGGC
AAAGGACTCAGCATTTGGGACACGTTTTCTCACACACCACTGAGGGTTGAGAACGATGCC
ATTGGAGACGTGGCCTGTGACAGTTATCACAAGATTGCTGAGGATCTGGTCACCCTGCAG
AACCTGGGTGTGTCCCACTACCGTTTTTCCATCTCCTGGTCTCGCATCCTCCCTGATGGA
ACCACCAGGTACATCAATGAAGCGGGCCTGAACTACTACGTGAGGCTCATCGATACACTG
CTGGCCGCCAGCATCCAGCCCCAGGTGACCATTTACCACTGGGACCTACCACAGACGCTC
CAAGATGTAGGAGGCTGGGAGAATGAGACCATCGTGCAGCGGTTTAAGGAGTATGCAGAT
GTGCTCTTCCAGAGGCTGGGAGACAAGGTGAAGTTTTGGATCACGTTGAATGAGCCCTTT
GTCATTGCTTACCAGGGCTATGGCTACGGAACAGCAGCTCCAGGAGTCTCCAATAGGCCT
GGCACTGCCCCCTACATTGTTGGCCACAATCTAATAAAGGCTCATGCTGAGGCCTGGCAT
CTGTACAACGATGTGTACCGCGCCAGTCAAGGTGGCGTGATTTCCATCACCATCAGCAGT
GACTGGGCTGAACCCAGAGATCCCTCTAACCAGGAGGATGTGGAGGCAGCCAGGAGATAT
GTTCAGTTCATGGGAGGCTGGTTTGCACATCCTATTTTCAAGAATGGAGATTACAATGAG
GTGATGAAGACGCGGATCCGTGACAGGAGCTTGGCTGCAGGCCTCAACAAGTCTCGGCTG
CCAGAATTTACAGAGAGTGAGAAGAGGAGGATCAACGGCACCTATGACTTTTTTGGGTTC
AATCACTACACCACTGTCCTCGCCTACAACCTCAACTATGCCACTGCCATCTCTTCTTTT
GATGCAGACAGAGGAGTTGCTTCCATCGCAGATCGCTCGTGGCCAGACTCTGGCTCCTTC
TGGCTGAAGATGACGCCTTTTGGCTTCAGGAGGATCCTGAACTGGTTAAAGGAGGAATAC
AATGACCCTCCAATTTATGTCACAGAGAATGGAGTGTCCCAGCGGGAAGAAACAGACCTC
AATGACACTGCAAGGATCTACTACCTTCGGACTTACATCAATGAGGCCCTCAAAGCTGTG
CAGGACAAGGTGGACCTTCGAGGATACACAGTTTGGAGTGCGATGGACAATTTTGAGTGG
GCCACAGGCTTTTCAGAGAGATTTGGTCTGCATTTTGTGAACTACAGTGACCCTTCTCTG
CCAAGGATCCCCAAAGCATCAGCGAAGTTCTACGCCTCTGTGGTCCGATGCAATGGCTTC
CCTGACCCCGCTACAGGGCCTCACGCTTGTCTCCACCAGCCAGATGCTGGACCCACCATC
AGCCCCGTGAGACAGGAGGAGGTGCAGTTCCTGGGGCTAATGCTCGGCACCACAGAAGCA
CAGACAGCTTTGTACGTTCTCTTTTCTCTTGTGCTTCTTGGAGTCTGTGGCTTGGCATTT
CTGTCATACAAGTACTGCAAGCGCTCTAAGCAAGGGAAAACACAACGAAGCCAACAGGAA
TTGAGCCCGGTGTCTTCATTCTGA
|
| Enzyme 119 GenBank Gene ID |
X07994 |
| Enzyme 119 GeneCard ID |
LCT |
| Enzyme 119 GenAtlas ID |
LCT |
| Enzyme 119 HGNC ID |
HGNC:6530 |
| Enzyme 119 Chromosome Location |
2 |
| Enzyme 119 Locus |
2q21 |
| Enzyme 119 SNPs |
SNPJam Report |
| Enzyme 119 General References |
- Mantei N, Villa M, Enzler T, Wacker H, Boll W, James P, Hunziker W, Semenza G: Complete primary structure of human and rabbit lactase-phlorizin hydrolase: implications for biosynthesis, membrane anchoring and evolution of the enzyme. EMBO J. 1988 Sep;7(9):2705-13. [PubMed ]
- Boll W, Wagner P, Mantei N: Structure of the chromosomal gene and cDNAs coding for lactase-phlorizin hydrolase in humans with adult-type hypolactasia or persistence of lactase. Am J Hum Genet. 1991 May;48(5):889-902. [PubMed ]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed ]
- Enattah NS, Sahi T, Savilahti E, Terwilliger JD, Peltonen L, Jarvela I: Identification of a variant associated with adult-type hypolactasia. Nat Genet. 2002 Feb;30(2):233-7. Epub 2002 Jan 14. [PubMed ]
- Wang Y, Du D, Fang L, Yang G, Zhang C, Zeng R, Ullrich A, Lottspeich F, Chen Z: Tyrosine phosphorylated Par3 regulates epithelial tight junction assembly promoted by EGFR signaling. EMBO J. 2006 Nov 1;25(21):5058-70. Epub 2006 Oct 19. [PubMed ]
- Kuokkanen M, Kokkonen J, Enattah NS, Ylisaukko-Oja T, Komu H, Varilo T, Peltonen L, Savilahti E, Jarvela I: Mutations in the translated region of the lactase gene (LCT) underlie congenital lactase deficiency. Am J Hum Genet. 2006 Feb;78(2):339-44. Epub 2005 Dec 15. [PubMed ]
|
| Enzyme 119 Metabolite References |
Not Available |
|
Enzyme 120
[top]
|
| Enzyme 120 ID |
5602 |
| Enzyme 120 Name |
Neutral alpha-glucosidase AB |
| Enzyme 120 Synonyms |
- Alpha-glucosidase 2
- Glucosidase II subunit alpha
|
| Enzyme 120 Gene Name |
GANAB |
| Enzyme 120 Protein Sequence |
>Neutral alpha-glucosidase AB
MAAVAAVAARRRRSWASLVLAFLGVCLGITLAVDRSNFKTCEESSFCKRQRSIRPGLSPY
RALLDSLQLGPDSLTVHLIHEVTKVLLVLELQGLQKNMTRFRIDELEPRRPRYRVPDVLV
ADPPIARLSVSGRDENSVELTMAEGPYKIILTARPFRLDLLEDRSLLLSVNARGLLEFEH
QRAPRVSQGSKDPAEGDGAQPEETPRDGDKPEETQGKAEKDEPGAWEETFKTHSDSKPYG
PMSVGLDFSLPGMEHVYGIPEHADNLRLKVTEGGEPYRLYNLDVFQYELYNPMALYGSVP
VLLAHNPHRDLGIFWLNAAETWVDISSNTAGKTLFGKMMDYLQGSGETPQTDVRWMSETG
IIDVFLLLGPSISDVFRQYASLTGTQALPPLFSLGYHQSRWNYRDEADVLEVDQGFDDHN
LPCDVIWLDIEHADGKRYFTWDPSRFPQPRTMLERLASKRRKLVAIVDPHIKVDSGYRVH
EELRNLGLYVKTRDGSDYEGWCWPGSAGYPDFTNPTMRAWWANMFSYDNYEGSAPNLFVW
NDMNEPSVFNGPEVTMLKDAQHYGGWEHRDVHNIYGLYVHMATADGLRQRSGGMERPFVL
ARAFFAGSQRFGAVWTGDNTAEWDHLKISIPMCLSLGLVGLSFCGADVGGFFKNPEPELL
VRWYQMGAYQPFFRAHAHLDTGRREPWLLPSQHNDIIRDALGQRYSLLPFWYTLLYQAHR
EGIPVMRPLWVQYPQDVTTFNIDDQYLLGDALLVHPVSDSGAHGVQVYLPGQGEVWYDIQ
SYQKHHGPQTLYLPVTLSSIPVFQRGGTIVPRWMRVRRSSECMKDDPITLFVALSPQGTA
QGELFLDDGHTFNYQTRQEFLLRRFSFSGNTLVSSSADPEGHFETPIWIERVVIIGAGKP
AAVVLQTKGSPESRLSFQHDPETSVLVLRKPGINVASDWSIHLR
|
| Enzyme 120 Number of Residues |
944 |
| Enzyme 120 Molecular Weight |
106873.1 |
| Enzyme 120 Theoretical pI |
6.06 |
| Enzyme 120 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 120 General Function |
Involved in catalytic activity |
| Enzyme 120 Specific Function |
Cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins |
| Enzyme 120 Pathways |
|
| Enzyme 120 Reactions |
- Hydrolysis of terminal (1->3)-alpha-D-glucosidic links in (1->3)-alpha-D-glucans ALL_REAC (other) R05980(G) R05981(G)
|
| Enzyme 120 Pfam Domain Function |
|
| Enzyme 120 Signals |
|
| Enzyme 120 Transmembrane Regions |
|
| Enzyme 120 Essentiality |
Not Available |
| Enzyme 120 GenBank ID Protein |
38202257 |
| Enzyme 120 UniProtKB/Swiss-Prot ID |
Q14697 |
| Enzyme 120 UniProtKB/Swiss-Prot Entry Name |
GANAB_HUMAN |
| Enzyme 120 PDB ID |
Not Available |
| Enzyme 120 Cellular Location |
Not Available |
| Enzyme 120 Gene Sequence |
>2835 bp
ATGGCGGCGGTAGCGGCAGTGGCGGCGCGTAGGAGGCGGTCTTGGGCGTCTTTGGTACTG
GCTTTTTTAGGGGTCTGCCTGGGGATTACCCTTGCTGTGGATAGAAGCAACTTTAAGACC
TGTGAAGAGAGTTCTTTCTGCAAGCGACAGAGAAGCATACGGCCAGGCCTCTCTCCATAC
CGAGCCTTGCTGGACTCTCTACAGCTTGGTCCTGATTCCCTCACGGTCCATCTGATCCAT
GAGGTCACCAAGGTGTTGCTGGTGCTAGAGCTTCAGGGGCTTCAAAAGAACATGACTCGG
TTCAGGATTGATGAGCTGGAGCCTCGGCGACCCCGATACCGTGTACCAGATGTTTTGGTG
GCTGATCCACCAATAGCCCGGCTTTCTGTCTCTGGTCGTGATGAGAACAGTGTGGAGTTA
ACCATGGCTGAGGGACCCTACAAGATCATCTTGACAGCACGGCCATTCCGCCTTGACCTA
CTAGAGGACCGAAGTCTTTTGCTTAGTGTCAATGCCCGAGGACTCTTGGAGTTTGAGCAT
CAGAGGGCCCCTAGGGTCTCGCAAGGATCAAAAGACCCAGCTGAGGGCGATGGGGCCCAG
CCTGAGGAAACACCCAGGGATGGCGACAAGCCAGAGGAGACTCAGGGGAAGGCAGAGAAA
GATGAGCCAGGAGCCTGGGAGGAGACATTCAAAACTCACTCTGACAGCAAGCCGTATGGC
CCCATGTCTGTGGGTTTGGACTTCTCTCTGCCAGGCATGGAGCATGTCTATGGGATCCCT
GAGCATGCAGACAACCTGAGGCTGAAGGTCACTGAGGGTGGGGAGCCATATCGCCTCTAC
AATTTGGATGTGTTCCAGTATGAGCTGTACAACCCAATGGCCTTGTATGGGTCTGTGCCT
GTGCTCCTGGCACACAACCCTCATCGCGACTTGGGCATCTTCTGGCTCAATGCTGCAGAG
ACCTGGGTTGATATATCTTCCAACACTGCCGGGAAGACCCTGTTTGGGAAGATGATGGAC
TACCTGCAGGGCTCTGGGGAGACCCCACAGACAGATGTTCGCTGGATGTCAGAGACTGGC
ATCATTGACGTCTTCCTGCTGCTGGGGCCCTCCATCTCTGATGTTTTCCGGCAATATGCT
AGTCTCACAGGAACCCAGGCGTTGCCCCCACTCTTCTCCCTCGGCTACCACCAGAGCCGT
TGGAACTACCGGGACGAGGCTGATGTGCTGGAAGTGGATCAGGGCTTTGATGATCACAAC
CTGCCCTGTGATGTCATCTGGCTAGACATTGAACATGCTGATGGCAAGCGGTATTTCACC
TGGGACCCCAGTCGCTTCCCTCAGCCCCGCACCATGCTTGAGCGCTTGGCTTCTAAGAGG
CGGAAGCTGGTGGCCATCGTAGACCCCCACATCAAGGTGGACTCCGGCTACCGAGTTCAC
GAGGAGCTGCGGAACCTGGGGCTGTATGTTAAAACCCGGGATGGCTCTGACTATGAGGGC
TGGTGCTGGCCAGGCTCAGCTGGTTACCCTGACTTCACTAATCCCACGATGAGGGCCTGG
TGGGCTAACATGTTCAGCTATGACAATTATGAGGGCTCAGCTCCCAACCTCTTTGTCTGG
AATGACATGAACGAACCATCTGTGTTCAATGGTCCTGAGGTCACCATGCTCAAGGATGCC
CAGCATTATGGGGGCTGGGAGCACCGGGATGTGCATAACATCTATGGCCTTTATGTGCAC
ATGGCGACTGCTGATGGGCTGAGACAGCGCTCTGGGGGCATGGAACGCCCCTTTGTCCTG
GCCAGGGCCTTCTTCGCTGGCTCCCAGCGCTTTGGAGCCGTGTGGACAGGGGACAACACT
GCCGAGTGGGACCATTTGAAGATCTCTATTCCTATGTGTCTCAGCTTGGGGCTGGTGGGA
CTTTCCTTCTGTGGGGCGGATGTGGGTGGCTTCTTCAAAAACCCAGAGCCAGAGCTGCTT
GTGCGCTGGTACCAGATGGGTGCTTACCAGCCATTCTTCCGGGCACATGCCCACTTGGAC
ACTGGGCGACGAGAGCCATGGCTGTTACCATCTCAGCACAATGATATAATCCGAGATGCC
TTGGGCCAGCGATATTCTTTGCTGCCCTTCTGGTACACCCTCTTATATCAGGCCCATCGG
GAAGGCATTCCTGTCATGAGGCCCCTGTGGGTGCAGTACCCTCAGGATGTGACTACCTTC
AATATAGATGATCAGTACTTGCTTGGGGATGCGTTGCTGGTTCACCCTGTATCAGACTCT
GGAGCCCATGGTGTCCAGGTCTATCTGCCTGGCCAAGGGGAGGTGTGGTATGACATTCAA
AGCTACCAGAAGCATCATGGTCCCCAGACCCTGTACCTGCCTGTAACTCTAAGCAGTATC
CCTGTGTTCCAGCGTGGAGGGACAATCGTGCCTCGATGGATGCGAGTGCGGCGGTCTTCA
GAATGTATGAAGGATGACCCCATCACTCTCTTTGTTGCACTTAGCCCTCAGGGTACAGCT
CAAGGAGAGCTCTTTCTGGATGATGGGCACACGTTCAACTATCAGACTCGCCAAGAGTTC
CTGCTGCGTCGATTCTCATTCTCTGGCAACACCCTTGTCTCCAGCTCAGCAGACCCTGAA
GGACACTTTGAGACACCAATCTGGATTGAGCGGGTGGTGATAATAGGGGCTGGAAAGCCA
GCAGCTGTGGTACTCCAGACAAAAGGATCTCCAGAAAGCCGCCTGTCCTTCCAGCATGAC
CCTGAGACCTCTGTGTTGGTCCTGCGCAAGCCTGGCATCAATGTGGCATCTGATTGGAGT
ATTCACCTGCGATAA
|
| Enzyme 120 GenBank Gene ID |
NM_198334.1 |
| Enzyme 120 GeneCard ID |
GANAB |
| Enzyme 120 GenAtlas ID |
GANAB |
| Enzyme 120 HGNC ID |
HGNC:4138 |
| Enzyme 120 Chromosome Location |
1 |
| Enzyme 120 Locus |
11q12.3 |
| Enzyme 120 SNPs |
SNPJam Report |
| Enzyme 120 General References |
- Pelletier MF, Marcil A, Sevigny G, Jakob CA, Tessier DC, Chevet E, Menard R, Bergeron JJ, Thomas DY: The heterodimeric structure of glucosidase II is required for its activity, solubility, and localization in vivo. Glycobiology. 2000 Aug;10(8):815-27. [PubMed ]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed ]
- Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H, et al.: Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995;2(1):37-43. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Martiniuk F, Ellenbogen A, Hirschhorn R: Identity of neutral alpha-glucosidase AB and the glycoprotein processing enzyme glucosidase II. Biochemical and genetic studies. J Biol Chem. 1985 Jan 25;260(2):1238-42. [PubMed ]
- Trombetta ES, Simons JF, Helenius A: Endoplasmic reticulum glucosidase II is composed of a catalytic subunit, conserved from yeast to mammals, and a tightly bound noncatalytic HDEL-containing subunit. J Biol Chem. 1996 Nov 1;271(44):27509-16. [PubMed ]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed ]
|
| Enzyme 120 Metabolite References |
Not Available |
|
Enzyme 121
[top]
|
| Enzyme 121 ID |
5603 |
| Enzyme 121 Name |
Glycogen debranching enzyme |
| Enzyme 121 Synonyms |
- Glycogen debrancher
- 4-alpha-glucanotransferase
- Oligo-1,4-1,4-glucantransferase
- Amylo-alpha-1,6-glucosidase
- Amylo-1,6-glucosidase
- Dextrin 6-alpha-D-glucosidase
|
| Enzyme 121 Gene Name |
AGL |
| Enzyme 121 Protein Sequence |
>Glycogen debranching enzyme
MGHSKQIRILLLNEMEKLEKTLFRLEQGYELQFRLGPTLQGKAVTVYTNYPFPGETFNRE
KFRSLDWENPTEREDDSDKYCKLNLQQSGSFQYYFLQGNEKSGGGYIVVDPILRVGADNH
VLPLDCVTLQTFLAKCLGPFDEWESRLRVAKESGYNMIHFTPLQTLGLSRSCYSLANQLE
LNPDFSRPNRKYTWNDVGQLVEKLKKEWNVICITDVVYNHTAANSKWIQEHPECAYNLVN
SPHLKPAWVLDRALWRFSCDVAEGKYKEKGIPALIENDHHMNSIRKIIWEDIFPKLKLWE
FFQVDVNKAVEQFRRLLTQENRRVTKSDPNQHLTIIQDPEYRRFGCTVDMNIALTTFIPH
DKGPAAIEECCNWFHKRMEELNSEKHRLINYHQEQAVNCLLGNVFYERLAGHGPKLGPVT
RKHPLVTRYFTFPFEEIDFSMEESMIHLPNKACFLMAHNGWVMGDDPLRNFAEPGSEVYL
RRELICWGDSVKLRYGNKPEDCPYLWAHMKKYTEITATYFQGVRLDNCHSTPLHVAEYML
DAARNLQPNLYVVAELFTGSEDLDNVFVTRLGISSLIREAMSAYNSHEEGRLVYRYGGEP
VGSFVQPCLRPLMPAIAHALFMDITHDNECPIVHRSAYDALPSTTIVSMACCASGSTRGY
DELVPHQISVVSEERFYTKWNPEALPSNTGEVNFQSGIIAARCAISKLHQELGAKGFIQV
YVDQVDEDIVAVTRHSPSIHQSVVAVSRTAFRNPKTSFYSKEVPQMCIPGKIEEVVLEAR
TIERNTKPYRKDENSINGTPDITVEIREHIQLNESKIVKQAGVATKGPNEYIQEIEFENL
SPGSVIIFRVSLDPHAQVAVGILRNHLTQFSPHFKSGSLAVDNADPILKIPFASLASRLT
LAELNQILYRCESEEKEDGGGCYDIPNWSALKYAGLQGLMSVLAEIRPKNDLGHPFCNNL
RSGDWMIDYVSNRLISRSGTIAEVGKWLQAMFFYLKQIPRYLIPCYFDAILIGAYTTLLD
TAWKQMSSFVQNGSTFVKHLSLGSVQLCGVGKFPSLPILSPALMDVPYRLNEITKEKEQC
CVSLAAGLPHFSSGIFRCWGRDTFIALRGILLITGRYVEARNIILAFAGTLRHGLIPNLL
GEGIYARYNCRDAVWWWLQCIQDYCKMVPNGLDILKCPVSRMYPTDDSAPLPAGTLDQPL
FEVIQEAMQKHMQGIQFRERNAGPQIDRNMKDEGFNITAGVDEETGFVYGGNRFNCGTWM
DKMGESDRARNRGIPATPRDGSAVEIVGLSKSAVRWLLELSKKNIFPYHEVTVKRHGKAI
KVSYDEWNRKIQDNFEKLFHVSEDPSDLNEKHPNLVHKRGIYKDSYGASSPWCDYQLRPN
FTIAMVVAPELFTTEKAWKALEIAEKKLLGPLGMKTLDPDDMVYCGIYDNALDNDNYNLA
KGFNYHQGPEWLWPIGYFLRAKLYFSRLMGPETTAKTIVLVKNVLSRHYVHLERSPWKGL
PELTNENAQYCPFSCETQAWSIATILETLYDL
|
| Enzyme 121 Number of Residues |
1532 |
| Enzyme 121 Molecular Weight |
174762.3 |
| Enzyme 121 Theoretical pI |
6.74 |
| Enzyme 121 GO Classification |
| Function |
- 4-alpha-glucanotransferase activity
- amylo-alpha-1,6-glucosidase activity
- binding
- catalytic activity
- cation binding
- glycogen debranching enzyme activity
- ion binding
|
| Process |
- alcohol metabolic process
- carbohydrate metabolic process
- glucose metabolic process
- glycogen biosynthetic process
- glycogen metabolic process
- hexose metabolic process
- metabolic process
- monosaccharide metabolic process
- primary metabolic process
- small molecule metabolic process
|
| Component |
| — |
|
| Enzyme 121 General Function |
Involved in catalytic activity |
| Enzyme 121 Specific Function |
Multifunctional enzyme acting as 1,4-alpha-D-glucan:1,4- alpha-D-glucan 4-alpha-D-glycosyltransferase and amylo-1,6- glucosidase in glycogen degradation |
| Enzyme 121 Pathways |
- Starch and Sucrose Metabolism (map00500 )
|
| Enzyme 121 Reactions |
- Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen phosphorylase limit dextrin ALL_REAC (other) R02109 R06158(G)
|
| Enzyme 121 Pfam Domain Function |
|
| Enzyme 121 Signals |
|
| Enzyme 121 Transmembrane Regions |
|
| Enzyme 121 Essentiality |
Not Available |
| Enzyme 121 GenBank ID Protein |
6580116 |
| Enzyme 121 UniProtKB/Swiss-Prot ID |
P35573 |
| Enzyme 121 UniProtKB/Swiss-Prot Entry Name |
GDE_HUMAN |
| Enzyme 121 PDB ID |
Not Available |
| Enzyme 121 Cellular Location |
Not Available |
| Enzyme 121 Gene Sequence |
>4599 bp
ATGGGACACAGTAAACAGATTCGAATTTTACTTCTGAACGAAATGGAGAAACTGGAAAAG
ACCCTCTTCAGACTTGAACAAGGGTATGAGCTACAGTTCCGATTAGGCCCAACTTTACAG
GGAAAAGCAGTTACCGTGTATACAAATTACCCATTTCCTGGAGAAACATTTAATAGAGAA
AAATTCCGTTCTCTGGATTGGGAAAATCCAACAGAAAGAGAAGATGATTCTGATAAATAC
TGTAAACTTAATCTGCAACAATCTGGTTCATTTCAGTATTATTTCCTTCAAGGAAATGAG
AAAAGTGGTGGAGGTTACATAGTTGTGGACCCCATTTTACGTGTTGGTGCTGATAATCAT
GTGCTACCCTTGGACTGTGTTACTCTTCAGACATTTTTAGCTAAGTGTTTGGGACCTTTT
GATGAATGGGAAAGCAGACTTAGGGTTGCAAAAGAATCAGGCTACAACATGATTCATTTT
ACCCCATTGCAGACTCTTGGACTATCTAGGTCATGCTACTCCCTTGCCAATCAGTTAGAA
TTAAATCCTGACTTTTCAAGACCTAATAGAAAGTATACCTGGAATGATGTTGGACAGCTA
GTGGAAAAATTAAAAAAGGAATGGAATGTTATTTGTATTACTGATGTTGTCTACAATCAT
ACTGCTGCTAATAGTAAATGGATCCAGGAACATCCAGAATGTGCCTATAATCTTGTGAAT
TCTCCACACTTAAAACCTGCCTGGGTCTTAGACAGAGCACTTTGGCGTTTCTCCTGTGAT
GTTGCAGAAGGGAAATACAAAGAAAAGGGAATACCTGCTTTGATTGAAAATGATCACCAT
ATGAATTCCATCCGAAAAATAATTTGGGAGGATATTTTTCCAAAGCTTAAACTTTGGGAA
TTTTTCCAAGTAGATGTCAACAAAGCGGTTGAGCAATTTAGAAGACTTCTTACACAAGAA
AATAGGCGAGTAACCAAGTCTGATCCAAACCAACACCTTACGATTATTCAAGATCCTGAA
TACAGACGGTTTGGCTGTACTGTAGATATGAACATTGCACTAACGACTTTCATACCACAT
GACAAGGGGCCAGCAGCAATTGAAGAATGCTGTAATTGGTTTCATAAAAGAATGGAGGAA
TTAAATTCAGAGAAGCATCGACTCATTAACTATCATCAGGAACAGGCAGTTAATTGCCTT
TTGGGAAATGTGTTTTATGAACGACTGGCTGGCCATGGTCCAAAACTAGGACCTGTCACT
AGAAAGCATCCTTTAGTTACCAGGTATTTTACTTTCCCATTTGAAGAGATAGACTTCTCC
ATGGAAGAATCTATGATTCATCTGCCAAATAAAGCTTGTTTTCTGATGGCACACAATGGA
TGGGTAATGGGAGATGATCCTCTTCGAAACTTTGCTGAACCGGGTTCAGAAGTTTACCTA
AGGAGAGAACTTATTTGCTGGGGAGACAGTGTTAAATTACGCTATGGGAATAAACCAGAG
GACTGTCCTTATCTCTGGGCACACATGAAAAAATACACTGAAATAACTGCAACTTATTTC
CAGGGAGTACGTCTTGATAACTGCCACTCAACACCTCTTCACGTAGCTGAGTACATGTTG
GATGCTGCTAGGAATTTGCAACCCAATTTATATGTAGTAGCTGAACTGTTCACAGGAAGT
GAAGATCTGGACAATGTCTTTGTTACTAGACTGGGCATTAGTTCCTTAATAAGAGAGGCA
ATGAGTGCATATAATAGTCATGAAGAGGGCAGATTAGTTTACCGATATGGAGGAGAACCT
GTTGGATCCTTTGTTCAGCCCTGTTTGAGGCCTTTAATGCCAGCTATTGCACATGCCCTG
TTTATGGATATTACGCATGATAATGAGTGTCCTATTGTGCATAGATCAGCGTATGATGCT
CTTCCAAGTACTACAATTGTTTCTATGGCATGTTGTGCTAGTGGAAGTACAAGAGGCTAT
GATGAATTAGTGCCTCATCAGATTTCAGTGGTTTCTGAAGAACGGTTTTACACTAAGTGG
AATCCTGAAGCATTGCCTTCAAACACAGGTGAAGTTAATTTCCAAAGCGGCATTATTGCA
GCCAGGTGTGCTATCAGTAAACTTCATCAGGAGCTTGGAGCCAAGGGTTTTATTCAGGTG
TATGTGGATCAAGTTGATGAAGACATAGTGGCAGTAACAAGACACTCACCTAGCATCCAT
CAGTCTGTTGTGGCTGTATCTAGAACTGCTTTCAGGAATCCCAAGACTTCATTTTACAGC
AAGGAAGTGCCTCAAATGTGCATCCCTGGCAAAATTGAAGAAGTAGTTCTTGAAGCTAGA
ACTATTGAGAGAAACACGAAACCTTATAGGAAGGATGAGAATTCAATCAATGGAACACCA
GATATCACAGTAGAAATTAGAGAACATATTCAGCTTAATGAAAGTAAAATTGTTAAACAA
GCTGGAGTTGCCACAAAAGGGCCCAATGAATATATTCAAGAAATAGAATTTGAAAACTTG
TCTCCAGGAAGTGTTATTATATTCAGAGTTAGTCTTGATCCACATGCACAAGTCGCTGTT
GGAATTCTTCGAAATCATCTGACACAATTCAGTCCTCACTTTAAATCTGGCAGCCTAGCT
GTTGACAATGCAGATCCTATATTAAAAATTCCTTTTGCTTCTCTTGCCTCCAGATTAACT
TTGGCTGAGCTAAATCAGATCCTTTACCGATGTGAATCAGAAGAAAAGGAAGATGGTGGA
GGGTGCTATGACATACCAAACTGGTCAGCCCTTAAATATGCAGGTCTTCAAGGTTTAATG
TCTGTATTGGCAGAAATAAGACCAAAGAATGACTTGGGGCATCCTTTTTGTAATAATTTG
AGATCTGGAGATTGGATGATTGACTATGTCAGTAACCGGCTTATTTCACGATCAGGAACT
ATTGCTGAAGTTGGTAAATGGTTGCAGGCTATGTTCTTCTACCTGAAGCAGATCCCACGT
TACCTTATCCCATGTTACTTTGATGCTATATTAATTGGTGCATATACCACTCTTCTGGAT
ACAGCATGGAAGCAGATGTCAAGCTTTGTTCAGAATGGTTCAACCTTTGTGAAACACCTT
TCATTGGGTTCAGTTCAACTGTGTGGAGTAGGAAAATTCCCTTCCCTGCCAATTCTTTCA
CCTGCCCTAATGGATGTACCTTATAGGTTAAATGAGATCACAAAAGAAAAGGAGCAATGT
TGTGTTTCTCTAGCTGCAGGCTTACCTCATTTTTCTTCTGGTATTTTCCGCTGCTGGGGA
AGGGATACTTTTATTGCACTTAGAGGTATACTGCTGATTACTGGACGCTATGTAGAAGCC
AGGAATATTATTTTAGCATTTGCGGGTACCCTGAGGCATGGTCTCATTCCTAATCTACTG
GGTGAAGGAATTTATGCCAGATACAATTGTCGGGATGCTGTGTGGTGGTGGCTGCAGTGT
ATCCAGGATTACTGTAAAATGGTTCCAAATGGTCTAGACATTCTCAAGTGCCCAGTTTCC
AGAATGTATCCTACAGATGATTCTGCTCCTTTGCCTGCTGGCACACTGGATCAGCCATTG
TTTGAAGTCATACAGGAAGCAATGCAAAAACACATGCAGGGCATACAGTTCCGAGAAAGG
AATGCTGGTCCCCAGATAGATCGAAACATGAAGGACGAAGGTTTTAATATAACTGCAGGA
GTTGATGAAGAAACAGGATTTGTTTATGGAGGAAATCGTTTCAATTGTGGCACATGGATG
GATAAAATGGGAGAAAGTGACAGAGCTAGAAACAGAGGAATCCCAGCCACACCAAGAGAT
GGGTCTGCTGTGGAAATTGTGGGCCTGAGTAAATCTGCTGTTCGCTGGTTGCTGGAATTA
TCCAAAAAAAATATTTTCCCTTATCATGAAGTCACAGTAAAAAGACATGGAAAGGCTATA
AAGGTCTCATATGATGAGTGGAACAGAAAAATACAAGACAACTTTGAAAAGCTATTTCAT
GTTTCCGAAGACCCTTCAGATTTAAATGAAAAGCATCCAAATCTGGTTCACAAACGTGGC
ATATACAAAGATAGTTATGGAGCTTCAAGTCCTTGGTGTGACTATCAGCTCAGGCCTAAT
TTTACCATAGCAATGGTTGTGGCCCCTGAGCTCTTTACTACAGAAAAAGCATGGAAAGCT
TTGGAGATTGCAGAAAAAAAATTGCTTGGTCCCCTTGGCATGAAAACTTTAGATCCAGAT
GATATGGTTTACTGTGGAATTTATGACAATGCATTAGACAATGACAACTACAATCTTGCT
AAAGGTTTCAATTATCACCAAGGACCTGAGTGGCTGTGGCCTATTGGGTATTTTCTTCGT
GCAAAATTATATTTTTCCAGATTGATGGGCCCGGAGACTACTGCAAAGACTATAGTTTTG
GTTAAAAATGTTCTTTCCCGACATTATGTTCATCTTGAGAGATCCCCTTGGAAAGGACTT
CCAGAACTGACCAATGAGAATGCCCAGTACTGTCCTTTCAGCTGTGAAACACAAGCCTGG
TCAATTGCTACTATTCTTGAGACACTTTATGATTTATAG
|
| Enzyme 121 GenBank Gene ID |
AB035443 |
| Enzyme 121 GeneCard ID |
AGL |
| Enzyme 121 GenAtlas ID |
AGL |
| Enzyme 121 HGNC ID |
HGNC:321 |
| Enzyme 121 Chromosome Location |
1 |
| Enzyme 121 Locus |
1p21 |
| Enzyme 121 SNPs |
SNPJam Report |
| Enzyme 121 General References |
- Yang BZ, Ding JH, Enghild JJ, Bao Y, Chen YT: Molecular cloning and nucleotide sequence of cDNA encoding human muscle glycogen debranching enzyme. J Biol Chem. 1992 May 5;267(13):9294-9. [PubMed ]
- Bao Y, Dawson TL Jr, Chen YT: Human glycogen debranching enzyme gene (AGL): complete structural organization and characterization of the 5' flanking region. Genomics. 1996 Dec 1;38(2):155-65. [PubMed ]
- Bao Y, Yang BZ, Dawson TL Jr, Chen YT: Isolation and nucleotide sequence of human liver glycogen debranching enzyme mRNA: identification of multiple tissue-specific isoforms. Gene. 1997 Sep 15;197(1-2):389-98. [PubMed ]
- Okubo M, Horinishi A, Takeuchi M, Suzuki Y, Sakura N, Hasegawa Y, Igarashi T, Goto K, Tahara H, Uchimoto S, Omichi K, Kanno H, Hayasaka K, Murase T: Heterogeneous mutations in the glycogen-debranching enzyme gene are responsible for glycogen storage disease type IIIa in Japan. Hum Genet. 2000 Jan;106(1):108-15. [PubMed ]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed ]
- Cheng A, Zhang M, Gentry MS, Worby CA, Dixon JE, Saltiel AR: A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's disease. Genes Dev. 2007 Oct 1;21(19):2399-409. [PubMed ]
- Okubo M, Kanda F, Horinishi A, Takahashi K, Okuda S, Chihara K, Murase T: Glycogen storage disease type IIIa: first report of a causative missense mutation (G1448R) of the glycogen debranching enzyme gene found in a homozygous patient. Hum Mutat. 1999 Dec;14(6):542-3. [PubMed ]
|
| Enzyme 121 Metabolite References |
Not Available |
|
Enzyme 122
[top]
|
| Enzyme 122 ID |
5611 |
| Enzyme 122 Name |
Trehalase |
| Enzyme 122 Synonyms |
- Alpha,alpha-trehalase
- Alpha,alpha-trehalose glucohydrolase
|
| Enzyme 122 Gene Name |
TREH |
| Enzyme 122 Protein Sequence |
>Trehalase
MPGRTWELCLLLLLGLGLGSQEALPPPCESEIYCHGELLNQVQMAKLYQDDKQFVDMPLS
IAPEQVLQTFTELSRDHNHSIPREQLQAFVHEHFQAKGQELQPWTPADWKDSPQFLQKIS
DAKLRAWAGQLHQLWKKLGKKMKPEVLSHPERFSLIYSEHPFIVPGGRFVEFYYWDSYWV
MEGLLLSEMAETVKGMLQNFLDLVKTYGHVPNGGRVYYLQRSQPPLLTLMMDCYLTHTND
TAFLQENIETLALELDFWTKNRTVSVSLEGKNYLLNRYYVPYGGPRPESYSKDVELADTL
PEGDREALWAELKAGAESGWDFSSRWLIGGPNPNSLSGIRTSKLVPVDLNAFLCQAEELM
SNFYSRLGNDSQATKYRILRSQRLAALNTVLWDEQTGAWFDYDLEKKKKNREFYPSNLTP
LWAGCFSDPGVADKALKYLEDNRILTYQYGIPTSLQKTGQQWDFPNAWAPLQDLVIRGLA
KAPLRRAQEVAFQLAQNWIRTNFDVYSQKSAMYEKYDVSNGGQPGGGGEYEVQEGFGWTN
GVVLMLLDRYGDRLTSGAKLAFLEPHCLAATLLPSLLLSLLPW
|
| Enzyme 122 Number of Residues |
583 |
| Enzyme 122 Molecular Weight |
66567.3 |
| Enzyme 122 Theoretical pI |
5.40 |
| Enzyme 122 GO Classification |
| Function |
- alpha,alpha-trehalase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
- trehalase activity
|
| Process |
- carbohydrate metabolic process
- disaccharide metabolic process
- metabolic process
- oligosaccharide metabolic process
- primary metabolic process
- trehalose metabolic process
|
| Component |
| — |
|
| Enzyme 122 General Function |
Involved in catalytic activity |
| Enzyme 122 Specific Function |
Intestinal trehalase is probably involved in the hydrolysis of ingested trehalose |
| Enzyme 122 Pathways |
- Starch and Sucrose Metabolism (map00500 )
|
| Enzyme 122 Reactions |
- alpha,alpha-trehalose + H2O = 2 D-glucose [RN:R00010 R06103]
|
| Enzyme 122 Pfam Domain Function |
|
| Enzyme 122 Signals |
|
| Enzyme 122 Transmembrane Regions |
|
| Enzyme 122 Essentiality |
Not Available |
| Enzyme 122 GenBank ID Protein |
2789461 |
| Enzyme 122 UniProtKB/Swiss-Prot ID |
O43280 |
| Enzyme 122 UniProtKB/Swiss-Prot Entry Name |
TREA_HUMAN |
| Enzyme 122 PDB ID |
Not Available |
| Enzyme 122 Cellular Location |
Not Available |
| Enzyme 122 Gene Sequence |
>1752 bp
ATGCCAGGGAGGACCTGGGAGCTGTGCCTGCTACTGCTGCTGGGGCTGGGACTGGGGTCC
CAGGAGGCCCTACCCCCACCCTGTGAGAGTGAGATTTACTGCCACGGGGAGCTCCTAAAC
CAAGTTCAAATGGCCAAGCTCTACCAGGATGACAAGCAGTTTGTGGACATGCCACTGTCT
ATAGCTCCAGAACAAGTCCTGCAGACCTTCACTGAGCTGTCCAGGGACCACAATCACAGC
ATCCCCAGGGAGCAGCTGCAGGCGTTTGTCCACGAACACTTCCAGGCCAAGGGGCAGGAG
CTGCAGCCCTGGACCCCTGCAGACTGGAAAGACAGCCCCCAGTTCCTGCAGAAGATTTCA
GATGCCAAACTGCGTGCCTGGGCAGGGCAGCTGCATCAGCTCTGGAAGAAGCTGGGGAAG
AAGATGAAGCCAGAGGTTCTCAGCCACCCTGAGCGGTTCTCTCTCATATACTCAGAACAT
CCTTTCATTGTGCCTGGCGGTCGCTTTGTTGAGTTCTACTACTGGGACTCCTACTGGGTC
ATGGAGGGTCTGCTCCTCTCAGAGATGGCTGAGACGGTGAAGGGCATGCTGCAGAACTTC
TTGGACCTGGTGAAAACCTATGGGCATGTCCCCAATGGTGGGCGCGTGTACTACTTGCAG
CGGAGCCAGCCCCCACTCTTGACCCTCATGATGGATTGCTACTTGACTCACACCAATGAC
ACCGCCTTTCTACAGGAAAACATTGAAACACTAGCCTTGGAATTGGACTTTTGGACCAAG
AACAGGACTGTCTCTGTGAGCTTGGAGGGAAAGAACTACCTCCTGAATCGCTATTATGTC
CCTTATGGGGGACCCAGGCCTGAGTCCTACAGCAAAGATGTGGAGTTGGCTGACACCTTG
CCAGAAGGAGACCGGGAGGCTCTGTGGGCTGAGCTCAAGGCTGGGGCTGAGTCTGGCTGG
GACTTCTCTTCACGCTGGCTCATTGGAGGCCCAAACCCCAACTCGCTTAGCGGCATCCGA
ACAAGCAAACTGGTGCCTGTTGACCTGAATGCCTTCCTATGCCAAGCAGAGGAGCTGATG
AGCAACTTCTATTCCAGGCTGGGGAACGACTCCCAGGCCACGAAGTACAGAATCCTGCGG
TCGCAGCGCTTGGCCGCCCTGAACACAGTCCTGTGGGATGAGCAGACCGGAGCCTGGTTC
GATTACGACCTTGAGAAGAAGAAGAAAAACCGGGAGTTTTACCCATCCAACCTCACTCCA
CTCTGGGCCGGGTGTTTCTCTGACCCTGGCGTGGCGGACAAGGCTCTGAAATACCTGGAG
GACAACCGGATCCTGACTTACCAGTATGGGATCCCGACCTCTCTCCAGAAGACAGGCCAG
CAGTGGGATTTCCCCAATGCCTGGGCCCCCCTGCAGGACTTGGTCATCAGAGGCCTGGCC
AAGGCACCTTTACGTCGGGCCCAGGAAGTGGCTTTCCAGCTGGCTCAGAATTGGATCCGA
ACCAATTTTGATGTCTACTCGCAGAAGTCAGCCATGTATGAGAAGTATGACGTCAGCAAC
GGTGGACAGCCCGGTGGGGGAGGAGAATATGAAGTTCAGGAGGGATTTGGCTGGGACGAA
GGTGTGGTCCTGATGCTGCTGGACCGCTATGGTGACCGGCTGACCTCAGGGGCCAAGCTG
GCTTTCCTGGAGCCCCACTGCCTGGCGGCCACCCTTCTGCCCAGCCTCCTGCTCAGCCTC
CTGCCATGGTGA
|
| Enzyme 122 GenBank Gene ID |
AB000824 |
| Enzyme 122 GeneCard ID |
TREH |
| Enzyme 122 GenAtlas ID |
TREH |
| Enzyme 122 HGNC ID |
HGNC:12266 |
| Enzyme 122 Chromosome Location |
1 |
| Enzyme 122 Locus |
11q23.3 |
| Enzyme 122 SNPs |
SNPJam Report |
| Enzyme 122 General References |
- Ishihara R, Taketani S, Sasai-Takedatsu M, Kino M, Tokunaga R, Kobayashi Y: Molecular cloning, sequencing and expression of cDNA encoding human trehalase. Gene. 1997 Nov 20;202(1-2):69-74. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Sasai-Takedatsu M, Taketani S, Nagata N, Furukawa T, Tokunaga R, Kojima T, Kobayashi Y: Human trehalase: characterization, localization, and its increase in urine by renal proximal tubular damage. Nephron. 1996;73(2):179-85. [PubMed ]
|
| Enzyme 122 Metabolite References |
Not Available |
|
Enzyme 123
[top]
|
| Enzyme 123 ID |
5613 |
| Enzyme 123 Name |
Glucose-6-phosphatase |
| Enzyme 123 Synonyms |
- G-6-Pase
- G6Pase
- Glucose-6-phosphatase alpha
- G6Pase-alpha
|
| Enzyme 123 Gene Name |
G6PC |
| Enzyme 123 Protein Sequence |
>Glucose-6-phosphatase
MEEGMNVLHDFGIQSTHYLQVNYQDSQDWFILVSVIADLRNAFYVLFPIWFHLQEAVGIK
LLWVAVIGDWLNLVFKWILFGQRPYWWVLDTDYYSNTSVPLIKQFPVTCETGPGSPSGHA
MGTAGVYYVMVTSTLSIFQGKIKPTYRFRCLNVILWLGFWAVQLNVCLSRIYLAAHFPHQ
VVAGVLSGIAVAETFSHIHSIYNASLKKYFLITFFLFSFAIGFYLLLKGLGVDLLWTLEK
AQRWCEQPEWVHIDTTPFASLLKNLGTLFGLGLALNSSMYRESCKGKLSKWLPFRLSSIV
ASLVLLHVFDSLKPPSQVELVFYVLSFCKSAVVPLASVSVIPYCLAQVLGQPHKKSL
|
| Enzyme 123 Number of Residues |
357 |
| Enzyme 123 Molecular Weight |
40483.2 |
| Enzyme 123 Theoretical pI |
8.61 |
| Enzyme 123 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 123 General Function |
Involved in catalytic activity |
| Enzyme 123 Specific Function |
Hydrolyzes glucose-6-phosphate to glucose in the endoplasmic reticulum. Forms with the glucose-6-phosphate transporter (SLC37A4/G6PT) the complex responsible for glucose production through glycogenolysis and gluconeogenesis. Hence, it is the key enzyme in homeostatic regulation of blood glucose levels |
| Enzyme 123 Pathways |
|
| Enzyme 123 Reactions |
- D-glucose 6-phosphate + H2O = D-glucose + phosphate [RN:R00303]
|
| Enzyme 123 Pfam Domain Function |
|
| Enzyme 123 Signals |
|
| Enzyme 123 Transmembrane Regions |
- 29-49
61-81
118-138
148-168
180-202
210-230
255-275
292-312
321-341
|
| Enzyme 123 Essentiality |
Not Available |
| Enzyme 123 GenBank ID Protein |
189054175 |
| Enzyme 123 UniProtKB/Swiss-Prot ID |
P35575 |
| Enzyme 123 UniProtKB/Swiss-Prot Entry Name |
G6PC_HUMAN |
| Enzyme 123 PDB ID |
Not Available |
| Enzyme 123 Cellular Location |
Not Available |
| Enzyme 123 Gene Sequence |
>1074 bp
ATGGAGGAAGGAATGAATGTTCTCCATGACTTTGGGATCCAGTCAACACATTACCTCCAG
GTGAATTACCAAGACTCCCAGGACTGGTTCATCTTGGTGTCCGTGATCGCAGACCTCAGG
AATGCCTTCTACGTCCTCTTCCCCATCTGGTTCCATCTTCAGGAAGCTGTGGGCATTAAA
CTCCTTTGGGTAGCTGTGATTGGAGACTGGCTCAACCTCGTCTTTAAGTGGATTCTCTTT
GGACAGCGTCCATACTGGTGGGTTTTGGATACTGACTACTACAGCAACACTTCCGTGCCC
CTGATAAAGCAGTTCCCTGTAACCTGTGAGACTGGACCAGGGAGCCCCTCTGGCCATGCC
ATGGGCACAGCAGGTGTATACTACGTGATGGTCACATCTACTCTTTCCATCTTTCAGGGA
AAGATAAAGCCGACCTACAGATTTCGGTGCTTGAATGTCATTTTGTGGTTGGGATTCTGG
GCTGTGCAGCTGAATGTCTGTCTGTCACGAATCTACCTTGCTGCTCATTTTCCTCATCAA
GTTGTTGCTGGAGTCCTGTCAGGCATTGCTGTTGCAGAAACTTTCAGCCACATCCACAGC
ATCTATAATGCCAGCCTCAAGAAATATTTTCTCATTACCTTCTTCCTGTTCAGCTTCGCC
ATCGGATTTTATCTGCTGCTCAAGGGACTGGGTGTAGACCTCCTGTGGACTCTGGAGAAA
GCCCAGAGGTGGTGCGAGCAGCCAGAATGGGTCCACATTGACACCACACCCTTTGCCAGC
CTCCTCAAGAACCTGGGCACGCTCTTTGGCCTGGGGCTGGCTCTCAACTCCAGCATGTAC
AGGGAGAGCTGCAAGGGGAAACTCAGCAAGTGGCTCCCATTCCGCCTCAGCTCTATTGTA
GCCTCCCTCGTCCTCCTGCACGTCTTTGACTCCTTGAAACCCCCATCCCAAGTCGAGCTG
GTCTTCTACGTCTTGTCCTTCTGCAAGAGTGCGGTAGTGCCCCTGGCATCCGTCAGTGTC
ATCCCCTACTGCCTCGCCCAGGTCCTGGGCCAGCCGCACAAGAAGTCGTTGTAA
|
| Enzyme 123 GenBank Gene ID |
AK313982 |
| Enzyme 123 GeneCard ID |
G6PC |
| Enzyme 123 GenAtlas ID |
G6PC |
| Enzyme 123 HGNC ID |
HGNC:4056 |
| Enzyme 123 Chromosome Location |
1 |
| Enzyme 123 Locus |
17q21 |
| Enzyme 123 SNPs |
SNPJam Report |
| Enzyme 123 General References |
- Lei KJ, Shelly LL, Pan CJ, Sidbury JB, Chou JY: Mutations in the glucose-6-phosphatase gene that cause glycogen storage disease type 1a. Science. 1993 Oct 22;262(5133):580-3. [PubMed ]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed ]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed ]
- Pan CJ, Lei KJ, Chou JY: Asparagine-linked oligosaccharides are localized to a luminal hydrophilic loop in human glucose-6-phosphatase. J Biol Chem. 1998 Aug 21;273(34):21658-62. [PubMed ]
- Ghosh A, Shieh JJ, Pan CJ, Sun MS, Chou JY: The catalytic center of glucose-6-phosphatase. HIS176 is the nucleophile forming the phosphohistidine-enzyme intermediate during catalysis. J Biol Chem. 2002 Sep 6;277(36):32837-42. Epub 2002 Jul 1. [PubMed ]
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