|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5285 |
| Enzyme 1 Name |
Acyl-protein thioesterase 1 |
| Enzyme 1 Synonyms |
- APT-1
- hAPT1
- Lysophospholipase 1
- Lysophospholipase I
- LPL-I
- LysoPLA I
|
| Enzyme 1 Gene Name |
LYPLA1 |
| Enzyme 1 Protein Sequence |
>Acyl-protein thioesterase 1
MCGNNMSTPLPAIVPAARKATAAVIFLHGLGDTGHGWAEAFAGIRSSHIKYICPHAPVRP
VTLNMNVAMPSWFDIIGLSPDSQEDESGIKQAAENIKALIDQEVKNGIPSNRIILGGFSQ
GGALSLYTALTTQQKLAGVTALSCWLPLRASFPQGPIGGANRDISILQCHGDCDPLVPLM
FGSLTVEKLKTLVNPANVTFKTYEGMMHSSCQQEMMDVKQFIDKLLPPID
|
| Enzyme 1 Number of Residues |
230 |
| Enzyme 1 Molecular Weight |
24669.4 |
| Enzyme 1 Theoretical pI |
6.77 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 1 General Function |
Involved in hydrolase activity |
| Enzyme 1 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 1 Pathways |
Not Available |
| Enzyme 1 Reactions |
Not Available |
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
5453722  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O75608  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
LYPA1_HUMAN  |
| Enzyme 1 PDB ID |
1FJ2  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>693 bp
ATGTGCGGCAATAACATGTCAACCCCGCTGCCCGCCATCGTGCCCGCCGCCCGGAAGGCC
ACCGCTGCGGTGATTTTCCTGCATGGATTGGGAGATACTGGGCACGGATGGGCAGAAGCC
TTTGCAGGTATCAGAAGTTCACATATCAAATATATCTGCCCGCATGCGCCTGTTAGGCCT
GTTACATTAAATATGAACGTGGCTATGCCTTCATGGTTTGATATTATTGGGCTTTCACCA
GATTCACAGGAGGATGAATCTGGGATTAAACAGGCAGCAGAAAATATAAAAGCTTTGATT
GATCAAGAAGTGAAGAATGGCATTCCTTCTAACAGAATTATTTTGGGAGGGTTTTCTCAG
GGAGGAGCTTTATCTTTATATACTGCCCTTACCACACAGCAGAAACTGGCAGGTGTCACT
GCACTCAGTTGCTGGCTTCCACTTCGGGCTTCCTTTCCACAGGGTCCTATCGGTGGTGCT
AATAGAGATATTTCTATTCTCCAGTGCCACGGGGATTGTGACCCTTTGGTTCCCCTGATG
TTTGGTTCTCTTACGGTGGAAAAACTAAAAACATTGGTGAATCCAGCCAATGTGACCTTT
AAAACCTATGAAGGTATGATGCACAGTTCGTGTCAACAGGAAATGATGGATGTCAAGCAA
TTCATTGATAAACTCCTACCTCCAATTGATTGA
|
| Enzyme 1 GenBank Gene ID |
NM_006330.2  |
| Enzyme 1 GeneCard ID |
LYPLA1  |
| Enzyme 1 GenAtlas ID |
LYPLA1  |
| Enzyme 1 HGNC ID |
HGNC:6737  |
| Enzyme 1 Chromosome Location |
8 |
| Enzyme 1 Locus |
8q11.23 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5286 |
| Enzyme 2 Name |
Group XV phospholipase A2 |
| Enzyme 2 Synonyms |
- 1-O-acylceramide synthase
- ACS
- LCAT-like lysophospholipase
- LLPL
- Lysophospholipase 3
- Lysosomal phospholipase A2
- LPLA2
|
| Enzyme 2 Gene Name |
PLA2G15 |
| Enzyme 2 Protein Sequence |
>Group XV phospholipase A2
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTV
VHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGK
TFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREM
IEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVL
ASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQ
DIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGD
GTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
|
| Enzyme 2 Number of Residues |
412 |
| Enzyme 2 Molecular Weight |
46657.4 |
| Enzyme 2 Theoretical pI |
6.72 |
| Enzyme 2 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 2 General Function |
Involved in phosphatidylcholine-sterol O-acyltransferase activity |
| Enzyme 2 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 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
Not Available |
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q8NCC3  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PAG15_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 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 2 GenBank Gene ID |
AB017494  |
| Enzyme 2 GeneCard ID |
PLA2G15  |
| Enzyme 2 GenAtlas ID |
PLA2G15  |
| Enzyme 2 HGNC ID |
HGNC:17163  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
16q22.1 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5287 |
| Enzyme 3 Name |
Calcium-dependent phospholipase A2 |
| Enzyme 3 Synonyms |
- Group V phospholipase A2
- PLA2-10
- Phosphatidylcholine 2-acylhydrolase 5
|
| Enzyme 3 Gene Name |
PLA2G5 |
| Enzyme 3 Protein Sequence |
>Calcium-dependent phospholipase A2
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
|
| Enzyme 3 Number of Residues |
138 |
| Enzyme 3 Molecular Weight |
15674.1 |
| Enzyme 3 Theoretical pI |
8.48 |
| Enzyme 3 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 3 General Function |
Involved in phospholipase A2 activity |
| Enzyme 3 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 3 Pathways |
|
| Enzyme 3 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
10862735  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P39877  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PA2G5_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>417 bp
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
|
| Enzyme 3 GenBank Gene ID |
AL158172  |
| Enzyme 3 GeneCard ID |
PLA2G5  |
| Enzyme 3 GenAtlas ID |
PLA2G5  |
| Enzyme 3 HGNC ID |
HGNC:9038  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p36-p34 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5288 |
| Enzyme 4 Name |
Group IIF secretory phospholipase A2 |
| Enzyme 4 Synonyms |
- GIIF sPLA2
- sPLA2-IIF
- Phosphatidylcholine 2-acylhydrolase 2F
|
| Enzyme 4 Gene Name |
PLA2G2F |
| Enzyme 4 Protein Sequence |
>Group IIF secretory phospholipase A2
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
|
| Enzyme 4 Number of Residues |
168 |
| Enzyme 4 Molecular Weight |
18658.0 |
| Enzyme 4 Theoretical pI |
4.94 |
| Enzyme 4 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 4 General Function |
Involved in phospholipase A2 activity |
| Enzyme 4 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 4 Pathways |
|
| Enzyme 4 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
12276060  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9BZM2  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PA2GF_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>507 bp
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
|
| Enzyme 4 GenBank Gene ID |
AF306566  |
| Enzyme 4 GeneCard ID |
PLA2G2F  |
| Enzyme 4 GenAtlas ID |
PLA2G2F  |
| Enzyme 4 HGNC ID |
HGNC:30040  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1p35 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5289 |
| Enzyme 5 Name |
Cytosolic phospholipase A2 |
| Enzyme 5 Synonyms |
- cPLA2
- Phospholipase A2 group IVA
- Phospholipase A2
- Phosphatidylcholine 2-acylhydrolase
- Lysophospholipase
|
| Enzyme 5 Gene Name |
PLA2G4A |
| Enzyme 5 Protein Sequence |
>Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
|
| Enzyme 5 Number of Residues |
749 |
| Enzyme 5 Molecular Weight |
85210.2 |
| Enzyme 5 Theoretical pI |
5.03 |
| Enzyme 5 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 5 General Function |
Involved in metabolic process |
| Enzyme 5 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 5 Pathways |
|
| Enzyme 5 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| 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 |
P47712  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PA24A_HUMAN  |
| Enzyme 5 PDB ID |
1CJY  |
| Enzyme 5 PDB File |
Show |
| Enzyme 5 3D Structure |
|
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 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 5 GenBank Gene ID |
M72393  |
| Enzyme 5 GeneCard ID |
PLA2G4A  |
| Enzyme 5 GenAtlas ID |
PLA2G4A  |
| Enzyme 5 HGNC ID |
HGNC:9035  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
1q25 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5290 |
| Enzyme 6 Name |
Phospholipase A2 |
| Enzyme 6 Synonyms |
- Group IB phospholipase A2
- Phosphatidylcholine 2-acylhydrolase 1B
|
| Enzyme 6 Gene Name |
PLA2G1B |
| Enzyme 6 Protein Sequence |
>Phospholipase A2
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
|
| Enzyme 6 Number of Residues |
148 |
| Enzyme 6 Molecular Weight |
16359.5 |
| Enzyme 6 Theoretical pI |
7.91 |
| Enzyme 6 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 6 General Function |
Involved in phospholipase A2 activity |
| Enzyme 6 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P04054  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PA21B_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>447 bp
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTATGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
|
| Enzyme 6 GenBank Gene ID |
M21054  |
| Enzyme 6 GeneCard ID |
PLA2G1B  |
| Enzyme 6 GenAtlas ID |
PLA2G1B  |
| Enzyme 6 HGNC ID |
HGNC:9030  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
12q23-q24.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 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 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5291 |
| Enzyme 7 Name |
Group XIIB secretory phospholipase A2-like protein |
| Enzyme 7 Synonyms |
- Group XIII secretory phospholipase A2-like protein
- GXIII sPLA2-like
- sPLA2-GXIIB
- GXIIB
|
| Enzyme 7 Gene Name |
PLA2G12B |
| Enzyme 7 Protein Sequence |
>Group XIIB secretory phospholipase A2-like protein
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
|
| Enzyme 7 Number of Residues |
195 |
| Enzyme 7 Molecular Weight |
21658.5 |
| Enzyme 7 Theoretical pI |
5.81 |
| Enzyme 7 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 7 General Function |
Involved in phospholipase A2 activity |
| Enzyme 7 Specific Function |
Not known; does not seem to have catalytic activity |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
Not Available |
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
15824793  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9BX93  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PG12B_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>588 bp
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCAGCCTGTGATTCC
CTGGTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGT
CAGCGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
|
| Enzyme 7 GenBank Gene ID |
AF339053  |
| Enzyme 7 GeneCard ID |
PLA2G12B  |
| Enzyme 7 GenAtlas ID |
PLA2G12B  |
| Enzyme 7 HGNC ID |
HGNC:18555  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
10q22.1 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5292 |
| Enzyme 8 Name |
Group 10 secretory phospholipase A2 |
| Enzyme 8 Synonyms |
- Group X secretory phospholipase A2
- GX sPLA2
- sPLA2-X
- Phosphatidylcholine 2-acylhydrolase 10
|
| Enzyme 8 Gene Name |
PLA2G10 |
| Enzyme 8 Protein Sequence |
>Group 10 secretory phospholipase A2
MGPLPVCLPIMLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPI
AYMKYGCFCGLGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGP
AENKCQELLCKCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
|
| Enzyme 8 Number of Residues |
165 |
| Enzyme 8 Molecular Weight |
18153.0 |
| Enzyme 8 Theoretical pI |
6.46 |
| Enzyme 8 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 8 General Function |
Involved in phospholipase A2 activity |
| Enzyme 8 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 8 Pathways |
|
| Enzyme 8 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O15496  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PA2GX_HUMAN  |
| Enzyme 8 PDB ID |
1LE7  |
| Enzyme 8 PDB File |
Show |
| Enzyme 8 3D Structure |
|
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>498 bp
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
|
| Enzyme 8 GenBank Gene ID |
U95301  |
| Enzyme 8 GeneCard ID |
PLA2G10  |
| Enzyme 8 GenAtlas ID |
PLA2G10  |
| Enzyme 8 HGNC ID |
HGNC:9029  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
16p13.1-p12 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5294 |
| Enzyme 9 Name |
Group IIE secretory phospholipase A2 |
| Enzyme 9 Synonyms |
- GIIE sPLA2
- sPLA2-IIE
- Phosphatidylcholine 2-acylhydrolase 2E
|
| Enzyme 9 Gene Name |
PLA2G2E |
| Enzyme 9 Protein Sequence |
>Group IIE secretory phospholipase A2
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
|
| Enzyme 9 Number of Residues |
142 |
| Enzyme 9 Molecular Weight |
15988.5 |
| Enzyme 9 Theoretical pI |
8.28 |
| Enzyme 9 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 9 General Function |
Involved in phospholipase A2 activity |
| Enzyme 9 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 9 Pathways |
|
| Enzyme 9 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q9NZK7  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PA2GE_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>429 bp
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
|
| Enzyme 9 GenBank Gene ID |
AF189279  |
| Enzyme 9 GeneCard ID |
PLA2G2E  |
| Enzyme 9 GenAtlas ID |
PLA2G2E  |
| Enzyme 9 HGNC ID |
HGNC:13414  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p36.13 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 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 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5295 |
| Enzyme 10 Name |
Acyl-protein thioesterase 2 |
| Enzyme 10 Synonyms |
- APT-2
- Lysophospholipase II
- LPL-II
- LysoPLA II
|
| Enzyme 10 Gene Name |
LYPLA2 |
| Enzyme 10 Protein Sequence |
>Acyl-protein thioesterase 2
MCGNTMSVPLLTDAATVSGAERETAAVIFLHGLGDTGHSWADALSTIRLPHVKYICPHAP
RIPVTLNMKMVMPSWFDLMGLSPDAPEDEAGIKKAAENIKALIEHEMKNGIPANRIVLGG
FSQGGALSLYTALTCPHPLAGIVALSCWLPLHRAFPQAANGSAKDLAILQCHGELDPMVP
VRFGALTAEKLRSVVTPARVQFKTYPGVMHSSCPQEMAAVKEFLEKLLPPV
|
| Enzyme 10 Number of Residues |
231 |
| Enzyme 10 Molecular Weight |
24736.7 |
| Enzyme 10 Theoretical pI |
7.25 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in hydrolase activity |
| Enzyme 10 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 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
9966764  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
O95372  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
LYPA2_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>696 bp
ATGTGTGGTAACACCATGTCTGTGCCCCTGCTCACCGATGCTGCCACCGTGTCTGGAGCT
GAGCGGGAAACGGCCGCGGTTATTTTTTTACATGGACTTGGAGACACAGGGCACAGCTGG
GCTGACGCCCTCTCCACCATCCGGCTCCCTCACGTCAAGTACATCTGTCCCCATGCGCCT
AGGATCCCTGTGACCCTCAACATGAAGATGGTGATGCCCTCCTGGTTTGACCTGATGGGG
CTGAGTCCAGATGCCCCAGAGGACGAGGCTGGCATCAAGAAGGCAGCAGAGAACATCAAG
GCCTTGATTGAGCATGAAATGAAGAACGGGATCCCTGCCAATCGAATCGTCCTGGGAGGC
TTTTCACAGGGCGGGGCCCTGTCCCTCTACACGGCCCTCACCTGCCCCCACCCTCTGGCT
GGCATCGTGGCGTTGAGCTGCTGGCTGCCTCTGCACCGGGCCTTCCCCCAGGCAGCTAAT
GGCAGTGCCAAGGACCTGGCCATACTCCAGTGCCATGGGGAGCTGGACCCCATGGTGCCC
GTACGGTTTGGGGCCCTGACGGCTGAGAAGCTCCGGTCTGTTGTCACACCTGCCAGGGTC
CAGTTCAAGACATACCCGGGTGTCATGCACAGCTCCTGTCCTCAGGAGATGGCAGCTGTG
AAGGAATTTCTTGAGAAGCTGCTGCCTCCTGTCTAA
|
| Enzyme 10 GenBank Gene ID |
NM_007260.2  |
| Enzyme 10 GeneCard ID |
LYPLA2  |
| Enzyme 10 GenAtlas ID |
LYPLA2  |
| Enzyme 10 HGNC ID |
HGNC:6738  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
1p36.11 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 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 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5296 |
| Enzyme 11 Name |
Group XIIA secretory phospholipase A2 |
| Enzyme 11 Synonyms |
- GXII sPLA2
- sPLA2-XII
- Phosphatidylcholine 2-acylhydrolase 12A
|
| Enzyme 11 Gene Name |
PLA2G12A |
| Enzyme 11 Protein Sequence |
>Group XIIA secretory phospholipase A2
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
|
| Enzyme 11 Number of Residues |
189 |
| Enzyme 11 Molecular Weight |
21067.0 |
| Enzyme 11 Theoretical pI |
7.27 |
| Enzyme 11 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 11 General Function |
Involved in phospholipase A2 activity |
| Enzyme 11 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl- phosphatidylcholine or -phosphatidylethanolamine |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
12276062  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9BZM1  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PG12A_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>570 bp
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTGGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
|
| Enzyme 11 GenBank Gene ID |
AF306567  |
| Enzyme 11 GeneCard ID |
PLA2G12A  |
| Enzyme 11 GenAtlas ID |
PLA2G12A  |
| Enzyme 11 HGNC ID |
HGNC:18554  |
| Enzyme 11 Chromosome Location |
4 |
| Enzyme 11 Locus |
4q25 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Gelb MH, Valentin E, Ghomashchi F, Lazdunski M, Lambeau G: Cloning and recombinant expression of a structurally novel human secreted phospholipase A2. J Biol Chem. 2000 Dec 22;275(51):39823-6. [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
]
- 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
]
- Murakami M, Masuda S, Shimbara S, Bezzine S, Lazdunski M, Lambeau G, Gelb MH, Matsukura S, Kokubu F, Adachi M, Kudo I: Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII). J Biol Chem. 2003 Mar 21;278(12):10657-67. Epub 2003 Jan 8. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5297 |
| Enzyme 12 Name |
85 kDa calcium-independent phospholipase A2 |
| Enzyme 12 Synonyms |
- CaI-PLA2
- iPLA2
- Group VI phospholipase A2
- GVI PLA2
|
| Enzyme 12 Gene Name |
PLA2G6 |
| Enzyme 12 Protein Sequence |
>85 kDa calcium-independent phospholipase A2
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHG
VPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHL
LCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGM
YFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFR
NYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNP
TLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKT
VFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVN
ALWETEVYIYEHREEFQKLIQLLLSP
|
| Enzyme 12 Number of Residues |
806 |
| Enzyme 12 Molecular Weight |
89902.3 |
| Enzyme 12 Theoretical pI |
7.28 |
| Enzyme 12 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in metabolic process |
| Enzyme 12 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 12 Pathways |
|
| Enzyme 12 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
3142700  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
O60733  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PA2G6_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 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 12 GenBank Gene ID |
AF064594  |
| Enzyme 12 GeneCard ID |
PLA2G6  |
| Enzyme 12 GenAtlas ID |
PLA2G6  |
| Enzyme 12 HGNC ID |
HGNC:9039  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
22q13.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 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 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5298 |
| Enzyme 13 Name |
Phosphatidylcholine-sterol acyltransferase |
| Enzyme 13 Synonyms |
- Lecithin-cholesterol acyltransferase
- Phospholipid-cholesterol acyltransferase
|
| Enzyme 13 Gene Name |
LCAT |
| Enzyme 13 Protein Sequence |
>Phosphatidylcholine-sterol acyltransferase
MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQL
EAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGV
QIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEY
YRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGS
IKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGR
DFQRFFADLHFEEGWYMWLQSRDLLAGLPAPGVEVYCLYGVGLPTPRTYIYDHGFPYTDP
VGVLYEDGDDTVATRSTELCGLWQGRQPQPVHLLPLHGIQHLNMVFSNLTLEHINAILLG
AYRQGPPASPTASPEPPPPE
|
| Enzyme 13 Number of Residues |
440 |
| Enzyme 13 Molecular Weight |
49577.5 |
| Enzyme 13 Theoretical pI |
6.04 |
| Enzyme 13 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 13 General Function |
Involved in phosphatidylcholine-sterol O-acyltransferase activity |
| Enzyme 13 Specific Function |
Central enzyme in the extracellular metabolism of plasma lipoproteins. Among other substrates it esterifies the free cholesterol transported in plasma lipoproteins |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- phosphatidylcholine + a sterol = 1-acylglycerophosphocholine + a sterol ester [RN:R02114]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
15928623  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P04180  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
LCAT_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1323 bp
ATGGGGCCGCCCGGCTCCCCATGGCAGTGGGTGACGCTGCTGCTGGGGCTGCTGCTCCCT
CCTGCCGCCCCCTTCTGGCTCCTCAATGTGCTCTTCCCCCCGCACACCACGCCCAAGGCT
GAGCTCAGTAACCACACACGGCCCGTCATCCTCGTGCCCGGCTGCCTGGGGAATCAGCTA
GAAGCCAAGCTGGACAAACCAGATGTGGTGAACTGGATGTGCTACCGCAAGACAGAGGAC
TTCTTCACCATCTGGCTGGATCTCAACATGTTCCTACCCCTTGGGGTAGACTGCTGGATC
GATAACACCAGGGTTGTCTACAACCGGAGCTCTGGGCTCGTGTCCAACGCCCCTGGTGTC
CAGATCCGCGTCCCTGGCTTTGGCAAGACCTACTCTGTGGAGTACCTGGACAGCAGCAAG
CTGGCAGGGTACCTGCACACACTGGTGCAGAACCTGGTCAACAATGGCTACGTGCGGGAC
GAGACTGTGCGCGCCGCCCCCTATGACTGGCGGCTGGAGCCCGGCCAGCAGGAGGAGTAC
TACCGCAAGCTCGCAGGGCTGGTGGAGGAGATGCACGCTGCCTATGGGAAGCCTGTCTTC
CTCATTGGCCACAGCCTCGGCTGTCTACACTTGCTCTATTTCCTGCTGCGCCAGCCCCAG
GCCTGGAAGGACCGCTTTATTGATGGCTTCATCTCTCTTGGGGCTCCCTGGGGTGGCTCC
ATCAAGCCCATGCTGGTCTTGGCCTCAGGTGACAACCAGGGCATCCCCATCATGTCCAGC
ATCAAGCTGAAAGAGGAGCAGCGCATAACCACCACCTCCCCCTGGATGTTTCCCTCTCGC
ATGGCGTGGCCTGAGGACCACGTGTTCATTTCCACACCCAGCTTCAACTACACAGGCCGT
GACTTCCAACGCTTCTTTGCAGACCTGCACTTTGAGGAAGGCTGGTACATGTGGCTGCAG
TCACGTGACCTCCTGGCAGGACTCCCAGCACCTGGTGTGGAAGTATACTGTCTTTACGGC
GTGGGCCTGCCCACGCCCCGCACCTACATCTACGACCACGGCTTCCCCTACACGGACCCT
GTGGGTGTGCTCTATGAGGATGGTGATGACACGGTGGCGACCCGCAGCACCGAGCTCTGT
GGCCTGTGGCAGGGCCGCCAGCCACAGCCTGTGCACCTGCTGCCCCTGCACGGGATACAG
CATCTCAACATGGTCTTCAGCAACCTGACCCTGGAGCACATCAATGCCATCCTGCTGGGT
GCCTACCGCCAGGGTCCCCCTGCATCCCCGACTGCCAGCCCAGAGCCCCCGCCTCCTGAA
TAA
|
| Enzyme 13 GenBank Gene ID |
BC014781  |
| Enzyme 13 GeneCard ID |
LCAT  |
| Enzyme 13 GenAtlas ID |
LCAT  |
| Enzyme 13 HGNC ID |
HGNC:6522  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
16q22.1 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- McLean J, Fielding C, Drayna D, Dieplinger H, Baer B, Kohr W, Henzel W, Lawn R: Cloning and expression of human lecithin-cholesterol acyltransferase cDNA. Proc Natl Acad Sci U S A. 1986 Apr;83(8):2335-9. [PubMed
]
- McLean J, Wion K, Drayna D, Fielding C, Lawn R: Human lecithin-cholesterol acyltransferase gene: complete gene sequence and sites of expression. Nucleic Acids Res. 1986 Dec 9;14(23):9397-406. [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
]
- Tata F, Chaves ME, Markham AF, Scrace GD, Waterfield MD, McIntyre N, Williamson R, Humphries SE: The isolation and characterisation of cDNA and genomic clones for human lecithin: cholesterol acyltransferase. Biochim Biophys Acta. 1987 Nov 20;910(2):142-8. [PubMed
]
- Rogne S, Skretting G, Larsen F, Myklebost O, Mevag B, Carlson LA, Holmquist L, Gjone E, Prydz H: The isolation and characterisation of a cDNA clone for human lecithin:cholesterol acyl transferase and its use to analyse the genes in patients with LCAT deficiency and fish eye disease. Biochem Biophys Res Commun. 1987 Oct 14;148(1):161-9. [PubMed
]
- Yang CY, Manoogian D, Pao Q, Lee FS, Knapp RD, Gotto AM Jr, Pownall HJ: Lecithin:cholesterol acyltransferase. Functional regions and a structural model of the enzyme. J Biol Chem. 1987 Mar 5;262(7):3086-91. [PubMed
]
- Schindler PA, Settineri CA, Collet X, Fielding CJ, Burlingame AL: Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion. Protein Sci. 1995 Apr;4(4):791-803. [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
]
- Skretting G, Prydz H: An amino acid exchange in exon I of the human lecithin: cholesterol acyltransferase (LCAT) gene is associated with fish eye disease. Biochem Biophys Res Commun. 1992 Jan 31;182(2):583-7. [PubMed
]
- Klein HG, Lohse P, Pritchard PH, Bojanovski D, Schmidt H, Brewer HB Jr: Two different allelic mutations in the lecithin-cholesterol acyltransferase gene associated with the fish eye syndrome. Lecithin-cholesterol acyltransferase (Thr123----Ile) and lecithin-cholesterol acyltransferase (Thr347----Met). J Clin Invest. 1992 Feb;89(2):499-506. [PubMed
]
- Taramelli R, Pontoglio M, Candiani G, Ottolenghi S, Dieplinger H, Catapano A, Albers J, Vergani C, McLean J: Lecithin cholesterol acyl transferase deficiency: molecular analysis of a mutated allele. Hum Genet. 1990 Jul;85(2):195-9. [PubMed
]
- Gotoda T, Yamada N, Murase T, Sakuma M, Murayama N, Shimano H, Kozaki K, Albers JJ, Yazaki Y, Akanuma Y: Differential phenotypic expression by three mutant alleles in familial lecithin:cholesterol acyltransferase deficiency. Lancet. 1991 Sep 28;338(8770):778-81. [PubMed
]
- Skretting G, Blomhoff JP, Solheim J, Prydz H: The genetic defect of the original Norwegian lecithin:cholesterol acyltransferase deficiency families. FEBS Lett. 1992 Sep 14;309(3):307-10. [PubMed
]
- Maeda E, Naka Y, Matozaki T, Sakuma M, Akanuma Y, Yoshino G, Kasuga M: Lecithin-cholesterol acyltransferase (LCAT) deficiency with a missense mutation in exon 6 of the LCAT gene. Biochem Biophys Res Commun. 1991 Jul 31;178(2):460-6. [PubMed
]
- Funke H, von Eckardstein A, Pritchard PH, Hornby AE, Wiebusch H, Motti C, Hayden MR, Dachet C, Jacotot B, Gerdes U, et al.: Genetic and phenotypic heterogeneity in familial lecithin: cholesterol acyltransferase (LCAT) deficiency. Six newly identified defective alleles further contribute to the structural heterogeneity in this disease. J Clin Invest. 1993 Feb;91(2):677-83. [PubMed
]
- Hill JS, O K, Wang X, Pritchard PH: Lecithin:cholesterol acyltransferase deficiency: identification of a causative gene mutation and a co-inherited protein polymorphism. Biochim Biophys Acta. 1993 Jun 19;1181(3):321-3. [PubMed
]
- Steyrer E, Haubenwallner S, Horl G, Giessauf W, Kostner GM, Zechner R: A single G to A nucleotide transition in exon IV of the lecithin: cholesterol acyltransferase (LCAT) gene results in an Arg140 to His substitution and causes LCAT-deficiency. Hum Genet. 1995 Jul;96(1):105-9. [PubMed
]
- Wiebusch H, Cullen P, Owen JS, Collins D, Sharp PS, Funke H, Assmann G: Deficiency of lecithin:cholesterol acyltransferase due to compound heterozygosity of two novel mutations (Gly33Arg and 30 bp ins) in the LCAT gene. Hum Mol Genet. 1995 Jan;4(1):143-5. [PubMed
]
- Kuivenhoven JA, Stalenhoef AF, Hill JS, Demacker PN, Errami A, Kastelein JJ, Pritchard PH: Two novel molecular defects in the LCAT gene are associated with fish eye disease. Arterioscler Thromb Vasc Biol. 1996 Feb;16(2):294-303. [PubMed
]
- Owen JS, Wiebusch H, Cullen P, Watts GF, Lima VL, Funke H, Assmann G: Complete deficiency of plasma lecithin-cholesterol acyltransferase (LCAT) activity due to a novel homozygous mutation (Gly-30-Ser) in the LCAT gene. Hum Mutat. 1996;8(1):79-82. [PubMed
]
- Okubo M, Aoyama Y, Shio H, Albers JJ, Murase T: A novel missense mutation (Asn5-->Ile) in lecithin: cholesterol acyltransferase (LCAT) gene in a Japanese patient with LCAT deficiency. Int J Clin Lab Res. 1996;26(4):250-4. [PubMed
]
- Blanco-Vaca F, Qu SJ, Fiol C, Fan HZ, Pao Q, Marzal-Casacuberta A, Albers JJ, Hurtado I, Gracia V, Pinto X, Marti T, Pownall HJ: Molecular basis of fish-eye disease in a patient from Spain. Characterization of a novel mutation in the LCAT gene and lipid analysis of the cornea. Arterioscler Thromb Vasc Biol. 1997 Jul;17(7):1382-91. [PubMed
]
- Argyropoulos G, Jenkins A, Klein RL, Lyons T, Wagenhorst B, St Armand J, Marcovina SM, Albers JJ, Pritchard PH, Garvey WT: Transmission of two novel mutations in a pedigree with familial lecithin:cholesterol acyltransferase deficiency: structure-function relationships and studies in a compound heterozygous proband. J Lipid Res. 1998 Sep;39(9):1870-6. [PubMed
]
- Sessa A, Battini G, Meroni M, Daidone G, Carnera I, Brambilla PL, Vigano G, Giordano F, Pallotti F, Torri Tarelli L, Calabresi L, Rolleri M, Bertolini S: Hypocomplementemic type II membranoproliferative glomerulonephritis in a male patient with familial lecithin-cholesterol acyltransferase deficiency due to two different allelic mutations. Nephron. 2001 Jul;88(3):268-72. [PubMed
]
- Nanjee MN, Stocks J, Cooke CJ, Molhuizen HO, Marcovina S, Crook D, Kastelein JP, Miller NE: A novel LCAT mutation (Phe382-->Val) in a kindred with familial LCAT deficiency and defective apolipoprotein B-100. Atherosclerosis. 2003 Sep;170(1):105-13. [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
]
- Calabresi L, Pisciotta L, Costantin A, Frigerio I, Eberini I, Alessandrini P, Arca M, Bon GB, Boscutti G, Busnach G, Frasca G, Gesualdo L, Gigante M, Lupattelli G, Montali A, Pizzolitto S, Rabbone I, Rolleri M, Ruotolo G, Sampietro T, Sessa A, Vaudo G, Cantafora A, Veglia F, Calandra S, Bertolini S, Franceschini G: The molecular basis of lecithin:cholesterol acyltransferase deficiency syndromes: a comprehensive study of molecular and biochemical findings in 13 unrelated Italian families. Arterioscler Thromb Vasc Biol. 2005 Sep;25(9):1972-8. Epub 2005 Jun 30. [PubMed
]
- Idzior-Walus B, Sieradzki J, Kostner G, Malecki MT, Klupa T, Wesolowska T, Rostworowski W, Hartwich J, Walus M, Kiec AD, Naruszewicz M: Familial lecithin-cholesterol acyltransferase deficiency: biochemical characteristics and molecular analysis of a new LCAT mutation in a Polish family. Atherosclerosis. 2006 Apr;185(2):413-20. Epub 2005 Jul 26. [PubMed
]
- Horl G, Kroisel PM, Wagner E, Tiran B, Petek E, Steyrer E: Compound heterozygosity (G71R/R140H) in the lecithin:cholesterol acyltransferase (LCAT) gene results in an intermediate phenotype between LCAT-deficiency and fish-eye disease. Atherosclerosis. 2006 Jul;187(1):101-9. Epub 2005 Oct 10. [PubMed
]
- Gigante M, Ranieri E, Cerullo G, Calabresi L, Iolascon A, Assmann G, Morrone L, Pisciotta L, Schena FP, Gesualdo L: LCAT deficiency: molecular and phenotypic characterization of an Italian family. J Nephrol. 2006 May-Jun;19(3):375-81. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5299 |
| Enzyme 14 Name |
Eosinophil lysophospholipase |
| Enzyme 14 Synonyms |
- Charcot-Leyden crystal protein
- CLC
- Galectin-10
- Gal-10
- Lysolecithin acylhydrolase
|
| Enzyme 14 Gene Name |
CLC |
| Enzyme 14 Protein Sequence |
>Eosinophil lysophospholipase
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR
|
| Enzyme 14 Number of Residues |
142 |
| Enzyme 14 Molecular Weight |
16480.8 |
| Enzyme 14 Theoretical pI |
7.50 |
| Enzyme 14 GO Classification |
| Function |
- binding
- carbohydrate binding
- sugar binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in sugar binding |
| Enzyme 14 Specific Function |
May have both lysophospholipase and carbohydrate-binding activities |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
3399666  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q05315  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
LPPL_HUMAN  |
| Enzyme 14 PDB ID |
1QKQ  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>429 bp
ATGTCCCTGCTACCCGTGCCATACACAGAGGCTGCCTCTTTGTCTACTGGTTCTACTGTG
ACAATCAAAGGGCGACCACTTGTCTGTTTCTTGAATGAACCATATCTGCAGGTGGATTTC
CACACTGAGATGAAGGAGGAATCAGACATTGTCTTCCATTTCCAAGTGTGCTTTGGTCGT
CGTGTGGTCATGAACAGCCGTGAGTATGGGGCCTGGAAGCAGCAGGTGGAATCCAAGAAC
ATGCCCTTTCAGGATGGCCAAGAATTTGAACTGAGCATCTCAGTGCTGCCAGATAAGTAC
CAGGTAATGGTCAATGGCCAATCCTCTTACACCTTTGACCATAGAATCAAGCCTGAGGCT
GTGAAGATGGTGCAAGTGTGGAGAGATATCTCCCTGACCAAATTTAATGTCAGCTATTTA
AAGAGATAA
|
| Enzyme 14 GenBank Gene ID |
AC005393  |
| Enzyme 14 GeneCard ID |
CLC  |
| Enzyme 14 GenAtlas ID |
CLC  |
| Enzyme 14 HGNC ID |
HGNC:2014  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
19q13.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 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 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5301 |
| Enzyme 15 Name |
Phospholipase A2, membrane associated |
| Enzyme 15 Synonyms |
- GIIC sPLA2
- Group IIA phospholipase A2
- Non-pancreatic secretory phospholipase A2
- NPS-PLA2
- Phosphatidylcholine 2-acylhydrolase 2A
|
| Enzyme 15 Gene Name |
PLA2G2A |
| Enzyme 15 Protein Sequence |
>Phospholipase A2, membrane associated
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
|
| Enzyme 15 Number of Residues |
144 |
| Enzyme 15 Molecular Weight |
16082.5 |
| Enzyme 15 Theoretical pI |
9.51 |
| Enzyme 15 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 15 General Function |
Involved in phospholipase A2 activity |
| Enzyme 15 Specific Function |
Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| 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 |
P14555  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
PA2GA_HUMAN  |
| Enzyme 15 PDB ID |
1DB4  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
|
| Enzyme 15 GenBank Gene ID |
M22430  |
| Enzyme 15 GeneCard ID |
PLA2G2A  |
| Enzyme 15 GenAtlas ID |
PLA2G2A  |
| Enzyme 15 HGNC ID |
HGNC:9031  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1p35 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Seilhamer JJ, Pruzanski W, Vadas P, Plant S, Miller JA, Kloss J, Johnson LK: Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. J Biol Chem. 1989 Apr 5;264(10):5335-8. [PubMed
]
- Kramer RM, Hession C, Johansen B, Hayes G, McGray P, Chow EP, Tizard R, Pepinsky RB: Structure and properties of a human non-pancreatic phospholipase A2. J Biol Chem. 1989 Apr 5;264(10):5768-75. [PubMed
]
- Kramer RM, Johansen B, Hession C, Pepinsky RB: Structure and properties of a secretable phospholipase A2 from human platelets. Adv Exp Med Biol. 1990;275:35-53. [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
]
- 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
]
- Kanda A, Ono T, Yoshida N, Tojo H, Okamoto M: The primary structure of a membrane-associated phospholipase A2 from human spleen. Biochem Biophys Res Commun. 1989 Aug 30;163(1):42-8. [PubMed
]
- Hara S, Kudo I, Matsuta K, Miyamoto T, Inoue K: Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid. J Biochem (Tokyo). 1988 Sep;104(3):326-8. [PubMed
]
- Lai CY, Wada K: Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme. Biochem Biophys Res Commun. 1988 Dec 15;157(2):488-93. [PubMed
]
- Minami T, Tojo H, Shinomura Y, Matsuzawa Y, Okamoto M: Purification and characterization of a phospholipase A2 from human ileal mucosa. Biochim Biophys Acta. 1993 Oct 13;1170(2):125-30. [PubMed
]
- Wery JP, Schevitz RW, Clawson DK, Bobbitt JL, Dow ER, Gamboa G, Goodson T Jr, Hermann RB, Kramer RM, McClure DB, et al.: Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 A resolution. Nature. 1991 Jul 4;352(6330):79-82. [PubMed
]
- Scott DL, White SP, Browning JL, Rosa JJ, Gelb MH, Sigler PB: Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. Science. 1991 Nov 15;254(5034):1007-10. [PubMed
]
- Schevitz RW, Bach NJ, Carlson DG, Chirgadze NY, Clawson DK, Dillard RD, Draheim SE, Hartley LW, Jones ND, Mihelich ED, et al.: Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2. Nat Struct Biol. 1995 Jun;2(6):458-65. [PubMed
]
- Kitadokoro K, Hagishita S, Sato T, Ohtani M, Miki K: Crystal structure of human secretory phospholipase A2-IIA complex with the potent indolizine inhibitor 120-1032. J Biochem (Tokyo). 1998 Apr;123(4):619-23. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5302 |
| Enzyme 16 Name |
Group IID secretory phospholipase A2 |
| Enzyme 16 Synonyms |
- GIID sPLA2
- sPLA2-IID
- PLA2IID
- Phosphatidylcholine 2-acylhydrolase 2D
- Secretory-type PLA, stroma-associated homolog
|
| Enzyme 16 Gene Name |
PLA2G2D |
| Enzyme 16 Protein Sequence |
>Group IID secretory phospholipase A2
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
|
| Enzyme 16 Number of Residues |
145 |
| Enzyme 16 Molecular Weight |
16546.1 |
| Enzyme 16 Theoretical pI |
8.28 |
| 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. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined |
| 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 |
5771420  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9UNK4  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
PA2GD_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>438 bp
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
|
| Enzyme 16 GenBank Gene ID |
AF112982  |
| Enzyme 16 GeneCard ID |
PLA2G2D  |
| Enzyme 16 GenAtlas ID |
PLA2G2D  |
| Enzyme 16 HGNC ID |
HGNC:9033  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
1p36.12 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 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 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5309 |
| Enzyme 17 Name |
Phospholipase D2 |
| Enzyme 17 Synonyms |
- PLD 2
- hPLD2
- Choline phosphatase 2
- PLD1C
- Phosphatidylcholine-hydrolyzing phospholipase D2
|
| Enzyme 17 Gene Name |
PLD2 |
| Enzyme 17 Protein Sequence |
>Phospholipase D2
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
|
| Enzyme 17 Number of Residues |
933 |
| Enzyme 17 Molecular Weight |
105986.1 |
| Enzyme 17 Theoretical pI |
7.68 |
| Enzyme 17 GO Classification |
| Function |
- binding
- catalytic activity
- lipid binding
- phosphoinositide binding
- phospholipid binding
- protein binding
|
| Process |
- cell communication
- cellular process
- metabolic process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in protein binding |
| Enzyme 17 Specific Function |
May have a role in signal-induced cytoskeletal regulation and/or endocytosis |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
2645858  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
O14939  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
PLD2_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 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 17 GenBank Gene ID |
AF033850  |
| Enzyme 17 GeneCard ID |
PLD2  |
| Enzyme 17 GenAtlas ID |
PLD2  |
| Enzyme 17 HGNC ID |
HGNC:9068  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
17p13.1 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 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 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5310 |
| Enzyme 18 Name |
Phosphatidylethanolamine N-methyltransferase |
| Enzyme 18 Synonyms |
- PEAMT
- PEMT
- PEMT2
|
| Enzyme 18 Gene Name |
PEMT |
| Enzyme 18 Protein Sequence |
>Phosphatidylethanolamine N-methyltransferase
MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTI
LLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGD
YFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLYE
EPFTAEIYRQKASGSHKRS
|
| Enzyme 18 Number of Residues |
199 |
| Enzyme 18 Molecular Weight |
22133.6 |
| Enzyme 18 Theoretical pI |
8.96 |
| Enzyme 18 GO Classification |
| Function |
- N-methyltransferase activity
- catalytic activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in N-methyltransferase activity |
| Enzyme 18 Specific Function |
Catalyzes three sequential methylation of phosphatidylethanolamine (PE) by AdoMet, thus producing phosphatidylcholine (PC) |
| Enzyme 18 Pathways |
- Phospholipid Synthesis (map00564
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 18 Reactions |
- S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine [RN:R02056]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
- 13-33
46-66
94-114
158-178
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
5459516  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q9UBM1  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
PEMT_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>600 bp
ATGACCCGGCTGCTGGGCTACGTGGACCCCCTGGATCCCAGCTTTGTGGCTGCCGTCATC
ACCATCACCTTCAATCCGCTCTACTGGAATGTGGTTGCACGATGGGAACACAAGACCCGC
AAGCTGAGCAGGGCCTTCGGATCCCCCTACCTGGCCTGCTACTCTCTAAGCATCACCATC
CTGCTCCTGAACTTCCTGCGCTCGCACTGCTTCACGCAGGCCATGCTGAGCCAGCCCAGG
ATGGAGAGCCTGGACACCCCCGCGGCCTACAGCCTGGGCCTCGCGCTCCTGGGACTGGGC
GTCGTGCTCGTGCTCTCCAGCTTCTTTGCACTGGGGTTCGCTGGAACTTTCCTAGGTGAT
TACTTCGGGATCCTCAAGGAGGCGAGAGTGACCGTGTTCCCCTTCAACATCCTGGACAAC
CCCATGTACTGGGGAAGCACAGCCAACTACCTGGGCTGGGCCATCATGCACGCCAGCCCC
ACGGGCCTGCTCCTGACGGTGCTGGTGGCCCTCACCTACATAATGGCTCTCCTATACGAA
GAGCCCTTCACCGCTGAGATCTACCGGCAGAAAGCCTCCGGGTCCCACAAGAGGAGCTGA
|
| Enzyme 18 GenBank Gene ID |
AB029821  |
| Enzyme 18 GeneCard ID |
PEMT  |
| Enzyme 18 GenAtlas ID |
PEMT  |
| Enzyme 18 HGNC ID |
HGNC:8830  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
17p11.2 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Walkey CJ, Shields DJ, Vance DE: Identification of three novel cDNAs for human phosphatidylethanolamine N-methyltransferase and localization of the human gene on chromosome 17p11.2. Biochim Biophys Acta. 1999 Jan 4;1436(3):405-12. [PubMed
]
- Shields DJ, Agellon LB, Vance DE: Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene. Biochim Biophys Acta. 2001 May 31;1532(1-2):105-14. [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
]
- 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
]
- Resseguie M, Song J, Niculescu MD, da Costa KA, Randall TA, Zeisel SH: Phosphatidylethanolamine N-methyltransferase (PEMT) gene expression is induced by estrogen in human and mouse primary hepatocytes. FASEB J. 2007 Aug;21(10):2622-32. Epub 2007 Apr 24. [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 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5311 |
| Enzyme 19 Name |
Phospholipase D1 |
| Enzyme 19 Synonyms |
- PLD 1
- hPLD1
- Choline phosphatase 1
- Phosphatidylcholine-hydrolyzing phospholipase D1
|
| Enzyme 19 Gene Name |
PLD1 |
| Enzyme 19 Protein Sequence |
>Phospholipase D1
MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSA
IYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKF
KHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRR
KQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC
CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRID
NLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKG
YFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLY
KEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGI
DLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKS
IDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGL
KPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQL
DKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLL
PKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIE
NQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQ
AIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLL
IADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCF
RVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFI
NKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
|
| Enzyme 19 Number of Residues |
1074 |
| Enzyme 19 Molecular Weight |
124183.1 |
| Enzyme 19 Theoretical pI |
9.07 |
| Enzyme 19 GO Classification |
| Function |
- binding
- catalytic activity
- lipid binding
- phosphoinositide binding
- phospholipid binding
- protein binding
|
| Process |
- cell communication
- cellular process
- metabolic process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in protein binding |
| Enzyme 19 Specific Function |
Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| 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 |
Q13393  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
PLD1_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>3225 bp
ATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAATTGCTGCTGAC
ATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGGGAGAGGAGGTA
GACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCCCTTTCTCTGCT
ATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCTCCGGCTGTCCA
ATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGGTACCAAGTATT
AATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTAAGAGGAAATTC
AAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTATCCGCATCCCC
ATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGCCTCGAGAGATG
CCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCCTTGGTAGAAGA
AAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATAGAAACTATCAT
GCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATTTGGGACCAAAG
GGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAGGCTTGAATTGC
TGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAGTGAAAGATTCC
TTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGCTGGTAGACAAA
GAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAATCCGAATTGAT
AATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTCGGTGGTGGGGA
GGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAGATCATCGATTT
GGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTAATGCCAAAGGA
TATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTTTTATCACAGAC
TGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAAATCGTTGGAGG
TTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCATAATGCTCTAC
AAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGACTTTGATGCGT
CTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCACCGTCTATTTG
TGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTGTGGGAGGGATT
GACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACGTGGGCAGTGTG
AAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAATGGAGTCTATG
GAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCATCCAGAAGAGT
ATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGTTCTCCAAATTT
AGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCATCAGCAGCATT
GACAGCACCTCCAGTTATTTTAATCACTATAGAAGTCATCACAATTTAATCCATGGTTTA
AAACCCCACTTCAAACTCTTTCACCCGTCCAGTGAGTCTGAGCAAGGACTCACTAGACCT
CATGCTGATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGGGAGAGCTGCATGGGGAA
ACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCAAAGACTGGGTTCAACTT
GATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCCGGATGCCCTGGCATGAC
ATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCACGTCACTTCATCCAGCGC
TGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTTCTTATCCTTTTCTGCTT
CCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGCCTGGGTCTGTCCATGCT
AACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTATAAAGTACCATGAAGAG
TCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGCACTATATCTATATCGAA
AACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCAACAAGATAGGCGATGCC
ATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAATACCGGGTATATGTCGTG
ATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCGGAGGAAATGCTCTACAG
GCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAAATTCCATCCTTGGACAG
TTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCATTCTGTGGTCTTAGAACA
CATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATGTCCACAGCAAGTTGTTA
ATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAAATGACCGCAGCATGCTG
GGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAGAGACTGTTCCTTCAGTA
ATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGACTTCGGCTACAGTGCTTT
AGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTCAGGATCCAGTGAGTGAC
AAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATGCTACAATTTATGACAAG
GTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTCAGCTGAGAGACTTTATA
AACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGGAGGAACTGAAGAAGATC
CGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAGAAAGCCTACTGCCTTCT
GTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTTAA
|
| Enzyme 19 GenBank Gene ID |
U38545  |
| Enzyme 19 GeneCard ID |
PLD1  |
| Enzyme 19 GenAtlas ID |
PLD1  |
| Enzyme 19 HGNC ID |
HGNC:9067  |
| Enzyme 19 Chromosome Location |
3 |
| Enzyme 19 Locus |
3q26 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA: Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem. 1995 Dec 15;270(50):29640-3. [PubMed
]
- Hammond SM, Jenco JM, Nakashima S, Cadwallader K, Gu Q, Cook S, Nozawa Y, Prestwich GD, Frohman MA, Morris AJ: Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha. J Biol Chem. 1997 Feb 7;272(6):3860-8. [PubMed
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5778 |
| Enzyme 20 Name |
Cytosolic phospholipase A2 gamma |
| Enzyme 20 Synonyms |
- cPLA2-gamma
- Phospholipase A2 group IVC
|
| Enzyme 20 Gene Name |
PLA2G4C |
| Enzyme 20 Protein Sequence |
>Cytosolic phospholipase A2 gamma
MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACL
GVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSL
QKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQ
PSWQEARAPETWFEFTPHHAGFPALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG
SALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPED
EGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTT
HNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFET
IRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIE
AWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCL
A
|
| Enzyme 20 Number of Residues |
541 |
| Enzyme 20 Molecular Weight |
60948.1 |
| Enzyme 20 Theoretical pI |
6.93 |
| Enzyme 20 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 20 General Function |
Involved in metabolic process |
| Enzyme 20 Specific Function |
Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
226693354  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q9UP65  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PA24C_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1626 bp
ATGGGAAGCTCTGAAGTTTCCATAATTCCTGGGCTCCAGAAAGAAGAAAAGGCGGCCGTG
GAGAGACGAAGACTTCATGTGCTGAAAGCTCTGAAGAAGCTAAGGATTGAGGCTGATGAG
GCCCCAGTTGTTGCTGTGCTGGGCTCAGGCGGAGGACTGCGGGCTCACATTGCCTGCCTT
GGGGTCCTGAGTGAGATGAAAGAACAGGGCCTGTTGGATGCCGTCACGTACCTCGCAGGG
GTCTCTGGATCCACTTGGGCAATATCTTCTCTCTACACCAATGATGGTGACATGGAAGCT
CTCGAGGCTGACCTGAAACATCGATTTACCCGACAGGAGTGGGACTTGGCTAAGAGCCTA
CAGAAAACCATCCAAGCAGCGAGGTCTGAGAATTACTCTCTGACCGACTTCTGGGCCTAC
ATGGTTATCTCTAAGCAAACCAGAGAACTGCCGGAGTCTCATTTGTCCAATATGAAGAAG
CCCGTGGAAGAAGGGACACTACCCTACCCAATATTTGCAGCCATTGACAATGACCTGCAA
CCTTCCTGGCAGGAGGCAAGAGCACCAGAGACCTGGTTCGAGTTCACCCCTCACCACGCT
GGCTTCTCTGCACTGGGGGCCTTTGTTTCCATAACCCACTTCGGAAGCAAATTCAAGAAG
GGAAGACTGGTCAGAACTCACCCTGAGAGAGACCTGACTTTCCTGAGAGGTTTATGGGGA
AGTGCTCTTGGTAACACTGAAGTCATTAGGGAATACATTTTTGACCAGTTAAGGAATCTG
ACCCTGAAAGGTTTATGGAGAAGGGCTGTTGCTAATGCTAAAAGCATTGGACACCTTATT
TTTGCCCGATTACTGAGGCTGCAAGAAAGTTCACAAGGGGAACATCCTCCCCCAGAAGAT
GAAGGCGGTGAGCCTGAACACACCTGGCTGACTGAGATGCTCGAGAATTGGACCAGGACC
TCCCTGGAAAAGCAGGAGCAGCCCCATGAGGACCCCGAAAGGAAAGGCTCACTCAGTAAC
TTGATGGATTTTGTGAAGAAAACAGGCATTTGCGCTTCAAAGTGGGAATGGGGGACCACT
CACAACTTCCTGTACAAACACGGTGGCATCCGGGACAAGATAATGAGCAGCCGGAAGCAC
CTCCACCTGGTGGATGCTGGTTTAGCCATCAACACTCCCTTCCCACTCGTGCTGCCCCCG
ACGCGGGAGGTTCACCTCATCCTCTCCTTCGACTTCAGTGCCGGAGATCCTTTCGAGACC
ATCCGGGCTACCACTGACTACTGCCGCCGCCACAAGATCCCCTTTCCCCAAGTAGAAGAG
GCTGAGCTGGATTTGTGGTCCAAGGCCCCCGCCAGCTGCTACATCCTGAAAGGAGAAACT
GGACCAGTGGTGATGCATTTTCCCCTGTTCAACATAGATGCCTGTGGAGGTGATATTGAG
GCATGGAGTGACACATACGACACATTCAAGCTTGCTGACACCTACACTCTAGATGTGGTG
GTGCTACTCTTGGCATTAGCCAAGAAGAATGTCAGGGAAAACAAGAAGAAGATCCTTAGA
GAGTTGATGAACGTGGCCGGGCTCTACTACCCGAAGGATAGTGCCCGAAGTTGCTGCTTG
GCATAG
|
| Enzyme 20 GenBank Gene ID |
NM_003706.2  |
| Enzyme 20 GeneCard ID |
PLA2G4C  |
| Enzyme 20 GenAtlas ID |
PLA2G4C  |
| Enzyme 20 HGNC ID |
HGNC:9037  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
19q13.3 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Underwood KW, Song C, Kriz RW, Chang XJ, Knopf JL, Lin LL: A novel calcium-independent phospholipase A2, cPLA2-gamma, that is prenylated and contains homology to cPLA2. J Biol Chem. 1998 Aug 21;273(34):21926-32. [PubMed
]
- Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [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
]
- 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
]
- Jenkins CM, Han X, Yang J, Mancuso DJ, Sims HF, Muslin AJ, Gross RW: Purification of recombinant human cPLA2 gamma and identification of C-terminal farnesylation, proteolytic processing, and carboxymethylation by MALDI-TOF-TOF analysis. Biochemistry. 2003 Oct 14;42(40):11798-807. [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
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5783 |
| Enzyme 21 Name |
Group 3 secretory phospholipase A2 |
| Enzyme 21 Synonyms |
- Group III secretory phospholipase A2
- GIII sPLA2
- sPLA2-III
- Phosphatidylcholine 2-acylhydrolase 3
|
| Enzyme 21 Gene Name |
PLA2G3 |
| Enzyme 21 Protein Sequence |
>Group 3 secretory phospholipase A2
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ
|
| Enzyme 21 Number of Residues |
509 |
| Enzyme 21 Molecular Weight |
57150.5 |
| Enzyme 21 Theoretical pI |
9.23 |
| Enzyme 21 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in phospholipase A2 activity |
| Enzyme 21 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine (PC). Preferential cleavage:1-palmitoyl-2-linoleoyl- phosphatidylethanolamine (PE) > 1-palmitoyl-2-linoleoyl-PC > 1- palmitoyl-2-arachidonoyl-PC > 1-palmitoyl-2-arachidonoyl-PE |
| 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 |
142976884  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9NZ20  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
PA2G3_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1530 bp
ATGGGGGTTCAGGCAGGGCTGTTTGGGATGCTGGGCTTCCTGGGGGTGGCCCTGGGGGGC
TCCCCTGCCCTCCGCTGGTACAGGACCTCCTGCCACTTGACCAAGGCCGTCCCTGGCAAC
CCACTGGGGTACCTGAGCTTCCTGGCCAAGGATGCTCAGGGACTGGCCCTGATCCATGCC
CGCTGGGATGCGCATAGGAGGCTGCAGTCATGTAGCTGGGAGGATGAGCCGGAGCTCACC
GCAGCCTACGGTGCTCTCTGTGCTCATGAGACTGCCTGGGGCTCCTTCATCCACACCCCC
GGACCCGAGCTGCAGAGAGCACTGGCCACTCTTCAGAGTCAGTGGGAGGCATGCCGAGCG
CTTGAGGAGAGTCCAGCAGGGGCCAGGAAGAAGCGAGCAGCAGGGCAGAGTGGAGTCCCT
GGTGGAGGGCACCAGCGAGAGAAGAGAGGATGGACCATGCCTGGCACACTGTGGTGTGGA
GTTGGAGATTCTGCTGGGAACTCCTCGGAGCTGGGGGTCTTCCAGGGACCTGATCTCTGT
TGCCGGGAACATGACCGCTGCCCACAGAACATCTCACCCTTGCAGTACAACTATGGCATC
CGAAACTACCGATTCCACACCATCTCCCACTGTGACTGTGACACCAGGTTTCAGCAATGC
CTACAGAATCAGCACGACTCCATCTCGGACATCGTGGGCGTGGCCTTCTTCAACGTGCTG
GAGATCCCCTGCTTTGTGCTGGAGGAGCAGGAGGCGTGTGTGGCGTGGTACTGGTGGGGC
GGGTGTAGGATGTACGGCACAGTGCCCCTCGCTCGCCTGCAGCCCAGGACCTTCTACAAT
GCCTCCTGGAGCTCCCGGGCCACCTCCCCAACTCCCAGCTCCCGGAGCCCAGCCCCTCCC
AAGCCTCGACAGAAGCAGCACCTTCGGAAGGGGCCACCACATCAGAAAGGGTCCAAGCGC
CCCAGCAAAGCCAACACCACAGCCCTCCAGGACCCTATGGTCTCTCCCAGGCTTGATGTG
GCCCCCACAGGCCTCCAGGGCCCACAGGGTGGCCTAAAACCTCAGGGTGCCCGCTGGGTC
TGCCGCAGCTTCCGCCGCCACCTGGACCAGTGTGAGCACCAGATTGGGCCCCGGGAAATC
GAGTTCCAGCTGCTCAACAGCGCCCAAGAGCCCCTCTTCCACTGCAACTGCACGCGCCGT
CTGGCACGCTTCCTGAGGCTCCACAGCCCACCCGAGGTTACCAACATGCTTTGGGAGCTG
CTGGGCACAACCTGCTTCAAGCTGGCCCCTCCACTGGACTGTGTGGAAGGCAAAAACTGT
TCCAGAGACCCTAGGGCCATCAGGGTGTCAGCCCGGCACTTGCGGAGGCTTCAGCAGAGG
CGACACCAGCTCCAGGATAAAGGCACAGATGAGAGGCAGCCATGGCCTTCAGAGCCCCTG
AGAGGCCCCATGTCATTCTACAACCAGTGCCTGCAGCTAACCCAGGCAGCCAGGAGACCC
GACAGGCAGCAGAAGTCCTGGAGCCAGTGA
|
| Enzyme 21 GenBank Gene ID |
NM_015715.3  |
| Enzyme 21 GeneCard ID |
PLA2G3  |
| Enzyme 21 GenAtlas ID |
PLA2G3  |
| Enzyme 21 HGNC ID |
HGNC:17934  |
| Enzyme 21 Chromosome Location |
2 |
| Enzyme 21 Locus |
22q12.2 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G: Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J Biol Chem. 2000 Mar 17;275(11):7492-6. [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
]
- Murakami M, Masuda S, Shimbara S, Bezzine S, Lazdunski M, Lambeau G, Gelb MH, Matsukura S, Kokubu F, Adachi M, Kudo I: Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII). J Biol Chem. 2003 Mar 21;278(12):10657-67. Epub 2003 Jan 8. [PubMed
]
- Murakami M, Masuda S, Shimbara S, Ishikawa Y, Ishii T, Kudo I: Cellular distribution, post-translational modification, and tumorigenic potential of human group III secreted phospholipase A(2). J Biol Chem. 2005 Jul 1;280(26):24987-98. Epub 2005 Apr 29. [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 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5800 |
| Enzyme 22 Name |
D-beta-hydroxybutyrate dehydrogenase, mitochondrial |
| Enzyme 22 Synonyms |
- BDH
- 3-hydroxybutyrate dehydrogenase
|
| Enzyme 22 Gene Name |
BDH1 |
| Enzyme 22 Protein Sequence |
>D-beta-hydroxybutyrate dehydrogenase, mitochondrial
MLATRLSRPLSRLPGKTLSACDRENGARRPLLLGSTSFIPIGRRTYASAAEPVGSKAVLV
TGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEV
EKVVEIVRSSLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFL
PLIRRAKGRVVNISSMLGRMANPARSPYCITKFGVEAFSDCLRYEMYPLGVKVSVVEPGN
FIAATSLYSPESIQAIAKKMWEELPEVVRKDYGKKYFDEKIAKMETYCSSGSTDTSPVID
AVTHALTATTPYTRYHPMDYYWWLRMQIMTHLPGAISDMIYIR
|
| Enzyme 22 Number of Residues |
343 |
| Enzyme 22 Molecular Weight |
38156.8 |
| Enzyme 22 Theoretical pI |
9.24 |
| Enzyme 22 GO Classification |
| Function |
- binding
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in oxidoreductase activity |
| Enzyme 22 Specific Function |
(R)-3-hydroxybutanoate + NAD(+) = acetoacetate + NADH |
| Enzyme 22 Pathways |
- Butyrate Metabolism (map00650
)
- Synthesis and Degradation of Ketone Bodies (map00072
)
|
| Enzyme 22 Reactions |
- (R)-3-hydroxybutanoate + NAD+ = acetoacetate + NADH + H+ [RN:R01361]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
13543367  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q02338  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
BDH_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1032 bp
ATGCTGGCCACCCGCCTCTCCAGACCCCTGTCACGGCTCCCAGGAAAAACCCTAAGTGCC
TGTGATAGAGAAAATGGAGCAAGACGCCCACTATTGCTTGGTTCTACTTCCTTTATCCCG
ATTGGCCGTCGGACTTATGCCAGTGCGGCGGAGCCGGTTGGCAGCAAAGCTGTCCTGGTC
ACAGGCTGTGACTCTGGATTTGGGTTCTCATTGGCCAAGCATCTGCATTCAAAAGGCTTC
CTTGTGTTTGCTGGCTGCTTGATGAAGGACAAAGGCCATGATGGGGTCAAGGAGCTGGAC
AGCCTAAACAGTGACCGATTGAGAACCGTCCAGCTCAATGTCTGCAGCAGCGAAGAGGTG
GAGAAAGTGGTGGAGATTGTCCGCTCGAGCCTGAAGGACCCTGAGAAAGGCATGTGGGGC
CTCGTTAACAATGCCGGCATCTCAACGTTCGGGGAGGTGGAGTTCACCAGCCTGGAGACC
TACAAGCAGGTGGCAGAAGTGAACCTTTGGGGCACAGTGCGGATGACGAAATCCTTTCTC
CCCCTCATCCGAAGGGCCAAAGGCCGCGTCGTCAATATCAGCAGCATGCTGGGCCGCATG
GCCAACCCGGCCCGCTCCCCGTACTGCATCACCAAGTTCGGGGTAGAGGCTTTCTCGGAC
TGCCTGCGCTATGAGATGTACCCCCTGGGCGTGAAGGTCAGCGTGGTGGAGCCCGGCAAC
TTCATCGCTGCCACCAGCCTTTACAGCCCTGAGAGCATTCAGGCCATCGCCAAGAAGATG
TGGGAGGAGCTGCCTGAGGTCGTGCGCAAGGACTACGGCAAGAAGTACTTTGATGAAAAG
ATCGCCAAGATGGAGACCTACTGCAGCAGTGGCTCCACAGACACGTCCCCTGTCATCGAT
GCTGTCACACACGCCCTGACCGCCACCACCCCCTACACCCGCTACCACCCCATGGACTAC
TACTGGTGGCTGCGAATGCAGATCATGACCCACTTGCCTGGAGCCATCTCCGACATGATC
TACATCCGCTGA
|
| Enzyme 22 GenBank Gene ID |
BC005844  |
| Enzyme 22 GeneCard ID |
BDH1  |
| Enzyme 22 GenAtlas ID |
BDH1  |
| Enzyme 22 HGNC ID |
HGNC:1027  |
| Enzyme 22 Chromosome Location |
3 |
| Enzyme 22 Locus |
3q29 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Marks AR, McIntyre JO, Duncan TM, Erdjument-Bromage H, Tempst P, Fleischer S: Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. J Biol Chem. 1992 Aug 5;267(22):15459-63. [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 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
6007 |
| Enzyme 23 Name |
Choline-phosphate cytidylyltransferase B |
| Enzyme 23 Synonyms |
- CCT-beta
- CTP:phosphocholine cytidylyltransferase B
- CCT B
- CT B
- Phosphorylcholine transferase B
|
| Enzyme 23 Gene Name |
PCYT1B |
| Enzyme 23 Protein Sequence |
>Choline-phosphate cytidylyltransferase B
MPVVTTDAESETGIPKSLSNEPPSETMEEIEHTCPQPRLTLTAPAPFADETNCQCQAPHE
KLTIAQARLGTPADRPVRVYADGIFDLFHSGHARALMQAKTLFPNSYLLVGVCSDDLTHK
FKGFTVMNEAERYEALRHCRYVDEVIRDAPWTLTPEFLEKHKIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFVPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKRY
RFQNQVDKMKEKVKNVEERSKEFVNRVEEKSHDLIQKWEEKSREFIGNFLELFGPDGAWK
QMFQERSSRMLQALSPKQSPVSSPTRSRSPSRSPSPTFSWLPLKTSPPSSPKAASASISS
MSEGDEDEK
|
| Enzyme 23 Number of Residues |
369 |
| Enzyme 23 Molecular Weight |
41939.8 |
| Enzyme 23 Theoretical pI |
6.36 |
| Enzyme 23 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 23 General Function |
Involved in catalytic activity |
| Enzyme 23 Specific Function |
Controls phosphatidylcholine synthesis |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- CTP + choline phosphate = diphosphate + CDP-choline [RN:R01890]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
21361202  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9Y5K3  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PCY1B_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1110 bp
ATGCCAGTAGTTACCACTGATGCTGAGTCAGAAACAGGTATCCCAAAATCCCTTTCCAAT
GAGCCTCCCTCAGAAACCATGGAGGAAATAGAGCACACATGCCCACAGCCTCGACTGACC
CTGACTGCACCTGCCCCATTTGCTGATGAAACCAACTGCCAGTGTCAAGCACCCCATGAA
AAACTGACCATTGCTCAGGCCCGCTTAGGAACACCAGCTGACAGGCCTGTCAGAGTATAC
GCCGATGGAATATTTGACCTCTTCCACTCAGGTCATGCAAGAGCCCTTATGCAAGCAAAA
ACACTGTTTCCCAACAGCTACTTGTTGGTAGGAGTTTGCAGTGATGATCTCACCCACAAA
TTCAAAGGTTTCACCGTGATGAATGAAGCCGAGAGATACGAAGCTCTCAGACACTGTCGC
TACGTAGACGAAGTTATCAGAGATGCTCCCTGGACACTCACGCCAGAGTTTCTGGAAAAA
CACAAGATTGACTTTGTGGCTCATGATGACATTCCGTATTCCTCTGCTGGCTCTGATGAT
GTTTACAAGCACATAAAGGAAGCAGGGATGTTCGTTCCAACGCAGAGAACAGAAGGCATC
TCAACATCGGACATCATTACCAGAATTGTTCGTGACTATGATGTTTATGCCCGACGTAAC
CTCCAGAGAGGGTATACAGCCAAGGAACTGAATGTCAGCTTTATAAATGAGAAGAGGTAC
CGTTTCCAGAACCAAGTGGACAAAATGAAGGAAAAAGTCAAGAATGTGGAGGAAAGATCA
AAGGAATTTGTGAACAGAGTGGAAGAAAAGAGCCATGATCTAATTCAAAAGTGGGAAGAG
AAGTCAAGGGAATTCATTGGCAACTTCCTAGAACTGTTTGGACCTGATGGAGCATGGAAG
CAGATGTTCCAGGAGAGGAGCAGCCGGATGCTGCAGGCCTTATCCCCGAAGCAGAGCCCT
GTGAGCAGCCCAACCCGGAGCCGGTCCCCTTCCCGCTCCCCATCGCCCACCTTCTCATGG
CTTCCACTCAAAACCTCACCCCCTTCCTCACCCAAAGCAGCCTCAGCCTCTATCAGCAGC
ATGAGCGAGGGGGATGAGGATGAAAAGTAG
|
| Enzyme 23 GenBank Gene ID |
NM_004845.4  |
| Enzyme 23 GeneCard ID |
PCYT1B  |
| Enzyme 23 GenAtlas ID |
PCYT1B  |
| Enzyme 23 HGNC ID |
HGNC:8755  |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Lykidis A, Murti KG, Jackowski S: Cloning and characterization of a second human CTP:phosphocholine cytidylyltransferase. J Biol Chem. 1998 May 29;273(22):14022-9. [PubMed
]
- Lykidis A, Baburina I, Jackowski S: Distribution of CTP:phosphocholine cytidylyltransferase (CCT) isoforms. Identification of a new CCTbeta splice variant. J Biol Chem. 1999 Sep 17;274(38):26992-7001. [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
]
- 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 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
6030 |
| Enzyme 24 Name |
Choline-phosphate cytidylyltransferase A |
| Enzyme 24 Synonyms |
- CCT-alpha
- CTP:phosphocholine cytidylyltransferase A
- CCT A
- CT A
- Phosphorylcholine transferase A
|
| Enzyme 24 Gene Name |
PCYT1A |
| Enzyme 24 Protein Sequence |
>Choline-phosphate cytidylyltransferase A
MDAQCSAKVNARKRRKEAPGPNGATEEDGVPSKVQRCAVGLRQPAPFSDEIEVDFSKPYV
RVTMEEASRGTPCERPVRVYADGIFDLFHSGHARALMQAKNLFPNTYLIVGVCSDELTHN
FKGFTVMNENERYDAVQHCRYVDEVVRNAPWTLTPEFLAEHRIDFVAHDDIPYSSAGSDD
VYKHIKEAGMFAPTQRTEGISTSDIITRIVRDYDVYARRNLQRGYTAKELNVSFINEKKY
HLQERVDKVKKKVKDVEEKSKEFVQKVEEKSIDLIQKWEEKSREFIGSFLEMFGPEGALK
HMLKEGKGRMLQAISPKQSPSSSPTRERSPSPSFRWPFSGKTSPPCSPANLSRHKAAAYD
ISEDEED
|
| Enzyme 24 Number of Residues |
367 |
| Enzyme 24 Molecular Weight |
41730.7 |
| Enzyme 24 Theoretical pI |
7.29 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- nucleotidyltransferase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in catalytic activity |
| Enzyme 24 Specific Function |
Controls phosphatidylcholine synthesis |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- CTP + choline phosphate = diphosphate + CDP-choline [RN:R01890]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
28204946  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
P49585  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
PCY1A_HUMAN  |
| Enzyme 24 PDB ID |
1PEH  |
| Enzyme 24 PDB File |
Show |
| Enzyme 24 3D Structure |
|
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1104 bp
ATGGATGCACAGTGTTCAGCCAAGGTCAATGCAAGGAAGAGGAGAAAAGAGGCGCCCGGA
CCCAACGGGGCAACAGAAGAAGATGGGGTTCCTTCCAAAGTGCAGCGCTGTGCAGTGGGC
TTACGGCAACCAGCTCCTTTTTCTGATGAAATTGAAGTTGACTTTAGTAAGCCCTATGTC
AGGGTAACTATGGAAGAAGCCAGCAGAGGAACTCCTTGTGAGCGACCTGTGAGAGTTTAT
GCCGATGGAATATTTGACTTATTTCACTCTGGTCACGCCCGAGCTCTGATGCAAGCGAAG
AACCTTTTCCCTAATACGTACCTCATTGTGGGAGTTTGCAGTGATGAGCTCACACACAAC
TTCAAAGGCTTCACGGTGATGAACGAGAATGAGCGCTATGACGCAGTCCAGCACTGCCGC
TACGTGGATGAGGTGGTGAGGAATGCGCCCTGGACGCTGACACCCGAGTTCCTGGCCGAA
CACCGGATTGATTTTGTAGCCCATGATGATATTCCTTATTCATCTGCTGGCAGTGATGAT
GTTTATAAGCACATCAAGGAGGCAGGCATGTTTGCTCCAACACAGAGGACAGAAGGTATC
TCCACATCAGACATCATCACCCGAATTGTGCGGGATTATGATGTGTATGCGAGGCGGAAC
CTGCAGAGGGGCTACACAGCAAAGGAGCTCAATGTCAGCTTTATCAACGAGAAGAAATAC
CACTTGCAGGAGAGGGTTGACAAAGTAAAGAAGAAAGTGAAAGATGTGGAGGAAAAGTCA
AAAGAATTTGTTCAGAAGGTGGAGGAAAAAAGCATTGACCTCATTCAGAAGTGGGAGGAG
AAGTCCCGAGAATTCATTGGAAGTTTTCTGGAAATGTTTGGTCCGGAAGGAGCACTGAAA
CATATGCTGAAAGAGGGGAAGGGCCGGATGCTGCAGGCCATCAGCCCGAAGCAGAGCCCC
AGCAGCAGCCCTACTCGCGAGCGCTCCCCCTCCCCCTCTTTCCGATGGCCCTTCTCCGGC
AAGACTTCCCCACCTTGCTCCCCAGCAAATCTCTCCAGGCACAAGGCTGCAGCCTATGAT
ATCAGTGAGGATGAAGAAGACTAA
|
| Enzyme 24 GenBank Gene ID |
BC046355  |
| Enzyme 24 GeneCard ID |
PCYT1A  |
| Enzyme 24 GenAtlas ID |
PCYT1A  |
| Enzyme 24 HGNC ID |
HGNC:8754  |
| Enzyme 24 Chromosome Location |
3 |
| Enzyme 24 Locus |
3q29 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Kalmar GB, Kay RJ, LaChance AC, Cornell RB: Primary structure and expression of a human CTP:phosphocholine cytidylyltransferase. Biochim Biophys Acta. 1994 Oct 18;1219(2):328-34. [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
]
- Johnson JE, Cornell RB: Membrane-binding amphipathic alpha-helical peptide derived from CTP:phosphocholine cytidylyltransferase. Biochemistry. 1994 Apr 12;33(14):4327-35. [PubMed
]
- Dunne SJ, Cornell RB, Johnson JE, Glover NR, Tracey AS: Structure of the membrane binding domain of CTP:phosphocholine cytidylyltransferase. Biochemistry. 1996 Sep 17;35(37):11975-84. [PubMed
]
- Xie M, Smith JL, Ding Z, Zhang D, Cornell RB: Membrane binding modulates the quaternary structure of CTP:phosphocholine cytidylyltransferase. J Biol Chem. 2004 Jul 2;279(27):28817-25. Epub 2004 Apr 6. [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
]
- Giorgianni F, Zhao Y, Desiderio DM, Beranova-Giorgianni S: Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line. Electrophoresis. 2007 Jun;28(12):2027-34. [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
]
- 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
]
- 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
]
- 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 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
6049 |
| Enzyme 25 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 2 |
| Enzyme 25 Synonyms |
- Sphingomyelin synthase 2
|
| Enzyme 25 Gene Name |
SGMS2 |
| Enzyme 25 Protein Sequence |
>Phosphatidylcholine:ceramide cholinephosphotransferase 2
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
|
| Enzyme 25 Number of Residues |
365 |
| Enzyme 25 Molecular Weight |
42279.8 |
| Enzyme 25 Theoretical pI |
9.00 |
| Enzyme 25 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 25 General Function |
Involved in catalytic activity |
| Enzyme 25 Specific Function |
Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Required for cell growth |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
- a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
- 80-100
128-148
159-179
206-226
248-268
275-295
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
Not Available |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q8NHU3  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
SMS2_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1098 bp
ATGGATATCATAGAGACAGCAAAACTTGAAGAACATTTGGAAAATCAACCCAGTGATCCT
ACGAACACTTATGCAAGACCCGCTGAACCTGTTGAAGAAGAAAACAAAAATGGCAATGGT
AAACCCAAGAGCTTATCCAGTGGGCTGCGAAAAGGCACCAAAAAGTACCCGGACTATATC
CAAATTGCTATGCCCACTGAATCAAGGAACAAATTTCCACTAGAGTGGTGGAAAACGGGC
ATTGCCTTCATATATGCAGTTTTCAACCTCGTCTTGACAACCGTCATGATCACAGTTGTA
CATGAGAGGGTCCCTCCCAAGGAGCTTAGCCCTCCACTCCCAGACAAGTTTTTTGATTAC
ATTGATAGGGTGAAATGGGCATTTTCTGTATCAGAAATAAATGGGATTATATTAGTTGGA
TTATGGATCACCCAGTGGCTGTTTCTGAGATACAAGTCAATAGTGGGACGCAGATTCTGT
TTTATTATTGGAACTTTATACCTGTATCGCTGCATTACAATGTATGTTACTACTCTACCT
GTGCCTGGAATGCATTTCCAGTGTGCTCCAAAGCTCAATGGAGACTCTCAGGCAAAAGTT
CAACGGATTCTACGATTGATTTCTGGTGGTGGATTGTCCATAACTGGATCACATATCTTA
TGTGGAGACTTCCTCTTCAGCGGTCACACGGTTACGCTGACACTGACTTATTTGTTCATC
AAAGAATATTCGCCTCGTCACTTCTGGTGGTATCATTTAATCTGCTGGCTGCTGAGTGCT
GCCGGGATCATCTGCATTCTTGTAGCACACGAACACTACACTATCGATGTGATCATTGCT
TATTATATCACAACACGACTGTTTTGGTGGTACCATTCAATGGCCAATGAAAAGAACTTG
AAGGTCTCTTCACAGACTAATTTCTTATCTCGAGCATGGTGGTTCCCCATCTTTTATTTT
TTTGAGAAAAATGTACAAGGCTCAATTCCTTGCTGCTTCTCCTGGCCGCTGTCTTGGCCT
CCTGGCTGCTTCAAATCATCATGCAAAAAGTATTCACGGGTTCAGAAGATTGGTGAAGAC
AATGAGAAATCGACCTGA
|
| Enzyme 25 GenBank Gene ID |
AF452717  |
| Enzyme 25 GeneCard ID |
SGMS2  |
| Enzyme 25 GenAtlas ID |
SGMS2  |
| Enzyme 25 HGNC ID |
HGNC:28395  |
| Enzyme 25 Chromosome Location |
4 |
| Enzyme 25 Locus |
4q25 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 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
]
- 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
]
- Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed
]
- Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC: Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice. J Lipid Res. 2006 Jun;47(6):1307-14. Epub 2006 Feb 28. [PubMed
]
- Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC: Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem. 2007 Jun 15;282(24):17537-47. Epub 2007 Apr 22. [PubMed
]
- Tani M, Kuge O: Sphingomyelin synthase 2 is palmitoylated at the COOH-terminal tail, which is involved in its localization in plasma membranes. Biochem Biophys Res Commun. 2009 Apr 10;381(3):328-32. Epub 2009 Feb 20. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
6054 |
| Enzyme 26 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 1 |
| Enzyme 26 Synonyms |
- Medulla oblongata-derived protein
- Protein Mob
- Sphingomyelin synthase 1
- Transmembrane protein 23
|
| Enzyme 26 Gene Name |
SGMS1 |
| Enzyme 26 Protein Sequence |
>Phosphatidylcholine:ceramide cholinephosphotransferase 1
MLSASTMKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSS
DNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKE
MIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFF
DHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTT
LPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYL
FIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQ
VLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT
|
| Enzyme 26 Number of Residues |
419 |
| Enzyme 26 Molecular Weight |
49207.3 |
| Enzyme 26 Theoretical pI |
8.51 |
| Enzyme 26 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 26 General Function |
Involved in catalytic activity |
| Enzyme 26 Specific Function |
Bidirectional lipid cholinephosphotransferase capable of converting phosphatidylcholine (PC) and ceramide to sphingomyelin (SM) and diacylglycerol (DAG) and vice versa. Direction is dependent on the relative concentrations of DAG and ceramide as phosphocholine acceptors. Directly and specifically recognizes the choline head group on the substrate. Also requires two fatty chains on the choline-P donor molecule in order to be recognized efficiently as a substrate. Does not function strictly as a SM synthase. Suppresses BAX-mediated apoptosis and also prevents cell death in response to stimuli such as hydrogen peroxide, osmotic stress, elevated temperature and exogenously supplied sphingolipids. May protect against cell death by reversing the stress-inducible increase in levels of proapoptotic ceramide. Required for cell growth |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
- a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
- 142-162
190-210
221-241
282-302
310-330
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
29789379  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q86VZ5  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
SMS1_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1242 bp
ATGAAGGAAGTGGTTTATTGGTCACCCAAGAAGGTGGCAGACTGGCTGCTGGAGAATGCT
ATGCCAGAATACTGTGAGCCTCTGGAGCATTTCACAGGCCAGGACTTGATCAACCTAACC
CAAGAGGATTTCAAAAAACCCCCCTTGTGCCGAGTCTCCTCTGACAATGGGCAGCGGCTC
CTGGACATGATAGAAACCCTGAAAATGGAGCACCATTTGGAAGCACACAAGAACGGCCAT
GCCAATGGGCACCTCAACATTGGCGTAGACATCCCCACCCCCGACGGCAGCTTCAGCATC
AAGATTAAACCCAACGGGATGCCAAATGGGTATAGGAAAGAGATGATAAAGATCCCCATG
CCAGAACTGGAGCGCTCTCAGTACCCCATGGAGTGGGGCAAGACTTTTCTGGCCTTTCTT
TATGCACTTTCCTGTTTCGTTCTCACCACAGTGATGATCTCGGTCGTCCACGAACGAGTA
CCTCCTAAGGAGGTGCAGCCTCCACTACCGGACACATTTTTTGACCATTTTAACCGGGTG
CAGTGGGCCTTTTCTATTTGTGAAATTAATGGCATGATCCTTGTAGGACTCTGGTTAATT
CAGTGGCTGCTCTTAAAATACAAGTCTATTATTAGCAGAAGATTTTTCTGCATAGTTGGC
ACGCTGTACCTGTATCGGTGTATTACAATGTATGTAACTACACTCCCAGTACCTGGTATG
CATTTCAACTGTTCTCCGAAGCTTTTCGGAGACTGGGAAGCCCAACTGCGAAGAATAATG
AAGCTCATTGCTGGAGGTGGCTTGTCTATCACTGGCTCTCACAACATGTGTGGGGACTAT
CTGTACAGCGGCCACACGGTCATGCTAACACTTACCTACTTATTTATCAAAGAGTATTCC
CCTCGGCGACTCTGGTGGTATCACTGGATTTGCTGGCTTCTCAGCGTAGTTGGAATCTTC
TGTATTCTCTTAGCGCATGACCACTACACTGTGGACGTGGTGGTGGCATATTACATCACC
ACGAGACTCTTCTGGTGGTATCACACTATGGCCAATCAGCAAGTGCTAAAGGAAGCTTCC
CAGATGAACCTCCTGGCCAGGGTGTGGTGGTACAGGCCATTTCAGTACTTTGAAAAGAAT
GTCCAAGGAATTGTACCTCGATCTTACCATTGGCCTTTCCCCTGGCCAGTAGTCCACCTC
AGTAGGCAAGTTAAATACAGCCGGCTGGTGAATGACACATAA
|
| Enzyme 26 GenBank Gene ID |
Not Available |
| Enzyme 26 GeneCard ID |
SGMS1  |
| Enzyme 26 GenAtlas ID |
SGMS1  |
| Enzyme 26 HGNC ID |
HGNC:29799  |
| Enzyme 26 Chromosome Location |
1 |
| Enzyme 26 Locus |
10q11.2 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Yamaoka S, Miyaji M, Kitano T, Umehara H, Okazaki T: Expression cloning of a human cDNA restoring sphingomyelin synthesis and cell growth in sphingomyelin synthase-defective lymphoid cells. J Biol Chem. 2004 Apr 30;279(18):18688-93. Epub 2004 Feb 19. [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
]
- Vladychenskaya IP, Dergunova LV, Dmitrieva VG, Limborska SA: Human gene MOB: structure specification and aspects of transcriptional activity. Gene. 2004 Sep 1;338(2):257-65. [PubMed
]
- Vladychenskaya IP, Dergunova LV, Limborska SA: In vitro and in silico analysis of the predicted human MOB gene encoding a phylogenetically conserved transmembrane protein. Biomol Eng. 2002 Feb;18(6):263-8. [PubMed
]
- Huitema K, van den Dikkenberg J, Brouwers JF, Holthuis JC: Identification of a family of animal sphingomyelin synthases. EMBO J. 2004 Jan 14;23(1):33-44. Epub 2003 Dec 18. [PubMed
]
- Dong J, Liu J, Lou B, Li Z, Ye X, Wu M, Jiang XC: Adenovirus-mediated overexpression of sphingomyelin synthases 1 and 2 increases the atherogenic potential in mice. J Lipid Res. 2006 Jun;47(6):1307-14. Epub 2006 Feb 28. [PubMed
]
- Tafesse FG, Huitema K, Hermansson M, van der Poel S, van den Dikkenberg J, Uphoff A, Somerharju P, Holthuis JC: Both sphingomyelin synthases SMS1 and SMS2 are required for sphingomyelin homeostasis and growth in human HeLa cells. J Biol Chem. 2007 Jun 15;282(24):17537-47. Epub 2007 Apr 22. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
6057 |
| Enzyme 27 Name |
Choline kinase alpha |
| Enzyme 27 Synonyms |
- CK
- CHETK-alpha
- Ethanolamine kinase
- EK
|
| Enzyme 27 Gene Name |
CHKA |
| Enzyme 27 Protein Sequence |
>Choline kinase alpha
MKTKFCTGGEAEPSPLGLLLSCGSGSAAPAPGVGQQRDAASDLESKQLGGQQPPLALPPP
PPLPLPLPLPQPPPPQPPADEQPEPRTRRRAYLWCKEFLPGAWRGLREDEFHISVIRGGL
SNMLFQCSLPDTTATLGDEPRKVLLRLYGAILQMRSCNKEGSEQAQKENEFQGAEAMVLE
SVMFAILAERSLGPKLYGIFPQGRLEQFIPSRRLDTEELSLPDISAEIAEKMATFHGMKM
PFNKEPKWLFGTMEKYLKEVLRIKFTEESRIKKLHKLLSYNLPLELENLRSLLESTPSPV
VFCHNDCQEGNILLLEGRENSEKQKLMLIDFEYSSYNYRGFDIGNHFCEWMYDYSYEKYP
FFRANIRKYPTKKQQLHFISSYLPAFQNDFENLSTEEKSIIKEEMLLEVNRFALASHFLW
GLWSIVQAKISSIEFGYMDYAQARFDAYFHQKRKLGV
|
| Enzyme 27 Number of Residues |
457 |
| Enzyme 27 Molecular Weight |
52248.5 |
| Enzyme 27 Theoretical pI |
6.52 |
| Enzyme 27 GO Classification |
Not Available |
| Enzyme 27 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 27 Specific Function |
Has a key role in phospholipid biosynthesis and may contribute to tumor cell growth. Catalyzes the first step in phosphatidylcholine biosynthesis. Contributes to phosphatidylethanolamine biosynthesis. Phosphorylates choline and ethanolamine. Has higher activity with choline |
| Enzyme 27 Pathways |
- Phospholipid Synthesis (map00564
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 27 Reactions |
- ATP + ethanolamine = ADP + O-phosphoethanolamine [RN:R01468]
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
47078276  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P35790  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
CHKA_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1374 bp
ATGAAAACCAAATTCTGCACCGGGGGCGAGGCGGAGCCCTCGCCGCTCGGGCTGCTGCTG
AGCTGCGGTAGCGGCAGCGCGGCCCCGGCGCCCGGCGTGGGGCAGCAGCGCGACGCCGCC
AGCGACCTCGAGTCCAAGCAGCTGGGCGGCCAACAGCCGCCGCTCGCGCTGCCCCCTCCG
CCGCCGCTGCCGCTGCCGCTGCCGCTGCCCCAGCCCCCGCCGCCGCAGCCGCCCGCAGAC
GAGCAGCCGGAGCCCCGGACGCGGCGCAGGGCCTATCTGTGGTGCAAGGAGTTCCTGCCC
GGCGCCTGGCGGGGCCTCCGCGAGGACGAGTTCCACATCAGTGTCATCAGAGGCGGCCTT
AGCAACATGCTGTTCCAGTGCTCCCTACCTGACACCACAGCCACCCTTGGTGATGAGCCT
CGGAAAGTGCTCCTGCGGCTGTATGGAGCGATTTTGCAGATGAGGTCCTGTAATAAAGAG
GGATCCGAACAAGCTCAGAAAGAAAATGAATTTCAAGGGGCTGAGGCCATGGTTCTGGAG
AGCGTTATGTTTGCCATTCTCGCAGAGAGGTCACTTGGGCCAAAACTCTATGGCATCTTT
CCCCAAGGCCGACTGGAGCAGTTCATCCCGAGCCGGCGATTAGATACTGAAGAATTAAGT
TTGCCAGATATTTCTGCAGAAATCGCCGAGAAAATGGCTACATTTCATGGTATGAAAATG
CCATTCAATAAGGAACCAAAATGGCTTTTTGGCACAATGGAAAAGTATCTAAAGGAAGTG
CTGAGAATTAAATTTACTGAGGAATCCAGAATTAAAAAGCTCCACAAATTGCTCAGTTAC
AATCTGCCCTTGGAACTGGAAAACCTGAGATCATTGCTTGAATCTACTCCATCTCCAGTT
GTATTTTGTCATAATGACTGTCAAGAAGGTAATATCTTGTTGCTGGAAGGCCGAGAGAAT
TCTGAAAAACAGAAACTGATGCTCATTGATTTCGAATACAGCAGTTACAATTACAGGGGA
TTCGACATTGGAAATCACTTCTGTGAGTGGATGTATGATTATAGCTATGAAAAATACCCT
TTTTTCAGAGCAAACATCCGGAAGTATCCCACCAAGAAACAACAGCTCCATTTTATTTCC
AGTTACTTGCCTGCATTCCAAAATGACTTTGAAAACCTCAGTACTGAAGAAAAATCCATT
ATAAAAGAAGAAATGTTGCTTGAAGTTAATAGGTTTGCCCTTGCATCTCATTTCCTCTGG
GGACTGTGGTCCATTGTACAAGCCAAGATTTCATCTATTGAATTTGGGTACATGGACTAC
GCCCAAGCAAGGTTTGATGCCTATTTCCACCAGAAGAGGAAGCTTGGGGTGTGA
|
| Enzyme 27 GenBank Gene ID |
NM_001277.2  |
| Enzyme 27 GeneCard ID |
CHKA  |
| Enzyme 27 GenAtlas ID |
CHKA  |
| Enzyme 27 HGNC ID |
HGNC:1937  |
| Enzyme 27 Chromosome Location |
1 |
| Enzyme 27 Locus |
11q13.2 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Hosaka K, Tanaka S, Nikawa J, Yamashita S: Cloning of a human choline kinase cDNA by complementation of the yeast cki mutation. FEBS Lett. 1992 Jun 15;304(2-3):229-32. [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
]
- Gallego-Ortega D, Ramirez de Molina A, Ramos MA, Valdes-Mora F, Barderas MG, Sarmentero-Estrada J, Lacal JC: Differential role of human choline kinase alpha and beta enzymes in lipid metabolism: implications in cancer onset and treatment. PLoS One. 2009 Nov 12;4(11):e7819. [PubMed
]
- Malito E, Sekulic N, Too WC, Konrad M, Lavie A: Elucidation of human choline kinase crystal structures in complex with the products ADP or phosphocholine. J Mol Biol. 2006 Nov 24;364(2):136-51. Epub 2006 Sep 3. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
6427 |
| Enzyme 28 Name |
Probable phospholipid-transporting ATPase IG |
| Enzyme 28 Synonyms |
- ATPase IQ
- ATPase class VI type 11C
|
| Enzyme 28 Gene Name |
ATP11C |
| Enzyme 28 Protein Sequence |
>Probable phospholipid-transporting ATPase IG
MQMVPSLPPASECAGEEKRVGTRTVFVGNHPVSETEAYIAQRFCDNRIVSSKYTLWNFLP
KNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDCLRHRAD
NEVNKSTVYIIENAKRVRKESEKIKVGDVVEVQADETFPCDLILLSSCTTDGTCYVTTAS
LDGESNCKTHYAVRDTIALCTAESIDTLRAAIECEQPQPDLYKFVGRINIYSNSLEAVAR
SLGPENLLLKGATLKNTEKIYGVAVYTGMETKMALNYQGKSQKRSAVEKSINAFLIVYLF
ILLTKAAVCTTLKYVWQSTPYNDEPWYNQKTQKERETLKVLKMFTDFLSFMVLFNFIIPV
SMYVTVEMQKFLGSFFISWDKDFYDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTEN
SMEFIECCIDGHKYKGVTQEVDGLSQTDGTLTYFDKVDKNREELFLRALCLCHTVEIKTN
DAVDGATESAELTYISSSPDEIALVKGAKRYGFTFLGNRNGYMRVENQRKEIEEYELLHT
LNFDAVRRRMSVIVKTQEGDILLFCKGADSAVFPRVQNHEIELTKVHVERNAMDGYRTLC
VAFKEIAPDDYERINRQLIEAKMALQDREEKMEKVFDDIETNMNLIGATAVEDKLQDQAA
ETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHE
LLIEYRKKLLHEFPKSTRSFKKAWTEHQEYGLIIDGSTLSLILNSSQDSSSNNYKSIFLQ
ICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKE
GRQAARNSDYSVPKFKHLKKLLLAHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGF
SQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTSDPRLYMKISGNAMLQLGPFL
YWTFLAAFEGTVFFFGTYFLFQTASLEENGKVYGNWTFGTIVFTVLVFTVTLKLALDTRF
WTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLSSVSTWLAIILLIFIS
LFPEILLIVLKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNVL
|
| Enzyme 28 Number of Residues |
1132 |
| Enzyme 28 Molecular Weight |
129476.0 |
| Enzyme 28 Theoretical pI |
6.63 |
| Enzyme 28 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 28 General Function |
Involved in ATP binding |
| Enzyme 28 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
- 67-85
87-107
291-311
347-367
880-900
909-929
956-976
996-1016
1027-1047
1070-1090
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
39573513  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q8NB49  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
AT11C_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>3399 bp
ATGCAGATGGTCCCATCTCTCCCTCCAGCCTCTGAGTGTGCTGGAGAAGAGAAACGAGTT
GGCACACGCACAGTGTTTGTTGGCAATCATCCAGTTTCGGAAACAGAAGCTTACATTGCA
CAAAGATTTTGTGATAATAGAATAGTCTCATCTAAGTATACACTTTGGAATTTTCTCCCA
AAGAATCTGTTTGAACAGTTTAGAAGAATTGCAAATTTTTATTTTCTCATAATCTTCCTT
GTACAGGTCACAGTAGACACACCAACTAGCCCAGTTACCAGTGGACTTCCACTTTTCTTT
GTTATAACTGTTACAGCCATCAAGCAGGGATATGAGGATTGGCTGAGACACAGAGCTGAC
AATGAAGTCAACAAAAGCACTGTTTACATTATTGAAAATGCAAAGCGAGTGAGAAAAGAA
AGTGAAAAAATCAAGGTTGGTGATGTAGTAGAAGTACAGGCAGATGAAACCTTTCCCTGT
GATCTTATTCTTCTATCATCTTGCACCACTGATGGAACCTGTTATGTCACTACAGCCAGT
CTTGATGGGGAATCCAATTGCAAGACACATTATGCAGTACGTGATACCATTGCACTGTGT
ACAGCAGAATCCATCGATACCCTCCGAGCAGCAATTGAATGTGAACAGCCTCAACCTGAC
CTCTACAAATTTGTTGGGCGAATCAATATCTACAGTAATAGTCTTGAGGCTGTTGCCAGG
TCTTTGGGACCTGAAAATCTCTTGCTGAAAGGAGCTACGCTAAAAAATACCGAGAAGATA
TATGGAGTTGCTGTTTACACTGGAATGGAAACCAAAATGGCTTTGAACTACCAAGGGAAA
TCTCAGAAACGTTCTGCTGTTGAAAAATCTATTAATGCTTTCCTGATTGTATATTTATTT
ATCTTACTGACCAAAGCTGCAGTATGCACTACTCTAAAGTATGTTTGGCAAAGTACCCCA
TACAATGATGAACCTTGGTATAACCAAAAGACTCAGAAAGAGCGAGAGACCTTGAAGGTT
TTAAAAATGTTCACCGACTTCCTATCATTTATGGTTCTATTCAACTTTATCATTCCTGTC
TCCATGTACGTCACAGTAGAAATGCAGAAATTCTTGGGCTCCTTCTTCATCTCATGGGAT
AAGGACTTTTATGATGAAGAAATTAATGAAGGAGCCCTGGTTAACACATCAGACCTTAAT
GAAGAACTTGGTCAGGTGGATTATGTATTTACAGATAAGACTGGAACACTCACTGAAAAC
AGCATGGAATTCATTGAATGCTGCATAGATGGCCACAAATATAAAGGTGTAACTCAAGAG
GTTGATGGATTATCTCAAACTGATGGAACTTTAACATATTTTGACAAAGTAGATAAGAAT
CGAGAAGAGCTGTTTCTACGTGCCTTGTGTTTATGTCATACTGTAGAAATCAAAACAAAC
GATGCTGTTGATGGAGCTACAGAATCAGCTGAATTAACCTATATCTCCTCTTCACCAGAT
GAAATAGCTTTGGTGAAAGGAGCTAAAAGGTACGGGTTCACATTTTTAGGAAATCGAAAT
GGATATATGAGAGTAGAGAACCAAAGAAAAGAAATAGAAGAATATGAACTTCTTCACACC
TTAAACTTTGATGCTGTCCGGCGACGTATGAGTGTAATTGTGAAGACTCAAGAAGGAGAC
ATACTTCTCTTTTGTAAAGGAGCAGACTCGGCAGTTTTTCCCAGAGTGCAAAATCATGAA
ATTGAGTTAACTAAAGTCCATGTGGAACGTAATGCAATGGATGGGTATCGGACACTCTGT
GTAGCCTTCAAAGAAATTGCTCCAGATGATTATGAAAGAATTAACAGACAGCTCATAGAG
GCAAAAATGGCCTTACAAGACAGAGAAGAAAAAATGGAAAAAGTTTTCGATGATATTGAG
ACAAACATGAATTTAATTGGAGCCACTGCAGTTGAAGACAAGCTACAAGATCAAGCTGCA
GAGACCATTGAAGCTCTGCATGCAGCAGGCCTGAAAGTCTGGGTGCTCACTGGGGACAAG
ATGGAGACAGCTAAATCCACATGCTATGCCTGCCGCCTTTTCCAGACCAACACTGAGCTC
TTAGAACTAACCACAAAAACCATTGAAGAAAGTGAAAGGAAAGAAGATCGATTACATGAA
TTATTGATAGAATATCGCAAGAAATTGCTGCATGAGTTTCCTAAAAGTACTAGAAGCTTT
AAAAAAGCATGGACAGAACATCAGGAATATGGATTAATCATAGATGGCTCCACATTGTCA
CTCATACTAAATTCTAGTCAAGACTCTAGTTCAAACAATTACAAAAGCATTTTCCTACAA
ATATGTATGAAGTGTACTGCAGTGCTCTGCTGTCGGATGGCACCATTACAGAAAGCCCAG
ATTGTCAGAATGGTGAAGAATTTAAAAGGCAGCCCAATAACTCTGTCGATAGGTGATGGT
GCCAATGATGTTAGTATGATCTTGGAATCCCATGTGGGAATAGGTATTAAAGGCAAAGAA
GGTCGCCAAGCAGCTAGGAATAGCGATTATTCTGTTCCAAAGTTTAAACACTTAAAGAAA
CTGCTGTTGGCTCATGGACATCTATATTATGTGAGAATAGCACACCTTGTACAGTACTTC
TTCTATAAGAACCTTTGTTTCATTTTGCCACAGTTTTTGTACCAGTTCTTCTGTGGATTC
TCACAACAGCCACTGTATGATGCTGCTTACCTTACAATGTACAATATCTGCTTCACATCC
TTGCCCATCCTGGCCTATAGTCTACTGGAACAGCACATCAACATTGACACTCTGACCTCA
GATCCCCGATTGTATATGAAAATTTCTGGCAATGCCATGCTACAGTTGGGCCCCTTCTTA
TATTGGACATTTCTGGCTGCCTTTGAAGGGACAGTGTTCTTCTTTGGGACTTACTTTCTT
TTTCAGACTGCATCCCTAGAAGAAAATGGAAAGGTATACGGAAACTGGACTTTTGGAACC
ATTGTTTTTACAGTCTTAGTATTCACTGTAACCCTGAAGCTTGCCTTGGATACCCGATTC
TGGACGTGGATAAATCACTTTGTGATTTGGGGTTCTTTAGCCTTCTATGTATTTTTCTCA
TTCTTCTGGGGAGGAATTATTTGGCCTTTTCTCAAGCAACAGAGAATGTATTTTGTATTT
GCCCAAATGCTGTCTTCTGTATCCACATGGTTGGCTATAATTCTTCTAATATTTATCAGC
CTGTTCCCTGAGATTCTTCTGATAGTATTAAAGAATGTAAGAAGAAGAAGTGCCAGGAGA
AATCTGAGCTGTAGAAGGGCATCTGACTCATTATCCGCCAGACCTTCAGTCAGACCTCTT
CTTTTACGAACATTCTCAGACGAATCTAATGTATTGTAA
|
| Enzyme 28 GenBank Gene ID |
AJ580093  |
| Enzyme 28 GeneCard ID |
ATP11C  |
| Enzyme 28 GenAtlas ID |
ATP11C  |
| Enzyme 28 HGNC ID |
HGNC:13554  |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Andrew Nesbit M, Bowl MR, Harding B, Schlessinger D, Whyte MP, Thakker RV: X-linked hypoparathyroidism region on Xq27 is evolutionarily conserved with regions on 3q26 and 13q34 and contains a novel P-type ATPase. Genomics. 2004 Dec;84(6):1060-70. [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
]
- 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
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [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
]
- 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
]
- 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 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
6428 |
| Enzyme 29 Name |
Probable phospholipid-transporting ATPase IH |
| Enzyme 29 Synonyms |
- ATPase IS
- ATPase class VI type 11A
|
| Enzyme 29 Gene Name |
ATP11A |
| Enzyme 29 Protein Sequence |
>Probable phospholipid-transporting ATPase IH
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNF
IPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHK
ADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTT
ASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPV
VRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVY
LCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYII
PVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLT
ENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHT
VQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNREN
HIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVER
NAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATA
VEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEE
QSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNY
RELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGI
GVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLY
QFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALL
RWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKL
ALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIV
LLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF
|
| Enzyme 29 Number of Residues |
1134 |
| Enzyme 29 Molecular Weight |
129754.6 |
| Enzyme 29 Theoretical pI |
6.58 |
| Enzyme 29 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 29 General Function |
Involved in ATP binding |
| Enzyme 29 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
- 62-82
89-110
297-318
350-372
882-902
915-934
965-986
1001-1023
1030-1050
1069-1093
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
150421684  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
P98196  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
AT11A_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>3405 bp
ATGGACTGCAGCCTCGTGCGGACGCTCGTGCACAGATACTGTGCAGGAGAAGAGAATTGG
GTGGACAGCAGGACCATCTACGTGGGACACAGGGAGCCACCTCCGGGCGCAGAGGCCTAC
ATCCCACAGAGATACCCAGACAACAGGATCGTCTCGTCCAAGTACACATTTTGGAACTTT
ATACCCAAGAATTTATTTGAACAATTCAGAAGAGTAGCCAACTTTTATTTCCTTATCATA
TTTCTGGTGCAGTTGATTATTGATACACCCACAAGTCCAGTGACAAGCGGACTTCCACTC
TTCTTTGTCATTACTGTGACGGCTATCAAACAGGGTTATGAAGACTGGCTTCGACATAAA
GCAGACAATGCCATGAACCAGTGTCCTGTTCATTTCATTCAGCACGGCAAGCTCGTTCGG
AAACAAAGTCGAAAGCTGCGAGTTGGGGACATTGTCATGGTTAAGGAGGACGAGACCTTT
CCCTGCGACTTGATCTTCCTTTCCAGCAACCGGGGAGATGGGACGTGCCACGTCACCACC
GCCAGCTTGGATGGAGAATCCAGCCATAAAACGCATTACGCGGTCCAGGACACCAAAGGC
TTCCACACAGAGGAGGATATCGGCGGACTTCACGCCACCATCGAGTGTGAGCAGCCCCAG
CCCGACCTCTACAAGTTCGTGGGTCGCATCAACGTTTACAGTGACCTGAATGACCCCGTG
GTGAGGCCCTTAGGATCGGAAAACCTGCTGCTTAGAGGAGCTACACTGAAGAACACTGAG
AAAATCTTTGGTGTGGCTATTTACACGGGAATGGAAACCAAGATGGCATTAAATTATCAA
TCAAAATCTCAGAAGCGATCTGCCGTGGAAAAATCGATGAATGCGTTCCTCATTGTGTAT
CTCTGCATTCTGATCAGCAAAGCCCTGATAAACACTGTGCTGAAATACATGTGGCAGAGT
GAGCCCTTTCGGGATGAGCCGTGGTATAATCAGAAAACGGAGTCGGAAAGGCAGAGGAAT
CTGTTCCTCAAGGCATTCACGGACTTCCTGGCCTTCATGGTCCTCTTTAACTACATCATC
CCTGTGTCCATGTACGTCACGGTCGAGATGCAGAAGTTCCTCGGCTCTTACTTCATCACC
TGGGACGAAGACATGTTTGACGAGGAGACTGGCGAGGGGCCTCTGGTGAACACGTCGGAC
CTCAATGAAGAGCTGGGACAGGTGGAGTACATCTTCACAGACAAGACCGGCACCCTCACG
GAAAACAACATGGAGTTCAAGGAGTGCTGCATCGAAGGCCATGTCTACGTGCCCCACGTC
ATCTGCAACGGGCAGGTCCTCCCAGAGTCGTCAGGAATCGACATGATTGACTCGTCCCCC
AGCGTCAACGGGAGGGAGCGCGAGGAGCTGTTTTTCCGGGCCCTCTGTCTCTGCCACACC
GTCCAGGTGAAAGACGATGACAGCGTAGACGGCCCCAGGAAATCGCCGGACGGGGGGAAA
TCCTGTGTGTACATCTCATCCTCGCCCGACGAGGTGGCGCTGGTCGAAGGTGTCCAGAGA
CTTGGCTTTACCTACCTAAGGCTGAAGGACAATTACATGGAGATATTAAACAGGGAGAAC
CACATCGAAAGGTTTGAATTGCTGGAAATTTTGAGTTTTGACTCAGTCAGAAGGAGAATG
AGTGTAATTGTAAAATCTGCTACAGGAGAAATTTATCTGTTTTGCAAAGGAGCAGATTCT
TCGATATTCCCCCGAGTGATAGAAGGCAAAGTTGACCAGATCCGAGCCAGAGTGGAGCGT
AACGCAGTGGAGGGGCTCCGAACTTTGTGTGTTGCTTATAAAAGGCTGATCCAAGAAGAA
TATGAAGGCATTTGTAAGCTGCTGCAGGCTGCCAAAGTGGCCCTTCAAGATCGAGAGAAA
AAGTTAGCAGAAGCCTATGAGCAAATAGAGAAAGATCTTACTCTGCTTGGTGCTACAGCT
GTTGAGGACCGGCTGCAGGAGAAAGCTGCAGACACCATCGAGGCCCTGCAGAAGGCCGGG
ATCAAAGTCTGGGTTCTCACGGGAGACAAGATGGAGACGGCCGCGGCCACGTGCTACGCC
TGCAAGCTCTTCCGCAGGAACACGCAGCTGCTGGAGCTGACCACCAAGAGGATCGAGGAG
CAGAGCCTGCACGACGTCCTGTTCGAGCTGAGCAAGACGGTCCTGCGCCACAGCGGGAGC
CTGACCAGAGACAACCTGTCCGGACTTTCAGCAGATATGCAGGACTACGGTTTAATTATC
GACGGAGCTGCACTGTCTCTGATAATGAAGCCTCGAGAAGACGGGAGTTCCGGCAACTAC
AGGGAGCTCTTCCTGGAAATCTGCCGGAGCTGCAGCGCGGTGCTCTGCTGCCGCATGGCG
CCCTTGCAGAAGGCTCAGATTGTTAAATTAATCAAATTTTCAAAAGAGCACCCAATCACG
TTAGCAATTGGCGATGGTGCAAATGATGTCAGCATGATTCTGGAAGCGCACGTGGGCATA
GGTGTCATCGGCAAGGAAGGCCGCCAGGCTGCCAGGAACAGCGACTATGCAATCCCAAAG
TTTAAGCATTTGAAGAAGATGCTGCTTGTTCACGGGCATTTTTATTACATTAGGATCTCT
GAGCTCGTGCAGTACTTCTTCTATAAGAACGTCTGCTTCATCTTCCCTCAGTTTTTATAC
CAGTTCTTCTGTGGGTTTTCACAACAGACTTTGTACGACACCGCGTATCTGACCCTCTAC
AACATCAGCTTCACCTCCCTCCCCATCCTCCTGTACAGCCTCATGGAGCAGCATGTTGGC
ATTGACGTGCTCAAGAGAGACCCGACCCTGTACAGGGACGTCGCCAAGAATGCCCTGCTG
CGCTGGCGCGTGTTCATCTACTGGACGCTCCTGGGACTGTTTGACGCACTGGTGTTCTTC
TTTGGTGCTTATTTCGTGTTTGAAAATACAACTGTGACAAGCAACGGGCAGATATTTGGA
AACTGGACGTTTGGAACGCTGGTATTCACCGTGATGGTGTTCACAGTTACACTAAAGCTT
GCATTGGACACACACTACTGGACTTGGATCAACCATTTTGTCATCTGGGGGTCGCTGCTG
TTCTACGTTGTCTTTTCGCTTCTCTGGGGAGGAGTGATCTGGCCGTTCCTCAACTACCAG
AGGATGTACTACGTGTTCATCCAGATGCTGTCCAGCGGGCCCGCCTGGCTGGCCATCGTG
CTGCTGGTGACCATCAGCCTCCTTCCCGACGTCCTCAAGAAAGTCCTGTGCCGGCAGCTG
TGGCCAACAGCAACAGAGAGAGTCCAGACTAAGAGCCAGTGCCTTTCTGTCGAGCAGTCA
ACCATCTTTATGCTTTCTCAGACTTCCAGCAGCCTGAGTTTCTGA
|
| Enzyme 29 GenBank Gene ID |
NM_015205.2  |
| Enzyme 29 GeneCard ID |
ATP11A  |
| Enzyme 29 GenAtlas ID |
ATP11A  |
| Enzyme 29 HGNC ID |
HGNC:13552  |
| Enzyme 29 Chromosome Location |
1 |
| Enzyme 29 Locus |
13q34 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed
]
- Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
6465 |
| Enzyme 30 Name |
Probable phospholipid-transporting ATPase VA |
| Enzyme 30 Synonyms |
- ATPase class V type 10A
- Aminophospholipid translocase VA
|
| Enzyme 30 Gene Name |
ATP10A |
| Enzyme 30 Protein Sequence |
>Probable phospholipid-transporting ATPase VA
MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLA
DNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILA
ITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPAD
ILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDL
SRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRS
KLERQMNCDVLWCVLLLVCMSLFSAVGHGLWIWRYQEKKSLFYVPKSDGSSLSPVTAAVY
SFLTMIIVLQVLIPISLYVSIEIVKACQVYFINQDMQLYDEETDSQLQCRALNITEDLGQ
IQYIFSDKTGTLTENKMVFRRCTVSGVEYSHDANAQRLARYQEADSEEEEVVPRGGSVSQ
RGSIGSHQSVRVVHRTQSTKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEK
VSECDKSLAVARHQEHLLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRTKVRVRFELK
SPVKTIEDFLRRFTPSCLTSGCSSIGSLAANKSSHKLGSSFPSTPSSDGMLLRLEERLGQ
PTSAIASNGYSSQADNWASELAQEQESERELRYEAESPDEAALVYAARAYNCVLVERLHD
QVSVELPHLGRLTFELLHTLGFDSVRKRMSVVIRHPLTDEINVYTKGADSVVMDLLQPCS
SVDARGRHQKKIRSKTQNYLNVYAAEGLRTLCIAKRVLSKEEYACWLQSHLEAESSLENS
EELLFQSAIRLETNLHLLGATGIEDRLQDGVPETISKLRQAGLQIWVLTGDKQETAVNIA
YACKLLDHDEEVITLNATSQEACAALLDQCLCYVQSRGLQRAPEKTKGKVSMRFSSLCPP
STSTASGRRPSLVIDGRSLAYALEKNLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRS
KLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPKFRYLERLLILHGHW
CYSRLANMVLYFFYKNTMFVGLLFWFQFFCGFSASTMIDQWYLIFFNLLFSSLPPLVTGV
LDRDVPANVLLTNPQLYKSGQNMEEYRPRTFWFNMADAAFQSLVCFSIPYLAYYDSNVDL
FTWGTPIVTIALLTFLLHLGIETKTWTWLNWITCGFSVLLFFTVALIYNASCATCYPPSN
PYWTMQALLGDPVFYLTCLMTPVAALLPRLFFRSLQGRVFPTQLQLARQLTRKSPRRCSA
PKETFAQGRLPKDSGTEHSSGRTVKTSVPLSQPSWHTQQPVCSLEASGEPSTVDMSMPVR
EHTLLEGLSAPAPMSSAPGEAVLRSPGGCPEESKVRAASTGRVTPLSSLFSLPTFSLLNW
ISSWSLVSRLGSVLQFSRTEQLADGQAGRGLPVQPHSGRSGLQGPDHRLLIGASSRRSQ
|
| Enzyme 30 Number of Residues |
1499 |
| Enzyme 30 Molecular Weight |
167686.6 |
| Enzyme 30 Theoretical pI |
8.43 |
| Enzyme 30 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 30 General Function |
Involved in ATP binding |
| Enzyme 30 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
- 87-106
111-128
310-332
363-384
1088-1108
1120-1140
1171-1192
1200-1222
1229-1249
1268-1292
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
14424433  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
O60312  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
AT10A_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>4500 bp
ATGGAGCGGGAGCCGGCGGGGACCGAGGAGCCCGGGCCTCCGGGACGGCGGAGGCGCCGA
GAGGGCAGGACGCGCACGGTGCGCTCCAACCTGCTGCCGCCCCCGGGCGCCGAGGACCCT
GCGGCTGGCGCGGCCAAGGGCGAGCGGCGACGGCGGCGCGGGTGTGCCCAGCACCTGGCC
GACAACCGGCTCAAGACTACCAAGTACACGCTGCTGTCCTTCCTGCCCAAGAACCTGTTC
GAGCAGTTCCACCGCCCGGCCAACGTGTACTTTGTCTTCATCGCGCTGCTCAACTTCGTG
CCGGCGGTGAACGCCTTCCAGCCCGGCCTGGCACTGGCGCCGGTGCTCTTCATCCTGGCC
ATCACGGCCTTCAGGGACCTGTGGGAGGACTACAGCCGCCACCGCTCCGACCACAAGATC
AACCACCTGGGCTGCCTGGTCTTCAGCAGGGAAGAAAAGAAATACGTGAACCGATTCTGG
AAAGAAATCCACGTGGGAGACTTTGTGCGTCTTCGCTGCAACGAAATCTTCCCTGCGGAC
ATTCTGCTGCTCTCCTCCAGTGACCCCGACGGGCTATGCCACATCGAGACCGCCAACCTG
GATGGAGAGACCAACCTGAAGCGGCGGCAGGTGGTCCGCGGCTTCTCGGAGCTTGTCTCC
GAATTCAATCCTTTGACGTTCACCAGCGTGATCGAATGCGAGAAGCCAAACAACGACCTG
AGTAGGTTTCGCGGCTGCATCATACATGACAACGGGAAAAAGGCCGGGCTGTATAAAGAA
AACCTGCTGCTGAGGGGCTGCACCCTTAGGAACACGGACGCAGTCGTCGGCATTGTCATC
TACGCAGGACATGAAACCAAGGCTCTGCTGAACAACAGTGGGCCCCGCTACAAGCGCAGC
AAGCTGGAGAGGCAGATGAACTGCGACGTGCTCTGGTGTGTCCTGCTCCTTGTTTGCATG
TCTCTGTTTTCAGCAGTCGGACATGGACTGTGGATATGGCGGTATCAAGAGAAGAAGTCA
TTATTTTATGTCCCCAAGTCTGATGGAAGCTCCTTATCCCCAGTCACAGCTGCAGTTTAC
TCATTTTTAACAATGATAATAGTTCTGCAGGTTTTGATCCCAATTTCCTTATACGTTTCC
ATTGAAATTGTTAAAGCATGCCAAGTGTACTTCATTAACCAGGACATGCAGTTGTATGAC
GAAGAAACAGACTCGCAGCTGCAGTGCCGAGCTCTGAACATCACGGAAGACTTAGGACAG
ATACAGTACATTTTCTCAGATAAAACTGGCACTTTGACAGAGAATAAGATGGTTTTCCGA
AGATGCACTGTGTCTGGTGTAGAATATTCTCATGATGCAAATGCGCAGCGTCTGGCCAGG
TACCAAGAGGCAGACTCGGAGGAGGAGGAGGTGGTGCCCAGAGGGGGCTCGGTGTCCCAG
CGCGGCAGCATCGGCAGCCACCAGAGTGTCCGGGTGGTGCACAGAACCCAGAGCACCAAG
TCCCACCGGCGCACGGGCAGCCGGGCCGAGGCCAAGAGGGCCAGCATGCTGTCCAAGCAC
ACGGCCTTCAGCAGCCCCATGGAGAAGGATATCACGCCCGACCCAAAGCTGCTGGAGAAG
GTGAGTGAGTGTGACAAGAGCCTAGCCGTGGCGAGGCATCAGGAGCACCTGCTGGCCCAC
CTCTCGCCTGAGCTGTCTGACGTCTTTGATTTCTTCATCGCACTCACCATCTGCAACACA
GTCGTCGTCACGTCCCCGGATCAGCCACGAACAAAGGTGAGGGTGAGGTTTGAGCTGAAG
TCCCCGGTGAAGACGATAGAAGACTTCCTGCGGAGGTTCACACCCAGCTGCCTGACCTCA
GGCTGCAGCAGCATCGGGAGCCTGGCCGCCAACAAGTCCAGCCACAAGTTGGGCTCCAGC
TTCCCGTCCACCCCGTCCAGCGACGGCATGCTTCTCAGGCTGGAGGAGAGGCTGGGCCAG
CCCACCTCGGCCATCGCCAGCAACGGCTACAGCAGCCAGGCGGACAACTGGGCCTCGGAG
CTTGCTCAGGAGCAGGAGTCAGAGCGCGAGCTGCGGTACGAGGCGGAGAGCCCGGATGAG
GCCGCACTGGTGTATGCGGCCAGAGCCTACAACTGCGTGCTTGTGGAGCGGCTGCACGAC
CAAGTGTCAGTGGAGCTGCCCCACCTGGGCAGGCTCACCTTCGAGCTCCTGCACACACTG
GGTTTCGATTCCGTCCGCAAGAGGATGTCAGTGGTGATCCGGCACCCGCTTACCGATGAG
ATCAACGTCTACACCAAGGGGGCCGACTCAGTGGTCATGGATCTCCTGCAGCCCTGCTCT
TCAGTTGACGCCAGAGGGAGGCATCAAAAAAAGATTCGGAGCAAAACTCAGAATTACCTC
AACGTGTATGCGGCGGAAGGCCTGCGCACCTTGTGCATCGCCAAGAGAGTTCTGAGTAAA
GAAGAGTATGCCTGCTGGTTGCAAAGCCACCTAGAAGCCGAATCCTCCCTGGAAAACAGC
GAGGAGCTCCTCTTCCAGTCTGCCATTCGCCTGGAGACCAACCTGCACTTGTTAGGTGCC
ACTGGGATTGAAGACCGCCTGCAGGACGGAGTCCCTGAAACTATTTCTAAATTGCGTCAA
GCGGGCCTGCAGATTTGGGTTCTCACTGGTGACAAACAAGAAACAGCTGTCAACATTGCA
TATGCCTGCAAACTGCTGGACCACGACGAGGAGGTCATCACCCTGAATGCCACCTCCCAG
GAGGCGTGTGCAGCCCTGCTAGACCAGTGCCTATGCTACGTGCAGTCCAGAGGCCTCCAG
AGAGCCCCTGAGAAGACCAAGGGCAAAGTGAGCATGAGGTTCTCCTCTCTCTGCCCACCC
TCCACGTCCACTGCCTCTGGCCGCAGACCCAGCCTCGTGATCGATGGGAGAAGCCTGGCC
TACGCTCTCGAGAAAAACCTGGAGGACAAATTCCTCTTCCTTGCCAAGCAGTGCCGCTCC
GTCCTCTGCTGTCGGTCGACGCCTCTGCAGAAGAGCATGGTGGTGAAGCTGGTGCGGAGC
AAGCTCAAGGCCATGACCCTGGCCATAGGTGATGGAGCCAATGATGTCAGCATGATCCAG
GTGGCAGATGTGGGTGTGGGAATCTCCGGCCAGGAGGGTATGCAGGCAGTGATGGCCAGC
GACTTTGCAGTGCCGAAATTCCGATACCTGGAGAGGCTCTTGATTCTTCACGGGCATTGG
TGCTACTCCCGACTTGCCAACATGGTGCTGTACTTCTTCTACAAAAACACAATGTTCGTG
GGCCTCCTGTTTTGGTTCCAGTTTTTCTGTGGCTTCTCTGCATCTACCATGATTGACCAG
TGGTATCTAATCTTCTTTAATCTGCTCTTCTCGTCACTTCCCCCGCTCGTGACTGGGGTG
CTGGACAGGGATGTGCCAGCCAATGTGCTGCTGACCAACCCGCAGCTCTACAAGAGTGGC
CAGAACATGGAGGAATACCGGCCACGAACGTTCTGGTTTAACATGGCCGACGCCGCCTTC
CAGAGCCTGGTTTGCTTTTCCATTCCTTACCTGGCCTACTATGACTCGAACGTGGACCTG
TTTACCTGGGGGACCCCTATTGTGACAATCGCGCTGCTCACTTTCCTGCTCCACCTGGGC
ATTGAAACCAAAACCTGGACCTGGCTCAACTGGATAACGTGTGGCTTCAGTGTCCTTTTG
TTTTTCACCGTGGCTTTGATTTACAATGCGTCTTGTGCCACGTGCTATCCTCCGTCCAAC
CCTTACTGGACTATGCAAGCCTTACTGGGTGACCCAGTGTTTTACTTGACTTGCCTGATG
ACGCCTGTCGCTGCACTGCTGCCCAGATTGTTTTTCAGATCCCTCCAGGGGAGGGTTTTC
CCCACACAACTTCAGCTGGCACGTCAGTTGACCAGGAAGTCCCCCAGGAGATGCAGTGCT
CCCAAAGAGACCTTTGCTCAGGGACGCCTCCCGAAGGACTCGGGAACCGAGCACTCATCA
GGGAGGACAGTCAAGACCTCTGTGCCCCTGTCCCAGCCTTCTTGGCACACACAGCAGCCG
GTCTGCTCCCTGGAGGCCAGCGGGGAGCCCAGCACAGTGGACATGAGCATGCCAGTGAGG
GAGCACACCCTGCTGGAGGGGCTGAGCGCACCGGCCCCCATGTCCTCTGCGCCAGGGGAG
GCTGTCCTGAGGAGTCCAGGAGGGTGTCCTGAGGAGTCCAAGGTGAGAGCTGCCAGCACC
GGCAGGGTGACCCCCCTGTCTTCCCTCTTCAGCCTGCCTACCTTCAGCTTACTCAACTGG
ATTTCCTCCTGGTCGCTGGTCAGCAGGCTGGGGAGTGTCTTACAGTTCTCCCGGACGGAG
CAGCTTGCAGATGGACAAGCGGGACGTGGACTTCCTGTCCAGCCCCACTCAGGCCGATCA
GGACTTCAAGGGCCAGACCACAGACTACTTATAGGAGCATCTTCAAGGCGGTCACAGTGA
|
| Enzyme 30 GenBank Gene ID |
NM_024490.3  |
| Enzyme 30 GeneCard ID |
ATP10A  |
| Enzyme 30 GenAtlas ID |
ATP10A  |
| Enzyme 30 HGNC ID |
HGNC:13542  |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
15q11.2 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Meguro M, Kashiwagi A, Mitsuya K, Nakao M, Kondo I, Saitoh S, Oshimura M: A novel maternally expressed gene, ATP10C, encodes a putative aminophospholipid translocase associated with Angelman syndrome. Nat Genet. 2001 May;28(1):19-20. [PubMed
]
- Herzing LB, Kim SJ, Cook EH Jr, Ledbetter DH: The human aminophospholipid-transporting ATPase gene ATP10C maps adjacent to UBE3A and exhibits similar imprinted expression. Am J Hum Genet. 2001 Jun;68(6):1501-5. Epub 2001 May 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
]
- 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
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
6488 |
| Enzyme 31 Name |
Probable phospholipid-transporting ATPase IC |
| Enzyme 31 Synonyms |
- ATPase class I type 8B member 1
- Familial intrahepatic cholestasis type 1
|
| Enzyme 31 Gene Name |
ATP8B1 |
| Enzyme 31 Protein Sequence |
>Probable phospholipid-transporting ATPase IC
MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRK
ECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAA
NLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEV
IKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFK
MSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVI
RNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHA
YWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFIN
WDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHR
DASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVD
RTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDR
KRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKE
IEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISK
LAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYA
KFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKR
RLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNM
IKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFA
FTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYI
VGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASAL
VITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNAL
RQPYIWLTIILAVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRR
GVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS
|
| Enzyme 31 Number of Residues |
1251 |
| Enzyme 31 Molecular Weight |
143694.1 |
| Enzyme 31 Theoretical pI |
7.16 |
| Enzyme 31 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 31 General Function |
Involved in ATP binding |
| Enzyme 31 Specific Function |
May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
- 109-130
137-156
341-362
390-411
950-970
983-1002
1033-1054
1069-1091
1098-1118
1139-1163
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
5031697  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
O43520  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
AT8B1_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>3756 bp
ATGAGTACAGAAAGAGACTCAGAAACGACATTTGACGAGGATTCTCAGCCTAATGACGAA
GTGGTTCCCTACAGTGATGATGAAACAGAAGATGAACTTGATGACCAGGGGTCTGCTGTT
GAACCAGAACAAAACCGAGTCAACAGGGAAGCAGAGGAGAACCGGGAGCCATTCAGAAAA
GAATGTACATGGCAAGTCAAAGCAAACGATCGCAAGTACCACGAACAACCTCACTTTATG
AACACAAAATTCTTGTGTATTAAGGAGAGTAAATATGCGAATAATGCAATTAAAACATAC
AAGTACAACGCATTTACCTTTATACCAATGAATCTGTTTGAGCAGTTTAAGAGAGCAGCC
AATTTATATTTCCTGGCTCTTCTTATCTTACAGGCAGTTCCTCAAATCTCTACCCTGGCT
TGGTACACCACACTAGTGCCCCTGCTTGTGGTGCTGGGCGTCACTGCAATCAAAGACCTG
GTGGACGATGTGGCTCGCCATAAAATGGATAAGGAAATCAACAATAGGACGTGTGAAGTC
ATTAAGGATGGCAGGTTCAAAGTTGCTAAGTGGAAAGAAATTCAAGTTGGAGACGTCATT
CGTCTGAAAAAAAATGATTTTGTTCCAGCTGACATTCTCCTGCTGTCTAGCTCTGAGCCT
AACAGCCTCTGCTATGTGGAAACAGCAGAACTGGATGGAGAAACCAATTTAAAATTTAAG
ATGTCACTTGAAATCACAGACCAGTACCTCCAAAGAGAAGATACATTGGCTACATTTGAT
GGTTTTATTGAATGTGAAGAACCCAATAACAGACTAGATAAGTTTACAGGAACACTATTT
TGGAGAAACACAAGTTTTCCTTTGGATGCTGATAAAATTTTGTTACGTGGCTGTGTAATT
AGGAACACCGATTTCTGCCACGGCTTAGTCATTTTTGCAGGTGCTGACACTAAAATAATG
AAGAATAGTGGGAAAACCAGATTTAAAAGAACTAAAATTGATTACTTGATGAACTACATG
GTTTACACGATCTTTGTTGTTCTTATTCTGCTTTCTGCTGGTCTTGCCATCGGCCATGCT
TATTGGGAAGCACAGGTGGGCAATTCCTCTTGGTACCTCTATGATGGAGAAGACGATACA
CCCTCCTACCGTGGATTCCTCATTTTCTGGGGCTATATCATTGTTCTCAACACCATGGTA
CCCATCTCTCTCTATGTCAGCGTGGAAGTGATTCGTCTTGGACAGAGTCACTTCATCAAC
TGGGACCTGCAAATGTACTATGCTGAGAAGGACACACCCGCAAAAGCTAGAACCACCACA
CTCAATGAACAGCTCGGGCAGATCCATTATATCTTCTCTGATAAGACGGGGACACTCACA
CAAAATATCATGACCTTTAAAAAGTGCTGTATCAACGGGCAGATATATGGGGACCATCGG
GATGCCTCTCAACACAACCACAACAAAATAGAGCAAGTTGATTTTAGCTGGAATACATAT
GCTGATGGGAAGCTTGCATTTTATGACCACTATCTTATTGAGCAAATCCAGTCAGGGAAA
GAGCCAGAAGTACGACAGTTCTTCTTCTTGCTCGCAGTTTGCCACACAGTCATGGTGGAT
AGGACTGATGGTCAGCTCAACTACCAGGCAGCCTCTCCCGATGAAGGTGCCCTGGTAAAC
GCTGCCAGGAACTTTGGCTTTGCCTTCCTCGCCAGGACCCAGAACACCATCACCATCAGT
GAACTGGGCACTGAAAGGACTTACAATGTTCTTGCCATTTTGGACTTCAACAGTGACCGG
AAGCGAATGTCTATCATTGTAAGAACCCCAGAAGGCAATATCAAGCTTTACTGTAAAGGT
GCTGACACTGTTATTTATGAACGGTTACATCGAATGAATCCTACTAAGCAAGAAACACAG
GATGCCCTGGATATCTTTGCAAATGAAACTCTTAGAACCCTATGCCTTTGCTACAAGGAA
ATTGAAGAAAAAGAATTTACAGAATGGAATAAAAAGTTTATGGCTGCCAGTGTGGCCTCC
ACCAACCGGGACGAAGCTCTGGATAAAGTATATGAGGAGATTGAAAAAGACTTAATTCTC
CTGGGAGCTACAGCTATTGAAGACAAGCTACAGGATGGAGTTCCAGAAACCATTTCAAAA
CTTGCAAAAGCTGACATTAAGATCTGGGTGCTTACTGGAGACAAAAAGGAAACTGCTGAA
AATATAGGATTTGCTTGTGAACTTCTGACTGAAGACACCACCATCTGCTATGGGGAGGAT
ATTAATTCTCTTCTTCATGCAAGGATGGAAAACCAGAGGAATAGAGGTGGCGTCTACGCA
AAGTTTGCACCTCCTGTGCAGGAATCTTTTTTTCCACCCGGTGGAAACCGTGCCTTAATC
ATCACTGGTTCTTGGTTGAATGAAATTCTTCTCGAGAAAAAGACCAAGAGAAATAAGATT
CTGAAGCTGAAGTTCCCAAGAACAGAAGAAGAAAGACGGATGCGGACCCAAAGTAAAAGG
AGGCTAGAAGCTAAGAAAGAGCAGCGGCAGAAAAACTTTGTGGACCTGGCCTGCGAGTGC
AGCGCAGTCATCTGCTGCCGCGTCACCCCCAAGCAGAAGGCCATGGTGGTGGACCTGGTG
AAGAGGTACAAGAAAGCCATCACGCTGGCCATCGGAGATGGGGCCAATGACGTGAACATG
ATCAAAACTGCCCACATTGGCGTTGGAATAAGTGGACAAGAAGGAATGCAAGCTGTCATG
TCGAGTGACTATTCCTTTGCTCAGTTCCGATATCTGCAGAGGCTACTGCTGGTGCATGGC
CGATGGTCTTACATAAGGATGTGCAAGTTCCTACGATACTTCTTTTACAAAAACTTTGCC
TTTACTTTGGTTCATTTCTGGTACTCCTTCTTCAATGGCTACTCTGCGCAGACTGCATAC
GAGGATTGGTTCATCACCCTCTACAACGTGCTGTACACCAGCCTGCCCGTGCTCCTCATG
GGGCTGCTCGACCAGGATGTGAGTGACAAACTGAGCCTCCGATTCCCTGGGTTATACATA
GTGGGACAAAGAGACTTACTATTCAACTATAAGAGATTCTTTGTAAGCTTGTTGCATGGG
GTCCTAACATCGATGATCCTCTTCTTCATACCTCTTGGAGCTTATCTGCAAACCGTAGGG
CAGGATGGAGAGGCACCTTCCGACTACCAGTCTTTTGCCGTCACCATTGCCTCTGCTCTT
GTAATAACAGTCAATTTCCAGATTGGCTTGGATACTTCTTATTGGACTTTTGTGAATGCT
TTTTCAATTTTTGGAAGCATTGCACTTTATTTTGGCATCATGTTTGACTTTCATAGTGCT
GGAATACATGTTCTCTTTCCATCTGCATTTCAATTTACAGGCACAGCTTCAAACGCTCTG
AGACAGCCATACATTTGGTTAACTATCATCCTGACTGTTGCTGTGTGCTTACTACCCGTC
GTTGCCATTCGATTCCTGTCAATGACCATCTGGCCATCAGAAAGTGATAAGATCCAGAAG
CATCGCAAGCGGTTGAAGGCGGAGGAGCAGTGGCAGCGACGGCAGCAGGTGTTCCGCCGG
GGCGTGTCAACGCGGCGCTCGGCCTACGCCTTCTCGCACCAGCGGGGCTACGCGGACCTC
ATCTCCTCCGGGCGCAGCATCCGCAAGAAGCGCTCGCCGCTTGATGCCATCGTGGCGGAT
GGCACCGCGGAGTACAGGCGCACCGGGGACAGCTGA
|
| Enzyme 31 GenBank Gene ID |
NM_005603.4  |
| Enzyme 31 GeneCard ID |
ATP8B1  |
| Enzyme 31 GenAtlas ID |
ATP8B1  |
| Enzyme 31 HGNC ID |
HGNC:3706  |
| Enzyme 31 Chromosome Location |
1 |
| Enzyme 31 Locus |
18q21-q22|18q21.31 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Bull LN, van Eijk MJ, Pawlikowska L, DeYoung JA, Juijn JA, Liao M, Klomp LW, Lomri N, Berger R, Scharschmidt BF, Knisely AS, Houwen RH, Freimer NB: A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. Nat Genet. 1998 Mar;18(3):219-24. [PubMed
]
- Nusbaum C, Zody MC, Borowsky ML, Kamal M, Kodira CD, Taylor TD, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Abouelleil A, Allen NR, Anderson S, Bloom T, Bugalter B, Butler J, Cook A, DeCaprio D, Engels R, Garber M, Gnirke A, Hafez N, Hall JL, Norman CH, Itoh T, Jaffe DB, Kuroki Y, Lehoczky J, Lui A, Macdonald P, Mauceli E, Mikkelsen TS, Naylor JW, Nicol R, Nguyen C, Noguchi H, O'Leary SB, O'Neill K, Piqani B, Smith CL, Talamas JA, Topham K, Totoki Y, Toyoda A, Wain HM, Young SK, Zeng Q, Zimmer AR, Fujiyama A, Hattori M, Birren BW, Sakaki Y, Lander ES: DNA sequence and analysis of human chromosome 18. Nature. 2005 Sep 22;437(7058):551-5. [PubMed
]
- Halleck MS, Pradhan D, Blackman C, Berkes C, Williamson P, Schlegel RA: Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs. Genome Res. 1998 Apr;8(4):354-61. [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
]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed
]
- Tygstrup N, Steig BA, Juijn JA, Bull LN, Houwen RH: Recurrent familial intrahepatic cholestasis in the Faeroe Islands. Phenotypic heterogeneity but genetic homogeneity. Hepatology. 1999 Feb;29(2):506-8. [PubMed
]
- Klomp LW, Bull LN, Knisely AS, van Der Doelen MA, Juijn JA, Berger R, Forget S, Nielsen IM, Eiberg H, Houwen RH: A missense mutation in FIC1 is associated with greenland familial cholestasis. Hepatology. 2000 Dec;32(6):1337-41. [PubMed
]
- Klomp LW, Vargas JC, van Mil SW, Pawlikowska L, Strautnieks SS, van Eijk MJ, Juijn JA, Pabon-Pena C, Smith LB, DeYoung JA, Byrne JA, Gombert J, van der Brugge G, Berger R, Jankowska I, Pawlowska J, Villa E, Knisely AS, Thompson RJ, Freimer NB, Houwen RH, Bull LN: Characterization of mutations in ATP8B1 associated with hereditary cholestasis. Hepatology. 2004 Jul;40(1):27-38. [PubMed
]
- Painter JN, Savander M, Ropponen A, Nupponen N, Riikonen S, Ylikorkala O, Lehesjoki AE, Aittomaki K: Sequence variation in the ATP8B1 gene and intrahepatic cholestasis of pregnancy. Eur J Hum Genet. 2005 Apr;13(4):435-9. [PubMed
]
- Mullenbach R, Bennett A, Tetlow N, Patel N, Hamilton G, Cheng F, Chambers J, Howard R, Taylor-Robinson SD, Williamson C: ATP8B1 mutations in British cases with intrahepatic cholestasis of pregnancy. Gut. 2005 Jun;54(6):829-34. [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 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
6516 |
| Enzyme 32 Name |
Probable phospholipid-transporting ATPase IIA |
| Enzyme 32 Synonyms |
- ATPase class II type 9A
|
| Enzyme 32 Gene Name |
ATP9A |
| Enzyme 32 Protein Sequence |
>Probable phospholipid-transporting ATPase IIA
MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINN
QKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIRE
AVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSE
KNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFT
REDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEV
NCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSW
VIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMIFKRLHLGTVAYGLDSMDE
VQSHIFSIYTQQSQDPPAQKGPTLTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTD
QAEAEKQYEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQILNFTILQ
IFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLV
VAKKSLAEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVR
PTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFR
RKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLT
CAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSA
ALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKS
EVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTS
LILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVIT
LVSCLPLYVLKYLRRRFSPPSYSKLTS
|
| Enzyme 32 Number of Residues |
1047 |
| Enzyme 32 Molecular Weight |
118581.5 |
| Enzyme 32 Theoretical pI |
7.81 |
| Enzyme 32 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 32 General Function |
Involved in ATP binding |
| Enzyme 32 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
- 70-91
97-119
304-325
333-354
842-862
875-893
924-942
950-972
979-999
1007-1030
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
65301139  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
O75110  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
ATP9A_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>3144 bp
ATGACGGACAACATCCCGCTGCAGCCGGTGCGCCAGAAGAAGCGGATGGACAGCAGGCCC
CGCGCCGGGTGCTGCGAGTGGCTGAGATGCTGCGGTGGAGGGGAGGCCAGGCCCCGCACT
GTCTGGCTGGGGCACCCCGAGAAGAGAGACCAGAGGTATCCTCGGAATGTCATCAACAAT
CAGAAGTACAATTTCTTCACCTTTCTTCCTGGGGTGCTGTTCAACCAGTTCAAATACTTT
TTCAACCTCTATTTCTTACTTCTTGCCTGCTCTCAGTTTGTTCCCGAAATGAGACTTGGT
GCACTCTATACCTACTGGGTTCCCCTGGGCTTCGTGCTGGCCGTCACTGTCATCCGTGAG
GCGGTGGAGGAGATCCGATGCTACGTGCGGGACAAGGAAGTCAACTCCCAGGTCTACAGC
CGGCTCACAGCACGAGGCACAGTGAAGGTGAAGAGTTCTAACATCCAAGTTGGAGACCTT
ATCATCGTTGAAAAGAACCAGCGGGTCCCTGCCGACATGATCTTCCTGAGGACATCAGAA
AAAAACGGGTCATGCTTCTTGCGGACGGATCAGCTGGATGGGGAGACGGACTGGAAGCTG
CGGCTTCCCGTGGCCTGCACGCAGAGGCTCCCCACGGCCGCCGACCTTCTTCAGATTCGA
TCGTATGTGTACGCAGAAGAGCCAAATATTGACATTCACAACTTCGTGGGAACTTTTACC
CGAGAAGACAGCGACCCCCCGATCAGCGAGAGCCTGAGCATAGAGAACACGCTGTGGGCT
GGCACTGTGGTCGCATCAGGTACTGTTGTGGGTGTTGTTCTTTACACTGGCAGAGAACTC
CGGAGTGTCATGAATACCTCAAATCCCCGAAGTAAGATCGGCCTGTTCGACTTGGAAGTG
AACTGCCTCACCAAGATCCTCTTTGGTGCCCTGGTGGTGGTCTCGCTGGTCATGGTTGCC
CTTCAGCACTTTGCAGGCCGTTGGTACCTGCAGATCATCCGCTTCCTCCTCTTGTTTTCC
AACATCATCCCCATTAGTTTGCGCGTGAACCTGGACATGGGCAAGATCGTGTACAGCTGG
GTGATTCGAAGGGACTCGAAAATCCCCGGGACCGTGGTTCGCTCCAGCACGATTCCTGAG
CAGCTGGGCAGGATTTCGTACTTACTCACAGACAAGACAGGCACTCTTACCCAGAACGAG
ATGATTTTCAAACGGCTCCATCTCGGAACAGTAGCCTACGGCCTCGACTCAATGGACGAA
GTACAAAGCCACATTTTCAGCATTTACACCCAGCAATCCCAGGACCCACCGGCTCAGAAG
GGCCCAACGCTCACCACTAAGGTCCGGCGGACCATGAGCAGCCGCGTGCACGAAGCCGTG
AAGGCCATCGCGCTCTGCCACAACGTGACTCCCGTGTATGAGTCCAACGGTGTGACTGAT
CAGGCTGAGGCCGAGAAGCAGTACGAAGACTCCTGCCGCGTATACCAGGCATCCAGCCCC
GATGAGGTGGCCCTGGTACAGTGGACGGAAAGTGTGGGCTTAACCCTGGTGGGCCGAGAC
CAGTCTTCCATGCAGCTGAGGACCCCTGGCGACCAGATCCTGAACTTCACCATCCTACAG
ATCTTCCCTTTCACCTATGAAAGCAAACGTATGGGCATCATCGTGCGGGATGAATCAACT
GGAGAAATTACGTTTTACATGAAGGGAGCAGATGTGGTCATGGCTGGCATTGTGCAGTAC
AATGACTGGTTGGAGGAAGAGTGTGGCAACATGGCCCGAGAAGGGCTGCGGGTGCTCGTG
GTGGCAAAGAAGTCTCTTGCAGAGGAGCAGTATCAGGACTTTGAAGCCCGCTACGTCCAG
GCCAAGCTGAGTGTGCACGACCGCTCCCTCAAAGTGGCCACGGTGATCGAGAGCCTGGAG
ATGGAGATGGAACTGCTGTGCCTGACGGGCGTGGAGGACCAGCTGCAGGCAGATGTGCGG
CCCACGCTGGAGACCCTGAGGAATGCTGGCATCAAGGTTTGGATGCTGACAGGGGACAAG
CTGGAGACAGCTACGTGCACAGCGAAGAATGCACATCTGGTGACCAGAAACCAAGACATC
CACGTTTTTCGGCTGGTGACCAACCGCGGGGAGGCTCACCTCGAGCTGAACGCCTTCCGC
AGGAAGCATGATTGTGCCCTGGTCATCTCGGGAGACTCCCTGGAGGTTTGCCTCAAGTAC
TATGAGTACGAGTTCATGGAGCTGGCCTGCCAGTGCCCGGCCGTAGTCTGCTGCCGATGT
GCCCCCACCCAGAAGGCCCAGATCGTGCGCCTGCTTCAGGAGCGCACGGGCAAGCTCACC
TGTGCAGTAGGGGACGGAGGCAATGACGTCAGCATGATTCAGGAATCTGACTGCGGCGTG
GGAGTGGAAGGAAAGGAAGGAAAACAGGCTTCGTTGGCTGCAGACTTCTCCATCACTCAA
TTTAAGCATCTTGGCCGGTTGCTTATGGTGCATGGCCGGAACAGCTACAAGCGGTCAGCC
GCCCTCAGCCAGTTCGTGATTCACAGGAGCCTCTGTATCAGCACCATGCAGGCTGTCTTT
TCCTCCGTGTTTTACTTTGCCTCCGTCCCTCTCTATCAAGGATTCCTCATCATTGGGTAC
TCCACAATTTACACCATGTTTCCTGTGTTTTCTCTGGTCCTGGACAAAGATGTCAAATCG
GAAGTTGCCATGCTGTATCCTGAGCTCTACAAGGATCTTCTCAAGGGACGGCCGTTGTCC
TACAAGACATTCTTAATATGGGTTTTGATTAGCATCTATCAAGGGAGCACCATCATGTAC
GGGGCGCTGCTGCTGTTTGAGTCGGAGTTCGTGCACATCGTGGCCATCTCCTTCACCTCG
CTGATCCTCACCGAGCTGCTCATGGTGGCGCTGACCATCCAGACCTGGCACTGGCTCATG
ACAGTGGCGGAGCTGCTCAGCCTGGCCTGCTACATCGCCTCCCTGGTGTTCTTACACGAG
TTCATCGATGTGTACTTCATCGCCACCTTGTCATTCTTGTGGAAAGTCTCCGTCATCACT
CTGGTCAGCTGCCTCCCCCTCTATGTCCTCAAGTACCTGCGAAGACGGTTCTCTCCCCCC
AGCTACTCAAAGCTCACATCATAG
|
| Enzyme 32 GenBank Gene ID |
NM_006045.1  |
| Enzyme 32 GeneCard ID |
ATP9A  |
| Enzyme 32 GenAtlas ID |
ATP9A  |
| Enzyme 32 HGNC ID |
HGNC:13540  |
| Enzyme 32 Chromosome Location |
2 |
| Enzyme 32 Locus |
20q13.2 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- 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
]
- Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [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
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
6535 |
| Enzyme 33 Name |
Probable phospholipid-transporting ATPase VD |
| Enzyme 33 Synonyms |
- ATPase class V type 10D
|
| Enzyme 33 Gene Name |
ATP10D |
| Enzyme 33 Protein Sequence |
>Probable phospholipid-transporting ATPase VD
MTEALQWARYHWRRLIRGATRDDDSGPYNYSSLLACGRKSSQTPKLSGRHRIVVPHIQPF
KDEYEKFSGAYVNNRIRTTKYTLLNFVPRNLFEQFHRAANLYFLFLVVLNWVPLVEAFQK
EITMLPLVVVLTIIAIKDGLEDYRKYKIDKQINNLITKVYSRKEKKYIDRCWKDVTVGDF
IRLSCNEVIPADMVLLFSTDPDGICHIETSGLDGESNLKQRQVVRGYAEQDSEVDPEKFS
SRIECESPNNDLSRFRGFLEHSNKERVGLSKENLLLRGCTIRNTEAVVGIVVYAGHETKA
MLNNSGPRYKRSKLERRANTDVLWCVMLLVIMCLTGAVGHGIWLSRYEKMHFFNVPEPDG
HIISPLLAGFYMFWTMIILLQVLIPISLYVSIEIVKLGQIYFIQSDVDFYNEKMDSIVQC
RALNIAEDLGQIQYLFSDKTGTLTENKMVFRRCSVAGFDYCHEENARRLESYQEAVSEDE
DFIDTVSGSLSNMAKPRAPSCRTVHNGPLGNKPSNHLAGSSFTLGSGEGASEVPHSRQAA
FSSPIETDVVPDTRLLDKFSQITPRLFMPLDETIQNPPMETLYIIDFFIALAICNTVVVS
APNQPRQKIRHPSLGGLPIKSLEEIKSLFQRWSVRRSSSPSLNSGKEPSSGVPNAFVSRL
PLFSRMKPASPVEEEVSQVCESPQCSSSSACCTETEKQHGDAGLLNGKAESLPGQPLACN
LCYEAESPDEAALVYAARAYQCTLRSRTPEQVMVDFAALGPLTFQLLHILPFDSVRKRMS
VVVRHPLSNQVVVYTKGADSVIMELLSVASPDGASLEKQQMIVREKTQKHLDDYAKQGLR
TLCIAKKVMSDTEYAEWLRNHFLAETSIDNREELLLESAMRLENKLTLLGATGIEDRLQE
GVPESIEALHKAGIKIWMLTGDKQETAVNIAYACKLLEPDDKLFILNTQSKDACGMLMST
ILKELQKKTQALPEQVSLSEDLLQPPVPRDSGLRAGLIITGKTLEFALQESLQKQFLELT
SWCQAVVCCRATPLQKSEVVKLVRSHLQVMTLAIGDGANDVSMIQVADIGIGVSGQEGMQ
AVMASDFAVSQFKHLSKLLLVHGHWCYTRLSNMILYFFYKNVAYVNLLFWYQFFCGFSGT
SMTDYWVLIFFNLLFTSAPPVIYGVLEKDVSAETLMQLPELYRSGQKSEAYLPHTFWITL
LDAFYQSLVCFFVPYFTYQGSDTDIFAFGNPLNTAALFIVLLHLVIESKSLTWIHLLVII
GSILSYFLFAIVFGAMCVTCNPPSNPYWIMQEHMLDPVFYLVCILTTSIALLPRFVYRVL
QGSLFPSPILRAKHFDRLTPEERTKALKKWRGAGKMNQVTSKYANQSAGKSGRRPMPGPS
AVFAMKSASSCAIEQGNLSLCETALDQGYSETKAFEMAGPSKGKES
|
| Enzyme 33 Number of Residues |
1426 |
| Enzyme 33 Molecular Weight |
160272.3 |
| Enzyme 33 Theoretical pI |
7.15 |
| Enzyme 33 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 33 General Function |
Involved in ATP binding |
| Enzyme 33 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
- 98-118
122-142
322-342
366-386
1114-1134
1146-1166
1196-1216
1225-1245
1253-1273
1293-1313
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
222352161  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q9P241  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
AT10D_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>4281 bp
ATGACTGAGGCTCTCCAATGGGCCAGATATCACTGGCGACGGCTGATCAGAGGTGCAACC
AGGGATGATGATTCAGGGCCATACAACTATTCCTCGTTGCTCGCCTGTGGGCGCAAGTCC
TCTCAGACCCCTAAACTGTCAGGAAGGCACCGGATTGTTGTTCCCCACATCCAGCCCTTC
AAGGATGAGTATGAGAAGTTCTCCGGAGCCTATGTGAACAATCGAATACGAACAACAAAG
TACACACTTCTGAATTTTGTGCCAAGAAATTTATTTGAACAATTTCACAGAGCTGCCAAT
TTATATTTCCTGTTCCTAGTTGTCCTGAACTGGGTACCTTTGGTAGAAGCCTTCCAAAAG
GAAATCACCATGTTGCCTCTGGTGGTGGTCCTTACAATTATCGCAATTAAAGATGGCCTG
GAAGATTATCGGAAATACAAAATTGACAAACAGATCAATAATTTAATAACTAAAGTTTAT
AGTAGGAAAGAGAAAAAATACATTGACCGATGCTGGAAAGACGTTACTGTTGGGGACTTT
ATTCGCCTCTCCTGCAACGAGGTCATCCCTGCAGACATGGTACTACTCTTTTCCACTGAT
CCAGATGGAATCTGTCACATTGAGACTTCTGGTCTTGATGGAGAGAGCAATTTAAAACAG
AGGCAGGTGGTTCGGGGATATGCAGAACAGGACTCTGAAGTTGATCCTGAGAAGTTTTCC
AGTAGGATAGAATGTGAAAGCCCAAACAATGACCTCAGCAGATTCCGAGGCTTCCTAGAA
CATTCCAACAAAGAACGCGTGGGTCTCAGTAAAGAAAATTTGTTGCTTAGAGGATGCACC
ATTAGAAACACAGAGGCTGTTGTGGGCATTGTGGTTTATGCAGGCCATGAAACCAAAGCA
ATGCTGAACAACAGTGGGCCACGGTATAAGCGCAGCAAATTAGAAAGAAGAGCAAACACA
GATGTCCTCTGGTGTGTCATGCTTCTGGTCATAATGTGCTTAACTGGCGCAGTAGGTCAT
GGAATCTGGCTGAGCAGGTATGAAAAGATGCATTTTTTCAATGTTCCCGAGCCTGATGGA
CATATCATATCACCACTGTTGGCAGGATTTTATATGTTTTGGACCATGATCATTTTGTTA
CAGGTCTTGATTCCTATTTCTCTCTATGTTTCCATCGAAATTGTGAAGCTTGGACAAATA
TATTTCATTCAAAGTGATGTGGATTTCTACAATGAAAAAATGGATTCTATTGTTCAGTGC
CGAGCCCTGAACATCGCCGAGGATCTGGGACAGATTCAGTACCTCTTTTCCGATAAGACA
GGAACCCTCACTGAGAATAAGATGGTTTTTCGAAGATGTAGTGTGGCAGGATTTGATTAC
TGCCATGAAGAAAATGCCAGGAGGTTGGAGTCCTATCAGGAAGCTGTCTCTGAAGATGAA
GATTTTATAGACACAGTCAGTGGTTCCCTCAGCAATATGGCAAAACCGAGAGCCCCCAGC
TGCAGGACAGTTCATAATGGGCCTTTGGGAAATAAGCCCTCAAATCATCTTGCTGGGAGC
TCTTTTACTCTAGGAAGTGGAGAAGGAGCCAGTGAAGTGCCTCATTCCAGACAGGCTGCT
TTCAGTAGCCCCATTGAAACAGACGTGGTACCAGACACCAGGCTTTTAGACAAATTTAGT
CAGATTACACCTCGGCTCTTTATGCCACTAGATGAGACCATCCAAAATCCACCAATGGAA
ACTTTGTACATTATCGACTTTTTCATTGCATTGGCAATTTGCAACACAGTAGTGGTTTCT
GCTCCTAACCAACCCCGACAAAAGATCAGACACCCTTCACTGGGGGGGTTGCCCATTAAG
TCTTTGGAAGAGATTAAAAGTCTTTTCCAGAGATGGTCTGTCCGAAGATCAAGTTCTCCA
TCGCTTAACAGTGGGAAAGAGCCATCTTCTGGAGTTCCAAACGCCTTTGTGAGCAGACTC
CCTCTCTTTAGTCGAATGAAACCAGCTTCACCTGTGGAGGAAGAGGTCTCCCAGGTGTGT
GAGAGCCCCCAGTGCTCCAGTAGCTCAGCTTGCTGCACAGAAACAGAGAAACAACACGGT
GATGCAGGCCTCCTGAATGGCAAGGCAGAGTCCCTCCCTGGACAGCCATTGGCCTGCAAC
CTGTGTTATGAGGCCGAGAGCCCAGACGAAGCGGCCTTAGTGTATGCCGCCAGGGCTTAC
CAATGCACTTTACGGTCTCGGACACCAGAGCAGGTCATGGTGGACTTTGCTGCTTTGGGA
CCATTAACATTTCAACTCCTACACATCCTGCCCTTTGACTCAGTAAGAAAAAGAATGTCT
GTTGTGGTCCGACACCCTCTTTCCAATCAAGTTGTGGTGTATACGAAAGGCGCTGATTCT
GTGATCATGGAGTTACTGTCGGTGGCTTCCCCAGATGGAGCAAGTCTGGAGAAACAACAG
ATGATAGTAAGGGAGAAAACCCAGAAGCACTTGGATGACTATGCCAAACAAGGCCTTCGT
ACTTTATGTATAGCAAAGAAGGTCATGAGTGACACTGAATATGCAGAGTGGCTGAGGAAT
CATTTTTTAGCTGAAACCAGCATTGACAACAGGGAAGAATTACTACTTGAATCTGCCATG
AGGTTGGAGAACAAACTTACATTACTTGGTGCTACTGGCATTGAAGACCGTCTGCAGGAG
GGAGTCCCTGAATCTATAGAAGCTCTTCACAAAGCGGGCATCAAGATCTGGATGCTGACA
GGGGACAAGCAGGAGACAGCTGTCAACATAGCTTATGCATGCAAACTACTGGAGCCAGAT
GACAAGCTTTTTATCCTCAATACCCAAAGTAAAGATGCCTGTGGGATGCTGATGAGCACA
ATTTTGAAAGAACTTCAGAAGAAAACTCAAGCCCTGCCAGAGCAAGTGTCATTAAGTGAA
GATTTACTTCAGCCTCCTGTCCCCCGGGACTCAGGGTTACGAGCTGGACTCATTATCACT
GGGAAGACCCTGGAGTTTGCCCTGCAAGAAAGTCTGCAAAAGCAGTTCCTGGAACTGACA
TCTTGGTGTCAAGCTGTGGTCTGCTGCCGAGCCACACCGCTGCAGAAAAGTGAAGTGGTG
AAATTGGTCCGCAGCCATCTCCAGGTGATGACCCTTGCTATTGGTGATGGTGCCAATGAT
GTTAGCATGATACAAGTGGCAGACATTGGGATAGGGGTCTCAGGTCAAGAAGGCATGCAG
GCTGTGATGGCCAGTGACTTTGCCGTTTCTCAGTTCAAACATCTCAGCAAGCTCCTTCTT
GTCCATGGACACTGGTGTTATACACGGCTTTCCAACATGATTCTCTATTTTTTCTATAAG
AATGTGGCCTATGTGAACCTCCTTTTCTGGTACCAGTTCTTTTGTGGATTTTCAGGAACA
TCCATGACTGATTACTGGGTTTTGATCTTCTTCAACCTCCTCTTCACATCTGCCCCTCCT
GTCATTTATGGTGTTTTGGAGAAAGATGTGTCTGCAGAGACCCTCATGCAACTGCCTGAA
CTTTACAGAAGTGGTCAGAAATCAGAGGCATACTTACCCCATACCTTCTGGATCACCTTA
TTGGATGCTTTTTATCAAAGCCTGGTCTGCTTCTTTGTGCCTTATTTTACCTACCAGGGC
TCAGATACTGACATCTTTGCATTTGGAAACCCCCTGAACACAGCCGCTCTGTTCATCGTT
CTCCTCCATCTGGTCATTGAAAGCAAGAGTTTGACTTGGATTCACTTGCTGGTCATCATT
GGTAGCATCTTGTCTTATTTTTTATTTGCCATAGTTTTTGGAGCCATGTGTGTAACTTGC
AACCCACCATCCAACCCTTACTGGATTATGCAGGAGCACATGCTGGATCCAGTATTCTAC
TTAGTTTGTATCCTCACGACGTCCATTGCTCTTCTGCCCAGGTTTGTATACAGAGTTCTT
CAGGGATCCCTGTTTCCATCTCCAATTCTGAGAGCTAAGCACTTTGACAGACTAACTCCA
GAGGAGAGGACTAAAGCTCTCAAGAAGTGGAGAGGGGCTGGAAAGATGAATCAAGTGACA
TCAAAGTATGCTAACCAATCAGCTGGCAAGTCAGGAAGAAGACCCATGCCTGGCCCTTCT
GCTGTATTTGCAATGAAGTCAGCAAGTTCCTGTGCTATTGAGCAAGGAAACTTATCTCTG
TGTGAAACTGCTTTAGATCAAGGCTACTCTGAAACTAAGGCCTTTGAGATGGCTGGACCC
TCCAAAGGTAAAGAAAGCTAG
|
| Enzyme 33 GenBank Gene ID |
NM_020453.3  |
| Enzyme 33 GeneCard ID |
ATP10D  |
| Enzyme 33 GenAtlas ID |
ATP10D  |
| Enzyme 33 HGNC ID |
HGNC:13549  |
| Enzyme 33 Chromosome Location |
4 |
| Enzyme 33 Locus |
4p12 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Flamant S, Pescher P, Lemercier B, Clement-Ziza M, Kepes F, Fellous M, Milon G, Marchal G, Besmond C: Characterization of a putative type IV aminophospholipid transporter P-type ATPase. Mamm Genome. 2003 Jan;14(1):21-30. [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
]
- 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
]
- Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
6543 |
| Enzyme 34 Name |
Probable phospholipid-transporting ATPase IB |
| Enzyme 34 Synonyms |
- ATPase class I type 8A member 2
- ML-1
|
| Enzyme 34 Gene Name |
ATP8A2 |
| Enzyme 34 Protein Sequence |
>Probable phospholipid-transporting ATPase IB
MSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFF
LFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNG
MWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLS
HTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQ
WVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNR
SHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMY
YIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREP
SSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNII
YQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIV
RTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYE
EWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIK
IWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDV
ALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIG
DGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCIL
YCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESM
LRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFV
GNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLTWLVFFGIYSTIWPTIPIAPDMRG
QATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELETKSRVLGKAVLR
DSNGKRLNERDRLIKRLGRKTPPTLFRGSSLQQGVPHGYAFSQEEHGAVSQEEVIRAYDT
TKKKSRKK
|
| Enzyme 34 Number of Residues |
1148 |
| Enzyme 34 Molecular Weight |
129240.4 |
| Enzyme 34 Theoretical pI |
7.84 |
| Enzyme 34 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 34 General Function |
Involved in ATP binding |
| Enzyme 34 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
- 45-66
72-94
277-298
324-345
838-858
871-890
921-942
957-979
986-1006
1025-1049
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
117168245  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q9NTI2  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
AT8A2_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>3567 bp
ATGCTGAACGGCGCAGGCCTGGACAAAGCTCTTAAGATGTCCCTGCCGCGGAGGTCGAGG
ATCCGCTCGTCCGTGGGACCTGTTCGTTCTTCTTTGGGCTATAAGAAGGCAGAGGATGAG
ATGTCCCGGGCCACGTCTGTTGGAGACCAGCTGGAGGCACCCGCCCGCACCATTTACCTC
AACCAACCGCATCTCAACAAATTCCGCGACAACCAGATCAGTACGGCCAAGTACAGCGTG
TTGACATTTCTACCTCGATTCTTGTATGAGCAGATTAGAAGAGCTGCTAATGCCTTCTTT
CTCTTCATTGCCTTATTACAGCAAATTCCAGATGTATCTCCAACAGGAAGATATACCACC
CTGGTGCCATTGATCATTATTTTAACAATTGCAGGCATCAAAGAGATTGTAGAAGATTTT
AAGCGACACAAGGCAGACAATGCAGTTAACAAAAAGAAAACAATAGTGTTAAGAAATGGT
ATGTGGCATACCATTATGTGGAAAGAGGTGGCAGTGGGAGACATTGTGAAGGTCGTCAAT
GGGCAGTATCTTCCAGCAGATGTGGTCCTGCTGTCATCCAGTGAACCTCAGGCAATGTGT
TATGTTGAAACAGCTAATCTGGATGGGGAGACGAACCTTAAAATACGTCAGGGTTTGAGT
CACACTGCTGACATGCAAACACGTGAAGTTCTGATGAAGTTATCTGGAACTATAGAGTGT
GAAGGGCCCAACCGCCACCTCTATGACTTCACTGGAAACTTGAACTTAGATGGGAAAAGC
CTTGTTGCCCTTGGGCCTGACCAGATCTTATTAAGAGGTACACAGCTTAGAAATACTCAG
TGGGTCTTTGGCATAGTTGTTTATACTGGACACGACACCAAACTCATGCAGAATTCAACC
AAAGCGCCTCTCAAGAGATCAAATGTTGAGAAGGTGACTAACGTGCAGATCCTGGTGTTG
TTTGGCATCCTCTTGGTCATGGCCTTGGTGAGCTCGGCGGGGGCCCTGTACTGGAACAGG
TCTCATGGTGAAAAGAACTGGTACATCAAGAAGATGGACACCACCTCAGATAATTTTGGA
TACAACCTACTGACGTTCATCATCTTATACAACAATCTTATTCCCATCAGTCTGTTGGTG
ACTCTTGAGGTTGTGAAGTATACTCAAGCCCTTTTCATAAACTGGGACACAGATATGTAT
TATATAGGAAATGACACTCCTGCCATGGCCAGGACATCAAACCTTAATGAAGAGCTTGGG
CAGGTGAAATATCTCTTTTCTGACAAGACTGGAACGCTTACATGCAATATCATGAACTTT
AAGAAGTGCAGCATTGCCGGAGTAACCTATGGTCACTTCCCAGAATTGGCAAGAGAGCCG
TCTTCAGATGACTTCTGTCGGATGCCTCCTCCCTGTAGTGATTCCTGTGACTTTGATGAC
CCCAGGCTGTTGAAGAACATTGAGGATCGCCATCCCACAGCCCCTTGCATTCAGGAGTTC
CTCACCCTTCTGGCCGTGTGCCACACGGTTGTTCCTGAGAAGGATGGAGATAACATCATC
TACCAGGCCTCTTCCCCAGATGAAGCTGCTTTGGTGAAAGGAGCTAAAAAGCTGGGCTTT
GTCTTCACAGCCAGAACACCATTCTCAGTCATCATAGAAGCGATGGGACAGGAACAAACA
TTCGGAATCCTTAATGTCCTGGAATTTTCTAGTGACAGAAAAAGAATGTCTGTAATTGTT
CGAACTCCTTCAGGACGACTTCGGCTTTACTGTAAAGGGGCTGATAATGTGATTTTTGAG
AGACTTTCAAAAGACTCAAAATATATGGAGGAAACATTATGCCATCTGGAATACTTTGCC
ACGGAAGGCTTGCGGACTCTCTGTGTGGCTTATGCTGATCTCTCTGAGAATGAGTATGAG
GAGTGGCTGAAAGTCTATCAGGAAGCCAGCACCATATTGAAGGACAGAGCTCAACGGTTG
GAAGAGTGTTACGAGATCATTGAGAAGAATTTGCTGCTACTTGGAGCCACAGCCATAGAA
GATCGCCTTCAAGCAGGAGTTCCAGAAACCATCGCAACACTGTTGAAGGCAGAAATTAAA
ATATGGGTGTTGACAGGAGACAAACAAGAAACTGCGATTAATATAGGGTATTCCTGCCGA
TTGGTATCGCAGAATATGGCCCTTATCCTATTGAAGGAGGACTCTTTGGATGCCACAAGG
GCAGCCATTACTCAGCACTGCACTGACCTTGGGAATTTGCTGGGCAAGGAAAATGACGTG
GCCCTGATCATCGATGGCCACACCCTGAAGTACGCGCTCTCCTTCGAAGTCCGGAGGAGT
TTCCTGGATTTGGCACTCTCGTGCAAAGCGGTCATATGCTGCAGAGTGTCTCCTCTGCAG
AAGTCTGAGATAGTGGATGTGGTGAAGAAGCGGGTGAAGGCCATCACCCTCGCCATCGGA
GACGGCGCCAACGATGTCGGGATGATCCAGACAGCCCACGTGGGTGTGGGAATCAGTGGG
AATGAAGGCATGCAGGCCACCAACAACTCGGATTACGCCATCGCACAGTTTTCCTACTTA
GAGAAGCTTCTGTTGGTTCATGGAGCCTGGAGCTACAACCGGGTGACCAAGTGCATCTTG
TACTGCTTCTATAAGAACGTGGTCCTGTATATTATTGAGCTTTGGTTCGCCTTTGTTAAT
GGATTTTCTGGGCAGATTTTATTTGAACGTTGGTGCATCGGCCTGTACAATGTGATTTTC
ACCGCTTTGCCGCCCTTCACTCTGGGAATCTTTGAGAGGTCTTGCACTCAGGAGAGCATG
CTCAGGTTTCCCCAGCTCTACAAAATCACCCAGAATGGCGAAGGCTTCAACACAAAGGTT
TTCTGGGGTCACTGCATCAACGCCTTGGTCCACTCCCTCATCCTCTTCTGGTTTCCCATG
AAAGCTCTGGAGCATGATACTGTGTTGACAAGTGGTCATGCTACCGACTATTTATTTGTT
GGAAATATTGTTTACACATATGTTGTTGTTACTGTTTGTCTGAAAGCTGGTTTGGAGACC
ACAGCTTGGACTAAATTCAGTCATCTGGCTGTCTGGGGAAGCATGCTGACCTGGCTGGTG
TTTTTTGGCATCTACTCGACCATCTGGCCCACCATTCCCATTGCTCCAGATATGAGAGGA
CAGGCAACTATGGTCCTGAGCTCCGCACACTTCTGGTTGGGATTATTTCTGGTTCCTACT
GCCTGTTTGATTGAAGATGTGGCATGGAGAGCAGCCAAGCACACCTGCAAAAAGACATTG
CTGGAGGAGGTGCAGGAGCTGGAAACCAAGTCTCGAGTCCTGGGAAAAGCGGTGCTGCGG
GATAGCAATGGAAAGAGGCTGAACGAGCGCGACCGCCTGATCAAGAGGCTGGGCCGGAAG
ACGCCCCCGACGCTGTTCCGGGGCAGCTCCCTGCAGCAGGGCGTCCCGCATGGGTATGCT
TTTTCTCAAGAAGAACACGGAGCTGTTAGTCAGGAAGAAGTCATCCGTGCTTATGACACC
ACCAAAAAGAAATCCAGGAAGAAATAA
|
| Enzyme 34 GenBank Gene ID |
NM_016529  |
| Enzyme 34 GeneCard ID |
ATP8A2  |
| Enzyme 34 GenAtlas ID |
ATP8A2  |
| Enzyme 34 HGNC ID |
HGNC:13533  |
| Enzyme 34 Chromosome Location |
1 |
| Enzyme 34 Locus |
13q12 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed
]
- Sun XL, Li D, Fang J, Noyes I, Casto B, Theil K, Shuler C, Milo GE: Changes in levels of normal ML-1 gene transcripts associated with the conversion of human nontumorigenic to tumorigenic phenotypes. Gene Expr. 1999;8(2):129-39. [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
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
6655 |
| Enzyme 35 Name |
Probable phospholipid-transporting ATPase IA |
| Enzyme 35 Synonyms |
- ATPase class I type 8A member 1
- Chromaffin granule ATPase II
|
| Enzyme 35 Gene Name |
ATP8A1 |
| Enzyme 35 Protein Sequence |
>Probable phospholipid-transporting ATPase IA
MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYN
IITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIED
IKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLISLSSSEPQAM
CYIETSNLDGETNLKIRQGLPATSDIKDVDSLMRISGRIECESPNRHLYDFVGNIRLDGH
GTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILI
LFCILIAMSLVCSVGSAIWNRRHSGKDWYLNLNYGGASNFGLNFLTFIILFNNLIPISLL
VTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQ
FKKCTIAGVAYGHVPEPEDYGCSPDEWQNSQFGDEKTFSDSSLLENLQNNHPTAPIICEF
LTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEER
YELLNVLEFTSARKRMSVIVRTPSGKLRLYCKGADTVIYDRLAETSKYKEITLKHLEQFA
TEGLRTLCFAVAEISESDFQEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIE
DKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCKLLKKNMGMIVINEGSLDGTR
ETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQ
KSEVVEMVKKQVKVVTLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYL
KNLLMIHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMF
TAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPL
KALQYGTAFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVV
FFGIYSSLWPAIPMAPDMSGEAAMLFSSGVFWMGLLFIPVASLLLDVVYKVIKRTAFKTL
VDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQD
ENGIVSQSEVIRAYDTTKQRPDEW
|
| Enzyme 35 Number of Residues |
1164 |
| Enzyme 35 Molecular Weight |
131368.2 |
| Enzyme 35 Theoretical pI |
6.83 |
| Enzyme 35 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 35 General Function |
Involved in ATP binding |
| Enzyme 35 Specific Function |
May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
- 66-86
93-115
298-319
345-366
858-878
891-910
941-962
977-999
1006-1026
1045-1070
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
Not Available |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q9Y2Q0  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
AT8A1_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>3492 bp
ATGCCCACCATGCGGAGGACCGTGTCGGAGATCCGCTCGCGCGCCGAAGGTTATGAGAAG
ACAGATGATGTTTCAGAGAAGACCTCACTGGCTGACCAGGAGGAAGTAAGGACTATTTTC
ATCAACCAGCCCCAGCTGACAAAATTCTGCAATAACCATGTCAGCACTGCAAAATACAAC
ATAATCACATTCCTTCCAAGATTTCTCTACTCTCAGTTCAGAAGAGCTGCTAATTCATTT
TTTCTCTTTATTGCACTGCTGCAGCAAATACCTGATGTGTCACCAACAGGTCGTTATACA
ACACTGGTTCCTCTCTTATTTATTTTAGCTGTGGCAGCTATCAAAGAGATAATAGAAGAT
ATTAAACGACATAAAGCTGATAATGCAGTGAACAAGAAACAAACGCAAGTTTTGAGAAAT
GGTGCTTGGGAAATTGTCCACTGGGAAAAGGTGGCAGTAGGGGAGATAGTGAAAGTGACC
AATGGGGAACATCTCCCAGCAGATCTCATCAGTCTGTCCTCAAGTGAGCCCCAAGCCATG
TGCTACATTGAAACATCCAACTTAGATGGTGAAACAAACTTGAAAATTAGACAGGGCTTA
CCAGCAACATCAGATATCAAAGACGTTGACAGTTTGATGAGGATTTCTGGCAGAATTGAG
TGTGAAAGTCCAAACAGACATCTCTACGATTTTGTTGGAAACATAAGGCTTGATGGACAT
GGCACCGTTCCACTGGGAGCAGATCAGATTCTTCTTCGAGGAGCTCAGTTGAGAAATACA
CAGTGGGTTCATGGAATAGTTGTCTACACTGGACATGACACCAAGCTGATGCAGAATTCA
ACAAGTCCACCACTTAAGCTCTCAAATGTGGAACGGATTACAAATGTACAAATTTTGATT
TTATTTTGTATCTTAATTGCCATGTCTCTTGTCTGTTCTGTGGGCTCAGCCATTTGGAAT
CGAAGGCATTCTGGAAAAGACTGGTATCTCAATCTAAACTATGGTGGCGCTAGTAATTTT
GGACTGAATTTCTTGACCTTCATCATCCTTTTCAACAATCTCATTCCTATCAGCTTATTG
GTTACATTAGAAGTTGTGAAATTTACCCAGGCATACTTCATAAATTGGGATCTTGACATG
CACTATGAACCCACAGACACTGCTGCTATGGCTCGAACATCTAATCTGAATGAGGAACTT
GGCCAGGTTAAATACATATTTTCTGACAAAACTGGTACTCTGACATGCAATGTAATGCAG
TTTAAGAAGTGCACCATAGCGGGAGTTGCTTATGGCCATGTCCCTGAACCTGAGGATTAT
GGCTGCTCTCCTGATGAATGGCAGAACTCACAGTTTGGAGATGAAAAAACATTTAGTGAT
TCATCATTGCTGGAAAATCTCCAAAATAATCATCCAACTGCACCTATAATATGTGAATTT
CTTACAATGATGGCAGTCTGTCACACAGCAGTGCCAGAGCGAGAAGGTGACAAGATTATT
TATCAAGCAGCATCTCCAGATGAGGGAGCATTGGTCAGAGCAGCCAAGCAATTGAATTTT
GTTTTCACTGGAAGAACACCCGACTCGGTGATTATAGATTCACTGGGGCAGGAAGAAAGA
TATGAATTGCTCAATGTCTTGGAGTTTACCAGTGCTAGGAAAAGAATGTCAGTGATTGTT
CGCACTCCATCTGGAAAGTTACGACTCTACTGCAAAGGAGCTGACACTGTAATTTATGAT
CGACTGGCAGAGACGTCAAAATACAAAGAAATTACCCTAAAACATTTAGAGCAGTTTGCT
ACAGAAGGGTTAAGAACTTTATGTTTTGCTGTGGCTGAGATTTCAGAGAGCGACTTTCAG
GAGTGGCGAGCAGTCTATCAGCGAGCATCTACATCTGTGCAGAACAGGCTACTCAAACTC
GAAGAGAGTTATGAGTTGATTGAAAAGAATCTTCAGCTACTTGGAGCAACAGCCATTGAG
GATAAATTACAAGATCAAGTGCCTGAAACCATAGAAACGCTAATGAAAGCAGACATCAAA
ATCTGGATCCTTACAGGGGACAAGCAAGAAACTGCCATTAACATCGGACACTCCTGCAAA
CTGTTGAAGAAGAACATGGGAATGATTGTTATAAATGAAGGCTCTCTTGATGGAACAAGG
GAAACTCTCAGTCGTCACTGTACTACCCTTGGTGATGCTCTCCGGAAAGAGAATGATTTT
GCTCTTATAATTGATGGGAAAACCCTCAAATATGCCTTAACCTTTGGAGTACGACAGTAT
TTCCTGGACTTAGCTTTGTCATGCAAAGCTGTCATTTGCTGTCGGGTTTCTCCTCTTCAA
AAATCTGAAGTTGTTGAGATGGTTAAGAAACAAGTCAAAGTCGTAACGCTTGCAATCGGT
GATGGAGCAAATGATGTCAGCATGATACAGACAGCGCACGTTGGTGTTGGTATCAGTGGC
AATGAAGGCCTGCAGGCAGCTAATTCCTCTGACTACTCCATAGCTCAGTTCAAATATTTG
AAGAATTTACTGATGATTCATGGTGCCTGGAACTATAACAGAGTCTCCAAGTGCATCTTA
TACTGCTTCTACAAGAATATAGTGCTCTATATTATCGAGATCTGGTTTGCCTTTGTTAAT
GGCTTTTCTGGACAGATCCTCTTTGAAAGATGGTGTATAGGTCTCTATAACGTGATGTTT
ACAGCAATGCCTCCTTTAACTCTTGGAATATTTGAGAGATCATGCAGAAAAGAGAACATG
TTGAAGTACCCTGAATTATACAAAACATCTCAGAATGCCCTGGACTTCAACACCAAGGTT
TTCTGGGTTCATTGTTTAAATGGCCTCTTCCACTCAGTTATTCTGTTTTGGTTTCCACTA
AAAGCCCTTCAGTATGGTACTGCATTTGGAAATGGGAAAACCTCGGATTATCTGCTACTG
GGAAACTTTGTGTACACTTTTGTGGTGATAACTGTGTGTTTGAAAGCTGGATTGGAGACA
TCATATTGGACATGGTTCAGCCACATAGCGATATGGGGGAGCATCGCACTCTGGGTGGTG
TTTTTTGGAATCTACTCATCTCTGTGGCCTGCCATTCCGATGGCCCCTGATATGTCAGGA
GAGGCAGCCATGTTGTTCAGTTCTGGAGTCTTTTGGATGGGCTTGTTATTCATCCCTGTG
GCATCTCTGCTCCTTGATGTGGTGTACAAGGTTATCAAGAGGACTGCTTTTAAAACATTG
GTCGATGAAGTTCAGGAGCTGGAGGCAAAATCTCAAGACCCAGGAGCAGTTGTACTTGGA
AAAAGCCTGACCGAGAGGGCGCAACTGCTCAAGAACGTCTTTAAGAAGAACCACGTGAAC
TTGTACCGCTCTGAATCCTTGCAACAAAATCTGCTCCATGGGTATGCGTTCTCTCAAGAT
GAAAATGGAATCGTTTCACAGTCTGAAGTGATAAGAGCATATGATACCACGAAACAGAGG
CCCGACGAATGG
|
| Enzyme 35 GenBank Gene ID |
AF067820  |
| Enzyme 35 GeneCard ID |
ATP8A1  |
| Enzyme 35 GenAtlas ID |
ATP8A1  |
| Enzyme 35 HGNC ID |
HGNC:13531  |
| Enzyme 35 Chromosome Location |
4 |
| Enzyme 35 Locus |
4p13 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Mouro I, Halleck MS, Schlegel RA, Mattei MG, Williamson P, Zachowski A, Devaux P, Cartron JP, Colin Y: Cloning, expression, and chromosomal mapping of a human ATPase II gene, member of the third subfamily of P-type ATPases and orthologous to the presumed bovine and murine aminophospholipid translocase. Biochem Biophys Res Commun. 1999 Apr 13;257(2):333-9. [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
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
6759 |
| Enzyme 36 Name |
Probable phospholipid-transporting ATPase IM |
| Enzyme 36 Synonyms |
- ATPase class I type 8B member 4
|
| Enzyme 36 Gene Name |
ATP8B4 |
| Enzyme 36 Protein Sequence |
>Probable phospholipid-transporting ATPase IM
MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFLPINLFEQFQRVANAYF
LCLLILQLIPEISSLTWFTTIVPLVLVITMTAVKDATDDYFRHKSDNQVNNRQSEVLINS
KLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALS
VTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTS
WCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLICLGIILAIGNSIWES
QTGDQFRTFLFWNEGEKSSVFSGFLTFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWD
RKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDD
LDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSE
ENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNT
RKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAY
RDLDDKYFKEWHKMLEDANAATEERDERIAGLYEEIERDLMLLGATAVEDKLQEGVIETV
TSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNL
FGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELAC
MCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQA
VLASDYSFAQFRYLQRLLLVHGRWSYFRMCKFLCYFFYKNFAFTLVHFWFGFFCGFSAQT
VYDQWFITLFNIVYTSLPVLAMGIFDQDVSDQNSVDCPQLYKPGQLNLLFNKRKFFICVL
HGIYTSLVLFFIPYGAFYNVAGEDGQHIADYQSFAVTMATSLVIVVSVQIALDTSYWTFI
NHVFIWGSIAIYFSILFTMHSNGIFGIFPNQFPFVGNARHSLTQKCIWLVILLTTVASVM
PVVAFRFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGE
LITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL
|
| Enzyme 36 Number of Residues |
1192 |
| Enzyme 36 Molecular Weight |
135867.0 |
| Enzyme 36 Theoretical pI |
6.99 |
| Enzyme 36 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 36 General Function |
Involved in ATP binding |
| Enzyme 36 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
- 45-66
73-92
277-298
328-349
872-892
905-924
955-976
991-1013
1020-1040
1061-1085
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
50083277  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q8TF62  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
AT8B4_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>3579 bp
ATGTTCTGCAGTGAAAAGAAATTGCGTGAAGTGGAACGGATAGTGAAAGCCAATGACCGT
GAATATAATGAAAAGTTCCAGTATGCGGATAATCGTATCCACACATCGAAATATAATATT
CTCACCTTCTTGCCAATTAATTTATTTGAACAGTTCCAAAGAGTGGCAAATGCCTATTTT
CTTTGCCTTCTGATTTTACAGCTAATTCCAGAAATTTCCTCCTTGACCTGGTTTACCACC
ATTGTGCCTTTGGTCCTGGTGATAACTATGACAGCTGTCAAAGATGCCACAGATGACTAT
TTTCGCCACAAGAGTGATAATCAAGTGAATAATCGGCAGTCTGAAGTGCTCATCAACAGC
AAACTGCAGAATGAAAAATGGATGAATGTCAAAGTGGGAGACATCATTAAATTAGAAAAT
AACCAATTTGTTGCTGCTGATTTACTTCTCCTATCAAGTAGTGAGCCACATGGTCTCTGT
TATGTTGAAACTGCTGAGCTTGATGGGGAAACGAACCTAAAAGTCCGCCATGCACTATCA
GTTACTTCAGAACTTGGAGCAGATATCAGCAGACTTGCAGGGTTTGATGGGATTGTTGTC
TGTGAGGTGCCTAACAACAAGTTAGATAAATTCATGGGAATCCTTTCTTGGAAAGACAGC
AAGCATTCCCTCAACAATGAGAAGATAATCCTGAGAGGCTGCATCCTGAGAAATACCAGC
TGGTGTTTTGGAATGGTTATTTTTGCAGGTCCTGACACTAAACTAATGCAGAATAGTGGT
AAGACAAAGTTTAAAAGGACAAGCATTGATAGATTGATGAATACTCTAGTACTATGGATT
TTTGGGTTTCTGATATGCTTGGGAATTATTCTTGCAATAGGAAATTCAATCTGGGAGAGT
CAAACTGGGGACCAATTCAGAACTTTCCTCTTTTGGAATGAAGGAGAGAAGAGCTCTGTG
TTCTCCGGATTCTTAACATTCTGGTCATATATTATTATTCTCAATACAGTTGTACCCATT
TCCTTATATGTGAGTGTGGAAGTAATTCGTCTAGGACACAGTTATTTTATAAACTGGGAC
CGGAAGATGTATTATTCTCGAAAAGCAATACCTGCAGTGGCTCGAACGACCACGCTCAAT
GAGGAACTGGGGCAGATTGAGTACATTTTCTCCGACAAAACGGGTACCCTCACTCAAAAC
ATCATGACCTTTAAAAGATGTTCCATTAATGGGAGAATCTATGGTGAAGTACATGATGAC
CTGGATCAGAAGACAGAAATAACTCAGGAAAAAGAGCCTGTGGATTTCTCAGTCAAATCT
CAAGCGGATAGAGAATTTCAGTTCTTTGACCACCATCTGATGGAATCCATTAAAATGGGT
GATCCCAAAGTTCATGAATTCCTTAGGTTACTTGCTCTCTGCCACACTGTAATGTCAGAA
GAGAATAGCGCAGGAGAGCTGATTTACCAAGTTCAGTCACCTGATGAAGGGGCTCTAGTG
ACTGCCGCTAGAAATTTTGGGTTCATTTTTAAATCCCGGACCCCAGAGACCATAACAATA
GAAGAATTGGGAACACTAGTTACTTATCAATTACTTGCCTTTTTGGATTTCAACAACACC
AGAAAAAGGATGTCTGTCATAGTTCGAAACCCAGAAGGACAGATAAAGCTTTATTCCAAA
GGAGCAGATACTATTCTGTTTGAAAAACTTCATCCTTCCAATGAAGTCCTTTTGTCTTTG
ACGTCAGACCACCTCAGTGAATTTGCAGGGGAAGGCCTTCGGACCTTGGCCATCGCATAC
AGAGACCTGGATGACAAGTACTTTAAAGAGTGGCATAAGATGCTTGAAGATGCGAATGCT
GCCACAGAAGAGAGGGATGAACGAATAGCTGGGCTATATGAAGAAATTGAAAGAGATTTG
ATGCTACTAGGTGCCACTGCTGTAGAAGATAAGTTACAGGAGGGTGTTATTGAAACAGTT
ACAAGTTTATCACTAGCCAATATTAAGATCTGGGTCCTAACAGGAGACAAACAAGAAACT
GCCATCAACATCGGTTATGCCTGCAACATGCTGACTGACGACATGAATGATGTGTTTGTG
ATAGCAGGGAATAATGCTGTGGAAGTGAGAGAAGAACTCAGGAAAGCAAAACAAAATTTG
TTTGGACAAAACAGAAATTTTTCCAATGGCCATGTAGTTTGTGAAAAAAAGCAGCAGCTG
GAGTTGGATTCTATTGTAGAAGAAACCATAACAGGAGATTATGCCTTAATCATAAATGGC
CACAGTTTGGCTCATGCCCTAGAAAGTGATGTCAAGAATGATCTCCTAGAACTTGCTTGC
ATGTGTAAGACTGTAATTTGCTGCAGGGTCACTCCACTCCAGAAAGCCCAAGTGGTAGAG
CTGGTGAAGAAGTACAGAAATGCTGTTACTTTGGCCATTGGTGATGGAGCCAATGATGTC
AGCATGATTAAAAGTGCTCACATTGGTGTTGGCATCAGCGGCCAGGAAGGATTGCAAGCA
GTCTTAGCCAGCGACTATTCATTTGCACAGTTTAGATATCTCCAAAGGCTTCTCCTTGTT
CATGGAAGGTGGTCTTATTTCCGAATGTGCAAATTCTTATGCTATTTCTTCTATAAGAAT
TTTGCATTTACACTTGTGCATTTCTGGTTTGGTTTCTTCTGTGGTTTCTCAGCCCAGACT
GTTTATGACCAGTGGTTCATCACCCTTTTTAACATTGTTTACACATCACTGCCTGTTTTA
GCCATGGGGATTTTTGACCAGGATGTGAGTGACCAGAACAGCGTGGACTGTCCCCAGCTC
TACAAACCAGGACAGCTGAATCTGCTTTTTAACAAGCGTAAATTTTTCATTTGCGTGTTG
CATGGAATCTACACCTCATTAGTCCTTTTCTTCATCCCCTATGGGGCCTTTTACAACGTG
GCTGGAGAAGATGGGCAACATATTGCTGACTACCAGTCCTTTGCAGTTACCATGGCCACA
TCTTTGGTCATTGTGGTCAGTGTGCAGATAGCCTTGGATACCAGTTACTGGACTTTCATT
AATCACGTCTTCATCTGGGGGAGCATTGCCATTTATTTCTCCATTTTATTTACAATGCAC
AGTAATGGCATCTTTGGCATCTTCCCAAACCAGTTTCCATTTGTTGGTAATGCACGACAT
TCCCTGACCCAGAAGTGCATCTGGCTTGTAATTCTCTTAACAACAGTGGCTTCAGTTATG
CCAGTGGTGGCATTCAGATTTTTGAAGGTGGATTTATACCCAACCCTGAGTGATCAGATC
CGCCGGTGGCAGAAGGCTCAAAAGAAGGCAAGGCCTCCAAGTAGCCGAAGGCCTCGGACC
CGCAGGTCAAGCTCAAGAAGGTCTGGATATGCTTTTGCTCACCAAGAAGGCTATGGAGAG
CTTATCACATCTGGAAAAAATATGCGAGCTAAAAATCCACCCCCAACATCAGGGCTGGAA
AAGACACATTATAATAGCACTAGCTGGATTGAAAATTTATGTAAGAAAACCACAGACACC
GTGAGCAGCTTTAGCCAGGATAAAACAGTGAAACTGTGA
|
| Enzyme 36 GenBank Gene ID |
NM_024837.2  |
| Enzyme 36 GeneCard ID |
ATP8B4  |
| Enzyme 36 GenAtlas ID |
ATP8B4  |
| Enzyme 36 HGNC ID |
HGNC:13536  |
| Enzyme 36 Chromosome Location |
1 |
| Enzyme 36 Locus |
15q21.2 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [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
]
- 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
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
6781 |
| Enzyme 37 Name |
Probable phospholipid-transporting ATPase IF |
| Enzyme 37 Synonyms |
- ATPase IR
- ATPase class VI type 11B
|
| Enzyme 37 Gene Name |
ATP11B |
| Enzyme 37 Protein Sequence |
>Probable phospholipid-transporting ATPase IF
MWRWIRQQLGFDPPHQSDTRTIYVANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLF
EQFRRVANFYFLIIFLVQLMIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHNSDNEVN
GAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGE
TNLKTHVAVPETALLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPE
SLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLVILISE
AVISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVT
VEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFR
ECSINGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHLNNLSHLTTSSSFRTSPENETE
LIKEHDLFFKAVSLCHTVQISNVQTDCTGDGPWQSNLAPSQLEYYASSPDEKALVEAAAR
IGIVFIGNSEETMEVKTLGKLERYKLLHILEFDSDRRRMSVIVQAPSGEKLLFAKGAESS
ILPKCIGGEIEKTRIHVDEFALKGLRTLCIAYRKFTSKEYEEIDKRIFEARTALQQREEK
LAAVFQFIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSC
GHFHRTMNILELINQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLF
MEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITLAVGDGANDVSMIQEAHVGIGIMG
KEGRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYC
LFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHVDPHVLQNKPTLYRDISKNRLLSIKT
FLYWTILGFSHAFIFFFGSYLLIGKDTSLLGNGQMFGNWTFGTLVFTVMVITVTVKMALE
THFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLLSSGSAWFAIILMV
VTCLFLDIIKKVFDRHLHPTSTEKAQLTETNAGIKCLDSMCCFPEGEAACASVGRMLERV
IGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC
|
| Enzyme 37 Number of Residues |
1177 |
| Enzyme 37 Molecular Weight |
134188.6 |
| Enzyme 37 Theoretical pI |
6.95 |
| Enzyme 37 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 37 General Function |
Involved in ATP binding |
| Enzyme 37 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
- 56-77
83-104
290-311
342-359
877-898
911-930
961-982
998-1020
1026-1047
1066-1090
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
62632750  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q9Y2G3  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
AT11B_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>3534 bp
ATGTGGCGCTGGATCCGGCAGCAGCTGGGTTTTGACCCACCACATCAGAGTGACACAAGA
ACCATCTACGTAGCCAACAGGTTTCCTCAGAATGGCCTTTACACACCTCAGAAATTTATA
GATAACAGGATCATTTCATCTAAGTACACTGTGTGGAATTTTGTTCCAAAAAATTTATTT
GAACAGTTCAGAAGAGTGGCAAACTTTTATTTTCTTATTATATTTTTGGTTCAGCTTATG
ATTGATACACCTACCAGTCCAGTTACCAGTGGACTTCCATTATTCTTTGTGATAACAGTA
ACTGCCATAAAGCAGGGATATGAAGATTGGTTACGGCATAACTCAGATAATGAAGTAAAT
GGAGCTCCTGTTTATGTTGTTCGAAGTGGTGGCCTTGTAAAAACTAGATCAAAAAACATT
CGGGTGGGTGATATTGTTCGAATAGCCAAAGATGAAATTTTTCCTGCAGACTTGGTGCTT
CTGTCCTCAGATCGACTGGATGGTTCCTGTCACGTTACAACTGCTAGTTTGGACGGAGAA
ACTAACCTGAAGACACATGTGGCAGTTCCAGAAACAGCATTATTACAAACAGTTGCCAAT
TTGGACACTCTAGTAGCTGTAATAGAATGCCAGCAACCAGAAGCAGACTTATACAGATTC
ATGGGACGAATGATCATAACCCAACAAATGGAAGAAATTGTAAGACCTCTGGGGCCGGAG
AGTCTCCTGCTTCGTGGAGCCAGATTAAAAAACACAAAAGAAATTTTTGGTGTTGCGGTA
TACACTGGAATGGAAACTAAGATGGCATTAAATTACAAGAGCAAATCACAGAAACGATCT
GCAGTAGAAAAGTCAATGAATACATTTTTGATAATTTATCTAGTAATTCTTATATCTGAA
GCTGTCATCAGCACTATCTTGAAGTATACATGGCAAGCTGAAGAAAAATGGGATGAACCT
TGGTATAACCAAAAAACAGAACATCAAAGAAATAGCAGTAAGATTCTGAGATTTATTTCA
GACTTCCTTGCTTTTTTGGTTCTCTACAATTTCATCATTCCAATTTCATTATATGTGACA
GTCGAAATGCAGAAATTTCTTGGATCATTTTTTATTGGCTGGGATCTTGATCTGTATCAT
GAAGAATCAGATCAGAAAGCTCAAGTCAATACTTCCGATCTGAATGAAGAGCTTGGACAG
GTAGAGTACGTGTTTACAGATAAAACTGGTACACTGACAGAAAATGAGATGCAGTTTCGG
GAATGTTCAATTAATGGCATGAAATACCAAGAAATTAATGGTAGACTTGTACCCGAAGGA
CCAACACCAGACTCTTCAGAAGGAAACTTATCTTATCTTAGTAGTTTATCCCATCTTAAC
AACTTATCCCATCTTACAACCAGTTCCTCTTTCAGAACCAGTCCTGAAAATGAAACTGAA
CTAATTAAAGAACATGATCTCTTCTTTAAAGCAGTCAGTCTCTGTCACACTGTACAGATT
AGCAATGTTCAAACTGACTGCACTGGTGATGGTCCCTGGCAATCCAACCTGGCACCATCG
CAGTTGGAGTACTATGCATCTTCACCAGATGAAAAGGCTCTAGTAGAAGCTGCTGCAAGG
ATTGGTATTGTGTTTATTGGCAATTCTGAAGAAACTATGGAGGTTAAAACTCTTGGAAAA
CTGGAACGGTACAAACTGCTTCATATTCTGGAATTTGATTCAGATCGTAGGAGAATGAGT
GTAATTGTTCAGGCACCTTCAGGTGAGAAGTTATTATTTGCTAAAGGAGCTGAGTCATCA
ATTCTCCCTAAATGTATAGGTGGAGAAATAGAAAAAACCAGAATTCATGTAGATGAATTT
GCTTTGAAAGGGCTAAGAACTCTGTGTATAGCATATAGAAAATTTACATCAAAAGAGTAT
GAGGAAATAGATAAACGCATATTTGAAGCCAGGACTGCCTTGCAGCAGCGGGAAGAGAAA
TTGGCAGCTGTTTTCCAGTTCATAGAGAAAGACCTGATATTACTTGGAGCCACAGCAGTA
GAAGACAGACTACAAGATAAAGTTCGAGAAACTATTGAAGCATTGAGAATGGCTGGTATC
AAAGTATGGGTACTTACTGGGGATAAACATGAAACAGCTGTTAGTGTGAGTTTATCATGT
GGCCATTTTCATAGAACCATGAACATCCTTGAACTTATAAACCAGAAATCAGACAGCGAG
TGTGCTGAACAATTGAGGCAGCTTGCCAGAAGAATTACAGAGGATCATGTGATTCAGCAT
GGGCTGGTAGTGGATGGGACCAGCCTATCTCTTGCACTCAGGGAGCATGAAAAACTATTT
ATGGAAGTTTGCAGAAATTGTTCAGCTGTATTATGCTGTCGTATGGCTCCACTGCAGAAA
GCAAAAGTAATAAGACTAATAAAAATATCACCTGAGAAACCTATAACATTGGCTGTTGGT
GATGGTGCTAATGACGTAAGCATGATACAAGAAGCCCATGTTGGCATAGGAATCATGGGT
AAAGAAGGAAGACAGGCTGCAAGAAACAGTGACTATGCAATAGCCAGATTTAAGTTCCTC
TCCAAATTGCTTTTTGTTCATGGTCATTTTTATTATATTAGAATAGCTACCCTTGTACAG
TATTTTTTTTATAAGAATGTGTGCTTTATCACACCCCAGTTTTTATATCAGTTCTACTGT
TTGTTTTCTCAGCAAACATTGTATGACAGCGTGTACCTGACTTTATACAATATTTGTTTT
ACTTCCCTACCTATTCTGATATATAGTCTTTTGGAACAGCATGTAGACCCTCATGTGTTA
CAAAATAAGCCCACCCTTTATCGAGACATTAGTAAAAACCGCCTCTTAAGTATTAAAACA
TTTCTTTATTGGACCATCCTGGGCTTCAGTCATGCCTTTATTTTCTTTTTTGGATCCTAT
TTACTAATAGGGAAAGATACATCTCTGCTTGGAAATGGCCAGATGTTTGGAAACTGGACA
TTTGGCACTTTGGTCTTCACAGTCATGGTTATTACAGTCACAGTAAAGATGGCTCTGGAA
ACTCATTTTTGGACTTGGATCAACCATCTCGTTACCTGGGGATCTATTATATTTTATTTT
GTATTTTCCTTGTTTTATGGAGGGATTCTCTGGCCATTTTTGGGCTCCCAGAATATGTAT
TTTGTGTTTATTCAGCTCCTGTCAAGTGGTTCTGCTTGGTTTGCCATAATCCTCATGGTT
GTTACATGTCTATTTCTTGATATCATAAAGAAGGTCTTTGACCGACACCTCCACCCTACA
AGTACTGAAAAGGCACAGCTTACTGAAACAAATGCAGGTATCAAGTGCTTGGACTCCATG
TGCTGTTTCCCGGAAGGAGAAGCAGCGTGTGCATCTGTTGGAAGAATGCTGGAACGAGTT
ATAGGAAGATGTAGTCCAACCCACATCAGCAGATCATGGAGTGCATCGGATCCTTTCTAT
ACCAACGACAGGAGCATCTTGACTCTCTCCACAATGGACTCATCTACTTGTTAA
|
| Enzyme 37 GenBank Gene ID |
NM_014616.1  |
| Enzyme 37 GeneCard ID |
ATP11B  |
| Enzyme 37 GenAtlas ID |
ATP11B  |
| Enzyme 37 HGNC ID |
HGNC:13553  |
| Enzyme 37 Chromosome Location |
3 |
| Enzyme 37 Locus |
3q27 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Halleck MS, Lawler JF JR, Blackshaw S, Gao L, Nagarajan P, Hacker C, Pyle S, Newman JT, Nakanishi Y, Ando H, Weinstock D, Williamson P, Schlegel RA: Differential expression of putative transbilayer amphipath transporters. Physiol Genomics. 1999 Nov 11;1(3):139-50. [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
]
- Halleck MS, Schlegel RA, Williamson PL: Reanalysis of ATP11B, a type IV P-type ATPase. J Biol Chem. 2002 Mar 22;277(12):9736-40. Epub 2002 Jan 14. [PubMed
]
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [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
]
- 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 |
6785 |
| Enzyme 38 Name |
Probable phospholipid-transporting ATPase IK |
| Enzyme 38 Synonyms |
- ATPase class I type 8B member 3
|
| Enzyme 38 Gene Name |
ATP8B3 |
| Enzyme 38 Protein Sequence |
>Probable phospholipid-transporting ATPase IK
MGTGPAQTPRSTRAGPEPSPAPPGPGDTGDSDVTQEGSGPAGIRGGETVIRAGMGDSPGR
GAPERRHKAQPGRARKYEWRPEGPTSMGSLGQREDLQDEDRNSAFTWKVQANNRAYNGQF
KEKVILCWQRKKYKTNVIRTAKYNFYSFLPLNLYEQFHRVSNLFFLIIIILQSIPDISTL
PWFSLSTPMVCLLFIRATRDLVDDMGRHKSDRAINNRPCQILMGKSFKQKKWQDLCVGDV
VCLRKDNIVPADMLLLASTEPSSLCYVETVDIDGETNLKFRQALMVTHKELATIKKMASF
QGTVTCEAPNSRMHHFVGCLEWNDKKYSLDIGNLLLRGCRIRNTDTCYGLVIYAGFDTKI
MKNCGKIHLKRTKLDLLMNKLVVVIFISVVLVCLVLAFGFGFSVKEFKDHHYYLSGVHGS
SVAAESFFVFWSFLILLSVTIPMSMFILSEFIYLGNSVFIDWDVQMYYKPQDVPAKARST
SLNDHLGQVEYIFSDKTGTLTQNILTFNKCCISGRVYGPDSEATTRPKENPYLWNKFADG
KLLFHNAALLHLVRTNGDEAVREFWRLLAICHTVMVRESPRERPDQLLYQAASPDEGALV
TAARNFGYVFLSRTQDTVTIMELGEERVYQVLAIMDFNSTRKRMSVLVRKPEGAICLYTK
GADTVIFERLHRRGAMEFATEEALAAFAQETLRTLCLAYREVAEDIYEDWQQRHQEASLL
LQNRAQALQQLLGATAIEDRLQDGVPETIKCLKKSNIKIWVLTGDKQETAVNIGFACELL
SENMLILEEKEISRILETYWENSNNLLTRESLSQVKLALVINGDFLDKLLVSLRKEPRAL
AQNVNMDEAWQELGQSRRDFLYARRLSLLCRRFGLPLAAPPAQDSRARRSSEVLQERAFV
DLASKCQAVICCRVTPKQKALIVALVKKYHQVVTLAIGDGANDINMIKTADVGVGLAGQE
GMQAVQNSDFVLGQFCFLQRLLLVHGRWSYVRICKFLRYFFYKSMASMMVQVWFACYNGF
TGQPLYEGWFLALFNLLYSTLPVLYIGLFEQDVSAEQSLEKPELYVVGQKDELFNYWVFV
QAIAHGVTTSLVNFFMTLWISRDTAGPASFSDHQSFAVVVALSCLLSITMEVILIIKYWT
ALCVATILLSLGFYAIMTTTTQSFWLFRVSPTTFPFLYADLSVMSSPSILLVVLLSVSIN
TFPVLALRVIFPALKELRAKEEKVEEGPSEEIFTMEPLPHVHRESRARRSSYAFSHREGY
ANLITQGTILRRGPGVSSDIASESLDPSDEEAASSPKESQ
|
| Enzyme 38 Number of Residues |
1300 |
| Enzyme 38 Molecular Weight |
146750.9 |
| Enzyme 38 Theoretical pI |
7.96 |
| Enzyme 38 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 38 General Function |
Involved in ATP binding |
| Enzyme 38 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
- 150-171
178-197
382-403
431-452
996-1016
1029-1048
1079-1100
1113-1135
1142-1162
1183-1207
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
44888835  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
O60423  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
AT8B3_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>3903 bp
ATGGGCACTGGCCCCGCTCAGACTCCCAGGAGCACCAGAGCTGGCCCTGAGCCAAGCCCT
GCCCCACCAGGACCTGGGGACACGGGTGACTCAGACGTGACTCAGGAAGGCTCAGGTCCT
GCTGGCATCCGCGGAGGTGAGACGGTGATCAGAGCTGGGATGGGAGACTCCCCAGGCAGA
GGGGCACCTGAGAGGAGGCACAAGGCCCAGCCTGGCCGGGCTAGGAAGTATGAATGGAGA
CCAGAAGGCCCCACCAGCATGGGCAGCCTCGGCCAGAGAGAAGATCTCCAAGATGAGGAC
AGGAACTCAGCATTCACCTGGAAGGTCCAGGCCAACAACCGTGCCTACAACGGGCAGTTC
AAGGAGAAGGTGATCCTGTGCTGGCAAAGGAAGAAATACAAGACCAATGTCATCCGCACG
GCCAAGTACAACTTCTACTCGTTCCTGCCGCTGAACCTGTACGAGCAGTTCCACCGCGTG
TCCAACCTGTTCTTCCTCATCATCATCATCCTGCAGAGCATTCCCGACATCTCCACGCTG
CCCTGGTTCTCGCTCAGTACCCCTATGGTCTGCCTCCTCTTCATCCGTGCCACCCGGGAC
CTGGTGGACGACATGGGGAGACACAAGAGTGACAGAGCCATCAACAACAGACCCTGCCAG
ATTCTGATGGGGAAGAGCTTCAAGCAGAAGAAATGGCAGGATCTGTGCGTGGGGGATGTG
GTCTGTCTCCGCAAGGACAACATCGTCCCAGCCGACATGCTCTTGCTGGCCAGCACGGAG
CCCAGCAGCCTGTGCTATGTGGAGACGGTGGACATTGACGGGGAGACCAACTTGAAGTTC
AGACAGGCCCTGATGGTCACCCACAAAGAACTGGCCACTATAAAGAAGATGGCGTCCTTT
CAAGGCACAGTGACGTGTGAGGCGCCTAACAGTCGGATGCACCACTTCGTGGGGTGCCTG
GAATGGAATGACAAGAAATACTCCCTGGACATTGGCAACCTCCTCCTCCGAGGCTGCAGG
ATTCGCAACACAGACACCTGCTATGGACTGGTCATTTATGCTGGTTTTGACACAAAAATT
ATGAAGAACTGTGGCAAGATCCATTTGAAGAGAACCAAGCTGGACCTCCTGATGAACAAG
CTGGTGGTTGTGATCTTCATCTCCGTGGTGCTTGTCTGCCTGGTGTTGGCCTTCGGCTTC
GGTTTCTCAGTCAAAGAATTCAAAGACCACCACTACTACCTCTCGGGGGTGCATGGGAGC
AGCGTGGCCGCAGAGTCCTTCTTCGTCTTCTGGAGCTTCCTCATCCTGCTCAGCGTCACC
ATCCCGATGTCCATGTTCATCCTGTCCGAGTTCATCTACCTGGGGAACAGCGTCTTCATC
GACTGGGACGTGCAGATGTACTACAAGCCGCAGGACGTGCCTGCCAAGGCCCGCAGCACC
AGCCTCAACGACCACCTGGGCCAGGTGGAATACATCTTCTCGGACAAGACGGGCACGCTC
ACGCAGAACATCTTGACCTTCAACAAGTGCTGCATCAGCGGCCGCGTCTATGGGCCGGAT
TCAGAGGCCACGACCCGACCTAAGGAGAACCCCTACCTCTGGAACAAGTTCGCCGACGGG
AAGCTGCTCTTCCACAATGCGGCCCTGCTGCACCTCGTGCGGACCAACGGGGACGAGGCC
GTGCGGGAGTTCTGGCGCCTGCTGGCCATCTGCCACACGGTGATGGTGCGGGAGAGCCCC
CGTGAGCGCCCAGACCAGCTGTTGTACCAGGCGGCCTCCCCCGACGAGGGGGCGCTGGTC
ACCGCAGCCCGGAACTTCGGCTACGTGTTCCTGTCCCGCACCCAGGACACCGTCACGATC
ATGGAGCTGGGGGAGGAACGGGTCTACCAGGTCCTGGCCATAATGGACTTCAACAGCACG
CGCAAACGGATGTCGGTGCTGGTTCGAAAGCCAGAGGGCGCCATCTGCCTGTACACCAAG
GGCGCCGACACGGTCATCTTCGAACGCTTGCACAGGAGGGGGGCAATGGAATTTGCCACA
GAGGAGGCCTTGGCTGCCTTTGCCCAGGAGACCCTGCGGACACTGTGCCTGGCCTACAGG
GAGGTGGCTGAGGACATTTACGAGGACTGGCAGCAGCGCCACCAGGAGGCCAGCCTCCTG
CTGCAGAACCGGGCACAGGCCCTGCAACAGCTGCTGGGAGCCACAGCCATCGAGGACAGA
CTCCAGGACGGTGTCCCTGAAACCATCAAATGTCTCAAGAAGAGCAACATCAAAATATGG
GTGCTCACCGGGGACAAGCAGGAAACGGCTGTGAACATCGGCTTCGCCTGCGAGCTGCTG
TCAGAGAATATGCTCATTCTGGAGGAGAAGGAGATTAGCCGCATCCTGGAGACCTACTGG
GAAAACAGTAACAACCTTCTAACCAGGGAGTCCCTGTCGCAGGTCAAGCTGGCCTTGGTC
ATTAACGGAGACTTCCTGGACAAACTGCTGGTGTCCCTGCGGAAGGAGCCGCGCGCCCTG
GCGCAGAACGTGAACATGGACGAGGCGTGGCAGGAGCTCGGCCAGTCCAGGAGGGATTTC
CTCTACGCCAGGCGCCTGTCCCTGCTGTGCCGGAGGTTCGGGCTCCCGCTGGCTGCACCG
CCAGCCCAGGACTCCAGAGCCCGCCGTAGCTCCGAGGTGCTGCAGGAGCGCGCCTTCGTG
GACCTGGCGTCCAAGTGCCAGGCGGTCATCTGCTGCCGCGTGACGCCCAAGCAGAAGGCC
CTGATCGTGGCCCTGGTCAAGAAGTACCACCAGGTGGTGACCCTGGCCATCGGGGACGGT
GCCAACGACATCAACATGATCAAGACCGCGGACGTGGGCGTGGGGCTGGCGGGCCAGGAG
GGCATGCAGGCAGTTCAGAACAGCGACTTCGTGCTCGGCCAGTTCTGCTTCCTGCAGCGC
CTCCTGCTGGTGCACGGCCGCTGGTCCTACGTGCGGATCTGCAAGTTCCTGCGCTACTTC
TTCTACAAGAGCATGGCCAGCATGATGGTGCAGGTCTGGTTTGCCTGCTACAACGGCTTC
ACCGGCCAGCCCCTGTATGAAGGATGGTTCCTGGCTCTTTTCAACCTCCTGTACAGCACC
CTGCCAGTTCTCTACATTGGGCTCTTTGAGCAGGACGTGAGCGCAGAGCAGAGCCTGGAG
AAGCCGGAGCTGTACGTGGTGGGGCAGAAGGACGAGCTCTTCAACTACTGGGTCTTCGTC
CAAGCCATCGCCCATGGTGTGACCACCTCTCTGGTCAACTTCTTCATGACACTGTGGATC
AGCCGCGACACGGCGGGACCCGCCAGCTTCAGCGACCACCAGTCCTTTGCGGTCGTGGTG
GCCCTGTCTTGCCTGCTGTCCATCACCATGGAGGTCATTCTTATCATCAAGTACTGGACC
GCCCTGTGCGTGGCGACCATCCTCCTCAGCCTTGGTTTCTACGCCATCATGACTACCACC
ACCCAGAGCTTCTGGCTCTTCAGAGTATCCCCCACGACCTTCCCGTTTCTGTATGCCGAC
CTCAGCGTGATGTCCTCTCCCTCCATCCTGCTGGTGGTCCTGCTGAGTGTGTCCATAAAC
ACCTTCCCTGTCCTGGCCCTCCGAGTCATCTTCCCAGCCCTCAAGGAGCTACGTGCCAAG
GAGGAGAAGGTGGAGGAGGGCCCCAGCGAGGAGATTTTCACCATGGAGCCCTTGCCTCAT
GTACACCGGGAGTCTCGTGCCCGCCGTTCCAGCTATGCTTTCTCCCACCGTGAGGGATAT
GCAAACCTCATCACTCAGGGCACAATTCTGCGGAGGGGACCAGGGGTCAGCAGTGACATA
GCATCTGAATCCCTAGACCCATCTGATGAAGAGGCAGCTTCGAGCCCAAAAGAGTCACAG
TGA
|
| Enzyme 38 GenBank Gene ID |
NM_138813.2  |
| Enzyme 38 GeneCard ID |
ATP8B3  |
| Enzyme 38 GenAtlas ID |
ATP8B3  |
| Enzyme 38 HGNC ID |
HGNC:13535  |
| Enzyme 38 Chromosome Location |
1 |
| Enzyme 38 Locus |
19p13.3 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- 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
]
- 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
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
7009 |
| Enzyme 39 Name |
Phosphatidylinositol transfer protein beta isoform |
| Enzyme 39 Synonyms |
- PI-TP-beta
- PtdIns transfer protein beta
- PtdInsTP beta
|
| Enzyme 39 Gene Name |
PITPNB |
| Enzyme 39 Protein Sequence |
>Phosphatidylinositol transfer protein beta isoform
MVLIKEFRVVLPCSVQEYQVGQLYSVAEASKNETGGGEGIEVLKNEPYEKDGEKGQYTHK
IYHLKSKVPAFVRMIAPEGSLVFHEKAWNAYPYCRTIVTNEYMKDDFFIKIETWHKPDLG
TLENVHGLDPNTWKTVEIVHIDIADRSQVEPADYKADEDPALFQSVKTKRGPLGPNWKKE
LANSPDCPQMCAYKLVTIKFKWWGLQSKVENFIQKQEKRIFTNFHRQLFCWIDKWIDLTM
EDIRRMEDETQKELETMRKRGSVRGTSAADV
|
| Enzyme 39 Number of Residues |
271 |
| Enzyme 39 Molecular Weight |
31539.9 |
| Enzyme 39 Theoretical pI |
6.87 |
| Enzyme 39 GO Classification |
| Function |
| — |
| Process |
- establishment of localization
- transport
|
| Component |
|
|
| Enzyme 39 General Function |
Involved in transport |
| Enzyme 39 Specific Function |
Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
Not Available |
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
6572213  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
P48739  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
PIPNB_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>816 bp
ATGGTGCTGATCAAGGAATTCCGTGTGGTTTTGCCATGTTCTGTTCAGGAGTATCAGGTT
GGGCAGCTTTACTCTGTTGCAGAAGCTAGTAAGAATGAGACTGGTGGTGGAGAAGGAATT
GAAGTCTTAAAGAATGAACCTTATGAGAAGGATGGAGAAAAGGGACAGTATACGCACAAA
ATTTATCACCTAAAGAGCAAAGTGCCTGCATTCGTGAGGATGATTGCTCCCGAGGGCTCC
TTGGTGTTTCATGAGAAAGCCTGGAATGCGTACCCCTACTGTAGAACAATTGTAACGAAT
GAATATATGAAAGATGATTTCTTCATTAAAATCGAAACATGGCACAAACCAGACTTGGGA
ACATTAGAAAATGTACATGGTTTAGATCCAAACACATGGAAAACTGTTGAAATTGTCCAT
ATAGATATTGCAGATAGAAGTCAAGTTGAACCAGCAGACTACAAAGCTGATGAAGACCCA
GCATTATTCCAGTCAGTCAAGACCAAGAGAGGCCCTTTGGGACCCAACTGGAAGAAGGAG
CTGGCAAACAGCCCTGACTGTCCCCAGATGTGTGCCTATAAGCTGGTGACCATCAAATTC
AAGTGGTGGGGACTGCAAAGCAAAGTAGAAAACTTCATTCAAAAGCAAGAAAAACGGATA
TTTACAAACTTCCATCGCCAGCTTTTTTGTTGGATTGACAAGTGGATCGATCTCACGATG
GAAGACATTAGGAGAATGGAAGACGAGACTCAGAAAGAACTAGAAACAATGCGTAAGAGG
GGTTCCGTTCGAGGCACGTCGGCTGCTGATGTCTAG
|
| Enzyme 39 GenBank Gene ID |
AL031591  |
| Enzyme 39 GeneCard ID |
PITPNB  |
| Enzyme 39 GenAtlas ID |
PITPNB  |
| Enzyme 39 HGNC ID |
HGNC:9002  |
| Enzyme 39 Chromosome Location |
2 |
| Enzyme 39 Locus |
22q12.1 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Tanaka S, Yamashita S, Hosaka K: Cloning and expression of human cDNA encoding phosphatidylinositol transfer protein beta. Biochim Biophys Acta. 1995 Dec 7;1259(3):199-202. [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
]
- 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
]
- 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 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
7307 |
| Enzyme 40 Name |
Multidrug resistance protein 3 |
| Enzyme 40 Synonyms |
- ATP-binding cassette sub-family B member 4
- P-glycoprotein 3
|
| Enzyme 40 Gene Name |
ABCB4 |
| Enzyme 40 Protein Sequence |
>Multidrug resistance protein 3
MDLEAAKNGTAWRPTSAEGDFELGISSKQKRKKTKTVKMIGVLTLFRYSDWQDKLFMSLG
TIMAIAHGSGLPLMMIVFGEMTDKFVDTAGNFSFPVNFSLSLLNPGKILEEEMTRYAYYY
SGLGAGVLVAAYIQVSFWTLAAGRQIRKIRQKFFHAILRQEIGWFDINDTTELNTRLTDD
ISKISEGIGDKVGMFFQAVATFFAGFIVGFIRGWKLTLVIMAISPILGLSAAVWAKILSA
FSDKELAAYAKAGAVAEEALGAIRTVIAFGGQNKELERYQKHLENAKEIGIKKAISANIS
MGIAFLLIYASYALAFWYGSTLVISKEYTIGNAMTVFFSILIGAFSVGQAAPCIDAFANA
RGAAYVIFDIIDNNPKIDSFSERGHKPDSIKGNLEFNDVHFSYPSRANVKILKGLNLKVQ
SGQTVALVGSSGCGKSTTVQLIQRLYDPDEGTINIDGQDIRNFNVNYLREIIGVVSQEPV
LFSTTIAENICYGRGNVTMDEIKKAVKEANAYEFIMKLPQKFDTLVGERGAQLSGGQKQR
IAIARALVRNPKILLLDEATSALDTESEAEVQAALDKAREGRTTIVIAHRLSTVRNADVI
AGFEDGVIVEQGSHSELMKKEGVYFKLVNMQTSGSQIQSEEFELNDEKAATRMAPNGWKS
RLFRHSTQKNLKNSQMCQKSLDVETDGLEANVPPVSFLKVLKLNKTEWPYFVVGTVCAIA
NGGLQPAFSVIFSEIIAIFGPGDDAVKQQKCNIFSLIFLFLGIISFFTFFLQGFTFGKAG
EILTRRLRSMAFKAMLRQDMSWFDDHKNSTGALSTRLATDAAQVQGATGTRLALIAQNIA
NLGTGIIISFIYGWQLTLLLLAVVPIIAVSGIVEMKLLAGNAKRDKKELEAAGKIATEAI
ENIRTVVSLTQERKFESMYVEKLYGPYRNSVQKAHIYGITFSISQAFMYFSYAGCFRFGA
YLIVNGHMRFRDVILVFSAIVFGAVALGHASSFAPDYAKAKLSAAHLFMLFERQPLIDSY
SEEGLKPDKFEGNITFNEVVFNYPTRANVPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQ
LLERFYDPLAGTVFVDFGFQLLDGQEAKKLNVQWLRAQLGIVSQEPILFDCSIAENIAYG
DNSRVVSQDEIVSAAKAANIHPFIETLPHKYETRVGDKGTQLSGGQKQRIAIARALIRQP
QILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVFQNGRVKEH
GTHQQLLAQKGIYFSMVSVQAGTQNL
|
| Enzyme 40 Number of Residues |
1286 |
| Enzyme 40 Molecular Weight |
141521.8 |
| Enzyme 40 Theoretical pI |
8.74 |
| Enzyme 40 GO Classification |
| Function |
- ATP binding
- ATPase activity
- ATPase activity, coupled to transmembrane movement of substances
- P-P-bond-hydrolysis-driven transmembrane transporter activity
- active transmembrane transporter activity
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- nucleoside binding
- nucleoside-triphosphatase activity
- nucleotide binding
- primary active transmembrane transporter activity
- purine nucleoside binding
- pyrophosphatase activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- establishment of localization
- transmembrane transport
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 40 General Function |
Involved in ATP binding |
| Enzyme 40 Specific Function |
Mediates ATP-dependent export of organic anions and drugs from the cytoplasm. Hydrolyzes ATP with low efficiency. Human MDR3 is not capable of conferring drug resistance. Mediates the translocation of phosphatidylcholine across the canalicular membrane of the hepatocyte |
| Enzyme 40 Pathways |
Not Available |
| Enzyme 40 Reactions |
- ATP + H2O + xenobioticin = ADP + phosphate + xenobioticout [RN:R00086]
|
| Enzyme 40 Pfam Domain Function |
|
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
- 51-73
119-139
189-210
218-238
297-318
333-354
712-732
756-776
832-852
854-873
934-956
973-994
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
9961250  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
P21439  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
MDR3_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>3861 bp
ATGGATCTTGAGGCGGCAAAGAACGGAACAGCCTGGCGCCCCACGAGCGCGGAGGGCGAC
TTTGAACTGGGCATCAGCAGCAAACAAAAAAGGAAAAAAACGAAGACAGTGAAAATGATT
GGAGTATTAACATTGTTTCGATACTCCGATTGGCAGGATAAATTGTTTATGTCGCTGGGT
ACCATCATGGCCATAGCTCACGGATCAGGTCTCCCCCTCATGATGATAGTATTTGGAGAG
ATGACTGACAAATTTGTTGATACTGCAGGAAACTTCTCCTTTCCAGTGAACTTTTCCTTG
TCGCTGCTAAATCCAGGCAAAATTCTGGAAGAAGAAATGACTAGATATGCATATTACTAC
TCAGGATTGGGTGCTGGAGTTCTTGTTGCTGCCTATATACAAGTTTCATTTTGGACTTTG
GCAGCTGGTCGACAGATCAGGAAAATTAGGCAGAAGTTTTTTCATGCTATTCTACGACAG
GAAATAGGATGGTTTGACATCAACGACACCACTGAACTCAATACGCGGCTAACAGATGAC
ATCTCCAAAATCAGTGAAGGAATTGGTGACAAGGTTGGAATGTTCTTTCAAGCAGTAGCC
ACGTTTTTTGCAGGATTCATAGTGGGATTCATCAGAGGATGGAAGCTCACCCTTGTGATA
ATGGCCATCAGCCCTATTCTAGGACTCTCTGCAGCCGTTTGGGCAAAGATACTCTCGGCA
TTTAGTGACAAAGAACTAGCTGCTTATGCAAAAGCAGGCGCCGTGGCAGAAGAGGCTCTG
GGGGCCATCAGGACTGTGATAGCTTTCGGGGGCCAGAACAAAGAGCTGGAAAGGTATCAG
AAACATTTAGAAAATGCCAAAGAGATTGGAATTAAAAAAGCTATTTCAGCAAACATTTCC
ATGGGTATTGCCTTCCTGTTAATATATGCATCATATGCACTGGCCTTCTGGTATGGATCC
ACTCTAGTCATATCAAAAGAATATACTATTGGAAATGCAATGACAGTTTTTTTTTCAATC
CTAATTGGAGCTTTCAGTGTTGGCCAGGCTGCCCCATGTATTGATGCTTTTGCCAATGCA
AGAGGAGCAGCATATGTGATCTTTGATATTATTGATAATAATCCTAAAATTGACAGTTTT
TCAGAGAGAGGACACAAACCAGACAGCATCAAAGGGAATTTGGAGTTCAATGATGTTCAC
TTTTCTTACCCTTCTCGAGCTAACGTCAAGATCTTGAAGGGCCTCAACCTGAAGGTGCAG
AGTGGGCAGACGGTGGCCCTGGTTGGAAGTAGTGGCTGTGGGAAGAGCACAACGGTCCAG
CTGATACAGAGGCTCTATGACCCTGATGAGGGCACAATTAACATTGATGGGCAGGATATT
AGGAACTTTAATGTAAACTATCTGAGGGAAATCATTGGTGTGGTGAGTCAGGAGCCGGTG
CTGTTTTCCACCACAATTGCTGAAAATATTTGTTATGGCCGTGGAAATGTAACCATGGAT
GAGATAAAGAAAGCTGTCAAAGAGGCCAACGCCTATGAGTTTATCATGAAATTACCACAG
AAATTTGACACCCTGGTTGGAGAGAGAGGGGCCCAGCTGAGTGGTGGGCAGAAGCAGAGG
ATCGCCATTGCACGTGCCCTGGTTCGCAACCCCAAGATCCTTCTGCTGGATGAGGCCACG
TCAGCATTGGACACAGAAAGTGAAGCTGAGGTACAGGCAGCTCTGGATAAGGCCAGAGAA
GGCCGGACCACCATTGTGATAGCACACCGACTGTCTACGGTCCGAAATGCAGATGTCATC
GCTGGGTTTGAGGATGGAGTAATTGTGGAGCAAGGAAGCCACAGCGAACTGATGAAGAAG
GAAGGGGTGTACTTCAAACTTGTCAACATGCAGACATCAGGAAGCCAGATCCAGTCAGAA
GAATTTGAACTAAATGATGAAAAGGCTGCCACTAGAATGGCCCCAAATGGCTGGAAATCT
CGCCTATTTAGGCATTCTACTCAGAAAAACCTTAAAAATTCACAAATGTGTCAGAAGAGC
CTTGATGTGGAAACCGATGGACTTGAAGCAAATGTGCCACCAGTGTCCTTTCTGAAGGTC
CTGAAACTGAATAAAACAGAATGGCCCTACTTTGTCGTGGGAACAGTATGTGCCATTGCC
AATGGGGGGCTTCAGCCGGCATTTTCAGTCATATTCTCAGAGATCATAGCGATTTTTGGA
CCAGGCGATGATGCAGTGAAGCAGCAGAAGTGCAACATATTCTCTTTGATTTTCTTATTT
CTGGGAATTATTTCTTTTTTTACTTTCTTCCTTCAGGGTTTCACGTTTGGGAAAGCTGGC
GAGATCCTCACCAGAAGACTGCGGTCAATGGCTTTTAAAGCAATGCTAAGACAGGACATG
AGCTGGTTTGATGACCATAAAAACAGTACTGGTGCACTTTCTACAAGACTTGCCACAGAT
GCTGCCCAAGTCCAAGGAGCCACAGGAACCAGGTTGGCTTTAATTGCACAGAATATAGCT
AACCTTGGAACTGGTATTATCATATCATTTATCTACGGTTGGCAGTTAACCCTATTGCTA
TTAGCAGTTGTTCCAATTATTGCTGTGTCAGGAATTGTTGAAATGAAATTGTTGGCTGGA
AATGCCAAAAGAGATAAAAAAGAACTGGAAGCTGCTGGAAAGATTGCAACAGAGGCAATA
GAAAATATTAGGACAGTTGTGTCTTTGACCCAGGAAAGAAAATTTGAATCAATGTATGTT
GAAAAATTGTATGGACCTTACAGGAATTCTGTGCAGAAGGCACACATCTATGGAATTACT
TTTAGTATCTCACAAGCATTTATGTATTTTTCCTATGCCGGTTGTTTTCGATTTGGTGCA
TATCTCATTGTGAATGGACATATGCGCTTCAGAGATGTTATTCTGGTGTTTTCTGCAATT
GTATTTGGTGCAGTGGCTCTAGGACATGCCAGTTCATTTGCTCCAGACTATGCTAAAGCT
AAGCTGTCTGCAGCCCACTTATTCATGCTGTTTGAAAGACAACCTCTGATTGACAGCTAC
AGTGAAGAGGGGCTGAAGCCTGATAAATTTGAAGGAAATATAACATTTAATGAAGTCGTG
TTCAACTATCCCACCCGAGCAAACGTGCCAGTGCTTCAGGGGCTGAGCCTGGAGGTGAAG
AAAGGCCAGACACTAGCCCTGGTGGGCAGCAGTGGCTGTGGGAAGAGCACGGTGGTCCAG
CTCCTGGAGCGGTTCTACGACCCCTTGGCGGGGACAGTGTTTGTGGACTTTGGTTTTCAG
CTTCTCGATGGTCAAGAAGCAAAGAAACTCAATGTCCAGTGGCTCAGAGCTCAACTCGGA
ATCGTGTCTCAGGAGCCTATCCTATTTGACTGCAGCATTGCCGAGAATATTGCCTATGGA
GACAACAGCCGGGTTGTATCACAGGATGAAATTGTGAGTGCAGCCAAAGCTGCCAACATA
CATCCTTTCATCGAGACGTTACCCCACAAATATGAAACAAGAGTGGGAGATAAGGGGACT
CAGCTCTCAGGAGGTCAAAAACAGAGGATTGCTATTGCCCGAGCCCTCATCAGACAACCT
CAAATCCTCCTGTTGGATGAAGCTACATCAGCTCTGGATACTGAAAGTGAAAAGGTTGTC
CAAGAAGCCCTGGACAAAGCCAGAGAAGGCCGCACCTGCATTGTGATTGCTCACCGCCTG
TCCACCATCCAGAATGCAGACTTAATAGTGGTGTTTCAGAATGGGAGAGTCAAGGAGCAT
GGCACGCATCAGCAGCTGCTGGCACAGAAAGGCATCTATTTTTCAATGGTCAGTGTCCAG
GCTGGGACACAGAACTTATGA
|
| Enzyme 40 GenBank Gene ID |
NM_018849.2  |
| Enzyme 40 GeneCard ID |
ABCB4  |
| Enzyme 40 GenAtlas ID |
ABCB4  |
| Enzyme 40 HGNC ID |
HGNC:45  |
| Enzyme 40 Chromosome Location |
7 |
| Enzyme 40 Locus |
7q21.1 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- van der Bliek AM, Kooiman PM, Schneider C, Borst P: Sequence of mdr3 cDNA encoding a human P-glycoprotein. Gene. 1988 Nov 30;71(2):401-11. [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
]
- Smit JJ, Mol CA, van Deemter L, Wagenaar E, Schinkel AH, Borst P: Characterization of the promoter region of the human MDR3 P-glycoprotein gene. Biochim Biophys Acta. 1995 Mar 14;1261(1):44-56. [PubMed
]
- Van der Bliek AM, Baas F, Ten Houte de Lange T, Kooiman PM, Van der Velde-Koerts T, Borst P: The human mdr3 gene encodes a novel P-glycoprotein homologue and gives rise to alternatively spliced mRNAs in liver. EMBO J. 1987 Nov;6(11):3325-31. [PubMed
]
- Lincke CR, Smit JJ, van der Velde-Koerts T, Borst P: Structure of the human MDR3 gene and physical mapping of the human MDR locus. J Biol Chem. 1991 Mar 15;266(8):5303-10. [PubMed
]
- de Vree JM, Jacquemin E, Sturm E, Cresteil D, Bosma PJ, Aten J, Deleuze JF, Desrochers M, Burdelski M, Bernard O, Oude Elferink RP, Hadchouel M: Mutations in the MDR3 gene cause progressive familial intrahepatic cholestasis. Proc Natl Acad Sci U S A. 1998 Jan 6;95(1):282-7. [PubMed
]
- Dixon PH, Weerasekera N, Linton KJ, Donaldson O, Chambers J, Egginton E, Weaver J, Nelson-Piercy C, de Swiet M, Warnes G, Elias E, Higgins CF, Johnston DG, McCarthy MI, Williamson C: Heterozygous MDR3 missense mutation associated with intrahepatic cholestasis of pregnancy: evidence for a defect in protein trafficking. Hum Mol Genet. 2000 May 1;9(8):1209-17. [PubMed
]
- Jacquemin E, De Vree JM, Cresteil D, Sokal EM, Sturm E, Dumont M, Scheffer GL, Paul M, Burdelski M, Bosma PJ, Bernard O, Hadchouel M, Elferink RP: The wide spectrum of multidrug resistance 3 deficiency: from neonatal cholestasis to cirrhosis of adulthood. Gastroenterology. 2001 May;120(6):1448-58. [PubMed
]
- Rosmorduc O, Hermelin B, Poupon R: MDR3 gene defect in adults with symptomatic intrahepatic and gallbladder cholesterol cholelithiasis. Gastroenterology. 2001 May;120(6):1459-67. [PubMed
]
- Lucena JF, Herrero JI, Quiroga J, Sangro B, Garcia-Foncillas J, Zabalegui N, Sola J, Herraiz M, Medina JF, Prieto J: A multidrug resistance 3 gene mutation causing cholelithiasis, cholestasis of pregnancy, and adulthood biliary cirrhosis. Gastroenterology. 2003 Apr;124(4):1037-42. [PubMed
]
- Rosmorduc O, Hermelin B, Boelle PY, Parc R, Taboury J, Poupon R: ABCB4 gene mutation-associated cholelithiasis in adults. Gastroenterology. 2003 Aug;125(2):452-9. [PubMed
]
- Mullenbach R, Linton KJ, Wiltshire S, Weerasekera N, Chambers J, Elias E, Higgins CF, Johnston DG, McCarthy MI, Williamson C: ABCB4 gene sequence variation in women with intrahepatic cholestasis of pregnancy. J Med Genet. 2003 May;40(5):e70. [PubMed
]
- Pauli-Magnus C, Lang T, Meier Y, Zodan-Marin T, Jung D, Breymann C, Zimmermann R, Kenngott S, Beuers U, Reichel C, Kerb R, Penger A, Meier PJ, Kullak-Ublick GA: Sequence analysis of bile salt export pump (ABCB11) and multidrug resistance p-glycoprotein 3 (ABCB4, MDR3) in patients with intrahepatic cholestasis of pregnancy. Pharmacogenetics. 2004 Feb;14(2):91-102. [PubMed
]
- Lang T, Haberl M, Jung D, Drescher A, Schlagenhaufer R, Keil A, Mornhinweg E, Stieger B, Kullak-Ublick GA, Kerb R: Genetic variability, haplotype structures, and ethnic diversity of hepatic transporters MDR3 (ABCB4) and bile salt export pump (ABCB11). Drug Metab Dispos. 2006 Sep;34(9):1582-99. Epub 2006 Jun 8. [PubMed
]
- Lang C, Meier Y, Stieger B, Beuers U, Lang T, Kerb R, Kullak-Ublick GA, Meier PJ, Pauli-Magnus C: Mutations and polymorphisms in the bile salt export pump and the multidrug resistance protein 3 associated with drug-induced liver injury. Pharmacogenet Genomics. 2007 Jan;17(1):47-60. [PubMed
]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
7319 |
| Enzyme 41 Name |
Lecithin retinol acyltransferase |
| Enzyme 41 Synonyms |
- Phosphatidylcholine--retinol O-acyltransferase
|
| Enzyme 41 Gene Name |
LRAT |
| Enzyme 41 Protein Sequence |
>Lecithin retinol acyltransferase
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTH
YGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGA
NILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDK
FCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
|
| Enzyme 41 Number of Residues |
230 |
| Enzyme 41 Molecular Weight |
25702.6 |
| Enzyme 41 Theoretical pI |
7.54 |
| Enzyme 41 GO Classification |
Not Available |
| Enzyme 41 General Function |
Involved in phosphatidylcholine-retinol O-acyltransfera |
| Enzyme 41 Specific Function |
Transfers the acyl group from the sn-1 position of phosphatidylcholine to all-trans retinol, producing all-trans retinyl esters. Retinyl esters are storage forms of vitamin A. LRAT plays a critical role in vision. It provides the all-trans retinyl ester substrates for the isomerohydrolase which processes the esters into 11-cis-retinol in the retinal pigment epithelium; due to a membrane-associated alcohol dehydrogenase, 11 cis-retinol is oxidized and converted into 11-cis-retinaldehyde which is the chromophore for rhodopsin and the cone photopigments |
| Enzyme 41 Pathways |
Not Available |
| Enzyme 41 Reactions |
- phosphatidylcholine + retinol---[cellular-retinol-binding-protein] = 2-acylglycerophosphocholine + retinyl-ester---[cellular-retinol-binding-protein] [RN:R04514]
|
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
4240391  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
O95237  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
LRAT_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>693 bp
ATGAAGAACCCCATGCTGGAGGTGGTGTCTTTACTACTGGAGAAGCTGCTCCTCATCTCC
AACTTCACGCTCTTTAGTTCGGGCGCCGCGGGCAAGGACAAAGGGAGGAACAGTTTTTAT
GAAACCAGCTCTTTCCACCGAGGCGACGTGCTGGAGGTGCCCCGGACCCACCTGACCCAC
TATGGCATCTACCTAGGAGACAACCGTGTTGCCCACATGATGCCCGACATCCTGTTGGCC
CTGACAGACGACATGGGGCGCACGCAGAAGGTGGTCTCCAACAAGCGTCTCATCCTGGGC
GTTATTGTCAAAGTGGCCAGCATCCGCGTGGACACAGTGGAGGACTTCGCCTACGGAGCT
AACATCCTGGTCAATCACCTGGACGAGTCCCTCCAGAAAAAGGCACTGCTCAACGAGGAG
GTGGCGCGGAGGGCTGAAAAGCTGCTGGGCTTTACCCCCTACAGCCTGCTGTGGAACAAC
TGCGAGCACTTCGTGACCTACTGCAGATATGGCACCCCGATCAGTCCCCAGTCCGACAAG
TTTTGTGAGACTGTGAAGATAATTATTCGTGATCAGAGAAGTGTTCTTGCTTCAGCAGTC
TTGGGATTGGCGTCTATAGTCTGTACGGGCTTGGTATCATACACTACCCTTCCTGCAATT
TTTATTCCATTCTTCCTATGGATGGCTGGCTAA
|
| Enzyme 41 GenBank Gene ID |
AF071510  |
| Enzyme 41 GeneCard ID |
LRAT  |
| Enzyme 41 GenAtlas ID |
LRAT  |
| Enzyme 41 HGNC ID |
HGNC:6685  |
| Enzyme 41 Chromosome Location |
4 |
| Enzyme 41 Locus |
4q32.1 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Ruiz A, Winston A, Lim YH, Gilbert BA, Rando RR, Bok D: Molecular and biochemical characterization of lecithin retinol acyltransferase. J Biol Chem. 1999 Feb 5;274(6):3834-41. [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
]
- Mondal MS, Ruiz A, Bok D, Rando RR: Lecithin retinol acyltransferase contains cysteine residues essential for catalysis. Biochemistry. 2000 May 2;39(17):5215-20. [PubMed
]
- den Hollander AI, Lopez I, Yzer S, Zonneveld MN, Janssen IM, Strom TM, Hehir-Kwa JY, Veltman JA, Arends ML, Meitinger T, Musarella MA, van den Born LI, Fishman GA, Maumenee IH, Rohrschneider K, Cremers FP, Koenekoop RK: Identification of novel mutations in patients with Leber congenital amaurosis and juvenile RP by genome-wide homozygosity mapping with SNP microarrays. Invest Ophthalmol Vis Sci. 2007 Dec;48(12):5690-8. [PubMed
]
- Nagatsuma K, Hayashi Y, Hano H, Sagara H, Murakami K, Saito M, Masaki T, Lu T, Tanaka M, Enzan H, Aizawa Y, Tajiri H, Matsuura T: Lecithin: retinol acyltransferase protein is distributed in both hepatic stellate cells and endothelial cells of normal rodent and human liver. Liver Int. 2009 Jan;29(1):47-54. Epub 2008 Jun 9. [PubMed
]
- Thompson DA, Li Y, McHenry CL, Carlson TJ, Ding X, Sieving PA, Apfelstedt-Sylla E, Gal A: Mutations in the gene encoding lecithin retinol acyltransferase are associated with early-onset severe retinal dystrophy. Nat Genet. 2001 Jun;28(2):123-4. [PubMed
]
- Senechal A, Humbert G, Surget MO, Bazalgette C, Bazalgette C, Arnaud B, Arndt C, Laurent E, Brabet P, Hamel CP: Screening genes of the retinoid metabolism: novel LRAT mutation in leber congenital amaurosis. Am J Ophthalmol. 2006 Oct;142(4):702-4. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
7395 |
| Enzyme 42 Name |
Phospholipid scramblase 1 |
| Enzyme 42 Synonyms |
- PL scramblase 1
- Ca(2+)-dependent phospholipid scramblase 1
- Erythrocyte phospholipid scramblase
- MmTRA1b
|
| Enzyme 42 Gene Name |
PLSCR1 |
| Enzyme 42 Protein Sequence |
>Phospholipid scramblase 1
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAG
FPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVL
TGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLR
CSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLI
DFMFFESTGSQEQKSGVW
|
| Enzyme 42 Number of Residues |
318 |
| Enzyme 42 Molecular Weight |
35048.8 |
| Enzyme 42 Theoretical pI |
4.57 |
| Enzyme 42 GO Classification |
Not Available |
| Enzyme 42 General Function |
Involved in calcium ion binding |
| Enzyme 42 Specific Function |
May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation |
| Enzyme 42 Pathways |
Not Available |
| Enzyme 42 Reactions |
Not Available |
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
3510297  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
O15162  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
PLS1_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>957 bp
ATGGACAAACAAAACTCACAGATGAATGCTTCTCACCCGGAAACAAACTTGCCAGTTGGG
TATCCTCCTCAGTATCCACCGACAGCATTCCAAGGACCTCCAGGATATAGTGGCTACCCT
GGGCCCCAGGTCAGCTACCCACCCCCACCAGCCGGCCATTCAGGTCCTGGCCCAGCTGGC
TTTCCTGTCCCAAATCAGCCAGTGTATAATCAGCCAGTATATAATCAGCCAGTTGGAGCT
GCAGGGGTACCATGGATGCCAGCGCCACAGCCTCCATTAAACTGTCCACCTGGATTAGAA
TATTTAAGTCAGATAGATCAGATACTGATTCATCAGCAAATTGAACTTCTGGAAGTTTTA
ACAGGTTTTGAAACTAATAACAAATATGAAATTAAGAACAGCTTTGGACAGAGGGTTTAC
TTTGCAGCGGAAGATACTGATTGCTGTACCCGAAATTGCTGTGGGCCATCTAGACCTTTT
ACCTTGAGGATTATTGATAATATGGGTCAAGAAGTCATAACTCTGGAGAGACCACTAAGA
TGTAGCAGCTGTTGTTGTCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGT
GTACCAATAGGTTATGTTATTCAGACTTGGCACCCATGTCTACCAAAGTTTACAATTCAA
AATGAGAAAAGAGAGGATGTACTAAAAATAAGTGGTCCATGTGTTGTGTGCAGCTGTTGT
GGAGATGTTGATTTTGAGATTAAATCTCTTGATGAACAGTGTGTGGTTGGCAAAATTTCC
AAGCACTGGACTGGAATTTTGAGAGAGGCATTTACAGACGCTGATAACTTTGGAATCCAG
TTCCCTTTAGACCTTGATGTTAAAATGAAAGCTGTAATGATTGGTGCCTGTTTCCTCATT
GACTTCATGTTTTTTGAAAGCACTGGCAGCCAGGAACAAAAATCAGGAGTGTGGTAG
|
| Enzyme 42 GenBank Gene ID |
AB006746  |
| Enzyme 42 GeneCard ID |
PLSCR1  |
| Enzyme 42 GenAtlas ID |
PLSCR1  |
| Enzyme 42 HGNC ID |
HGNC:9092  |
| Enzyme 42 Chromosome Location |
3 |
| Enzyme 42 Locus |
3q23 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Zhou Q, Zhao J, Stout JG, Luhm RA, Wiedmer T, Sims PJ: Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids. J Biol Chem. 1997 Jul 18;272(29):18240-4. [PubMed
]
- Kasukabe T, Kobayashi H, Kaneko Y, Okabe-Kado J, Honma Y: Identity of human normal counterpart (MmTRA1b) of mouse leukemogenesis-associated gene (MmTRA1a) product as plasma membrane phospholipid scramblase and chromosome mapping of the human MmTRA1b/phospholipid scramblase gene. Biochem Biophys Res Commun. 1998 Aug 19;249(2):449-55. [PubMed
]
- Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [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
]
- 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
]
- Basse F, Stout JG, Sims PJ, Wiedmer T: Isolation of an erythrocyte membrane protein that mediates Ca2+-dependent transbilayer movement of phospholipid. J Biol Chem. 1996 Jul 19;271(29):17205-10. [PubMed
]
- Frasch SC, Henson PM, Kailey JM, Richter DA, Janes MS, Fadok VA, Bratton DL: Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta. J Biol Chem. 2000 Jul 28;275(30):23065-73. [PubMed
]
- Sun J, Zhao J, Schwartz MA, Wang JY, Wiedmer T, Sims PJ: c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1. J Biol Chem. 2001 Aug 3;276(31):28984-90. Epub 2001 Jun 4. [PubMed
]
- Zhao J, Zhou Q, Wiedmer T, Sims PJ: Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids. Biochemistry. 1998 May 5;37(18):6361-6. [PubMed
]
- Zhou Q, Sims PJ, Wiedmer T: Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids. Biochemistry. 1998 Feb 24;37(8):2356-60. [PubMed
]
- Dong B, Zhou Q, Zhao J, Zhou A, Harty RN, Bose S, Banerjee A, Slee R, Guenther J, Williams BR, Wiedmer T, Sims PJ, Silverman RH: Phospholipid scramblase 1 potentiates the antiviral activity of interferon. J Virol. 2004 Sep;78(17):8983-93. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
7675 |
| Enzyme 43 Name |
Phosphatidylserine synthase 1 |
| Enzyme 43 Synonyms |
- PSS-1
- PtdSer synthase 1
- Serine-exchange enzyme I
|
| Enzyme 43 Gene Name |
PTDSS1 |
| Enzyme 43 Protein Sequence |
>Phosphatidylserine synthase 1
MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTR
DDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLF
LNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKA
LLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFL
EMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLT
ELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVI
GFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECE
DGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK
|
| Enzyme 43 Number of Residues |
473 |
| Enzyme 43 Molecular Weight |
55527.2 |
| Enzyme 43 Theoretical pI |
8.52 |
| Enzyme 43 GO Classification |
| Function |
| — |
| Process |
- glycerophospholipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylserine biosynthetic process
- phosphatidylserine metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 43 General Function |
Involved in phosphatidylserine biosynthetic process |
| Enzyme 43 Specific Function |
Catalyzes a base-exchange reaction in which the polar head group of phosphatidylcholine is replaced by L-serine |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
Not Available |
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
- 36-56
73-93
103-123
161-181
187-207
217-237
287-307
310-330
356-376
384-404
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
Not Available |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
P48651  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
PTSS1_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>1422 bp
ATGGCGTCCTGCGTGGGGAGCCGGACCCTAAGCAAGGATGATGTGAACTACAAAATGCAT
TTCCGGATGATCAACGAGCAGCAAGTGGAGGACATCACCATTGACTTCTTCTACCGGCCG
CATACCATCACCCTGCTCAGCTTCACCATCGTCAGCCTCATGTACTTCGCCTTTACCAGG
GATGACTCTGTTCCAGAAGACAACATCTGGAGAGGCATCCTCTCTGTTATTTTCTTCTTT
CTTATCATCAGTGTGTTAGCTTTCCCCAATGGTCCGTTCACTCGACCTCATCCAGCCTTA
TGGCGAATGGTTTTTGGACTCAGTGTGCTCTACTTCCTGTTCCTGGTATTCCTACTCTTC
CTGAATTTCGAGCAGGTTAAATCTCTAATGTATTGGCTAGATCCAAATCTTCGATACGCC
ACAAGGGAAGCAGATGTCATGGAGTATGCTGTGAACTGCCATGTGATCACCTGGGAGAGG
ATTATCAGCCACTTTGATATTTTTGCATTTGGACATTTCTGGGGCTGGGCCATGAAGGCC
TTGCTGATCCGTAGTTACGGTCTCTGCTGGACAATCAGTATTACCTGGGAGCTGACTGAG
CTCTTCTTCATGCATCTCCTCCCCAATTTTGCCGAGTGCTGGTGGGATCAAGTCATTCTG
GACATCCTGTTGTGCAATGGCGGTGGCATTTGGCTGGGCATGGTCGTTTGCCGGTTTTTA
GAGATGAGGACTTACCACTGGGCAAGCTTCAAGGACATTCATACCACCACCGGGAAGATC
AAGAGAGCTGTTCTGCAGTTCACTCCTGCTAGCTGGACCTATGTTCGATGGTTTGACCCC
AAATCTTCTTTTCAGAGAGTAGCTGGAGTGTACCTTTTCATGATCATCTGGCAGCTGACT
GAGTTGAATACCTTCTTCTTGAAGCATATCTTTGTGTTCCAAGCCAGTCATCCATTAAGT
TGGGGTAGAATTCTCTTTATTGGTGGCATCACAGCTCCCACAGTGAGACAGTACTACGCT
TACCTCACCGACACACAGTGCAAGCGCGTAGGAACACAATGCTGGGTGTTTGGGGTCATT
GGTTTCCTGGAGGCCATTGTTTGCATAAAATTTGGACAAGATCTCTTCTCTAAGACCCAA
ATACTCTATGTTGTGCTTTGGCTTCTTTGCGTGGCTTTCACCACTTTCCTCTGTCTGTAC
GGCATGATTTGGTATGCAGAACACTATGGTCACCGAGAAAAGACCTACTCGGAGTGTGAA
GATGGCACCTACAGTCCAGAGATCTCCTGGCATCACAGGAAAGGGACAAAAGGTTCTGAA
GACAGCCCACCCAAGCATGCAGGCAACAACGAAAGCCATTCTTCCAGGAGAAGGAATCGG
CATTCCAAGTCAAAAGTCACCAATGGCGTTGGAAAGAAATGA
|
| Enzyme 43 GenBank Gene ID |
D14694  |
| Enzyme 43 GeneCard ID |
PTDSS1  |
| Enzyme 43 GenAtlas ID |
PTDSS1  |
| Enzyme 43 HGNC ID |
HGNC:9587  |
| Enzyme 43 Chromosome Location |
8 |
| Enzyme 43 Locus |
8q22 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [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
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [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
]
- 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
]
- 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
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
8021 |
| Enzyme 44 Name |
Phosphatidylinositol transfer protein alpha isoform |
| Enzyme 44 Synonyms |
- PI-TP-alpha
- PtdIns transfer protein alpha
- PtdInsTP alpha
|
| Enzyme 44 Gene Name |
PITPNA |
| Enzyme 44 Protein Sequence |
>Phosphatidylinositol transfer protein alpha isoform
MVLLKEYRVILPVSVDEYQVGQLYSVAEASKNETGGGEGVEVLVNEPYEKDGEKGQYTHK
IYHLQSKVPTFVRMLAPEGALNIHEKAWNAYPYCRTVITNEYMKEDFLIKIETWHKPDLG
TQENVHKLEPEAWKHVEAVYIDIADRSQVLSKDYKAEEDPAKFKSIKTGRGPLGPNWKQE
LVNQKDCPYMCAYKLVTVKFKWWGLQNKVENFIHKQERRLFTNFHRQLFCWLDKWVDLTM
DDIRRMEEETKRQLDEMRQKDPVKGMTADD
|
| Enzyme 44 Number of Residues |
270 |
| Enzyme 44 Molecular Weight |
31806.2 |
| Enzyme 44 Theoretical pI |
6.52 |
| Enzyme 44 GO Classification |
| Function |
| — |
| Process |
- establishment of localization
- transport
|
| Component |
|
|
| Enzyme 44 General Function |
Involved in phosphatidylcholine transmembrane transport |
| Enzyme 44 Specific Function |
Catalyzes the transfer of PtdIns and phosphatidylcholine between membranes |
| Enzyme 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
Not Available |
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
28175608  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
Q00169  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
PIPNA_HUMAN  |
| Enzyme 44 PDB ID |
1T27  |
| Enzyme 44 PDB File |
Show |
| Enzyme 44 3D Structure |
|
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>813 bp
ATGGTGCTGCTCAAGGAGTATCGAGTAATCCTGCCTGTGTCTGTAGATGAGTATCAAGTG
GGGCAGCTGTATTCTGTGGCTGAGGCCAGTAAAAATGAAACGGGTGGTGGCGAAGGCGTG
GAGGTCCTGGTGAATGAGCCCTACGAGAAGGACGGTGAGAAAGGCCAGTACACACATAAG
ATCTACCACCTGCAGAGCAAAGTACCCACGTTTGTTCGAATGCTGGCCCCAGAGGGAGCC
CTGAATATACACGAGAAAGCCTGGAATGCTTACCCCTACTGCAGAACCGTTATTACAAAT
GAGTACATGAAAGAAGACTTTCTGATTAAAATTGAAACCTGGCACAAACCAGATCTTGGC
ACGCAGGAGAATGTGCATAAGCTGGAGCCTGAGGCGTGGAAACACGTGGAAGCCGTATAT
ATAGACATTGCAGATCGAAGCCAAGTGCTCAGCAAGGATTACAAGGCAGAGGAAGACCCA
GCAAAATTTAAATCTATCAAAACAGGCCGAGGACCCTTGGGCCCCAATTGGAAGCAAGAG
CTTGTAAACCAGAAGGACTGCCCATATATGTGTGCATACAAACTGGTGACCGTCAAGTTC
AAGTGGTGGGGCCTGCAGAACAAAGTGGAGAACTTCATCCATAAGCAAGAGAGGCGTCTG
TTTACAAACTTCCACAGGCAGCTGTTCTGTTGGCTCGATAAGTGGGTTGACCTGACCATG
GACGACATTCGAAGGATGGAAGAAGAGACGAAGAGACAGCTGGATGAAATGAGACAAAAG
GACCCAGTGAAAGGAATGACAGCAGATGACTAA
|
| Enzyme 44 GenBank Gene ID |
BC045108  |
| Enzyme 44 GeneCard ID |
PITPNA  |
| Enzyme 44 GenAtlas ID |
Not Available |
| Enzyme 44 HGNC ID |
Not Available |
| Enzyme 44 Chromosome Location |
1 |
| Enzyme 44 Locus |
17p13.3 |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
- Dickeson SK, Helmkamp GM Jr, Yarbrough LR: Sequence of a human cDNA encoding phosphatidylinositol transfer protein and occurrence of a related sequence in widely divergent eukaryotes. Gene. 1994 May 16;142(2):301-5. [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
]
- 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
]
- 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 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
8048 |
| Enzyme 45 Name |
Phospholipid transfer protein |
| Enzyme 45 Synonyms |
- Lipid transfer protein II
|
| Enzyme 45 Gene Name |
PLTP |
| Enzyme 45 Protein Sequence |
>Phospholipid transfer protein
MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGH
FYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASA
EGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLL
NQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFP
LTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLD
MLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQP
EVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQI
GVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADV
RASTAPTPSTAAV
|
| Enzyme 45 Number of Residues |
493 |
| Enzyme 45 Molecular Weight |
54738.8 |
| Enzyme 45 Theoretical pI |
7.01 |
| Enzyme 45 GO Classification |
| Function |
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 45 General Function |
Involved in lipid binding |
| Enzyme 45 Specific Function |
Converts HDL into larger and smaller particles. May play a key role in extracellular phospholipid transport and modulation of hdl particles |
| Enzyme 45 Pathways |
Not Available |
| Enzyme 45 Reactions |
Not Available |
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
18143452  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
P55058  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
PLTP_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>1482 bp
ATGGCCCTCTTCGGGGCCCTCTTCCTAGCGCTGCTGGCAGGCGCACATGCAGAGTTCCCA
GGCTGCAAGATCCGCGTCACCTCCAAGGCGCTGGAGCTGGTGAAGCAGGAGGGGCTGCGC
TTTCTGGAGCAAGAGCTGGAGACTATCACCATTCCGGACCTGCGGGGCAAAGAAGGCCAC
TTCTACTACAACATCTCTGAGGTGAAGGTCACAGAGCTGCAACTGACATCTTCCGAGCTC
GATTTCCAGCCACAGCAGGAGCTGATGCTTCAAATCACCAATGCCTCCTTGGGGCTGCGC
TTCCGGAGACAGCTGCTCTACTGGTTCTTCTATGATGGGGGCTACATCAACGCCTCAGCT
GAGGGTGTGTCCATCCGCACTGGTCTGGAGCTCTCCCGGGATCCCGCTGGACGGATGAAA
GTGTCCAATGTCTCCTGCCAGGCCTCTGTCTCCAGAATGCACGCGGCCTTCGGGGGAACC
TTCAAGAAGGTGTATGATTTTCTCTCCACGTTCATCACCTCAGGGATGCGCTTCCTCCTC
AACCAGCAGATCTGCCCTGTCCTCTACCACGCAGGGACGGTCCTGCTCAACTCCCTCCTG
GACACCGTGCCTGTGCGCAGTTCTGTGGACGAGCTTGTTGGCATTGACTATTCCCTCATG
AAGGATCCTGTGGCTTCCACCAGCAACCTGGACATGGACTTCCGGGGGGCCTTCTTCCCC
CTGACTGAGAGGAACTGGAGCCTCCCCAACCGGGCAGTGGAGCCCCAGCTGCAGGAGGAA
GAGCGGATGGTGTATGTGGCCTTCTCTGAGTTCTTCTTCGACTCTGCCATGGAGAGCTAC
TTCCGGGCGGGGGCCCTGCAGCTGTTGCTGGTGGGGGACAAGGTGCCCCACGACCTGGAC
ATGCTGCTGAGGGCCACCTACTTTGGGAGCATTGTCCTGCTGAGCCCAGCAGTGATTGAC
TCCCCATTGAAGCTGGAGCTGCGGGTCCTGGCCCCACCGCGCTGCACCATCAAGCCCTCT
GGCACCACCATCTCTGTCACTGCTAGCGTCACCATTGCCCTGGTCCCACCAGACCAGCCT
GAGGTCCAGCTGTCCAGCATGACTATGGACGCCCGTCTCAGCGCCAAGATGGCTCTCCGG
GGGAAGGCCCTGCGCACGCAGCTGGACCTGCGCAGGTTCCGAATCTATTCCAACCATTCT
GCACTGGAGTCGCTGGCTCTGATCCCATTACAGGCCCCTCTGAAGACCATGCTGCAGATT
GGGGTGATGCCCATGCTCAATGAGCGGACCTGGCGTGGGGTGCAGATCCCACTACCTGAG
GGCATCAACTTTGTGCATGAGGTGGTGACGAACCATGCGGGATTCCTCACCATCGGGGCT
GATCTCCACTTTGCCAAAGGGCTGCGAGAGGTGATTGAGAAGAACCGGCCTGCTGATGTC
AGGGCGTCCACTGCCCCCACACCGTCCACAGCAGCTGTCTGA
|
| Enzyme 45 GenBank Gene ID |
AB076694  |
| Enzyme 45 GeneCard ID |
PLTP  |
| Enzyme 45 GenAtlas ID |
PLTP  |
| Enzyme 45 HGNC ID |
HGNC:9093  |
| Enzyme 45 Chromosome Location |
2 |
| Enzyme 45 Locus |
20q13.12 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
- Day JR, Albers JJ, Lofton-Day CE, Gilbert TL, Ching AF, Grant FJ, O'Hara PJ, Marcovina SM, Adolphson JL: Complete cDNA encoding human phospholipid transfer protein from human endothelial cells. J Biol Chem. 1994 Mar 25;269(12):9388-91. [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, 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
]
- Qu SJ, Fan HZ, Kilinc C, Pownall HJ: Role of cysteine residues in human plasma phospholipid transfer protein. J Protein Chem. 1999 Feb;18(2):193-8. [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
]
- 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
]
- 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
]
- 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 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
8362 |
| Enzyme 46 Name |
Cholinephosphotransferase 1 |
| Enzyme 46 Synonyms |
- hCPT1
- AAPT1-like protein
- Diacylglycerol cholinephosphotransferase 1
|
| Enzyme 46 Gene Name |
CHPT1 |
| Enzyme 46 Protein Sequence |
>Cholinephosphotransferase 1
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
|
| Enzyme 46 Number of Residues |
406 |
| Enzyme 46 Molecular Weight |
45096.5 |
| Enzyme 46 Theoretical pI |
6.92 |
| Enzyme 46 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, for other substituted phosphate groups
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
|
|
| Enzyme 46 General Function |
Involved in phosphotransferase activity, for other substituted phosphate groups |
| Enzyme 46 Specific Function |
Catalyzes phosphatidylcholine biosynthesis from CDP- choline. It thereby plays a central role in the formation and maintenance of vesicular membranes |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
- CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine [RN:R01321]
|
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
- 66-86
93-113
153-173
193-213
226-248
261-281
295-315
349-369
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
50726996  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
Q8WUD6  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
CHPT1_HUMAN  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>1221 bp
ATGGCGGCAGGCGCCGGGGCCGGGTCCGCGCCGCGCTGGCTGAGGGCGCTGAGCGAGCCG
CTGAGCGCGGCGCAGCTGCGGCGACTGGAGGAGCACCGCTACAGCGCGGCGGGCGTCTCG
CTGCTCGAGCCGCCGCTGCAGCTCTACTGGACCTGGCTGCTCCAGTGGATCCCGCTCTGG
ATGGCCCCCAACTCCATCACCCTGCTGGGGCTCGCCGTCAACGTGGTCACCACGCTCGTG
CTCATCTCCTACTGTCCCACGGCCACCGAAGAGGCACCATACTGGACATACCTTTTATGT
GCACTGGGACTTTTTATTTACCAGTCACTGGATGCTATTGATGGGAAACAAGCCAGAAGA
ACAAACTCTTGTTCCCCTTTAGGGGAGCTCTTTGACCATGGCTGTGACTCTCTTTCCACA
GTATTTATGGCAGTGGGAGCTTCAATTGCCGCTCGCTTAGGAACTTATCCTGACTGGTTT
TTTTTCTGCTCTTTTATTGGGATGTTTGTGTTTTATTGCGCTCATTGGCAGACTTATGTT
TCAGGCATGTTGAGATTTGGAAAAGTGGATGTAACTGAAATTCAGATAGCTTTAGTGATT
GTCTTTGTGTTGTCTGCATTTGGAGGAGCAACAATGTGGGACTATACGATTCCTATTCTA
GAAATAAAATTGAAGATCCTTCCAGTTCTTGGATTTCTAGGTGGAGTAATATTTTCCTGT
TCAAATTATTTCCATGTTATCCTCCATGGTGGTGTTGGCAAGAATGGATCCACTATAGCA
GGCACCAGTGTCTTGTCACCTGGACTCCACATAGGACTAATTATTATACTGGCAATAATG
ATCTATAAAAAGTCAGCAACTGATGTGTTTGAAAAGCATCCTTGTCTTTATATCCTAATG
TTTGGATGTGTCTTTGCTAAAGTCTCACAAAAATTAGTGGTAGCTCACATGACCAAAAGT
GAACTATATCTTCAAGACACTGTCTTTTTGGGGCCAGGTCTTTTGTTTTTAGACCAGTAC
TTTAATAACTTTATAGACGAATATGTTGTTCTATGGATGGCAATGGTGATTTCTTCATTT
GATATGGTGATATACTTTAGTGCTTTGTGCCTGCAAATTTCAAGACACCTTCATCTAAAT
ATATTCAAGACTGCATGTCATCAAGCACCTGAACAGGTTCAAGTTCTTTCTTCAAAGAGT
CATCAGAATAACATGGATTGA
|
| Enzyme 46 GenBank Gene ID |
NM_020244.2  |
| Enzyme 46 GeneCard ID |
CHPT1  |
| Enzyme 46 GenAtlas ID |
CHPT1  |
| Enzyme 46 HGNC ID |
HGNC:17852  |
| Enzyme 46 Chromosome Location |
1 |
| Enzyme 46 Locus |
12q |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- Henneberry AL, Wistow G, McMaster CR: Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. [PubMed
]
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [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
]
- Sinha Roy S, Mukherjee S, Kabir S, Rajaratnam V, Smith M, Das SK: Inhibition of cholinephosphotransferase activity in lung injury induced by 2-chloroethyl ethyl sulfide, a mustard analog. J Biochem Mol Toxicol. 2005;19(5):289-97. [PubMed
]
- Ghosh A, Akech J, Mukherjee S, Das SK: Differential expression of cholinephosphotransferase in normal and cancerous human mammary epithelial cells. Biochem Biophys Res Commun. 2002 Oct 4;297(4):1043-8. [PubMed
]
- Henneberry AL, Wright MM, McMaster CR: The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity. Mol Biol Cell. 2002 Sep;13(9):3148-61. [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 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
8626 |
| Enzyme 47 Name |
2-acylglycerol O-acyltransferase 2 |
| Enzyme 47 Synonyms |
- Acyl-CoA:monoacylglycerol acyltransferase 2
- MGAT2
- hMGAT2
- Diacylglycerol O-acyltransferase candidate 5
- hDC5
- Diacylglycerol acyltransferase 2-like protein 5
- Monoacylglycerol O-acyltransferase 2
|
| Enzyme 47 Gene Name |
MOGAT2 |
| Enzyme 47 Protein Sequence |
>2-acylglycerol O-acyltransferase 2
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLD
RDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN
LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNL
LGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEE
VNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
|
| Enzyme 47 Number of Residues |
334 |
| Enzyme 47 Molecular Weight |
38195.3 |
| Enzyme 47 Theoretical pI |
9.77 |
| Enzyme 47 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 47 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 47 Specific Function |
Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity |
| Enzyme 47 Pathways |
|
| Enzyme 47 Reactions |
- acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
|
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
37537527  |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
Q3SYC2  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
MOGT2_HUMAN  |
| Enzyme 47 PDB ID |
Not Available |
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>1005 bp
ATGGTAGAGTTCGCGCCCTTGTTTATGCCGTGGGAGCGCAGGCTGCAGACACTTGCTGTC
CTACAGTTTGTCTTCTCCTTCTTGGCACTGGCCGAGATCTGCACTGTGGGCTTCATAGCC
CTCCTGTTTACAAGATTCTGGCTCCTCACTGTCCTGTATGCGGCCTGGTGGTATCTGGAC
CGAGACAAGCCACGGCAGGGGGGCCGGCACATCCAGGCCATCAGGTGCTGGACTATATGG
AAGTACATGAAGGACTATTTCCCCATCTCGCTGGTCAAGACTGCTGAGCTGGACCCCTCT
CGGAACTACATTGCGGGCTTCCACCCCCATGGAGTCCTGGCAGTCGGAGCCTTTGCCAAC
CTGTGCACTGAGAGCACAGGCTTCTCTTCGATCTTCCCCGGTATCCGCCCCCATCTGATG
ATGCTGACCTTGTGGTTCCGGGCCCCCTTCTTCAGAGATTACATCATGTCTGCAGGGTTG
GTCACATCAGAAAAGGAGAGTGCTGCTCACATTCTGAACAGGAAGGGTGGCGGAAACTTG
CTGGGCATCATTGTAGGGGGTGCCCAGGAGGCCCTGGATGCCAGGCCTGGATCCTTCACG
CTGTTACTGCGGAACCGAAAGGGCTTCGTCAGGCTCGCCCTGACACACGGGGCACCCCTG
GTGCCAATCTTCTCCTTCGGGGAGAATGACCTATTTGACCAGATTCCCAACTCTTCTGGC
TCCTGGTTACGCTATATCCAGAATCGGTTGCAGAAGATCATGGGCATCTCCCTCCCACTC
TTTCATGGCCGTGGTGTCTTCCAGTACAGCTTTGGTTTAATACCCTACCGCCGGCCCATC
ACCACTGTGGTGGGGAAGCCCATCGAGGTACAGAAGACGCTGCATCCCTCGGAGGAGGAG
GTGAACCAGCTGCACCAGCGTTATATCAAAGAGCTGTGCAACCTCTTCGAGGCCCACAAA
CTTAAGTTCAACATCCCTGCTGACCAGCACTTGGAGTTCTGCTGA
|
| Enzyme 47 GenBank Gene ID |
NM_025098.2  |
| Enzyme 47 GeneCard ID |
MOGAT2  |
| Enzyme 47 GenAtlas ID |
MOGAT2  |
| Enzyme 47 HGNC ID |
HGNC:23248  |
| Enzyme 47 Chromosome Location |
1 |
| Enzyme 47 Locus |
11q13.5 |
| Enzyme 47 SNPs |
SNPJam Report  |
| Enzyme 47 General References |
- Yen CL, Farese RV Jr: MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine. J Biol Chem. 2003 May 16;278(20):18532-7. Epub 2003 Mar 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
]
- Lockwood JF, Cao J, Burn P, Shi Y: Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity. Am J Physiol Endocrinol Metab. 2003 Nov;285(5):E927-37. Epub 2003 Jun 24. [PubMed
]
|
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
8755 |
| Enzyme 48 Name |
Phospholipase A2, group XIIA, isoform CRA_b |
| Enzyme 48 Synonyms |
- SubName: cDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2 (EC 3.1.1.4)
- SubName: cDNA, FLJ93563, Homo sapiens phospholipase A2, group XII (PLA2G12), mRNA
|
| Enzyme 48 Gene Name |
PLA2G12A |
| Enzyme 48 Protein Sequence |
>Phospholipase A2, group XIIA, isoform CRA_b
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
|
| Enzyme 48 Number of Residues |
189 |
| Enzyme 48 Molecular Weight |
21067.0 |
| Enzyme 48 Theoretical pI |
7.27 |
| Enzyme 48 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 48 General Function |
Involved in phospholipase A2 activity |
| Enzyme 48 Specific Function |
Not Available |
| Enzyme 48 Pathways |
|
| Enzyme 48 Reactions |
Not Available |
| Enzyme 48 Pfam Domain Function |
|
| Enzyme 48 Signals |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
22761446  |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
Q542Y6  |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
Q542Y6_HUMAN  |
| Enzyme 48 PDB ID |
Not Available |
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>570 bp
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTAGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
|
| Enzyme 48 GenBank Gene ID |
AK075389  |
| Enzyme 48 GeneCard ID |
PLA2G12A  |
| Enzyme 48 GenAtlas ID |
PLA2G12A  |
| Enzyme 48 HGNC ID |
HGNC:18554  |
| Enzyme 48 Chromosome Location |
4 |
| Enzyme 48 Locus |
4q25 |
| Enzyme 48 SNPs |
SNPJam Report  |
| Enzyme 48 General References |
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed
]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
8937 |
| Enzyme 49 Name |
Choline/ethanolaminephosphotransferase 1 |
| Enzyme 49 Synonyms |
- hCEPT1
|
| Enzyme 49 Gene Name |
CEPT1 |
| Enzyme 49 Protein Sequence |
>Choline/ethanolaminephosphotransferase 1
MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAG
RSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYI
ACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPD
WMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIP
VLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLA
AMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLD
QYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH
|
| Enzyme 49 Number of Residues |
416 |
| Enzyme 49 Molecular Weight |
46553.1 |
| Enzyme 49 Theoretical pI |
8.25 |
| Enzyme 49 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, for other substituted phosphate groups
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
|
|
| Enzyme 49 General Function |
Involved in phosphotransferase activity, for other substituted phosphate groups |
| Enzyme 49 Specific Function |
Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity |
| Enzyme 49 Pathways |
|
| Enzyme 49 Reactions |
- CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine [RN:R01321]
|
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
- 87-107
115-135
186-206
209-229
239-259
283-303
317-337
365-385
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
4584877  |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q9Y6K0  |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
CEPT1_HUMAN  |
| Enzyme 49 PDB ID |
Not Available |
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>1251 bp
ATGAGTGGGCATCGATCAACAAGGAAAAGATGTGGAGATTCTCACCCGGAGTCCCCAGTG
GGCTTCGGGCATATGAGTACTACAGGATGTGTATTAAATAAATTGTTTCAGTTACCAACA
CCACCATTGTCAAGACACCAACTAAAGCGGCTAGAAGAACACAGATATCAAAGTGCTGGA
CGGTCCCTGCTTGAGCCCTTAATGCAAGGGTATTGGGAATGGCTCGTTAGAAGAGTTCCC
TCCTGGATTGCCCCAAATCTCATCACCATCATTGGACTGTCAATAAACATCTGTACAACT
ATTTTATTAGTCTTCTACTGCCCTACAGCTACAGAGCAGGCACCTCTGTGGGCATATATT
GCTTGTGCCTGTGGCCTTTTCATTTACCAGTCTTTGGATGCTATTGATGGGAAACAGGCA
AGAAGAACCAATAGTAGTTCTCCTCTGGGAGAACTTTTTGATCATGGCTGTGATTCACTA
TCAACAGTTTTTGTGGTTCTTGGAACTTGTATTGCAGTGCAGCTGGGGACAAACCCTGAT
TGGATGTTTTTTTGTTGTTTTGCGGGGACATTTATGTTCTATTGTGCGCACTGGCAAACG
TATGTTTCTGGAACATTGCGATTTGGAATAATTGATGTGACTGAAGTGCAAATCTTCATA
ATAATCATGCATTTGCTGGCAGTGATTGGAGGACCACCTTTTTGGCAATCTATGATTCCA
GTGCTGAATATTCAAATGAAAATTTTTCCTGCACTTTGTACTGTAGCAGGGACCATATTT
TCCTGTACAAATTACTTCCGTGTAATCTTCACAGGTGGTGTTGGCAAAAATGGATCAACA
ATAGCAGGAACAAGTGTCCTTTCTCCTTTTCTCCATATTGGATCAGTGATTACATTAGCT
GCAATGATCTACAAGAAATCTGCAGTTCAGCTTTTTGAAAAGCATCCCTGTCTTTATATA
CTGACATTTGGTTTTGTGTCTGCTAAAATCACTAATAAGCTTGTGGTTGCACACATGACG
AAAAGTGAAATGCATTTGCATGACACAGCATTCATAGGTCCGGCACTTTTGTTTCTGGAC
CAGTATTTTAACAGCTTTATTGATGAATATATTGTACTTTGGATTGCCCTGGTTTTCTCT
TTCTTTGATTTGATCCGCTACTGTGTCAGTGTTTGCAATCAGATTGCGTCTCACCTGCAC
ATACATGTCTTCAGAATCAAGGTCTCTACAGCTCATTCTAATCATCATTAA
|
| Enzyme 49 GenBank Gene ID |
AF068302  |
| Enzyme 49 GeneCard ID |
CEPT1  |
| Enzyme 49 GenAtlas ID |
CEPT1  |
| Enzyme 49 HGNC ID |
HGNC:24289  |
| Enzyme 49 Chromosome Location |
1 |
| Enzyme 49 Locus |
1p13.3 |
| Enzyme 49 SNPs |
SNPJam Report  |
| Enzyme 49 General References |
- Henneberry AL, McMaster CR: Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem J. 1999 Apr 15;339 ( Pt 2):291-8. [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
]
- 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
]
- Henneberry AL, Wistow G, McMaster CR: Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. [PubMed
]
- Wright MM, McMaster CR: PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1). Lipids. 2002 Jul;37(7):663-72. [PubMed
]
- Henneberry AL, Wright MM, McMaster CR: The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity. Mol Biol Cell. 2002 Sep;13(9):3148-61. [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 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
10050 |
| Enzyme 50 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3 |
| Enzyme 50 Synonyms |
- Phosphoinositide phospholipase C-delta-3
- Phospholipase C-delta-3
- PLC-delta-3
|
| Enzyme 50 Gene Name |
PLCD3 |
| Enzyme 50 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDE
DVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREG
HQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQR
ERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEG
AEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYE
LNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQ
IGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFT
LSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVK
GKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRL
RTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQ
EMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRT
TLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTL
QFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATL
FIQIRIQRS
|
| Enzyme 50 Number of Residues |
789 |
| Enzyme 50 Molecular Weight |
89257.5 |
| Enzyme 50 Theoretical pI |
6.97 |
| Enzyme 50 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 50 General Function |
Involved in calcium ion binding |
| Enzyme 50 Specific Function |
Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow |
| Enzyme 50 Pathways |
|
| Enzyme 50 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
Not Available |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
Q8N3E9  |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
PLCD3_HUMAN  |
| Enzyme 50 PDB ID |
Not Available |
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>2370 bp
ATGCTGTGCGGCCGCTGGAGGCGTTGCCGCCGCCCGCCCGAGGAGCCCCCGGTGGCCGCC
CAGGTCGCAGCCCAAGTCGCGGCGCCGGTCGCTCTCCCGTCCCCGCCGACTCCCTCCGAT
GGCGGCACCAAGAGGCCCGGGCTGCGGGCGCTGAAGAAGATGGGCCTGACGGAGGACGAG
GACGTGCGCGCCATGCTGCGGGGCTCCCGGCTCCGCAAGATCCGCTCGCGCACGTGGCAC
AAGGAGCGGCTGTACCGGCTGCAGGAGGACGGCCTGAGCGTGTGGTTCCAGCGGCGCATC
CCGCGTGCGCCATCGCAGCACATCTTCTTCGTGCAGCACATCGAGGCGGTCCGCGAGGGC
CACCAGTCCGAGGGCCTGCGGCGCTTCGGGGGTGCCTTCGCGCCAGCGCGCTGCCTCACC
ATCGCCTTCAAGGGCCGCCGCAAGAACCTGGACCTGGCGGCGCCCACGGCTGAGGAAGCG
CAGCGCTGGGTGCGCGGTCTGACCAAGCTCCGCGCGCGCCTGGACGCCATGAGCCAGCGC
GAGCGGCTAGACCACTGGATCCACTCCTATCTGCACCGGGCTGACTCCAACCAGGACAGC
AAGATGAGCTTCAAGGAGATCAAGAGCCTGCTGAGAATGGTCAACGTGGACATGAACGAC
ATGTACGCCTACCTCCTCTTCAAGGAGTGTGACCACTCCAACAACGACCGTCTAGAGGGG
GCTGAGATCGAGGAGTTCCTGCGGCGGCTGCTGAAGCGGCCGGAGCTGGAGGAGATCTTC
CATCAGTACTCGGGCGAGGACCGCGTGCTGAGTGCCCCTGAGCTGCTGGAGTTCCTGGAG
GACCAGGGCGAGGAGGGCGCCACACTGGCCCGCGCCCAGCAGCTCATTCAGACCTATGAG
CTCAACGAGACAGCCAAGCAGCATGAGCTGATGACACTGGATGGCTTCATGATGTACCTG
TTGTCGCCGGAGGGGGCTGCCTTGGACAACACCCACACGTGTGTGTTCCAGGACATGAAC
CAGCCCCTTGCCCACTACTTCATCTCTTCCTCCCACAACACCTATCTGACTGACTCCCAG
ATCGGGGGGCCCAGCAGCACCGAGGCCTATGTTAGGGCCTTTGCCCAGGGATGCCGCTGC
GTGGAGCTGGACTGCTGGGAGGGGCCAGGAGGGGAGCCCGTCATCTATCATGGCCATACC
CTCACCTCCAAGATTCTCTTCCGGGACGTGGTCCAAGCCGTGCGCGACCATGCCTTCACG
CTGTCCCCTTACCCTGTCATCCTATCCCTGGAGAACCACTGCGGGCTGGAGCAGCAGGCT
GCCATGGCCCGCCACCTCTGCACCATCCTGGGGGACATGCTGGTGACACAGGCGCTGGAC
TCCCCAAATCCCGAGGAGCTGCCATCCCCAGAGCAGCTGAAGGGCCGGGTCCTGGTGAAG
GGAAAGAAGTTGCCCGCTGCTCGGAGCGAGGATGGCCGGGCTCTGTCGGATCGGGAGGAG
GAGGAGGAGGATGACGAGGAGGAAGAAGAGGAGGTGGAGGCTGCAGCGCAGAGGCGGCTG
GCCAAGCAGATCTCCCCGGAGCTGTCGGCCCTGGCTGTGTACTGCCACGCCACCCGCCTG
CGGACCCTGCACCCTGCCCCCAACGCCCCACAACCCTGCCAGGTCAGCTCCCTCAGCGAG
CGCAAAGCCAAGAAACTCATTCGGGAGGCAGGGAACAGCTTTGTCAGGCACAATGCCCGC
CAGCTGACCCGCGTGTACCCGCTGGGGCTGCGGATGAACTCAGCCAACTACAGTCCCCAG
GAGATGTGGAACTCGGGCTGTCAGCTGGTGGCCTTGAACTTCCAGACGCCAGGCTACGAG
ATGGACCTCAATGCCGGGCGCTTCCTAGTCAATGGGCAGTGTGGCTACGTCCTAAAACCT
GCCTGCCTGCGGCAACCTGACTCGACCTTTGACCCCGAGTACCCAGGACCTCCCAGAACC
ACTCTCAGCATCCAGGTGCTGACTGCACAGCAGCTGCCCAAGCTGAATGCCGAGAAGCCA
CACTCCATTGTGGACCCCCTGGTGCGCATTGAGATCCATGGGGTGCCCGCAGACTGTGCC
CGGCAGGAGACTGACTACGTGCTCAACAATGGCTTCAACCCCCGCTGGGGGCAGACCCTG
CAGTTCCAGCTGCGGGCTCCGGAGCTGGCACTGGTCCGGTTTGTGGTGGAAGATTATGAC
GCCACCTCCCCCAATGACTTTGTGGGCCAGTTTACACTGCCTCTTAGCAGCCTAAAGCAA
GGGTACCGCCACATACACCTGCTTTCCAAGGACGGGGCCTCACTGTCACCAGCCACGCTC
TTCATCCAAATCCGCATCCAGCGCTCCTGA
|
| Enzyme 50 GenBank Gene ID |
AK074240  |
| Enzyme 50 GeneCard ID |
PLCD3  |
| Enzyme 50 GenAtlas ID |
PLCD3  |
| Enzyme 50 HGNC ID |
HGNC:9061  |
| Enzyme 50 Chromosome Location |
1 |
| Enzyme 50 Locus |
17q21.31 |
| Enzyme 50 SNPs |
SNPJam Report  |
| Enzyme 50 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
]
- 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
]
- Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed
]
- Pawelczyk T, Matecki A: Expression, purification and kinetic properties of human recombinant phospholipase C delta 3. Acta Biochim Pol. 1997;44(2):221-9. [PubMed
]
- Ghosh S, Pawelczyk T, Lowenstein JM: Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties. Protein Expr Purif. 1997 Mar;9(2):262-78. [PubMed
]
- Pawelczyk T, Matecki A: Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium. Eur J Biochem. 1998 Oct 1;257(1):169-77. [PubMed
]
- Kim H, Suh PG, Ryu SH, Park SH: Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization. Cytogenet Cell Genet. 1999;87(3-4):209-10. [PubMed
]
- Pawelczyk T, Matecki A: Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes. Eur J Biochem. 1999 Jun;262(2):291-8. [PubMed
]
- Lin FG, Cheng HF, Lee IF, Kao HJ, Loh SH, Lee WH: Downregulation of phospholipase C delta3 by cAMP and calcium. Biochem Biophys Res Commun. 2001 Aug 17;286(2):274-80. [PubMed
]
- Ananthanarayanan B, Das S, Rhee SG, Murray D, Cho W: Membrane targeting of C2 domains of phospholipase C-delta isoforms. J Biol Chem. 2002 Feb 1;277(5):3568-75. Epub 2001 Nov 12. [PubMed
]
- Landreville S, Coulombe S, Carrier P, Gelb MH, Guerin SL, Salesse C: Expression of phospholipases A2 and C in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004 Nov;45(11):3997-4003. [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
]
- Naito Y, Okada M, Yagisawa H: Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. J Biochem. 2006 Dec;140(6):785-91. Epub 2006 Oct 14. [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 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
12907 |
| Enzyme 51 Name |
Lysophospholipid acyltransferase 5 |
| Enzyme 51 Synonyms |
- LPLAT 5
- 1-acylglycerophosphocholine O-acyltransferase
- 1-acylglycerophosphoserine O-acyltransferase
- Lysophosphatidylcholine acyltransferase
- LPCAT
- Lyso-PC acyltransferase
- Lysophosphatidylcholine acyltransferase 3
- Lyso-PC acyltransferase 3
- Lysophosphatidylserine acyltransferase
- LPSAT
- Lyso-PS acyltransferase
- Membrane-bound O-acyltransferase domain-containing protein 5
- O-acyltransferase domain-containing protein 5
|
| Enzyme 51 Gene Name |
LPCAT3 |
| Enzyme 51 Protein Sequence |
>Lysophospholipid acyltransferase 5
MASSAEGDEGTVVALAGVLQSGFQELSLNKLATSLGASEQALRLIISIFLGYPFALFYRH
YLFYKETYLIHLFHTFTGLSIAYFNFGNQLYHSLLCIVLQFLILRLMGRTITAVLTTFCF
QMAYLLAGYYYTATGNYDIKWTMPHCVLTLKLIGLAVDYFDGGKDQNSLSSEQQKYAIRG
VPSLLEVAGFSYFYGAFLVGPQFSMNHYMKLVQGELIDIPGKIPNSIIPALKRLSLGLFY
LVGYTLLSPHITEDYLLTEDYDNHPFWFRCMYMLIWGKFVLYKYVTCWLVTEGVCILTGL
GFNGFEEKGKAKWDACANMKVWLFETNPRFTGTIASFNINTNAWVARYIFKRLKFLGNKE
LSQGLSLLFLALWHGLHSGYLVCFQMEFLIVIVERQAARLIQESPTLSKLAAITVLQPFY
YLVQQTIHWLFMGYSMTAFCLFTWDKWLKVYKSIYFLGHIFFLSLLFILPYIHKAMVPRK
EKLKKME
|
| Enzyme 51 Number of Residues |
487 |
| Enzyme 51 Molecular Weight |
56034.5 |
| Enzyme 51 Theoretical pI |
8.87 |
| Enzyme 51 GO Classification |
Not Available |
| Enzyme 51 General Function |
Involved in 1-acylglycerophosphocholine O-acyltransfera |
| Enzyme 51 Specific Function |
Acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3- phosphocholine or PC) (LPCAT activity). Catalyzes also the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero- 3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn- glycero-3-phospho-L-serine or PS) (LPSAT activity). Has also weak lysophosphatidylethanolamine acyltransferase activity (LPEAT activity). Favors polyunsaturated fatty acyl-CoAs as acyl donors compared to saturated fatty acyl-CoAs. Seems to be the major enzyme contributing to LPCAT activity in the liver. Lysophospholipid acyltransferases (LPLATs) catalyze the reacylation step of the phospholipid remodeling pathway also known as the Lands cycle |
| Enzyme 51 Pathways |
Not Available |
| Enzyme 51 Reactions |
- acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl-sn-glycero-3-phosphocholine [RN:R01318]
|
| Enzyme 51 Pfam Domain Function |
|
| Enzyme 51 Signals |
|
| Enzyme 51 Transmembrane Regions |
- 44-64
84-104
111-131
180-200
227-247
285-305
364-384
422-442
453-473
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
42542394  |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
Q6P1A2  |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
MBOA5_HUMAN  |
| Enzyme 51 PDB ID |
Not Available |
| Enzyme 51 Cellular Location |
Not Available |
| Enzyme 51 Gene Sequence |
>1464 bp
ATGGCGTCCTCAGCGGAGGGGGACGAGGGGACTGTGGTGGCGCTGGCGGGGGTTCTGCAG
TCGGGTTTCCAGGAGCTGAGCCTTAACAAGTTGGCGACGTCCCTGGGCGCGTCAGAACAG
GCGCTGCGGCTGATCATCTCCATCTTCCTGGGTTACCCCTTTGCTTTGTTTTATCGGCAT
TACCTTTTCTACAAGGAGACCTACCTCATCCACCTCTTCCATACCTTTACAGGCCTCTCA
ATTGCTTATTTTAACTTTGGAAACCAGCTCTACCACTCCCTGCTGTGTATTGTGCTTCAG
TTCCTCATCCTTCGACTAATGGGCCGCACCATCACTGCCGTCCTCACTACCTTTTGCTTC
CAGATGGCCTACCTTCTGGCTGGATACTATTACACTGCCACCGGCAACTACGATATCAAG
TGGACAATGCCACATTGTGTTCTGACTTTGAAGCTGATTGGTTTGGCTGTTGACTACTTT
GACGGAGGGAAAGATCAGAATTCCTTGTCCTCTGAGCAACAGAAATATGCCATACGTGGT
GTTCCTTCCCTGCTGGAAGTTGCTGGTTTCTCCTACTTCTATGGGGCCTTCTTGGTAGGG
CCCCAGTTCTCAATGAATCACTACATGAAGCTGGTGCAGGGAGAGCTGATTGACATACCA
GGAAAGATACCAAACAGCATCATTCCTGCTCTCAAGCGCCTGAGTCTGGGCCTTTTCTAC
CTAGTGGGCTACACACTGCTCAGCCCCCACATCACAGAAGACTATCTCCTCACTGAAGAC
TATGACAACCACCCCTTCTGGTTCCGCTGCATGTACATGCTGATCTGGGGCAAGTTTGTG
CTGTACAAATATGTCACCTGTTGGCTGGTCACAGAAGGAGTATGCATTTTGACGGGCCTG
GGCTTCAATGGCTTTGAAGAAAAGGGCAAGGCAAAGTGGGATGCCTGTGCCAACATGAAG
GTGTGGCTCTTTGAAACAAACCCCCGCTTCACTGGCACCATTGCCTCATTCAACATCAAC
ACCAACGCCTGGGTGGCCCGCTACATCTTCAAACGACTCAAGTTCCTTGGAAATAAAGAA
CTCTCTCAGGGTCTCTCGTTGCTATTCCTGGCCCTCTGGCACGGCCTGCACTCAGGATAC
CTGGTCTGCTTCCAGATGGAATTCCTCATTGTTATTGTGGAAAGACAGGCTGCCAGGCTC
ATTCAAGAGAGCCCCACCCTGAGCAAGCTGGCCGCCATTACTGTCCTCCAGCCCTTCTAC
TATTTGGTGCAACAGACCATCCACTGGCTCTTCATGGGTTACTCCATGACTGCCTTCTGC
CTCTTCACGTGGGACAAATGGCTTAAGGTGTATAAATCCATCTATTTCCTTGGCCACATC
TTCTTCCTGAGCCTACTATTCATATTGCCTTATATTCACAAAGCAATGGTGCCAAGGAAA
GAGAAGTTAAAGAAGATGGAATAA
|
| Enzyme 51 GenBank Gene ID |
NM_005768.5  |
| Enzyme 51 GeneCard ID |
LPCAT3  |
| Enzyme 51 GenAtlas ID |
LPCAT3  |
| Enzyme 51 HGNC ID |
HGNC:30244  |
| Enzyme 51 Chromosome Location |
1 |
| Enzyme 51 Locus |
12p13 |
| Enzyme 51 SNPs |
SNPJam Report  |
| Enzyme 51 General References |
- 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
]
- 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
]
- Ansari-Lari MA, Shen Y, Muzny DM, Lee W, Gibbs RA: Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. Genome Res. 1997 Mar;7(3):268-80. [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
]
- Zhao Y, Chen YQ, Bonacci TM, Bredt DS, Li S, Bensch WR, Moller DE, Kowala M, Konrad RJ, Cao G: Identification and characterization of a major liver lysophosphatidylcholine acyltransferase. J Biol Chem. 2008 Mar 28;283(13):8258-65. Epub 2008 Jan 14. [PubMed
]
- Gijon MA, Riekhof WR, Zarini S, Murphy RC, Voelker DR: Lysophospholipid acyltransferases and arachidonate recycling in human neutrophils. J Biol Chem. 2008 Oct 31;283(44):30235-45. Epub 2008 Sep 3. [PubMed
]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
12908 |
| Enzyme 52 Name |
Putative inactive group IIC secretory phospholipase A2 |
| Enzyme 52 Synonyms |
- Phosphatidylcholine 2-acylhydrolase-like protein GIIC
|
| Enzyme 52 Gene Name |
PLA2G2C |
| Enzyme 52 Protein Sequence |
>Putative inactive group IIC secretory phospholipase A2
MKVIAILTLLLFCSPTHSSFWQFQRRVKHITGRSAFFSYYGYGCYCGLGDKGIPVDDTDR
HSPSSPSPYEKLKEFSCQPVLNSYQFHIVNGAVVCGCTLGPGASCHCRLKACECDKQSVH
CFKESLPTYEKNFKQFSSQPRCGRHKPWC
|
| Enzyme 52 Number of Residues |
149 |
| Enzyme 52 Molecular Weight |
16844.2 |
| Enzyme 52 Theoretical pI |
8.60 |
| Enzyme 52 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 52 General Function |
Involved in phospholipase A2 activity |
| Enzyme 52 Specific Function |
Inactive phospholipase (Probable) |
| Enzyme 52 Pathways |
Not Available |
| Enzyme 52 Reactions |
Not Available |
| 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 |
Q5R387  |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
PA2GC_HUMAN  |
| Enzyme 52 PDB ID |
Not Available |
| Enzyme 52 Cellular Location |
Not Available |
| Enzyme 52 Gene Sequence |
Not Available |
| Enzyme 52 GenBank Gene ID |
Not Available |
| Enzyme 52 GeneCard ID |
PLA2G2C  |
| Enzyme 52 GenAtlas ID |
PLA2G2C  |
| Enzyme 52 HGNC ID |
HGNC:9032  |
| Enzyme 52 Chromosome Location |
1 |
| Enzyme 52 Locus |
1p36.12 |
| Enzyme 52 SNPs |
SNPJam Report  |
| Enzyme 52 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
]
- Seilhamer JJ, Randall TL, Johnson LK, Heinzmann C, Klisak I, Sparkes RS, Lusis AJ: Novel gene exon homologous to pancreatic phospholipase A2: sequence and chromosomal mapping of both human genes. J Cell Biochem. 1989 Mar;39(3):327-37. [PubMed
]
|
| Enzyme 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
12909 |
| Enzyme 53 Name |
Lysophosphatidylcholine acyltransferase 1 |
| Enzyme 53 Synonyms |
- LPC acyltransferase 1
- LPCAT-1
- LysoPC acyltransferase 1
- 1-acylglycerophosphocholine O-acyltransferase
- 1-alkylglycerophosphocholine O-acetyltransferase
- Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
- Acetyl-CoA:lyso-PAF acetyltransferase
- Lyso-PAF acetyltransferase
- LysoPAFAT
- Acyltransferase-like 2
- Phosphonoformate immuno-associated protein 3
|
| Enzyme 53 Gene Name |
LPCAT1 |
| Enzyme 53 Protein Sequence |
>Lysophosphatidylcholine acyltransferase 1
MRLRGCGPRAAPASSAGASDARLLAPPGRNPFVHELRLSALQKAQVALMTLTLFPVRLLV
AAAMMLLAWPLALVASLGSAEKEPEQPPALWRKVVDFLLKAIMRTMWFAGGFHRVAVKGR
QALPTEAAILTLAPHSSYFDAIPVTMTMSSIVMKAESRDIPIWGTLIQYIRPVFVSRSDQ
DSRRKTVEEIKRRAQSNGKWPQIMIFPEGTCTNRTCLITFKPGAFIPGAPVQPVVLRYPN
KLDTITWTWQGPGALEILWLTLCQFHNQVEIEFLPVYSPSEEEKRNPALYASNVRRVMAE
ALGVSVTDYTFEDCQLALAEGQLRLPADTCLLEFARLVRGLGLKPEKLEKDLDRYSERAR
MKGGEKIGIAEFAASLEVPVSDLLEDMFSLFDESGSGEVDLRECVVALSVVCRPARTLDT
IQLAFKMYGAQEDGSVGEGDLSCILKTALGVAELTVTDLFRAIDQEEKGKITFADFHRFA
EMYPAFAEEYLYPDQTHFESCAETSPAPIPNGFCADFSPENSDAGRKPVRKKLD
|
| Enzyme 53 Number of Residues |
534 |
| Enzyme 53 Molecular Weight |
59150.7 |
| Enzyme 53 Theoretical pI |
5.82 |
| Enzyme 53 GO Classification |
| Function |
- acyltransferase activity
- binding
- calcium ion binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 53 General Function |
Involved in acyltransferase activity |
| Enzyme 53 Specific Function |
Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-independent. Mediates the conversion of 1-acyl-sn-glycero-3-phosphocholine (LPC) into phosphatidylcholine (PC). Displays a clear preference for saturated fatty acyl-CoAs, and 1-myristoyl or 1-palmitoyl LPC as acyl donors and acceptors, respectively. May synthesize phosphatidylcholine in pulmonary surfactant, thereby playing a pivotal role in respiratory physiology |
| Enzyme 53 Pathways |
|
| Enzyme 53 Reactions |
- acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
|
| Enzyme 53 Pfam Domain Function |
|
| Enzyme 53 Signals |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
100811832  |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
Q8NF37  |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
PCAT1_HUMAN  |
| Enzyme 53 PDB ID |
Not Available |
| Enzyme 53 Cellular Location |
Not Available |
| Enzyme 53 Gene Sequence |
>1605 bp
ATGAGGCTGCGGGGATGCGGACCCCGGGCCGCCCCTGCCTCCAGCGCAGGGGCCAGCGAC
GCTCGGCTGCTGGCGCCCCCGGGGCGGAACCCCTTCGTGCACGAGCTGCGCCTCAGCGCC
CTGCAGAAGGCCCAGGTGGCCCTCATGACACTGACGCTCTTCCCGGTCCGGCTCCTGGTT
GCCGCTGCCATGATGCTGCTGGCCTGGCCCCTCGCACTTGTCGCATCCCTGGGCTCTGCG
GAGAAGGAACCCGAGCAGCCCCCGGCCCTGTGGAGGAAGGTTGTGGACTTCCTGCTGAAG
GCCATCATGCGCACCATGTGGTTCGCCGGCGGCTTCCACCGGGTGGCCGTGAAGGGGCGG
CAGGCGCTGCCCACCGAGGCGGCCATCCTCACGCTCGCGCCTCACTCGTCCTACTTCGAC
GCCATCCCTGTGACCATGACGATGTCCTCCATCGTGATGAAGGCAGAGAGCAGAGACATC
CCGATCTGGGGAACTCTGATCCAGTATATACGGCCTGTGTTCGTGTCCCGGTCAGACCAG
GATTCTCGCAGGAAAACAGTAGAAGAAATCAAGAGACGGGCGCAGTCCAACGGAAAGTGG
CCACAGATAATGATTTTTCCAGAAGGAACTTGTACAAACAGGACCTGCCTAATTACCTTC
AAACCTGGTGCATTCATCCCTGGAGCGCCCGTCCAGCCTGTGGTTTTACGATATCCAAAT
AAACTGGACACCATCACATGGACGTGGCAAGGACCTGGAGCGCTGGAAATCCTGTGGCTC
ACGCTGTGTCAGTTTCACAACCAAGTGGAAATCGAGTTCCTTCCTGTGTACAGCCCTTCT
GAGGAGGAGAAGAGGAACCCCGCGCTGTATGCCAGCAACGTGCGGCGAGTCATGGCCGAG
GCCTTGGGTGTCTCCGTGACTGACTACACGTTCGAGGACTGCCAGCTGGCCCTGGCGGAA
GGACAGCTCCGTCTCCCCGCTGACACTTGCCTTTTAGAATTTGCCAGGCTCGTGCGGGGC
CTCGGGCTAAAACCAGAAAAGCTTGAAAAAGATCTGGACAGATACTCAGAAAGAGCCAGG
ATGAAGGGAGGAGAGAAGATAGGTATTGCGGAGTTTGCCGCCTCCCTGGAAGTCCCCGTT
TCTGACTTGCTGGAAGACATGTTTTCACTGTTCGACGAGAGCGGCAGCGGCGAGGTGGAC
CTGCGAGAGTGTGTGGTTGCCCTGTCTGTCGTCTGCCGGCCGGCCCGGACCCTGGACACC
ATCCAGCTGGCTTTCAAGATGTACGGAGCGCAAGAGGACGGCAGCGTCGGCGAAGGTGAC
CTGTCCTGCATCCTCAAGACGGCCCTGGGGGTGGCAGAGCTCACCGTGACCGACCTATTC
CGAGCCATTGACCAAGAGGAGAAGGGGAAGATCACATTCGCTGACTTCCACAGGTTTGCA
GAAATGTACCCTGCCTTCGCAGAGGAATACCTGTACCCGGATCAGACACATTTCGAAAGC
TGTGCAGAGACCTCACCTGCGCCAATCCCAAACGGCTTCTGTGCCGATTTCAGCCCGGAA
AACTCAGACGCTGGGCGGAAGCCTGTTCGCAAGAAGCTGGATTAG
|
| Enzyme 53 GenBank Gene ID |
AB244719  |
| Enzyme 53 GeneCard ID |
LPCAT1  |
| Enzyme 53 GenAtlas ID |
LPCAT1  |
| Enzyme 53 HGNC ID |
HGNC:25718  |
| Enzyme 53 Chromosome Location |
5 |
| Enzyme 53 Locus |
5p15.33 |
| Enzyme 53 SNPs |
SNPJam Report  |
| Enzyme 53 General References |
- Nakanishi H, Shindou H, Hishikawa D, Harayama T, Ogasawara R, Suwabe A, Taguchi R, Shimizu T: Cloning and characterization of mouse lung-type acyl-CoA:lysophosphatidylcholine acyltransferase 1 (LPCAT1). Expression in alveolar type II cells and possible involvement in surfactant production. J Biol Chem. 2006 Jul 21;281(29):20140-7. Epub 2006 May 16. [PubMed
]
- Jikuya H, Takano J, Kikuno R, Hirosawa M, Nagase T, Nomura N, Ohara O: Characterization of long cDNA clones from human adult spleen. II. The complete sequences of 81 cDNA clones. DNA Res. 2003 Feb 28;10(1):49-57. [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
]
- 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
]
- Chen X, Hyatt BA, Mucenski ML, Mason RJ, Shannon JM: Identification and characterization of a lysophosphatidylcholine acyltransferase in alveolar type II cells. Proc Natl Acad Sci U S A. 2006 Aug 1;103(31):11724-9. Epub 2006 Jul 24. [PubMed
]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
12910 |
| Enzyme 54 Name |
Lysophosphatidylcholine acyltransferase 2 |
| Enzyme 54 Synonyms |
- LPC acyltransferase 2
- LPCAT-2
- LysoPC acyltransferase 2
- 1-acylglycerophosphocholine O-acyltransferase
- 1-alkylglycerophosphocholine O-acetyltransferase
- Acetyl-CoA:lyso-platelet-activating factor acetyltransferase
- Acetyl-CoA:lyso-PAF acetyltransferase
- Lyso-PAF acetyltransferase
- LysoPAFAT
- Acyltransferase-like 1
|
| Enzyme 54 Gene Name |
LPCAT2 |
| Enzyme 54 Protein Sequence |
>Lysophosphatidylcholine acyltransferase 2
MSRCAQAAEVAATVPGAGVGNVGLRPPMVPRQASFFPPPVPNPFVQQTQIGSARRVQIVL
LGIILLPIRVLLVALILLLAWPFAAISTVCCPEKLTHPITGWRRKITQTALKFLGRAMFF
SMGFIVAVKGKIASPLEAPVFVAAPHSTFFDGIACVVAGLPSMVSRNENAQVPLIGRLLR
AVQPVLVSRVDPDSRKNTINEIIKRTTSGGEWPQILVFPEGTCTNRSCLITFKPGAFIPG
VPVQPVLLRYPNKLDTVTWTWQGYTFIQLCMLTFCQLFTKVEVEFMPVQVPNDEEKNDPV
LFANKVRNLMAEALGIPVTDHTYEDCRLMISAGQLTLPMEAGLVEFTKISRKLKLDWDGV
RKHLDEYASIASSSKGGRIGIEEFAKYLKLPVSDVLRQLFALFDRNHDGSIDFREYVIGL
AVLCNPSNTEEIIQVAFKLFDVDEDGYITEEEFSTILQASLGVPDLDVSGLFKEIAQGDS
ISYEEFKSFALKHPEYAKIFTTYLDLQTCHVFSLPKEVQTTPSTASNKVSPEKHEESTSD
KKDD
|
| Enzyme 54 Number of Residues |
544 |
| Enzyme 54 Molecular Weight |
60207.3 |
| Enzyme 54 Theoretical pI |
6.51 |
| Enzyme 54 GO Classification |
| Function |
- acyltransferase activity
- binding
- calcium ion binding
- catalytic activity
- cation binding
- ion binding
- metal ion binding
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
|
| Component |
| — |
|
| Enzyme 54 General Function |
Involved in acyltransferase activity |
| Enzyme 54 Specific Function |
Possesses both acyltransferase and acetyltransferase activities. Activity is calcium-dependent. Involved in platelet- activating factor (PAF) biosynthesis by catalyzing the conversion of the PAF precursor, 1-O-alkyl-sn-glycero-3-phosphocholine (lyso- PAF) into 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (PAF). Also converts lyso-PAF to 1-alkyl-phosphatidylcholine (PC), a major component of cell membranes and a PAF precursor. Under resting conditions, acyltransferase activity is preferred. Upon acute inflammatory stimulus, acetyltransferase activity is enhanced and PAF synthesis increases |
| Enzyme 54 Pathways |
Not Available |
| Enzyme 54 Reactions |
- acetyl-CoA + 1-alkyl-sn-glycero-3-phosphocholine = CoA + 2-acetyl-1-alkyl-sn-glycero-3-phosphocholine [RN:R03437]
|
| Enzyme 54 Pfam Domain Function |
|
| Enzyme 54 Signals |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
126364244  |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
Q7L5N7  |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
PCAT2_HUMAN  |
| Enzyme 54 PDB ID |
Not Available |
| Enzyme 54 Cellular Location |
Not Available |
| Enzyme 54 Gene Sequence |
>1635 bp
ATGAGCCGGTGCGCCCAGGCGGCGGAAGTGGCGGCCACAGTGCCAGGTGCCGGCGTCGGG
AACGTGGGGCTGCGGCCGCCCATGGTGCCCCGTCAGGCGTCCTTCTTCCCGCCGCCGGTG
CCGAACCCCTTCGTGCAGCAGACGCAGATCGGCTCCGCGAGGCGGGTCCAGATTGTCCTT
CTTGGGATTATCTTGCTTCCAATTCGTGTCTTATTGGTTGCGTTAATTTTATTACTTGCA
TGGCCATTTGCTGCAATTTCAACAGTATGCTGTCCTGAAAAGCTGACCCACCCAATAACT
GGTTGGAGGAGGAAAATTACTCAAACAGCTTTGAAATTTCTGGGTCGTGCTATGTTCTTT
TCAATGGGATTTATAGTTGCTGTAAAAGGAAAGATTGCAAGTCCTTTGGAAGCACCAGTT
TTTGTTGCTGCCCCTCATTCAACATTCTTTGATGGAATTGCCTGTGTTGTAGCTGGGTTA
CCTTCTATGGTATCTCGAAATGAGAATGCACAAGTCCCTCTGATTGGCAGACTGTTACGG
GCTGTGCAACCAGTTTTGGTGTCCCGTGTAGATCCGGATTCCCGAAAAAACACAATAAAT
GAAATAATAAAGCGAACAACATCAGGAGGAGAATGGCCCCAGATACTAGTTTTCCCAGAA
GGTACTTGTACTAATCGTTCCTGTTTGATTACTTTTAAACCAGGAGCCTTCATTCCAGGA
GTTCCAGTGCAGCCAGTCCTCCTCAGATACCCAAACAAGCTGGATACTGTGACCTGGACA
TGGCAAGGATATACATTCATTCAGCTTTGTATGCTTACTTTCTGCCAGCTCTTCACAAAG
GTAGAAGTTGAGTTTATGCCAGTTCAAGTACCAAATGATGAAGAAAAAAATGATCCTGTC
CTTTTTGCCAATAAAGTCCGGAATTTAATGGCAGAAGCTCTGGGAATACCAGTAACAGAT
CATACCTATGAAGACTGCAGATTGATGATTTCAGCAGGACAGCTAACATTGCCTATGGAA
GCTGGGCTGGTGGAATTTACTAAAATTAGCCGAAAATTGAAATTAGATTGGGATGGTGTT
CGTAAGCATTTGGATGAATATGCATCTATTGCGAGTTCCTCAAAAGGAGGAAGAATTGGA
ATTGAAGAATTCGCCAAGTATTTAAAGTTGCCTGTTTCAGATGTCTTGAGACAACTTTTT
GCACTCTTTGACAGGAACCATGATGGCAGCATTGACTTCCGAGAGTATGTGATTGGCCTG
GCTGTCTTGTGCAACCCTTCCAACACAGAGGAGATCATCCAGGTGGCATTTAAGCTGTTT
GACGTTGATGAGGATGGCTACATAACGGAGGAAGAGTTCTCCACCATTCTACAGGCTTCC
CTTGGAGTGCCTGACCTTGATGTTTCTGGTCTCTTCAAGGAAATAGCCCAAGGGGACTCA
ATTTCCTATGAGGAATTTAAAAGTTTTGCCTTAAAGCATCCAGAATATGCTAAGATATTT
ACAACATACCTAGACCTCCAGACGTGCCATGTGTTTTCATTACCAAAAGAAGTCCAGACA
ACCCCCTCCACCGCCAGTAATAAAGTCAGCCCTGAAAAGCATGAAGAGAGTACCTCAGAC
AAAAAAGATGACTGA
|
| Enzyme 54 GenBank Gene ID |
AB244718  |
| Enzyme 54 GeneCard ID |
LPCAT2  |
| Enzyme 54 GenAtlas ID |
LPCAT2  |
| Enzyme 54 HGNC ID |
HGNC:26032  |
| Enzyme 54 Chromosome Location |
1 |
| Enzyme 54 Locus |
16q12.2 |
| Enzyme 54 SNPs |
SNPJam Report  |
| Enzyme 54 General References |
- Shindou H, Hishikawa D, Nakanishi H, Harayama T, Ishii S, Taguchi R, Shimizu T: A single enzyme catalyzes both platelet-activating factor production and membrane biogenesis of inflammatory cells. Cloning and characterization of acetyl-CoA:LYSO-PAF acetyltransferase. J Biol Chem. 2007 Mar 2;282(9):6532-9. Epub 2006 Dec 20. [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
]
|
| Enzyme 54 Metabolite References |
Not Available |
|
Enzyme 55
[top]
|
| Enzyme 55 ID |
12911 |
| Enzyme 55 Name |
Phospholipase D3 |
| Enzyme 55 Synonyms |
- PLD 3
- Choline phosphatase 3
- HindIII K4L homolog
- Hu-K4
- Phosphatidylcholine-hydrolyzing phospholipase D3
|
| Enzyme 55 Gene Name |
PLD3 |
| Enzyme 55 Protein Sequence |
>Phospholipase D3
MKPKLMYQELKVPAEEPANELPMNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLW
EYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLDFPNASTGNPSTSQAWLGLLAGAHSSL
DIASFYWTLTNNDTHTQEPSAQQGEEVLRQLQTLAPKGVNVRIAVSKPSGPQPQADLQAL
LQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCL
ARDLTKIFEAYWFLGQAGSSIPSTWPRFYDTRYNQETPMEICLNGTPALAYLASAPPPLC
PSGRTPDLKALLNVVDNARSFIYVAVMNYLPTLEFSHPHRFWPAIDDGLRRATYERGVKV
RLLISCWGHSEPSMRAFLLSLAALRDNHTHSDIQVKLFVVPADEAQARIPYARVNHNKYM
VTERATYIGTSNWSGNYFTETAGTSLLVTQNGRGGLRSQLEAIFLRDWDSPYSHDLDTSA
DSVGNACRLL
|
| Enzyme 55 Number of Residues |
490 |
| Enzyme 55 Molecular Weight |
54704.9 |
| Enzyme 55 Theoretical pI |
6.45 |
| Enzyme 55 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 55 General Function |
Involved in catalytic activity |
| Enzyme 55 Specific Function |
A phosphatidylcholine + H(2)O = choline + a phosphatidate |
| Enzyme 55 Pathways |
|
| Enzyme 55 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| Enzyme 55 Pfam Domain Function |
|
| Enzyme 55 Signals |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
72534684  |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
Q8IV08  |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
PLD3_HUMAN  |
| Enzyme 55 PDB ID |
Not Available |
| Enzyme 55 Cellular Location |
Not Available |
| Enzyme 55 Gene Sequence |
>1473 bp
ATGAAGCCTAAACTGATGTACCAGGAGCTGAAGGTGCCTGCAGAGGAGCCCGCCAATGAG
CTGCCCATGAATGAGATTGAGGCGTGGAAGGCTGCGGAAAAGAAAGCCCGCTGGGTCCTG
CTGGTCCTCATTCTGGCGGTTGTGGGCTTCGGAGCCCTGATGACTCAGCTGTTTCTATGG
GAATACGGCGACTTGCATCTCTTTGGGCCCAACCAGCGCCCAGCCCCCTGCTATGACCCT
TGCGAAGCAGTGCTGGTGGAAAGCATTCCTGAGGGCCTGGACTTCCCCAATGCCTCCACG
GGGAACCCTTCCACCAGCCAGGCCTGGCTGGGCCTGCTCGCCGGTGCGCACAGCAGCCTG
GACATCGCCTCCTTCTACTGGACCCTCACCAACAATGACACCCACACGCAGGAGCCCTCT
GCCCAGCAGGGTGAGGAGGTCCTCCGGCAGCTGCAGACCCTGGCACCAAAGGGCGTGAAC
GTCCGCATCGCTGTGAGCAAGCCCAGCGGGCCCCAGCCACAGGCGGACCTGCAGGCTCTG
CTGCAGAGCGGTGCCCAGGTCCGCATGGTGGACATGCAGAAGCTGACCCATGGCGTCCTG
CATACCAAGTTCTGGGTGGTGGACCAGACCCACTTCTACCTGGGCAGTGCCAACATGGAC
TGGCGTTCACTGACCCAGGTCAAGGAGCTGGGCGTGGTCATGTACAACTGCAGCTGCCTG
GCTCGAGACCTGACCAAGATCTTTGAGGCCTACTGGTTCCTGGGCCAGGCAGGCAGCTCC
ATCCCATCAACTTGGCCCCGGTTCTATGACACCCGCTACAACCAAGAGACACCAATGGAG
ATCTGCCTCAATGGAACCCCTGCTCTGGCCTACCTGGCGAGTGCGCCCCCACCCCTGTGT
CCAAGTGGCCGCACTCCAGACCTGAAGGCTCTACTCAACGTGGTGGACAATGCCCGGAGT
TTCATCTACGTCGCTGTCATGAACTACCTGCCCACTCTGGAGTTCTCCCACCCTCACAGG
TTCTGGCCTGCCATTGACGATGGGCTGCGGCGGGCCACCTACGAGCGTGGCGTCAAGGTG
CGCCTGCTCATCAGCTGCTGGGGACACTCGGAGCCATCCATGCGGGCCTTCCTGCTCTCT
CTGGCTGCCCTGCGTGACAACCATACCCACTCTGACATCCAGGTGAAACTCTTTGTGGTC
CCCGCGGATGAGGCCCAGGCTCGAATCCCATATGCCCGTGTCAACCACAACAAGTACATG
GTGACTGAACGCGCCACCTACATCGGAACCTCCAACTGGTCTGGCAACTACTTCACGGAG
ACGGCGGGCACCTCGCTGCTGGTGACGCAGAATGGGAGGGGCGGCCTGCGGAGCCAGCTG
GAGGCCATTTTCCTGAGGGACTGGGACTCCCCTTACAGCCATGACCTTGACACCTCAGCT
GACAGCGTGGGCAACGCCTGCCGCCTGCTCTGA
|
| Enzyme 55 GenBank Gene ID |
NM_001031696.2  |
| Enzyme 55 GeneCard ID |
PLD3  |
| Enzyme 55 GenAtlas ID |
PLD3  |
| Enzyme 55 HGNC ID |
HGNC:17158  |
| Enzyme 55 Chromosome Location |
1 |
| Enzyme 55 Locus |
19q13.2 |
| Enzyme 55 SNPs |
SNPJam Report  |
| Enzyme 55 General References |
- Cao JX, Koop BF, Upton C: A human homolog of the vaccinia virus HindIII K4L gene is a member of the phospholipase D superfamily. Virus Res. 1997 Apr;48(1):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
]
- Munck A, Bohm C, Seibel NM, Hashemol Hosseini Z, Hampe W: Hu-K4 is a ubiquitously expressed type 2 transmembrane protein associated with the endoplasmic reticulum. FEBS J. 2005 Apr;272(7):1718-26. [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 55 Metabolite References |
Not Available |
|
Enzyme 56
[top]
|
| Enzyme 56 ID |
12912 |
| Enzyme 56 Name |
Phospholipase D4 |
| Enzyme 56 Synonyms |
- PLD 4
- Choline phosphatase 4
- Phosphatidylcholine-hydrolyzing phospholipase D4
|
| Enzyme 56 Gene Name |
PLD4 |
| Enzyme 56 Protein Sequence |
>Phospholipase D4
MLKPLWKAAVAPTWPCSMPPRRPWDREAGTLQVLGALAVLWLGSVALICLLWQVPRPPTW
GQVQPKDVPRSWEHGSSPAWEPLEAEARQQRDSCQLVLVESIPQDLPSAAGSPSAQPLGQ
AWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAVATSS
PTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQV
KELGAVIYNCSHLAQDLEKTFQTYWVLGVPKAVLPKTWPQNFSSHFNRFQPFHGLFDGVP
TTAYFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDN
ALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSN
IPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQSPGAQPAGATVQEQLRQL
FERDWSSRYAVGLDGQAPGQDCVWQG
|
| Enzyme 56 Number of Residues |
506 |
| Enzyme 56 Molecular Weight |
55626.1 |
| Enzyme 56 Theoretical pI |
8.46 |
| Enzyme 56 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 56 General Function |
Involved in catalytic activity |
| Enzyme 56 Specific Function |
A phosphatidylcholine + H(2)O = choline + a phosphatidate |
| Enzyme 56 Pathways |
|
| Enzyme 56 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| Enzyme 56 Pfam Domain Function |
|
| Enzyme 56 Signals |
|
| Enzyme 56 Transmembrane Regions |
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
94681038  |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
Q96BZ4  |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
PLD4_HUMAN  |
| Enzyme 56 PDB ID |
Not Available |
| Enzyme 56 Cellular Location |
Not Available |
| Enzyme 56 Gene Sequence |
>1521 bp
ATGCTGAAGCCTCTTTGGAAAGCAGCAGTGGCCCCCACATGGCCATGCTCCATGCCGCCC
CGCCGCCCGTGGGACAGAGAGGCTGGCACGTTGCAGGTCCTGGGAGCGCTGGCTGTGCTG
TGGCTGGGCTCCGTGGCTCTTATCTGCCTCCTGTGGCAAGTGCCCCGTCCTCCCACCTGG
GGCCAGGTGCAGCCCAAGGACGTGCCCAGGTCCTGGGAGCATGGCTCCAGCCCAGCTTGG
GAGCCCCTGGAAGCAGAGGCCAGGCAGCAGAGGGACTCCTGCCAGCTTGTCCTTGTGGAA
AGCATCCCCCAGGACCTGCCATCTGCAGCCGGCAGCCCCTCTGCCCAGCCTCTGGGCCAG
GCCTGGCTGCAGCTGCTGGACACTGCCCAGGAGAGCGTCCACGTGGCTTCATACTACTGG
TCCCTCACAGGGCCTGACATCGGGGTCAACGACTCGTCTTCCCAGCTGGGAGAGGCTCTT
CTGCAGAAGCTGCAGCAGCTGCTGGGCAGGAACATTTCCCTGGCTGTGGCCACCAGCAGC
CCGACACTGGCCAGGACATCCACCGACCTGCAGGTTCTGGCTGCCCGAGGTGCCCATGTA
CGACAGGTGCCCATGGGGCGGCTCACCAGGGGTGTTTTGCACTCCAAATTCTGGGTTGTG
GATGGACGGCACATATACATGGGCAGTGCCAACATGGACTGGCGGTCTCTGACGCAGGTG
AAGGAGCTTGGCGCTGTCATCTATAACTGCAGCCACCTGGCCCAAGACCTGGAGAAGACC
TTCCAGACCTACTGGGTACTGGGGGTGCCCAAGGCTGTCCTCCCCAAAACCTGGCCTCAG
AACTTCTCATCTCACTTCAACCGTTTCCAGCCCTTCCACGGCCTCTTTGATGGGGTGCCC
ACCACTGCCTACTTCTCAGCGTCGCCACCAGCACTCTGTCCCCAGGGCCGCACCCGGGAC
CTGGAGGCGCTGCTGGCGGTGATGGGGAGCGCCCAGGAGTTCATCTATGCCTCCGTGATG
GAGTATTTCCCCACCACGCGCTTCAGCCACCCCCCGAGGTACTGGCCGGTGCTGGACAAC
GCGCTGCGGGCGGCAGCCTTCGGCAAGGGCGTGCGCGTGCGCCTGCTGGTCGGCTGCGGA
CTCAACACGGACCCCACCATGTTCCCCTACCTGCGGTCCCTGCAGGCGCTCAGCAACCCC
GCGGCCAACGTCTCTGTGGACGTGAAAGTCTTCATCGTGCCGGTGGGGAACCATTCCAAC
ATCCCATTCAGCAGGGTGAACCACAGCAAGTTCATGGTCACGGAGAAGGCAGCCTACATA
GGCACCTCCAACTGGTCGGAGGATTACTTCAGCAGCACGGCGGGGGTGGGCTTGGTGGTC
ACCCAGAGCCCTGGCGCGCAGCCCGCGGGGGCCACGGTGCAGGAGCAGCTGCGGCAGCTC
TTTGAGCGGGACTGGAGTTCGCGCTACGCCGTCGGCCTGGACGGACAGGCTCCGGGCCAG
GACTGCGTTTGGCAGGGCTGA
|
| Enzyme 56 GenBank Gene ID |
NM_138790.2  |
| Enzyme 56 GeneCard ID |
PLD4  |
| Enzyme 56 GenAtlas ID |
PLD4  |
| Enzyme 56 HGNC ID |
HGNC:23792  |
| Enzyme 56 Chromosome Location |
1 |
| Enzyme 56 Locus |
14q32.33 |
| Enzyme 56 SNPs |
SNPJam Report  |
| Enzyme 56 General References |
- 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
]
- Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R: Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nat Methods. 2005 Aug;2(8):591-8. [PubMed
]
|
| Enzyme 56 Metabolite References |
Not Available |
|
Enzyme 57
[top]
|
| Enzyme 57 ID |
12913 |
| Enzyme 57 Name |
Inactive phospholipase D5 |
| Enzyme 57 Synonyms |
- Inactive PLD 5
- Inactive choline phosphatase 5
- Inactive phosphatidylcholine-hydrolyzing phospholipase D5
- PLDc
|
| Enzyme 57 Gene Name |
PLD5 |
| Enzyme 57 Protein Sequence |
>Inactive phospholipase D5
MEIRQHEWLSASPHEGFEQMRLKSRPKEPSPSLTRVGANFYSSVKQQDYSASVWLRRKDK
LEHSQQKCIVIFALVCCFAILVALIFSAVDIMGEDEDGLSEKNCQNKCRIALVENIPEGL
NYSENAPFHLSLFQGWMNLLNMAKKSVDIVSSHWDLNHTHPSACQGQRLFEKLLQLTSQN
IEIKLVSDVTADSKVLEALKLKGAEVTYMNMTAYNKGRLQSSFWIVDKQHVYIGSAGLDW
QSLGQMKELGVIFYNCSCLVLDLQRIFALYSSLKFKSRVPQTWSKRLYGVYDNEKKLQLQ
LNETKSQAFVSNSPKLFCPKNRSFDIDAIYSVIDDAKQYVYIAVMDYLPISSTSTKRTYW
PDLDAKIREALVLRSVRVRLLLSFWKETDPLTFNFISSLKAICTEIANCSLKVKFFDLER
ENACATKEQKNHTFPRLNRNKYMVTDGAAYIGNFDWVGNDFTQNAGTGLVINQADVRNNR
SIIKQLKDVFERDWYSPYAKTLQPTKQPNCSSLFKLKPLSNKTATDDTGGKDPRNV
|
| Enzyme 57 Number of Residues |
536 |
| Enzyme 57 Molecular Weight |
61311.7 |
| Enzyme 57 Theoretical pI |
8.94 |
| Enzyme 57 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 57 General Function |
Involved in catalytic activity |
| Enzyme 57 Specific Function |
Not Available |
| Enzyme 57 Pathways |
Not Available |
| Enzyme 57 Reactions |
Not Available |
| Enzyme 57 Pfam Domain Function |
|
| Enzyme 57 Signals |
|
| Enzyme 57 Transmembrane Regions |
|
| Enzyme 57 Essentiality |
Not Available |
| Enzyme 57 GenBank ID Protein |
307775443  |
| Enzyme 57 UniProtKB/Swiss-Prot ID |
Q8N7P1  |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
PLD5_HUMAN  |
| Enzyme 57 PDB ID |
Not Available |
| Enzyme 57 Cellular Location |
Not Available |
| Enzyme 57 Gene Sequence |
>1611 bp
ATGGAGATCCGGCAGCACGAGTGGCTCTCGGCCTCCCCCCATGAGGGCTTCGAGCAGATG
AGGCTCAAAAGCCGCCCCAAGGAGCCCTCCCCAAGCCTGACCCGAGTGGGCGCGAACTTC
TACAGCAGCGTCAAGCAGCAGGACTACAGCGCCAGCGTCTGGCTTCGGAGGAAAGACAAG
CTGGAGCACTCCCAGCAGAAGTGCATCGTGATCTTTGCCCTGGTGTGCTGCTTTGCCATT
CTGGTTGCACTGATCTTTTCAGCCGTGGACATCATGGGAGAGGATGAGGATGGACTCTCA
GAAAAAAATTGCCAAAATAAATGTCGAATTGCCCTGGTGGAAAATATTCCTGAAGGCCTT
AACTATTCAGAAAATGCACCATTTCACTTATCACTTTTCCAAGGCTGGATGAATTTACTC
AACATGGCCAAAAAGTCTGTTGACATAGTGTCTTCCCATTGGGATCTCAACCACACTCAT
CCATCAGCATGTCAGGGTCAACGTCTTTTTGAAAAGTTGCTCCAGCTGACTTCGCAAAAT
ATTGAAATCAAGCTAGTGAGTGATGTAACAGCTGATTCAAAGGTATTAGAAGCCTTGAAA
TTAAAGGGAGCCGAGGTGACGTACATGAACATGACCGCTTACAACAAGGGCCGGCTGCAG
TCCTCCTTCTGGATCGTGGACAAACAGCACGTGTATATCGGCAGTGCCGGTTTGGACTGG
CAATCCCTGGGACAGATGAAAGAACTCGGTGTCATCTTCTACAACTGCAGCTGCCTGGTC
CTAGATTTACAAAGGATATTTGCTCTATATAGTTCATTAAAATTCAAAAGCAGAGTGCCT
CAAACCTGGTCCAAAAGACTCTATGGAGTCTATGACAATGAAAAGAAATTGCAACTTCAG
TTGAATGAAACCAAATCTCAAGCATTTGTATCGAATTCTCCAAAACTCTTTTGCCCTAAA
AACAGAAGTTTTGACATAGATGCCATCTACAGTGTGATAGATGATGCCAAGCAGTATGTG
TACATCGCTGTCATGGACTACCTGCCTATCTCCAGCACAAGCACCAAAAGGACTTACTGG
CCAGACTTGGATGCAAAAATAAGAGAAGCATTAGTTTTACGAAGCGTTAGAGTTCGACTC
CTTTTAAGCTTCTGGAAGGAAACTGATCCCCTTACGTTTAACTTTATTTCATCTCTTAAA
GCGATTTGCACTGAAATAGCCAACTGCAGTTTGAAAGTTAAATTTTTTGATCTGGAAAGA
GAGAATGCTTGTGCTACAAAAGAACAAAAGAATCACACCTTTCCTAGGTTAAATCGCAAC
AAGTACATGGTGACAGATGGAGCAGCTTATATTGGAAATTTTGATTGGGTAGGGAATGAT
TTCACTCAGAATGCTGGCACGGGCCTTGTTATCAACCAGGCAGATGTGAGGAACAACAGA
AGCATCATTAAGCAACTTAAAGATGTGTTTGAAAGGGACTGGTATTCACCGTATGCCAAA
ACCTTACAGCCAACCAAACAGCCGAACTGCTCAAGCCTGTTCAAACTCAAACCCCTCTCC
AACAAAACTGCCACAGACGACACAGGCGGAAAGGATCCCCGGAACGTATAA
|
| Enzyme 57 GenBank Gene ID |
NM_152666.2  |
| Enzyme 57 GeneCard ID |
PLD5  |
| Enzyme 57 GenAtlas ID |
PLD5  |
| Enzyme 57 HGNC ID |
HGNC:26879  |
| Enzyme 57 Chromosome Location |
1 |
| Enzyme 57 Locus |
1q43 |
| Enzyme 57 SNPs |
SNPJam Report  |
| Enzyme 57 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
]
- 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 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
12914 |
| Enzyme 58 Name |
Phosphatidylcholine transfer protein |
| Enzyme 58 Synonyms |
- PC-TP
- START domain-containing protein 2
- StARD2
- StAR-related lipid transfer protein 2
|
| Enzyme 58 Gene Name |
PCTP |
| Enzyme 58 Protein Sequence |
>Phosphatidylcholine transfer protein
MELAAGSFSEEQFWEACAELQQPALAGADWQLLVETSGISIYRLLDKKTGLYEYKVFGVL
EDCSPTLLADIYMDSDYRKQWDQYVKELYEQECNGETVVYWEVKYPFPMSNRDYVYLRQR
RDLDMEGRKIHVILARSTSMPQLGERSGVIRVKQYKQSLAIESDGKKGSKVFMYYFDNPG
GQIPSWLINWAAKNGVPNFLKDMARACQNYLKKT
|
| Enzyme 58 Number of Residues |
214 |
| Enzyme 58 Molecular Weight |
24843.1 |
| Enzyme 58 Theoretical pI |
5.44 |
| Enzyme 58 GO Classification |
Not Available |
| Enzyme 58 General Function |
Involved in phosphatidylcholine binding |
| Enzyme 58 Specific Function |
Catalyzes the transfer of phosphatidylcholine between membranes. Binds a single lipid molecule |
| Enzyme 58 Pathways |
Not Available |
| Enzyme 58 Reactions |
Not Available |
| Enzyme 58 Pfam Domain Function |
|
| Enzyme 58 Signals |
|
| Enzyme 58 Transmembrane Regions |
|
| Enzyme 58 Essentiality |
Not Available |
| Enzyme 58 GenBank ID Protein |
156151415  |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
Q9UKL6  |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
PPCT_HUMAN  |
| Enzyme 58 PDB ID |
1LN1  |
| Enzyme 58 PDB File |
Show |
| Enzyme 58 3D Structure |
|
| Enzyme 58 Cellular Location |
Not Available |
| Enzyme 58 Gene Sequence |
>645 bp
ATGGAGCTGGCCGCCGGAAGCTTCTCGGAGGAGCAGTTCTGGGAGGCCTGCGCCGAGCTC
CAGCAGCCCGCTCTGGCCGGGGCCGACTGGCAGCTCCTAGTGGAGACCTCGGGCATCAGC
ATCTACCGGCTGCTGGACAAGAAGACTGGACTTTATGAGTATAAAGTCTTTGGTGTTCTG
GAGGACTGCTCACCAACTCTACTGGCAGACATCTATATGGACTCAGATTACAGAAAACAA
TGGGACCAGTATGTTAAAGAACTCTATGAACAAGAATGCAACGGAGAGACTGTGGTCTAC
TGGGAAGTGAAGTACCCTTTTCCCATGTCCAACAGAGACTATGTCTACCTTCGGCAGCGG
CGAGACCTGGACATGGAAGGGAGGAAGATCCATGTGATCCTGGCCCGGAGCACCTCCATG
CCTCAGCTTGGCGAGAGGTCTGGGGTGATCCGGGTGAAGCAATACAAGCAGAGCCTGGCG
ATCGAGAGTGACGGCAAGAAGGGGAGCAAAGTTTTCATGTATTACTTCGATAACCCGGGT
GGCCAAATTCCGTCCTGGCTCATTAACTGGGCCGCCAAGAATGGAGTTCCTAACTTCTTG
AAAGACATGGCAAGAGCCTGTCAGAACTACCTCAAGAAAACCTAA
|
| Enzyme 58 GenBank Gene ID |
NM_021213.3  |
| Enzyme 58 GeneCard ID |
PCTP  |
| Enzyme 58 GenAtlas ID |
PCTP  |
| Enzyme 58 HGNC ID |
HGNC:8752  |
| Enzyme 58 Chromosome Location |
1 |
| Enzyme 58 Locus |
17q21-q24 |
| Enzyme 58 SNPs |
SNPJam Report  |
| Enzyme 58 General References |
- van Helvoort A, de Brouwer A, Ottenhoff R, Brouwers JF, Wijnholds J, Beijnen JH, Rijneveld A, van der Poll T, van der Valk MA, Majoor D, Voorhout W, Wirtz KW, Elferink RP, Borst P: Mice without phosphatidylcholine transfer protein have no defects in the secretion of phosphatidylcholine into bile or into lung airspaces. Proc Natl Acad Sci U S A. 1999 Sep 28;96(20):11501-6. [PubMed
]
- Cohen DE, Green RM, Wu MK, Beier DR: Cloning, tissue-specific expression, gene structure and chromosomal localization of human phosphatidylcholine transfer protein. Biochim Biophys Acta. 1999 Oct 28;1447(2-3):265-70. [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
]
- Chan WW, Roderick SL, Cohen DE: Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data. Biochim Biophys Acta. 2002 Apr 1;1596(1):1-5. [PubMed
]
- Roderick SL, Chan WW, Agate DS, Olsen LR, Vetting MW, Rajashankar KR, Cohen DE: Structure of human phosphatidylcholine transfer protein in complex with its ligand. Nat Struct Biol. 2002 Jul;9(7):507-11. [PubMed
]
|
| Enzyme 58 Metabolite References |
Not Available |
|
Enzyme 59
[top]
|
| Enzyme 59 ID |
12915 |
| Enzyme 59 Name |
Phospholipid scramblase 2 |
| Enzyme 59 Synonyms |
- PL scramblase 2
- Ca(2+)-dependent phospholipid scramblase 2
|
| Enzyme 59 Gene Name |
PLSCR2 |
| Enzyme 59 Protein Sequence |
>Phospholipid scramblase 2
MPAPPPPLNCPPGLEYLSQIDMILIHQQIELLEVLFSFESSNMYEIKNSFGQRIYFAAED
TNFCIRNCCGRSRPFTLRITDNVGREVITLERPLRCNCCCCPCCLQEIEIQAPPGVPVGY
VTQTWHPCLTKFTIKNQKREDVLKISGPCIVCSCIAGVDFEITSLDEQIVVGRISKHWSG
FLREAFTDADNFGIQFPRDLDVKMKAVMIGACFLIDYMFFERTR
|
| Enzyme 59 Number of Residues |
224 |
| Enzyme 59 Molecular Weight |
25522.5 |
| Enzyme 59 Theoretical pI |
5.34 |
| Enzyme 59 GO Classification |
Not Available |
| Enzyme 59 General Function |
Involved in calcium ion binding |
| Enzyme 59 Specific Function |
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system |
| Enzyme 59 Pathways |
Not Available |
| Enzyme 59 Reactions |
Not Available |
| Enzyme 59 Pfam Domain Function |
|
| Enzyme 59 Signals |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
9651165  |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
Q9NRY7  |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
PLS2_HUMAN  |
| Enzyme 59 PDB ID |
Not Available |
| Enzyme 59 Cellular Location |
Not Available |
| Enzyme 59 Gene Sequence |
>675 bp
ATGCCAGCACCACCACCACCATTAAACTGTCCGCCAGGATTGGAATACTTAAGTCAGATA
GATATGATACTAATTCATCAGCAAATTGAACTTCTGGAAGTTCTATTCAGTTTTGAAAGT
AGTAACATGTATGAAATCAAGAACAGCTTTGGGCAGAGGATTTATTTTGCAGCAGAAGAT
ACTAATTTCTGTATCCGAAATTGCTGTGGGCGGTCTAGACCTTTTACCTTGAGGATTACT
GATAATGTGGGTCGAGAAGTCATAACTCTGGAAAGACCACTAAGATGTAACTGTTGTTGT
TGCCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGTGTACCAGTAGGTTAT
GTTACTCAGACCTGGCACCCATGTCTAACAAAGTTTACAATTAAAAATCAGAAAAGAGAG
GATGTACTAAAAATTAGTGGTCCATGTATCGTGTGCAGCTGTATTGCGGGTGTTGATTTT
GAGATTACATCTCTTGATGAACAAATTGTGGTTGGCAGGATTTCTAAGCACTGGTCTGGG
TTTTTAAGAGAGGCATTTACTGATGCTGACAACTTTGGAATCCAATTCCCTAGAGACCTT
GATGTTAAAATGAAAGCCGTGATGATTGGTGCCTGTTTCCTCATTGACTACATGTTTTTT
GAAAGAACTAGGTAA
|
| Enzyme 59 GenBank Gene ID |
AF159441  |
| Enzyme 59 GeneCard ID |
PLSCR2  |
| Enzyme 59 GenAtlas ID |
PLSCR2  |
| Enzyme 59 HGNC ID |
HGNC:16494  |
| Enzyme 59 Chromosome Location |
3 |
| Enzyme 59 Locus |
3q24 |
| Enzyme 59 SNPs |
SNPJam Report  |
| Enzyme 59 General References |
- Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [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 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
12916 |
| Enzyme 60 Name |
Phospholipid scramblase 3 |
| Enzyme 60 Synonyms |
- PL scramblase 3
- Ca(2+)-dependent phospholipid scramblase 3
|
| Enzyme 60 Gene Name |
PLSCR3 |
| Enzyme 60 Protein Sequence |
>Phospholipid scramblase 3
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVAL
GSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAA
EESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTI
GHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQW
GGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAVTS
|
| Enzyme 60 Number of Residues |
295 |
| Enzyme 60 Molecular Weight |
31648.1 |
| Enzyme 60 Theoretical pI |
6.63 |
| Enzyme 60 GO Classification |
Not Available |
| Enzyme 60 General Function |
Involved in calcium ion binding |
| Enzyme 60 Specific Function |
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system |
| Enzyme 60 Pathways |
Not Available |
| Enzyme 60 Reactions |
Not Available |
| Enzyme 60 Pfam Domain Function |
|
| Enzyme 60 Signals |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
31543417  |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
Q9NRY6  |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
PLS3_HUMAN  |
| Enzyme 60 PDB ID |
Not Available |
| Enzyme 60 Cellular Location |
Not Available |
| Enzyme 60 Gene Sequence |
>888 bp
ATGGCAGGCTACTTGCCCCCCAAAGGCTACGCCCCTTCGCCCCCACCTCCCTACCCTGTC
ACCCCTGGGTACCCGGAGCCGGCGCTACATCCTGGGCCCGGGCAGGCGCCAGTGCCCGCC
CAGGTACCTGCCCCAGCTCCCGGCTTCGCCCTCTTCCCCTCGCCTGGCCCCGTGGCCTTG
GGGTCTGCTGCCCCCTTCTTGCCACTGCCAGGGGTGCCTTCTGGCCTCGAATTCCTGGTG
CAGATTGATCAGATTTTGATTCACCAGAAGGCTGAGCGAGTGGAAACGTTCCTAGGCTGG
GAGACCTGTAATCGGTATGAACTGCGCTCTGGGGCCGGGCAGCCCCTGGGTCAGGCGGCC
GAGGAGAGCAACTGCTGCGCCCGTCTGTGCTGTGGCGCCCGCCGGCCGCTGCGTGTCCGC
CTGGCCGACCCCGGGGACCGTGAGGTGCTGCGTTTGCTCCGCCCGCTGCACTGTGGCTGC
AGCTGCTGCCCCTGTGGCCTCCAGGAGATGGAAGTACAGGCTCCACCAGGCACCACCATT
GGCCACGTGCTACAGACCTGGCATCCCTTCCTCCCCAAGTTCTCCATCCAGGATGCCGAT
CGCCAGACAGTCTTGCGAGTGGTGGGGCCCTGCTGGACCTGTGGCTGTGGCACAGACACC
AACTTTGAGGTGAAGACTCGGGATGAATCCCGCAGTGTGGGCCGCATCAGCAAGCAGTGG
GGGGGCCTGGTCCGAGAAGCCCTCACAGATGCAGATGACTTTGGCCTACAGTTCCCGCTG
GACCTGGATGTGAGGGTGAAGGCTGTGCTGCTGGGAGCCACATTCCTCATTGACTACATG
TTCTTTGAGAAGCGAGGAGGCGCTGGGCCCTCTGCCGTCACCAGTTAG
|
| Enzyme 60 GenBank Gene ID |
NM_020360.2  |
| Enzyme 60 GeneCard ID |
PLSCR3  |
| Enzyme 60 GenAtlas ID |
PLSCR3  |
| Enzyme 60 HGNC ID |
HGNC:16495  |
| Enzyme 60 Chromosome Location |
1 |
| Enzyme 60 Locus |
17p13.1 |
| Enzyme 60 SNPs |
SNPJam Report  |
| Enzyme 60 General References |
- Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [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
]
- 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
]
- Shibata H, Suzuki H, Kakiuchi T, Inuzuka T, Yoshida H, Mizuno T, Maki M: Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants. J Biol Chem. 2008 Apr 11;283(15):9623-32. Epub 2008 Feb 6. [PubMed
]
|
| Enzyme 60 Metabolite References |
Not Available |
|
Enzyme 61
[top]
|
| Enzyme 61 ID |
12917 |
| Enzyme 61 Name |
Phospholipid scramblase 4 |
| Enzyme 61 Synonyms |
- PL scramblase 4
- Ca(2+)-dependent phospholipid scramblase 4
- Cell growth-inhibiting gene 43 protein
- TRA1
|
| Enzyme 61 Gene Name |
PLSCR4 |
| Enzyme 61 Protein Sequence |
>Phospholipid scramblase 4
MSGVVPTAPEQPAGEMENQTKPPDPRPDAPPEYNSHFLPGPPGTAVPPPTGYPGGLPMGY
YSPQQPSTFPLYQPVGGIHPVRYQPGKYPMPNQSVPITWMPGPTPMANCPPGLEYLVQLD
NIHVLQHFEPLEMMTCFETNNRYDIKNNSDQMVYIVTEDTDDFTRNAYRTLRPFVLRVTD
CMGREIMTMQRPFRCTCCCFCCPSARQELEVQCPPGVTIGFVAEHWNLCRAVYSIQNEKK
ENVMRVRGPCSTYGCGSDSVFEVKSLDGISNIGSIIRKWNGLLSAMADADHFDIHFPLDL
DVKMKAMIFGACFLIDFMYFERSPPQRSR
|
| Enzyme 61 Number of Residues |
329 |
| Enzyme 61 Molecular Weight |
37005.2 |
| Enzyme 61 Theoretical pI |
5.62 |
| Enzyme 61 GO Classification |
Not Available |
| Enzyme 61 General Function |
Involved in calcium ion binding |
| Enzyme 61 Specific Function |
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system |
| Enzyme 61 Pathways |
Not Available |
| Enzyme 61 Reactions |
Not Available |
| Enzyme 61 Pfam Domain Function |
|
| Enzyme 61 Signals |
|
| Enzyme 61 Transmembrane Regions |
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
9622872  |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
Q9NRQ2  |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
PLS4_HUMAN  |
| Enzyme 61 PDB ID |
Not Available |
| Enzyme 61 Cellular Location |
Not Available |
| Enzyme 61 Gene Sequence |
>990 bp
ATGTCAGGTGTGGTACCCACAGCCCCTGAACAGCCTGCAGGTGAAATGGAAAATCAAACA
AAACCACCAGATCCAAGGCCTGATGCTCCTCCTGAATACAGTTCTCATTTTTTACCAGGA
CCCCCTGGAACAGCTGTCCCTCCACCTACTGGCTACCCAGGAGGCTTGCCTATGGGATAC
TACAGTCCACAGCAACCCAGTACCTTCCCTTTGTACCAGCCAGTTGGTGGTATCCATCCT
GTCCGGTATCAGCCTGGCAAATATCCTATGCCAAATCAGTCTGTTCCAATAACATGGATG
CCAGGGCCAACTCCTATGGCAAACTGCCCTCCTGGTCTGGAATACTTAGTTCAGTTGGAC
AACATACATGTTCTTCAGCATTTTGAGCCTCTGGAAATGATGACATGTTTTGAAACTAAT
AATAGATATGATATTAAAAACAACTCAGACCAGATGGTTTACGTTGTAACCGAAGACACA
GATGACTTTACCAGGAATGCCTATCGGACACTAAGGCCCTTCGTCCTCCGGGTCACTGAT
TGTATGGGCCGAGAAATCATGACAATGCAGAGACCCTTCAGATGCACCTGCTGTTGCTTC
TGTTGCCCCTCTGCCAGACAAGAGCTGGAGGTGCAGTGTCCTCCTGGTGTCACCATTGGC
TTTGTTGCGGAACATTGGAACCTGTGCAGGGCGGTGTACAGCATCCAAAATGAGAAGAAA
GAAAATGTGATGAGAGTTCGTGGGCCATGCTCAACCTATGGCTGTGGTTCAGATTCTGTT
TTTGAGGTCAAATCCCTTGATGGCATATCCAACATCGGCAGTATTATCCGGAAGTGGAAT
GGTTTGTTATCAGCAATGGCAGATGCTGACCATTTTGACATTCACTTCCCACTAGACCTG
GATGTGAAGATGAAAGCCATGATTTTTGGAGCTTGCTTCCTCATTGACTTCATGTATTTT
GAAAGATCTCCACCACAACGTTCAAGATAG
|
| Enzyme 61 GenBank Gene ID |
AF199023  |
| Enzyme 61 GeneCard ID |
PLSCR4  |
| Enzyme 61 GenAtlas ID |
PLSCR4  |
| Enzyme 61 HGNC ID |
HGNC:16497  |
| Enzyme 61 Chromosome Location |
3 |
| Enzyme 61 Locus |
3q24 |
| Enzyme 61 SNPs |
SNPJam Report  |
| Enzyme 61 General References |
- Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [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
]
- 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
]
- Shibata H, Suzuki H, Kakiuchi T, Inuzuka T, Yoshida H, Mizuno T, Maki M: Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants. J Biol Chem. 2008 Apr 11;283(15):9623-32. Epub 2008 Feb 6. [PubMed
]
|
| Enzyme 61 Metabolite References |
Not Available |
|
Enzyme 62
[top]
|
| Enzyme 62 ID |
12918 |
| Enzyme 62 Name |
Phospholipid scramblase family member 5 |
| Enzyme 62 Synonyms |
Not Available |
| Enzyme 62 Gene Name |
PLSCR5 |
| Enzyme 62 Protein Sequence |
>Phospholipid scramblase family member 5
MASKDAQNQRRGLPGFLPGAPDPDQSLPASSNPGNQAWQLSLPLPSSFLPTVSLPPGLEY
LSQLDLIIIHQQVELLGMILGTETSNKYEIKNSLGQRIYFAVEESICFNRTFCSTLRSCT
LRITDNSGREVITVNRPLRCNSCWCPCYLQELEIQAPPGTIVGYVTQKWDPFLPKFTIQN
ANKEDILKIVGPCVTCGCFGDVDFEVKTINEKLTIGKISKYWSGFVNDVFTNADNFGIHV
PADLDVTVKAAMIGACFLFDFMFFEHSLAGL
|
| Enzyme 62 Number of Residues |
271 |
| Enzyme 62 Molecular Weight |
30026.2 |
| Enzyme 62 Theoretical pI |
4.90 |
| Enzyme 62 GO Classification |
Not Available |
| Enzyme 62 General Function |
Not Available |
| Enzyme 62 Specific Function |
Not Available |
| Enzyme 62 Pathways |
Not Available |
| Enzyme 62 Reactions |
Not Available |
| Enzyme 62 Pfam Domain Function |
|
| Enzyme 62 Signals |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
146229354  |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
A0PG75  |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
PLS5_HUMAN  |
| Enzyme 62 PDB ID |
Not Available |
| Enzyme 62 Cellular Location |
Not Available |
| Enzyme 62 Gene Sequence |
>816 bp
ATGGCCTCTAAAGATGCCCAGAACCAAAGAAGAGGTCTGCCTGGTTTTCTTCCTGGAGCT
CCAGACCCAGACCAAAGCCTTCCTGCCTCTTCCAATCCAGGGAACCAAGCATGGCAGCTG
AGTCTCCCTCTGCCAAGCAGTTTCCTGCCAACAGTCAGTCTCCCTCCTGGTCTAGAATAT
TTAAGCCAGTTAGACCTGATAATTATACACCAGCAGGTGGAGCTGCTTGGAATGATACTT
GGTACTGAGACCTCCAACAAATATGAGATTAAAAACAGCTTGGGACAAAGAATTTACTTT
GCAGTGGAGGAAAGCATCTGCTTCAATCGTACTTTCTGTTCCACTCTGCGATCTTGCACC
CTGAGGATCACAGATAACTCAGGTCGAGAGGTCATTACAGTGAACAGGCCCTTGAGATGT
AACAGCTGCTGGTGCCCTTGCTACCTACAAGAGTTAGAAATCCAAGCCCCTCCTGGTACT
ATAGTTGGTTACGTTACGCAGAAGTGGGACCCCTTTCTGCCTAAATTCACAATCCAAAAT
GCAAACAAAGAAGATATTTTGAAAATTGTTGGTCCTTGTGTGACATGTGGCTGTTTTGGC
GATGTGGATTTTGAGGTGAAAACCATTAATGAAAAGCTTACAATTGGGAAGATTTCAAAG
TACTGGTCAGGATTTGTAAATGATGTCTTCACAAATGCTGACAATTTCGGAATTCATGTT
CCTGCAGATCTAGATGTAACAGTCAAAGCAGCAATGATCGGTGCCTGTTTTCTCTTTGAT
TTTATGTTCTTTGAACATTCACTGGCTGGATTATAA
|
| Enzyme 62 GenBank Gene ID |
NM_001085420.1  |
| Enzyme 62 GeneCard ID |
PLSCR5  |
| Enzyme 62 GenAtlas ID |
PLSCR5  |
| Enzyme 62 HGNC ID |
HGNC:19952  |
| Enzyme 62 Chromosome Location |
3 |
| Enzyme 62 Locus |
3q24 |
| Enzyme 62 SNPs |
SNPJam Report  |
| Enzyme 62 General References |
- 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
]
|
| Enzyme 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
12919 |
| Enzyme 63 Name |
Probable phospholipid-transporting ATPase VB |
| Enzyme 63 Synonyms |
- ATPase class V type 10B
|
| Enzyme 63 Gene Name |
ATP10B |
| Enzyme 63 Protein Sequence |
>Probable phospholipid-transporting ATPase VB
MALSVDSSWHRWQWRVRDGFPHCPSETTPLLSPEKGRQSYNLTQQRVVFPNNSIFHQDWE
EVSRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITML
PLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKC
NEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELFHNTIVC
EKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNS
GPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFLPS
ALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNI
AEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLETPKELDSDGEEWTQY
QCLSFSARWAQDPATMRSQKGAQPLRRSQSARVPIQGHYRQRSMGHRESSQPPVAFSSSI
EKDVTPDKNLLTKVRDAALWLETLSDSRPAKASLSTTSSIADFFLALTICNSVMVSTTTE
PRQRVTIKPSSKALGTSLEKIQQLFQKLKLLSLSQSFSSTAPSDTDLGESLGANVATTDS
DERDDASVCSGGDSTDDGGYRSSMWDQGDILESGSGTSLEEALEAPATDLARPEFCYEAE
SPDEAALVHAAHAYSFTLVSRTPEQVTVRLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHP
LTGEIVVYTKGADSVIMDLLEDPACVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIA
KKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDT
IATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEEL
KQFRELQKPDRKLFGFRLPSKTPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQ
YCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQA
VMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSST
MIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMV
DAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTIFHGVVLLG
SFLMYFLVSLLYNATCVICNSPTNPYWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQ
GTCGKSLISKAQKIDKLPPDKRNLEIQSWRSRQRPAPVPEVARPTHHPVSSITGQDFSAS
TPKSSNPPKRKHVEESVLHEQRCGTECMRDDSCSGDSSAQLSSGEHLLGPNRIMAYSRGQ
TDMCRCSKRSSHRRSQSSLTI
|
| Enzyme 63 Number of Residues |
1461 |
| Enzyme 63 Molecular Weight |
165388.9 |
| Enzyme 63 Theoretical pI |
6.87 |
| Enzyme 63 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 63 General Function |
Involved in ATP binding |
| Enzyme 63 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 63 Pathways |
Not Available |
| Enzyme 63 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 63 Pfam Domain Function |
|
| Enzyme 63 Signals |
|
| Enzyme 63 Transmembrane Regions |
- 83-104
111-132
317-338
369-390
1112-1132
1145-1164
1195-1216
1224-1246
1253-1273
1292-1316
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
149944474  |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
O94823  |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
AT10B_HUMAN  |
| Enzyme 63 PDB ID |
Not Available |
| Enzyme 63 Cellular Location |
Not Available |
| Enzyme 63 Gene Sequence |
>4386 bp
ATGGCCCTCTCAGTGGACTCATCGTGGCATCGGTGGCAGTGGAGAGTCAGAGATGGCTTC
CCCCATTGTCCATCGGAAACCACACCGCTGCTCTCTCCAGAGAAAGGGAGACAGAGCTAC
AACTTGACACAGCAGCGGGTCGTGTTCCCCAACAACAGCATATTCCATCAAGATTGGGAA
GAGGTCTCCAGGAGATACCCTGGCAACAGAACCTGCACAACCAAATACACCCTCTTCACC
TTCCTGCCCCGGAATCTCTTTGAGCAATTTCATAGATGGGCTAACCTCTATTTCCTGTTC
CTGGTGATTTTGAACTGGATGCCCTCCATGGAAGTCTTCCACAGAGAAATCACCATGTTA
CCATTGGCCATTGTCCTGTTCGTCATCATGATCAAGGATGGCATGGAGGACTTCAAGAGA
CACCGCTTTGATAAAGCAATAAACTGCTCCAACATTCGAATTTATGAAAGAAAAGAGCAG
ACCTATGTGCAGAAGTGCTGGAAGGATGTGCGCGTGGGAGACTTCATCCAAATGAAATGC
AATGAGATTGTCCCAGCAGACATACTCCTCCTTTTTTCCTCTGACCCCAATGGGATATGC
CATCTGGAAACTGCCAGCTTGGATGGAGAGACAAACCTCAAGCAAAGATGTGTCGTGAAG
GGCTTCTCACAGCAGGAGGTACAGTTCGAACCAGAGCTTTTCCACAATACCATCGTGTGT
GAGAAACCCAACAACCACCTCAACAAATTTAAGGGTTATATGGAGCATCCTGACCAGACC
AGGACTGGCTTTGGCTGTGAGAGTCTTCTGCTTCGAGGCTGCACCATCAGAAACACCGAG
ATGGCTGTTGGCATTGTCATCTATGCAGGCCATGAGACGAAAGCCATGCTGAACAACAGT
GGCCCCCGGTACAAACGCAGCAAGATTGAGCGGCGCATGAATATAGACATCTTCTTCTGC
ATTGGGATCCTCATCCTCATGTGCCTTATTGGAGCTGTAGGTCACAGCATCTGGAATGGG
ACCTTTGAAGAACACCCTCCCTTCGATGTGCCAGATGCCAATGGCAGCTTCCTTCCCAGT
GCCCTTGGGGGCTTCTACATGTTCCTCACAATGATCATCCTGCTCCAGGTGCTGATCCCC
ATCTCTTTGTATGTCTCCATTGAGCTGGTGAAGCTCGGGCAAGTGTTCTTCTTGAGCAAT
GACCTTGACCTGTATGATGAAGAGACCGATTTATCCATTCAATGTCGAGCCCTCAACATC
GCAGAGGACTTGGGCCAGATCCAGTACATCTTCTCCGATAAGACGGGGACCCTGACAGAG
AACAAGATGGTGTTCCGACGTTGCACCATCATGGGCAGCGAGTATTCTCACCAAGAAAAT
GCTAAGCGACTGGAGACCCCAAAGGAGCTGGACTCAGATGGTGAAGAGTGGACCCAATAC
CAATGCCTGTCCTTCTCGGCTAGATGGGCCCAGGATCCAGCAACTATGAGAAGCCAAAAA
GGTGCTCAGCCTCTGAGGAGGAGCCAGAGTGCCCGGGTGCCCATCCAGGGCCACTACCGG
CAAAGGTCTATGGGGCACCGTGAAAGCTCACAGCCTCCTGTGGCCTTCAGCAGCTCCATA
GAAAAAGATGTAACTCCAGATAAAAACCTACTGACCAAGGTTCGAGATGCTGCCCTGTGG
TTGGAGACCTTGTCAGACAGCAGACCTGCCAAGGCTTCCCTCTCCACCACCTCCTCCATT
GCTGATTTCTTCCTTGCCTTAACCATCTGCAACTCTGTCATGGTGTCCACAACCACCGAG
CCCAGGCAGAGGGTCACCATCAAACCCTCAAGCAAGGCTCTGGGGACGTCCCTGGAGAAG
ATTCAGCAGCTCTTCCAGAAGTTGAAGCTATTGAGCCTCAGCCAGTCATTCTCATCCACT
GCACCCTCTGACACAGACCTCGGGGAGAGCTTAGGGGCCAACGTGGCCACCACAGACTCG
GATGAGAGAGATGATGCATCTGTGTGCAGTGGAGGTGACTCCACTGATGACGGTGGCTAC
AGGAGCAGCATGTGGGACCAGGGCGACATCCTGGAGTCTGGGTCAGGCACTTCCTTGGAG
GAGGCATTGGAGGCCCCAGCCACAGACCTGGCCAGGCCTGAGTTCTGTTACGAGGCTGAG
AGCCCTGATGAGGCCGCCCTGGTGCACGCTGCCCATGCCTACAGCTTCACACTAGTGTCC
CGGACACCTGAGCAGGTGACTGTGCGCCTGCCCCAGGGCACCTGCCTCACCTTCAGCCTC
CTCTGCACCCTGGGCTTTGACTCTGTCAGGAAGAGAATGTCTGTGGTTGTGAGGCACCCA
CTGACTGGCGAGATTGTTGTCTACACCAAGGGTGCTGACTCGGTCATCATGGACCTGCTG
GAAGACCCAGCCTGCGTACCTGACATTAATATGGAAAAGAAGCTGAGAAAAATCCGAGCC
CGGACCCAAAAGCATCTAGACTTGTATGCAAGAGATGGCCTGCGCACACTATGCATTGCC
AAGAAGGTTGTAAGCGAAGAGGACTTCCGGAGATGGGCCAGTTTCCGGCGTGAGGCTGAG
GCATCCCTCGACAACCGAGATGAGCTTCTCATGGAAACTGCACAGCATCTGGAGAATCAA
CTCACCTTACTTGGAGCCACTGGGATCGAAGACCGGCTGCAGGAAGGAGTTCCAGATACG
ATTGCCACTCTGCGGGAGGCTGGGATCCAGCTCTGGGTCCTGACTGGAGATAAGCAGGAG
ACAGCGGTCAACATTGCCCATTCCTGCAGACTGTTAAATCAGACCGACACTGTTTATACC
ATCAATACAGAGAATCAGGAGACCTGTGAATCCATCCTCAATTGTGCATTGGAAGAGCTA
AAGCAATTTCGTGAACTACAGAAGCCAGACCGCAAGCTCTTTGGATTCCGCTTACCTTCC
AAGACACCATCCATCACCTCAGAAGCTGTGGTTCCAGAAGCTGGATTGGTCATCGATGGG
AAGACATTGAATGCCATCTTCCAGGGAAAGCTAGAGAAGAAGTTTCTGGAATTGACCCAG
TATTGTCGGTCCGTCCTGTGCTGCCGCTCCACGCCACTCCAGAAGAGTATGATAGTCAAG
CTGGTGCGAGACAAGTTGCGCGTCATGACCCTTTCCATAGGTGATGGAGCAAATGATGTA
AGCATGATTCAAGCTGCTGATATTGGAATTGGAATATCTGGACAGGAAGGCATGCAGGCT
GTCATGTCCAGCGACTTTGCCATCACCCGCTTTAAGCATCTCAAGAAGTTGCTGCTCGTG
CATGGCCACTGGTGTTACTCGCGCCTGGCCAGGATGGTGGTGTACTACCTCTACAAGAAC
GTGTGCTACGTCAACCTGCTCTTCTGGTATCAGTTCTTCTGTGGTTTCTCCAGCTCCACC
ATGATTGATTACTGGCAGATGATATTCTTCAATCTCTTCTTTACCTCCTTGCCTCCTCTT
GTCTTTGGAGTCCTTGACAAAGACATCTCTGCAGAAACACTCCTGGCATTGCCTGAGCTA
TACAAGAGTGGCCAGAACTCTGAGTGCTATAACCTGTCGACTTTCTGGATTTCTATGGTG
GATGCATTCTACCAGAGCCTCATCTGTTTCTTTATCCCTTACCTGGCCTATAAGGGCTCT
GATATAGATGTCTTTACCTTTGGGACACCAATCAACACCATCTCCCTCACCACAATCCTT
TTGCACCAGGCAATGGAAATGAAGACATGGACCATTTTCCACGGAGTCGTGCTCCTCGGC
AGCTTCCTGATGTACTTTCTGGTATCCCTCCTGTACAATGCCACCTGCGTCATCTGCAAC
AGCCCCACCAATCCCTATTGGGTGATGGAAGGCCAGCTCTCAAACCCCACTTTCTACCTC
GTCTGCTTTCTCACACCAGTTGTTGCTCTTCTCCCAAGATACTTTTTCCTGTCTCTGCAA
GGAACTTGTGGGAAGTCTCTAATCTCAAAAGCTCAGAAAATTGACAAACTCCCCCCAGAC
AAAAGAAACCTGGAAATCCAGAGTTGGAGAAGCAGACAGAGGCCTGCCCCTGTCCCCGAA
GTGGCTCGACCAACTCACCACCCAGTGTCATCTATCACAGGACAGGACTTCAGTGCCAGC
ACCCCAAAGAGCTCTAACCCTCCCAAGAGGAAGCATGTGGAAGAGTCAGTACTCCACGAA
CAGAGATGTGGCACGGAGTGCATGAGGGATGACTCATGCTCAGGGGACTCCTCAGCTCAA
CTCTCATCCGGGGAGCACCTGCTGGGACCTAACAGGATAATGGCCTACTCAAGAGGACAG
ACTGATATGTGCCGGTGCTCAAAGAGGAGCAGCCATCGCCGATCCCAGAGTTCACTGACC
ATATGA
|
| Enzyme 63 GenBank Gene ID |
NM_025153.2  |
| Enzyme 63 GeneCard ID |
ATP10B  |
| Enzyme 63 GenAtlas ID |
ATP10B  |
| Enzyme 63 HGNC ID |
HGNC:13543  |
| Enzyme 63 Chromosome Location |
5 |
| Enzyme 63 Locus |
5q34 |
| Enzyme 63 SNPs |
SNPJam Report  |
| Enzyme 63 General References |
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [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
]
- 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
]
|
| Enzyme 63 Metabolite References |
Not Available |
|
Enzyme 64
[top]
|
| Enzyme 64 ID |
12920 |
| Enzyme 64 Name |
Probable phospholipid-transporting ATPase ID |
| Enzyme 64 Synonyms |
- ATPase class I type 8B member 2
|
| Enzyme 64 Gene Name |
ATP8B2 |
| Enzyme 64 Protein Sequence |
>Probable phospholipid-transporting ATPase ID
MTVPKEMPEKWARAQAPPSWSRKKPSWGTEEERRARANDREYNEKFQYASNCIKTSKYNI
LTFLPVNLFEQFQEVANTYFLFLLILQLIPQISSLSWFTTIVPLVLVLTITAVKDATDDY
FRHKSDNQVNNRQSQVLINGILQQEQWMNVCVGDIIKLENNQFVAADLLLLSSSEPHGLC
YIETAELDGETNMKVRQAIPVTSELGDISKLAKFDGEVICEPPNNKLDKFSGTLYWKENK
FPLSNQNMLLRGCVLRNTEWCFGLVIFAGPDTKLMQNSGRTKFKRTSIDRLMNTLVLWIF
GFLVCMGVILAIGNAIWEHEVGMRFQVYLPWDEAVDSAFFSGFLSFWSYIIILNTVVPIS
LYVSVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVEYIFSDKTGTLTQNI
MVFNKCSINGHSYGDVFDVLGHKAELGERPEPVDFSFNPLADKKFLFWDPSLLEAVKIGD
PHTHEFFRLLSLCHTVMSEEKNEGELYYKAQSPDEGALVTAARNFGFVFRSRTPKTITVH
EMGTAITYQLLAILDFNNIRKRMSVIVRNPEGKIRLYCKGADTILLDRLHHSTQELLNTT
MDHLNEYAGEGLRTLVLAYKDLDEEYYEEWAERRLQASLAQDSREDRLASIYEEVENNMM
LLGATAIEDKLQQGVPETIALLTLANIKIWVLTGDKQETAVNIGYSCKMLTDDMTEVFIV
TGHTVLEVREELRKAREKMMDSSRSVGNGFTYQDKLSSSKLTSVLEAVAGEYALVINGHS
LAHALEADMELEFLETACACKAVICCRVTPLQKAQVVELVKKYKKAVTLAIGDGANDVSM
IKTAHIGVGISGQEGIQAVLASDYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFA
FTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGVFDQDVPEQRSMEYPKLYE
PGQLNLLFNKREFFICIAQGIYTSVLMFFIPYGVFADATRDDGTQLADYQSFAVTVATSL
VIVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPNQFRFVGNAQNTL
AQPTVWLTIVLTTVVCIMPVVAFRFLRLNLKPDLSDTVRYTQLVRKKQKAQHRCMRRVGR
TGSRRSGYAFSHQEGFGELIMSGKNMRLSSLALSSFTTRSSSSWIESLRRKKSDSASSPS
GGADKPLKG
|
| Enzyme 64 Number of Residues |
1209 |
| Enzyme 64 Molecular Weight |
137439.1 |
| Enzyme 64 Theoretical pI |
6.99 |
| Enzyme 64 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- 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
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 64 General Function |
Involved in ATP binding |
| Enzyme 64 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 64 Pathways |
Not Available |
| Enzyme 64 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 64 Pfam Domain Function |
|
| Enzyme 64 Signals |
|
| Enzyme 64 Transmembrane Regions |
- 65-86
93-112
296-317
347-368
890-910
923-942
973-994
1009-1031
1038-1058
1079-1103
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
40316837  |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
P98198  |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
AT8B2_HUMAN  |
| Enzyme 64 PDB ID |
Not Available |
| Enzyme 64 Cellular Location |
Not Available |
| Enzyme 64 Gene Sequence |
>3672 bp
ATGGATACCTTGAGAGCTGTTCCCCTTTTTTCAATATCTGGCCTCTTCTCCTTTCCCTAC
AGGGTCTCCCATGGGATTGCTGGGATCTTGCTGGGTGAGATGGCAGTGTGTGCAAAAAAG
CGCCCCCCAGAAGAAGAAAGGAGGGCGCGGGCTAATGACCGAGAATACAATGAGAAATTC
CAGTATGCGAGTAACTGCATCAAGACCTCCAAGTACAATATTCTCACCTTCCTGCCTGTC
AACCTCTTTGAGCAGTTCCAGGAAGTTGCCAACACTTACTTCCTGTTCCTCCTCATTCTG
CAGTTGATCCCCCAGATCTCTTCCCTGTCCTGGTTCACCACCATTGTGCCTTTGGTTCTT
GTCCTCACCATCACAGCTGTTAAAGATGCCACTGATGACTATTTCCGCCACAAGAGCGAT
AACCAGGTGAATAACCGCCAGTCTCAGGTGCTGATCAATGGAATCCTCCAGCAGGAGCAG
TGGATGAATGTCTGTGTTGGTGATATTATCAAGCTAGAAAATAACCAGTTTGTGGCGGCG
GATCTCCTCCTCCTTTCCAGCAGTGAGCCCCATGGGCTGTGTTACATAGAGACAGCAGAA
CTTGATGGCGAGACCAACATGAAAGTACGTCAGGCGATTCCAGTCACCTCAGAATTGGGA
GACATCAGTAAGCTTGCCAAGTTTGACGGTGAAGTGATCTGTGAACCTCCCAACAACAAA
CTGGACAAATTCAGCGGAACCCTCTACTGGAAGGAAAATAAGTTCCCTCTGAGCAACCAG
AACATGCTGCTGCGGGGCTGTGTGCTGCGAAACACCGAGTGGTGCTTCGGGCTGGTCATC
TTTGCAGGTCCCGACACTAAGCTGATGCAAAACAGCGGCAGAACAAAGTTCAAAAGAACG
AGTATCGATCGCCTAATGAATACCCTGGTGCTCTGGATTTTTGGATTCCTGGTTTGCATG
GGGGTGATCCTGGCCATTGGCAATGCCATCTGGGAGCACGAGGTGGGGATGCGTTTCCAG
GTCTACCTGCCGTGGGATGAGGCAGTGGACAGTGCCTTCTTCTCTGGCTTCCTCTCCTTC
TGGTCCTACATCATCATCCTCAACACCGTTGTGCCCATTTCACTCTATGTCAGTGTGGAG
GTCATCCGTCTGGGCCACAGCTACTTCATCAACTGGGATAAGAAGATGTTCTGCATGAAG
AAGCGGACGCCTGCAGAAGCCCGCACCACCACCCTAAACGAGGAGCTGGGCCAGGTGGAG
TACATCTTCTCCGACAAGACGGGCACCCTCACCCAGAACATCATGGTTTTCAACAAGTGC
TCCATCAATGGCCACAGCTATGGTGATGTGTTTGACGTCCTGGGACACAAAGCTGAATTG
GGAGAGAGGCCTGAACCTGTTGACTTCTCCTTCAATCCTCTGGCTGACAAGAAGTTCTTA
TTTTGGGACCCCAGCCTGCTGGAGGCTGTCAAGATCGGGGACCCCCACACGCATGAGTTC
TTCCGCCTCCTTTCCCTGTGTCATACTGTCATGTCAGAAGAAAAGAACGAAGGAGAGCTG
TACTACAAAGCTCAGTCCCCAGATGAGGGGGCCCTGGTCACCGCAGCCAGGAACTTTGGT
TTTGTTTTCCGCTCTCGCACCCCCAAAACAATCACCGTCCATGAGATGGGCACAGCCATC
ACCTACCAGCTGCTGGCCATCCTGGACTTCAACAACATCCGCAAGCGGATGTCGGTCATA
GTGCGGAATCCAGAGGGGAAGATCCGACTCTACTGCAAAGGGGCTGACACTATCCTACTG
GACAGACTGCACCACTCCACTCAAGAGCTGCTCAACACCACCATGGACCACCTTAATGAG
TACGCAGGGGAAGGGCTGAGGACCCTGGTGCTGGCCTACAAGGATCTGGATGAAGAGTAC
TACGAGGAGTGGGCTGAGCGACGCCTCCAGGCCAGCCTGGCCCAGGACAGCCGGGAGGAC
AGGCTGGCTAGCATCTATGAGGAGGTTGAGAACAACATGATGCTGCTGGGTGCAACGGCC
ATTGAGGACAAACTTCAGCAAGGGGTTCCAGAGACCATTGCCCTCCTGACACTGGCCAAC
ATCAAGATTTGGGTGCTAACCGGAGACAAGCAAGAGACGGCTGTGAACATCGGCTATTCC
TGCAAGATGCTGACGGATGACATGACTGAGGTTTTCATAGTCACTGGCCATACTGTCCTG
GAGGTGCGGGAGGAGCTCAGGAAAGCCCGGGAGAAGATGATGGACTCATCCCGCTCCGTA
GGCAACGGCTTCACCTATCAGGACAAGCTTTCTTCTTCCAAGCTAACTTCTGTCCTGGAG
GCCGTTGCTGGGGAGTACGCCCTGGTCATAAATGGTCACAGCCTGGCCCACGCACTGGAG
GCAGACATGGAGCTGGAGTTTCTGGAGACAGCGTGTGCCTGCAAAGCTGTCATCTGCTGC
CGGGTGACCCCCTTGCAGAAGGCACAGGTGGTAGAACTGGTCAAGAAGTACAAGAAGGCT
GTGACGCTTGCCATTGGAGACGGAGCCAATGATGTCAGCATGATCAAAACGGCTCACATT
GGTGTGGGGATCAGTGGGCAGGAAGGGATCCAGGCTGTCTTGGCCTCCGATTACTCCTTC
TCCCAGTTCAAGTTCCTGCAGCGCCTCCTGCTGGTGCATGGGCGCTGGTCCTACCTGCGA
ATGTGCAAGTTTCTTTGCTATTTCTTCTACAAAAACTTTGCTTTCACCATGGTCCACTTC
TGGTTTGGCTTCTTCTGTGGCTTCTCAGCCCAGACCGTCTATGACCAGTATTTCATCACC
CTGTATAACATCGTGTACACCTCCCTGCCAGTCCTGGCTATGGGGGTCTTTGATCAGGAT
GTCCCCGAGCAGCGGAGCATGGAGTACCCTAAGCTGTATGAGCCGGGCCAGCTGAACCTT
CTCTTCAACAAGCGGGAGTTCTTCATCTGCATCGCCCAGGGCATCTACACCTCCGTGCTC
ATGTTCTTCATTCCCTATGGGGTGTTTGCTGATGCCACCCGGGATGATGGCACTCAGCTG
GCTGACTACCAGTCCTTTGCAGTCACTGTGGCCACATCCTTGGTCATTGTGGTTAGCGTG
CAGATTGGGCTCGACACAGGCTACTGGACGGCCATCAACCACTTCTTCATCTGGGGAAGC
CTTGCTGTTTACTTTGCCATCCTCTTTGCCATGCACAGCAATGGGCTCTTCGACATGTTT
CCCAACCAGTTCCGGTTTGTGGGGAATGCCCAGAACACCTTGGCCCAGCCCACGGTGTGG
CTGACCATTGTGCTCACCACAGTCGTCTGCATCATGCCCGTGGTTGCCTTCCGATTCCTC
AGGCTCAACCTGAAGCCGGATCTCTCCGACACGGTCCGCTACACACAGCTCGTGAGGAAG
AAGCAGAAGGCCCAGCACCGCTGCATGCGGCGGGTTGGCCGCACTGGCTCCCGGCGCTCC
GGCTATGCCTTCTCCCATCAGGAGGGCTTCGGGGAGCTCATCATGTCTGGCAAGAACATG
CGGCTGAGCTCTCTCGCGCTCTCCAGCTTCACCACCCGCTCCAGCTCCAGCTGGATTGAG
AGCCTGCGCAGGAAGAAGAGTGACAGTGCCAGTAGCCCCAGTGGCGGTGCCGACAAGCCC
CTCAAGGGCTGA
|
| Enzyme 64 GenBank Gene ID |
Not Available |
| Enzyme 64 GeneCard ID |
ATP8B2  |
| Enzyme 64 GenAtlas ID |
ATP8B2  |
| Enzyme 64 HGNC ID |
HGNC:13534  |
| Enzyme 64 Chromosome Location |
1 |
| Enzyme 64 Locus |
1q21.3 |
| Enzyme 64 SNPs |
SNPJam Report  |
| Enzyme 64 General References |
- Harris MJ, Arias IM: FIC1, a P-type ATPase linked to cholestatic liver disease, has homologues (ATP8B2 and ATP8B3) expressed throughout the body. Biochim Biophys Acta. 2003 Jul 21;1633(2):127-31. [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
]
- 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
]
- Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [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
]
- 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 64 Metabolite References |
Not Available |
|
Enzyme 65
[top]
|
| Enzyme 65 ID |
12922 |
| Enzyme 65 Name |
Phospholipase B1, membrane-associated |
| Enzyme 65 Synonyms |
- Phospholipase B
- hPLB
- Phospholipase B/lipase
- PLB/LIP
- Phospholipase A2
- Lysophospholipase
|
| Enzyme 65 Gene Name |
PLB1 |
| Enzyme 65 Protein Sequence |
>Phospholipase B1, membrane-associated
MGLRPGIFLLELLLLLGQGTPQIHTSPRKSTLEGQLWPETLKNSPFPCNPNKLGVNMPSK
SVHSLKPSDIKFVAAIGNLEIPPDPGTGDLEKQDWTERPQQVCMGVMTVLSDIIRYFSPS
VPMPVCHTGKRVIPHDGAEDLWIQAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLC
PSAQQNGLAAGGVDELMGVLDYLQQEVPRAFVNLVDLSEVAEVSRQYHGTWLSPAPEPCN
CSEETTRLAKVVMQWSYQEAWNSLLASSRYSEQESFTVVFQPFFYETTPSLHSEDPRLQD
STTLAWHLWNRMMEPAGEKDEPLSVKHGRPMKCPSQESPYLFSYRNSNYLTRLQKPQDKL
EVREGAEIRCPDKDPSDTVPTSVHRLKPADINVIGALGDSLTAGNGAGSTPGNVLDVLTQ
YRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKETSPNAFLNQAVAGGRAEDL
PVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDI
LHAEVPRAFVNLVTVLEIVNLRELYQEKKVYCPRMILRSLCPCVLKFDDNSTELATLIEF
NKKFQEKTHQLIESGRYDTREDFTVVVQPFFENVDMPKTSEGLPDNSFFAPDCFHFSSKS
HSRAASALWNNMLEPVGQKTTRHKFENKINITCPNQVQPFLRTYKNSMQGHGTWLPCRDR
APSALHPTSVHALRPADIQVVAALGDSLTAGNGIGSKPDDLPDVTTQYRGLSYSAGGDGS
LENVTTLPNILREFNRNLTGYAVGTGDANDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKD
DHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVLHREVPRVLVNLV
DFLNPTIMRQVFLGNPDKCPVQQASVLCNCVLTLRENSQELARLEAFSRAYRSSMRELVG
SGRYDTQEDFSVVLQPFFQNIQLPVLADGLPDTSFFAPDCIHPNQKFHSQLARALWTNML
EPLGSKTETLDLRAEMPITCPTQNEPFLRTPRNSNYTYPIKPAIENWGSDFLCTEWKASN
SVPTSVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTT
LPNILKKFNPYLLGFSTSTWEGTAGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKD
WKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSEELPRAFVNVVEVMELASLY
QGQGGKCAMLAAQNNCTCLRHSQSSLEKQELKKVNWNLQHGISSFSYWHQYTQREDFAVV
VQPFFQNTLTPLNERGDTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVGRKTTSNNFT
HSRAKLKCPSPESPYLYTLRNSRLLPDQAEEAPEVLYWAVPVAAGVGLVVGIIGTVVWRC
RRGGRREDPPMSLRTVAL
|
| Enzyme 65 Number of Residues |
1458 |
| Enzyme 65 Molecular Weight |
163079.3 |
| Enzyme 65 Theoretical pI |
5.72 |
| Enzyme 65 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 65 General Function |
Involved in hydrolase activity |
| Enzyme 65 Specific Function |
Membrane-associated phospholipase. Exhibits a calcium- independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids |
| Enzyme 65 Pathways |
Not Available |
| Enzyme 65 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 65 Pfam Domain Function |
|
| Enzyme 65 Signals |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
283436112  |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
Q6P1J6  |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
PLB1_HUMAN  |
| Enzyme 65 PDB ID |
Not Available |
| Enzyme 65 Cellular Location |
Not Available |
| Enzyme 65 Gene Sequence |
>4377 bp
ATGGGGCTGCGGCCAGGCATTTTCCTCCTGGAGCTGCTGCTGCTTCTGGGGCAAGGGACC
CCTCAGATCCATACCTCTCCTAGAAAGAGTACATTGGAAGGGCAGCTATGGCCAGAGACC
CTGAAGAATTCTCCATTCCCATGCAACCCAAATAAATTAGGAGTGAATATGCCTTCTAAA
TCAGTTCACTCTCTGAAGCCTTCTGATATTAAATTTGTGGCAGCCATTGGCAATCTGGAA
ATTCCTCCAGACCCAGGGACGGGCGATCTGGAGAAGCAAGACTGGACTGAAAGGCCACAG
CAGGTGTGCATGGGAGTGATGACAGTCCTTTCAGACATCATCAGATATTTCAGTCCTTCT
GTTCCAATGCCTGTGTGCCACACTGGAAAGAGAGTCATACCCCACGATGGTGCTGAAGAC
TTGTGGATTCAGGCTCAAGAACTGGTGAGAAACATGAAAGAGAACCTGCAACTTGACTTT
CAATTTGACTGGAAGCTCATCAATGTGTTCTTCAGTAATGCAAGCCAGTGTTACCTGTGC
CCCTCTGCTCAACAGAATGGGCTTGCGGCGGGCGGCGTGGATGAGCTGATGGGGGTGCTG
GACTACCTGCAGCAGGAGGTCCCCAGAGCATTTGTAAACCTGGTGGACCTCTCTGAGGTT
GCAGAGGTCTCTCGTCAGTATCACGGCACTTGGCTCAGCCCTGCACCAGAGCCCTGTAAT
TGCTCAGAGGAGACCACCCGGCTGGCCAAGGTGGTGATGCAGTGGTCTTATCAGGAAGCC
TGGAACAGCCTCCTGGCCTCCAGCAGGTACAGTGAGCAGGAGTCCTTCACCGTGGTTTTC
CAGCCTTTCTTCTATGAGACCACCCCATCTCTACACTCGGAGGACCCCCGACTCCAGGAT
TCTACCACGCTGGCCTGGCATCTCTGGAATAGGATGATGGAGCCAGCAGGAGAGAAAGAT
GAGCCATTGAGTGTAAAACACGGGAGGCCAATGAAGTGTCCCTCTCAGGAGAGCCCCTAT
CTGTTCAGCTACAGAAACAGCAACTACCTGACCAGACTGCAGAAACCCCAAGACAAGCTT
GAGGTAAGAGAAGGAGCGGAAATCAGATGTCCTGACAAAGACCCCTCCGATACGGTTCCC
ACCTCAGTTCATAGGCTGAAGCCGGCTGACATCAACGTAATTGGAGCCCTGGGTGACTCT
CTCACGGCAGGCAATGGGGCCGGGTCCACACCTGGGAACGTCTTGGACGTCTTGACTCAG
TACCGAGGCCTGTCCTGGAGCGTCGGCGGAGATGAGAACATCGGCACCGTTACCACCCTG
GCGAACATCCTCCGGGAATTCAACCCTTCCCTGAAGGGCTTCTCTGTTGGCACTGGGAAA
GAAACCAGTCCTAATGCCTTCTTAAACCAGGCTGTGGCAGGAGGCCGAGCTGAGGATCTA
CCTGTCCAGGCCAGGAGGCTGGTGGACCTGATGAAGAATGACACGAGGATACACTTTCAG
GAAGACTGGAAGATAATAACCCTGTTTATAGGCGGCAATGACCTCTGTGATTTCTGCAAT
GATCTGGTCCACTATTCTCCCCAGAACTTCACAGACAACATTGGAAAGGCCCTGGACATC
CTCCATGCTGAGGTTCCTCGGGCATTTGTGAACCTGGTGACGGTGCTTGAGATCGTCAAC
CTGAGGGAGCTGTACCAGGAGAAAAAAGTCTACTGCCCAAGGATGATCCTCAGGTCTCTG
TGTCCCTGTGTCCTGAAGTTTGATGATAACTCAACAGAACTTGCTACCCTCATCGAATTC
AACAAGAAGTTTCAGGAGAAGACCCACCAACTGATTGAGAGTGGGCGATATGACACAAGG
GAAGATTTTACTGTGGTTGTGCAGCCGTTCTTTGAAAACGTGGACATGCCAAAGACCTCG
GAAGGATTGCCTGACAACTCTTTCTTCGCTCCTGACTGTTTCCACTTCAGCAGCAAGTCT
CACTCCCGAGCAGCCAGTGCTCTCTGGAACAATATGCTGGAGCCTGTTGGCCAGAAGACG
ACTCGTCATAAGTTTGAAAACAAGATCAATATCACATGTCCGAACCAGGTCCAGCCGTTT
CTGAGGACCTACAAGAACAGCATGCAGGGTCATGGGACCTGGCTGCCATGCAGGGACAGA
GCCCCTTCTGCCTTGCACCCTACCTCAGTGCATGCCCTGAGACCTGCAGACATCCAAGTT
GTGGCTGCTCTGGGGGATTCTCTGACCGCTGGCAATGGAATTGGCTCCAAACCAGACGAC
CTCCCCGATGTCACCACACAGTATCGGGGACTGTCATACAGTGCAGGAGGGGACGGCTCC
CTGGAGAATGTGACCACCTTACCTAATATCCTTCGGGAGTTTAACAGAAACCTCACAGGC
TACGCCGTGGGCACGGGTGATGCCAATGACACGAATGCATTCCTCAATCAAGCTGTTCCC
GGAGCAAAGGCTGAGGATCTTATGAGCCAAGTCCAAACTCTGATGCAGAAGATGAAAGAT
GATCATAGAGTAAATTTCCATGAAGACTGGAAGGTCATCACAGTGCTGATCGGAGGCAGC
GATTTATGTGACTACTGCACAGATTCGAATCTGTATTCTGCAGCCAACTTTGTTCACCAT
CTCCGCAATGCCTTGGACGTCCTGCATAGAGAGGTGCCCAGAGTCCTGGTCAACCTCGTG
GACTTCCTGAACCCCACTATCATGCGGCAGGTGTTCCTGGGAAACCCAGACAAGTGCCCA
GTGCAGCAGGCCAGCGTTTTGTGTAACTGCGTTCTGACCCTGCGGGAGAACTCCCAAGAG
CTAGCCAGGCTGGAGGCCTTCAGCCGAGCCTACCGGAGCAGCATGCGCGAGCTGGTGGGG
TCAGGCCGCTATGACACGCAGGAGGACTTCTCTGTGGTGCTGCAGCCCTTCTTCCAGAAC
ATCCAGCTCCCTGTCCTGGCGGATGGGCTCCCAGATACGTCCTTCTTTGCCCCAGACTGC
ATCCACCCAAATCAGAAATTCCACTCCCAGCTGGCCAGAGCCCTTTGGACCAATATGCTT
GAACCACTTGGAAGCAAAACAGAGACCCTGGACCTGAGAGCAGAGATGCCCATCACCTGT
CCCACTCAGAATGAGCCCTTCCTGAGAACCCCTCGGAATAGTAACTACACGTACCCCATC
AAGCCAGCCATTGAGAACTGGGGCAGTGACTTCCTGTGTACAGAGTGGAAGGCTTCCAAT
AGTGTTCCAACCTCTGTCCACCAGCTCCGACCAGCAGACATCAAAGTGGTGGCCGCCCTG
GGTGACTCTCTGACTACAGCAGTGGGAGCTCGACCAAACAACTCCAGTGACCTACCCACA
TCTTGGAGGGGACTCTCTTGGAGCATTGGAGGGGATGGGAACTTGGAGACTCACACCACA
CTGCCCAACATTCTGAAGAAGTTCAACCCTTACCTCCTTGGCTTCTCTACCAGCACCTGG
GAGGGGACAGCAGGACTAAATGTGGCAGCGGAAGGGGCCAGAGCTAGGGACATGCCAGCC
CAGGCCTGGGACCTGGTAGAGCGAATGAAAAACAGCCCCGACATCAACCTGGAGAAAGAC
TGGAAGCTGGTCACACTCTTCATTGGGGTCAACGACTTGTGTCATTACTGTGAGAATCCG
GAGGCCCACTTGGCCACGGAATATGTTCAGCACATCCAACAGGCCCTGGACATCCTCTCT
GAGGAGCTCCCAAGGGCTTTCGTCAACGTGGTGGAGGTCATGGAGCTGGCTAGCCTGTAC
CAGGGCCAAGGCGGGAAATGTGCCATGCTGGCAGCTCAGAACAACTGCACTTGCCTCAGA
CACTCGCAAAGCTCCCTGGAGAAGCAAGAACTGAAGAAAGTGAACTGGAACCTCCAGCAT
GGCATCTCCAGTTTCTCCTACTGGCACCAATACACACAGCGTGAGGACTTTGCGGTTGTG
GTGCAGCCTTTCTTCCAAAACACACTCACCCCACTGAACGAGAGAGGGGACACTGACCTC
ACCTTCTTCTCCGAGGACTGTTTTCACTTCTCAGACCGCGGGCATGCCGAGATGGCCATC
GCACTCTGGAACAACATGCTGGAACCAGTGGGCCGCAAGACTACCTCCAACAACTTCACC
CACAGCCGAGCCAAACTCAAGTGCCCCTCTCCTGAGAGCCCTTACCTCTACACCCTGCGG
AACAGCCGATTGCTCCCAGACCAGGCTGAAGAAGCCCCCGAGGTGCTCTACTGGGCTGTC
CCAGTGGCAGCGGGAGTCGGCCTTGTGGTGGGCATCATCGGGACAGTGGTCTGGAGGTGC
AGGAGAGGTGGCCGGAGGGAAGATCCTCCAATGAGCCTGCGCACTGTGGCCCTCTAG
|
| Enzyme 65 GenBank Gene ID |
NM_153021.4  |
| Enzyme 65 GeneCard ID |
PLB1  |
| Enzyme 65 GenAtlas ID |
PLB1  |
| Enzyme 65 HGNC ID |
HGNC:30041  |
| Enzyme 65 Chromosome Location |
2 |
| Enzyme 65 Locus |
2p23.2 |
| Enzyme 65 SNPs |
SNPJam Report  |
| Enzyme 65 General References |
- 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
]
- 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
]
- Maury E, Prevost MC, Nauze M, Redoules D, Tarroux R, Charveron M, Salles JP, Perret B, Chap H, Gassama-Diagne A: Human epidermis is a novel site of phospholipase B expression. Biochem Biophys Res Commun. 2002 Jul 12;295(2):362-9. [PubMed
]
|
| Enzyme 65 Metabolite References |
Not Available |
|
Enzyme 66
[top]
|
| Enzyme 66 ID |
12926 |
| Enzyme 66 Name |
Phosphatidylethanolamine-binding protein 1 |
| Enzyme 66 Synonyms |
- PEBP-1
- HCNPpp
- Neuropolypeptide h3
- Prostatic-binding protein
- Raf kinase inhibitor protein
- RKIP
- Hippocampal cholinergic neurostimulating peptide
- HCNP
|
| Enzyme 66 Gene Name |
PEBP1 |
| Enzyme 66 Protein Sequence |
>Phosphatidylethanolamine-binding protein 1
MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDS
GKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSGTVLSDYVGSGPPKGTGLHRY
VWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKL
YEQLSGK
|
| Enzyme 66 Number of Residues |
187 |
| Enzyme 66 Molecular Weight |
21056.6 |
| Enzyme 66 Theoretical pI |
7.65 |
| Enzyme 66 GO Classification |
Not Available |
| Enzyme 66 General Function |
Involved in ATP binding |
| Enzyme 66 Specific Function |
HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor |
| Enzyme 66 Pathways |
Not Available |
| Enzyme 66 Reactions |
Not Available |
| Enzyme 66 Pfam Domain Function |
|
| Enzyme 66 Signals |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
189065145  |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
P30086  |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
PEBP1_HUMAN  |
| Enzyme 66 PDB ID |
1BEH  |
| Enzyme 66 PDB File |
Show |
| Enzyme 66 3D Structure |
|
| Enzyme 66 Cellular Location |
Not Available |
| Enzyme 66 Gene Sequence |
>564 bp
ATGCCGGTGGACCTCAGCAAGTGGTCCGGGCCCTTGAGCCTGCAAGAAGTGGACGAGCAG
CCGCAGCACCCGCTGCATGTCACCTACGCCGGGGCGGCGGTGGACGAGCTGGGCAAAGTG
CTGACGCCCACCCAGGTTAAGAATAGACCCACCAGCATTTCGTGGGATGGTCTTGATTCA
GGGAAGCTCTACACCTTGGTCCTGACAGACCCGGATGCTCCCAGCAGGAAGGATCCCAAA
TACAGAGAATGGCATCATTTCCTGGTGGTCAACATGAAGGGCAATGACATCAGCAGTGGC
ACAGTCCTCTCCGATTATGTGGGCTCGGGGCCTCCCAAGGGCACAGGCCTCCACCGCTAT
GTCTGGCTGGTTTACGAGCAGGACAGGCCGCTAAAGTGTGACGAGCCCATCCTCAGCAAC
CGATCTGGAGACCACCGTGGCAAATTCAAGGTGGCGTCCTTCCGTAAAAAGTATGAGCTC
AGGGCCCCGGTGGCTGGCACGTGTTACCAGGCCGAGTGGGATGACTATGTGCCCAAACTG
TACGAGCAGCTGTCTGGGAAGTAG
|
| Enzyme 66 GenBank Gene ID |
AK311927  |
| Enzyme 66 GeneCard ID |
PEBP1  |
| Enzyme 66 GenAtlas ID |
PEBP1  |
| Enzyme 66 HGNC ID |
HGNC:8630  |
| Enzyme 66 Chromosome Location |
1 |
| Enzyme 66 Locus |
12q24.23 |
| Enzyme 66 SNPs |
SNPJam Report  |
| Enzyme 66 General References |
- Hori N, Chae KS, Murakawa K, Matoba R, Fukushima A, Okubo K, Matsubara K: A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding protein. Gene. 1994 Mar 25;140(2):293-4. [PubMed
]
- Tohdoh N, Tojo S, Agui H, Ojika K: Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein. Brain Res Mol Brain Res. 1995 Jun;30(2):381-4. [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
]
- 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
]
- Seddiqi N, Bollengier F, Alliel PM, Perin JP, Bonnet F, Bucquoy S, Jolles P, Schoentgen F: Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues. J Mol Evol. 1994 Dec;39(6):655-60. [PubMed
]
- Ojika K, Mitake S, Tohdoh N, Appel SH, Otsuka Y, Katada E, Matsukawa N: Hippocampal cholinergic neurostimulating peptides (HCNP). Prog Neurobiol. 2000 Jan;60(1):37-83. [PubMed
]
- Yeung K, Seitz T, Li S, Janosch P, McFerran B, Kaiser C, Fee F, Katsanakis KD, Rose DW, Mischak H, Sedivy JM, Kolch W: Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP. Nature. 1999 Sep 9;401(6749):173-7. [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
]
- 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
]
- Banfield MJ, Barker JJ, Perry AC, Brady RL: Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure. 1998 Oct 15;6(10):1245-54. [PubMed
]
|
| Enzyme 66 Metabolite References |
Not Available |
|
Enzyme 67
[top]
|
| Enzyme 67 ID |
12927 |
| Enzyme 67 Name |
Phosphatidylethanolamine-binding protein 4 |
| Enzyme 67 Synonyms |
- PEBP-4
- hPEBP4
- Protein cousin-of-RKIP 1
|
| Enzyme 67 Gene Name |
PEBP4 |
| Enzyme 67 Protein Sequence |
>Phosphatidylethanolamine-binding protein 4
MGWTMRLVTAALLLGLMMVVTGDEDENSPCAHEALLDEDTLFCQGLEVFYPELGNIGCKV
VPDCNNYRQKITSWMEPIVKFPGAVDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKG
ADLKKGKIQGQELSAYQAPSPPAHSGFHRYQFFVYLQEGKVISLLPKENKTRGSWKMDRF
LNRFHLGEPEASTQFMTQNYQDSPTLQAPRERASEPKHKNQAEIAAC
|
| Enzyme 67 Number of Residues |
227 |
| Enzyme 67 Molecular Weight |
25733.2 |
| Enzyme 67 Theoretical pI |
6.51 |
| Enzyme 67 GO Classification |
Not Available |
| Enzyme 67 General Function |
Not Available |
| Enzyme 67 Specific Function |
Seems to promote cellular resistance to TNF-induced apoptosis by inhibiting activation of the Raf-1/MEK/ERK pathway, JNK and phosphatidylethanolamine externalization |
| Enzyme 67 Pathways |
Not Available |
| Enzyme 67 Reactions |
Not Available |
| Enzyme 67 Pfam Domain Function |
|
| Enzyme 67 Signals |
|
| Enzyme 67 Transmembrane Regions |
|
| Enzyme 67 Essentiality |
Not Available |
| Enzyme 67 GenBank ID Protein |
14585855  |
| Enzyme 67 UniProtKB/Swiss-Prot ID |
Q96S96  |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
PEBP4_HUMAN  |
| Enzyme 67 PDB ID |
Not Available |
| Enzyme 67 Cellular Location |
Not Available |
| Enzyme 67 Gene Sequence |
>684 bp
ATGGGTTGGACAATGAGGCTGGTCACAGCAGCACTGTTACTGGGTCTCATGATGGTGGTC
ACTGGAGACGAGGATGAGAACAGCCCGTGTGCCCATGAGGCCCTCTTGGACGAGGACACC
CTCTTTTGCCAGGGCCTTGAAGTTTTCTACCCAGAGTTGGGGAACATTGGCTGCAAGGTT
GTTCCTGATTGTAACAACTACAGACAGAAGATCACCTCCTGGATGGAGCCGATAGTCAAG
TTCCCGGGGGCCGTGGACGGCGCAACCTATATCCTGGTGATGGTGGATCCAGATGCCCCT
AGCAGAGCAGAACCCAGACAGAGATTCTGGAGACATTGGCTGGTAACAGATATCAAGGGC
GCCGACCTGAAGGAAGGGAAGATTCAGGGCCAGGAGTTATCAGCCTACCAGGCTCCCTCC
CCACCGGCACACAGTGGCTTCCATCGCTACCAGTTCTTTGTCTATCTTCAGGAAGGAAAA
GTCATCTCTCTCCTTCCCAAGGAAAACAAAACTCGAGGCTCTTGGAAAATGGACAGATTT
CTGAACCGTTTCCACCTGGGCGAACCTGAAGCAAGCACCCAGTTCATGACCCAGAACTAC
CAGGACTCACCAACCCTCCAGGCTCCCAGAGAAAGGGCCAGCGAGCCCAAGCACAAAAAC
CAGGCGGAGATAGCTGCCTGCTAG
|
| Enzyme 67 GenBank Gene ID |
AY037148  |
| Enzyme 67 GeneCard ID |
PEBP4  |
| Enzyme 67 GenAtlas ID |
PEBP4  |
| Enzyme 67 HGNC ID |
HGNC:28319  |
| Enzyme 67 Chromosome Location |
8 |
| Enzyme 67 Locus |
8p21.3 |
| Enzyme 67 SNPs |
SNPJam Report  |
| Enzyme 67 General References |
- Wang X, Li N, Liu B, Sun H, Chen T, Li H, Qiu J, Zhang L, Wan T, Cao X: A novel human phosphatidylethanolamine-binding protein resists tumor necrosis factor alpha-induced apoptosis by inhibiting mitogen-activated protein kinase pathway activation and phosphatidylethanolamine externalization. J Biol Chem. 2004 Oct 29;279(44):45855-64. Epub 2004 Aug 9. [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
]
- 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 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
12958 |
| Enzyme 68 Name |
Membrane-associated phosphatidylinositol transfer protein 1 |
| Enzyme 68 Synonyms |
- Drosophila retinal degeneration B homolog
- Phosphatidylinositol transfer protein, membrane-associated 1
- PITPnm 1
- Pyk2 N-terminal domain-interacting receptor 2
- NIR-2
|
| Enzyme 68 Gene Name |
PITPNM1 |
| Enzyme 68 Protein Sequence |
>Membrane-associated phosphatidylinositol transfer protein 1
MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTH
KVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGG
QQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYHSVKTGRGPLSDDWARTA
AQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELSMAD
IRALEEETARMLAQRMAKCNTGSEGSEAQPPGKPSTEARSAASNTGTPDGPEAPPGPDAS
PDASFGKQWSSSSRSSYSSQHGGAVSPQSLSEWRMQNIARDSENSSEEEFFDAHEGFSDS
EEVFPKEMTKWNSNDFIDAFASPVEAEGTPEPGAEAAKGIEDGAQAPRDSEGLDGAGELG
AEACAVHALFLILHSGNILDSGPGDANSKQADVQTLSSAFEAVTRIHFPEALGHVALRLV
PCPPICAAAYALVSNLSPYSHDGDSLSRSQDHIPLAALPLLATSSSRYQGAVATVIARTN
QAYSAFLRSPEGAGFCGQVALIGDGVGGILGFDALCHSANAGTGSRGSSRRGSMNNELLS
PEFGPVRDPLADGVEGLGRGSPEPSALPPQRIPSDMASPEPEGSQNSLQAAPATTSSWEP
RRASTAFCPPAASSEAPDGPSSTARLDFKVSGFFLFGSPLGLVLALRKTVMPALEAAQMR
PACEQIYNLFHAADPCASRLEPLLAPKFQAIAPLTVPRYQKFPLGDGSSLLLADTLQTHS
SLFLEELEMLVPSTPTSTSGAFWKGSELATDPPAQPAAPSTTSEVVKILERWWGTKRIDY
SLYCPEALTAFPTVTLPHLFHASYWESADVVAFILRQVIEKERPQLAECEEPSIYSPAFP
REKWQRKRTQVKIRNVTSNHRASDTVVCEGRPQVLSGRFMYGPLDVVTLTGEKVDVYIMT
QPLSGKWIHFGTEVTNSSGRLTFPVPPERALGIGVYPVRMVVRGDHTYAECCLTVVARGT
EAVVFSIDGSFTASVSIMGSDPKVRAGAVDVVRHWQDSGYLIVYVTGRPDMQKHRVVAWL
SQHNFPHGVVSFCDGLTHDPLRQKAMFLQSLVQEVELNIVAGYGSPKDVAVYAALGLSPS
QTYIVGRAVRKLQAQCQFLSDGYVAHLGQLEAGSHSHASSGPPRAALGKSSYGVAAPVDF
LRKQSQLLRSRGPSQAEREGPGTPPTTLARGKARSISLKLDSEE
|
| Enzyme 68 Number of Residues |
1244 |
| Enzyme 68 Molecular Weight |
134846.3 |
| Enzyme 68 Theoretical pI |
5.81 |
| Enzyme 68 GO Classification |
| Function |
- binding
- cation binding
- ion binding
- metal ion binding
|
| Process |
- establishment of localization
- transport
|
| Component |
|
|
| Enzyme 68 General Function |
Involved in metal ion binding |
| Enzyme 68 Specific Function |
Regulates RHOA activity, and plays a role in cytoskeleton remodeling. Necessary for normal completion of cytokinesis. Plays a role in maintaining normal diacylglycerol levels in the Golgi apparatus. Binds phosphatidyl inositol phosphates (in vitro). May catalyze the transfer of phosphatidylinositol and phosphatidylcholine between membranes. Necessary for maintaining the normal structure of the endoplasmic reticulum and the Golgi apparatus. Required for protein export from the endoplasmic reticulum and the Golgi. Binds calcium ions |
| Enzyme 68 Pathways |
Not Available |
| Enzyme 68 Reactions |
Not Available |
| Enzyme 68 Pfam Domain Function |
|
| Enzyme 68 Signals |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
12667436  |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
O00562  |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
PITM1_HUMAN  |
| Enzyme 68 PDB ID |
Not Available |
| Enzyme 68 Cellular Location |
Not Available |
| Enzyme 68 Gene Sequence |
>3735 bp
ATGCTCATCAAGGAATACCACATTCTGCTGCCCATGAGCCTGGACGAGTACCAGGTGGCC
CAGCTCTACATGATCCAGAAAAAGAGCCGGGAGGAGTCTAGTGGTGAGGGCAGCGGCGTG
GAGATCCTGGCCAACCGGCCCTACACGGATGGGCCCGGGGGCAGCGGGCAATACACACAC
AAGGTGTACCACGTGGGCTCCCACATCCCAGGCTGGTTCCGGGCACTGCTGCCCAAGGCT
GCCCTGCAGGTAGAAGAGGAATCCTGGAATGCCTACCCCTACACCCGAACCCGGTACACC
TGCCCTTTCGTGGAGAAATTCTCCATTGAAATTGAGACCTATTACCTGCCTGATGGGGGG
CAGCAGCCAAACGTCTTCAACCTGAGCGGGGCCGAGAGGAGACAGCGCATCCTGGACACC
ATCGACATCGTGCGGGATGCAGTGGCCCCAGGCGAGTACAAAGCAGAAGAGGACCCCCGG
CTTTATCACTCGGTCAAGACGGGCCGAGGGCCACTGTCTGATGACTGGGCACGGACGGCG
GCACAGACGGGGCCCCTTATGTGTGCCTATAAGCTGTGCAAGGTTGAGTTCCGCTACTGG
GGCATGCAAGCCAAGATCGAGCAGTTCATCCATGATGTAGGTCTGCGTCGGGTGATGCTG
CGGGCCCACCGCCAGGCCTGGTGCTGGCAGGATGAGTGGACAGAGCTGAGCATGGCTGAC
ATCCGGGCACTGGAAGAGGAGACTGCTCGCATGCTGGCCCAGCGCATGGCCAAGTGCAAC
ACAGGCAGTGAGGGGTCCGAGGCCCAGCCCCCCGGGAAACCGAGCACCGAGGCCCGGTCT
GCGGCCAGCAACACTGGCACCCCCGATGGGCCTGAGGCCCCCCCAGGCCCAGATGCCTCC
CCCGATGCCAGCTTTGGGAAGCAGTGGTCCTCATCCTCCCGTTCCTCCTACTCATCCCAA
CATGGAGGGGCTGTGTCTCCCCAGAGCTTGTCTGAGTGGCGCATGCAGAACATTGCCCGA
GACTCTGAGAACAGCTCCGAGGAAGAGTTCTTTGATGCCCACGAAGGCTTCTCGGACAGT
GAGGAGGTCTTCCCCAAGGAGATGACCAAGTGGAACTCCAATGACTTCATTGATGCCTTT
GCCTCCCCAGTGGAGGCAGAGGGAACGCCAGAGCCTGGAGCCGAGGCAGCTAAAGGCATT
GAGGATGGGGCCCAAGCACCCAGGGACTCAGAGGGCCTGGATGGAGCCGGGGAGCTGGGG
GCTGAGGCATGCGCAGTCCACGCCCTCTTCCTTATCCTGCACAGCGGCAACATCCTGGAC
TCAGGCCCTGGAGACGCCAACTCCAAGCAGGCGGATGTGCAGACGCTGAGCTCCGCCTTC
GAGGCCGTCACCCGCATCCACTTCCCTGAGGCCTTGGGCCACGTGGCGCTGCGACTGGTG
CCCTGTCCACCCATCTGCGCCGCCGCCTATGCCCTTGTCTCCAACCTGAGCCCTTACAGC
CACGATGGGGACAGCCTGTCTCGCTCCCAAGACCACATTCCACTGGCTGCCCTGCCACTG
CTGGCCACCTCATCCTCCCGCTACCAGGGCGCCGTGGCCACCGTCATTGCCCGCACCAAC
CAGGCCTACTCAGCCTTCCTGCGCTCACCTGAGGGTGCCGGCTTCTGTGGGCAGGTCGCA
CTGATTGGAGATGGTGTTGGTGGCATCCTGGGCTTTGATGCACTCTGCCACAGTGCTAAC
GCGGGCACCGGGAGTCGGGGCAGCAGCCGCCGTGGGAGCATGAACAATGAGCTGCTCTCT
CCGGAGTTTGGCCCAGTGCGGGACCCCCTGGCAGATGGTGTGGAAGGCCTGGGTCGGGGC
AGCCCAGAACCCTCGGCCTTGCCTCCCCAGCGCATCCCCAGCGACATGGCCAGTCCTGAG
CCCGAGGGCTCTCAGAACAGCCTTCAGGCAGCCCCCGCAACCACCTCCTCCTGGGAGCCC
CGGCGGGCAAGCACGGCCTTCTGCCCACCCGCTGCCAGTTCCGAGGCACCTGACGGCCCC
AGCAGCACTGCCCGCCTTGACTTCAAGGTCTCTGGCTTCTTCCTCTTCGGCTCCCCACTG
GGCCTGGTGCTGGCTCTGCGCAAAACTGTGATGCCCGCCCTGGAGGCAGCCCAGATGCGC
CCAGCCTGTGAACAGATCTACAACCTCTTCCACGCGGCCGACCCCTGCGCCTCACGCCTC
GAGCCCCTGCTGGCCCCGAAGTTCCAGGCCATCGCCCCACTGACCGTGCCCCGCTACCAG
AAGTTCCCCCTGGGAGATGGCTCATCCCTGCTGCTGGCCGACACTCTGCAGACGCACTCC
AGCCTCTTTCTGGAGGAGCTGGAGATGCTGGTGCCCTCAACACCCACCTCTACTAGCGGT
GCCTTCTGGAAGGGCAGTGAGTTGGCCACTGACCCCCCGGCCCAGCCAGCCGCCCCCAGC
ACCACCAGTGAGGTGGTTAAGATCCTGGAGCGCTGGTGGGGGACCAAGCGGATCGACTAC
TCGCTGTACTGCCCCGAGGCGCTCACCGCCTTTCCCACCGTCACGCTGCCCCACCTCTTC
CACGCCAGCTACTGGGAGTCCGCCGACGTGGTGGCGTTCATCCTGCGCCAGGTGATCGAG
AAGGAGCGGCCACAGCTGGCGGAATGCGAGGAGCCGTCCATCTACAGCCCGGCCTTCCCC
AGGGAGAAGTGGCAGCGAAAACGCACGCAGGTCAAGATCCGGAACGTCACTTCCAACCAC
CGGGCGAGCGACACGGTGGTGTGCGAGGGGCCGCCCCAGGTGCTAAGCGGGCGCTTCATG
TACGGGCCCCTGGACGTCGTCACGCTCACTGGAGAGAAGGTGGATGTCTACATCATGACG
CAGCCGCTGTCGGGCAAGTGGATCCACTTTGGCACCGAAGTCACCAATAGCTCGGGCCGC
CTCACCTTCCCAGTTCCCCCAGAACGCGCGCTGGGCATTGGTGTCTACCCCGTGCGCATG
GTGGTCAGGGGCGACCACACCTATGCCGAATGCTGCCTGACTGTGGTGGCCCGCGGCACG
GAGGCTGTGGTCTTCAGCATCGACGGCTCCTTCACCGCCAGCGTCTCCATCATGGGCAGC
GACCCCAAGGTGCGAGCTGGCGCCGTGGACGTGGTCAGGCACTGGCAGGACTCCGGCTAC
CTGATCGTGTATGTCACAGGCCGGCCGGATATGCAGAAGCACCGCGTGGTGGCATGGCTG
TCGCAGCACAACTTCCCCCACGGCGTCGTCTCCTTCTGCGACGGCCTCACCCACGACCCA
CTACGCCAGAAGGCAATGTTTCTGCAGAGCCTGGTGCAGGAGGTAGAACTGAACATCGTG
GCCGGTTATGGGTCTCCCAAAGATGTGGCTGTATACGCGGCGCTGGGGCTGTCCCCGAGC
CAGACCTACATCGTGGGCCGTGCCGTGCGGAAGCTACAGGCGCAGTGCCAGTTCCTGTCA
GACGGCTATGTGGCCCACCTGGGCCAGCTGGAAGCGGGCTCGCACTCGCATGCCTCCTCG
GGACCCCCGAGAGCTGCCTTGGGCAAGAGCAGCTATGGTGTGGCTGCCCCCGTGGACTTC
CTGCGCAAACAGAGCCAGCTGCTTCGCTCGAGGGGCCCCAGCCAGGCGGAGCGTGAGGGC
CCGGGAACACCACCCACCACCCTGGCACGGGGCAAAGCACGGAGCATCAGCCTGAAGCTG
GACAGCGAGGAGTGA
|
| Enzyme 68 GenBank Gene ID |
AF334584  |
| Enzyme 68 GeneCard ID |
PITPNM1  |
| Enzyme 68 GenAtlas ID |
PITPNM1  |
| Enzyme 68 HGNC ID |
HGNC:9003  |
| Enzyme 68 Chromosome Location |
1 |
| Enzyme 68 Locus |
11q13 |
| Enzyme 68 SNPs |
SNPJam Report  |
| Enzyme 68 General References |
- Rubboli F, Bulfone A, Bogni S, Marchitiello A, Zollo M, Borsani G, Ballabio A, Banfi S: A mammalian homologue of the Drosophila retinal degeneration B gene: implications for the evolution of phototransduction mechanisms. Genes Funct. 1997 Jun;1(3):205-13. [PubMed
]
- Lev S, Hernandez J, Martinez R, Chen A, Plowman G, Schlessinger J: Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol Cell Biol. 1999 Mar;19(3):2278-88. [PubMed
]
- Ocaka L, Spalluto C, Wilson DI, Hunt DM, Halford S: Chromosomal localization, genomic organization and evolution of the genes encoding human phosphatidylinositol transfer protein membrane-associated (PITPNM) 1, 2 and 3. Cytogenet Genome Res. 2005;108(4):293-302. [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
]
- Litvak V, Shaul YD, Shulewitz M, Amarilio R, Carmon S, Lev S: Targeting of Nir2 to lipid droplets is regulated by a specific threonine residue within its PI-transfer domain. Curr Biol. 2002 Sep 3;12(17):1513-8. [PubMed
]
- Tian D, Litvak V, Toledo-Rodriguez M, Carmon S, Lev S: Nir2, a novel regulator of cell morphogenesis. Mol Cell Biol. 2002 Apr;22(8):2650-62. [PubMed
]
- Litvak V, Argov R, Dahan N, Ramachandran S, Amarilio R, Shainskaya A, Lev S: Mitotic phosphorylation of the peripheral Golgi protein Nir2 by Cdk1 provides a docking mechanism for Plk1 and affects cytokinesis completion. Mol Cell. 2004 May 7;14(3):319-30. [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
]
- Amarilio R, Ramachandran S, Sabanay H, Lev S: Differential regulation of endoplasmic reticulum structure through VAP-Nir protein interaction. J Biol Chem. 2005 Feb 18;280(7):5934-44. Epub 2004 Nov 15. [PubMed
]
- Litvak V, Dahan N, Ramachandran S, Sabanay H, Lev S: Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function. Nat Cell Biol. 2005 Mar;7(3):225-34. Epub 2005 Feb 20. [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
]
- 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 68 Metabolite References |
Not Available |
|
Enzyme 69
[top]
|
| Enzyme 69 ID |
12959 |
| Enzyme 69 Name |
Membrane-associated phosphatidylinositol transfer protein 2 |
| Enzyme 69 Synonyms |
- Phosphatidylinositol transfer protein, membrane-associated 2
- PITPnm 2
- Pyk2 N-terminal domain-interacting receptor 3
- NIR-3
|
| Enzyme 69 Gene Name |
PITPNM2 |
| Enzyme 69 Protein Sequence |
>Membrane-associated phosphatidylinositol transfer protein 2
MIIKEYRIPLPMTVEEYRIAQLYMIQKKSRNETYGEGSGVEILENRPYTDGPGGSGQYTH
KVYHVGMHIPSWFRSILPKAALRVVEESWNAYPYTRTRFTCPFVEKFSIDIETFYKTDAG
ENPDVFNLSPVEKNQLTIDFIDIVKDPVPHNEYKTEEDPKLFQSTKTQRGPLSENWIEEY
KKQVFPIMCAYKLCKVEFRYWGMQSKIERFIHDTGLRRVMVRAHRQAWCWQDEWYGLSME
NIRELEKEAQLMLSRKMAQFNEDGEEATELVKHEAVSDQTSGEPPEPSSSNGEPLVGRGL
KKQWSTSSKSSRSSKRGASPSRHSISEWRMQSIARDSDESSDDEFFDAHEDLSDTEEMFP
KDITKWSSNDLMDKIESPEPEDTQDGLYRQGAPEFRVASSVEQLNIIEDEVSQPLAAPPS
KIHVLLLVLHGGTILDTGAGDPSSKKGDANTIANVFDTVMRVHYPSALGRLAIRLVPCPP
VCSDAFALVSNLSPYSHDEGCLSSSQDHIPLAALPLLATSSPQYQEAVATVIQRANLAYG
DFIKSQEGMTFNGQVCLIGDCVGGILAFDALCYSNQPVSESQSSSRRGSVVSMQDNDLLS
PGILMNAAHCCGGGGGGGGGGGSSGGGGSSGGSSLESSRHLSRSNVDIPRSNGTEDPKRQ
LPRKRSDSSTYELDTIQQHQAFLSSLHASVLRTEPCSRHSSSSTMLDGTGALGRFDFEIT
DLFLFGCPLGLVLALRKTVIPALDVFQLRPACQQVYNLFHPADPSASRLEPLLERRFHAL
PPFSVPRYQRYPLGDGCSTLLADVLQTHNAAFQEHGAPSSPGTAPASRGFRRASEISIAS
QVSGMAESYTASSIAQKAPDALSHTPSVRRLSLLALPAPSPTTPGPHPPARKASPGLERA
PGLPELDIGEVAAKWWGQKRIDYALYCPDALTAFPTVALPHLFHASYWESTDVVSFLLRQ
VMRHDNSSILELDGKEVSVFTPSKPREKWQRKRTHVKLRNVTANHRINDALANEDGPQVL
TGRFMYGPLDMVTLTGEKVDVHIMTQPPSGEWLYLDTLVTNNSGRVSYTIPESHRLGVGV
YPIKMVVRGDHTFADSYITVLPKGTEFVVFSIDGSFAASVSIMGSDPKVRAGAVDVVRHW
QDLGYLIIYVTGRPDMQKQRVVAWLAQHNFPHGVVSFCDGLVHDPLRHKANFLKLLISEL
HLRVHAAYGSTKDVAVYSAISLSPMQIYIVGRPTKKLQQQCQFITDGYAAHLAQLKYSHR
ARPARNTATRMALRKGSFGLPGQGDFLRSRNHLLRTISAQPSGPSHRHERTQSQADGEQR
GQRSMSVAAGCWGRAMTGRLEPGAAAGPK
|
| Enzyme 69 Number of Residues |
1349 |
| Enzyme 69 Molecular Weight |
148931.9 |
| Enzyme 69 Theoretical pI |
7.17 |
| Enzyme 69 GO Classification |
| Function |
- binding
- cation binding
- ion binding
- metal ion binding
|
| Process |
- establishment of localization
- transport
|
| Component |
|
|
| Enzyme 69 General Function |
Involved in metal ion binding |
| Enzyme 69 Specific Function |
Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions |
| Enzyme 69 Pathways |
Not Available |
| Enzyme 69 Reactions |
Not Available |
| Enzyme 69 Pfam Domain Function |
|
| Enzyme 69 Signals |
|
| Enzyme 69 Transmembrane Regions |
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
24308237  |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
Q9BZ72  |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
PITM2_HUMAN  |
| Enzyme 69 PDB ID |
Not Available |
| Enzyme 69 Cellular Location |
Not Available |
| Enzyme 69 Gene Sequence |
>4050 bp
ATGATTATAAAGGAATATCGGATTCCTCTGCCAATGACCGTGGAGGAGTACCGCATCGCC
CAGCTGTACATGATACAGAAGAAGAGCCGTAACGAGACATATGGCGAAGGCAGCGGCGTG
GAGATCCTGGAGAACCGGCCGTACACAGATGGCCCAGGCGGCTCTGGGCAGTACACACAC
AAGGTGTATCATGTGGGCATGCACATTCCCAGCTGGTTCCGCTCCATCCTGCCCAAGGCA
GCCCTGCGGGTGGTGGAGGAGTCTTGGAATGCCTACCCCTACACCCGAACCAGGTTCACC
TGTCCTTTCGTGGAGAAATTCTCCATCGACATTGAAACCTTTTATAAAACTGATGCTGGA
GAAAACCCCGACGTGTTCAACCTCTCTCCTGTGGAAAAGAACCAGCTGACAATCGACTTC
ATCGACATTGTCAAAGACCCTGTGCCCCACAACGAGTATAAGACAGAAGAGGACCCCAAG
CTGTTCCAGTCAACCAAGACCCAGCGGGGGCCCCTGTCCGAGAACTGGATCGAGGAGTAC
AAGAAGCAGGTCTTCCCCATCATGTGCGCATACAAGCTCTGCAAGGTGGAGTTCCGCTAC
TGGGGCATGCAGTCCAAGATCGAGAGGTTCATCCACGACACCGGACTACGGAGGGTGATG
GTGCGGGCTCACCGGCAGGCCTGGTGCTGGCAGGACGAGTGGTATGGGCTGAGCATGGAG
AACATCCGGGAGCTGGAGAAGGAGGCACAGCTCATGCTTTCCCGTAAGATGGCCCAGTTC
AATGAGGATGGTGAGGAGGCCACTGAGCTCGTCAAGCACGAAGCCGTCTCGGACCAGACC
TCTGGGGAGCCCCCGGAGCCCAGCAGCAGCAATGGGGAGCCCCTAGTGGGGCGCGGCCTC
AAGAAACAGTGGTCCACATCCTCCAAGTCGTCTCGGTCGTCCAAGCGGGGAGCGAGTCCT
TCCCGCCACAGCATCTCAGAGTGGAGGATGCAGAGTATTGCCAGGGACTCGGATGAGAGC
TCAGATGATGAGTTCTTCGATGCGCACGAGGACCTGTCCGACACAGAGGAAATGTTCCCC
AAGGACATCACCAAGTGGAGCTCCAATGACCTCATGGACAAGATCGAGAGCCCAGAGCCG
GAAGACACACAAGATGGTCTGTACCGCCAGGGTGCCCCTGAGTTCAGGGTGGCCTCCAGT
GTGGAGCAGCTGAACATCATAGAGGACGAGGTTAGCCAGCCGCTGGCTGCACCGCCCTCC
AAGATCCACGTGCTGCTACTGGTGCTGCACGGAGGCACCATCCTGGACACAGGCGCCGGG
GACCCCAGCTCCAAGAAGGGCGATGCTAACACCATCGCCAACGTGTTCGACACCGTCATG
CGCGTGCACTACCCCAGCGCCCTGGGCCGCCTTGCCATCCGCCTGGTGCCCTGCCCGCCC
GTCTGCTCTGACGCCTTTGCCCTGGTCTCCAACCTCAGCCCCTACAGCCATGACGAAGGC
TGTCTGTCCAGCAGTCAGGACCACATTCCCCTGGCTGCCCTCCCCCTGCTGGCCACCTCC
TCCCCCCAGTACCAGGAGGCAGTTGCCACAGTGATTCAGCGAGCCAACCTTGCCTATGGG
GACTTCATCAAGTCCCAGGAGGGCATGACCTTCAATGGGCAGGTCTGCCTGATTGGGGAC
TGCGTCGGGGGCATCCTGGCATTTGATGCCCTGTGCTACAGTAACCAGCCGGTGTCTGAG
AGTCAGAGCAGCAGCCGCCGGGGCAGCGTGGTCAGCATGCAGGACAATGACCTGCTGTCC
CCGGGCATCCTGATGAATGCAGCACACTGCTGCGGTGGTGGCGGTGGCGGCGGTGGCGGT
GGTGGCAGCAGTGGTGGTGGTGGCAGTAGTGGTGGCTCCAGCCTGGAGAGCAGTCGGCAC
CTGAGCCGAAGCAACGTCGACATCCCCCGCAGCAACGGCACTGAGGACCCCAAAAGGCAA
CTGCCCCGCAAGAGGAGCGACTCATCCACCTACGAGCTGGATACCATCCAGCAGCACCAG
GCCTTCCTGTCCAGCCTCCATGCCAGCGTGCTGAGGACTGAGCCCTGCTCACGCCATTCC
AGCAGCTCCACCATGCTGGATGGCACAGGTGCCCTGGGCAGGTTTGACTTTGAGATCACC
GACCTCTTCCTCTTCGGGTGCCCGCTGGGGCTGGTCCTGGCCTTGAGGAAGACTGTCATC
CCAGCCCTGGATGTTTTCCAGCTGCGGCCGGCCTGCCAGCAAGTCTACAACCTCTTCCAC
CCCGCGGACCCGTCAGCTTCACGCCTGGAGCCGCTGCTGGAACGGCGCTTTCACGCCCTG
CCGCCTTTCAGCGTCCCCCGCTACCAACGCTACCCGCTGGGGGATGGCTGCTCCACGCTG
CTGGCGGATGTGCTCCAGACCCACAATGCAGCCTTCCAAGAGCATGGCGCCCCCTCCTCG
CCGGGCACTGCCCCTGCCAGTCGTGGCTTCCGCCGAGCCAGTGAGATCAGCATCGCCAGC
CAGGTGTCAGGCATGGCTGAGAGCTACACGGCATCCAGCATCGCCCAGAAGGCCCCCGAT
GCGCTCAGCCATACCCCCAGCGTCAGGCGTCTGTCCCTGCTCGCCCTGCCCGCCCCCAGC
CCCACCACCCCTGGCCCCCACCCTCCAGCCAGGAAGGCAAGCCCTGGCCTGGAGAGGGCC
CCTGGCCTCCCTGAGCTGGACATTGGAGAAGTCGCTGCAAAGTGGTGGGGCCAGAAGCGG
ATCGACTACGCCCTGTACTGCCCTGACGCCCTCACGGCCTTCCCCACGGTGGCTCTGCCT
CACCTCTTCCACGCCAGCTACTGGGAGTCAACAGACGTGGTCTCCTTTCTGCTGAGACAG
GTCATGAGGCATGACAACTCCAGCATCTTGGAGCTGGATGGCAAGGAAGTGTCGGTGTTC
ACCCCCTCAAAGCCAAGGGAGAAGTGGCAGCGCAAGCGGACCCACGTGAAGCTGCGGAAC
GTGACGGCCAACCACCGGATCAATGATGCCCTTGCCAATGAGGACGGCCCCCAGGTTCTG
ACGGGCAGGTTCATGTATGGGCCCCTGGACATGGTCACCCTGACTGGGGAGAAGGTGGAT
GTGCACATCATGACCCAGCCGCCCTCAGGCGAGTGGCTCTACCTGGATACGCTGGTGACC
AACAACAGTGGGCGTGTCTCCTACACCATCCCTGAGTCGCACCGCCTGGGCGTGGGTGTC
TACCCTATCAAGATGGTGGTCAGGGGAGACCACACGTTTGCCGACAGCTACATCACCGTG
CTGCCCAAGGGCACAGAGTTCGTGGTCTTCAGCATCGACGGTTCCTTTGCCGCTAGCGTG
TCCATCATGGGCAGCGACCCCAAGGTGCGGGCCGGGGCCGTGGACGTGGTGCGGCACTGG
CAGGACCTGGGCTACCTCATCATCTACGTGACGGGCCGGCCCGACATGCAGAAGCAGCGG
GTGGTGGCGTGGCTGGCCCAGCACAACTTCCCCCATGGCGTGGTGTCCTTCTGTGACGGC
CTGGTGCATGACCCGCTGCGGCACAAGGCCAACTTCCTGAAGCTGCTCATCTCCGAGCTG
CACCTGCGCGTGCACGCGGCCTATGGCTCCACCAAGGACGTGGCGGTGTACAGCGCCATT
AGCCTGTCCCCCATGCAGATCTACATCGTGGGCCGGCCCACCAAGAAGCTGCAGCAGCAG
TGCCAGTTCATCACGGATGGCTACGCGGCCCACCTGGCGCAGCTGAAGTACAGCCACCGG
GCGCGGCCCGCTCGCAACACGGCCACCCGCATGGCGCTGCGCAAGGGCAGCTTCGGCCTG
CCCGGCCAGGGCGACTTTCTGCGCTCCCGGAACCACCTGCTTCGCACCATCTCGGCCCAG
CCCAGCGGGCCCAGCCACCGGCACGAGCGGACACAGAGCCAGGCGGATGGCGAGCAGCGG
GGCCAGCGCAGCATGAGTGTGGCGGCCGGCTGCTGGGGCCGCGCCATGACTGGCCGCCTG
GAGCCGGGGGCAGCCGCGGGCCCCAAGTAG
|
| Enzyme 69 GenBank Gene ID |
NM_020845.2  |
| Enzyme 69 GeneCard ID |
PITPNM2  |
| Enzyme 69 GenAtlas ID |
PITPNM2  |
| Enzyme 69 HGNC ID |
HGNC:21044  |
| Enzyme 69 Chromosome Location |
1 |
| Enzyme 69 Locus |
12q24.31 |
| Enzyme 69 SNPs |
SNPJam Report  |
| Enzyme 69 General References |
- Lev S, Hernandez J, Martinez R, Chen A, Plowman G, Schlessinger J: Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol Cell Biol. 1999 Mar;19(3):2278-88. [PubMed
]
- Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed
]
|
| Enzyme 69 Metabolite References |
Not Available |
|
Enzyme 70
[top]
|
| Enzyme 70 ID |
12960 |
| Enzyme 70 Name |
Membrane-associated phosphatidylinositol transfer protein 3 |
| Enzyme 70 Synonyms |
- Phosphatidylinositol transfer protein, membrane-associated 3
- PITPnm 3
- Pyk2 N-terminal domain-interacting receptor 1
- NIR-1
|
| Enzyme 70 Gene Name |
PITPNM3 |
| Enzyme 70 Protein Sequence |
>Membrane-associated phosphatidylinositol transfer protein 3
MAKAGRAGGPPPGGGAPWHLRNVLSDSVESSDDEFFDAREEMAEGKNAILIGMSQWNSND
LVEQIETMGKLDEHQGEGTAPCTSSILQEKQRELYRVSLRRQRFPAQGSIEIHEDSEEGC
PQRSCKTHVLLLVLHGGNILDTGAGDPSCKAADIHTFSSVLEKVTRAHFPAALGHILIKF
VPCPAICSEAFSLVSHLNPYSHDEGCLSSSQDHVPLAALPLLAISSPQYQDAVATVIERA
NQVYREFLKSSDGIGFSGQVCLIGDCVGGLLAFDAICYSAGPSGDSPASSSRKGSISSTQ
DTPVAVEEDCSLASSKRLSKSNIDISSGLEDEEPKRPLPRKQSDSSTYDCEAITQHHAFL
SSIHSSVLKDESETPAAGGPQLPEVSLGRFDFDVSDFFLFGSPLGLVLAMRRTVLPGLDG
FQVRPACSQVYSFFHCADPSASRLEPLLEPKFHLVPPVSVPRYQRFPLGDGQSLLLADAL
HTHSPLFLEGSSRDSPPLLDAPASPPQASRFQRPGRRMSEGSSHSESSESSDSMAPVGAS
RITAKWWGSKRIDYALYCPDVLTAFPTVALPHLFHASYWESTDVVAFILRQVMRYESVNI
KESARLDPAALSPANPREKWLRKRTQVKLRNVTANHRANDVIAAEDGPQVLVGRFMYGPL
DMVALTGEKVDILVMAEPSSGRWVHLDTEITNSSGRITYNVPRPRRLGVGVYPVKMVVRG
DQTCAMSYLTVLPRGMECVVFSIDGSFAASVSIMGSDPKVRPGAVDVVRHWQDLGYMILY
ITGRPDMQKQRVVSWLSQHNFPQGMIFFSDGLVHDPLRQKAIFLRNLMQECFIKISAAYG
STKDISVYSVLGLPASQIFIVGRPTKKYQTQCQFLSEGYAAHLAALEASHRSRPKKNNSR
MILRKGSFGLHAQPEFLRKRNHLRRTMSVQQPDPPAANPKPERAQSQPESDKDHERPLPA
LSWARGPPKFESVP
|
| Enzyme 70 Number of Residues |
974 |
| Enzyme 70 Molecular Weight |
106780.1 |
| Enzyme 70 Theoretical pI |
7.14 |
| Enzyme 70 GO Classification |
| Function |
- binding
- cation binding
- ion binding
- metal ion binding
|
| Process |
- establishment of localization
- transport
|
| Component |
|
|
| Enzyme 70 General Function |
Involved in metal ion binding |
| Enzyme 70 Specific Function |
Catalyzes the transfer of phosphatidylinositol and phosphatidylcholine between membranes (in vitro). Binds calcium ions |
| Enzyme 70 Pathways |
Not Available |
| Enzyme 70 Reactions |
Not Available |
| Enzyme 70 Pfam Domain Function |
|
| Enzyme 70 Signals |
|
| Enzyme 70 Transmembrane Regions |
|
| Enzyme 70 Essentiality |
Not Available |
| Enzyme 70 GenBank ID Protein |
190358515  |
| Enzyme 70 UniProtKB/Swiss-Prot ID |
Q9BZ71  |
| Enzyme 70 UniProtKB/Swiss-Prot Entry Name |
PITM3_HUMAN  |
| Enzyme 70 PDB ID |
Not Available |
| Enzyme 70 Cellular Location |
Not Available |
| Enzyme 70 Gene Sequence |
>2925 bp
ATGGCCAAGGCGGGCCGTGCAGGTGGTCCTCCCCCGGGCGGCGGTGCCCCCTGGCACCTT
CGAAATGTCCTCAGTGACTCTGTGGAGAGCTCAGATGATGAATTCTTTGATGCCAGAGAG
GAGATGGCTGAAGGGAAGAATGCCATCCTCATTGGGATGAGCCAGTGGAACTCCAATGAC
CTCGTGGAGCAGATCGAGACCATGGGGAAACTGGACGAGCATCAAGGAGAAGGGACCGCG
CCGTGCACATCCAGCATCCTCCAGGAGAAGCAGCGAGAACTGTACCGGGTTTCCTTGAGA
AGACAGAGGTTCCCAGCCCAGGGAAGCATCGAGATCCACGAAGACAGCGAGGAAGGCTGC
CCGCAGCGCTCCTGCAAGACACATGTCCTCCTGCTGGTCCTGCATGGGGGAAACATCCTG
GACACGGGTGCCGGGGACCCGTCCTGCAAGGCAGCCGACATCCACACCTTCAGCTCCGTG
CTGGAGAAGGTCACACGAGCCCATTTCCCTGCTGCCCTGGGCCACATCCTCATCAAGTTC
GTCCCCTGTCCTGCCATCTGCTCTGAGGCTTTCTCGCTTGTCTCTCACCTGAACCCCTAC
AGCCACGATGAGGGCTGCCTCAGCAGCAGCCAGGACCACGTCCCTCTGGCCGCCCTTCCC
CTGTTGGCCATCTCCTCCCCGCAGTACCAGGATGCTGTCGCCACCGTCATCGAGCGAGCC
AACCAGGTCTACAGAGAGTTCCTGAAGTCCTCTGATGGGATTGGCTTCAGTGGGCAGGTG
TGTCTCATCGGGGACTGTGTGGGGGGCCTCCTGGCCTTCGATGCCATCTGCTACAGTGCG
GGGCCCTCAGGGGACAGCCCTGCCAGCAGCAGCCGGAAGGGGAGCATCAGCAGCACCCAG
GACACCCCAGTCGCGGTGGAGGAAGATTGCAGCCTGGCCAGCAGCAAGCGTCTCAGCAAA
AGCAACATTGACATCTCCAGTGGGTTGGAGGATGAGGAGCCCAAGAGGCCGTTGCCGCGG
AAACAGAGCGACTCCTCCACCTATGACTGCGAGGCCATCACCCAGCACCATGCCTTCCTC
TCAAGCATCCACTCCAGCGTGCTAAAGGATGAGTCTGAGACCCCGGCGGCTGGGGGGCCG
CAGCTCCCTGAGGTCAGCCTGGGCCGCTTTGACTTCGATGTGTCCGACTTCTTCCTCTTC
GGCTCGCCACTGGGCCTGGTCCTGGCCATGCGGAGGACGGTGCTGCCTGGGCTGGACGGC
TTCCAGGTGCGTCCTGCCTGCAGCCAGGTCTACAGCTTCTTCCATTGCGCAGACCCCTCT
GCCTCACGGCTCGAGCCACTGCTGGAGCCCAAGTTCCACCTGGTGCCGCCTGTCAGCGTG
CCTCGCTACCAGAGGTTCCCACTGGGCGATGGGCAGTCCCTCCTCCTCGCTGATGCCCTA
CACACCCACAGCCCCCTCTTCCTGGAGGGCAGCTCCCGGGACAGCCCGCCACTTCTGGAT
GCCCCTGCCTCGCCCCCTCAGGCCTCGAGGTTCCAGCGCCCAGGACGGAGGATGAGCGAG
GGGAGCTCCCACAGCGAGAGCTCGGAGTCCTCGGACAGCATGGCACCCGTGGGTGCCTCC
CGCATCACAGCCAAGTGGTGGGGAAGCAAGAGGATCGACTATGCCCTGTACTGCCCTGAT
GTCCTCACGGCCTTCCCCACCGTGGCCCTGCCCCACCTCTTCCACGCCAGTTACTGGGAG
TCCACAGACGTGGTGGCCTTCATCCTGAGACAGGTAATGCGCTATGAGAGCGTGAACATC
AAGGAAAGCGCCCGCCTGGACCCTGCAGCACTGAGTCCTGCCAACCCCCGGGAGAAGTGG
CTTCGTAAGCGGACTCAGGTCAAGCTGAGGAATGTCACGGCTAATCACCGGGCCAATGAT
GTGATTGCTGCTGAAGATGGCCCCCAGGTCCTGGTGGGGCGGTTCATGTACGGGCCCCTC
GACATGGTGGCTCTGACTGGAGAGAAGGTGGACATCCTAGTAATGGCAGAGCCATCCTCA
GGCCGCTGGGTACACCTGGACACAGAGATCACCAACAGCAGTGGTCGCATCACATACAAT
GTGCCGCGGCCCCGGCGCCTGGGGGTTGGTGTCTATCCTGTGAAGATGGTCGTCAGGGGC
GACCAGACCTGTGCCATGAGCTACCTCACGGTGTTGCCCAGGGGCATGGAGTGTGTAGTG
TTCAGCATTGATGGGTCCTTCGCGGCCAGCGTGTCTATCATGGGAAGCGACCCCAAGGTC
CGGCCGGGTGCAGTGGATGTTGTCCGGCACTGGCAGGACTTGGGCTACATGATCCTTTAC
ATCACGGGACGGCCGGACATGCAGAAGCAGCGGGTGGTGTCGTGGCTGTCCCAGCACAAC
TTCCCACAGGGCATGATCTTCTTCTCCGATGGGCTGGTGCATGACCCGCTGCGGCAGAAG
GCCATCTTCCTGCGCAACCTCATGCAGGAGTGCTTCATCAAAATCAGTGCGGCCTATGGC
TCCACGAAGGACATCTCTGTCTACAGCGTGCTGGGCCTGCCTGCCTCCCAGATCTTCATT
GTGGGCCGGCCCACCAAGAAGTACCAAACCCAGTGCCAGTTCCTGAGCGAGGGCTACGCC
GCACACCTGGCCGCGCTGGAGGCCAGCCACCGCTCACGCCCAAAGAAGAACAACTCGCGC
ATGATCCTGCGCAAGGGCAGCTTCGGGCTGCACGCGCAGCCAGAGTTCCTGCGGAAGCGC
AACCACCTGCGCAGAACCATGTCAGTGCAGCAGCCCGACCCGCCCGCCGCCAACCCCAAG
CCCGAGCGGGCCCAGAGCCAGCCCGAGTCGGACAAAGACCACGAGCGGCCGCTGCCGGCG
CTCAGCTGGGCGCGTGGGCCCCCCAAGTTCGAGTCGGTGCCCTGA
|
| Enzyme 70 GenBank Gene ID |
NM_031220.3  |
| Enzyme 70 GeneCard ID |
PITPNM3  |
| Enzyme 70 GenAtlas ID |
PITPNM3  |
| Enzyme 70 HGNC ID |
HGNC:21043  |
| Enzyme 70 Chromosome Location |
1 |
| Enzyme 70 Locus |
17p13 |
| Enzyme 70 SNPs |
SNPJam Report  |
| Enzyme 70 General References |
- Lev S, Hernandez J, Martinez R, Chen A, Plowman G, Schlessinger J: Identification of a novel family of targets of PYK2 related to Drosophila retinal degeneration B (rdgB) protein. Mol Cell Biol. 1999 Mar;19(3):2278-88. [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
]
- 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
]
- 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
]
- Kohn L, Kadzhaev K, Burstedt MS, Haraldsson S, Hallberg B, Sandgren O, Golovleva I: Mutation in the PYK2-binding domain of PITPNM3 causes autosomal dominant cone dystrophy (CORD5) in two Swedish families. Eur J Hum Genet. 2007 Jun;15(6):664-71. Epub 2007 Mar 21. [PubMed
]
|
| Enzyme 70 Metabolite References |
Not Available |
|
Enzyme 71
[top]
|
| Enzyme 71 ID |
13574 |
| Enzyme 71 Name |
Cytosolic phospholipase A2 delta |
| Enzyme 71 Synonyms |
- cPLA2-delta
- Phospholipase A2 group IVD
|
| Enzyme 71 Gene Name |
PLA2G4D |
| Enzyme 71 Protein Sequence |
>Cytosolic phospholipase A2 delta
MESLSPGGPPGHPYQGEASTCWQLTVRVLEARNLRWADLLSEADPYVILQLSTAPGMKFK
TKTLTDTSHPVWNEAFRFLIQSQVKNVLELSIYDEDSVTEDDICFKVLYDISEVLPGKLL
RKTFSQSPQGEEELDVEFLMEETSDRPENLITNKVIVARELSCLDVHLDSTGSTAVVADQ
DKLELELVLKGSYEDTQTSFLGTASAFRFHYMAALETELSGRLRSSRSNGWNGDNSAGYL
TVPLRPLTIGKEVTMDVPAPNAPGVRLQLKAEGCPEELAVHLGFNLCAEEQAFLSRRKQV
VAKALKQALQLDRDLQEDEVPVVGIMATGGGARAMTSLYGHLLALQKLGLLDCVTYFSGI
SGSTWTMAHLYGDPEWSQRDLEGPIRYAREHLAKSKLEVFSPERLASYRRELELRAEQGH
PTTFVDLWALVLESMLHGQVMDQKLSGQRAALERGQNPLPLYLSLNVKENNLETLDFKEW
VEFSPYEVGFLKYGAFVPPELFGSEFFMGRLMRRIPEPRICFLEAIWSNIFSLNLLDAWY
DLTSSGESWKQHIKDKTRSLEKEPLTTSGTSSRLEASWLQPGTALAQAFKGFLTGRPLHQ
RSPNFLQGLQLHQDYCSHKDFSTWADYQLDSMPSQLTPKEPRLCLVDAAYFINTSSPSMF
RPGRRLDLILSFDYSLSAPFEALQQTELYCRARGLPFPRVEPSPQDQHQPRECHLFSDPA
CPEAPILLHFPLVNASFKDHSAPGVQRSPAELQGGQVDLTGATCPYTLSNMTYKEEDFER
LLRLSDYNVQTSQGAILQALRTALKHRTLEARPPRAQT
|
| Enzyme 71 Number of Residues |
818 |
| Enzyme 71 Molecular Weight |
91951.4 |
| Enzyme 71 Theoretical pI |
5.19 |
| Enzyme 71 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 71 General Function |
Involved in metabolic process |
| Enzyme 71 Specific Function |
Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Not arachidonic acid-specific but has linoleic acid-specific activity. May play a role in inflammation in psoriatic lesions |
| Enzyme 71 Pathways |
|
| Enzyme 71 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 71 Pfam Domain Function |
|
| Enzyme 71 Signals |
|
| Enzyme 71 Transmembrane Regions |
|
| Enzyme 71 Essentiality |
Not Available |
| Enzyme 71 GenBank ID Protein |
29467442  |
| Enzyme 71 UniProtKB/Swiss-Prot ID |
Q86XP0  |
| Enzyme 71 UniProtKB/Swiss-Prot Entry Name |
PA24D_HUMAN  |
| Enzyme 71 PDB ID |
Not Available |
| Enzyme 71 Cellular Location |
Not Available |
| Enzyme 71 Gene Sequence |
>2457 bp
ATGGAGAGCCTGTCACCTGGGGGACCAACTGGCCACCCTTACCAGGGGGAGGCCTCTACC
TGCTGGCAGCTCACAGTGAGGGTCCTGGAGGCGCGGAACCTGCGCTGGGCTGACCTGTTG
AGTGAGGCCGACCCTTACGTGATCCTACAGCTGTCGACCGCACCTGGAATGAAGTTTAAG
ACCAAGACGCTCACCGACACCAGTCATCCTGTGTGGAATGAGGCCTTCCGTTTCCTTATC
CAAAGTCAGGTCAAGAATGTTCTGGAGCTTAGCATCTATGATGAGGACTCAGTCACGGAG
GATGACATCTGCTTCAAGGTTCTCTATGACATCTCAGAAGTCCTCCCTGGCAAGCTGCTC
CGGAAAACCTTCTCCCAGAGTCCCCAGGGAGAGGAGGAGCTGGATGTGGAGTTCCTGATG
GAAGAAACGTCAGATCGCCCAGAAAACCTCATCACCAACAAAGTCATTGTGGCCCGAGAG
CTGTCATGCCTGGATGTGCATCTGGACAGCACAGGGAGCACCGCTGTGGTTGCAGATCAG
GACAAGCTGGAGCTGGAGCTGGTGCTGAAGGGGTCCTATGAGGACACACAGACATCCTTC
CTGGGCACAGCCTCTGCCTTCCGCTTCCACTACATGGCAGCCCTAGAGACAGAGCTGAGC
GGGCGCCTGAGGAGCTCCAGAAGCAATGGCTGGAATGGGGACAACTCAGCTGGGTACCTC
ACTGTGCCCCTGAGGCCCTTGACCATTGGGAAGGAGGTGACTATGGATGTTCCTGCTCCA
AATGCCCCAGGAGTGAGGCTGCAGCTCAAGGCAGAGGGCTGCCCTGAGGAGCTGGCCGTG
CACCTGGGCTTCAATCTCTGTGCAGAGGAGCAGGCCTTCCTGAGCAGGAGGAAGCAGGTG
GTGGCCAAGGCCCTGAAGCAGGCCCTGCAGCTGGACAGAGACCTGCAGGAGGATGAGGTA
CCCGTTGTGGGCATCATGGCCACAGGAGGAGGTGCCCGGGCCATGACCTCACTCTACGGC
CACCTATTGGCCTTGCAGAAGCTGGGCCTCCTAGACTGTGTGACCTACTTCAGTGGCATC
TCTGGCTCTACGTGGACAATGGCCCACCTGTACGGGGACCCTGAGTGGTCGCAGAGGGAC
CTGGAGGGACCTATCAGATACGCCCGGGAGCACCTGGCCAAGAGCAAGCTGGAGGTCTTT
TCCCCAGAGCGCCTGGCGAGCTACCGCCGGGAGCTGGAGCTGCGGGCTGAGCAGGGCCAC
CCCACGACCTTTGTGGACCTGTGGGCGCTAGTGCTGGAGTCCATGCTGCACGGCCAGGTG
ATGGATCAGAAGCTGTCAGGACAGAGAGCCGCCCTGGAACGGGGTCAGAACCCTCTGCCC
CTCTACTTGAGCCTCAATGTCAAAGAGAACAATCTGGAGACACTGGACTTCAAGGAGTGG
GTTGAGTTCTCCCCCTATGAGGTCGGTTTCCTGAAGTACGGGGCCTTCGTCCCTCCTGAG
CTCTTCGGCTCCGAGTTCTTCATGGGACGGCTGATGAGGAGGATCCCGGAGCCCCGGATC
TGCTTTCTGGAAGCCATCTGGAGCAACATTTTCTCCCTGAACCTGCTGGATGCCTGGTAT
GACCTCACCAGTTCTGGGGAGTCCTGGAAACAGCACATCAAGGACAAGACCAGGAGCTTA
GAGAAGGAGCCCCTGACCACCTCGGGGACCTCCTCGCGGCTGGAGGCCTCGTGGCTGCAG
CCAGGCACGGCGCTGGCCCAGGCATTTAAAGGCTTCCTGACAGGCAGGCCCCTCCACCAG
CGCAGCCCCAACTTCCTCCAGGGCCTCCAGCTGCACCAGGACTACTGTAGCCACAAAGAC
TTCTCCACCTGGGCAGACTACCAGCTTGACTCCATGCCCAGCCAGCTGACCCCCAAGGAG
CCCCGGCTCTGCCTGGTGGACGCCGCCTACTTCATCAACACCAGCTCTCCCTCCATGTTC
CGGCCAGGCCGCAGGCTGGACCTCATCCTCTCCTTCGACTACTCCCTATCTGCGCCCTTC
GAGGCACTGCAGCAGACGGAGCTGTACTGCCGGGCCCGGGGGCTGCCCTTCCCCCGGGTG
GAACCCAGCCCTCAGGACCAGCACCAGCCAAGGGAATGCCACCTCTTCTCAGACCCCGCC
TGCCCCGAGGCCCCGATCCTGCTGCACTTCCCGCTGGTCAATGCCTCCTTCAAGGACCAC
TCAGCCCCCGGTGTCCAGCGCAGCCCCGCAGAGCTCCAGGGTGGCCAAGTGGATCTCACC
GGGGCCACCTGCCCCTACACCCTGTCCAACATGACCTACAAGGAGGAAGACTTCGAGCGC
CTGCTGCGGCTCAGTGACTACAACGTGCAGACCAGCCAGGGTGCCATCCTGCAGGCCCTG
AGGACCGCGCTGAAGCACCGGACTCTAGAGGCGAGGCCTCCAAGGGCACAGACCTGA
|
| Enzyme 71 GenBank Gene ID |
AB090876  |
| Enzyme 71 GeneCard ID |
PLA2G4D  |
| Enzyme 71 GenAtlas ID |
PLA2G4D  |
| Enzyme 71 HGNC ID |
HGNC:30038  |
| Enzyme 71 Chromosome Location |
1 |
| Enzyme 71 Locus |
15q15.1 |
| Enzyme 71 SNPs |
SNPJam Report  |
| Enzyme 71 General References |
- Chiba H, Michibata H, Wakimoto K, Seishima M, Kawasaki S, Okubo K, Mitsui H, Torii H, Imai Y: Cloning of a gene for a novel epithelium-specific cytosolic phospholipase A2, cPLA2delta, induced in psoriatic skin. J Biol Chem. 2004 Mar 26;279(13):12890-7. Epub 2004 Jan 6. [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
]
- 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
]
- Tao R, Yu Y, Zhang X, Shi J, Guo Y, Wang C, Han B, Xu Q, Shang H, Zhang X, Xie L, Liu S, Ju G, Shen Y, Wei J: A family based study of the genetic association between the PLA2G4D gene and schizophrenia. Prostaglandins Leukot Essent Fatty Acids. 2005 Dec;73(6):419-22. Epub 2005 Oct 6. [PubMed
]
|
| Enzyme 71 Metabolite References |
Not Available |
|
Enzyme 72
[top]
|
| Enzyme 72 ID |
13575 |
| Enzyme 72 Name |
Cytosolic phospholipase A2 epsilon |
| Enzyme 72 Synonyms |
- cPLA2-epsilon
- Phospholipase A2 group IVE
|
| Enzyme 72 Gene Name |
PLA2G4E |
| Enzyme 72 Protein Sequence |
>Cytosolic phospholipase A2 epsilon
MLLRQMHARVSHSLPDPCQAEDSRPSATCALKAPQTSWDGLLREGLSPCHLLTVRVIRMK
NVRQADMLSQTDCFVSLWLPTASQKKLRTRTISNCPNPEWNESFNFQIQSRVKNVLELSV
CDEDTVTPDDHLLTVLYDLTKLCFRKKTHVKFPLNPQGMEELEVEFLLEESPSPPETLVT
NGVLVSRGHGWLLLSGEQDQGRKQWAKDLLVMVNESFENTQRVRPCLEPCCPTSACFHYP
KYFQSQVHVEVPKSHWSCGLCCRSRKKGPISQPLDCLSDGQVMTLPVGGGESLGSPETLD
VRLGFSLCPAELEFLQKRKVVVAKALKQVLQLEEDLQEDEVPLIAIMATGGGTRSMTSMY
GHLLGLQKLNLLDCASYITGLSGATWTMATLYRDPDWSSKNLEPAIFEARRHVVKDKLPS
LFPDQLRKFQEELRQRSQEGYRVTFTDFWGLLIETCLGDERNECKLSDQRAALSCGQNPL
PIYLTINVKDDVSNQDFREWFEFSPYEVGLQKYGAFIPSELFGSEFFMGRLVKRIPESRI
CYMLGLWSSIFSLNLLDAWNLSHTSEEFFHRWTREKVQDIEDEPILPEIPKCDANILETT
VVIPGSWLSNSFREILTHRSFVSEFHNFLSGLQLHTNYLQNGQFSRWKDTVLDGFPNQLT
ESANHLCLLDTAFFVNSSYPPLLRPERKADLIIHLNYCAGSQTKPLKQTCEYCTVQNIPF
PKYELPDENENLKECYLMENPQEPDAPIVTFFPLINDTFRKYKAPGVERSPEELEQGQVD
IYGPKTPYATKELTYTEATFDKLVKLSEYNILNNKDTLLQALRLAVEKKKRLKGQCPS
|
| Enzyme 72 Number of Residues |
838 |
| Enzyme 72 Molecular Weight |
95686.5 |
| Enzyme 72 Theoretical pI |
5.78 |
| Enzyme 72 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 72 General Function |
Involved in metabolic process |
| Enzyme 72 Specific Function |
Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position |
| Enzyme 72 Pathways |
|
| Enzyme 72 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 72 Pfam Domain Function |
|
| Enzyme 72 Signals |
|
| Enzyme 72 Transmembrane Regions |
|
| Enzyme 72 Essentiality |
Not Available |
| Enzyme 72 GenBank ID Protein |
Not Available |
| Enzyme 72 UniProtKB/Swiss-Prot ID |
Q3MJ16  |
| Enzyme 72 UniProtKB/Swiss-Prot Entry Name |
PA24E_HUMAN  |
| Enzyme 72 PDB ID |
Not Available |
| Enzyme 72 Cellular Location |
Not Available |
| Enzyme 72 Gene Sequence |
Not Available |
| Enzyme 72 GenBank Gene ID |
Not Available |
| Enzyme 72 GeneCard ID |
PLA2G4E  |
| Enzyme 72 GenAtlas ID |
PLA2G4E  |
| Enzyme 72 HGNC ID |
HGNC:24791  |
| Enzyme 72 Chromosome Location |
1 |
| Enzyme 72 Locus |
15q15.1 |
| Enzyme 72 SNPs |
SNPJam Report  |
| Enzyme 72 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 72 Metabolite References |
Not Available |
|
Enzyme 73
[top]
|
| Enzyme 73 ID |
13576 |
| Enzyme 73 Name |
Cytosolic phospholipase A2 zeta |
| Enzyme 73 Synonyms |
- cPLA2-zeta
- Phospholipase A2 group IVF
|
| Enzyme 73 Gene Name |
PLA2G4F |
| Enzyme 73 Protein Sequence |
>Cytosolic phospholipase A2 zeta
MLWALWPRWLADKMLPLLGAVLLQKREKRGPLWRHWRRETYPYYDLQVKVLRATNIRGTD
LLSKADCYVQLWLPTASPSPAQTRIVANCSDPEWNETFHYQIHGAVKNVLELTLYDKDIL
GSDQLSLLLFDLRSLKCGQPHKHTFPLNHQDSQELQVEFVLEKSQVPASEVITNGVLVAH
PCLRIQGTLRGDGTAPREEYGSRQLQLAVPGAYEKPQLLPLQPPTEPGLPPTFTFHVNPV
LSSRLHVELMELLAAVQSGPSAELEAQTSKLGEGGILLSSLPLGQEEQCSVALGEGQEVA
LSMKVEMSSGDLDLRLGFDLSDGEQEFLDRRKQVVSKALQQVLGLSEALDSGQVPVVAVL
GSGGGTRAMSSLYGSLAGLQELGLLDTVTYLSGVSGSTWCISTLYRDPAWSQVALQGPIE
RAQVHVCSSKMGALSTERLQYYTQELGVRERSGHSVSLIDLWGLLVEYLLYQEENPAKLS
DQQEAVRQGQNPYPIYTSVNVRTNLSGEDFAEWCEFTPYEVGFPKYGAYVPTELFGSELF
MGRLLQLQPEPRICYLQGMWGSAFATSLDEIFLKTAGSGLSFLEWYRGSVNITDDCQKPQ
LHNPSRLRTRLLTPQGPFSQAVLDIFTSRFTSAQSFNFTRGLCLHKDYVAGREFVAWKDT
HPDAFPNQLTPMRDCLYLVDGGFAINSPFPLALLPQRAVDLILSFDYSLEAPFEVLKMTE
KYCLDRGIPFPSIEVGPEDVEEARECYLFAKAEDPRSPIVLHFPLVNRTFRTHLAPGVER
QTAEEKAFGDFVINRPDTPYGMMNFTYEPQDFYRLVALSRYNVLNNVETLKCALQLALDR
HQARERAGA
|
| Enzyme 73 Number of Residues |
849 |
| Enzyme 73 Molecular Weight |
95049.4 |
| Enzyme 73 Theoretical pI |
5.11 |
| Enzyme 73 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 73 General Function |
Involved in metabolic process |
| Enzyme 73 Specific Function |
Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Has higher enzyme activity for phosphatidylethanolamine than phosphatidylcholine |
| Enzyme 73 Pathways |
|
| Enzyme 73 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 73 Pfam Domain Function |
|
| Enzyme 73 Signals |
|
| Enzyme 73 Transmembrane Regions |
|
| Enzyme 73 Essentiality |
Not Available |
| Enzyme 73 GenBank ID Protein |
281371376  |
| Enzyme 73 UniProtKB/Swiss-Prot ID |
Q68DD2  |
| Enzyme 73 UniProtKB/Swiss-Prot Entry Name |
PA24F_HUMAN  |
| Enzyme 73 PDB ID |
Not Available |
| Enzyme 73 Cellular Location |
Not Available |
| Enzyme 73 Gene Sequence |
>2550 bp
ATGCTTTGGGCACTCTGGCCAAGGTGGCTGGCAGACAAGATGCTGCCCCTCCTGGGGGCA
GTGCTGCTTCAGAAGAGAGAGAAGAGGGGCCCTCTGTGGAGGCACTGGCGGCGGGAAACC
TACCCATACTATGACCTCCAGGTGAAGGTGCTGAGGGCCACAAACATCCGGGGCACAGAC
CTGCTGTCCAAAGCCGACTGCTATGTGCAACTGTGGCTGCCCACGGCGTCCCCAAGCCCT
GCCCAGACTAGGATAGTGGCCAACTGCAGTGACCCCGAGTGGAATGAGACCTTCCACTAC
CAGATCCATGGTGCTGTGAAGAACGTCCTGGAGCTCACCCTCTATGACAAGGACATCCTG
GGCAGCGACCAGCTCTCTCTGCTCCTGTTTGACCTGAGAAGCCTCAAGTGTGGCCAACCT
CACAAACACACCTTCCCACTCAACCACCAGGATTCACAAGAGCTGCAGGTGGAATTTGTT
CTGGAGAAGAGCCAGGTGCCTGCATCTGAAGTCATCACCAACGGGGTTCTGGTGGCTCAC
CCCTGTCTGAGAATCCAGGGCACGCTCCGGGGAGATGGGACAGCCCCACGGGAAGAGTAC
GGCTCTAGGCAGCTCCAGCTGGCAGTGCCTGGAGCCTACGAGAAGCCACAGCTCTTGCCC
CTGCAGCCTCCCACAGAGCCAGGCCTCCCACCCACCTTTACCTTCCACGTGAACCCAGTG
CTGAGCTCCAGGCTACACGTGGAGCTGATGGAGCTGCTGGCAGCTGTGCAGAGTGGCCCC
AGCGCAGAGTTGGAGGCTCAGACCAGCAAGCTGGGCGAGGGGGGCATCCTGCTCTCCTCT
CTGCCCCTAGGCCAGGAGGAACAGTGTTCTGTGGCCCTGGGGGAGGGCCAGGAGGTGGCT
CTGAGCATGAAGGTGGAAATGAGCTCCGGGGACCTAGACCTACGCCTTGGCTTTGACCTC
TCTGACGGGGAGCAGGAGTTTCTGGACAGGAGGAAGCAGGTCGTGTCCAAGGCCCTGCAG
CAAGTGCTGGGATTGAGTGAGGCTCTGGACAGTGGCCAGGTGCCTGTAGTGGCTGTGTTG
GGTTCCGGGGGTGGAACCCGAGCCATGTCTTCTCTGTACGGCAGCCTGGCAGGGTTGCAG
GAGCTCGGCCTTCTAGACACTGTGACCTACCTGAGTGGGGTCTCTGGGTCTACCTGGTGC
ATCTCCACACTCTACAGGGACCCAGCCTGGTCCCAGGTGGCCTTGCAGGGCCCCATTGAG
CGTGCCCAGGTTCACGTCTGCAGCAGTAAGATGGGAGCTTTGTCCACGGAGCGGCTACAG
TACTACACTCAGGAACTGGGGGTCCGGGAGCGCAGTGGCCACAGCGTGTCCCTCATCGAC
CTCTGGGGCCTCCTTGTTGAGTATCTCCTGTACCAGGAGGAGAACCCTGCCAAGCTGTCT
GACCAACAGGAGGCGGTCCGCCAGGGTCAGAACCCTTACCCCATTTACACCAGTGTCAAC
GTCCGCACCAACTTGAGTGGGGAAGATTTTGCAGAGTGGTGCGAGTTCACGCCCTATGAG
GTTGGCTTCCCCAAGTACGGGGCTTATGTTCCCACCGAGCTCTTCGGCTCAGAACTCTTC
ATGGGACGATTGCTGCAGCTCCAGCCTGAACCCCGGATCTGTTACCTGCAAGGTATGTGG
GGCAGCGCCTTTGCCACCAGCCTGGATGAGATCTTCCTAAAGACCGCCGGCTCGGGCCTC
AGCTTCCTGGAGTGGTACAGAGGCAGTGTGAATATCACAGACGACTGCCAGAAGCCTCAG
CTGCACAACCCCTCGAGGCTGCGAACGAGGCTCCTCACCCCACAGGGGCCCTTCTCCCAG
GCTGTGCTGGACATATTCACCTCCCGCTTCACTTCCGCCCAGAGCTTTAACTTCACCCGG
GGTCTCTGCTTGCACAAGGACTATGTGGCTGGCAGGGAGTTCGTGGCCTGGAAAGACACA
CACCCGGACGCCTTCCCCAACCAGCTCACCCCCATGCGGGACTGCCTGTACCTGGTGGAC
GGAGGCTTTGCCATCAACTCTCCGTTCCCACTGGCTCTGCTGCCTCAGAGAGCAGTGGAC
CTCATTCTGTCCTTTGACTATTCCTTGGAAGCCCCTTTTGAGGTCTTGAAGATGACAGAG
AAGTACTGCCTGGACCGAGGAATCCCCTTCCCTAGCATCGAGGTGGGCCCTGAGGACATG
GAGGAGGCCCGTGAGTGCTATCTGTTTGCCAAGGCTGAGGACCCCCGCTCCCCCATTGTG
CTGCACTTCCCCCTGGTTAACCGTACCTTCCGCACACACCTGGCCCCAGGTGTGGAGCGA
CAAACAGCTGAGGAGAAGGCCTTTGGGGACTTTGTCATCAACAGGCCAGACACCCCCTAT
GGCATGATGAACTTCACCTATGAGCCCCAGGACTTTTATCGGCTGGTGGCCCTCAGTCGA
TACAACGTCCTGAACAACGTGGAGACCTTGAAGTGCGCCCTCCAGCTGGCTCTGGACCGG
CACCAGGCTCGGGAGAGGGCAGGGGCCTGA
|
| Enzyme 73 GenBank Gene ID |
NM_213600.3  |
| Enzyme 73 GeneCard ID |
PLA2G4F  |
| Enzyme 73 GenAtlas ID |
PLA2G4F  |
| Enzyme 73 HGNC ID |
HGNC:27396  |
| Enzyme 73 Chromosome Location |
1 |
| Enzyme 73 Locus |
15q15.1 |
| Enzyme 73 SNPs |
SNPJam Report  |
| Enzyme 73 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
]
- 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
]
- 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 73 Metabolite References |
Not Available |
|
Enzyme 74
[top]
|
| Enzyme 74 ID |
14017 |
| Enzyme 74 Name |
ADP-ribosylation factor GTPase-activating protein 1 |
| Enzyme 74 Synonyms |
- ARF GAP 1
- ADP-ribosylation factor 1 GTPase-activating protein
- ARF1 GAP
- ARF1-directed GTPase-activating protein
|
| Enzyme 74 Gene Name |
ARFGAP1 |
| Enzyme 74 Protein Sequence |
>ADP-ribosylation factor GTPase-activating protein 1
MASPRTRKVLKEVRVQDENNVCFECGAFNPQWVSVTYGIWICLECSGRHRGLGVHLSFVR
SVTMDKWKDIELEKMKAGGNAKFREFLESQEDYDPCWSLQEKYNSRAAALFRDKVVALAE
GREWSLESSPAQNWTPPQPRTLPSMVHRVSGQPQSVTASSDKAFEDWLNDDLGSYQGAQG
NRYVGFGNTPPPQKKEDDFLNNAMSSLYSGWSSFTTGASRFASAAKEGATKFGSQASQKA
SELGHSLNENVLKPAQEKVKEGKIFDDVSSGVSQLASKVQGVGSKGWRDVTTFFSGKAEG
PLDSPSEGHSYQNSGLDHFQNSNIDQSFWETFGSAEPTKTRKSPSSDSWTCADTSTERRS
SDSWEVWGSASTNRNSNSDGGEGGEGTKKAVPPAVPTDDGWDNQNW
|
| Enzyme 74 Number of Residues |
406 |
| Enzyme 74 Molecular Weight |
44667.6 |
| Enzyme 74 Theoretical pI |
5.34 |
| Enzyme 74 GO Classification |
| Function |
- ARF GTPase activator activity
- GTPase regulator activity
- binding
- cation binding
- enzyme regulator activity
- ion binding
- metal ion binding
- nucleoside-triphosphatase regulator activity
- small GTPase regulator activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of ARF GTPase activity
- regulation of GTP catabolic process
- regulation of GTPase activity
- regulation of Ras GTPase activity
- regulation of biological process
- regulation of cellular metabolic process
- regulation of metabolic process
- regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- regulation of nucleotide catabolic process
- regulation of nucleotide metabolic process
- regulation of purine nucleotide catabolic process
|
| Component |
| — |
|
| Enzyme 74 General Function |
Involved in ARF GTPase activator activity |
| Enzyme 74 Specific Function |
GTPase-activating protein (GAP) for the ADP ribosylation factor 1 (ARF1). Involved in membrane trafficking and /or vesicle transport. Promotes hydrolysis of the ARF1-bound GTP and thus, is required for the dissociation of coat proteins from Golgi-derived membranes and vesicles, a prerequisite for vesicle's fusion with target compartment. Probably regulates ARF1-mediated transport via its interaction with the KDELR proteins and RNP24. Overexpression induces the redistribution of the entire Golgi complex to the endoplasmic reticulum, as when ARF1 is deactivated. Its activity is stimulated by phosphoinosides and inhibited by phosphatidylcholine |
| Enzyme 74 Pathways |
Not Available |
| Enzyme 74 Reactions |
Not Available |
| Enzyme 74 Pfam Domain Function |
|
| Enzyme 74 Signals |
|
| Enzyme 74 Transmembrane Regions |
|
| Enzyme 74 Essentiality |
Not Available |
| Enzyme 74 GenBank ID Protein |
8922652  |
| Enzyme 74 UniProtKB/Swiss-Prot ID |
Q8N6T3  |
| Enzyme 74 UniProtKB/Swiss-Prot Entry Name |
ARFG1_HUMAN  |
| Enzyme 74 PDB ID |
Not Available |
| Enzyme 74 Cellular Location |
Not Available |
| Enzyme 74 Gene Sequence |
>1221 bp
ATGGCCAGCCCAAGAACCAGGAAGGTTCTTAAAGAAGTCAGGGTGCAGGATGAGAACAAC
GTTTGTTTTGAGTGTGGCGCGTTCAATCCTCAGTGGGTCAGTGTGACCTACGGCATCTGG
ATCTGCCTGGAGTGCTCGGGGAGACACCGCGGGCTTGGGGTTCACCTCAGCTTTGTGCGC
TCTGTTACTATGGACAAGTGGAAGGACATTGAGCTTGAGAAGATGAAAGCTGGTGGGAAT
GCTAAGTTCCGAGAGTTCCTGGAGTCTCAGGAGGATTACGATCCTTGCTGGTCCTTGCAG
GAGAAGTACAACAGCAGAGCCGCGGCCCTCTTTAGGGATAAGGTGGTCGCTCTGGCCGAA
GGCAGAGAGTGGTCTCTGGAGTCATCACCTGCCCAGAACTGGACCCCACCTCAGCCCAGG
ACGCTGCCGTCCATGGTGCACCGAGTCTCTGGCCAGCCGCAGAGTGTGACCGCCTCCTCG
GACAAGGCTTTTGAAGACTGGCTGAATGATGACCTCGGCTCCTATCAAGGGGCCCAGGGG
AATCGCTACGTGGGGTTTGGGAACACGCCACCGCCTCAGAAGAAAGAAGATGACTTCCTC
AACAACGCCATGTCCTCCCTGTACTCGGGCTGGAGCAGCTTCACCACTGGAGCCAGCCGG
TTTGCCTCGGCAGCCAAGGAGGGCGCTACAAAGTTTGGATCCCAAGCGAGTCAGAAGGCG
TCCGAGCTGGGCCACAGCCTGAACGAGAACGTCCTCAAGCCTGCGCAGGAGAAGGTGAAG
GAGGGAAAGATTTTTGATGATGTCTCCAGTGGGGTCTCTCAGTTGGCGTCCAAGGTCCAG
GGAGTCGGTAGTAAGGGATGGCGGGACGTCACCACCTTTTTTTCGGGGAAAGCAGAGGGC
CCCTTGGACAGCCCCTCGGAGGGCCACAGTTATCAGAACAGCGGTCTGGACCACTTCCAA
AACAGCAACATAGACCAGAGCTTCTGGGAGACCTTTGGAAGTGCTGAGCCCACCAAGACC
CGCAAGTCCCCGAGCAGCGACAGCTGGACGTGCGCGGACACCTCCACCGAGAGGAGGAGC
TCGGACAGCTGGGAGGTGTGGGGCTCGGCCTCCACCAACAGGAACAGCAACAGCGACGGC
GGGGAGGGCGGGGAGGGCACCAAGAAGGCAGTGCCGCCGGCCGTGCCCACTGATGATGGC
TGGGACAACCAGAACTGGTAG
|
| Enzyme 74 GenBank Gene ID |
NM_018209.2  |
| Enzyme 74 GeneCard ID |
ARFGAP1  |
| Enzyme 74 GenAtlas ID |
ARFGAP1  |
| Enzyme 74 HGNC ID |
HGNC:15852  |
| Enzyme 74 Chromosome Location |
2 |
| Enzyme 74 Locus |
20q13.33 |
| Enzyme 74 SNPs |
SNPJam Report  |
| Enzyme 74 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
- 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
]
|
| Enzyme 74 Metabolite References |
Not Available |
|
Enzyme 75
[top]
|
| Enzyme 75 ID |
14866 |
| Enzyme 75 Name |
Cytosolic phospholipase A2 beta |
| Enzyme 75 Synonyms |
- cPLA2-beta
- Phospholipase A2 group IVB
|
| Enzyme 75 Gene Name |
PLA2G4B |
| Enzyme 75 Protein Sequence |
>Cytosolic phospholipase A2 beta
MAVAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVW
NQSFHFRIHRQLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEG
RLEVEFRLQSLADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGP
QEASVGTGTFRFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMR
VELKKEAGLRELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIM
ATGGGIRAMTSLYGQLAGLKELGLLDCVSYITGASGSTWALANLYEDPEWSQKDLAGPTE
LLKTQVTKNKLGVLAPSQLQRYRQELAERARLGYPSCFTNLWALINEALLHDEPHDHKLS
DQREALSHGQNPLPIYCALNTKGQSLTTFEFGEWCEFSPYEVGFPKYGAFIPSELFGSEF
FMGQLMKRLPESRICFLEGIWSNLYAANLQDSLYWASEPSQFWDRWVRNQANLDKEQVPL
LKIEEPPSTAGRIAEFFTDLLTWRPLAQATHNFLRGLHFHKDYFQHPHFSTWKATTLDGL
PNQLTPSEPHLCLLDVGYLINTSCLPLLQPTRDVDLILSLDYNLHGAFQQLQLLGRFCQE
QGIPFPPISPSPEEQLQPRECHTFSDPTCPGAPAVLHFPLVSDSFREYSAPGVRRTPEEA
AAGEVNLSSSDSPYHYTKVTYSQEDVDKLLHLTHYNVCNNQEQLLEALRQAVQRRRQRRP
H
|
| Enzyme 75 Number of Residues |
781 |
| Enzyme 75 Molecular Weight |
87977.0 |
| Enzyme 75 Theoretical pI |
5.85 |
| Enzyme 75 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 75 General Function |
Involved in metabolic process |
| Enzyme 75 Specific Function |
Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine |
| Enzyme 75 Pathways |
Not Available |
| Enzyme 75 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 75 Pfam Domain Function |
|
| Enzyme 75 Signals |
|
| Enzyme 75 Transmembrane Regions |
|
| Enzyme 75 Essentiality |
Not Available |
| Enzyme 75 GenBank ID Protein |
194387976  |
| Enzyme 75 UniProtKB/Swiss-Prot ID |
P0C869  |
| Enzyme 75 UniProtKB/Swiss-Prot Entry Name |
PA24B_HUMAN  |
| Enzyme 75 PDB ID |
Not Available |
| Enzyme 75 Cellular Location |
Not Available |
| Enzyme 75 Gene Sequence |
>2346 bp
ATGGCTGTGGCAGAGGTGTCCAGGACCTGCCTGCTCACGGTTCGTGTCCTGCAGGCCCAT
CGCCTACCCTCTAAGGACCTAGTGACCCCCTCTGACTGCTACGTGACTCTCTGGCTGCCC
ACGGCCTGCAGCCACAGGCTCCAGACACGCACGGTCAAGAACAGCAGTAGCCCTGTCTGG
AACCAGAGCTTTCACTTCAGGATCCACAGGCAGCTCAAGAATGTCATGGAACTGAAAGTC
TTTGACCAGGACCTGGTGACCGGAGATGACCCTGTGTTGTCAGTACTGTTTGATGCGGGG
ACTCTGCGGGCTGGGGAGTTCCGGCGCGAGAGCTTCTCACTGAGCCCTCAGGGTGAGGGG
CGCCTGGAAGTTGAATTTCGCCTGCAGAGTCTGGCTGACCGTGGCGAGTGGCTCGTCAGC
AATGGCGTTCTGGTGGCCCGGGAGCTCTCCTGCTTGCACGTTCAACTGGAGGAGACAGGA
GACCAGAAGTCCTCAGAGCACAGAGTTCAGCTTGTGGTTCCTGGGTCCTGTGAGGGTCCG
CAGGAGGCCTCTGTGGGCACTGGCACCTTCTGCTTCCACTGCCCAGCCTGCTGGGAGCAG
GAGCTGAGTATTCGCCTGCAGGATGCCCCCGAGGAGCAACTAAAGGCGCCACTGAGTGCC
CTGCCCTCTGGTCAAGTGGTGAGGCTTGTCTTCCCCACGTCCCAGGAGCCCCTGATGAGA
GTGGAGCTGAAAAAAGAAGCAGGACTGAGGGAGCTGGCCGTGCGACTGGGCTTCGGGCCC
TGTGCAGAGGAGCAGGCCTTCCTGAGCAGGAGGAAGCAGGTGGTGGCCGCGGCCTTGAGG
CAGGCCCTGCAGCTGGATGGAGACCTGCAGGAGGATGAGATCCCAGTGGTAGCTATTATG
GCCACTGGTGGTGGGATCCGGGCAATGACTTCCCTGTATGGGCAGCTGGCTGGCCTGAAG
GAGCTGGGCCTCTTGGATTGCGTCTCCTACATCACCGGGGCCTCGGGCTCCACCTGGGCC
TTGGCCAACCTTTATGAGGACCCAGAGTGGTCTCAGAAGGACCTGGCAGGGCCCACTGAG
TTGCTGAAGACCCAGGTGACCAAGAACAAGCTGGGTGTGCTGGCCCCCAGCCAGCTGCAG
CGGTACCGGCAGGAGCTGGCCGAGCGTGCCCGCTTGGGCTACCCAAGCTGCTTCACCAAC
CTGTGGGCCCTCATCAACGAGGCGCTGCTGCATGATGAGCCCCATGATCACAAGCTCTCA
GATCAACGGGAGGCCCTGAGTCATGGCCAGAACCCTCTGCCCATCTACTGTGCCCTCAAC
ACCAAAGGGCAGAGCCTGACCACTTTTGAATTTGGGGAGTGGTGCGAGTTCTCTCCCTAC
GAGGTCGGCTTCCCCAAGTACGGGGCCTTCATCCCCTCTGAGCTCTTTGGCTCCGAGTTC
TTTATGGGGCAGCTGATGAAGAGGCTTCCTGAGTCCCGCATCTGCTTCTTAGAAGGTATC
TGGAGCAACCTGTATGCAGCCAACCTCCAGGACAGCTTATACTGGGCCTCAGAGCCCAGC
CAGTTCTGGGACCGCTGGGTCAGGAACCAGGCCAACCTGGACAAGGAGCAGGTCCCCCTT
CTGAAGATAGAAGAACCACCCTCAACAGCCGGCAGGATAGCTGAGTTTTTCACCGATCTT
CTGACGTGGCGTCCACTGGCCCAGGCCACACATAATTTCCTGTGTGGCCTCCATTTCCAC
AAAGACTACTTTCAGCATCCTCACTTCTCCACATGGAAAGCTACCACTCTGGATGGGCTC
CCCAACCAGCTGACACCCTCGGAGCCCCACCTGTGCCTGCTGGATGTTGGCTACCTCATC
AATACCAGCTGCCTGCCCCTCCTGCAGCCCACTCGGGACGTGGACCTCATCCTGTCATTG
GACTACAACCTCCACGGAGCCTTCCAGCAGTTGCAGCTCCTGGGCCGGTTCTGCCAGGAG
CAGGGGATCCCGTTCCCACCCATCTCGCCCAGCCCCGAAGAGCAGCTCCAGCCTCGGGAG
TGCCACACCTTCTCTGACCCCACCTGCCCCGGAGCCCCTGCGGTGCTGCACTTTCCTCTG
GTCAGCGACTCCTTCCGGGAGTACTCGGCCCCTGGGGTCCGGCGGACACCCGAGGAGGCG
GCAGCTGAGGAGGTGAACCTGTCTTCATCGGACTCTCCCTACCACTACACGAAGGTGACC
TACAGCCAGGAGGACGTGGACAAGCTGCTGCACCTGACACATTACAATGTCTGCAACAAC
CAGGAGCAGCTGCTGGAGGCTCTGCGCCAGGCAGTGCAGCGGAGGCGGCAGCGCAGGCCC
CACTGA
|
| Enzyme 75 GenBank Gene ID |
AK299419  |
| Enzyme 75 GeneCard ID |
PLA2G4B  |
| Enzyme 75 GenAtlas ID |
PLA2G4B  |
| Enzyme 75 HGNC ID |
HGNC:9036  |
| Enzyme 75 Chromosome Location |
1 |
| Enzyme 75 Locus |
15q11.2-q21.3 |
| Enzyme 75 SNPs |
SNPJam Report  |
| Enzyme 75 General References |
- Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed
]
- Song C, Chang XJ, Bean KM, Proia MS, Knopf JL, Kriz RW: Molecular characterization of cytosolic phospholipase A2-beta. J Biol Chem. 1999 Jun 11;274(24):17063-7. [PubMed
]
- Ghosh M, Loper R, Gelb MH, Leslie CC: Identification of the expressed form of human cytosolic phospholipase A2beta (cPLA2beta): cPLA2beta3 is a novel variant localized to mitochondria and early endosomes. J Biol Chem. 2006 Jun 16;281(24):16615-24. Epub 2006 Apr 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
]
- 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
]
|
| Enzyme 75 Metabolite References |
Not Available |
|
Enzyme 76
[top]
|
| Enzyme 76 ID |
15207 |
| Enzyme 76 Name |
Phospholipase D1 variant |
| Enzyme 76 Synonyms |
Not Available |
| Enzyme 76 Gene Name |
Not Available |
| Enzyme 76 Protein Sequence |
>Phospholipase D1 variant
ANAQVLAAPSPCSPFAFTLSKVNMSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEG
EEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRV
PSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP
REMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDL
GPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLL
VDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKD
HRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGN
RWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSST
VYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAM
ESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSI
SSIDSTSNTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPR
MPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVP
GSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFN
KIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGEN
SILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANIN
DRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQ
DPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEE
ELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
|
| Enzyme 76 Number of Residues |
1059 |
| Enzyme 76 Molecular Weight |
122007.8 |
| Enzyme 76 Theoretical pI |
9.03 |
| Enzyme 76 GO Classification |
| Function |
- binding
- catalytic activity
- lipid binding
- phosphoinositide binding
- phospholipid binding
- protein binding
|
| Process |
- cell communication
- cellular process
- metabolic process
|
| Component |
| — |
|
| Enzyme 76 General Function |
Involved in protein binding |
| Enzyme 76 Specific Function |
Not Available |
| Enzyme 76 Pathways |
Not Available |
| Enzyme 76 Reactions |
Not Available |
| Enzyme 76 Pfam Domain Function |
|
| Enzyme 76 Signals |
|
| Enzyme 76 Transmembrane Regions |
|
| Enzyme 76 Essentiality |
Not Available |
| Enzyme 76 GenBank ID Protein |
62089400  |
| Enzyme 76 UniProtKB/Swiss-Prot ID |
Q59EA4  |
| Enzyme 76 UniProtKB/Swiss-Prot Entry Name |
Q59EA4_HUMAN  |
| Enzyme 76 PDB ID |
Not Available |
| Enzyme 76 Cellular Location |
Not Available |
| Enzyme 76 Gene Sequence |
>3182 bp
CCGCCAACGCGCAGGTGCTAGCGGCCCCTTCGCCCTGCAGCCCCTTTGCTTTTACTCTGT
CCAAAGTTAACATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAA
TTGCTGCTGACATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGG
GAGAGGAGGTAGACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCC
CTTTCTCTGCTATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCT
CCGGCTGTCCAATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGG
TACCAAGTATTAATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTA
AGAGGAAATTCAAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTA
TCCGCATCCCCATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGC
CTCGAGAGATGCCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCC
TTGGTAGAAGAAAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATA
GAAACTATCATGCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATT
TGGGACCAAAGGGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAG
GCTTGAATTGCTGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAG
TGAAAGATTCCTTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGC
TGGTAGACAAAGAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAA
TCCGAATTGATAATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTC
GGTGGTGGGGAGGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAG
ATCATCGATTTGGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTA
ATGCCAAAGGATATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTT
TTATCACAGACTGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAA
ATCGTTGGAGGTTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCA
TAATGCTCTACAAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGA
CTTTGATGCGTCTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCA
CCGTCTATTTGTGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTG
TGGGAGGGATTGACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACG
TGGGCAGTGTGAAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAA
TGGAGTCTATGGAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCA
TCCAGAAGAGTATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGT
TCTCCAAATTTAGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCA
TCAGCAGCATTGACAGCACCTCCAATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGG
GAGAGCTGCATGGGGAAACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCA
AAGACTGGGTTCAACTTGATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCC
GGATGCCCTGGCATGACATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCAC
GTCACTTCATCCAGCGCTGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTT
CTTATCCTTTTCTGCTTCCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGC
CTGGGTCTGTCCATGCTAACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTA
TAAAGTACCATGAAGAGTCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGC
ACTATATCTATATCGAAAACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCA
ACAAGATAGGCGATGCCATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAAT
ACCGGGTATATGTCGTGATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCG
GAGGAAATGCTCTACAGGCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAA
ATTCCATCCTTGGACAGTTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCAT
TCTGTGGTCTTAGAACACATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATG
TCCACAGCAAGTTGTTAATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAA
ATGACCGCAGCATGCTGGGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAG
AGACTGTTCCTTCAGTAATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGAC
TTCGGCTACAGTGCTTTAGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTC
AGGATCCAGTGAGTGACAAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATG
CTACAATTTATGACAAGGTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTC
AGCTGAGAGACTTTATAAACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGG
AGGAACTGAAGAAGATCCGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAG
AAAGCCTACTGCCTTCTGTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTT
AA
|
| Enzyme 76 GenBank Gene ID |
AB209907  |
| Enzyme 76 GeneCard ID |
Not Available |
| Enzyme 76 GenAtlas ID |
Not Available |
| Enzyme 76 HGNC ID |
HGNC:9067  |
| Enzyme 76 Chromosome Location |
Not Available |
| Enzyme 76 Locus |
Not Available |
| Enzyme 76 SNPs |
Not Available |
| Enzyme 76 General References |
Not Available |
| Enzyme 76 Metabolite References |
Not Available |
|
Enzyme 77
[top]
|
| Enzyme 77 ID |
15268 |
| Enzyme 77 Name |
cDNA FLJ75813, highly similar to Homo sapiens lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase) (LRAT), mRNA (Lecithin retinol acyltransferase) (Phosphatidylcholine-- retinol O-acyltransferase) |
| Enzyme 77 Synonyms |
Not Available |
| Enzyme 77 Gene Name |
LRAT |
| Enzyme 77 Protein Sequence |
>cDNA FLJ75813, highly similar to Homo sapiens lecithin retinol acyltransferase (phosphatidylcholine--retinol O-acyltransferase) (LRAT), mRNA (Lecithin retinol acyltransferase) (Phosphatidylcholine-- retinol O-acyltransferase)
MKNPMLEVVSLLLEKLLLISNFTLFSSGAAGEDKGRNSFYETSSFHRGDVLEVPRTHLTH
YGIYLGDNRVAHMMPDILLALTDDMGRTQKVVSNKRLILGVIVKVASIRVDTVEDFAYGA
NILVNHLDESLQKKALLNEEVARRAEKLLGFTPYSLLWNNCEHFVTYCRYGTPISPQSDK
FCETVKIIIRDQRSVLASAVLGLASIVCTGLVSYTTLPAIFIPFFLWMAG
|
| Enzyme 77 Number of Residues |
230 |
| Enzyme 77 Molecular Weight |
25703 |
| Enzyme 77 Theoretical pI |
7.54 |
| Enzyme 77 GO Classification |
Not Available |
| Enzyme 77 General Function |
Not Available |
| Enzyme 77 Specific Function |
Not Available |
| Enzyme 77 Pathways |
Not Available |
| Enzyme 77 Reactions |
Not Available |
| Enzyme 77 Pfam Domain Function |
Not Available |
| Enzyme 77 Signals |
|
| Enzyme 77 Transmembrane Regions |
|
| Enzyme 77 Essentiality |
Not Available |
| Enzyme 77 GenBank ID Protein |
158258633  |
| Enzyme 77 UniProtKB/Swiss-Prot ID |
A8K983  |
| Enzyme 77 UniProtKB/Swiss-Prot Entry Name |
A8K983_HUMAN  |
| Enzyme 77 PDB ID |
Not Available |
| Enzyme 77 Cellular Location |
Not Available |
| Enzyme 77 Gene Sequence |
>693 bp
ATGAAGAACCCCATGCTGGAGGTGGTGTCTTTACTACTGGAGAAGCTGCTCCTCATCTCC
AACTTCACGCTCTTTAGTTCGGGCGCCGCGGGCGAAGACAAAGGGAGGAACAGTTTTTAT
GAAACCAGCTCTTTCCACCGAGGCGACGTGCTGGAGGTGCCCCGGACCCACCTGACCCAC
TATGGCATCTACCTAGGAGACAACCGTGTTGCCCACATGATGCCCGACATCCTGTTGGCC
CTGACAGACGACATGGGGCGTACGCAGAAGGTGGTCTCCAACAAGCGTCTCATCCTGGGC
GTTATTGTCAAAGTGGCCAGCATCCGCGTGGACACAGTGGAGGACTTCGCCTACGGAGCT
AACATCCTGGTCAATCACCTGGACGAGTCCCTCCAGAAAAAGGCACTGCTCAACGAGGAG
GTGGCGCGGAGGGCTGAAAAGCTGCTGGGCTTTACCCCCTACAGCCTGCTGTGGAACAAC
TGCGAGCACTTCGTGACCTACTGCAGATATGGCACCCCGATCAGTCCCCAGTCCGACAAG
TTTTGTGAGACTGTGAAGATAATTATTCGTGATCAGAGAAGTGTTCTTGCTTCAGCAGTC
TTGGGATTGGCGTCTATAGTCTGTACGGGCTTGGTATCATACACTACCCTTCCTGCAATT
TTTATTCCATTCTTCCTATGGATGGCTGGCTAA
|
| Enzyme 77 GenBank Gene ID |
AK292598  |
| Enzyme 77 GeneCard ID |
A8K983  |
| Enzyme 77 GenAtlas ID |
Not Available |
| Enzyme 77 HGNC ID |
Not Available |
| Enzyme 77 Chromosome Location |
Not Available |
| Enzyme 77 Locus |
Not Available |
| Enzyme 77 SNPs |
SNPJam Report  |
| Enzyme 77 General References |
Not Available |
| Enzyme 77 Metabolite References |
Not Available |
|
Enzyme 78
[top]
|
| Enzyme 78 ID |
15299 |
| Enzyme 78 Name |
cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a) |
| Enzyme 78 Synonyms |
Not Available |
| Enzyme 78 Gene Name |
PLA2G2A |
| Enzyme 78 Protein Sequence |
>cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
|
| Enzyme 78 Number of Residues |
144 |
| Enzyme 78 Molecular Weight |
16083 |
| Enzyme 78 Theoretical pI |
9.51 |
| Enzyme 78 GO Classification |
Not Available |
| Enzyme 78 General Function |
Not Available |
| Enzyme 78 Specific Function |
Not Available |
| Enzyme 78 Pathways |
Not Available |
| Enzyme 78 Reactions |
Not Available |
| Enzyme 78 Pfam Domain Function |
Not Available |
| Enzyme 78 Signals |
|
| Enzyme 78 Transmembrane Regions |
|
| Enzyme 78 Essentiality |
Not Available |
| Enzyme 78 GenBank ID Protein |
158256040  |
| Enzyme 78 UniProtKB/Swiss-Prot ID |
A8K5I7  |
| Enzyme 78 UniProtKB/Swiss-Prot Entry Name |
A8K5I7_HUMAN  |
| Enzyme 78 PDB ID |
1DB4  |
| Enzyme 78 PDB File |
Show |
| Enzyme 78 3D Structure |
|
| Enzyme 78 Cellular Location |
Not Available |
| Enzyme 78 Gene Sequence |
>435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
|
| Enzyme 78 GenBank Gene ID |
AK291302  |
| Enzyme 78 GeneCard ID |
A8K5I7  |
| Enzyme 78 GenAtlas ID |
Not Available |
| Enzyme 78 HGNC ID |
Not Available |
| Enzyme 78 Chromosome Location |
Not Available |
| Enzyme 78 Locus |
Not Available |
| Enzyme 78 SNPs |
SNPJam Report  |
| Enzyme 78 General References |
Not Available |
| Enzyme 78 Metabolite References |
Not Available |
|
Enzyme 79
[top]
|
| Enzyme 79 ID |
16479 |
| Enzyme 79 Name |
cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-) |
| Enzyme 79 Synonyms |
- SubName: Lysophospholipase 3 (Lysosomal phospholipase A2), isoform CRA_a
|
| Enzyme 79 Gene Name |
LYPLA3 |
| Enzyme 79 Protein Sequence |
>cDNA FLJ10843 fis, clone NT2RP4001345, highly similar to 1-O-acylceramide synthase (EC 2.3.1.-)
MGLHLRPYRVGLLPDGLLFLLLLLMLLADPALPAGRHPPVVLVPGDLGNQLEAKLDKPTV
VHYLCSKKTESYFTIWLNLELLLPVIIDCWIDNIRLVYNKTSRATQFPDGVDVRVPGFGK
TFSLEFLDPSKSSVGSYFHTMVESLVGWGYTRGEDVRGAPYDWRRAPNENGPYFLALREM
IEEMYQLYGGPVVLVAHSMGNMYTLYFLQRQPQAWKDKYIRAFVSLGAPWGGVAKTLRVL
ASGDNNRIPVIGPLKIREQQRSAVSTSWLLPYNYTWSPEKVFVQTPTINYTLRDYRKFFQ
DIGFEDGWLMRQDTEGLVEATMPPGVQLHCLYGTGVPTPDSFYYESFPDRDPKICFGDGD
GTVNLKSALQCQAWQSRQEHQVLLQELPGSEHIEMLANATTLAYLKRVLLGP
|
| Enzyme 79 Number of Residues |
412 |
| Enzyme 79 Molecular Weight |
46658 |
| Enzyme 79 Theoretical pI |
6.72 |
| Enzyme 79 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 groups other than amino-acyl groups
|
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 79 General Function |
Not Available |
| Enzyme 79 Specific Function |
Not Available |
| Enzyme 79 Pathways |
Not Available |
| Enzyme 79 Reactions |
Not Available |
| Enzyme 79 Pfam Domain Function |
|
| Enzyme 79 Signals |
|
| Enzyme 79 Transmembrane Regions |
|
| Enzyme 79 Essentiality |
Not Available |
| Enzyme 79 GenBank ID Protein |
Not Available |
| Enzyme 79 UniProtKB/Swiss-Prot ID |
B3KMF3  |
| Enzyme 79 UniProtKB/Swiss-Prot Entry Name |
B3KMF3_HUMAN  |
| Enzyme 79 PDB ID |
Not Available |
| Enzyme 79 Cellular Location |
Not Available |
| Enzyme 79 Gene Sequence |
Not Available |
| Enzyme 79 GenBank Gene ID |
AK001705  |
| Enzyme 79 GeneCard ID |
B3KMF3  |
| Enzyme 79 GenAtlas ID |
Not Available |
| Enzyme 79 HGNC ID |
Not Available |
| Enzyme 79 Chromosome Location |
16 |
| Enzyme 79 Locus |
16q22.1 |
| Enzyme 79 SNPs |
SNPJam Report  |
| Enzyme 79 General References |
Not Available |
| Enzyme 79 Metabolite References |
Not Available |
|
Enzyme 80
[top]
|
| Enzyme 80 ID |
16483 |
| Enzyme 80 Name |
cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c) |
| Enzyme 80 Synonyms |
Not Available |
| Enzyme 80 Gene Name |
CHPT1 |
| Enzyme 80 Protein Sequence |
>cDNA FLJ90730 fis, clone PLACE1010011, highly similar to Homo sapiens choline phosphotransferase 1 (CHPT1), mRNA (Choline phosphotransferase 1, isoform CRA_c)
MAAGAGAGSAPRWLRALSEPLSAAQLRRLEEHRYSAAGVSLLEPPLQLYWTWLLQWIPLW
MAPNSITLLGLAVNVVTTLVLISYCPTATEEAPYWTYLLCALGLFIYQSLDAIDGKQARR
TNSCSPLGELFDHGCDSLSTVFMAVGASIAARLGTYPDWFFFCSFIGMFVFYCAHWQTYV
SGMLRFGKVDVTEIQIALVIVFVLSAFGGATMWDYTIPILEIKLKILPVLGFLGGVIFSC
SNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATDVFEKHPCLYILM
FGCVFAKVSQKLVVAHMTKSELYLQDTVFLGPGLLFLDQYFNNFIDEYVVLWMAMVISSF
DMVIYFSALCLQISRHLHLNIFKTACHQAPEQVQVLSSKSHQNNMD
|
| Enzyme 80 Number of Residues |
406 |
| Enzyme 80 Molecular Weight |
45097 |
| Enzyme 80 Theoretical pI |
6.92 |
| Enzyme 80 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- phospholipid biosynthesis
- phospholipid metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 80 General Function |
Lipid transport and metabolism |
| Enzyme 80 Specific Function |
Not Available |
| Enzyme 80 Pathways |
Not Available |
| Enzyme 80 Reactions |
Not Available |
| Enzyme 80 Pfam Domain Function |
|
| Enzyme 80 Signals |
|
| Enzyme 80 Transmembrane Regions |
|
| Enzyme 80 Essentiality |
Not Available |
| Enzyme 80 GenBank ID Protein |
Not Available |
| Enzyme 80 UniProtKB/Swiss-Prot ID |
B3KQM2  |
| Enzyme 80 UniProtKB/Swiss-Prot Entry Name |
B3KQM2_HUMAN  |
| Enzyme 80 PDB ID |
Not Available |
| Enzyme 80 Cellular Location |
Not Available |
| Enzyme 80 Gene Sequence |
Not Available |
| Enzyme 80 GenBank Gene ID |
AK075211  |
| Enzyme 80 GeneCard ID |
B3KQM2  |
| Enzyme 80 GenAtlas ID |
Not Available |
| Enzyme 80 HGNC ID |
Not Available |
| Enzyme 80 Chromosome Location |
12 |
| Enzyme 80 Locus |
12q |
| Enzyme 80 SNPs |
SNPJam Report  |
| Enzyme 80 General References |
Not Available |
| Enzyme 80 Metabolite References |
Not Available |
|
Enzyme 81
[top]
|
| Enzyme 81 ID |
16561 |
| Enzyme 81 Name |
Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a) |
| Enzyme 81 Synonyms |
Not Available |
| Enzyme 81 Gene Name |
PLA2G6 |
| Enzyme 81 Protein Sequence |
>Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRQLQDLMHISRARKPAFILGSMRDEK
RTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSM
AYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPA
ELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGG
LLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNP
WELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVS
DTVLVNALWETEVYIYEHREEFQKLIQLLLSP
|
| Enzyme 81 Number of Residues |
752 |
| Enzyme 81 Molecular Weight |
84094 |
| Enzyme 81 Theoretical pI |
7.24 |
| Enzyme 81 GO Classification |
| Function |
| — |
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 81 General Function |
Not Available |
| Enzyme 81 Specific Function |
Not Available |
| Enzyme 81 Pathways |
Not Available |
| Enzyme 81 Reactions |
Not Available |
| 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 |
B0QYE8  |
| Enzyme 81 UniProtKB/Swiss-Prot Entry Name |
B0QYE8_HUMAN  |
| Enzyme 81 PDB ID |
Not Available |
| Enzyme 81 Cellular Location |
Not Available |
| Enzyme 81 Gene Sequence |
Not Available |
| Enzyme 81 GenBank Gene ID |
AL022322  |
| Enzyme 81 GeneCard ID |
B0QYE8  |
| Enzyme 81 GenAtlas ID |
Not Available |
| Enzyme 81 HGNC ID |
Not Available |
| Enzyme 81 Chromosome Location |
22 |
| Enzyme 81 Locus |
22q13.1 |
| Enzyme 81 SNPs |
SNPJam Report  |
| Enzyme 81 General References |
Not Available |
| Enzyme 81 Metabolite References |
Not Available |
|
Enzyme 82
[top]
|
| Enzyme 82 ID |
16875 |
| Enzyme 82 Name |
Phospholipase D6 |
| Enzyme 82 Synonyms |
- PLD 6
- Choline phosphatase 6
- Phosphatidylcholine-hydrolyzing phospholipase D6
|
| Enzyme 82 Gene Name |
PLD6 |
| Enzyme 82 Protein Sequence |
>Phospholipase D6
MGRLSWQVAAAAAVGLALTLEALPWVLRWLRSRRRRPRREALFFPSQVTCTEALLRAPGA
ELAELPEGCPCGLPHGESALSRLLRALLAARASLDLCLFAFSSPQLGRAVQLLHQRGVRV
RVVTDCDYMALNGSQIGLLRKAGIQVRHDQDPGYMHHKFAIVDKRVLITGSLNWTTQAIQ
NNRENVLITEDDEYVRLFLEEFERIWEQFNPTKYTFFPPKKSHGSCAPPVSRAGGRLLSW
HRTCGTSSESQT
|
| Enzyme 82 Number of Residues |
252 |
| Enzyme 82 Molecular Weight |
28272.3 |
| Enzyme 82 Theoretical pI |
9.67 |
| Enzyme 82 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 82 General Function |
Involved in catalytic activity |
| Enzyme 82 Specific Function |
A phosphatidylcholine + H(2)O = choline + a phosphatidate |
| Enzyme 82 Pathways |
Not Available |
| Enzyme 82 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| Enzyme 82 Pfam Domain Function |
Not Available |
| Enzyme 82 Signals |
|
| Enzyme 82 Transmembrane Regions |
|
| Enzyme 82 Essentiality |
Not Available |
| Enzyme 82 GenBank ID Protein |
21749147  |
| Enzyme 82 UniProtKB/Swiss-Prot ID |
Q8N2A8  |
| Enzyme 82 UniProtKB/Swiss-Prot Entry Name |
PLD6_HUMAN  |
| Enzyme 82 PDB ID |
Not Available |
| Enzyme 82 Cellular Location |
Not Available |
| Enzyme 82 Gene Sequence |
>759 bp
ATGGGACGGTTGAGTTGGCAGGTGGCGGCCGCGGCGGCTGTGGGCCTGGCTCTGACTCTG
GAGGCGCTGCCTTGGGTGCTGCGCTGGCTGCGGTCCAGGCGGCGGCGGCCGCGGCGCGAG
GCGCTGTTCTTCCCGTCTCAGGTGACCTGTACCGAGGCCCTGCTGCGGGCTCCGGGCGCG
GAGCTGGCCGAGCTCCCCGAGGGCTGCCCGTGCGGCCTGCCCCACGGCGAGAGCGCGCTA
AGCCGCCTGCTGCGTGCCCTGCTGGCCGCCCGCGCCAGCCTGGATCTCTGCCTGTTCGCC
TTCTCCAGCCCGCAGCTGGGCCGCGCCGTGCAGTTGCTGCACCAGCGTGGGGTGCGAGTG
CGGGTCGTCACCGACTGCGACTACATGGCCCTCAACGGCTCGCAAATCGGTCTGCTGCGC
AAGGCAGGGATCCAGGTCCGGCACGATCAAGACCCAGGCTACATGCATCACAAGTTTGCC
ATCGTGGACAAGAGGGTGCTCATCACTGGCTCGCTCAACTGGACCACGCAAGCCATCCAG
AACAACAGGGAGAATGTTCTCATCACGGAGGACGACGAGTACGTGCGGCTTTTTCTGGAA
GAATTTGAGCGCATCTGGGAACAGTTTAACCCTACAAAGTATACCTTTTTCCCACCAAAG
AAAAGTCACGGAAGCTGTGCCCCACCTGTCTCCAGAGCTGGAGGGAGATTGCTTTCATGG
CACAGAACTTGCGGCACCTCCAGCGAAAGCCAAACCTAA
|
| Enzyme 82 GenBank Gene ID |
AK090899  |
| Enzyme 82 GeneCard ID |
PLD6  |
| Enzyme 82 GenAtlas ID |
PLD6  |
| Enzyme 82 HGNC ID |
HGNC:30447  |
| Enzyme 82 Chromosome Location |
1 |
| Enzyme 82 Locus |
17p11.2 |
| Enzyme 82 SNPs |
SNPJam Report  |
| Enzyme 82 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
]
- 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 |
16935 |
| Enzyme 83 Name |
Neuropathy target esterase |
| Enzyme 83 Synonyms |
- Patatin-like phospholipase domain-containing protein 6
|
| Enzyme 83 Gene Name |
PNPLA6 |
| Enzyme 83 Protein Sequence |
>Neuropathy target esterase
MGTSSHGLATNSSGAKVAERDGFQDVLAPGEGSAGRICGAQPVPFVPQVLGVMIGAGVAV
VVTAVLILLVVRRLRVPKTPAPDGPRYRFRKRDKVLFYGRKIMRKVSQSTSSLVDTSVSA
TSRPRMRKKLKMLNIAKKILRIQKETPTLQRKEPPPAVLEADLTEGDLANSHLPSEVLYM
LKNVRVLGHFEKPLFLELCRHMVFQRLGQGDYVFRPGQPDASIYVVQDGLLELCLPGPDG
KECVVKEVVPGDSVNSLLSILDVITGHQHPQRTVSARAARDSTVLRLPVEAFSAVFTKYP
ESLVRVVQIIMVRLQRVTFLALHNYLGLTNELFSHEIQPLRLFPSPGLPTRTSPVRGSKR
MVSTSATDEPRETPGRPPDPTGAPLPGPTGDPVKPTSLETPSAPLLSRCVSMPGDISGLQ
GGPRSDFDMAYERGRISVSLQEEASGGSLAAPARTPTQEPREQPAGACEYSYCEDESATG
GCPFGPYQGRQTSSIFEAAKQELAKLMRIEDPSLLNSRVLLHHAKAGTIIARQGDQDVSL
HFVLWGCLHVYQRMIDKAEDVCLFVAQPGELVGQLAVLTGEPLIFTLRAQRDCTFLRISK
SDFYEIMRAQPSVVLSAAHTVAARMSPFVRQMDFAIDWTAVEAGRALYRQGDRSDCTYIV
LNGRLRSVIQRGSGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELAKLPEGTLG
HIKRRYPQVVTRLIHLLSQKILGNLQQLQGPFPAGSGLGVPPHSELTNPASNLATVAILP
VCAEVPMVAFTLELQHALQAIGPTLLLNSDIIRARLGASALDSIQEFRLSGWLAQQEDAH
RIVLYQTDASLTPWTVRCLRQADCILIVGLGDQEPTLGQLEQMLENTAVRALKQLVLLHR
EEGAGPTRTVEWLNMRSWCSGHLHLRCPRRLFSRRSPAKLHELYEKVFSRRADRHSDFSR
LARVLTGNTIALVLGGGGARGCSHIGVLKALEEAGVPVDLVGGTSIGSFIGALYAEERSA
SRTKQRAREWAKSMTSVLEPVLDLTYPVTSMFTGSAFNRSIHRVFQDKQIEDLWLPYFNV
TTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGHLLMDGGYINNLPADIARSM
GAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWADKVKVPDMAEIQSRLAYVSCV
RQLEVVKSSSYCEYLRPPIDCFKTMDFGKFDQIYDVGYQYGKAVFGGWSRGNVIEKMLTD
RRSTDLNESRRADVLAFPSSGFTDLAEIVSRIEPPTSYVSDGCADGEESDCLTEYEEDAG
PDCSRDEGGSPEGASPSTASEMEEEKSILRQRRCLPQEPPGSATDA
|
| Enzyme 83 Number of Residues |
1366 |
| Enzyme 83 Molecular Weight |
149993.3 |
| Enzyme 83 Theoretical pI |
7.85 |
| Enzyme 83 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lysophospholipase activity
|
| Process |
- glycerophospholipid metabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylcholine metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- membrane
- organelle membrane
|
|
| Enzyme 83 General Function |
Involved in metabolic process |
| Enzyme 83 Specific Function |
Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy |
| Enzyme 83 Pathways |
Not Available |
| Enzyme 83 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 83 Pfam Domain Function |
|
| Enzyme 83 Signals |
|
| Enzyme 83 Transmembrane Regions |
|
| Enzyme 83 Essentiality |
Not Available |
| Enzyme 83 GenBank ID Protein |
116256487  |
| Enzyme 83 UniProtKB/Swiss-Prot ID |
Q8IY17  |
| Enzyme 83 UniProtKB/Swiss-Prot Entry Name |
PLPL6_HUMAN  |
| Enzyme 83 PDB ID |
Not Available |
| Enzyme 83 Cellular Location |
Not Available |
| Enzyme 83 Gene Sequence |
>3984 bp
ATGGAGGCTCCGCTGCAAACTGGAATGGTGCTTGGCGTGATGATCGGGGCCGGAGTGGCG
GTGGTGGTCACGGCCGTGCTCATCCTCCTGGTGGTGCGGAGGCTGCGAGTGCCAAAAACC
CCAGCCCCGGATGGCCCCCGGTATCGGTTCCGGAAGAGGGACAAAGTGCTCTTCTATGGC
CGGAAGATTATGCGGAAGGTGTCACAATCCACCTCCTCCCTCGTGGATACCTCTGTCTCC
GCCACCTCCCGGCCACGCATGAGGAAGAAACTGAAGATGCTCAACATTGCCAAGAAGATC
CTGCGCATCCAGAAAGAGACGCCCACGCTGCAGCGGAAGGAGCCCCCGCCCGCAGTGCTA
GAAGCTGACCTGACCGAGGGCGACCTGGCTAACTCCCATCTGCCCTCTGAAGTGCTTTAT
ATGCTCAAGAACGTCCGGGTGCTGGGCCACTTCGAGAAGCCACTCTTCCTGGAGCTCTGC
CGCCACATGGTCTTCCAGCGGCTGGGCCAGGGTGACTACGTCTTCCGGCCGGGCCAGCCA
GATGCCAGCATCTACGTGGTGCAGGACGGGCTGCTGGAGCTCTGTCTGCCAGGGCCTGAC
GGGAAGGAGTGTGTGGTGAAGGAAGTGGTTCCTGGGGACAGCGTCAACAGCCTTCTCAGC
ATCCTGGATGTCATCACCGGTCACCAGCATCCCCAGCGGACCGTGTCTGCCCGGGCGGCC
CGGGACTCCACGGTGCTGCGCCTGCCGGTGGAAGCATTCTCCGCGGTCTTCACCAAGTAC
CCGGAGAGCTTGGTGCGGGTCGTGCAGATCATCATGGTGCGGCTGCAGCGAGTCACCTTC
CTGGCACTGCACAACTACCTGGGTCTGACCAATGAGCTCTTCAGCCACGAGATCCAGCCC
CTGCGTCTGTTCCCCAGCCCCGGCCTCCCAACTCGCACCAGCCCTGTGCGGGGCTCCAAG
AGAATGGTCAGCACCTCAGCTACAGACGAGCCCAGGGAGACCCCAGGGCGGCCACCCGAT
CCCACCGGGGCCCCGCTGCCTGGACCTACAGGGGACCCTGTGAAGCCCACATCCCTGGAA
ACCCCCTCGGCCCCTCTGCTGAGCCGCTGCGTCTCCATGCCAGGGGACATCTCAGGCTTG
CAGGGTGGCCCCCGCTCCGACTTCGACATGGCCTATGAGCGTGGCCGGATCTCCGTGTCC
CTGCAGGAAGAGGCCTCCGGGGGGTCCCTGGCAGCCCCCGCTCGGACCCCCACTCAGGAG
CCTCGTGAGCAGCCGGCAGGCGCCTGTGAATACAGCTACTGTGAGGATGAGTCGGCCACT
GGTGGCTGCCCTTTCGGGCCCTACCAGGGCCGCCAGACCAGCAGCATCTTCGAGGCAGCA
AAGCAGGAGCTGGCCAAGCTGATGCGGATTGAGGACCCCTCCCTCCTGAACAGCAGAGTC
TTGCTGCACCACGCCAAAGCTGGCACCATCATTGCCCGCCAGGGAGACCAGGACGTGAGC
CTGCACTTCGTGCTCTGGGGCTGCCTGCACGTGTACCAGCGCATGATCGACAAGGCGGAG
GACGTGTGCCTGTTCGTAGCGCAGCCCGGGGAACTGGTGGGGCAGCTGGCGGTGCTCACT
GGCGAACCTCTCATCTTCACACTGCGAGCCCAACGCGACTGCACCTTCCTGCGGATCTCC
AAGTCCGACTTCTATGAGATCATGCGCGCACAGCCCAGTGTGGTGCTGAGTGCGGCGCAC
ACGGTGGCAGCCAGGATGTCGCCCTTCGTGCGCCAGATGGACTTCGCCATCGACTGGACT
GCAGTGGAGGCGGGACGCGCGCTGTACAGGCAGGGCGACCGCTCCGACTGCACTTACATC
GTGCTCAATGGGCGGCTGCGTAGCGTGATCCAGCGAGGCAGTGGCAAGAAGGAGCTGGTG
GGCGAGTACGGCCGCGGCGACCTCATCGGCGTGGTGGAGGCACTGACCCGGCAGCCGCGA
GCCACGACGGTGCACGCGGTGCGCGACACGGAGCTGGCCAAGCTTCCCGAGGGCACCTTG
GGTCACATCAAACGCCGGTACCCGCAGGTCGTGACCCGCCTTATCCACCTACTGAGCCAG
AAAATTCTAGGGAATTTGCAGCAGCTGCAAGGACCCTTCCCAGCAGGCTCTGGGTTGGGT
GTGCCCCCACACTCGGAACTCACCAACCCAGCCAGCAACCTGGCAACTGTGGCAATCCTG
CCTGTGTGTGCTGAGGTCCCCATGGTGGCCTTCACGCTGGAGCTGCAGCACGCCCTGCAG
GCCATCGGTCCGACGCTACTCCTTAACAGTGACATCATCCGGGCACGCCTGGGGGCCTCC
GCACTGGATAGCATCCAAGAGTTCCGGCTGTCAGGGTGGCTGGCCCAGCAGGAGGATGCA
CACCGTATCGTACTCTACCAGACGGACGCCTCGCTGACGCCCTGGACCGTGCGCTGCCTG
CGACAGGCCGACTGCATCCTCATTGTGGGCCTGGGGGACCAGGAGCCTACCCTCGGCCAG
CTGGAGCAGATGCTGGAGAACACGGCTGTGCGCGCCCTTAAGCAGCTAGTCCTGCTCCAC
CGAGAGGAGGGCGCGGGCCCCACGCGCACCGTGGAGTGGCTAAATATGCGCAGCTGGTGC
TCGGGGCACCTGCACCTGCGCTGTCCGCGCCGCCTCTTTTCGCGCCGCAGCCCTGCCAAG
CTGCATGAGCTCTACGAGAAGGTTTTCTCCAGGCGCGCGGACCGGCACAGCGACTTCTCC
CGCTTGGCGAGGGTGCTCACGGGGAACACCATTGCCCTTGTGCTAGGCGGGGGCGGGGCC
AGGGGCTGCTCGCACATCGGAGTACTAAAGGCATTAGAGGAGGCGGGGGTCCCCGTGGAC
CTGGTGGGCGGCACGTCCATTGGCTCTTTCATCGGAGCGTTGTACGCGGAGGAGCGCAGC
GCCAGCCGCACGAAGCAGCGGGCCCGGGAGTGGGCCAAGAGCATGACTTCGGTGCTGGAA
CCTGTGTTGGACCTCACGTACCCAGTCACCTCCATGTTCACTGGGTCTGCCTTTAACCGC
AGCATCCATCGGGTCTTCCAGGATAAGCAGATTGAGGACCTGTGGCTGCCTTACTTCAAC
GTGACCACAGATATCACCGCCTCAGCCATGCGAGTCCACAAAGATGGCTCCCTGTGGCGG
TACGTGCGCGCCAGCATGACGCTGTCGGGCTACCTGCCCCCGCTGTGCGACCCCAAGGAC
GGGCACCTACTCATGGATGGCGGCTACATCAACAATCTGCCAGCGGACATCGCCCGCAGC
ATGGGTGCCAAAACGGTCATCGCCATTGACGTGGGGAGCCAGGATGAGACGGACCTCAGC
ACCTACGGGGACAGCCTGTCCGGCTGGTGGCTGCTGTGGAAGCGGCTGAATCCCTGGGCT
GACAAGGTAAAGGTTCCAGACATGGCTGAAATCCAGTCCCGCCTGGCCTACGTGTCCTGT
GTGCGGCAGCTAGAGGTTGTCAAGTCCAGCTCCTACTGCGAGTACCTGCGCCCGCCCATC
GACTGCTTCAAGACCATGGACTTTGGGAAGTTCGACCAGATCTATGATGTGGGCTACCAG
TACGGGAAGGCGGTGTTTGGAGGCTGGAGCCGTGGCAACGTCATTGAGAAAATGCTCACA
GACCGGCGGTCTACAGACCTTAATGAGAGCCGCCGTGCAGACGTGCTTGCCTTCCCAAGC
TCTGGCTTCACTGACTTGGCAGAGATTGTGTCCCGGATTGAGCCCCCCACGAGCTATGTC
TCTGATGGCTGTGCTGACGGAGAGGAGTCAGATTGTCTGACAGAGTATGAGGAGGACGCC
GGACCCGACTGCTCGAGGGATGAAGGGGGGTCCCCCGAGGGCGCAAGCCCCAGCACTGCC
TCCGAGATGGAGGAGGAGAAGTCGATTCTCCGGCAACGACGCTGTCTGCCCCAGGAGCCG
CCCGGCTCAGCCACAGATGCCTGA
|
| Enzyme 83 GenBank Gene ID |
Not Available |
| Enzyme 83 GeneCard ID |
PNPLA6  |
| Enzyme 83 GenAtlas ID |
PNPLA6  |
| Enzyme 83 HGNC ID |
HGNC:16268  |
| Enzyme 83 Chromosome Location |
1 |
| Enzyme 83 Locus |
19p13.2 |
| Enzyme 83 SNPs |
SNPJam Report  |
| Enzyme 83 General References |
- Lush MJ, Li Y, Read DJ, Willis AC, Glynn P: Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man. Biochem J. 1998 May 15;332 ( Pt 1):1-4. [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
]
- 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
]
- Lotti M: The pathogenesis of organophosphate polyneuropathy. Crit Rev Toxicol. 1991;21(6):465-87. [PubMed
]
- Zaccheo O, Dinsdale D, Meacock PA, Glynn P: Neuropathy target esterase and its yeast homologue degrade phosphatidylcholine to glycerophosphocholine in living cells. J Biol Chem. 2004 Jun 4;279(23):24024-33. Epub 2004 Mar 25. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [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
]
- Rainier S, Bui M, Mark E, Thomas D, Tokarz D, Ming L, Delaney C, Richardson RJ, Albers JW, Matsunami N, Stevens J, Coon H, Leppert M, Fink JK: Neuropathy target esterase gene mutations cause motor neuron disease. Am J Hum Genet. 2008 Mar;82(3):780-5. Epub 2008 Feb 28. [PubMed
]
|
| Enzyme 83 Metabolite References |
Not Available |
|
Enzyme 84
[top]
|
| Enzyme 84 ID |
17304 |
| Enzyme 84 Name |
Apolipoprotein A-V |
| Enzyme 84 Synonyms |
- Apo-AV
- ApoA-V
- Apolipoprotein A5
- Regeneration-associated protein 3
|
| Enzyme 84 Gene Name |
APOA5 |
| Enzyme 84 Protein Sequence |
>Apolipoprotein A-V
MASMAAVLTWALALLSAFSATQARKGFWDYFSQTSGDKGRVEQIHQQKMAREPATLKDSL
EQDLNNMNKFLEKLRPLSGSEAPRLPQDPVGMRRQLQEELEEVKARLQPYMAEAHELVGW
NLEGLRQQLKPYTMDLMEQVALRVQELQEQLRVVGEDTKAQLLGGVDEAWALLQGLQSRV
VHHTGRFKELFHPYAESLVSGIGRHVQELHRSVAPHAPASPARLSRCVQVLSRKLTLKAK
ALHARIQQNLDQLREELSRAFAGTGTEEGAGPDPQMLSEEVRQRLQAFRQDTYLQIAAFT
RAIDQETEEVQQQLAPPPPGHSAFAPEFQQTDSGKVLSKLQARLDDLWEDITHSLHDQGH
SHLGDP
|
| Enzyme 84 Number of Residues |
366 |
| Enzyme 84 Molecular Weight |
41212.3 |
| Enzyme 84 Theoretical pI |
6.40 |
| Enzyme 84 GO Classification |
| Function |
|
| Process |
- cellular macromolecule metabolic process
- establishment of localization
- lipid transport
- lipoprotein metabolic process
- macromolecule metabolic process
- metabolic process
- transport
|
| Component |
|
|
| Enzyme 84 General Function |
Involved in lipid binding |
| Enzyme 84 Specific Function |
Minor apolipoprotein mainly associated with HDL and to a lesser extent with VLDL. May also be associated with chylomicrons. Important determinant of plasma triglyceride (TG) levels by both being a potent stimulator of apo-CII lipoprotein lipase (LPL) TG hydrolysis and a inhibitor of the hepatic VLDL-TG production rate (without affecting the VLDL-apoB production rate). Activates poorly lecithin:cholesterol acyltransferase (LCAT) and does not enhance efflux of cholesterol from macrophages |
| Enzyme 84 Pathways |
Not Available |
| Enzyme 84 Reactions |
Not Available |
| Enzyme 84 Pfam Domain Function |
|
| Enzyme 84 Signals |
|
| Enzyme 84 Transmembrane Regions |
|
| Enzyme 84 Essentiality |
Not Available |
| Enzyme 84 GenBank ID Protein |
262231737  |
| Enzyme 84 UniProtKB/Swiss-Prot ID |
Q6Q788  |
| Enzyme 84 UniProtKB/Swiss-Prot Entry Name |
APOA5_HUMAN  |
| Enzyme 84 PDB ID |
Not Available |
| Enzyme 84 Cellular Location |
Not Available |
| Enzyme 84 Gene Sequence |
>1101 bp
ATGGCAAGCATGGCTGCCGTGCTCACCTGGGCTCTGGCTCTTCTTTCAGCGTTTTCGGCC
ACCCAGGCACGGAAAGGCTTCTGGGACTACTTCAGCCAGACCAGCGGGGACAAAGGCAGG
GTGGAGCAGATCCATCAGCAGAAGATGGCTCGCGAGCCCGCGACCCTGAAAGACAGCCTT
GAGCAAGACCTCAACAATATGAACAAGTTCCTGGAAAAGCTGAGGCCTCTGAGTGGGAGC
GAGGCTCCTCGGCTCCCACAGGACCCGGTGGGCATGCGGCGGCAGCTGCAGGAGGAGTTG
GAGGAGGTGAAGGCTCGCCTCCAGCCCTACATGGCAGAGGCGCACGAGCTGGTGGGCTGG
AATTTGGAGGGCTTGCGGCAGCAACTGAAGCCCTACACGATGGATCTGATGGAGCAGGTG
GCCCTGCGCGTGCAGGAGCTGCAGGAGCAGTTGCGCGTGGTGGGGGAAGACACCAAGGCC
CAGTTGCTGGGGGGCGTGGACGAGGCTTGGGCTTTGCTGCAGGGACTGCAGAGCCGCGTG
GTGCACCACACCGGCCGCTTCAAAGAGCTCTTCCACCCATACGCCGAGAGCCTGGTGAGC
GGCATCGGGCGCCACGTGCAGGAGCTGCACCGCAGTGTGGCTCCGCACGCCCCCGCCAGC
CCCGCGCGCCTCAGTCGCTGCGTGCAGGTGCTCTCCCGGAAGCTCACGCTCAAGGCCAAG
GCCCTGCACGCACGCATCCAGCAGAACCTGGACCAGCTGCGCGAAGAGCTCAGCAGAGCC
TTTGCAGGCACTGGGACTGAGGAAGGGGCCGGCCCGGACCCCCAGATGCTCTCCGAGGAG
GTGCGCCAGCGACTTCAGGCTTTCCGCCAGGACACCTACCTGCAGATAGCTGCCTTCACT
CGCGCCATCGACCAGGAGACTGAGGAGGTCCAGCAGCAGCTGGCGCCACCTCCACCAGGC
CACAGTGCCTTCGCCCCAGAGTTTCAACAAACAGACAGTGGCAAGGTTCTGAGCAAGCTG
CAGGCCCGTCTGGATGACCTGTGGGAAGACATCACTCACAGCCTTCATGACCAGGGCCAC
AGCCATCTGGGGGACCCCTGA
|
| Enzyme 84 GenBank Gene ID |
NM_001166598.1  |
| Enzyme 84 GeneCard ID |
APOA5  |
| Enzyme 84 GenAtlas ID |
APOA5  |
| Enzyme 84 HGNC ID |
HGNC:17288  |
| Enzyme 84 Chromosome Location |
1 |
| Enzyme 84 Locus |
11q23 |
| Enzyme 84 SNPs |
SNPJam Report  |
| Enzyme 84 General References |
- van der Vliet HN, Sammels MG, Leegwater AC, Levels JH, Reitsma PH, Boers W, Chamuleau RA: Apolipoprotein A-V: a novel apolipoprotein associated with an early phase of liver regeneration. J Biol Chem. 2001 Nov 30;276(48):44512-20. Epub 2001 Sep 27. [PubMed
]
- Fullerton SM, Buchanan AV, Sonpar VA, Taylor SL, Smith JD, Carlson CS, Salomaa V, Stengard JH, Boerwinkle E, Clark AG, Nickerson DA, Weiss KM: The effects of scale: variation in the APOA1/C3/A4/A5 gene cluster. Hum Genet. 2004 Jun;115(1):36-56. Epub 2004 Apr 24. [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
]
- Pennacchio LA, Olivier M, Hubacek JA, Cohen JC, Cox DR, Fruchart JC, Krauss RM, Rubin EM: An apolipoprotein influencing triglycerides in humans and mice revealed by comparative sequencing. Science. 2001 Oct 5;294(5540):169-73. [PubMed
]
- Beckstead JA, Oda MN, Martin DD, Forte TM, Bielicki JK, Berger T, Luty R, Kay CM, Ryan RO: Structure-function studies of human apolipoprotein A-V: a regulator of plasma lipid homeostasis. Biochemistry. 2003 Aug 12;42(31):9416-23. [PubMed
]
- Prieur X, Coste H, Rodriguez JC: The human apolipoprotein AV gene is regulated by peroxisome proliferator-activated receptor-alpha and contains a novel farnesoid X-activated receptor response element. J Biol Chem. 2003 Jul 11;278(28):25468-80. Epub 2003 Apr 22. [PubMed
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- Weinberg RB, Cook VR, Beckstead JA, Martin DD, Gallagher JW, Shelness GS, Ryan RO: Structure and interfacial properties of human apolipoprotein A-V. J Biol Chem. 2003 Sep 5;278(36):34438-44. Epub 2003 Jun 16. [PubMed
]
- O'Brien PJ, Alborn WE, Sloan JH, Ulmer M, Boodhoo A, Knierman MD, Schultze AE, Konrad RJ: The novel apolipoprotein A5 is present in human serum, is associated with VLDL, HDL, and chylomicrons, and circulates at very low concentrations compared with other apolipoproteins. Clin Chem. 2005 Feb;51(2):351-9. Epub 2004 Nov 4. [PubMed
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- 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
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- Zhou W, Ross MM, Tessitore A, Ornstein D, Vanmeter A, Liotta LA, Petricoin EF 3rd: An initial characterization of the serum phosphoproteome. J Proteome Res. 2009 Dec;8(12):5523-31. [PubMed
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- Pennacchio LA, Olivier M, Hubacek JA, Krauss RM, Rubin EM, Cohen JC: Two independent apolipoprotein A5 haplotypes influence human plasma triglyceride levels. Hum Mol Genet. 2002 Nov 15;11(24):3031-8. [PubMed
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- Vrablik M, Horinek A, Ceska R, Adamkova V, Poledne R, Hubacek JA: Ser19-->Trp polymorphism within the apolipoprotein AV gene in hypertriglyceridaemic people. J Med Genet. 2003 Aug;40(8):e105. [PubMed
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- Marcais C, Verges B, Charriere S, Pruneta V, Merlin M, Billon S, Perrot L, Drai J, Sassolas A, Pennacchio LA, Fruchart-Najib J, Fruchart JC, Durlach V, Moulin P: Apoa5 Q139X truncation predisposes to late-onset hyperchylomicronemia due to lipoprotein lipase impairment. J Clin Invest. 2005 Oct;115(10):2862-9. [PubMed
]
|
| Enzyme 84 Metabolite References |
Not Available |
|
Enzyme 85
[top]
|
| Enzyme 85 ID |
17305 |
| Enzyme 85 Name |
Uteroglobin |
| Enzyme 85 Synonyms |
- Clara cell phospholipid-binding protein
- CCPBP
- Clara cells 10 kDa secretory protein
- CC10
- Secretoglobin family 1A member 1
- Urinary protein 1
- UP-1
- UP1
- Urine protein 1
|
| Enzyme 85 Gene Name |
SCGB1A1 |
| Enzyme 85 Protein Sequence |
>Uteroglobin
MKLAVTLTLVTLALCCSSASAEICPSFQRVIETLLMDTPSSYEAAMELFSPDQDMREAGA
QLKKLVDTLPQKPRESIIKLMEKIAQSSLCN
|
| Enzyme 85 Number of Residues |
91 |
| Enzyme 85 Molecular Weight |
9993.6 |
| Enzyme 85 Theoretical pI |
4.71 |
| Enzyme 85 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 85 General Function |
Involved in binding |
| Enzyme 85 Specific Function |
Binds phosphatidylcholine, phosphatidylinositol, polychlorinated biphenyls (PCB) and weakly progesterone, potent inhibitor of phospholipase A2 |
| Enzyme 85 Pathways |
Not Available |
| Enzyme 85 Reactions |
Not Available |
| Enzyme 85 Pfam Domain Function |
|
| Enzyme 85 Signals |
|
| Enzyme 85 Transmembrane Regions |
|
| Enzyme 85 Essentiality |
Not Available |
| Enzyme 85 GenBank ID Protein |
189053293  |
| Enzyme 85 UniProtKB/Swiss-Prot ID |
P11684  |
| Enzyme 85 UniProtKB/Swiss-Prot Entry Name |
UTER_HUMAN  |
| Enzyme 85 PDB ID |
Not Available |
| Enzyme 85 Cellular Location |
Not Available |
| Enzyme 85 Gene Sequence |
>276 bp
ATGAAACTCGCTGTCACCCTCACCCTGGTCACACTGGCTCTCTGCTGCAGCTCCGCTTCT
GCAGAGATCTGCCCGAGCTTTCAGCGTGTCATCGAAACCCTCCTCATGGACACACCCTCC
AGTTATGAGGCTGCCATGGAACTTTTCAGCCCTGATCAAGACATGAGGGAGGCAGGGGCT
CAGCTGAAGAAGCTGGTGGACACCCTCCCCCAAAAGCCCAGAGAAAGCATCATTAAGCTC
ATGGAAAAAATAGCCCAAAGCTCACTGTGTAATTAG
|
| Enzyme 85 GenBank Gene ID |
AK312165  |
| Enzyme 85 GeneCard ID |
SCGB1A1  |
| Enzyme 85 GenAtlas ID |
SCGB1A1  |
| Enzyme 85 HGNC ID |
HGNC:12523  |
| Enzyme 85 Chromosome Location |
1 |
| Enzyme 85 Locus |
11q12.3-q13.1 |
| Enzyme 85 SNPs |
SNPJam Report  |
| Enzyme 85 General References |
- Singh G, Katyal SL, Brown WE, Phillips S, Kennedy AL, Anthony J, Squeglia N: Amino-acid and cDNA nucleotide sequences of human Clara cell 10 kDa protein. Biochim Biophys Acta. 1988 Sep 7;950(3):329-37. [PubMed
]
- Hay JG, Danel C, Chu CS, Crystal RG: Human CC10 gene expression in airway epithelium and subchromosomal locus suggest linkage to airway disease. Am J Physiol. 1995 Apr;268(4 Pt 1):L565-75. [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
]
- Wolf M, Klug J, Hackenberg R, Gessler M, Grzeschik KH, Beato M, Suske G: Human CC10, the homologue of rabbit uteroglobin: genomic cloning, chromosomal localization and expression in endometrial cell lines. Hum Mol Genet. 1992 Sep;1(6):371-8. [PubMed
]
- Okutani R, Itoh Y, Hirata H, Kasahara T, Mukaida N, Kawai T: Simple and high-yield purification of urine protein 1 using immunoaffinity chromatography: evidence for the identity of urine protein 1 and human Clara cell 10-kilodalton protein. J Chromatogr. 1992 May 20;577(1):25-35. [PubMed
]
- Bernard A, Roels H, Lauwerys R, Witters R, Gielens C, Soumillion A, Van Damme J, De Ley M: Human urinary protein 1: evidence for identity with the Clara cell protein and occurrence in respiratory tract and urogenital secretions. Clin Chim Acta. 1992 May 15;207(3):239-49. [PubMed
]
- Ghafouri B, Stahlbom B, Tagesson C, Lindahl M: Newly identified proteins in human nasal lavage fluid from non-smokers and smokers using two-dimensional gel electrophoresis and peptide mass fingerprinting. Proteomics. 2002 Jan;2(1):112-20. [PubMed
]
- Umland TC, Swaminathan S, Singh G, Warty V, Furey W, Pletcher J, Sax M: Structure of a human Clara cell phospholipid-binding protein-ligand complex at 1.9 A resolution. Nat Struct Biol. 1994 Aug;1(8):538-45. [PubMed
]
|
| Enzyme 85 Metabolite References |
Not Available |