|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5671 |
| Enzyme 1 Name |
Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 |
| Enzyme 1 Synonyms |
- Forssman glycolipid synthase-like protein
|
| Enzyme 1 Gene Name |
GBGT1 |
| Enzyme 1 Protein Sequence |
>Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
MHRRRLALGLGFCLLAGTSLSVLWVYLENWLPVSYVPYYLPCPEIFNMKLHYKREKPLQP
VVWSQYPQPKLLEHRPTQLLTLTPWLAPIVSEGTFNPELLQHIYQPLNLTIGVTVFAVGK
YTHFIQSFLESAEEFFMRGYRVHYYIFTDNPAAVPGVPLGPHRLLSSIPIQGHSHWEETS
MRRMETISQHIAKRAHREVDYLFCLDVDMVFRNPWGPETLGDLVAAIHPSYYAVPRQQFP
YERRRVSTAFVADSEGDFYYGGAVFGGQVARVYEFTRGCHMAILADKANGIMAAWREESH
LNRHFISNKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKDISCLRS
|
| Enzyme 1 Number of Residues |
347 |
| Enzyme 1 Molecular Weight |
40126.9 |
| Enzyme 1 Theoretical pI |
8.63 |
| Enzyme 1 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolic process
- metabolic process
- primary metabolic process
|
| Component |
|
|
| Enzyme 1 General Function |
Involved in transferase activity, transferring hexosyl groups |
| Enzyme 1 Specific Function |
Catalyzes the formation of some glycolipid via the addition of N-acetylgalactosamine (GalNAc) in alpha-1,3-linkage to some substrate. Glycolipids probably serve for adherence of some pathogens |
| 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 |
6272650  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q8N5D6  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
GBGT1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1044 bp
ATGCATCGCCGGAGACTGGCCCTGGGTCTGGGGTTCTGCCTGTTGGCGGGCACAAGCCTC
AGTGTCCTGTGGGTGTATCTTGAGAACTGGCTGCCAGTCTCCTATGTCCCCTATTATCTC
CCCTGCCCAGAGATCTTCAACATGAAGCTGCACTACAAGAGGGAGAAGCCACTCCAGCCC
GTGGTATGGTCACAGTACCCTCAGCCCAAGCTGCTGGAGCACAGGCCCACACAGCTGCTG
ACACTCACACCCTGGTTGGCGCCCATCGTCTCCGAGGGAACCTTCAACCCAGAGCTTCTG
CAGCACATCTACCAGCCACTGAACCTGACCATTGGGGTCACGGTGTTTGCCGTGGGGAAG
TACACTCATTTCATCCAGTCCTTCCTGGAGTCAGCCGAGGAGTTCTTCATGCGTGGGTAC
CGGGTGCACTACTACATCTTCACTGACAACCCTGCAGCCGTTCCCGGGGTCCCGCTGGGT
CCCCACCAGCTTCTCAGCTCCATCCCCATCCAGGGTCACTCCCACTGGGAGGAGACATCC
ATGCGCCGGATGGAGACCATCAGCCAGCACATTGCTAAGAGGGCTCACCGGGAGGTGGAC
TACTTTTTCTGCCTTGATGTGGACATGGTGTTTCGGAACCCGTGGGGCCCTGAGACCTTG
GGAGACCTGGTGGCTGCCATTCACCCAAGCTACTACGCCGTTCCCCGCCAGCAGTTCCCC
TATGAGCGCAGGCGTGTTTCCACTGCCTTTGTGGCAGACAGGGAAGGGGACTTCTATTAT
GGTGGGGCAGTCTTCGGGGGGCAGGTGGCCAGGGTATATGAGTTTACTAGGGGCTGCCAC
ATGGCCATCCTGGCGGACAAGGCCAATGGCATCATGGCTGCCTGGCGGGAGGAAAGCCAC
CTGAACCGTCACTTCATCTCAAACAAGCCGTCCAAGGTGCTGTCCCCCGAGTACCTCTGG
GACGACAGGAAGCCCCAGCCACCCAGCCTGAAGCTGATCCGCTTTTCTACACTGGACAAG
GATATCAGCTGCCTGAGGAGCTGA
|
| Enzyme 1 GenBank Gene ID |
AF163572  |
| Enzyme 1 GeneCard ID |
GBGT1  |
| Enzyme 1 GenAtlas ID |
GBGT1  |
| Enzyme 1 HGNC ID |
HGNC:20460  |
| Enzyme 1 Chromosome Location |
9 |
| Enzyme 1 Locus |
9q34.13-q34.3 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Xu H, Storch T, Yu M, Elliott SP, Haslam DB: Characterization of the human Forssman synthetase gene. An evolving association between glycolipid synthesis and host-microbial interactions. J Biol Chem. 1999 Oct 8;274(41):29390-8. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5829 |
| Enzyme 2 Name |
N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase |
| Enzyme 2 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class L protein
- PIG-L
|
| Enzyme 2 Gene Name |
PIGL |
| Enzyme 2 Protein Sequence |
>N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL
|
| Enzyme 2 Number of Residues |
252 |
| Enzyme 2 Molecular Weight |
28531.0 |
| Enzyme 2 Theoretical pI |
8.23 |
| Enzyme 2 GO Classification |
Not Available |
| Enzyme 2 General Function |
Involved in N-acetylglucosaminylphosphatidylinositol de |
| Enzyme 2 Specific Function |
Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol |
| Enzyme 2 Pathways |
Not Available |
| Enzyme 2 Reactions |
- 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate [RN:R03482 R05917]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
4239986  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9Y2B2  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PIGL_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>759 bp
ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA
|
| Enzyme 2 GenBank Gene ID |
AB017165  |
| Enzyme 2 GeneCard ID |
PIGL  |
| Enzyme 2 GenAtlas ID |
PIGL  |
| Enzyme 2 HGNC ID |
HGNC:8966  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
17p12-p11.2 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Watanabe R, Ohishi K, Maeda Y, Nakamura N, Kinoshita T: Mammalian PIG-L and its yeast homologue Gpi12p are N-acetylglucosaminylphosphatidylinositol de-N-acetylases essential in glycosylphosphatidylinositol biosynthesis. Biochem J. 1999 Apr 1;339 ( Pt 1):185-92. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
6049 |
| Enzyme 3 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 2 |
| Enzyme 3 Synonyms |
- Sphingomyelin synthase 2
|
| Enzyme 3 Gene Name |
SGMS2 |
| Enzyme 3 Protein Sequence |
>Phosphatidylcholine:ceramide cholinephosphotransferase 2
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
|
| Enzyme 3 Number of Residues |
365 |
| Enzyme 3 Molecular Weight |
42279.8 |
| Enzyme 3 Theoretical pI |
9.00 |
| Enzyme 3 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 3 General Function |
Involved in catalytic activity |
| Enzyme 3 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 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
- 80-100
128-148
159-179
206-226
248-268
275-295
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q8NHU3  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SMS2_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1098 bp
ATGGATATCATAGAGACAGCAAAACTTGAAGAACATTTGGAAAATCAACCCAGTGATCCT
ACGAACACTTATGCAAGACCCGCTGAACCTGTTGAAGAAGAAAACAAAAATGGCAATGGT
AAACCCAAGAGCTTATCCAGTGGGCTGCGAAAAGGCACCAAAAAGTACCCGGACTATATC
CAAATTGCTATGCCCACTGAATCAAGGAACAAATTTCCACTAGAGTGGTGGAAAACGGGC
ATTGCCTTCATATATGCAGTTTTCAACCTCGTCTTGACAACCGTCATGATCACAGTTGTA
CATGAGAGGGTCCCTCCCAAGGAGCTTAGCCCTCCACTCCCAGACAAGTTTTTTGATTAC
ATTGATAGGGTGAAATGGGCATTTTCTGTATCAGAAATAAATGGGATTATATTAGTTGGA
TTATGGATCACCCAGTGGCTGTTTCTGAGATACAAGTCAATAGTGGGACGCAGATTCTGT
TTTATTATTGGAACTTTATACCTGTATCGCTGCATTACAATGTATGTTACTACTCTACCT
GTGCCTGGAATGCATTTCCAGTGTGCTCCAAAGCTCAATGGAGACTCTCAGGCAAAAGTT
CAACGGATTCTACGATTGATTTCTGGTGGTGGATTGTCCATAACTGGATCACATATCTTA
TGTGGAGACTTCCTCTTCAGCGGTCACACGGTTACGCTGACACTGACTTATTTGTTCATC
AAAGAATATTCGCCTCGTCACTTCTGGTGGTATCATTTAATCTGCTGGCTGCTGAGTGCT
GCCGGGATCATCTGCATTCTTGTAGCACACGAACACTACACTATCGATGTGATCATTGCT
TATTATATCACAACACGACTGTTTTGGTGGTACCATTCAATGGCCAATGAAAAGAACTTG
AAGGTCTCTTCACAGACTAATTTCTTATCTCGAGCATGGTGGTTCCCCATCTTTTATTTT
TTTGAGAAAAATGTACAAGGCTCAATTCCTTGCTGCTTCTCCTGGCCGCTGTCTTGGCCT
CCTGGCTGCTTCAAATCATCATGCAAAAAGTATTCACGGGTTCAGAAGATTGGTGAAGAC
AATGAGAAATCGACCTGA
|
| Enzyme 3 GenBank Gene ID |
AF452717  |
| Enzyme 3 GeneCard ID |
SGMS2  |
| Enzyme 3 GenAtlas ID |
SGMS2  |
| Enzyme 3 HGNC ID |
HGNC:28395  |
| Enzyme 3 Chromosome Location |
4 |
| Enzyme 3 Locus |
4q25 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
6054 |
| Enzyme 4 Name |
Phosphatidylcholine:ceramide cholinephosphotransferase 1 |
| Enzyme 4 Synonyms |
- Medulla oblongata-derived protein
- Protein Mob
- Sphingomyelin synthase 1
- Transmembrane protein 23
|
| Enzyme 4 Gene Name |
SGMS1 |
| Enzyme 4 Protein Sequence |
>Phosphatidylcholine:ceramide cholinephosphotransferase 1
MLSASTMKEVVYWSPKKVADWLLENAMPEYCEPLEHFTGQDLINLTQEDFKKPPLCRVSS
DNGQRLLDMIETLKMEHHLEAHKNGHANGHLNIGVDIPTPDGSFSIKIKPNGMPNGYRKE
MIKIPMPELERSQYPMEWGKTFLAFLYALSCFVLTTVMISVVHERVPPKEVQPPLPDTFF
DHFNRVQWAFSICEINGMILVGLWLIQWLLLKYKSIISRRFFCIVGTLYLYRCITMYVTT
LPVPGMHFNCSPKLFGDWEAQLRRIMKLIAGGGLSITGSHNMCGDYLYSGHTVMLTLTYL
FIKEYSPRRLWWYHWICWLLSVVGIFCILLAHDHYTVDVVVAYYITTRLFWWYHTMANQQ
VLKEASQMNLLARVWWYRPFQYFEKNVQGIVPRSYHWPFPWPVVHLSRQVKYSRLVNDT
|
| Enzyme 4 Number of Residues |
419 |
| Enzyme 4 Molecular Weight |
49207.3 |
| Enzyme 4 Theoretical pI |
8.51 |
| Enzyme 4 GO Classification |
| Function |
|
| Process |
| — |
| Component |
|
|
| Enzyme 4 General Function |
Involved in catalytic activity |
| Enzyme 4 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 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
- a ceramide + a phosphatidylcholine = a sphingomyelin + a 1,2-diacyl-sn-glycerol [RN:R08969]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
- 142-162
190-210
221-241
282-302
310-330
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
29789379  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q86VZ5  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
SMS1_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 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 4 GenBank Gene ID |
Not Available |
| Enzyme 4 GeneCard ID |
SGMS1  |
| Enzyme 4 GenAtlas ID |
SGMS1  |
| Enzyme 4 HGNC ID |
HGNC:29799  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
10q11.2 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6055 |
| Enzyme 5 Name |
Sphingomyelin phosphodiesterase |
| Enzyme 5 Synonyms |
- Acid sphingomyelinase
- aSMase
|
| Enzyme 5 Gene Name |
SMPD1 |
| Enzyme 5 Protein Sequence |
>Sphingomyelin phosphodiesterase
MPRYGASLRQSCPRSGREQGQDGTAGAPGLLWMGLVLALALALALALSDSRVLWAPAEAH
PLSPQGHPARLHRIVPRLRDVFGWGNLTCPICKGLFTAINLGLKKEPNVARVGSVAIKLC
NLLKIAPPAVCQSIVHLFEDDMVEVWRRSVLSPSEACGLLLGSTCGHWDIFSSWNISLPT
VPKPPPKPPSPPAPGAPVSRILFLTDLHWDHDYLEGTDPDCADPLCCRRGSGLPPASRPG
AGYWGEYSKCDLPLRTLESLLSGLGPAGPFDMVYWTGDIPAHDVWHQTRQDQLRALTTVT
ALVRKFLGPVPVYPAVGNHESTPVNSFPPPFIEGNHSSRWLYEAMAKAWEPWLPAEALRT
LRIGGFYALSPYPGLRLISLNMNFCSRENFWLLINSTDPAGQLQWLVGELQAAEDRGDKV
HIIGHIPPGHCLKSWSWNYYRIVARYENTLAAQFFGHTHVDEFEVFYDEETLSRPLAVAF
LAPSATTYIGLNPGYRVYQIDGNYSGSSHVVLDHETYILNLTQANIPGAIPHWQLLYRAR
ETYGLPNTLPTAWHNLVYRMRGDMQLFQTFWFLYHKGHPPSEPCGTPCRLATLCAQLSAR
ADSPALCRHLMPDGSLPEAQSLWPRPLFC
|
| Enzyme 5 Number of Residues |
629 |
| Enzyme 5 Molecular Weight |
69751.3 |
| Enzyme 5 Theoretical pI |
7.30 |
| Enzyme 5 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- phospholipase activity
- sphingomyelin phosphodiesterase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- sphingomyelin catabolic process
- sphingomyelin metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in hydrolase activity |
| Enzyme 5 Specific Function |
Converts sphingomyelin to ceramide. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Isoform 2 and isoform 3 have lost catalytic activity |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
179095  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P17405  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
ASM_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1890 bp
ATGCCCCGCTACGGAGCGTCACTCCGCCAGAGCTGCCCCAGGTCCGGCCGGGAGCAGGGA
CAAGACGGGACCGCCGGAGCCCCCGGACTCCTTTGGATGGGCCTGGTGCTGGCGCTGGCG
CTGGCGCTGGCGCTGGCTCTGTCTGACTCTCGGGTTCTCTGGGCTCCGGCAGAGGCTCAC
CCTCTTTCTCCCCAAGGCCATCCTGCCAGGTTACATCGCATAGTGCCCCGGCTCCGAGAT
GTCTTTGGGTGGGGGAACCTCACCTGCCCAATCTGCAAAGGTCTATTCACCGCCATCAAC
CTCGGGCTGAAGAAGGAACCCAATGTGGCTCGCGTGGGCTCCGTGGCCATCAAGCTGTGC
AATCTGCTGAAGATAGCACCACCTGCCGTGTGCCAATCCATTGTCCACCTCTTTGAGGAT
GACATGGTGGAGGTGTGGAGACGCTCAGTGCTGAGCCCATCTGAGGCCTGTGGCCTGCTC
CTGGGCTCCACCTGTGGGCACTGGGACATTTTCTCATCTTGGAACATCTCTTTGCCTACT
GTGCCGAAGCCGCCCCCCAAACCCCCTAGCCCCCCAGCCCCAGGTGCCCCTGTCAGCCGC
ATCCTCTTCCTCACTGACCTGCACTGGGATCATGACTACCTGGAGGGCACGGACCCTGAC
TGTGCAGACCCACTGTGCTGCCGCCGGGGTTCTGGCCTGCCGCCCGCATCCCGGCCAGGT
GCCGGATACTGGGGCGAATACAGCAAGTGTGACCTGCCCCTGAGGACCCTGGAGAGCCTG
TTGAGTGGGCTGGGCCCAGCCGGCCCTTTTGATATGGTGTACTGGACAGGAGACATCCCC
GCACATGATGTCTGGCACCAGACTCGTCAGGACCAACTGCGGGCCCTGACCACCGTCACA
GCACTTGTGAGGAAGTTCCTGGGGCCAGTGCCAGTGTACCCTGCTGTGGGTAACCATGAA
AGCATACCTGTCAATAGCTTCCCTCCCCCCTTCATTGAGGGCAACCACTCCTCCCGCTGG
CTCTATGAAGCGATGGCCAAGGCTTGGGAGCCCTGGCTGCCTGCCGAAGCCCTGCGCACC
CTCAGAATTGGGGGGTTCTATGCTCTTTCCCCATACCCCGGTCTCCGCCTCATCTCTCTC
AATATGAATTTTTGTTCCCGTGAGAACTTCTGGCTCTTGATCAACTCCACGGATCCCGCA
GGACAGCTCCAGTGGCTGGTGGGGGAGCTTCAGGCTGCTGAGGATCGAGGAGACAAAGTG
CATATAATTGGCCACATTCCCCCAGGGCACTGTCTGAAGAGCTGGAGCTGGAATTATTAC
CGAATTGTAGCCAGGTATGAGAACACCCTGGCTGCTCAGTTCTTTGGCCACACTCATGTG
GATGAATTTGAGGTCTTCTATGATGAAGAGACTCTGAGCCGGCCGCTGGCTGTAGCCTTC
CTGGCACCCAGTGCAACTACCTACATCGGCCTTAATCCTGGTTACCGTGTGTACCAAATA
GATGGAAACTACTCCAGGAGCTCTCACGTGGTCCTGGACCATGAGACCTACATCCTGAAT
CTGACCCAGGCAAACATACCGGGAGCCATACCGCACTGGCAGCTTCTCTACAGGGCTCGA
GAAACCTATGGGCTGCCCAACACACTGCCTACCGCCTGGCACAACCTGGTATATCGCATG
CGGGGCGACATGCAACTTTTCCAGACCTTCTGGTTTCTCTACCATAAGGGCCACCCACCC
TCGGAGCCCTGTGGCACGCCCTGCCGTCTGGCTACTCTTTGTGCCCAGCTCTCTGCCCGT
GCTGACAGCCCTGCTCTGTGCCGCCACCTGATGCCAGATGGGAGCCTCCCAGAGGCCCAG
AGCCTGTGGCCAAGGCCACTGTTTTGCTAG
|
| Enzyme 5 GenBank Gene ID |
M59916  |
| Enzyme 5 GeneCard ID |
SMPD1  |
| Enzyme 5 GenAtlas ID |
SMPD1  |
| Enzyme 5 HGNC ID |
HGNC:11120  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
11p15.4-p15.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Schuchman EH, Suchi M, Takahashi T, Sandhoff K, Desnick RJ: Human acid sphingomyelinase. Isolation, nucleotide sequence and expression of the full-length and alternatively spliced cDNAs. J Biol Chem. 1991 May 5;266(13):8531-9. [PubMed
]
- Newrzella D, Stoffel W: Molecular cloning of the acid sphingomyelinase of the mouse and the organization and complete nucleotide sequence of the gene. Biol Chem Hoppe Seyler. 1992 Dec;373(12):1233-8. [PubMed
]
- Schuchman EH, Levran O, Pereira LV, Desnick RJ: Structural organization and complete nucleotide sequence of the gene encoding human acid sphingomyelinase (SMPD1). Genomics. 1992 Feb;12(2):197-205. [PubMed
]
- Ida H, Rennert OM, Eto Y, Chan WY: Cloning of a human acid sphingomyelinase cDNA with a new mutation that renders the enzyme inactive. J Biochem (Tokyo). 1993 Jul;114(1):15-20. [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
]
- Quintern LE, Schuchman EH, Levran O, Suchi M, Ferlinz K, Reinke H, Sandhoff K, Desnick RJ: Isolation of cDNA clones encoding human acid sphingomyelinase: occurrence of alternatively processed transcripts. EMBO J. 1989 Sep;8(9):2469-73. [PubMed
]
- Ferlinz K, Hurwitz R, Moczall H, Lansmann S, Schuchman EH, Sandhoff K: Functional characterization of the N-glycosylation sites of human acid sphingomyelinase by site-directed mutagenesis. Eur J Biochem. 1997 Jan 15;243(1-2):511-7. [PubMed
]
- Lansmann S, Schuette CG, Bartelsen O, Hoernschemeyer J, Linke T, Weisgerber J, Sandhoff K: Human acid sphingomyelinase. Eur J Biochem. 2003 Mar;270(6):1076-88. [PubMed
]
- Dastani Z, Ruel IL, Engert JC, Genest J Jr, Marcil M: Sphingomyelin phosphodiesterase-1 (SMPD1) coding variants do not contribute to low levels of high-density lipoprotein cholesterol. BMC Med Genet. 2007 Dec 18;8:79. [PubMed
]
- Ferlinz K, Hurwitz R, Sandhoff K: Molecular basis of acid sphingomyelinase deficiency in a patient with Niemann-Pick disease type A. Biochem Biophys Res Commun. 1991 Sep 30;179(3):1187-91. [PubMed
]
- Levran O, Desnick RJ, Schuchman EH: Niemann-Pick disease: a frequent missense mutation in the acid sphingomyelinase gene of Ashkenazi Jewish type A and B patients. Proc Natl Acad Sci U S A. 1991 May 1;88(9):3748-52. [PubMed
]
- Levran O, Desnick RJ, Schuchman EH: Niemann-Pick type B disease. Identification of a single codon deletion in the acid sphingomyelinase gene and genotype/phenotype correlations in type A and B patients. J Clin Invest. 1991 Sep;88(3):806-10. [PubMed
]
- Levran O, Desnick RJ, Schuchman EH: Identification and expression of a common missense mutation (L302P) in the acid sphingomyelinase gene of Ashkenazi Jewish type A Niemann-Pick disease patients. Blood. 1992 Oct 15;80(8):2081-7. [PubMed
]
- Takahashi T, Desnick RJ, Takada G, Schuchman EH: Identification of a missense mutation (S436R) in the acid sphingomyelinase gene from a Japanese patient with type B Niemann-Pick disease. Hum Mutat. 1992;1(1):70-1. [PubMed
]
- Takahashi T, Suchi M, Desnick RJ, Takada G, Schuchman EH: Identification and expression of five mutations in the human acid sphingomyelinase gene causing types A and B Niemann-Pick disease. Molecular evidence for genetic heterogeneity in the neuronopathic and non-neuronopathic forms. J Biol Chem. 1992 Jun 25;267(18):12552-8. [PubMed
]
- Sperl W, Bart G, Vanier MT, Christomanou H, Baldissera I, Steichen-Gersdorf E, Paschke E: A family with visceral course of Niemann-Pick disease, macular halo syndrome and low sphingomyelin degradation rate. J Inherit Metab Dis. 1994;17(1):93-103. [PubMed
]
- Schuchman EH: Two new mutations in the acid sphingomyelinase gene causing type a Niemann-pick disease: N389T and R441X. Hum Mutat. 1995;6(4):352-4. [PubMed
]
- Takahashi T, Suchi M, Sato W, Ten SB, Sakuragawa N, Desnick RJ, Schuchman EH, Takada G: Identification and expression of a missense mutation (Y446C) in the acid sphingomyelinase gene from a Japanese patient with type A Niemann-Pick disease. Tohoku J Exp Med. 1995 Oct;177(2):117-23. [PubMed
]
- Ida H, Rennert OM, Maekawa K, Eto Y: Identification of three novel mutations in the acid sphinogomyelinase gene of Japanese patients with Niemann-Pick disease type A and B. Hum Mutat. 1996;7(1):65-7. [PubMed
]
- Pavlu H, Elleder M: Two novel mutations in patients with atypical phenotypes of acid sphingomyelinase deficiency. J Inherit Metab Dis. 1997 Aug;20(4):615-6. [PubMed
]
- Simonaro CM, Desnick RJ, McGovern MM, Wasserstein MP, Schuchman EH: The demographics and distribution of type B Niemann-Pick disease: novel mutations lead to new genotype/phenotype correlations. Am J Hum Genet. 2002 Dec;71(6):1413-9. Epub 2002 Oct 4. [PubMed
]
- Sikora J, Pavlu-Pereira H, Elleder M, Roelofs H, Wevers RA: Seven novel acid sphingomyelinase gene mutations in Niemann-Pick type A and B patients. Ann Hum Genet. 2003 Jan;67(Pt 1):63-70. [PubMed
]
- Ricci V, Stroppiano M, Corsolini F, Di Rocco M, Parenti G, Regis S, Grossi S, Biancheri R, Mazzotti R, Filocamo M: Screening of 25 Italian patients with Niemann-Pick A reveals fourteen new mutations, one common and thirteen private, in SMPD1. Hum Mutat. 2004 Jul;24(1):105. [PubMed
]
- Pittis MG, Ricci V, Guerci VI, Marcais C, Ciana G, Dardis A, Gerin F, Stroppiano M, Vanier MT, Filocamo M, Bembi B: Acid sphingomyelinase: identification of nine novel mutations among Italian Niemann Pick type B patients and characterization of in vivo functional in-frame start codon. Hum Mutat. 2004 Aug;24(2):186-7. [PubMed
]
- Dardis A, Zampieri S, Filocamo M, Burlina A, Bembi B, Pittis MG: Functional in vitro characterization of 14 SMPD1 mutations identified in Italian patients affected by Niemann Pick Type B disease. Hum Mutat. 2005 Aug;26(2):164. [PubMed
]
- Pavlu-Pereira H, Asfaw B, Poupctova H, Ledvinova J, Sikora J, Vanier MT, Sandhoff K, Zeman J, Novotna Z, Chudoba D, Elleder M: Acid sphingomyelinase deficiency. Phenotype variability with prevalence of intermediate phenotype in a series of twenty-five Czech and Slovak patients. A multi-approach study. J Inherit Metab Dis. 2005;28(2):203-27. [PubMed
]
- Mussig K, Harzer K, Mayrhofer H, Krageloh-Mann I, Haring HU, Machicao F: Clinical findings in Niemann-Pick disease type B. Intern Med J. 2006 Feb;36(2):135-6. [PubMed
]
- Rodriguez-Pascau L, Gort L, Schuchman EH, Vilageliu L, Grinberg D, Chabas A: Identification and characterization of SMPD1 mutations causing Niemann-Pick types A and B in Spanish patients. Hum Mutat. 2009 Jul;30(7):1117-22. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6223 |
| Enzyme 6 Name |
Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1 |
| Enzyme 6 Synonyms |
- Beta-1,3-glucuronyltransferase 1
- Glucuronosyltransferase P
- GlcAT-P
- UDP-GlcUA:glycoprotein beta-1,3-glucuronyltransferase
- GlcUAT-P
|
| Enzyme 6 Gene Name |
B3GAT1 |
| Enzyme 6 Protein Sequence |
>Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
MPKRRDILAIVLIVLPWTLLITVWHQSTLAPLLAVHKDEGSDPRRETPPGADPREYCTSD
RDIVEVVRTEYVYTRPPPWSDTLPTIHVVTPTYSRPVQKAELTRMANTLLHVPNLHWLVV
EDAPRRTPLTARLLRDTGLNYTHLHVETPRNYKLRGDARDPRIPRGTMQRNLALRWLRET
FPRNSSQPGVVYFADDDNTYSLELFEEMRSTRRVSVWPVAFVGGLRYEAPRVNGAGKVVG
WKTVFDPHRPFAIDMAGFAVNLRLILQRSQAYFKLRGVKGGYQESSLLRELVTLNDLEPK
AANCTKILVWHTRTEKPVLVNEGKKGFTDPSVEI
|
| Enzyme 6 Number of Residues |
334 |
| Enzyme 6 Molecular Weight |
38255.7 |
| Enzyme 6 Theoretical pI |
10.03 |
| Enzyme 6 GO Classification |
| Function |
- UDP-glycosyltransferase activity
- catalytic activity
- galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity
- glucuronosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
| — |
| Component |
|
|
| Enzyme 6 General Function |
Involved in galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase activity |
| Enzyme 6 Specific Function |
Involved in the biosynthesis of L2/HNK-1 carbohydrate epitope on glycoproteins. Can also play a role in glycosaminoglycan biosynthesis. Substrates include asialo- orosomucoid (ASOR), asialo-fetuin, and asialo-neural cell adhesion molecule. Requires sphingomyelin for activity:stearoyl- sphingomyelin was the most effective, followed by palmitoyl- sphingomyelin and lignoceroyl-sphingomyelin. Activity was demonstrated only for sphingomyelin with a saturated fatty acid and not for that with an unsaturated fatty acid, regardless of the length of the acyl group |
| Enzyme 6 Pathways |
- Chondroitin / Heparan sulfate biosynthesis (map00532
)
|
| Enzyme 6 Reactions |
- UDP-glucuronate + 3-beta-D-galactosyl-4-beta-D-galactosyl-O-beta-D-xylosylprotein = UDP + 3-beta-D-glucuronosyl-3-beta-D-galactosyl-4-beta-D-galactosyl-O- beta-D-xylosylprotein [RN:R04607 R05928]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
8051678  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9P2W7  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
B3GA1_HUMAN  |
| Enzyme 6 PDB ID |
1V84  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1005 bp
ATGCCGAAGAGACGGGACATCCTAGCGATCGTCCTCATCGTGCTGCCCTGGACTCTGCTC
ATCACTGTCTGGCACCAGAGCACCCTCGCACCCCTGCTCGCGGTACATAAGGATGAGGGC
AGTGACCCCCGACGCGAAACGCCGCCCGGCGCCGACCCCAGGGAGTACTGCACGTCTGAC
CGCGACATCGTGGAGGTGGTGCGCACCGAGTACGTGTACACGCGGCCCCCGCCATGGTCC
GACACGCTGCCCACCATCCACGTGGTGACGCCCACCTACAGCCGCCCGGTGCAGAAGGCC
GAGCTGACGCGCATGGCCAACACGCTGCTGCACGTGCCCAACCTCCACTGGCTGGTGGTG
GAGGATGCGCCGCGCCGGACGCCGCTGACCGCGCGCCTGCTGCGCGACACCGGCCTCAAC
TACACGCACCTGCACGTGGAGACGCCCCGCAACTACAAGCTGCGCGGAGACGCCCGCGAC
CCACGCATCCCGCGGGGCACCATGCAGCGCAACCTGGCCCTGCGCTGGCTGCGCGAGACC
TTCCCGCGCAACTCCAGCCAGCCTGGCGTGGTCTACTTCGCCGACGACGACAACACCTAC
AGCCTGGAGCTCTTCGAAGAGATGCGCAGCACCAGGAGGGTGTCCGTGTGGCCCGTCGCC
TTCGTGGGTGGCCTGCGGTACGAGGCCCCACGGGTGAACGGGGCAGGGAAGGTGGTCCGC
TGGAAGACGGTGTTTGACCCCCACCGGCCATTTGCAATAGACATGGCTGGATTTGCCGTC
AACCTGCGGCTCATTCTGCAGCGAAGCCAGGCCTACTTCAAGCTGCGAGGTGTGAAGGGA
GGCTACCAGGAAAGCAGCCTCCTTCGAGAACTTGTCACCCTCAACGACCTGGAGCCCAAG
GCAGCCAACTGCACCAAGATCCTGGTGTGGCACACACGGACAGAGAAGCCAGTGCTGGTG
AATGAGGGCAAGAAGGGCTTCACTGACCCCTCGGTGGAGATCTGA
|
| Enzyme 6 GenBank Gene ID |
AB029396  |
| Enzyme 6 GeneCard ID |
B3GAT1  |
| Enzyme 6 GenAtlas ID |
B3GAT1  |
| Enzyme 6 HGNC ID |
HGNC:921  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
11q25 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Mitsumoto Y, Oka S, Sakuma H, Inazawa J, Kawasaki T: Cloning and chromosomal mapping of human glucuronyltransferase involved in biosynthesis of the HNK-1 carbohydrate epitope. Genomics. 2000 Apr 15;65(2):166-73. [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
]
- Kakuda S, Shiba T, Ishiguro M, Tagawa H, Oka S, Kajihara Y, Kawasaki T, Wakatsuki S, Kato R: Structural basis for acceptor substrate recognition of a human glucuronyltransferase, GlcAT-P, an enzyme critical in the biosynthesis of the carbohydrate epitope HNK-1. J Biol Chem. 2004 May 21;279(21):22693-703. Epub 2004 Mar 1. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6228 |
| Enzyme 7 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q |
| Enzyme 7 Synonyms |
- N-acetylglucosamyl transferase component GPI1
- Phosphatidylinositol-glycan biosynthesis class Q protein
- PIG-Q
|
| Enzyme 7 Gene Name |
PIGQ |
| Enzyme 7 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
MVLKAFFPTCCVSTDSGLLVGRWVPEQSSAVVLAVLHFPFIPIQVKQLLAQVRQASQVGV
AVLGTWCHCRQEPEESLGRFLESLGAVFPHEPWLRLCRERGGTFWSCEATHRQAPTAPGA
PGEDQVMLIFYDQRQVLLSQLHLPTVLPDRQAGATTASTGGLAAVFDTVARSEVLFRSDR
FDEGPVRLSHWQSEGVEASILAELARRASGPICLLLASLLSLVSAVSACRVFKLWPLSFL
GSKLSTCEQLRHRLEHLTLIFSTRKAENPAQLMRKANTVASVLLDVALGLMLLSWLHGRS
RIGHLADALVPVADHVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIH
LMSPFVEHILWHVGLSACLGLTVALSLLSDIIALLTFHIYCFYVYGARLYCLKIHGLSSL
WRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILLFLLPTTALYYLVFTLLRLLVVAV
QGLIHLLVDLINSLPLYSLGLRLCRPYRLADKPTALQPRGAHLPPPQLWLPPQALLGRPV
PQAVPWGAHLPLEAERGQAGLRELLARLAPPHGHSQPSALPGWHQLSWRMSCALWTLLCA
PEHGRPCYHTLGLEVIGSEQMWGWPARLAALHHWHCLPWDPLPTCCGHHGGEHSNPRCPE
HCPMPTLCTQVQRVRPPQQPQVEGWSPWGLPSGSALAVGVEGPCQDEPPSPRHPLAPSAE
QHPASGGLKQSLTPVPSGPGPSLPEPHGVYLRMFPGEVAL
|
| Enzyme 7 Number of Residues |
760 |
| Enzyme 7 Molecular Weight |
84081.4 |
| Enzyme 7 Theoretical pI |
8.08 |
| Enzyme 7 GO Classification |
| Function |
- UDP-glycosyltransferase activity
- acetylglucosaminyltransferase activity
- catalytic activity
- phosphatidylinositol N-acetylglucosaminyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 7 General Function |
Involved in phosphatidylinositol N-acetylglucosaminyltransferase activity |
| Enzyme 7 Specific Function |
Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis |
| Enzyme 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
- 278-298
349-371
378-400
446-468
475-497
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
22538453  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9BRB3  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PIGQ_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>2283 bp
ATGGTGCTCAAGGCCTTCTTCCCCACGTGCTGCGTCTCGACGGACAGCGGGCTGCTGGTG
GGACGGTGGGTGCCGGAGCAGAGCAGCGCCGTGGTCCTGGCGGTCCTGCACTTTCCCTTC
ATCCCCATCCAGGTCAAGCAGCTCCTGGCCCAGGTGCGGCAGGCCAGCCAGGTGGGCGTG
GCCGTGCTGGGCACCTGGTGCCACTGCCGGCAGGAGCCCGAGGAGAGCCTGGGCCGCTTC
CTGGAGAGCCTGGGTGCTGTCTTCCCCCATGAGCCCTGGCTGCGGCTGTGCCGGGAGAGA
GGCGGCACGTTCTGGAGCTGCGAGGCCACCCACCGGCAAGCGCCCACTGCCCCCGGTGCC
CCTGGTGAGGACCAGGTCATGCTCATCTTCTATGACCAGCGCCAGGTGTTGCTGTCACAG
CTACACCTGCCCACCGTCCTGCCCGACCGCCAGGCTGGAGCCACCACTGCCAGCACGGGG
GGCCTGGCTGCCGTCTTCGACACGGTAGCACGCAGTGAGGTGCTCTTCCGCAGTGACCGC
TTTGATGAGGGCCCCGTGCGGCTGAGCCACTGGCAGTCGGAGGGCGTGGAGGCCAGCATC
CTCGCGGAGCTGGCCAGGCGAGCCTCGGGACCCATTTGCCTGCTGTTGGCCAGCCTGCTG
TCGCTGGTCTCAGCTGTCAGTGCCTGCCGAGTGTTCAAGCTCTGGCCCCTGTCCTTCCTC
GGGAGCAAACTCTCCACGTGCGAACAGCTCCGGCACCGGCTGGAGCACCTCACGCTAATC
TTCAGTACACGGAAGGCGGAGAACCCTGCCCAGCTGATGAGGAAGGCCAACACGGTGGCC
TCTGTGCTGCTGGACGTGGCCCTGGGCCTCATGCTGCTGTCCTGGCTCCACGGGAGAAGC
CGCATCGGGCATCTGGCCGACGCCCTCGTTCCTGTGGCTGACCACGTGGCCGAGGAGCTC
CAGCATCTGCTGCAGTGGCTGATGGGTGCTCCCGCCGGGCTCAAGATGAACCGTGCACTG
GACCAGGTGCTGGGCCGCTTCTTCCTCTACCACATCCACCTGTGGATCAGCTACATCCAC
CTCATGTCCCCCTTCGTGGAGCACATCCTTTGGCACGTGGGCCTCTCGGCCTGCCTGGGC
CTGACGGTGGCCCTGTCCCTCCTCTCGGACATTATCGCCCTCCTCACCTTCCACATCTAC
TGCTTTTACGTCTATGGAGCCAGGCTGTACTGCCTGAAGATCCATGGCCTGTCCTCACTG
TGGCGTCTGTTCCGGGGGAAGAAGTGGAACGTTCTGCGCCAGCGCGTGGACTCCTGTTCC
TATGACCTGGACCAGCTGTTCATCGGGACTCTGCTCTTCACCATCCTGCTCTTCCTCCTG
CCTACCACAGCCCTGTACTACCTGGTGTTCACCCTGCTCCGGCTCCTGGTGGTCGCCGTG
CAGGGCCTGATCCATCTGCTCGTGGACCTCATCAACTCCCTGCCGCTGTACTCACTGGGT
CTTCGGCTCTGCCGGCCCTACAGGCTGGCGGATAAACCCACTGCCCTACAGCCGCGTGGT
GCACACCTACCGCCTCCCCAGCTGTGGCTGCCACCCCAAGCACTCCTGGGGCGCCCTGTG
CCGCAAGCTGTTCCTTGGGGAGCTCATCTACCCCTGGAGGCAGAGAGGGGACAAGCAGGA
CTGAGGGAACTGCTGGCTCGCCTGGCACCACCACACGGCCACAGCCAGCCATCTGCTCTG
CCAGGGTGGCACCAGCTCAGCTGGCGCATGTCCTGTGCTTTGTGGACGCTGCTGTGTGCT
CCTGAACACGGCAGGCCCTGCTATCACACCTTGGGCTTGGAGGTCATTGGGAGTGAGCAG
ATGTGGGGGTGGCCAGCCAGGCTGGCCGCACTCCATCACTGGCACTGCCTGCCTTGGGAC
CCGCTTCCCACCTGCTGCGGTCACCATGGTGGCGAGCACAGCAACCCCAGGTGTCCAGAG
CACTGCCCCATGCCCACCCTGTGTACCCAGGTCCAGAGGGTCCGTCCACCACAGCAGCCC
CAGGTGGAGGGCTGGTCTCCCTGGGGGCTCCCCAGTGGCTCTGCCCTGGCTGTGGGGGTG
GAGGGACCTTGCCAGGATGAACCCCCCAGTCCCAGGCACCCTCTAGCTCCCTCAGCCGAA
CAGCACCCTGCATCTGGGGGATTGAAGCAGTCGCTGACCCCCGTCCCCAGCGGGCCCGGG
CCCTCACTCCCTGAACCACACGGGGTTTATTTGCGGATGTTCCCTGGAGAGGTCGCTTTG
TGA
|
| Enzyme 7 GenBank Gene ID |
NM_148920.1  |
| Enzyme 7 GeneCard ID |
PIGQ  |
| Enzyme 7 GenAtlas ID |
PIGQ  |
| Enzyme 7 HGNC ID |
HGNC:14135  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
16p13.3 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Tiede A, Schubert J, Nischan C, Jensen I, Westfall B, Taron CH, Orlean P, Schmidt RE: Human and mouse Gpi1p homologues restore glycosylphosphatidylinositol membrane anchor biosynthesis in yeast mutants. Biochem J. 1998 Sep 15;334 ( Pt 3):609-16. [PubMed
]
- Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [PubMed
]
- Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [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
]
- Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa K, Julius M, Kinoshita T: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 2000 Aug 15;19(16):4402-11. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6229 |
| Enzyme 8 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit A |
| Enzyme 8 Synonyms |
- GlcNAc-PI synthesis protein
- Phosphatidylinositol-glycan biosynthesis class A protein
- PIG-A
|
| Enzyme 8 Gene Name |
PIGA |
| Enzyme 8 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
|
| Enzyme 8 Number of Residues |
484 |
| Enzyme 8 Molecular Weight |
54126.1 |
| Enzyme 8 Theoretical pI |
8.41 |
| Enzyme 8 GO Classification |
| Function |
| — |
| Process |
- GPI anchor biosynthetic process
- biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in biosynthetic process |
| Enzyme 8 Specific Function |
Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis |
| Enzyme 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
- UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
23398601  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P37287  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PIGA_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>1455 bp
ATGGCCTGTAGAGGAGGAGCTGGGAATGGCCACCGTGCCTCAGCTACACTCTCTCGGGTT
AGCCCTGGAAGTCTTTACACATGTAGAACCCGTACCCATAATATATGCATGGTATCTGAC
TTTTTCTACCCAAATATGGGAGGCGTGGAAAGCCACATTTACCAGCTCTCTCAGTGCCTG
ATTGAAAGAGGGCATAAGGTTATAATTGTCACCCATGCTTATGGAAATCGAAAAGGCATC
CGTTACCTCACCAGTGGCCTCAAAGTCTATTACTTGCCTCTGAAAGTCATGTACAACCAG
TCTACAGCCACGACCCTCTTTCACAGTCTGCCATTGCTCAGGTACATATTTGTTCGGGAG
AGAGTCACGATAATCCATTCACATAGTTCTTTTTCTGCTATGGCCCATGATGCTCTCTTC
CACGCCAAGACAATGGGGCTTCAGACAGTCTTCACGGACCATTCCCTTTTTGGATTTGCT
GATGTCAGCTCGGTGCTTACAAACAAGCTTCTAACCGTGTCTCTTTGTGATACAAACCAC
ATCATTTGTGTGTCTTATACTAGTAAGGAAAATACTGTACTAAGAGCAGCACTGAATCCT
GAAATAGTGTCCGTCATTCCTAATGCTGTAGATCCTACTGACTTCACTCCAGACCCATTT
AGAAGGCATGATAGTATAACTATTGTTGTTGTCAGCAGACTTGTTTACAGAAAAGGGATC
GATTTGCTTAGTGGTATAATACCTGAACTCTGTCAGAAATATCCAGATTTAAATTTCATA
ATTGGAGGAGAGGGACCAAAGAGAATCATTTTGGAAGAAGTTCGGGAAAGATACCAGCTG
CATGACAGGGTGCGTCTTTTGGGAGCTTTAGAACACAAGGATGTTAGAAATGTCTTAGTT
CAAGGACATATTTTTCTGAATACCTCCCTTACTGAAGCATTCTGCATGGCGATCGTGGAA
GCAGCCAGTTGTGGTTTACAGGTTGTAAGTACCAGAGTTGGTGGAATTCCTGAGGTGCTT
CCAGAAAACCTTATTATTTTATGTGAGCCTTCAGTAAAATCTTTGTGTGAAGGATTGGAA
AAGGCTATTTTCCAACTGAAGTCAGGGACATTGCCAGCTCCAGAAAACATCCATAACATA
GTAAAGACTTTCTACACCTGGAGGAATGTTGCAGAAAGAACTGAAAAGGTATATGACCGG
GTATCAGTGGAAGCTGTGTTGCCAATGGACAAACGACTGGACAGACTTATTTCTCACTGC
GGCCCAGTAACAGGCTACATCTTTGCTTTGTTGGCAGTTTTCAACTTCCTCTTCCTCATT
TTCTTGAGATGGATGACTCCAGATTCTATCATTGATGTTGCAATAGATGCCACTGGGCCA
CGGGGTGCCTGGACTAATAACTATTCTCACAGTAAAAGAGGGGGTGAGAATAATGAGATA
TCTGAAACCAGGTAG
|
| Enzyme 8 GenBank Gene ID |
BC038236  |
| Enzyme 8 GeneCard ID |
PIGA  |
| Enzyme 8 GenAtlas ID |
PIGA  |
| Enzyme 8 HGNC ID |
HGNC:8957  |
| Enzyme 8 Chromosome Location |
Not Available |
| Enzyme 8 Locus |
Not Available |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Miyata T, Takeda J, Iida Y, Yamada N, Inoue N, Takahashi M, Maeda K, Kitani T, Kinoshita T: The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993 Feb 26;259(5099):1318-20. [PubMed
]
- Bessler M, Hillmen P, Longo L, Luzzatto L, Mason PJ: Genomic organization of the X-linked gene (PIG-A) that is mutated in paroxysmal nocturnal haemoglobinuria and of a related autosomal pseudogene mapped to 12q21. Hum Mol Genet. 1994 May;3(5):751-7. [PubMed
]
- Iida Y, Takeda J, Miyata T, Inoue N, Nishimura J, Kitani T, Maeda K, Kinoshita T: Characterization of genomic PIG-A gene: a gene for glycosylphosphatidylinositol-anchor biosynthesis and paroxysmal nocturnal hemoglobinuria. Blood. 1994 Jun 1;83(11):3126-31. [PubMed
]
- Yu J, Nagarajan S, Ueda E, Knez JJ, Petersen RB, Medof ME: Characterization of alternatively spliced PIG-A transcripts in normal and paroxysmal nocturnal hemoglobinuria cells. Braz J Med Biol Res. 1994 Feb;27(2):195-201. [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
]
- Takeda J, Miyata T, Kawagoe K, Iida Y, Endo Y, Fujita T, Takahashi M, Kitani T, Kinoshita T: Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993 May 21;73(4):703-11. [PubMed
]
- Murakami Y, Siripanyaphinyo U, Hong Y, Tashima Y, Maeda Y, Kinoshita T: The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol Biol Cell. 2005 Nov;16(11):5236-46. Epub 2005 Sep 14. [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
]
- Bessler M, Mason PJ, Hillmen P, Miyata T, Yamada N, Takeda J, Luzzatto L, Kinoshita T: Paroxysmal nocturnal haemoglobinuria (PNH) is caused by somatic mutations in the PIG-A gene. EMBO J. 1994 Jan 1;13(1):110-7. [PubMed
]
- Ware RE, Rosse WF, Howard TA: Mutations within the Piga gene in patients with paroxysmal nocturnal hemoglobinuria. Blood. 1994 May 1;83(9):2418-22. [PubMed
]
- Nafa K, Bessler M, Castro-Malaspina H, Jhanwar S, Luzzatto L: The spectrum of somatic mutations in the PIG-A gene in paroxysmal nocturnal hemoglobinuria includes large deletions and small duplications. Blood Cells Mol Dis. 1998 Sep;24(3):370-84. [PubMed
]
- Yoon JH, Cho HI, Park SS, Chang YH, Kim BK: Mutation analysis of the PIG-A gene in Korean patients with paroxysmal nocturnal haemoglobinuria. J Clin Pathol. 2002 Jun;55(6):410-3. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6230 |
| Enzyme 9 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit H |
| Enzyme 9 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class H protein
- PIG-H
|
| Enzyme 9 Gene Name |
PIGH |
| Enzyme 9 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCE
NSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVK
DIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAH
QKATSTSP
|
| Enzyme 9 Number of Residues |
188 |
| Enzyme 9 Molecular Weight |
21080.4 |
| Enzyme 9 Theoretical pI |
6.72 |
| Enzyme 9 GO Classification |
Not Available |
| Enzyme 9 General Function |
Involved in phosphatidylinositol N-acetylglucosaminyltr |
| Enzyme 9 Specific Function |
Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
- UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
189054281  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q14442  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PIGH_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>567 bp
ATGGAGGATGAGCGGAGCTTTTCGGATATCTGCGGCGGCCGCCTGGCGCTGCAGCGCCGC
TACTACTCCCCGTCCTGCCGGGAATTCTGCCTCAGCTGCCCTCGGCTCTCGCTGCGTTCG
CTCACCGCTGTCACCTGCACGGTGTGGCTGGCGGCCTACGGACTCTTCACCCTCTGCGAG
AACAGCATGATCCTCTCTGCTGCCATCTTCATCACCCTCTTAGGTCTGCTTGGTTATCTC
CATTTTGTGAAGATTGATCAGGAGACTCTGTTAATCATTGATTCCCTTGGCATTCAGATG
ACTTCATCTTATGCTTCAGGCAAAGAAAGCACTACCTTCATAGAAATGGGCAAGGTCAAG
GATATTGTCATCAATGAGGCCATTTACATGCAGAAGGTGATTTACTACCTCTGCATCTTA
TTGAAAGATCCAGTGGAACCACATGGGATATCCCAAGTAGTACCCGTCTTCCAGAGTGCC
AAGCCCCGGCTGGACTGCTTGATTGAAGTATACAGGAGCTGCCAGGAGATCCTGGCACAC
CAGAAAGCCACATCAACAAGCCCATGA
|
| Enzyme 9 GenBank Gene ID |
AK314108  |
| Enzyme 9 GeneCard ID |
PIGH  |
| Enzyme 9 GenAtlas ID |
PIGH  |
| Enzyme 9 HGNC ID |
HGNC:8964  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
14q24.1 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Kamitani T, Chang HM, Rollins C, Waneck GL, Yeh ET: Correction of the class H defect in glycosylphosphatidylinositol anchor biosynthesis in Ltk- cells by a human cDNA clone. J Biol Chem. 1993 Oct 5;268(28):20733-6. [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
]
- Watanabe R, Inoue N, Westfall B, Taron CH, Orlean P, Takeda J, Kinoshita T: The first step of glycosylphosphatidylinositol biosynthesis is mediated by a complex of PIG-A, PIG-H, PIG-C and GPI1. EMBO J. 1998 Feb 16;17(4):877-85. [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 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6231 |
| Enzyme 10 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit P |
| Enzyme 10 Synonyms |
- Down syndrome critical region protein 5
- Down syndrome critical region protein C
- Phosphatidylinositol-glycan biosynthesis class P protein
- PIG-P
|
| Enzyme 10 Gene Name |
PIGP |
| Enzyme 10 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
MVPRSTSLTLIVFLFHRLSKAPGKMVENSPSPLPERAIYGFVLFLSSQFGFILYLVWAFI
PESWLNSLGLTYWPQKYWAVALPVYLLIAIVIGYVLLFGINMMSTSPLDSIHTITDNYAK
NQQQKKYQEEAIPALRDISISEVNQMFFLAAKELYTKN
|
| Enzyme 10 Number of Residues |
158 |
| Enzyme 10 Molecular Weight |
18089.1 |
| Enzyme 10 Theoretical pI |
9.20 |
| Enzyme 10 GO Classification |
Not Available |
| Enzyme 10 General Function |
Involved in phosphatidylinositol N-acetylglucosaminyltr |
| Enzyme 10 Specific Function |
Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
- UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
24497597  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
P57054  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PIGP_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>477 bp
ATGGTGCCACGGAGCACATCGCTGACGCTGATTGTGTTCCTTTTCCACAGATTGTCTAAA
GCCCCAGGAAAAATGGTGGAAAATTCACCGTCGCCATTGCCAGAAAGAGCGATTTATGGC
TTTGTTCTTTTCTTAAGCTCCCAATTTGGCTTCATACTTTACCTCGTGTGGGCCTTTATT
CCTGAATCTTGGCTAAACTCTTTAGGTTTAACCTATTGGCCTCAAAAATATTGGGCAGTT
GCATTACCTGTCTACCTCCTTATTGCTATAGTAATTGGCTACGTGCTCTTGTTTGGGATT
AACATGATGAGTACCTCTCCACTCGACTCCATCCATACAATCACAGATAACTATGCAAAA
AATCAACAGCAGAAGAAATACCAAGAGGAGGCCATTCCAGCCTTAAGAGATATTTCTATT
AGTGAAGTAAACCAAATGTTCTTTCTTGCAGCCAAAGAACTTTACACCAAAAACTGA
|
| Enzyme 10 GenBank Gene ID |
NM_153681.2  |
| Enzyme 10 GeneCard ID |
PIGP  |
| Enzyme 10 GenAtlas ID |
PIGP  |
| Enzyme 10 HGNC ID |
HGNC:3046  |
| Enzyme 10 Chromosome Location |
2 |
| Enzyme 10 Locus |
21q22.2 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Shibuya K, Kudoh J, Minoshima S, Kawasaki K, Asakawa S, Shimizu N: Isolation of two novel genes, DSCR5 and DSCR6, from Down syndrome critical region on human chromosome 21q22.2. Biochem Biophys Res Commun. 2000 May 19;271(3):693-8. [PubMed
]
- Togashi T, Choi DK, Taylor TD, Suzuki Y, Sugano S, Hattori M, Sakaki Y: A novel gene, DSCR5, from the distal Down syndrome critical region on chromosome 21q22.2. DNA Res. 2000 Jun 30;7(3):207-12. [PubMed
]
- Watanabe R, Murakami Y, Marmor MD, Inoue N, Maeda Y, Hino J, Kangawa K, Julius M, Kinoshita T: Initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-P and is regulated by DPM2. EMBO J. 2000 Aug 15;19(16):4402-11. [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
]
- Goshima N, Kawamura Y, Fukumoto A, Miura A, Honma R, Satoh R, Wakamatsu A, Yamamoto J, Kimura K, Nishikawa T, Andoh T, Iida Y, Ishikawa K, Ito E, Kagawa N, Kaminaga C, Kanehori K, Kawakami B, Kenmochi K, Kimura R, Kobayashi M, Kuroita T, Kuwayama H, Maruyama Y, Matsuo K, Minami K, Mitsubori M, Mori M, Morishita R, Murase A, Nishikawa A, Nishikawa S, Okamoto T, Sakagami N, Sakamoto Y, Sasaki Y, Seki T, Sono S, Sugiyama A, Sumiya T, Takayama T, Takayama Y, Takeda H, Togashi T, Yahata K, Yamada H, Yanagisawa Y, Endo Y, Imamoto F, Kisu Y, Tanaka S, Isogai T, Imai J, Watanabe S, Nomura N: Human protein factory for converting the transcriptome into an in vitro-expressed proteome,. Nat Methods. 2008 Dec;5(12):1011-7. [PubMed
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [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
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6232 |
| Enzyme 11 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit C |
| Enzyme 11 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class C protein
- PIG-C
|
| Enzyme 11 Gene Name |
PIGC |
| Enzyme 11 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQ
QLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADL
KSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLN
MAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAV
GGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS
|
| Enzyme 11 Number of Residues |
297 |
| Enzyme 11 Molecular Weight |
33582.2 |
| Enzyme 11 Theoretical pI |
8.55 |
| Enzyme 11 GO Classification |
| Function |
- UDP-glycosyltransferase activity
- acetylglucosaminyltransferase activity
- catalytic activity
- phosphatidylinositol N-acetylglucosaminyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 11 General Function |
Involved in phosphatidylinositol N-acetylglucosaminyltransferase activity |
| Enzyme 11 Specific Function |
Part of the complex catalyzing the transfer of N- acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
- UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol [RN:R02654 R05916]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
- 51-71
80-100
154-174
239-259
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
2547042  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q92535  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PIGC_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>894 bp
ATGTATGCTCAACCTGTGACTAACACCAAGGAGGTCAAGTGGCAGAAGGTCTTGTATGAG
CGACAGCCCTTTCCTGATAACTATGTGGACCGGCGATTCCTGGAAGAGCTCCGGAAAAAC
ATCCATGCTCGGAAATACCAATATTGGGCTGTGGTATTTGAGTCCAGTGTGGTGATCCAG
CAGCTGTGCAGTGTTTGTGTTTTTGTGGTTATCTGGTGGTATATGGATGAGGGTCTTCTG
GCCCCCCATTGGCTTTTAGGGACTGGCCTGGCTTCTTCACTGATTGGGTATGTTTTGTTT
GATCTCATTGATGGAGGTGAAGGGCGGAAGAAGAGTGGGCAGACCCGGTGGGCTGACCTG
AAGAGTGCCCTAGTCTTCATTACTTTCACTTATGGGTTTTCACCAGTGCTGAAGACCCTT
ACAGAGTCTGTCAGCACTGACACCATCTATGCCATGTCAGTCTTCATGCTGTTAGGCCAT
CTCATCTTTTTTGACTATGGTGCCAATGCTGCCATTGTATCCAGCACACTATCCTTGAAC
ATGGCCATCTTTGCTTCTGTATGCTTGGCATCACGTCTTCCCCGGTCCCTGCATGCCTTC
ATCATGGTGACATTTGCCATTCAGATTTTTGCCCTGTGGCCCATGTTGCAGAAGAAACTA
AAGGCATGTACTCCCCGGAGCTATGTGGGGGTCACACTGCTTTTTGCATTTTCAGCCGTG
GGAGGCCTACTGTCCATTAGTGCTGTGGGAGCCGTACTCTTTGCCCTTCTGCTGATGTCT
ATCTCATGTCTGTGTTCATTCTACCTCATTCGCTTGCAGCTTTTTAAAGAAAACATTCAT
GGGCCTTGGGATGAAGCTGAAATCAAGGAAGACTTGTCCAGGTTCCTCAGTTAA
|
| Enzyme 11 GenBank Gene ID |
AB000360  |
| Enzyme 11 GeneCard ID |
PIGC  |
| Enzyme 11 GenAtlas ID |
PIGC  |
| Enzyme 11 HGNC ID |
HGNC:8960  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
1q23-q25 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Inoue N, Watanabe R, Takeda J, Kinoshita T: PIG-C, one of the three human genes involved in the first step of glycosylphosphatidylinositol biosynthesis is a homologue of Saccharomyces cerevisiae GPI2. Biochem Biophys Res Commun. 1996 Sep 4;226(1):193-9. [PubMed
]
- Hong Y, Ohishi K, Inoue N, Endo Y, Fujita T, Takeda J, Kinoshita T: Structures and chromosomal localizations of the glycosylphosphatidylinositol synthesis gene PIGC and its pseudogene PIGCP1. Genomics. 1997 Sep 15;44(3):347-9. [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 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
6378 |
| Enzyme 12 Name |
Ectonucleotide pyrophosphatase/phosphodiesterase family member 7 |
| Enzyme 12 Synonyms |
- E-NPP 7
- NPP-7
- Alkaline sphingomyelin phosphodiesterase
- Intestinal alkaline sphingomyelinase
- Alk-SMase
|
| Enzyme 12 Gene Name |
ENPP7 |
| Enzyme 12 Protein Sequence |
>Ectonucleotide pyrophosphatase/phosphodiesterase family member 7
MRGLAVLLTVALATLLAPGAGAPVQSQGSQNKLLLVSFDGFRWNYDQDVDTPNLDAMARD
GVKARYMTPAFVTMTSPCHFTLVTGKYIENHGVVHNMYYNTTSKVKLPYHATLGIQRWWD
NGSVPIWITAQRQGLRAGSFFYPGGNVTYQGVAVTRSRKEGIAHNYKNETEWRANIDTVM
AWFTEEDLDLVTLYFGEPDSTGHRYGPESPERREMVRQVDRTVGYLRESIARNHLTDRLN
LIITSDHGMTTVDKRAGDLVEFHKFPNFTFRDIEFELLDYGPNGMLLPKEGRLEKVYDAL
KDAHPKLHVYKKEAFPEAFHYANNPRVTPLLMYSDLGYVIHGRINVQFNNGEHGFDNKDM
DMKTIFRAVGPSFRAGLEVEPFESVHVYELMCRLLGIVPEANDGHLATLLPMLHTESALP
PDGRPTLLPKGRSALPPSSRPLLVMGLLGTVILLSEVA
|
| Enzyme 12 Number of Residues |
458 |
| Enzyme 12 Molecular Weight |
51493.4 |
| Enzyme 12 Theoretical pI |
6.88 |
| Enzyme 12 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in catalytic activity |
| Enzyme 12 Specific Function |
Converts sphingomyelin to ceramide. Also has phospholipase C activity toward palmitoyl lyso-phosphocholine. Does not appear to have nucleotide pyrophosphatase activity |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
45545421  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q6UWV6  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
ENPP7_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1377 bp
ATGAGAGGCCTGGCCGTCCTCCTCACTGTGGCTCTGGCCACGCTCCTGGCTCCCGGGGCC
GGAGCACCGGTACAAAGTCAGGGCTCCCAGAACAAGCTGCTCCTGGTGTCCTTCGACGGC
TTCCGCTGGAACTACGACCAGGATGTGGACACCCCCAACCTGGACGCCATGGCCCGAGAC
GGGGTGAAGGCACGCTACATGACCCCCGCCTTTGTCACCATGACCAGCCCCTGCCACTTC
ACCCTGGTCACCGGCAAATATATCGAGAACCACGGGGTGGTTCACAACATGTACTACAAC
ACCACCAGCAAGGTGAAGCTGCCCTACCACGCCACGCTGGGCATCCAGAGGTGGTGGGAC
AACGGCAGCGTGCCCATCTGGATCACAGCCCAGAGGCAGGGCCTGAGGGCTGGCTCCTTC
TTCTACCCGGGCGGGAACGTCACCTACCAAGGGGTGGCTGTGACGCGGAGCCGGAAAGAA
GGCATCGCACACAACTACAAAAATGAGACGGAGTGGAGAGCGAACATCGACACAGTGATG
GCGTGGTTCACAGAGGAGGACCTGGATCTGGTCACACTCTACTTCGGGGAGCCGGACTCC
ACGGGCCACAGGTACGGCCCCGAGTCCCCGGAGAGGAGGGAGATGGTGCGGCAGGTGGAC
CGGACCGTGGGCTACCTCCGGGAGAGCATCGCGCGCAACCACCTCACAGACCGCCTCAAC
CTGATCATCACATCCGACCACGGCATGACGACCGTGGACAAACGGGCTGGCGACCTGGTT
GAATTCCACAAGTTCCCCAACTTCACCTTCCGGGACATCGAGTTTGAGCTCCTGGACTAC
GGACCAAACGGGATGCTGCTCCCTAAAGAAGGGAGGCTGGAGAAGGTGTACGATGCCCTC
AAGGACGCCCACCCCAAGCTCCACGTCTACAAGAAGGAGGCGTTCCCCGAGGCCTTCCAC
TACGCCAACAACCCCAGGGTCACACCCCTGCTGATGTACAGCGACCTTGGCTACGTCATC
CATGGGAGAATTAACGTCCAGTTCAACAATGGGGAGCACGGCTTTGACAACAAGGACATG
GACATGAAGACCATCTTCCGCGCTGTGGGCCCTAGCTTCAGGGCGGGCCTGGAGGTGGAG
CCCTTTGAGAGCGTCCACGTGTACGAGCTCATGTGCCGGCTGCTGGGCATCGTGCCCGAG
GCCAACGATGGGCACCTAGCTACTCTGCTGCCCATGCTGCACACAGAATCTGCTCTTCCG
CCTGATGGAAGGCCTACTCTCCTGCCCAAGGGAAGATCTGCTCTCCCGCCCAGCAGCAGG
CCCCTCCTCGTGATGGGACTGCTGGGGACCGTGATTCTTCTGTCTGAGGTCGCATAA
|
| Enzyme 12 GenBank Gene ID |
NM_178543.3  |
| Enzyme 12 GeneCard ID |
ENPP7  |
| Enzyme 12 GenAtlas ID |
ENPP7  |
| Enzyme 12 HGNC ID |
HGNC:23764  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
17q25.3 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Duan RD, Bergman T, Xu N, Wu J, Cheng Y, Duan J, Nelander S, Palmberg C, Nilsson A: Identification of human intestinal alkaline sphingomyelinase as a novel ecto-enzyme related to the nucleotide phosphodiesterase family. J Biol Chem. 2003 Oct 3;278(40):38528-36. Epub 2003 Jul 28. [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
]
- 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
]
- Duan RD, Cheng Y, Hansen G, Hertervig E, Liu JJ, Syk I, Sjostrom H, Nilsson A: Purification, localization, and expression of human intestinal alkaline sphingomyelinase. J Lipid Res. 2003 Jun;44(6):1241-50. Epub 2003 Apr 1. [PubMed
]
- Wu J, Cheng Y, Nilsson A, Duan RD: Identification of one exon deletion of intestinal alkaline sphingomyelinase in colon cancer HT-29 cells and a differentiation-related expression of the wild-type enzyme in Caco-2 cells. Carcinogenesis. 2004 Aug;25(8):1327-33. Epub 2004 Mar 11. [PubMed
]
- Wu J, Hansen GH, Nilsson A, Duan RD: Functional studies of human intestinal alkaline sphingomyelinase by deglycosylation and mutagenesis. Biochem J. 2005 Feb 15;386(Pt 1):153-60. [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 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
6379 |
| Enzyme 13 Name |
Sphingomyelin phosphodiesterase 2 |
| Enzyme 13 Synonyms |
- Lyso-platelet-activating factor-phospholipase C
- Lyso-PAF-PLC
- Neutral sphingomyelinase
- N-SMase
- nSMase
|
| Enzyme 13 Gene Name |
SMPD2 |
| Enzyme 13 Protein Sequence |
>Sphingomyelin phosphodiesterase 2
MKPNFSLRLRIFNLNCWGIPYLSKHRADRMRRLGDFLNQESFDLALLEEVWSEQDFQYLR
QKLSPTYPAAHHFRSGIIGSGLCVFSKHPIQELTQHIYTLNGYPYMIHHGDWFSGKAVGL
LVLHLSGMVLNAYVTHLHAEYNRQKDIYLAHRVAQAWELAQFIHHTSKKADVVLLCGDLN
MHPEDLGCCLLKEWTGLHDAYLETRDFKGSEEGNTMVPKNCYVSQQELKPFPFGVRIDYV
LYKAVSGFYISCKSFETTTGFDPHRGTPLSDHEALMATLFVRHSPPQQNPSSTHGPAERS
PLMCVLKEAWTELGLGMAQARWWATFASYVIGLGLLLLALLCVLAAGGGAGEAAILLWTP
SVGLVLWAGAFYLFHVQEVNGLYRAQAELQHVLGRAREAQDLGPEPQPALLLGQQEGDRT
KEQ
|
| Enzyme 13 Number of Residues |
423 |
| Enzyme 13 Molecular Weight |
47645.3 |
| Enzyme 13 Theoretical pI |
6.98 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Involved in metal ion binding |
| Enzyme 13 Specific Function |
Converts sphingomyelin to ceramide. Hydrolyze 1-acyl-2- lyso-sn-glycero-3-phosphocholine (lyso-PC) and 1-O-alkyl-2-lyso- sn-glycero-3-phosphocholine (lyso-platelet-activating factor). The physiological substrate seems to be Lyso-PAF |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
3021428  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
O60906  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
NSMA_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1272 bp
ATGAAGCTCAACTTCTCCCTGCGACTGCGGATCTTCAACCTCAACTGCTGGGGCATTCCG
TACTTGAGCAAGCACCGGGCCGACCGCATGAGGCGCCTGGGAGACTTTCTGAACCAGGAG
AGCTTCGACCTGGCTTTGCTGGAGGAGGTGTGGAGTGAGCAGGACTTCCAGTACCTGAGA
CAGAAGCTGTCACCTACCTACCCAGCTGCACACCACTTCCGGAGCGGAATCATTGGCAGT
GGCCTCTGTGTCTTCTCCAAACATCCAATCCAGGAGCTTACCCAGCACATCTACACTCTC
AATGGCTACCCCTACATGATCCATCATGGTGACTGGTTCAGTGGGAAGGCTGTGGGGCTG
CTGGTGCTCCATCTAAGTGGCATGGTGCTCAACGCCTATGTGACCCATCTCCATGCCGAA
TACAATCGACAGAAGGACATCTACCTAGCACATCGTGTGGCCCAAGCTTGGGAATTGGCC
CAGTTCATCCACCACACATCCAAGAAGGCAGACGTGGTTCTGTTGTGTGGAGACCTCAAC
ATGCACCCAGAAGACCTGGGCTGCTGCCTGCTGAAGGAGTGGACAGGGCTTCATGATGCC
TATCTTGAAACTCGGGACTTCAAGGGCTCTGAGGAAGGCAACACAATGGTACCCAAGAAC
TGCTACGTCAGCCAGCAGGAGCTGAAGCCATTTCCCTTTGGTGTCCGCATTGACTACGTG
CTTTACAAGGCAGTTTCTGGGTTTTACATCTCCTGTAAGAGTTTTGAAACCACTACAGGC
TTTGACCCTCACAGTGGCACCCCCCTCTCTGATCATGAAGCCCTGATGGCTACTCTGTTT
GTGAGGCACAGCCCCCCACAGCAGAACCCCAGCTCTACCCACGGACCAGCAGAGAGGTCG
CCGTTGATGTGTGTGCTAAAGGAGGCCTGGACGGAGCTGGGTCTGGGCATGGCTCAGGCT
CGCTGGTGGGCCACCTTCGCTAGCTATGTGATTGGCCTGGGGCTGCTTCTCCTGGCACTG
CTGTGTGTCCTGGCGGCTGGAGGAGGGGCCGGGGAAGCTGCCATACTGCTCTGGACCCCC
AGTGTAGGGCTGGTGCTGTGGGCAGGTGCATTCTACCTCTTCCACGTACAGGAGGTCAAT
GGCTTATATAGGGCCCAGGCTGAGCTCCAGCATGTGCTAGGAAGGGCAAGGGAGGCCCAG
GATCTGGGCCCAGAGCCTCAGCCAGCCCTACTCCTGGGGCAGCAGGAGGGGGACAGAACT
AAAGAACAATAA
|
| Enzyme 13 GenBank Gene ID |
AJ222801  |
| Enzyme 13 GeneCard ID |
SMPD2  |
| Enzyme 13 GenAtlas ID |
SMPD2  |
| Enzyme 13 HGNC ID |
HGNC:11121  |
| Enzyme 13 Chromosome Location |
6 |
| Enzyme 13 Locus |
6q21 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Tomiuk S, Hofmann K, Nix M, Zumbansen M, Stoffel W: Cloned mammalian neutral sphingomyelinase: functions in sphingolipid signaling? Proc Natl Acad Sci U S A. 1998 Mar 31;95(7):3638-43. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Sawai H, Domae N, Nagan N, Hannun YA: Function of the cloned putative neutral sphingomyelinase as lyso-platelet activating factor-phospholipase C. J Biol Chem. 1999 Dec 31;274(53):38131-9. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
7010 |
| Enzyme 14 Name |
Proactivator polypeptide |
| Enzyme 14 Synonyms |
- Saposin-A
- Protein A
- Saposin-B-Val
- Saposin-B
- Cerebroside sulfate activator
- CSAct
- Dispersin
- Sphingolipid activator protein 1
- SAP-1
- Sulfatide/GM1 activator
- Saposin-C
- A1 activator
- Co-beta-glucosidase
- Glucosylceramidase activator
- Sphingolipid activator protein 2
- SAP-2
- Saposin-D
- Component C
- Protein C
|
| Enzyme 14 Gene Name |
PSAP |
| Enzyme 14 Protein Sequence |
>Proactivator polypeptide
MYALFLLASLLGAALAGPVLGLKECTRGSAVWCQNVKTASDCGAVKHCLQTVWNKPTVKS
LPCDICKDVVTAAGDMLKDNATEEEILVYLEKTCDWLPKPNMSASCKEIVDSYLPVILDI
IKGEMSRPGEVCSALNLCESLQKHLAELNHQKQLESNKIPELDMTEVVAPFMANIPLLLY
PQDGPRSKPQPKDNGDVCQDCIQMVTDIQTAVRTNSTFVQALVEHVKEECDRLGPGMADI
CKNYISQYSEIAIQMMMHMQPKEICALVGFCDEVKEMPMQTLVPAKVASKNVIPALELVE
PIKKHEVPAKSDVYCEVCEFLVKEVTKLIDNNKTEKEILDAFDKMCSKLPKSLSEECQEV
VDTYGSSILSILLEEVSPELVCSMLHLCSGTRLPALTVHVTQPKDGGFCEVCKKLVGYLD
RNLEKNSTKQEILAALEKGCSFLPDPYQKQCDQFVAEYEPVLIEILVEVMDPSFVCLKIG
ACPSAHKPLLGTEKCIWGPSYWCQNTETAAQCNAVEHCKRHVWN
|
| Enzyme 14 Number of Residues |
524 |
| Enzyme 14 Molecular Weight |
58112.1 |
| Enzyme 14 Theoretical pI |
4.82 |
| Enzyme 14 GO Classification |
| Function |
| — |
| Process |
- cellular lipid metabolic process
- lipid metabolic process
- membrane lipid metabolic process
- metabolic process
- primary metabolic process
- sphingolipid metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- lysosome
- lytic vacuole
- membrane-bounded organelle
- organelle
- vacuole
|
|
| Enzyme 14 General Function |
Involved in lipid metabolic process |
| Enzyme 14 Specific Function |
Saposin-D is a specific sphingomyelin phosphodiesterase activator (EC 3.1.4.12) |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
16306656  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P07602  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
SAP_HUMAN  |
| Enzyme 14 PDB ID |
1N69  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1575 bp
ATGTACGCCCTCTTCCTCCTGGCCAGCCTCCTGGGCGCGGCTCTAGCCGGCCCGGTCCTT
GGACTGAAAGAATGCACCAGGGGCTCGGCAGTGTGGTGCCAGAATGTGAAGACGGCGTCC
GACTGCGGGGCAGTGAAGCACTGCCTGCAGACCGTTTGGAACAAGCCAACAGTGAAATCC
CTTCCCTGCGACATATGCAAAGACGTTGTCACCGCAGCTGGTGATATGCTGAAGGACAAT
GCCACTGAGGAGGAGATCCTTGTTTACTTGGAGAAGACCTGTGACTGGCTTCCGAAACCG
AACATGTCTGCTTCATGCAAGGAGATAGTGGACTCCTACCTCCCTGTCATCCTGGACATC
ATTAAAGGAGAAATGAGCCGTCCTGGGGAGGTGTGCTCTGCTCTCAACCTCTGCGAGTCT
CTCCAGAAGCACCTAGCAGAGCTGAATCACCAGAAGCAGCTGGAGTCCAATAAGATCCCA
GAGCTGGACATGACTGAGGTGGTGGCCCCCTTCATGGCCAACATCCCTCTCCTCCTCTAC
CCTCAGGACGGCCCCCGCAGCAAGCCCCAGCCAAAGGATAATGGGGACGTTTGCCAGGAC
TGCATTCAGATGGTGACTGACATCCAGACTGCTGTACGGACCAACTCCACCTTTGTCCAG
GCCTTGGTGGAACATGTCAAGGAGGAGTGTGACCGCCTGGGCCCTGGCATGGCCGACATA
TGCAAGAACTATATCAGCCAGTATTCTGAAATTGCTATCCAGATGATGATGCACATGCAA
CCCAAGGAGATCTGTGCGCTGGTTGGGTTCTGTGATGAGGTGAAAGAGATGCCCATGCAG
ACTCTGGTCCCCGCCAAAGTGGCCTCCAAGAATGTCATCCCTGCCCTGGAACTGGTGGAG
CCCATTAAGAAGCACGAGGTCCCAGCAAAGTCTGATGTTTACTGTGAGGTGTGTGAATTC
CTGGTGAAGGAGGTGACCAAGCTGATTGACAACAACAAGACTGAGAAAGAAATACTCGAC
GCTTTTGACAAAATGTGCTCGAAGCTGCCGAAGTCCCTGTCGGAAGAGTGCCAGGAGGTG
GTGGACACGTACGGCAGCTCCATCCTGTCCATCCTGCTGGAGGAGGTCAGCCCTGAGCTG
GTGTGCAGCATGCTGCACCTCTGCTCTGGCACGCGGCTGCCTGCACTGACCGTTCACGTG
ACTCAGCCAAAGGACGGTGGCTTCTGCGAAGTGTGCAAGAAGCTGGTGGGTTATTTGGAT
CGCAACCTGGAGAAAAACAGCACCAAGCAGGAGATCCTGGCTGCTCTTGAGAAAGGCTGC
AGCTTCCTGCCAGACCCTTACCAGAAGCAGTGTGATCAGTTTGTGGCAGAGTACGAGCCC
GTGCTGATCGAGATCCTGGTGGAGGTGATGGATCCTTCCTTCGTGTGCTTGAAAATTGGA
GCCTGCCCCTCGGCCCATAAGCCCTTGTTGGGAACTGAGAAGTGTATATGGGGCCCAAGC
TACTGGTGCCAGAACACAGAGACAGCAGCCCAGTGCAATGCTGTCGAGCATTGCAAACGC
CATGTGTGGAACTAG
|
| Enzyme 14 GenBank Gene ID |
BC001503  |
| Enzyme 14 GeneCard ID |
PSAP  |
| Enzyme 14 GenAtlas ID |
PSAP  |
| Enzyme 14 HGNC ID |
HGNC:9498  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
10q21-q22 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Rorman EG, Grabowski GA: Molecular cloning of a human co-beta-glucosidase cDNA: evidence that four sphingolipid hydrolase activator proteins are encoded by single genes in humans and rats. Genomics. 1989 Oct;5(3):486-92. [PubMed
]
- Nakano T, Sandhoff K, Stumper J, Christomanou H, Suzuki K: Structure of full-length cDNA coding for sulfatide activator, a Co-beta-glucosidase and two other homologous proteins: two alternate forms of the sulfatide activator. J Biochem (Tokyo). 1989 Feb;105(2):152-4. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- O'Brien JS, Kretz KA, Dewji N, Wenger DA, Esch F, Fluharty AL: Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus. Science. 1988 Aug 26;241(4869):1098-101. [PubMed
]
- Rorman EG, Scheinker V, Grabowski GA: Structure and evolution of the human prosaposin chromosomal gene. Genomics. 1992 Jun;13(2):312-8. [PubMed
]
- Hiraiwa M, O'Brien JS, Kishimoto Y, Galdzicka M, Fluharty AL, Ginns EI, Martin BM: Isolation, characterization, and proteolysis of human prosaposin, the precursor of saposins (sphingolipid activator proteins). Arch Biochem Biophys. 1993 Jul;304(1):110-6. [PubMed
]
- Kondoh K, Hineno T, Sano A, Kakimoto Y: Isolation and characterization of prosaposin from human milk. Biochem Biophys Res Commun. 1991 Nov 27;181(1):286-92. [PubMed
]
- Holtschmidt H, Sandhoff K, Furst W, Kwon HY, Schnabel D, Suzuki K: The organization of the gene for the human cerebroside sulfate activator protein. FEBS Lett. 1991 Mar 25;280(2):267-70. [PubMed
]
- Morimoto S, Martin BM, Yamamoto Y, Kretz KA, O'Brien JS, Kishimoto Y: Saposin A: second cerebrosidase activator protein. Proc Natl Acad Sci U S A. 1989 May;86(9):3389-93. [PubMed
]
- Tyynela J, Palmer DN, Baumann M, Haltia M: Storage of saposins A and D in infantile neuronal ceroid-lipofuscinosis. FEBS Lett. 1993 Sep 6;330(1):8-12. [PubMed
]
- Dewji NN, Wenger DA, O'Brien JS: Nucleotide sequence of cloned cDNA for human sphingolipid activator protein 1 precursor. Proc Natl Acad Sci U S A. 1987 Dec;84(23):8652-6. [PubMed
]
- Dewji N, Wenger D, Fujibayashi S, Donoviel M, Esch F, Hill F, O'Brien JS: Molecular cloning of the sphingolipid activator protein-1 (SAP-1), the sulfatide sulfatase activator. Biochem Biophys Res Commun. 1986 Jan 29;134(2):989-94. [PubMed
]
- Kleinschmidt T, Christomanou H, Braunitzer G: Complete amino-acid sequence of the naturally occurring A2 activator protein for enzymic sphingomyelin degradation: identity to the sulfatide activator protein (SAP-1). Biol Chem Hoppe Seyler. 1988 Dec;369(12):1361-5. [PubMed
]
- Furst W, Schubert J, Machleidt W, Meyer HE, Sandhoff K: The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein. Eur J Biochem. 1990 Sep 24;192(3):709-14. [PubMed
]
- Kleinschmidt T, Christomanou H, Braunitzer G: Complete amino-acid sequence and carbohydrate content of the naturally occurring glucosylceramide activator protein (A1 activator) absent from a new human Gaucher disease variant. Biol Chem Hoppe Seyler. 1987 Dec;368(12):1571-8. [PubMed
]
- Morimoto S, Martin BM, Kishimoto Y, O'Brien JS: Saposin D: a sphingomyelinase activator. Biochem Biophys Res Commun. 1988 Oct 14;156(1):403-10. [PubMed
]
- Furst W, Machleidt W, Sandhoff K: The precursor of sulfatide activator protein is processed to three different proteins. Biol Chem Hoppe Seyler. 1988 May;369(5):317-28. [PubMed
]
- Fluharty AL, Lombardo C, Louis A, Stevens RL, Whitelegge J, Waring AJ, To T, Fluharty CB, Faull KF: Preparation of the cerebroside sulfate activator (CSAct or saposin B) from human urine. Mol Genet Metab. 1999 Nov;68(3):391-403. [PubMed
]
- Vaccaro AM, Salvioli R, Barca A, Tatti M, Ciaffoni F, Maras B, Siciliano R, Zappacosta F, Amoresano A, Pucci P: Structural analysis of saposin C and B. Complete localization of disulfide bridges. J Biol Chem. 1995 Apr 28;270(17):9953-60. [PubMed
]
- Faull KF, Johnson J, Kim MJ, To T, Whitelegge JP, Stevens RL, Fluharty CB, Fluharty AL: Structure of the asparagine-linked sugar chains of porcine kidney and human urine cerebroside sulfate activator protein. J Mass Spectrom. 2000 Dec;35(12):1416-24. [PubMed
]
- Tatti M, Salvioli R, Ciaffoni F, Pucci P, Andolfo A, Amoresano A, Vaccaro AM: Structural and membrane-binding properties of saposin D. Eur J Biochem. 1999 Jul;263(2):486-94. [PubMed
]
- Ahn VE, Faull KF, Whitelegge JP, Higginson J, Fluharty AL, Prive GG: Expression, purification, crystallization, and preliminary X-ray analysis of recombinant human saposin B. Protein Expr Purif. 2003 Jan;27(1):186-93. [PubMed
]
- Faull KF, Whitelegge JP, Higginson J, To T, Johnson J, Krutchinsky AN, Standing KG, Waring AJ, Stevens RL, Fluharty CB, Fluharty AL: Cerebroside sulfate activator protein (Saposin B): chromatographic and electrospray mass spectrometric properties. J Mass Spectrom. 1999 Oct;34(10):1040-54. [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
]
- Ahn VE, Faull KF, Whitelegge JP, Fluharty AL, Prive GG: Crystal structure of saposin B reveals a dimeric shell for lipid binding. Proc Natl Acad Sci U S A. 2003 Jan 7;100(1):38-43. Epub 2002 Dec 23. [PubMed
]
- Gieselmann V, Zlotogora J, Harris A, Wenger DA, Morris CP: Molecular genetics of metachromatic leukodystrophy. Hum Mutat. 1994;4(4):233-42. [PubMed
]
- Rafi MA, Zhang XL, DeGala G, Wenger DA: Detection of a point mutation in sphingolipid activator protein-1 mRNA in patients with a variant form of metachromatic leukodystrophy. Biochem Biophys Res Commun. 1990 Jan 30;166(2):1017-23. [PubMed
]
- Kretz KA, Carson GS, Morimoto S, Kishimoto Y, Fluharty AL, O'Brien JS: Characterization of a mutation in a family with saposin B deficiency: a glycosylation site defect. Proc Natl Acad Sci U S A. 1990 Apr;87(7):2541-4. [PubMed
]
- Holtschmidt H, Sandhoff K, Kwon HY, Harzer K, Nakano T, Suzuki K: Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease. J Biol Chem. 1991 Apr 25;266(12):7556-60. [PubMed
]
- Schnabel D, Schroder M, Furst W, Klein A, Hurwitz R, Zenk T, Weber J, Harzer K, Paton BC, Poulos A, et al.: Simultaneous deficiency of sphingolipid activator proteins 1 and 2 is caused by a mutation in the initiation codon of their common gene. J Biol Chem. 1992 Feb 15;267(5):3312-5. [PubMed
]
- Schnabel D, Schroder M, Sandhoff K: Mutation in the sphingolipid activator protein 2 in a patient with a variant of Gaucher disease. FEBS Lett. 1991 Jun 17;284(1):57-9. [PubMed
]
- Regis S, Filocamo M, Corsolini F, Caroli F, Keulemans JL, van Diggelen OP, Gatti R: An Asn > Lys substitution in saposin B involving a conserved amino acidic residue and leading to the loss of the single N-glycosylation site in a patient with metachromatic leukodystrophy and normal arylsulphatase A activity. Eur J Hum Genet. 1999 Feb-Mar;7(2):125-30. [PubMed
]
- Wrobe D, Henseler M, Huettler S, Pascual Pascual SI, Chabas A, Sandhoff K: A non-glycosylated and functionally deficient mutant (N215H) of the sphingolipid activator protein B (SAP-B) in a novel case of metachromatic leukodystrophy (MLD). J Inherit Metab Dis. 2000 Feb;23(1):63-76. [PubMed
]
- Hulkova H, Cervenkova M, Ledvinova J, Tochackova M, Hrebicek M, Poupetova H, Befekadu A, Berna L, Paton BC, Harzer K, Boor A, Smid F, Elleder M: A novel mutation in the coding region of the prosaposin gene leads to a complete deficiency of prosaposin and saposins, and is associated with a complex sphingolipidosis dominated by lactosylceramide accumulation. Hum Mol Genet. 2001 Apr 15;10(9):927-40. [PubMed
]
- Spiegel R, Bach G, Sury V, Mengistu G, Meidan B, Shalev S, Shneor Y, Mandel H, Zeigler M: A mutation in the saposin A coding region of the prosaposin gene in an infant presenting as Krabbe disease: first report of saposin A deficiency in humans. Mol Genet Metab. 2005 Feb;84(2):160-6. [PubMed
]
- Tylki-Szymanska A, Czartoryska B, Vanier MT, Poorthuis BJ, Groener JA, Lugowska A, Millat G, Vaccaro AM, Jurkiewicz E: Non-neuronopathic Gaucher disease due to saposin C deficiency. Clin Genet. 2007 Dec;72(6):538-42. Epub 2007 Oct 7. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
7061 |
| Enzyme 15 Name |
Ganglioside GM2 activator |
| Enzyme 15 Synonyms |
- Cerebroside sulfate activator protein
- GM2-AP
- Shingolipid activator protein 3
- SAP-3
- Ganglioside GM2 activator isoform short
|
| Enzyme 15 Gene Name |
GM2A |
| Enzyme 15 Protein Sequence |
>Ganglioside GM2 activator
MQSLMQAPLLIALGLLLAAPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIIV
PGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIP
TGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKR
LGCIKIAASLKGI
|
| Enzyme 15 Number of Residues |
193 |
| Enzyme 15 Molecular Weight |
20838.1 |
| Enzyme 15 Theoretical pI |
4.96 |
| Enzyme 15 GO Classification |
Not Available |
| Enzyme 15 General Function |
Involved in sphingolipid activator protein activity |
| Enzyme 15 Specific Function |
Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3 |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
Not Available |
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
4587479  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P17900  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
SAP3_HUMAN  |
| Enzyme 15 PDB ID |
1PUB  |
| Enzyme 15 PDB File |
Show |
| Enzyme 15 3D Structure |
|
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>582 bp
ATGCAGTCCCTGATGCAGGCTCCCCTCCTGATCGCCCTGGGCTTGCTTCTCGCGACCCCT
GCGCAAGCCCACCTGAAAAAGCCATCCCAGCTCAGTAGCTTTTCCTGGGATAACTGTGAT
GAAGGGAAGGACCCTGCGGTGATCAGAAGCCTGACTCTGGAGCCTGACCCCATCGTCGTT
CCTGGAAATGTGACCCTCAGTGTCGTGGGCAGCACCAGTGTCCCCCTGAGTTCTCCTCTG
AAGGTGGATTTAGTTTTGGAGAAGGAGGTGGCTGGCCTCTGGATCAAGATCCCATGCACA
GACTACATTGGCAGCTGTACCTTTGAACACTTCTGTGATGTGCTTGACATGTTAATTCCT
ACTGGGGAGCCCTGCCCAGAGCCCCTGCGTACCTATGGGCTTCCTTGCCACTGTCCCTTC
AAAGAAGGAACCTACTCACTGCCCAAGAGCGAATTCGTTGTGCCTGACCTGGAGCTGCCC
AGTTGGCTCACCACCGGGAACTACCGCATAGAGAGCGTCCTGAGCAGCAGTGGGAAGCGT
CTGGGCTGCATCAAGATCGCTGCCTCTCTAAAGGGCATATAG
|
| Enzyme 15 GenBank Gene ID |
AF124719  |
| Enzyme 15 GeneCard ID |
GM2A  |
| Enzyme 15 GenAtlas ID |
GM2A  |
| Enzyme 15 HGNC ID |
HGNC:4367  |
| Enzyme 15 Chromosome Location |
5 |
| Enzyme 15 Locus |
5q33.1 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Xie B, McInnes B, Neote K, Lamhonwah AM, Mahuran D: Isolation and expression of a full-length cDNA encoding the human GM2 activator protein. Biochem Biophys Res Commun. 1991 Jun 28;177(3):1217-23. [PubMed
]
- Klima H, Tanaka A, Schnabel D, Nakano T, Schroder M, Suzuki K, Sandhoff K: Characterization of full-length cDNAs and the gene coding for the human GM2 activator protein. FEBS Lett. 1991 Sep 9;289(2):260-4. [PubMed
]
- Nagarajan S, Chen HC, Li SC, Li YT, Lockyer JM: Evidence for two cDNA clones encoding human GM2-activator protein. Biochem J. 1992 Mar 15;282 ( Pt 3):807-13. [PubMed
]
- Xie B, Kennedy JL, McInnes B, Auger D, Mahuran D: Identification of a processed pseudogene related to the functional gene encoding the GM2 activator protein: localization of the pseudogene to human chromosome 3 and the functional gene to human chromosome 5. Genomics. 1992 Nov;14(3):796-8. [PubMed
]
- Chen B, Rigat B, Curry C, Mahuran DJ: Structure of the GM2A gene: identification of an exon 2 nonsense mutation and a naturally occurring transcript with an in-frame deletion of exon 2. Am J Hum Genet. 1999 Jul;65(1):77-87. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Schroder M, Klima H, Nakano T, Kwon H, Quintern LE, Gartner S, Suzuki K, Sandhoff K: Isolation of a cDNA encoding the human GM2 activator protein. FEBS Lett. 1989 Jul 17;251(1-2):197-200. [PubMed
]
- Furst W, Schubert J, Machleidt W, Meyer HE, Sandhoff K: The complete amino-acid sequences of human ganglioside GM2 activator protein and cerebroside sulfate activator protein. Eur J Biochem. 1990 Sep 24;192(3):709-14. [PubMed
]
- Wright CS, Li SC, Rastinejad F: Crystal structure of human GM2-activator protein with a novel beta-cup topology. J Mol Biol. 2000 Dec 1;304(3):411-22. [PubMed
]
- Schroder M, Schnabel D, Suzuki K, Sandhoff K: A mutation in the gene of a glycolipid-binding protein (GM2 activator) that causes GM2-gangliosidosis variant AB. FEBS Lett. 1991 Sep 23;290(1-2):1-3. [PubMed
]
- Schroder M, Schnabel D, Hurwitz R, Young E, Suzuki K, Sandhoff K: Molecular genetics of GM2-gangliosidosis AB variant: a novel mutation and expression in BHK cells. Hum Genet. 1993 Nov;92(5):437-40. [PubMed
]
- Schepers U, Glombitza G, Lemm T, Hoffmann A, Chabas A, Ozand P, Sandhoff K: Molecular analysis of a GM2-activator deficiency in two patients with GM2-gangliosidosis AB variant. Am J Hum Genet. 1996 Nov;59(5):1048-56. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
7905 |
| Enzyme 16 Name |
T-cell surface glycoprotein CD1e, membrane-associated |
| Enzyme 16 Synonyms |
- hCD1e
- R2G1
- CD1e antigen
- T-cell surface glycoprotein CD1e, soluble
- sCD1e
|
| Enzyme 16 Gene Name |
CD1E |
| Enzyme 16 Protein Sequence |
>T-cell surface glycoprotein CD1e, membrane-associated
MLLLFLLFEGLCCPGENTAAPQALQSYHLAAEEQLSFRMLQTSSFANHSWAHSEGSGWLG
DLQTHGWDTVLGTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEYP
FEIQILAGCRMNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKE
ILQSLLGHTCPRFLAGLMEAGESELKRKVKPEAWLSCGPSPGPGRLQLVCHVSGFYPKPV
WVMWMRGEQEQRGTQRGDVLPNADETWYLRATLDVAAGEAAGLSCRVKHSSLGGHDLIIH
WGGYSIFLILICLTVIVTLVILVVVDSRLKKQSSNKNILSPHTPSPVFLMGANTQDTKNS
RHQFCLAQVSWIKNRVLKKWKTRLNQLW
|
| Enzyme 16 Number of Residues |
388 |
| Enzyme 16 Molecular Weight |
43626.1 |
| Enzyme 16 Theoretical pI |
8.69 |
| Enzyme 16 GO Classification |
| Function |
| — |
| Process |
- antigen processing and presentation
- immune response
- immune system process
|
| Component |
|
|
| Enzyme 16 General Function |
Involved in immune response |
| Enzyme 16 Specific Function |
T-cell surface glycoprotein CD1e, soluble is required for the presentation of glycolipid antigens on the cell surface. The membrane-associated form is not active |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
8249469  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P15812  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
CD1E_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1164 bp
ATGCTGCTCCTGTTCCTCCTCTTCGAGGGTCTCTGCTGTCCTGGGGAAAATACAGCAGCT
CCCCAGGCTCTACAATCCTATCATCTAGCAGCAGAGGAGCAGCTGTCCTTCCGCATGCTC
CAAACTTCCTCCTTTGCCAACCACAGCTGGGCACACAGTGAGGGCTCAGGATGGCTGGGT
GACCTGCAGACTCATGGCTGGGACACTGTCTTGGGCACCATCCGCTTTCTGAAGCCCTGG
TCCCATGGAAACTTCAGCAAGCAGGAGCTGAAAAACTTACAGTCACTGTTCCAGTTATAC
TTCCATAGTTTTATCCGGATAGTGCAAGCTTCTGCTGGTCAATTTCAGCTTGAATACCCC
TTCGAGATCCAGATATTAGCTGGCTGTAGAATGAATGCCCCACAAATCTTCTTAAATATG
GCATATCAAGGGTCAGATTTCCTGAGTTTCCAAGGAATTTCCTGGGAGCCATCTCCAGGA
GCAGGGATCCGGGCCCAGAACATCTGTAAAGTGCTCAATCGCTACCTAGATATTAAGGAA
ATACTGCAAAGCCTTCTTGGTCACACCTGCCCTCGATTTCTAGCGGGGCTCATGGAAGCA
GGGGAGTCAGAACTGAAACGGAAAGTGAAGCCAGAGGCCTGGCTGTCCTGTGGCCCCAGT
CCTGGCCCTGGCCGTCTGCAGCTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTG
TGGGTGATGTGGATGCGGGGTGAGCAGGAGCAGCGGGGCACTCAGCGAGGGGACGTCCTG
CCTAATGCTGACGAGACATGGTATCTCCGAGCAACCCTGGATGTGGCGGCTGGGGAGGCA
GCTGGCCTGTCCTGTCGGGTGAAACACAGCAGTCTAGGGGGCCATGATCTAATCATCCAT
TGGGGTGGATATTCCATCTTTCTCATCCTGATCTGTTTGACTGTGATAGTTACCCTGGTC
ATATTGGTTGTAGTTGACTCACGGTTAAAAAAACAGAGTTCAAATAAGAACATTCTTTCT
CCCCACACACCCAGCCCTGTCTTTCTCATGGGAGCCAACACTCAGGACACCAAGAATTCA
AGACATCAGTTCTGCTTGGCACAAGTATCGTGGATCAAAAACAGAGTATTGAAGAAGTGG
AAGACACGCCTAAACCAACTCTGG
|
| Enzyme 16 GenBank Gene ID |
AJ289111  |
| Enzyme 16 GeneCard ID |
CD1E  |
| Enzyme 16 GenAtlas ID |
CD1E  |
| Enzyme 16 HGNC ID |
HGNC:1638  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
1q22-q23 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Calabi F, Jarvis JM, Martin L, Milstein C: Two classes of CD1 genes. Eur J Immunol. 1989 Feb;19(2):285-92. [PubMed
]
- Angenieux C, Salamero J, Fricker D, Cazenave JP, Goud B, Hanau D, de La Salle H: Characterization of CD1e, a third type of CD1 molecule expressed in dendritic cells. J Biol Chem. 2000 Dec 1;275(48):37757-64. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed
]
- Tamouza R, Sghiri R, Ramasawmy R, Neonato MG, Mombo LE, Poirier JC, Schaeffer V, Fortier C, Labie D, Girot R, Toubert A, Krishnamoorthy R, Charron D: Two novel CD1 E alleles identified in black African individuals. Tissue Antigens. 2002 May;59(5):417-20. [PubMed
]
- Mirones I, Oteo M, Parra-Cuadrado JF, Martinez-Naves E: Identification of two novel human CD1E alleles. Tissue Antigens. 2000 Aug;56(2):159-61. [PubMed
]
- Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed
]
- de la Salle H, Mariotti S, Angenieux C, Gilleron M, Garcia-Alles LF, Malm D, Berg T, Paoletti S, Maitre B, Mourey L, Salamero J, Cazenave JP, Hanau D, Mori L, Puzo G, De Libero G: Assistance of microbial glycolipid antigen processing by CD1e. Science. 2005 Nov 25;310(5752):1321-4. [PubMed
]
- Maitre B, Angenieux C, Salamero J, Hanau D, Fricker D, Signorino F, Proamer F, Cazenave JP, Goud B, Tourne S, de la Salle H: Control of the intracellular pathway of CD1e. Traffic. 2008 Apr;9(4):431-45. Epub 2008 Jan 15. [PubMed
]
- Maitre B, Angenieux C, Wurtz V, Layre E, Gilleron M, Collmann A, Mariotti S, Mori L, Fricker D, Cazenave JP, van Dorsselaer A, Gachet C, de Libero G, Puzo G, Hanau D, de la Salle H: The assembly of CD1e is controlled by an N-terminal propeptide which is processed in endosomal compartments. Biochem J. 2009 May 1;419(3):661-8. [PubMed
]
- Tourne S, Maitre B, Collmann A, Layre E, Mariotti S, Signorino-Gelo F, Loch C, Salamero J, Gilleron M, Angenieux C, Cazenave JP, Mori L, Hanau D, Puzo G, De Libero G, de la Salle H: Cutting edge: a naturally occurring mutation in CD1e impairs lipid antigen presentation. J Immunol. 2008 Mar 15;180(6):3642-6. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
8178 |
| Enzyme 17 Name |
Epididymal secretory protein E1 |
| Enzyme 17 Synonyms |
- Human epididymis-specific protein 1
- He1
- Niemann-Pick disease type C2 protein
|
| Enzyme 17 Gene Name |
NPC2 |
| Enzyme 17 Protein Sequence |
>Epididymal secretory protein E1
MRFLAATFLLLALSTAAQAEPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVT
FTSNIQSKSSKAVVHGILMGVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYP
SIKLVVEWQLQDDKNQSLFCWEIPVQIVSHL
|
| Enzyme 17 Number of Residues |
151 |
| Enzyme 17 Molecular Weight |
16570.1 |
| Enzyme 17 Theoretical pI |
7.77 |
| Enzyme 17 GO Classification |
Not Available |
| Enzyme 17 General Function |
Involved in cholesterol binding |
| Enzyme 17 Specific Function |
May be involved in the regulation of the lipid composition of sperm membranes during the maturation in the epididymis |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
12803417  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
P61916  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
NPC2_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>456 bp
ATGCGTTTCCTGGCAGCTACATTCCTGCTCCTGGCGCTCAGCACCGCTGCCCAGGCCGAA
CCGGTGCAGTTCAAGGACTGCGGTTCTGTGGATGGAGTTATAAAGGAAGTGAATGTGAGC
CCATGCCCCACCCAACCCTGCCAGCTGAGCAAAGGACAGTCTTACAGCGTCAATGTCACC
TTCACCAGCAATATTCAGTCTAAAAGCAGCAAGGCCGTGGTGCATGGCATCCTGATGGGC
GTCCCAGTTCCCTTTCCCATTCCTGAGCCTGATGGTTGTAAGAGTGGAATTAACTGCCCT
ATCCAAAAAGACAAGACCTATAGCTACCTGAATAAACTACCAGTGAAAAGCGAATATCCC
TCTATAAAACTGGTGGTGGAGTGGCAACTTCAGGATGACAAAAACCAAAGTCTCTTCTGC
TGGGAAATCCCAGTACAGATCGTTTCTCATCTCTAA
|
| Enzyme 17 GenBank Gene ID |
BC002532  |
| Enzyme 17 GeneCard ID |
NPC2  |
| Enzyme 17 GenAtlas ID |
NPC2  |
| Enzyme 17 HGNC ID |
HGNC:14537  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
14q24.3 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Krull N, Ivell R, Osterhoff C, Kirchhoff C: Region-specific variation of gene expression in the human epididymis as revealed by in situ hybridization with tissue-specific cDNAs. Mol Reprod Dev. 1993 Jan;34(1):16-24. [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
]
- Naureckiene S, Sleat DE, Lackland H, Fensom A, Vanier MT, Wattiaux R, Jadot M, Lobel P: Identification of HE1 as the second gene of Niemann-Pick C disease. Science. 2000 Dec 22;290(5500):2298-301. [PubMed
]
- Leong WF, Chow VT: Transcriptomic and proteomic analyses of rhabdomyosarcoma cells reveal differential cellular gene expression in response to enterovirus 71 infection. Cell Microbiol. 2006 Apr;8(4):565-80. [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
]
- Millat G, Chikh K, Naureckiene S, Sleat DE, Fensom AH, Higaki K, Elleder M, Lobel P, Vanier MT: Niemann-Pick disease type C: spectrum of HE1 mutations and genotype/phenotype correlations in the NPC2 group. Am J Hum Genet. 2001 Nov;69(5):1013-21. Epub 2001 Sep 20. [PubMed
]
- Klunemann HH, Elleder M, Kaminski WE, Snow K, Peyser JM, O'Brien JF, Munoz D, Schmitz G, Klein HE, Pendlebury WW: Frontal lobe atrophy due to a mutation in the cholesterol binding protein HE1/NPC2. Ann Neurol. 2002 Dec;52(6):743-9. [PubMed
]
- Park WD, O'Brien JF, Lundquist PA, Kraft DL, Vockley CW, Karnes PS, Patterson MC, Snow K: Identification of 58 novel mutations in Niemann-Pick disease type C: correlation with biochemical phenotype and importance of PTC1-like domains in NPC1. Hum Mutat. 2003 Oct;22(4):313-25. [PubMed
]
- Chikh K, Rodriguez C, Vey S, Vanier MT, Millat G: Niemann-Pick type C disease: subcellular location and functional characterization of NPC2 proteins with naturally occurring missense mutations. Hum Mutat. 2005 Jul;26(1):20-8. [PubMed
]
- Millat G, Bailo N, Molinero S, Rodriguez C, Chikh K, Vanier MT: Niemann-Pick C disease: use of denaturing high performance liquid chromatography for the detection of NPC1 and NPC2 genetic variations and impact on management of patients and families. Mol Genet Metab. 2005 Sep-Oct;86(1-2):220-32. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
8289 |
| Enzyme 18 Name |
Antigen-presenting glycoprotein CD1d |
| Enzyme 18 Synonyms |
- R3G1
- CD1d antigen
|
| Enzyme 18 Gene Name |
CD1D |
| Enzyme 18 Protein Sequence |
>Antigen-presenting glycoprotein CD1d
MGCLLFLLLWALLQAWGSAEVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSN
DSDTVRSLKPWSQGTFSDQQWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGC
EVHPGNASNNFFHVAFQGKDILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLL
NGTCPQFVSGLLESGKSELKKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMR
GEQEQQGTQPGDILPNADETWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGGSYT
SMGLIALAVLACLLFLLIVGFTSRFKRQTSYQGVL
|
| Enzyme 18 Number of Residues |
335 |
| Enzyme 18 Molecular Weight |
37717.0 |
| Enzyme 18 Theoretical pI |
8.28 |
| Enzyme 18 GO Classification |
| Function |
| — |
| Process |
- antigen processing and presentation
- immune response
- immune system process
|
| Component |
|
|
| Enzyme 18 General Function |
Involved in immune response |
| Enzyme 18 Specific Function |
Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
Not Available |
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
619800  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P15813  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
CD1D_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1008 bp
ATGGGGTGCCTGCTGTTTCTGCTGCTCTGGGCGCTCCTCCAGGCTTGGGGAAGCGCTGAA
GTCCCGCAAAGGCTTTTCCCCCTCCGCTGCCTCCAGATCTCGTCCTTCGCCAATAGCAGC
TGGACGCGCACCGACGGCTTGGCGTGGCTGGGGGAGCTGCAGACGCACAGCTGGAGCAAC
GACTCGGACACCGTCCGCTCTCTGAAGCCTTGGTCCCAGGGCACGTTCAGCGACCAGCAG
TGGGAGACGCTGCAGCATATATTTCGGGTTTATCGAAGCAGCTTCACCAGGGACGTGAAG
GAATTCGCCAAAATGCTACGCTTATCCTATCCCTTGGAGCTCCAGGTGTCCGCTGGCTGT
GAGGTGCACCCTGGGAACGCCTCAAATAACTTCTTCCATGTAGCATTTCAAGGAAAAGAT
ATCCTGAGTTTCCAAGGAACTTCTTGGGAGCCAACCCAAGAGGCCCCACTTTGGGTAAAC
TTGGCCATTCAAGTGCTCAACCAGGACAAGTGGACGAGGGAAACAGTGCAGTGGCTCCTT
AATGGCACCTGCCCCCAATTTGTCAGTGGCCTCCTTGAGTCAGGGAAGTCGGAACTGAAG
AAGCAAGTGAAGCCCAAGGCCTGGCTGTCCCGTGGCCCCAGTCCTGGCCCTGGCCGTCTG
CTGCTGGTGTGCCATGTCTCAGGATTCTACCCAAAGCCTGTATGGGTGAAGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCCAGGGGACATCCTGCCCAATGCTGACGAGACA
TGGTATCTCCGAGCAACCCTGGATGTGGTGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGGTGGGAGCTACACC
TCCATGGGCTTGATTGCCTTGGCAGTCCTGGCGTGCTTGCTGTTCCTCCTCATTGTGGGC
TTTACCTCCCGGTTTAAGAGGCAAACTTCCTATCAGGGCGTCCTGTGA
|
| Enzyme 18 GenBank Gene ID |
J04142  |
| Enzyme 18 GeneCard ID |
CD1D  |
| Enzyme 18 GenAtlas ID |
CD1D  |
| Enzyme 18 HGNC ID |
HGNC:1637  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
1q22-q23 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Calabi F, Jarvis JM, Martin L, Milstein C: Two classes of CD1 genes. Eur J Immunol. 1989 Feb;19(2):285-92. [PubMed
]
- Balk SP, Bleicher PA, Terhorst C: Isolation and characterization of a cDNA and gene coding for a fourth CD1 molecule. Proc Natl Acad Sci U S A. 1989 Jan;86(1):252-6. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed
]
- Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed
]
- Rodionov DG, Nordeng TW, Pedersen K, Balk SP, Bakke O: A critical tyrosine residue in the cytoplasmic tail is important for CD1d internalization but not for its basolateral sorting in MDCK cells. J Immunol. 1999 Feb 1;162(3):1488-95. [PubMed
]
- Kang SJ, Cresswell P: Regulation of intracellular trafficking of human CD1d by association with MHC class II molecules. EMBO J. 2002 Apr 2;21(7):1650-60. [PubMed
]
- Brutkiewicz RR: CD1d ligands: the good, the bad, and the ugly. J Immunol. 2006 Jul 15;177(2):769-75. [PubMed
]
- Chen X, Wang X, Keaton JM, Reddington F, Illarionov PA, Besra GS, Gumperz JE: Distinct endosomal trafficking requirements for presentation of autoantigens and exogenous lipids by human CD1d molecules. J Immunol. 2007 May 15;178(10):6181-90. [PubMed
]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed
]
- Koch M, Stronge VS, Shepherd D, Gadola SD, Mathew B, Ritter G, Fersht AR, Besra GS, Schmidt RR, Jones EY, Cerundolo V: The crystal structure of human CD1d with and without alpha-galactosylceramide. Nat Immunol. 2005 Aug;6(8):819-26. Epub 2005 Jul 10. [PubMed
]
- Borg NA, Wun KS, Kjer-Nielsen L, Wilce MC, Pellicci DG, Koh R, Besra GS, Bharadwaj M, Godfrey DI, McCluskey J, Rossjohn J: CD1d-lipid-antigen recognition by the semi-invariant NKT T-cell receptor. Nature. 2007 Jul 5;448(7149):44-9. Epub 2007 Jun 20. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
8469 |
| Enzyme 19 Name |
GPI mannosyltransferase 1 |
| Enzyme 19 Synonyms |
- GPI mannosyltransferase I
- GPI-MT-I
- Phosphatidylinositol-glycan biosynthesis class M protein
- PIG-M
|
| Enzyme 19 Gene Name |
PIGM |
| Enzyme 19 Protein Sequence |
>GPI mannosyltransferase 1
MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAAR
FVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLG
RRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMK
IYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFA
LSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLI
LLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVL
LMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERI
KYD
|
| Enzyme 19 Number of Residues |
423 |
| Enzyme 19 Molecular Weight |
49459.2 |
| Enzyme 19 Theoretical pI |
9.31 |
| Enzyme 19 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
- organelle membrane
|
|
| Enzyme 19 General Function |
Involved in transferase activity, transferring hexosyl groups |
| Enzyme 19 Specific Function |
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
- 18-38
80-100
139-161
170-190
226-246
288-308
315-337
339-350
358-378
385-405
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
11414879  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9H3S5  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
PIGM_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1272 bp
ATGGGCTCCACCAAGCACTGGGGCGAATGGCTCCTGAACTTGAAGGTGGCTCCAGCCGGC
GTCTTTGGTGTGGCCTTTCTAGCCAGAGTCGCCCTGGTTTTCTATGGCGTCTTCCAGGAC
CGGACCCTGCACGTGAGGTATACGGACATCGACTACCAGGTCTTCACCGACGCCGCGCGC
TTCGTCACGGAGGGGCGCTCGCCTTACCTGAGAGCCACGTACCGTTACACCCCGCTGCTG
GGTTGGCTCCTCACTCCCAACATCTACCTCAGCGAGCTCTTTGGAAAGTTTCTCTTCATC
AGCTGCGACCTCCTCACCGCTTTCCTCTTATACCGCCTGCTGCTGCTGAAGGGGCTGGGG
CGCCGCCAGGCTTGTGGCTACTGTGTCTTTTGGCTTCTTAACCCCCTGCCTATGGCAGTA
TCCAGCCGCGGTAATGCGGACTCTATTGTCGCCTCCCTGGTCCTGATGGTCCTCTACTTG
ATAAAGAAAAGACTCGTCGCGTGTGCAGCTGTATTCTATGGTTTCGCGGTGCATATGAAG
ATATATCCAGTGACTTACATCCTTCCCATAACCCTCCACCTGCTTCCAGATCGCGACAAT
GACAAAAGCCTCCGTCAATTCCGGTACACTTTCCAGGCTTGTTTGTACGAGCTCCTGAAA
AGGCTGTGTAATCGGGCTGTGCTGCTGTTTGTAGCAGTTGCTGGACTCACGTTTTTTGCC
CTGAGCTTTGGTTTTTACTATGAGTACGGCTGGGAATTTTTGGAACACACCTACTTTTAT
CACCTGACTAGGCGGGATATCCGTCACAACTTTTCTCCGTACTTCTACATGCTGTATTTG
ACTGCAGAGAGCAAGTGGAGTTTTTCCCTGGGAATTGCTGCATTCCTGCCACAGCTCATC
TTGCTTTCAGCTGTGTCTTTCGCCTATTACAGAGACCTCGTTTTTTGTTGTTTTCTTCAT
ACGTCCATTTTTGTGACTTTTAACAAAGTCTGCACCTCCCAGTACTTTCTTTGGTACCTC
TGCTTACTGCCTCTTGTGATGCCACTAGTCAGAATGCCTTGGAAAAGAGCTGTAGTTCTC
CTAATGTTATGGTTTATAGGGCAGGCCATGTGGCTGGCTCCTGCCTATGTTCTAGAGTTT
CAAGGAAAGAACACCTTTCTGTTTATTTGGTTAGCTGGTTTGTTCTTTCTTCTTATCAAT
TGTTCCATCCTGATTCAAATTATTTCCCATTACAAAGAAGAACCCCTGACAGAGAGAATC
AAATATGACTAG
|
| Enzyme 19 GenBank Gene ID |
AB028127  |
| Enzyme 19 GeneCard ID |
PIGM  |
| Enzyme 19 GenAtlas ID |
PIGM  |
| Enzyme 19 HGNC ID |
HGNC:18858  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
1q23.2 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Maeda Y, Watanabe R, Harris CL, Hong Y, Ohishi K, Kinoshita K, Kinoshita T: PIG-M transfers the first mannose to glycosylphosphatidylinositol on the lumenal side of the ER. EMBO J. 2001 Jan 15;20(1-2):250-61. [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
]
- 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
]
- Almeida AM, Murakami Y, Layton DM, Hillmen P, Sellick GS, Maeda Y, Richards S, Patterson S, Kotsianidis I, Mollica L, Crawford DH, Baker A, Ferguson M, Roberts I, Houlston R, Kinoshita T, Karadimitris A: Hypomorphic promoter mutation in PIGM causes inherited glycosylphosphatidylinositol deficiency. Nat Med. 2006 Jul;12(7):846-51. Epub 2006 Jun 11. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
8495 |
| Enzyme 20 Name |
Phosphatidylinositol-glycan biosynthesis class W protein |
| Enzyme 20 Synonyms |
- PIG-W
|
| Enzyme 20 Gene Name |
PIGW |
| Enzyme 20 Protein Sequence |
>Phosphatidylinositol-glycan biosynthesis class W protein
MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTD
FVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNIS
LESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAM
VCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFF
TIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLN
ANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVN
VEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTN
KKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVV
NLYMFSNCLIVYVLYLQDKTVQFW
|
| Enzyme 20 Number of Residues |
504 |
| Enzyme 20 Molecular Weight |
56881.3 |
| Enzyme 20 Theoretical pI |
9.44 |
| Enzyme 20 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
|
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
- organelle membrane
|
|
| Enzyme 20 General Function |
Involved in transferase activity, transferring acyl groups |
| Enzyme 20 Specific Function |
Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI- anchor. Acetylation during GPI-anchor biosynthesis is not essential for the subsequent mannosylation and is usually removed soon after the attachment of GPIs to proteins |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
- 22-42
74-94
132-152
163-183
203-223
238-258
261-281
306-326
339-359
371-391
449-469
474-494
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
31339065  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q7Z7B1  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PIGW_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>1515 bp
ATGTCTGAAAAGCAGATGAAGGAAGCTTTTGTCAGTAACCTCAATGGAACCACCGTGCTG
GAAATCACCCAGGGATTGTGCTTTCCTGCATTCTGTATCCTGTGCAGAGGGTTCCTGATC
ATTTTCTCACAGTACTTGTGTTCTTTTTCACCTACCTGGAAAACTAGATTCCTCACTGAC
TTTGTTGTCCTAATAGTTCCCATGGTAGCCACTTTGACCATTTGGGCTTCATTTATCCTC
CTTGAGCTTCTCGGTGTAATTATCTTTGGGGCAGGGCTGTTGTATCAAATATACCGAAGG
AGGACCTGCTATGCCAGACTGCCTTTCCTAAAAATCCTTGAAAAATTCTTGAACATCAGT
CTAGAATCAGAATACAATCCAGCCATCTCCTGTTTCCGTGTAATTACCAGTGCGTTTACT
GCTATTGCTATTTTGGCTGTGGACTTCCCACTTTTTCCCAGAAGATTTGCCAAAACTGAG
CTCTATGGGACAGGAGCAATGGATTTTGGAGTAGGTGGCTTTGTTTTTGGGTCTGCAATG
GTTTGTCTAGAGGTCAGGAGGAGAAAATATATGGAAGGGTCCAAATTGCATTACTTTACA
AACTCATTGTACTCTGTTTGGCCATTAGTCTTCCTAGGAATCGGACGATTAGCCATTATA
AAATCAATAGGCTATCAGGAACATTTAACAGAGTATGGAGTTCACTGGAACTTTTTCTTT
ACCATAATAGTTGTGAAATTGATAACACCACTGCTGTTGATTATTTTTCCCCTAAATAAG
TCCTGGATTATTGCCCTCGGCATTACTGTATTATACCAGCTAGCCCTTGACTTTACCTCA
CTGAAGAGGTTAATATTATATGGCACTGATGGTAGTGGCACACGGGTTGGTCTATTAAAT
GCCAACCGCGAAGGAATAATCTCTACCCTGGGGTATGTGGCAATACACATGGCTGGTGTG
CAAACAGGGTTATATATGCATAAGAACCGATCACATATCAAAGACTTGATAAAAGTAGCC
TGTTTTCTTTTACTGGCAGCTATTAGCCTCTTCATATCTCTTTACGTAGTTCAAGTAAAT
GTAGAAGCAGTATCTCGAAGAATGGCAAATTTAGCCTTTTGTATTTGGATAGTTGCTTCT
AGCCTGATCCTTCTTAGTAGTTTATTACTGGGTGATATAATTTTGAGTTTTGCCAAATTT
CTAATTAAAGGAGCTCTAGTACCATGTTCTTGGAAACTTATCCAGTCACCTGTTACAAAT
AAAAAGCATTCAGAATCTCTAGTCCCTGAAGCCGAAAGAATGGAACCCAGTCTTTGTTTA
ATCACAGCTCTAAACAGAAAACAGTTAATATTTTTCTTGCTGTCAAATATAACAACTGGC
CTGATCAACCTGATGGTAGATACATTACACAGCAGTACCTTGTGGGCCTTATTTGTGGTC
AATCTCTATATGTTTTCCAACTGTTTAATTGTATATGTACTATATTTGCAAGATAAGACT
GTACAATTTTGGTGA
|
| Enzyme 20 GenBank Gene ID |
AB097818  |
| Enzyme 20 GeneCard ID |
PIGW  |
| Enzyme 20 GenAtlas ID |
PIGW  |
| Enzyme 20 HGNC ID |
HGNC:23213  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
17q12 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Murakami Y, Siripanyapinyo U, Hong Y, Kang JY, Ishihara S, Nakakuma H, Maeda Y, Kinoshita T: PIG-W is critical for inositol acylation but not for flipping of glycosylphosphatidylinositol-anchor. Mol Biol Cell. 2003 Oct;14(10):4285-95. Epub 2003 Jun 13. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
8621 |
| Enzyme 21 Name |
Phosphatidylinositol-glycan biosynthesis class X protein |
| Enzyme 21 Synonyms |
- PIG-X
|
| Enzyme 21 Gene Name |
PIGX |
| Enzyme 21 Protein Sequence |
>Phosphatidylinositol-glycan biosynthesis class X protein
MAARVAAVRAAAWLLLGAATGLTRGPAAAFTAARSDAGIRAMCSEIILRQEVLKDGFHRD
LLIKVKFGESIEDLHTCRLLIKQDIPAGLYVDPYELASLRERNITEAVMVSENFDIEAPN
YLSKESEVLIYARRDSQCIDCFQAFLPVHCRYHRPHSEDGEASIVVNNPDLLMFCDQEFP
ILKCWAHSEVAAPCALENEDICQWNKMKYKSVYKNVILQVPVGLTVHTSLVCSVTLLITI
LCSTLILVAVFKYGHFSL
|
| Enzyme 21 Number of Residues |
258 |
| Enzyme 21 Molecular Weight |
28788.1 |
| Enzyme 21 Theoretical pI |
6.30 |
| Enzyme 21 GO Classification |
| Function |
| — |
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- membrane
- organelle membrane
|
|
| Enzyme 21 General Function |
Involved in GPI anchor biosynthetic process |
| Enzyme 21 Specific Function |
Essential component of glycosylphosphatidylinositol- mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the mannosyltransferase PIGM |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
Not Available |
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
261490706  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q8TBF5  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
PIGX_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>777 bp
CTGGCGGCTCGGGTGGCGGCGGTTCGGGCGGCCGCCTGGCTGCTCCTCGGGGCGGCGACC
GGGCTCACGCGCGGGCCCGCCGCGGCCTTCACCGCCGCGCGCTCTGACGCCGGCATAAGG
GCCATGTGTTCTGAAATTATTTTGAGGCAAGAAGTTTTGAAAGATGGTTTCCACAGAGAC
CTTTTAATCAAAGTGAAGTTTGGGGAAAGCATTGAGGACTTGCACACCTGCCGTCTCTTA
ATTAAACAGGACATTCCTGCAGGACTTTATGTGGATCCGTATGAGTTGGCTTCATTACGA
GAGAGAAACATAACAGAGGCAGTGATGGTTTCAGAAAATTTTGATATAGAGGCCCCTAAC
TATTTGTCCAAGGAGTCTGAAGTTCTCATTTATGCCAGACGAGATTCACAGTGCATTGAC
TGTTTTCAAGCCTTTTTGCCTGTGCACTGCCGCTATCATCGGCCGCACAGTGAAGATGGA
GAAGCCTCGATTGTGGTCAATAACCCAGATTTGTTGATGTTTTGTGACCAAGAGTTCCCG
ATTTTGAAATGCTGGGCTCACTCAGAAGTGGCAGCCCCTTGTGCTTTGGAGAATGAGGAT
ATCTGCCAATGGAACAAGATGAAGTATAAATCAGTATATAAGAATGTGATTCTACAAGTT
CCAGTGGGACTGACTGTACATACCTCTCTAGTATGTTCTGTGACTCTGCTCATTACAATC
CTGTGCTCTACATTGATCCTTGTAGCAGTTTTCAAATATGGCCATTTTTCCCTATAA
|
| Enzyme 21 GenBank Gene ID |
NM_017861.3  |
| Enzyme 21 GeneCard ID |
PIGX  |
| Enzyme 21 GenAtlas ID |
PIGX  |
| Enzyme 21 HGNC ID |
HGNC:26046  |
| Enzyme 21 Chromosome Location |
3 |
| Enzyme 21 Locus |
3q29 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 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
]
- 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
]
- Ashida H, Hong Y, Murakami Y, Shishioh N, Sugimoto N, Kim YU, Maeda Y, Kinoshita T: Mammalian PIG-X and yeast Pbn1p are the essential components of glycosylphosphatidylinositol-mannosyltransferase I. Mol Biol Cell. 2005 Mar;16(3):1439-48. Epub 2005 Jan 5. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
8625 |
| Enzyme 22 Name |
GPI mannosyltransferase 4 |
| Enzyme 22 Synonyms |
- GPI mannosyltransferase IV
- GPI-MT-IV
- Phosphatidylinositol-glycan biosynthesis class Z protein
- PIG-Z
- SMP3 homolog
- hSMP3
|
| Enzyme 22 Gene Name |
PIGZ |
| Enzyme 22 Protein Sequence |
>GPI mannosyltransferase 4
MQICGSSVASVAAGTSFQVLGPVCWQQLDLKMAVRVLWGGLSLLRVLWCLLPQTGYVHPD
EFFQSPEVMAEDILGVQAARPWEFYPSSSCRSVLFPLLISGSTFWLLRLWEELGPWPGLV
SGYALLVGPRLLLTALSFALDGAVYHLAPPMGADRWNALALLSGSYVTLVFYTRTFSNTI
EGLLFTWLLVLVSSHVTWGPTRKEPAPGPRWRSWLLGGIVAAGFFNRPTFLAFAVVPLYL
WGTRGATNPGLKSLTREALVLLPGATLTAAVFVATDSWYFSSPATSRNLVLTPVNFLHYN
LNPQNLARHGTHARLTHLAVNGFLLFGVLHAQALQAAWQQLQVGLQASAQMGLLRALGAR
SLLSSPRSYLLLLYFMPLALLSAFSHQEARFLIPLLVPLVLLCSPQTQPVPWKGTVVLFN
ALGALLFGCLHQGGLVPGLEYLEQVVHAPVLPSTPTHYTLLFTHTYMPPRHLLHLPGLGA
PVEVVDMGGTEDWALCQTLKSFTRQPACQVAGGPWLCRLFVVTPGTTRRAVEKCSFPFKN
ETLLFPHLTLEDPPALSSLLSGAWRDHLSLHIVELGEET
|
| Enzyme 22 Number of Residues |
579 |
| Enzyme 22 Molecular Weight |
63472.6 |
| Enzyme 22 Theoretical pI |
8.28 |
| Enzyme 22 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- intrinsic to endoplasmic reticulum membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 22 General Function |
Involved in transferase activity, transferring glycosyl groups |
| Enzyme 22 Specific Function |
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers a fourth mannose to some trimannosyl-GPIs during GPI precursor assembly. The presence of a fourth mannose in GPI is facultative and only scarcely detected, suggesting that it only exists in some tissues |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
- 131-151
156-173
180-200
216-236
258-278
369-389
391-411
416-436
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
30581137  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q86VD9  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
PIGZ_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1740 bp
ATGCAGATCTGTGGATCCAGCGTAGCATCTGTAGCAGCTGGGACATCATTCCAGGTTTTG
GGCCCGGTGTGTTGGCAACAACTGGATCTGAAGATGGCAGTCAGGGTGCTTTGGGGTGGT
CTCAGCCTGCTCCGAGTGCTGTGGTGTCTCCTTCCGCAGACGGGCTATGTGCACCCAGAT
GAGTTCTTCCAGTCCCCTGAGGTGATGGCAGAGGACATCCTGGGCGTTCAGGCCGCGCGG
CCCTGGGAGTTTTACCCCAGCAGCTCCTGCCGCTCGGTGCTCTTCCCCCTGCTGATCTCT
GGTTCCACCTTCTGGCTGCTCAGGCTCTGGGAGGAGCTGGGGCCGTGGCCTGGCCTGGTG
AGCGGCTATGCGCTGCTGGTGGGGCCTCGACTCCTCCTCACTGCCCTTTCCTTTGCTCTG
GACGGGGCCGTGTACCACCTGGCCCCGCCGATGGGGGCGGATCGCTGGAACGCCCTGGCC
CTGCTGTCTGGTTCCTACGTCACCCTGGTCTTCTACACAAGGACCTTCTCCAACACCATT
GAGGGACTCCTCTTCACGTGGCTGCTGGTGCTGGTATCCTCCCATGTAACGTGGGGCCCT
ACACGCAAGGAGCCGGCGCCGGGTCCACGGTGGCGCAGCTGGCTTCTTGGAGGCATTGTG
GCTGCTGGCTTCTTCAACCGGCCCACCTTTCTGGCCTTTGCTGTGGTCCCCCTCTACCTC
TGGGGCACTCGTGGAGCCACAAACCCTGGTTTGAAGTCTCTGACCCGGGAGGCCCTGGTG
CTGCTCCCTGGGGCAGCCCTCACAGCAGCGGTGTTTGTGGCCACGGACAGCTGGTATTTC
TCCAGCCCCGCTACATCCAGGAACCTTGTCCTGACACCTGTCAACTTCTTGCACTACAAC
CTGAATCCCCAAAACCTGGCGAGACATGGCACGCACGCGCGGCTCACTCACCTGGCAGTC
AACGGCTTCCTGCTCTTCGGGGTGCTGCATGCCCAGGCCCTGCAGGCTGCGTGGCAACGG
CTGCAAGTCGGCCTCCAGGCCTCTGCACAAATGGGCCTCCTGAGGGCACTGGGTGCCCGG
AGCCTGCTGTCCAGCCCCAGGTCCTATCTCCTTCTCCTCTACTTCATGCCTCTGGCCCTG
CTATCTGCCTTTAGCCACCAGGAGGCTCGGTTCCTGATTCCCCTCCTGGTCCCCCTGGTC
CTGCTTTGTAGTCCACAGACGCAGCCTGTGCCTTGGAAGGGCACTGTGGTCCTCTTCAAC
GCCCTCGGTGCCCTCCTCTTCGGCTGCCTGCATCAGGGGGGCCTGGTGCCTGGCCTGGAG
TACCTGGAGCAGGTGGTCCATGCCCCTGTGCTCCCAAGCACACCCACCCACTACACACTC
CTCTTCACTCACACCTACATGCCCCCCCGGCACCTCCTACACCTCCCAGGCCTGGGGGCA
CCAGTGGAGGTGGTGGACATGGGGGGGACTGAGGACTGGGCCCTGTGCCAAACCCTGAAA
AGCTTCACCAGACAACCAGCCTGCCAAGTGGCTGGTGGGCCATGGCTCTGCCGCCTCTTT
GTGGTAACCCCTGGCACCACCAGGCGTGCCGTGGAGAAGTGCAGCTTCCCCTTCAAGAAT
GAAACACTTTTATTTCCCCATCTGACCCTGGAGGATCCACCAGCCCTGTCCTCCTTGCTG
AGTGGGGCTTGGAGGGACCACCTCAGTCTTCACATTGTGGAGCTGGGGGAAGAAACCTGA
|
| Enzyme 22 GenBank Gene ID |
NM_025163.2  |
| Enzyme 22 GeneCard ID |
PIGZ  |
| Enzyme 22 GenAtlas ID |
PIGZ  |
| Enzyme 22 HGNC ID |
HGNC:30596  |
| Enzyme 22 Chromosome Location |
3 |
| Enzyme 22 Locus |
3q29 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 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
]
- 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
]
- Taron BW, Colussi PA, Wiedman JM, Orlean P, Taron CH: Human Smp3p adds a fourth mannose to yeast and human glycosylphosphatidylinositol precursors in vivo. J Biol Chem. 2004 Aug 20;279(34):36083-92. Epub 2004 Jun 18. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
10050 |
| Enzyme 23 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3 |
| Enzyme 23 Synonyms |
- Phosphoinositide phospholipase C-delta-3
- Phospholipase C-delta-3
- PLC-delta-3
|
| Enzyme 23 Gene Name |
PLCD3 |
| Enzyme 23 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 23 Number of Residues |
789 |
| Enzyme 23 Molecular Weight |
89257.5 |
| Enzyme 23 Theoretical pI |
6.97 |
| Enzyme 23 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 23 General Function |
Involved in calcium ion binding |
| Enzyme 23 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 23 Pathways |
|
| Enzyme 23 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q8N3E9  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PLCD3_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 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 23 GenBank Gene ID |
AK074240  |
| Enzyme 23 GeneCard ID |
PLCD3  |
| Enzyme 23 GenAtlas ID |
PLCD3  |
| Enzyme 23 HGNC ID |
HGNC:9061  |
| Enzyme 23 Chromosome Location |
1 |
| Enzyme 23 Locus |
17q21.31 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 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 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
11996 |
| Enzyme 24 Name |
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 |
| Enzyme 24 Synonyms |
- BGnT-5
- Beta-1,3-Gn-T5
- Beta-1,3-N-acetylglucosaminyltransferase 5
- Beta3Gn-T5
- Lactotriaosylceramide synthase
- Lc(3)Cer synthase
- Lc3 synthase
|
| Enzyme 24 Gene Name |
B3GNT5 |
| Enzyme 24 Protein Sequence |
>UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI
|
| Enzyme 24 Number of Residues |
378 |
| Enzyme 24 Molecular Weight |
44052.3 |
| Enzyme 24 Theoretical pI |
8.00 |
| Enzyme 24 GO Classification |
| Function |
- catalytic activity
- galactosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
|
|
| Enzyme 24 General Function |
Involved in galactosyltransferase activity |
| Enzyme 24 Specific Function |
Beta-1,3-N-acetylglucosaminyltransferase that plays a key role in the synthesis of lacto- or neolacto-series carbohydrate chains on glycolipids, notably by participating in biosynthesis of HNK-1 and Lewis X carbohydrate structures. Has strong activity toward lactosylceramide (LacCer) and neolactotetraosylceramide (nLc(4)Cer; paragloboside), resulting in the synthesis of Lc(3)Cer and neolactopentaosylceramide (nLc(5)Cer), respectively. Probably plays a central role in regulating neolacto-series glycolipid synthesis during embryonic development |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
13568434  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q9BYG0  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
B3GN5_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1137 bp
ATGAGAATGTTGGTTAGTGGCAGAAGAGTCAAAAAATGGCAGTTAATTATTCAGTTATTT
GCTACTTGTTTTTTAGCGAGCCTCATGTTTTTTTGGGAACCAATCGATAATCACATTGTG
AGCCATATGAAGTCATATTCTTACAGATACCTCATAAATAGCTATGACTTTGTGAATGAT
ACCCTGTCTCTTAAGCACACCTCAGCGGGGCCTCGCTACCAATACTTGATTAACCACAAG
GAAAAGTGTCAAGCTCAAGACGTCCTCCTTTTACTGTTTGTAAAAACTGCTCCTGAAAAC
TATGATCGACGTTCCGGAATTAGAAGGACGTGGGGCAATGAAAATTATGTTCGGTCTCAG
CTGAATGCCAACATCAAAACTCTGTTTGCCTTAGGAACTCCTAATCCACTGGAGGGAGAA
GAACTACAAAGAAAACTGGCTTGGGAAGATCAAAGGTACAATGATATAATTCAGCAAGAC
TTTGTTGATTCTTTCTACAATCTTACTCTGAAATTACTTATGCAGTTCAGTTGGGCAAAT
ACCTATTGTCCACATGCCAAATTTCTTATGACTGCTGATGATGACATATTTATTCACATG
CCAAATCTGATTGAGTACCTTCAAAGTTTAGAACAAATTGGTGTTCAAGACTTTTGGATT
GGTCGTGTTCATCGTGGTGCCCCTCCCATTAGAGATAAAAGCAGCAAATACTACGTGTCC
TATGAAATGTACCAGTGGCCAGCTTACCCTGACTACACAGCCGGAGCTGCCTATGTAATC
TCCGGTGATGTAGCTGCCAAAGTCTATGAGGCATCACAGACACTAAATTCAAGTCTTTAC
ATAGACGATGTGTTCATGGGCCTCTGTGCCAATAAAATAGGGATAGTACCGCAGGACCAT
GTGTTTTTTTCTGGAGAGGGTAAAACTCCTTATCATCCCTGCATCTATGAAAAAATGATG
ACATCTCATGGACACTTAGAAGATCTCCAGGACCTTTGGAAGAATGCTACAGATCCTAAA
GTAAAAACCATTTCCAAAGGTTTTTTTGGTCAAATATACTGCAGATTAATGAAGATAATT
CTCCTTTGTAAAATTAGCTATGTGGACACATACCCTTGTAGGGCTGCGTTTATCTAA
|
| Enzyme 24 GenBank Gene ID |
AB045278  |
| Enzyme 24 GeneCard ID |
B3GNT5  |
| Enzyme 24 GenAtlas ID |
B3GNT5  |
| Enzyme 24 HGNC ID |
HGNC:15684  |
| Enzyme 24 Chromosome Location |
3 |
| Enzyme 24 Locus |
3q28 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Togayachi A, Akashima T, Ookubo R, Kudo T, Nishihara S, Iwasaki H, Natsume A, Mio H, Inokuchi J, Irimura T, Sasaki K, Narimatsu H: Molecular cloning and characterization of UDP-GlcNAc:lactosylceramide beta 1,3-N-acetylglucosaminyltransferase (beta 3Gn-T5), an essential enzyme for the expression of HNK-1 and Lewis X epitopes on glycolipids. J Biol Chem. 2001 Jun 22;276(25):22032-40. Epub 2001 Mar 30. [PubMed
]
- Henion TR, Zhou D, Wolfer DP, Jungalwala FB, Hennet T: Cloning of a mouse beta 1,3 N-acetylglucosaminyltransferase GlcNAc(beta 1,3)Gal(beta 1,4)Glc-ceramide synthase gene encoding the key regulator of lacto-series glycolipid biosynthesis. J Biol Chem. 2001 Aug 10;276(32):30261-9. Epub 2001 May 30. [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 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
12250 |
| Enzyme 25 Name |
Sphingomyelin phosphodiesterase 3 |
| Enzyme 25 Synonyms |
- Neutral sphingomyelinase 2
- nSMase-2
- nSMase2
- Neutral sphingomyelinase II
|
| Enzyme 25 Gene Name |
SMPD3 |
| Enzyme 25 Protein Sequence |
>Sphingomyelin phosphodiesterase 3
MVLYTTPFPNSCLSALHCVSWALIFPCYWLVDRLAASFIPTTYEKRQRADDPCCLQLLCT
ALFTPIYLALLVASLPFAFLGFLFWSPLQSARRPYIYSRLEDKGLAGGAALLSEWKGTGP
GKSFCFATANVCLLPDSLARVNNLFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSIS
AASFSSLVSPQGGDGVARAVPGSIKRTASVEYKGDGGRHPGDEAANGPASGDPVDSSSPE
DACIVRIGGEEGGRPPEADDPVPGGQARNGAGGGPRGQTPNHNQQDGDSGSLGSPSASRE
SLVKGRAGPDTSASGEPGANSKLLYKASVVKKAAARRRRHPDEAFDHEVSAFFPANLDFL
CLQEVFDKRAATKLKEQLHGYFEYILYDVGVYGCQGCCSFKCLNSGLLFASRYPIMDVAY
HCYPNKCNDDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPQEDSAIRCGQLDLLQ
DWLADFRKSTSSSSAANPEELVAFDVVCGDFNFDNCSSDDKLEQQHSLFTHYRDPCRLGP
GEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSSGQKGRKELLK
GNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSSGEEEA
|
| Enzyme 25 Number of Residues |
655 |
| Enzyme 25 Molecular Weight |
71080.1 |
| Enzyme 25 Theoretical pI |
5.53 |
| Enzyme 25 GO Classification |
Not Available |
| Enzyme 25 General Function |
Involved in metal ion binding |
| Enzyme 25 Specific Function |
Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization |
| Enzyme 25 Pathways |
|
| Enzyme 25 Reactions |
- sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
8247250  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q9NY59  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
NSMA2_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1968 bp
ATGGTTTTGTACACGACCCCCTTTCCTAACAGCTGTCTGTCCGCCCTGCACTGTGTGTCC
TGGGCCCTTATCTTTCCATGCTACTGGCTGGTGGACCGGCTCGCTGCCTCCTTCATACCC
ACCACCTACGAGAAGCGCCAGCGGGCAGACGACCCGTGCTGCCTGCAGCTGCTCTGCACT
GCCCTCTTCACGCCCATCTACCTGGCCCTCCTGGTGGCCTCGCTGCCCTTTGCGTTTCTC
GGCTTTCTCTTCTGGTCCCCACTGCAGTCGGCCCGCCGGCCCTACATCTATTCACGGCTG
GAAGACAAGGGCCTGGCCGGTGGGGCAGCCCTGCTCAGTGAATGGAAGGGCACGGGGCCT
GGCAAAAGCTTCTGCTTTGCCACTGCCAACGTCTGCCTCCTGCCCGACTCACTCGCCAGG
GTCAACAACCTTTTTAACACCCAAGCGCGGGCCAAGGAGATCGGGCAGAGAATCCGCAAT
GGGGCCGCCCGGCCCCAGATCAAAATTTACATCGACTCCCCCACCAATACCTCCATCAGC
GCCGCTAGCTTCAGCAGCCTGGTGTCACCACAGGGCGGCGATGGGGTGGCCCGGGCCGTC
CCCGGGAGCATTAAGAGGACAGCCTCTGTGGAGTACAAGGGTGACGGTGGGCGGCACCCC
GGTGACGAGGCTGCCAACGGCCCAGCCTCTGGGGACCCTGTCGACAGCAGCAGCCCGGAG
GATGCCTGCATCGTGCGCATCGGTGGCGAGGAGGGCGGCCGGCCACCTGAAGCTGACGAC
CCTGTGCCTGGGGGCCAGGCCAGGAACGGAGCTGGCGGGGGCCCAAGGGGCCAGACGCCC
AACCATAATCAGCAGGACGGGGATTCAGGGAGCCTGGGCAGCCCCTCGGCCTCCCGGGAG
TCCCTGGTGAAGGGGCGAGCTGGGCCAGACACCAGTGCCAGCGGGGAGCCAGGTGCCAAC
AGCAAGCTCCTGTACAAGGCCTCGGTGGTGAAGAAGGCGGCTGCACGCAGGAGGCGGCAC
CCCGACGAGGCCTTCGACCATGAGGTCTCCGCCTTCTTCCCCGCCAACCTGGACTTCCTG
TGCCTGCAGGAGGTGTTTGACAAGCGAGCAGCCACCAAATTGAAAGAGCAGCTGCACGGC
TACTTCGAGTACATCCTGTACGACGTCGGGGTCTACGGCTGCCAGGGCTGCTGCAGCTTC
AAGTGTCTCAACAGCGGCCTCCTCTTTGCCAGCCGCTACCCCATCATGGACGTGGCCTAT
CACTGTTACCCCAACAAGTGTAACGACGATGCCCTGGCCTCTAAGGGAGCTCTGTTTCTC
AAGGTGCAGGTGGGAAGCACACCTCAGGACCAAAGAATCGTCGGGTACATCGCCTGCACA
CACCTGCATGCCCCACAAGAGGACAGCGCCATCCGGTGTGGGCAGCTGGACCTGCTTCAG
GACTGGCTGGCTGATTTCCGAAAATCTACCTCCTCGTCCAGCGCAGCCAACCCCGAGGAG
CTGGTGGCATTTGACGTCGTCTGTGGAGATTTCAACTTTGATAACTGCTCCTCTGACGAC
AAGCTGGAGCAGCAACACTCCCTGTTCACCCACTACAGGGACCCCTGCCGCCTGGGGCCT
GGTGAGGAGAAGCCGTGGGCCATCGGTACTCTGCTGGACACGAACGGCCTGTACGATGAG
GATGTGTGCACCCCCGACAACCTGCAGAAGGTCCTGGAGAGTGAGGAGGGCCGCAGGGAG
TACCTGGCGTTTCCCACCAGCAAGAGCTCGGGCCAGAAGGGGCGGAAGGAGCTGCTGAAG
GGCAACGGCCGGCGCATCGACTACATGCTGCATGCAGAGGAGGGGCTGTGCCCAGACTGG
AAGGCCGAGGTGGAAGAATTCAGTTTTATCACCCAGCTGTCCGGCCTGACGGACCACCTG
CCAGTAGCCATGCGACTGATGGTGTCTTCGGGGGAGGAGGAGGCATAG
|
| Enzyme 25 GenBank Gene ID |
AJ250460  |
| Enzyme 25 GeneCard ID |
SMPD3  |
| Enzyme 25 GenAtlas ID |
SMPD3  |
| Enzyme 25 HGNC ID |
HGNC:14240  |
| Enzyme 25 Chromosome Location |
1 |
| Enzyme 25 Locus |
16q22.1 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Hofmann K, Tomiuk S, Wolff G, Stoffel W: Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5895-900. [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
]
- Miura Y, Gotoh E, Nara F, Nishijima M, Hanada K: Hydrolysis of sphingosylphosphocholine by neutral sphingomyelinases. FEBS Lett. 2004 Jan 16;557(1-3):288-92. [PubMed
]
- Marchesini N, Osta W, Bielawski J, Luberto C, Obeid LM, Hannun YA: Role for mammalian neutral sphingomyelinase 2 in confluence-induced growth arrest of MCF7 cells. J Biol Chem. 2004 Jun 11;279(24):25101-11. Epub 2004 Mar 29. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
12558 |
| Enzyme 26 Name |
Beta-1,3-galactosyltransferase 5 |
| Enzyme 26 Synonyms |
- Beta-1,3-GalTase 5
- Beta3Gal-T5
- Beta3GalT5
- b3Gal-T5
- Beta-3-Gx-T5
- UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5
- UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5
|
| Enzyme 26 Gene Name |
B3GALT5 |
| Enzyme 26 Protein Sequence |
>Beta-1,3-galactosyltransferase 5
MAFPKMRLMYICLLVLGALCLYFSMYSLNPFKEQSFVYKKDGNFLKLPDTDCRQTPPFLV
LLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVDQESQRHGDII
QKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFF
TGFLKLNEFPIRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIK
LEDVFVGLCLERLNIRLEELHSQPTFFPGGLRFSVCLFRRIVACHFIKPRTLLDYWQALE
NSRGEDCPPV
|
| Enzyme 26 Number of Residues |
310 |
| Enzyme 26 Molecular Weight |
36188.9 |
| Enzyme 26 Theoretical pI |
9.02 |
| Enzyme 26 GO Classification |
| Function |
- catalytic activity
- galactosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid glycosylation
- protein modification process
|
| Component |
|
|
| Enzyme 26 General Function |
Involved in galactosyltransferase activity |
| Enzyme 26 Specific Function |
Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
4835503  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q9Y2C3  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
B3GT5_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>933 bp
ATGGCTTTCCCGAAGATGAGATTGATGTATATTTGCCTTCTGGTTCTGGGGGCTCTTTGT
TTGTATTTTAGCATGTACAGTCTAAATCCTTTCAAAGAACAGTCCTTTGTTTACAAGAAA
GACGGGAACTTCCTTAAGCTCCCAGATACAGACTGCAGGCAGACACCTCCCTTCCTCGTC
CTGCTGGTGACCTCATCCCACAAACAGTTGGCTGAGCGCATGGCCATCCGGCAGACGTGG
GGGAAAGAGAGGATGGTGAAGGGAAAGCAGCTGAAGACATTCTTCCTCCTGGGGACCACC
AGCAGTGCAGCGGAAACGAAAGAGGTGGACCAGGAGAGCCAGCGACACGGGGACATTATC
CAGAAGGATTTCCTAGACGTCTATTACAATCTGACCCTGAAGACCATGATGGGCATAGAA
TGGGTCCATCGCTTTTGTCCTCAGGCGGCGTTTGTGATGAAAACAGACTCAGACATGTTC
ATCAATGTTGACTATCTGACTGAACTGCTTCTGAAGAAAAACAGAACAACCAGGTTTTTC
ACTGGCTTCTTGAAACTCAATGAGTTTCCCATCAGGCAGCCATTCAGCAAGTGGTTTGTC
AGTAAATCTGAATATCCGTGGGACAGGTACCCACCATTCTGCTCCGGCACCGGCTACGTG
TTTTCTGGCGACGTGGCGAGTCAGGTGTACAATGTCTCCAAGAGCGTCCCATACATTAAA
CTGGAAGACGTGTTTGTGGGGCTCTGCCTCGAAAGGCTGAACATCAGATTGGAGGAGCTC
CACTCCCAGCCGACCTTTTTTCCAGGGGGCTTACGCTTCTCCGTATGCCTCTTCAGGAGG
ATCGTGGCCTGCCACTTCATCAAGCCTCGGACTCTCTTGGACTACTGGCAGGCTCTAGAG
AATTCCCGGGGGGAAGATTGTCCGCCTGTCTGA
|
| Enzyme 26 GenBank Gene ID |
AB020337  |
| Enzyme 26 GeneCard ID |
B3GALT5  |
| Enzyme 26 GenAtlas ID |
B3GALT5  |
| Enzyme 26 HGNC ID |
HGNC:920  |
| Enzyme 26 Chromosome Location |
2 |
| Enzyme 26 Locus |
21q22.3 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Isshiki S, Togayachi A, Kudo T, Nishihara S, Watanabe M, Kubota T, Kitajima M, Shiraishi N, Sasaki K, Andoh T, Narimatsu H: Cloning, expression, and characterization of a novel UDP-galactose:beta-N-acetylglucosamine beta1,3-galactosyltransferase (beta3Gal-T5) responsible for synthesis of type 1 chain in colorectal and pancreatic epithelia and tumor cells derived therefrom. J Biol Chem. 1999 Apr 30;274(18):12499-507. [PubMed
]
- Zhou D, Berger EG, Hennet T: Molecular cloning of a human UDP-galactose:GlcNAcbeta1,3GalNAc beta1, 3 galactosyltransferase gene encoding an O-linked core3-elongation enzyme. Eur J Biochem. 1999 Jul;263(2):571-6. [PubMed
]
- Dunn CA, Medstrand P, Mager DL: An endogenous retroviral long terminal repeat is the dominant promoter for human beta1,3-galactosyltransferase 5 in the colon. Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12841-6. Epub 2003 Oct 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
]
- Hattori M, Fujiyama A, Taylor TD, Watanabe H, Yada T, Park HS, Toyoda A, Ishii K, Totoki Y, Choi DK, Groner Y, Soeda E, Ohki M, Takagi T, Sakaki Y, Taudien S, Blechschmidt K, Polley A, Menzel U, Delabar J, Kumpf K, Lehmann R, Patterson D, Reichwald K, Rump A, Schillhabel M, Schudy A, Zimmermann W, Rosenthal A, Kudoh J, Schibuya K, Kawasaki K, Asakawa S, Shintani A, Sasaki T, Nagamine K, Mitsuyama S, Antonarakis SE, Minoshima S, Shimizu N, Nordsiek G, Hornischer K, Brant P, Scharfe M, Schon O, Desario A, Reichelt J, Kauer G, Blocker H, Ramser J, Beck A, Klages S, Hennig S, Riesselmann L, Dagand E, Haaf T, Wehrmeyer S, Borzym K, Gardiner K, Nizetic D, Francis F, Lehrach H, Reinhardt R, Yaspo ML: The DNA sequence of human chromosome 21. Nature. 2000 May 18;405(6784):311-9. [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
]
- Amado M, Almeida R, Schwientek T, Clausen H: Identification and characterization of large galactosyltransferase gene families: galactosyltransferases for all functions. Biochim Biophys Acta. 1999 Dec 6;1473(1):35-53. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
12947 |
| Enzyme 27 Name |
GPI mannosyltransferase 3 |
| Enzyme 27 Synonyms |
- GPI mannosyltransferase III
- GPI-MT-III
- Phosphatidylinositol-glycan biosynthesis class B protein
- PIG-B
|
| Enzyme 27 Gene Name |
PIGB |
| Enzyme 27 Protein Sequence |
>GPI mannosyltransferase 3
MRRPLSKCGMEPGGGDASLTLHGLQNRSHGKIKLRKRKSTLYFNTQEKSARRRGDLLGEN
IYLLLFTIALRILNCFLVQTSFVPDEYWQSLEVSHHMVFNYGYLTWEWTERLRSYTYPLI
FASIYKILHLLGKDSVQLLIWIPRLAQALLSAVADVRLYSLMKQLENQEVARWVFFCQLC
SWFTWYCCTRTLTNTMETVLTIIALFYYPLEGSKSMNSVKYSSLVALAFIIRPTAVILWT
PLLFRHFCQEPRKLDLILHHFLPVGFVTLSLSLMIDRIFFGQWTLVQFNFLKFNVLQNWG
TFYGSHPWHWYFSQGFPVILGTHLPFFIHGCYLAPKRYRILLVTVLWTLLVYSMLSHKEF
RFIYPVLPFCMVFCGYSLTHLKTWKKPALSFLFLSNLFLALYTGLVHQRGTLDVMSHIQK
VCYNNPNKSSASIFIMMPCHSTPYYSHVHCPLPMRFLQCPPDLTGKSHYLDEADVFYLNP
LNWLHREFHDDASLPTHLITFSILEEEISAFLISSNYKRTAVFFHTHLPEGRIGSHIYVY
ERKLKGKFNMKMKF
|
| Enzyme 27 Number of Residues |
554 |
| Enzyme 27 Molecular Weight |
65055.9 |
| Enzyme 27 Theoretical pI |
9.57 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- intrinsic to endoplasmic reticulum membrane
- intrinsic to membrane
- intrinsic to organelle membrane
- membrane part
|
|
| Enzyme 27 General Function |
Involved in transferase activity, transferring glycosyl groups |
| Enzyme 27 Specific Function |
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the third alpha-1,2-mannose to Man2-GlcN-acyl-PI during GPI precursor assembly |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
- 63-83
136-156
192-212
224-244
255-275
315-335
340-360
362-382
387-407
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
62898221  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q92521  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
PIGB_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1665 bp
ATGAGGAGGCCCCTAAGCAAGTGCGGAATGGAGCCGGGGGGCGGAGATGCCAGCCTCACT
TTGCATGGTCTCCAGAACCGCTCCCACGGCAAGATAAAGCTGCGAAAGAGAAAGTCTACC
TTGTACTTCAACACCCAGGAGAAGAGCGCCAGGCGCCGCGGGGATCTTCTTGGAGAAAAT
ATTTATCTGCTCTTGTTTACCATAGCTTTACGAATATTAAACTGCTTTTTAGTGCAGACA
AGTTTTGTTCCAGATGAATACTGGCAGTCTCTTGAAGTTTCACATCACATGGTTTTCAAT
TATGGTTATTTGACTTGGGAATGGACAGAGAGACTGAGGAGTTACACTTATCCCTTAATC
TTTGCAAGCATTTACAAGATTCTTCATCTTTTAGGGAAAGATAGTGTTCAGTTGCTGATT
TGGATTCCTAGACTTGCCCAAGCACTTCTGTCTGCTGTAGCAGATGTGAGACTTTACTCA
TTAATGAAGCAACTAGAAAATCAGGAAGTGGCAAGATGGGTGTTTTTTTGCCAGTTGTGC
TCCTGGTTCACATGGTATTGCTGTACCAGAACCCTTACAAACACCATGGAAATTGTTCTC
ACTATAATTGCTCTTTTCTACTATCCTTTGGAAGGTTCAAAGTCTATGAACAGTGTCAAA
TACTCATCCCTGGTGGCACTTGCCTTCATAATTCGTCCCACAGCTGTCATTCTGTGGACA
CCTTTGCTCTTCAGACATTTCTGTCAAGAACCAAGAAAGCTTGATCTTATTCTACATCAT
TTTTTACCTGTAGGCTTTGTTACTTTGAGTTTGTCTCTGATGATTGATCGTATTTTTTTT
GGCCAATGGACTCTGGTTCAATTTAATTTTTTGAAATTTAACGTGCTGCAGAACTTGGGA
ACATTTTATGGTTCTCATCCATGGCACTGGTACTTCAGTCAAGGATTTCCAGTTATCTTG
GGTACTCACTTACCCTTCTTTATTCATGGCTGCTATCTAGCACCAAAGAGATACCGGATA
CTTTTGGTGACTGTGCTGTGGACACTGCTTGTTTATAGCATGTTGAGCCACAAAGAATTC
AGGTTTATTTATCCAGTTTTACCATTCTGTATGGTGTTCTGTGGATACTCATTAACCCAC
CTGAAAACATGGAAGAAACCAGCTCTAAGTTTCCTGTTTTTATCAAATTTGTTCCTCGCC
CTTTATACTGGTTTAGTTCATCAACGAGGTACTCTTGATGTCATGAGTCATATTCAAAAA
GTTTGTTACAACAATCCCAATAAATCTTCAGCTTCAATATTTATAATGATGCCTTGCCAC
TCTACTCCTTATTACAGCCATGTTCACTGCCCACTTCCCATGAGATTTCTCCAGTGCCCG
CCAGACCTGACTGGAAAAAGTCATTATCTTGATGAAGCAGATGTATTTTACCTAAATCCC
TTAAACTGGTTACATAGAGAGTTTCATGATGATGCATCATTGCCTACTCACTTGATCACC
TTCAGCATTTTGGAAGAGGAAATAAGCGCTTTCCTAATTTCAAGCAATTATAAAAGAACT
GCTGTTTTCTTCCACACTCACTTGCCAGAGGGTCGAATTGGAAGTCACATATATGTCTAT
GAACGGAAGTTAAAAGGGAAATTCAACATGAAGATGAAATTCTGA
|
| Enzyme 27 GenBank Gene ID |
AK223330  |
| Enzyme 27 GeneCard ID |
PIGB  |
| Enzyme 27 GenAtlas ID |
PIGB  |
| Enzyme 27 HGNC ID |
HGNC:8959  |
| Enzyme 27 Chromosome Location |
1 |
| Enzyme 27 Locus |
15q21-q22 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Takahashi M, Inoue N, Ohishi K, Maeda Y, Nakamura N, Endo Y, Fujita T, Takeda J, Kinoshita T: PIG-B, a membrane protein of the endoplasmic reticulum with a large lumenal domain, is involved in transferring the third mannose of the GPI anchor. EMBO J. 1996 Aug 15;15(16):4254-61. [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
]
- Mohney RP, Knez JJ, Ravi L, Sevlever D, Rosenberry TL, Hirose S, Medof ME: Glycoinositol phospholipid anchor-defective K562 mutants with biochemical lesions distinct from those in Thy-1- murine lymphoma mutants. J Biol Chem. 1994 Mar 4;269(9):6536-42. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
12948 |
| Enzyme 28 Name |
Phosphatidylinositol-glycan biosynthesis class F protein |
| Enzyme 28 Synonyms |
- PIG-F
- GPI11 homolog
|
| Enzyme 28 Gene Name |
PIGF |
| Enzyme 28 Protein Sequence |
>Phosphatidylinositol-glycan biosynthesis class F protein
MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYL
VVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILS
TFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERP
WQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
|
| Enzyme 28 Number of Residues |
219 |
| Enzyme 28 Molecular Weight |
24889.3 |
| Enzyme 28 Theoretical pI |
8.64 |
| Enzyme 28 GO Classification |
| Function |
| — |
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
- organelle membrane
|
|
| Enzyme 28 General Function |
Involved in GPI anchor biosynthetic process |
| Enzyme 28 Specific Function |
Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
- 11-31
42-62
86-106
113-133
155-175
189-209
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
4505797  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q07326  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
PIGF_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>660 bp
ATGAAAGATAACGATATCAAGAGACTACTGTATACCCATCTTTTATGCATATTTTCAATT
ATCCTAAGTGTCTTCATTCCATCACTCTTCTTGGAGAACTTCTCAATATTGGAAACACAC
TTGACATGGTTGTGCATCTGTTCTGGTTTTGTAACTGCTGTCAATCTAGTACTATATTTA
GTAGTGAAACCAAATACATCCTCTAAAAGAAGTTCATTATCACACAAGGTAACTGGATTT
TTGAAATGCTGTATCTACTTTCTTATGTCTTGTTTCTCCTTTCATGTAATTTTTGTTCTG
TATGGAGCACCACTGATAGAGTTGGCATTGGAAACATTTTTATTTGCAGTTATTTTGTCT
ACTTTTACTACTGTGCCTTGCTTATGTTTGTTAGGACCAAACCTCAAAGCATGGCTAAGA
GTGTTCAGTAGAAATGGAGTTACATCCATATGGGAGAATAGTCTCCAGATCACTACAATT
TCTAGCTTTGTAGGAGCATGGCTTGGAGCACTTCCTATTCCACTGGATTGGGAAAGACCA
TGGCAGGTATGGCCCATCTCCTGTACGCTTGGAGCGACCTTTGGCTACGTGGCTGGCCTT
GTTATTTCACCACTCTGGATATACTGGAATAGAAAGCAACTTACATACAAGAACAATTAA
|
| Enzyme 28 GenBank Gene ID |
NM_002643.3  |
| Enzyme 28 GeneCard ID |
PIGF  |
| Enzyme 28 GenAtlas ID |
PIGF  |
| Enzyme 28 HGNC ID |
HGNC:8962  |
| Enzyme 28 Chromosome Location |
2 |
| Enzyme 28 Locus |
2p21-p16 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Inoue N, Kinoshita T, Orii T, Takeda J: Cloning of a human gene, PIG-F, a component of glycosylphosphatidylinositol anchor biosynthesis, by a novel expression cloning strategy. J Biol Chem. 1993 Apr 5;268(10):6882-5. [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
]
- Shishioh N, Hong Y, Ohishi K, Ashida H, Maeda Y, Kinoshita T: GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9728-34. Epub 2005 Jan 4. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
12949 |
| Enzyme 29 Name |
GPI ethanolamine phosphate transferase 2 |
| Enzyme 29 Synonyms |
- GPI7 homolog
- hGPI7
- Phosphatidylinositol-glycan biosynthesis class G protein
- PIG-G
|
| Enzyme 29 Gene Name |
PIGG |
| Enzyme 29 Protein Sequence |
>GPI ethanolamine phosphate transferase 2
MRLGSGTFATCCVAIEVLGIAVFLRGFFPAPVRSSARAEHGAEPPAPEPSAGASSNWTTL
PPPLFSKVVIVLIDALRDDFVFGSKGVKFMPYTTYLVEKGASHSFVAEAKPPTVTMPRIK
ALMTGSLPGFVDVIRNLNSPALLEDSVIRQAKAAGKRIVFYGDETWVKLFPKHFVEYDGT
TSFFVSDYTEVDNNVTRHLDKVLKRGDWDILILHYLGLDHIGHISGPNSPLIGQKLSEMD
SVLMKIHTSLQSKERETPLPNLLVLCGDHGMSETGSHGASSTEEVNTPLILISSAFERKP
GDIRHPKHVQQTDVAATLAIALGLPIPKDSVGSLLFPVVEGRPMREQLRFLHLNTVQLSK
LLQENVPSYEKDPGFEQFKMSERLHGNWIRLYLEEKHSEVLFNLGSKVLRQYLDALKTLS
LSLSAQVAQYDIYSMMVGTVVVLEVLTLLLLSVPQALRRKAELEVPLSSPGFSLLFYLVI
LVLSAVHVIVCTSAESSCYFCGLSWLAAGGVMVLASALLCVIVSVLTNVLVGGNTPRKNP
MHPSSRWSELDLLILLGTAGHVLSLGASSFVEEEHQTWYFLVNTLCLALSQETYRNYFLG
DDGEPPCGLCVEQGHDGATAAWQDGPGCDVLERDKGHGSPSTSEVLRGREKWMVLASPWL
ILACCRLLRSLNQTGVQWAHRPDLGHWLTSSDHKAELSVLAALSLLVVFVLVQRGCSPVS
KAALALGLLGVYCYRAAIGSVRFPWRPDSKDISKGIIEARFVYVFVLGILFTGTKDLLKS
QVIAADFKLKTVGLWEIYSGLVLLAALLFRPHNLPVLAFSLLIQTLMTKFIWKPLRHDAA
EITVMHYWFGQAFFYFQGNSNNIATVDISAGFVGLDTYVEIPAVLLTAFGTYAGPVLWAS
HLVHFLSSETRSGSALSHACFCYALICSIPVFTYIVLVTSLRYHLFIWSVFSPKLLYEGM
HLLITAAVCVFFTAMDQTRLTQS
|
| Enzyme 29 Number of Residues |
983 |
| Enzyme 29 Molecular Weight |
108171.7 |
| Enzyme 29 Theoretical pI |
7.15 |
| Enzyme 29 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 29 General Function |
Involved in catalytic activity |
| Enzyme 29 Specific Function |
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
- 432-452
471-491
506-526
552-572
699-719
721-741
752-772
789-809
812-832
879-899
919-939
955-975
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
58430451  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q5H8A4  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
PIGG_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>2952 bp
ATGCGGCTGGGCTCCGGGACTTTCGCTACCTGTTGCGTAGCGATCGAGGTGCTAGGGATC
GCGGTCTTCCTTCGGGGATTCTTCCCGGCTCCCGTTCGTTCCTCTGCCAGAGCGGAACAC
GGAGCGGAGCCCCCAGCGCCCGAACCCTCGGCTGGAGCCAGTTCTAACTGGACCACGCTG
CCACCACCTCTCTTCAGTAAAGTTGTTATTGTTCTGATAGATGCCTTGAGAGATGATTTT
GTGTTTGGGTCAAAGGGTGTGAAATTTATGCCCTACACAACTTACCTTGTGGAAAAAGGA
GCATCTCACAGTTTTGTGGCTGAAGCAAAGCCACCTACAGTTACTATGCCTCGAATCAAG
GCATTGATGACGGGGAGCCTTCCTGGCTTTGTCGACGTCATCAGGAACCTCAATTCTCCT
GCACTGCTGGAAGACAGTGTGATAAGACAAGCAAAAGCAGCTGGAAAAAGAATAGTCTTT
TATGGAGATGAAACCTGGGTTAAATTATTCCCAAAGCATTTTGTGGAATATGATGGAACA
ACCTCATTTTTCGTGTCAGATTACACAGAGGTGGATAATAATGTCACGAGGCATTTGGAT
AAAGTATTAAAAAGAGGAGATTGGGACATATTAATCCTCCACTACCTGGGGCTGGACCAC
ATTGGCCACATTTCAGGGCCCAACAGCCCCCTGATTGGGCAGAAGCTGAGCGAGATGGAC
AGCGTGCTGATGAAGATCCACACCTCACTGCAGTCGAAGGAGAGAGAGACGCCTTTACCC
AATTTGCTGGTTCTTTGTGGTGACCATGGCATGTCTGAAACAGGAAGTCACGGGGCCTCC
TCCACCGAGGAGGTGAATACACCTCTGATTTTAATCAGTTCTGCGTTTGAAAGGAAACCC
GGTGATATCCGACATCCAAAGCACGTCCAACAGACGGATGTGGCTGCGACACTGGCGATA
GCACTTGGCTTACCGATTCCAAAAGACAGTGTAGGGAGCCTCCTATTCCCAGTTGTGGAA
GGAAGACCAATGAGAGAGCAGTTGAGATTTTTACATTTGAATACAGTGCAGCTTAGTAAA
CTGTTGCAAGAGAATGTGCCGTCATATGAAAAAGATCCTGGGTTTGAGCAGTTTAAAATG
TCAGAAAGATTGCATGGGAACTGGATCAGACTGTACTTGGAGGAAAAGCATTCAGAAGTC
CTATTCAACCTGGGCTCCAAGGTTCTCAGGCAGTACCTGGATGCTCTGAAGACGCTGAGC
TTGTCCCTGAGTGCACAAGTGGCCCAGTACGACATCTATTCGATGATGGTGGGGACTGTC
GTGGTTTTGGAGGTTCTCACCCTGCTCCTGCTCAGCGTCCCACAGGCACTGCGCAGAAAG
GCTGAGCTGGAAGTCCCACTGTCATCTCCTGGGTTTTCTCTGCTCTTTTATTTGGTGATC
CTGGTTCTTTCGGCCGTTCACGTCATTGTGTGCACCTCAGCTGAAAGTTCGTGCTACTTC
TGTGGCCTCTCGTGGCTGGCGGCAGGTGGGGTGATGGTGCTGGCCTCGGCGCTGCTGTGT
GTGATTGTGTCTGTTCTGACCAACGTGCTCGTGGGTGGAAACACCCCAAGGAAGAACCCC
ATGCATCCCAGCTCAAGGTGGTCAGAGCTAGACCTTCTTATTCTGTTGGGGACGGCGGGC
CACGTCTTGAGCCTGGGCGCCAGCAGCTTCGTGGAGGAGGAGCACCAGACCTGGTACTTC
CTTGTGAACACCCTGTGTCTAGCTCTGAGCCAAGAAACCTACAGAAACTACTTTCTGGGA
GATGACGGTGAGCCTCCGTGTGGCCTCTGTGTGGAACAAGGGCATGACGGGGCCACAGCA
GCGTGGCAGGACGGGCCTGGCTGTGATGTCCTGGAGCGAGACAAAGGCCACGGAAGCCCC
TCTACCTCCGAAGTGCTCAGAGGCCGCGAGAAGTGGATGGTGCTGGCCAGTCCGTGGCTA
ATACTGGCCTGCTGCCGGCTGCTGCGCTCCCTAAACCAGACAGGTGTGCAGTGGGCTCAC
CGGCCTGACCTCGGCCACTGGCTCACCAGCTCTGACCACAAAGCCGAGCTCTCTGTCCTG
GCTGCCCTCTCCCTCCTCGTAGTTTTTGTGCTGGTGCAGAGGGGGTGCTCCCCTGTGTCC
AAGGCTGCCCTGGCGCTGGGGCTGCTGGGCGTCTACTGCTACCGGGCGGCCATCGGGAGT
GTCCGGTTCCCGTGGCGGCCGGACAGCAAGGACATTTCCAAGGGTATTATTGAAGCTCGT
TTTGTTTATGTCTTTGTCCTTGGCATTCTGTTCACGGGCACCAAAGACTTACTTAAATCT
CAAGTCATTGCTGCAGACTTCAAACTCAAGACTGTAGGTTTATGGGAGATATATAGTGGA
TTAGTTCTTCTGGCAGCCTTGCTCTTTAGACCACATAATCTTCCGGTCTTAGCATTTAGC
CTCTTGATTCAGACTCTAATGACTAAATTCATCTGGAAGCCCCTGAGACACGATGCAGCT
GAGATTACTGTGATGCATTATTGGTTTGGTCAAGCATTCTTCTATTTTCAGGGCAACTCC
AACAACATTGCCACCGTGGACATCTCCGCAGGCTTCGTGGGCTTAGACACCTACGTGGAA
ATCCCAGCCGTGCTCCTGACAGCGTTTGGGACGTACGCAGGGCCTGTGCTGTGGGCCAGC
CACTTAGTGCACTTCCTGAGCTCAGAAACACGCAGTGGTTCAGCACTGAGTCATGCTTGC
TTCTGCTACGCACTGATTTGTTCTATTCCAGTTTTCACGTACATCGTTTTGGTGACATCT
CTGCGTTATCATTTATTTATATGGAGTGTATTTTCTCCAAAACTTCTCTACGAGGGAATG
CACCTGCTCATTACAGCTGCTGTCTGTGTATTCTTCACGGCAATGGATCAAACCAGACTC
ACACAGTCTTAG
|
| Enzyme 29 GenBank Gene ID |
AB162713  |
| Enzyme 29 GeneCard ID |
PIGG  |
| Enzyme 29 GenAtlas ID |
PIGG  |
| Enzyme 29 HGNC ID |
HGNC:25985  |
| Enzyme 29 Chromosome Location |
4 |
| Enzyme 29 Locus |
4p16.3 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Shishioh N, Hong Y, Ohishi K, Ashida H, Maeda Y, Kinoshita T: GPI7 is the second partner of PIG-F and involved in modification of glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9728-34. Epub 2005 Jan 4. [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
]
- 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
]
- 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 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
12950 |
| Enzyme 30 Name |
GPI ethanolamine phosphate transferase 1 |
| Enzyme 30 Synonyms |
- MCD4 homolog
- Phosphatidylinositol-glycan biosynthesis class N protein
- PIG-N
|
| Enzyme 30 Gene Name |
PIGN |
| Enzyme 30 Protein Sequence |
>GPI ethanolamine phosphate transferase 1
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALY
ELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENP
VEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFD
NVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKE
IVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQ
FDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESM
FTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSL
CKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKP
SHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYP
LSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSL
LLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLST
VLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMST
YLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLY
LDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFV
LVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMS
MTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
|
| Enzyme 30 Number of Residues |
931 |
| Enzyme 30 Molecular Weight |
105809.2 |
| Enzyme 30 Theoretical pI |
8.87 |
| Enzyme 30 GO Classification |
| Function |
- catalytic activity
- transferase activity
|
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- membrane
- organelle membrane
|
|
| Enzyme 30 General Function |
Involved in catalytic activity |
| Enzyme 30 Specific Function |
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
- 2-24
443-463
483-503
509-529
544-564
566-586
592-612
619-639
650-670
686-706
724-744
787-807
825-845
859-879
895-915
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
4206155  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
O95427  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
PIGN_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>2796 bp
ATGCTGCTGTTCTTTACTTTGGGATTGCTTATACATTTTGTGTTCTTCGCCTCCATCTTT
GACATTTATTTTACATCTCCTTTGGTTCATGGAATGACTCCTCAGTTTACACCATTGCCT
CCTCCAGCGAGAAGATTAGTGTTGTTTGTTGCTGATGGCCTTCGAGCAGATGCACTTTAC
GAATTAGATGAAAATGGAAACTCTAGAGCACCGTTTATTAGGAATATCATAATGCATGAA
GGCAGCTGGGGCATATCTCATACACGTGTGCCAACAGAATCTCGGCCAGGTCATGTAGCT
CTGATAGCTGGGTTTTATGAAGATGTCAGTGCAGTTGCCAAAGGATGGAAGGAAAATCCT
GTAGAGTTTGATTCTCTTTTTAATGAAAGTAAATACACATGGAGCTGGGGAAGCCCAGAT
ATCCTGCCTATGTTTGCCAAAGGTGCTAGTGGAGACCACGTTTATACATATAGTTATGAT
GCTAAAAGAGAGGATTTTGGTGCTCAAGATGCAACAAAACTGGATACGTGGGTTTTTGAT
AATGTTAAGGACTTCTTTCATCATGCCAGAAACAACCAGTCTTTGTTTTCTAAAATAAAT
GAAGAGAAAATAGTTTTTTTCTTACATTTATTAGGAATAGATACAAACGGACATGCTCAT
CGACCATCCTCGAGAGACTACAAGCACAATATTAAAAAAGTTGATGATGGAGTTAAAGAA
ATCGTGTCTATGTTTAACCACTTCTATGGAAATGATGGGAAAACAACATTTATCTTTACC
TCTGACCATGGAATGACAGACTGGGGTTCCCATGGGGCTGGTCATCCTTCAGAGACTTTA
ACTCCTTTAGTCACTTGGGGAGCTGGAATCAAGTATCCCCAAAGAGTATCAGCTCAGCAA
TTTGATGATGCATTTTTGAAAGAGTGGAGATTGGAGAATTGGAAGAGGCTAGATGTCAAT
CAGGCTGATATTGCACCATTGATGACTTCCCTTATTGGAGTTCCCTTTCCTCTTAACTCA
GTGGGAATCCTTCCTGTGGATTATCTTAACAACACTGATCTCTTCAAAGCAGAGAGCATG
TTTACAAATGCAGTACAGATTCTTGAACAGTTCAAGGTGAAAATGACTCAGAAGAAAGAA
GTTACTTTACCATTTTTGTTTACACCATTTAAACTGCTTTCTGATTCCAAACAGTTCAAC
ATTTTAAGAAAAGCAAGATCTTATATAAAACACAGAAAGTTTGATGAAGTGGTCTCCCTT
TGCAAGGAGCTAATTCATCTTGCATTGAAAGGATTGTCCTATTATCACACATATGACAGA
TTCTTTTTGGGCGTCAATGTTGTTATTGGTTTTGTGGGATGGATATCTTATGCCTCTTTG
TTGATCATCAAGTCTCATTCCAACCTTATAAAAGGTGTTAGTAAAGAAGTGAAGAAACCA
AGCCATCTCCTGCCTTGTAGTTTTGTAGCTATTGGCATTTTAGTAGCATTTTTTCTGCTG
ATTCAAGCCTGTCCCTGGACATATTATGTATATGGTTTGTTGCCACTGCCAATATGGTAT
GCGGTTCTAAGAGAATTTCAAGTTATTCAGGACCTTGTTGTATCAGTGTTGACCTATCCT
CTGAGCCATTTTGTTGGGTACCTGTTAGCCTTTACCCTGGGAATTGAAGTATTAGTTCTC
AGTTTTTTCTACCGCTATATGCTTACCGCTGGACTTACTGCCTTTGCAGCTTGGCCATTT
CTCACTCGGCTGTGGACTCGAGCAAAGATGACCTCACTGAGTTGGACTTTCTTCTCTTTG
CTCCTGGCAGTGTTCCCACTGATGCCGGTTGTAGGTCGAAAGCCAGACATCTCTCTAGTG
ATGGGTGCAGGCTTGCTGGTTCTTCTGTTATCCCTGTGTGTTGTAACATCTCTCATGAAA
AGAAAAGATAGCTTTATAAAGGAAGAGCTATTGGTACATCTGTTACAGGTGCTGAGCACA
GTGCTCTCCATGTATGTTGTGTATAGCACTCAGAGTAGTTTACTCAGGAAGCAAGGACTG
CCTCTCATGAATCAAATTATTAGCTGGGCAACATTAGCCTCTTCCTTGGTTGTGCCACTA
CTGAGTTCTCCAGTTCTCTTTCAGCGATTGTTCAGCATACTTCTTTCATTGATGTCAACC
TACCTACTTCTAAGCACAGGGTATGAAGCTCTCTTTCCACTAGTGTTGTCTTGTTTGATG
TTTGTCTGGATAAACATAGAACAAGAAACTCTACAACAATCTGGTGTTTGCTGTAAACAA
AAGCTCACCAGTATCCAGTTCTCTTATAATACTGATATAACTCAGTTTCGACAGCTATAT
CTGGATGACATCCGTAGGGCCTTTTTCCTTGTTTTCTTCTTAGTGACAGCATTTTTTGGA
ACTGGAAATATAGCTTCTATTAACAGCTTTGATCTTGCCTCTGTCTATTGCTTTCTGACT
GTGTTCAGTCCTTTTATGATGGGAGCCCTGATGATGTGGAAGATTTTAATCCCCTTTGTT
CTTGTTATGTGTGCTTTTGAAGCAGTTCAGTTGACTACTCAGTTATCGTCAAAAAGCCTT
TTTCTCATTGTTCTCGTCATATCAGACATTATGGCTTTGCATTTTTTCTTCTTGGTCAAG
GATTATGGCAGCTGGCTTGATATTGGGACAAGCATCAGCCACTATGTGATTGTCATGTCC
ATGACCATCTTTTTGGTGTTCCTCAATGGCCTGGCCCAGCTGCTCACAACGAAGAAACTC
AGACTATGTGGCAAACCCAAAAGTCACTTCATGTGA
|
| Enzyme 30 GenBank Gene ID |
AF109219  |
| Enzyme 30 GeneCard ID |
PIGN  |
| Enzyme 30 GenAtlas ID |
PIGN  |
| Enzyme 30 HGNC ID |
HGNC:8967  |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
18q21.33 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Gaynor EC, Mondesert G, Grimme SJ, Reed SI, Orlean P, Emr SD: MCD4 encodes a conserved endoplasmic reticulum membrane protein essential for glycosylphosphatidylinositol anchor synthesis in yeast. Mol Biol Cell. 1999 Mar;10(3):627-48. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
12951 |
| Enzyme 31 Name |
GPI ethanolamine phosphate transferase 3 |
| Enzyme 31 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class O protein
- PIG-O
|
| Enzyme 31 Gene Name |
PIGO |
| Enzyme 31 Protein Sequence |
>GPI ethanolamine phosphate transferase 3
MQKASVLLFLAWVCFLFYAGIALFTSGFLLTRLELTNHSSCQEPPGPGSLPWGSQGKPGA
CWMASRFSRVVLVLIDALRFDFAQPQHSHVPREPPVSLPFLGKLSSLQRILEIQPHHARL
YRSQVDPPTTTMQRLKALTTGSLPTFIDAGSNFASHAIVEDNLIKQLTSAGRRVVFMGDD
TWKDLFPGAFSKAFFFPSFNVRDLDTVDNGILEHLYPTMDSGEWDVLIAHFLGVDHCGHK
HGPHHPEMAKKLSQMDQVIQGLVERLENDTLLVVAGDHGMTTNGDHGGDSELEVSAALFL
YSPTAVFPSTPPEEPEVIPQVSLVPTLALLLGLPIPFGNIGEVMAELFSGGEDSQPHSSA
LAQASALHLNAQQVSRFLHTYSAATQDLQAKELHQLQNLFSKASADYQWLLQSPKGAEAT
LPTVIAELQQFLRGARAMCIESWARFSLVRMAGGTALLAASCFICLLASQWAISPGFPFC
PLLLTPVAWGLVGAIAYAGLLGTIELKLDLVLLGAVAAVSSFLPFLWKAWAGWGSKRPLA
TLFPIPGPVLLLLLFRLAVFFSDSFVVAEARATPFLLGSFILLLVVQLHWEGQLLPPKLL
TMPRLGTSATTNPPRHNGAYALRLGIGLLLCTRLAGLFHRCPEETPVCHSSPWLSPLASM
VGGRAKNLWYGACVAALVALLAAVRLWLRRYGNLKSPEPPMLFVRWGLPLMALGTAAYWA
LASGADEAPPRLRVLVSGASMVLPRAVAGLAASGLALLLWKPVTVLVKAGAGAPRTRTVL
TPFSGPPTSQADLDYVVPQIYRHMQEEFRGRLERTKSQGPLTVAAYQLGSVYSAAMVTAL
TLLAFPLLLLHAERISLVFLLLFLQSFLLLHLLAAGIPVTTPGPFTVPWQAVSAWALMAT
QTFYSTGHQPVFPAIHWHAAFVGFPEGHGSCTWLPALLVGANTFASHLLFAVGCPLLLLW
PFLCESQGLRKRQQPPGNEADARVRPEEEEEPLMEMRLRDAPQHFYAALLQLGLKYLFIL
GIQILACALAASILRRHLMVWKVFAPKFIFEAVGFIVSSVGLLLGIALVMRVDGAVSSWF
RQLFLAQQR
|
| Enzyme 31 Number of Residues |
1089 |
| Enzyme 31 Molecular Weight |
118697.6 |
| Enzyme 31 Theoretical pI |
8.18 |
| Enzyme 31 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 31 General Function |
Involved in catalytic activity |
| Enzyme 31 Specific Function |
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
- 4-24
457-477
482-502
510-530
541-561
575-595
668-688
701-721
747-767
830-850
857-877
944-964
1014-1034
1048-1068
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
23397648  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
Q8TEQ8  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
PIGO_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>3270 bp
ATGCAGAAAGCCTCAGTGTTGCTCTTCCTGGCCTGGGTCTGCTTCCTCTTCTACGCTGGC
ATTGCCCTCTTCACCAGTGGCTTCCTGCTCACCCGTTTGGAGCTCACCAACCATAGCAGC
TGCCAAGAGCCCCCAGGCCCTGGGTCCCTGCCATGGGGGAGCCAAGGGAAACCTGGGGCC
TGCTGGATGGCTTCCCGATTTTCGCGGGTTGTGTTGGTGCTGATAGATGCTCTGCGATTT
GACTTCGCCCAGCCCCAGCATTCACACGTGCCTAGAGAGCCTCCTGTCTCCCTACCCTTC
CTGGGCAAACTAAGCTCCTTGCAGAGGATCCTGGAGATTCAGCCCCACCATGCCCGGCTC
TACCGATCTCAGGTTGACCCTCCTACCACCACCATGCAGCGCCTCAAGGCCCTCACCACT
GGCTCACTGCCTACCTTTATTGATGCTGGTAGTAACTTCGCCAGCCACGCCATAGTGGAA
GACAATCTCATTAAGCAGCTCACCAGTGCAGGAAGGCGTGTAGTCTTCATGGGAGATGAT
ACCTGGAAAGACCTTTTCCCTGGTGCTTTCTCCAAAGCTTTCTTCTTCCCATCCTTCAAT
GTCAGAGACCTAGACACAGTGGACAATGGCATCCTGGAACACCTCTACCCCACCATGGAC
AGTGGTGAATGGGACGTGCTGATTGCTCACTTCCTGGGTGTGGACCACTGTGGCCACAAG
CATGGCCCTCACCACCCTGAAATGGCCAAGAAACTTAGCCAGATGGACCAGGTGATCCAG
GGACTTGTGGAGCGTCTGGAGAATGACACACTGCTGGTAGTGGCTGGGGACCATGGGATG
ACCACAAATGGAGACCATGGAGGGGACAGTGAGCTGGAGGTCTCAGCTGCTCTCTTTCTG
TATAGCCCCACAGCAGTCTTCCCCAGCACCCCACCAGAGGAGCCAGAGGTGATTCCTCAA
GTTAGCCTTGTGCCCACGCTGGCCCTGCTGCTGGGCCTGCCCATCCCATTTGGGAATATC
GGGGAAGTGATGGCTGAGCTATTCTCAGGGGGTGAGGACTCCCAGCCCCACTCCTCTGCT
TTAGCCCAAGCCTCAGCTCTCCATCTCAATGCTCAGCAGGTGTCCCGATTTCTTCATACC
TACTCAGCTGCTACTCAGGACCTTCAAGCTAAGGAGCTTCATCAGCTGCAGAACCTCTTC
TCCAAGGCCTCTGCTGACTACCAGTGGCTTCTCCAGAGCCCCAAGGGGGCTGAGGCGACA
CTGCCGACTGTGATTGCTGAGCTGCAGCAGTTCCTGCGGGGAGCTCGGGCCATGTGCATC
GAGTCTTGGGCTCGTTTCTCTCTGGTCCGCATGGCGGGGGGTACTGCTCTCTTGGCTGCT
TCCTGCTTTATCTGCCTGCTGGCATCTCAGTGGGCAATATCCCCAGGCTTTCCATTCTGC
CCTCTACTCCTGACACCTGTGGCCTGGGGCCTGGTTGGGGCCATAGCGTATGCTGGACTC
CTGGGAACTATTGAGCTGAAGCTAGATCTAGTGCTTCTAGGGGCTGTGGCTGCAGTGAGC
TCATTCCTCCCTTTTCTGTGGAAAGCCTGGGCTGGCTGGGGGTCCAAGAGGCCCCTGGCA
ACCCTGTTTCCCATCCCTGGGCCCGTCCTGTTACTCCTGCTGTTTCGCTTGGCTGTGTTC
TTCTCTGATAGTTTTGTTGTAGCTGAGGCCAGGGCCACCCCCTTCCTTTTGGGCTCATTC
ATCCTGCTCCTGGTTGTCCAGCTTCACTGGGAGGGCCAGCTGCTTCCACCTAAGCTACTC
ACAATGCCCCGCCTTGGCACTTCAGCCACAACAAACCCCCCACGGCACAATGGTGCATAT
GCCCTGAGGCTTGGAATTGGGTTGCTTTTATGTACAAGGCTAGCTGGGCTTTTTCATCGT
TGCCCTGAAGAGACACCTGTTTGCCACTCCTCTCCCTGGCTGAGTCCTCTGGCATCCATG
GTGGGTGGTCGAGCCAAGAATTTGTGGTATGGAGCTTGTGTGGCGGCGCTGGTGGCCCTG
TTAGCTGCCGTGCGCTTGTGGCTTCGCCGCTATGGTAATCTCAAGAGCCCCGAGCCACCC
ATGCTCTTTGTGCGCTGGGGACTGCCCCTAATGGCATTGGGTACTGCTGCCTACTGGGCA
TTGGCGTCGGGGGCAGATGAGGCTCCCCCCCGTCTCCGGGTCCTGGTCTCTGGGGCATCC
ATGGTGCTGCCTCGGGCTGTAGCAGGGCTGGCTGCTTCAGGGCTCGCGCTGCTGCTCTGG
AAGCCTGTGACAGTGCTGGTGAAGGCTGGGGCAGGCGCTCCAAGGACCAGGACTGTCCTC
ACTCCCTTCTCAGGCCCCCCCACTTCTCAAGCTGACTTGGATTATGTGGTCCCTCAAATC
TACCGACACATGCAGGAGGAGTTCCGGGGCCGGTTAGAGAGGACCAAATCTCAGGGTCCC
CTGACTGTGGCTGCTTATCAGTTGGGGAGTGTCTACTCAGCTGCTATGGTCACAGCCCTC
ACCCTGTTGGCCTTCCCACTTCTGCTGTTGCATGCGGAGCGCATCAGCCTTGTGTTCCTG
CTTCTGTTTCTGCAGAGCTTCCTTCTCCTACATCTGCTTGCTGCTGGGATACCCGTCACC
ACCCCTGGTCCTTTTACTGTGCCATGGCAGGCAGTCTCGGCTTGGGCCCTCATGGCCACA
CAGACCTTCTACTCCACAGGCCACCAGCCTGTCTTTCCAGCCATCCATTGGCATGCAGCC
TTCGTGGGATTCCCAGAGGGTCATGGCTCCTGTACTTGGCTGCCTGCTTTGCTAGTGGGA
GCCAACACCTTTGCCTCCCACCTCCTCTTTGCAGTAGGTTGCCCACTGCTCCTGCTCTGG
CCTTTCCTGTGTGAGAGTCAAGGGCTGCGGAAGAGACAGCAGCCCCCAGGGAATGAAGCT
GATGCCAGAGTCAGACCCGAGGAGGAAGAGGAGCCACTGATGGAGATGCGGCTCCGGGAT
GCGCCTCAGCACTTCTATGCAGCACTGCTGCAGCTGGGCCTCAAGTACCTCTTTATCCTT
GGTATTCAGATTCTGGCCTGTGCCTTGGCAGCCTCCATCCTTCGCAGGCATCTCATGGTC
TGGAAAGTGTTTGCCCCTAAGTTCATATTTGAGGCTGTGGGCTTCATTGTGAGCAGCGTG
GGACTTCTCCTGGGCATAGCTTTGGTGATGAGAGTGGATGGTGCTGTGAGCTCCTGGTTC
AGGCAGCTATTTCTGGCCCAGCAGAGGTAG
|
| Enzyme 31 GenBank Gene ID |
NM_032634.2  |
| Enzyme 31 GeneCard ID |
PIGO  |
| Enzyme 31 GenAtlas ID |
PIGO  |
| Enzyme 31 HGNC ID |
HGNC:23215  |
| Enzyme 31 Chromosome Location |
9 |
| Enzyme 31 Locus |
9p13.3 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 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
]
- 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
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Takeda S, Kadowaki S, Haga T, Takaesu H, Mitaku S: Identification of G protein-coupled receptor genes from the human genome sequence. FEBS Lett. 2002 Jun 5;520(1-3):97-101. [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 |
12952 |
| Enzyme 32 Name |
GPI transamidase component PIG-S |
| Enzyme 32 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class S protein
|
| Enzyme 32 Gene Name |
PIGS |
| Enzyme 32 Protein Sequence |
>GPI transamidase component PIG-S
MAAAGAAATHLEVARGKRAALFFAAVAIVLGLPLWWKTTETYRASLPYSQISGLNALQLR
LMVPVTVVFTRESVPLDDQEKLPFTVVHEREIPLKYKMKIKCRFQKAYRRALDHEEEALS
SGSVQEAEAMLDEPQEQAEGSLTVYVISEHSSLLPQDMMSYIGPKRTAVVRGIMHREAFN
IIGRRIVQVAQAMSLTEDVLAAALADHLPEDKWSAEKRRPLKSSLGYEITFSLLNPDPKS
HDVYWDIEGAVRRYVQPFLNALGAAGNFSVDSQILYYAMLGVNPRFDSASSSYYLDMHSL
PHVINPVESRLGSSAASLYPVLNFLLYVPELAHSPLYIQDKDGAPVATNAFHSPRWGGIM
VYNVDSKTYNASVLPVRVEVDMVRVMEVFLAQLRLLFGIAQPQLPPKCLLSGPTSEGLMT
WELDRLLWARSVENLATATTTLTSLAQLLGKISNIVIKDDVASEVYKAVAAVQKSAEELA
SGHLASAFVASQEAVTSSELAFFDPSLLHLLYFPDDQKFAIYIPLFLPMAVPILLSLVKI
FLETRKSWRKPEKTD
|
| Enzyme 32 Number of Residues |
555 |
| Enzyme 32 Molecular Weight |
61655.5 |
| Enzyme 32 Theoretical pI |
6.46 |
| Enzyme 32 GO Classification |
Not Available |
| Enzyme 32 General Function |
Involved in protein binding |
| Enzyme 32 Specific Function |
Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
14456613  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q96S52  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
PIGS_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1668 bp
ATGGCGGCCGCCGGGGCTGCGGCTACACACCTAGAGGTGGCCCGGGGCAAGCGCGCCGCC
CTCTTCTTCGCTGCGGTGGCCATCGTGCTGGGGCTACCGCTCTGGTGGAAGACCACGGAG
ACCTACCGGGCCTCGTTGCCTTACTCCCAGATCAGTGGCCTGAATGCCCTTCAGCTCCGC
CTCATGGTGCCTGTCACTGTCGTGTTTACGCGGGAGTCAGTGCCCCTGGACGACCAGGAG
AAGCTGCCCTTCACCGTTGTGCATGAAAGAGAGATTCCTCTGAAATACAAAATGAAAATC
AAATGCCGTTTCCAGAAGGCCTATCGGAGGGCTTTGGACCATGAGGAGGAGGCCCTGTCA
TCGGGCAGTGTGCAAGAGGCAGAAGCCATGTTAGATGAGCCTCAGGAACAAGCGGAGGGC
TCCCTGACTGTGTACGTGATATCTGAACACTCCTCACTTCTTCCCCAGGACATGATGAGC
TACATTGGGCCCAAGAGGACAGCAGTGGTGCGGGGGATAATGCACCGGGAGGCCTTTAAC
ATCATTGGCCGCCGCATAGTCCAGGTGGCCCAGGCCATGTCTTTGACTGAGGATGTGCTT
GCTGCTGCTCTGGCTGACCACCTTCCAGAGGACAAGTGGAGCGCTGAGAAGAGGCGGCCT
CTCAAGTCCAGCTTGGGCTATGAGATCACCTTCAGTTTACTCAACCCAGACCCCAAGTCC
CATGATGTCTACTGGGACATTGAGGGGGCTGTCCGGCGCTATGTGCAACCTTTCCTGAAT
GCCCTCGGTGCCGCTGGCAACTTCTCTGTGGACTCTCAGATTCTTTACTATGCAATGTTG
GGGGTGAATCCCCGCTTTGACTCAGCTTCCTCCAGCTACTATTTGGACATGCACAGCCTC
CCCCATGTCATCAACCCAGTGGAGTCCCGGCTGGGATCCAGTGCTGCCTCCTTGTACCCT
GTGCTCAACTTTCTACTCTACGTGCCTGAGCTTGCACACTCACCGCTGTACATTCAGGAC
AAGGATGGCGCTCCAGTGGCCACCAATGCCTTCCATAGTCCCCGCTGGGGTGGCATTATG
GTATATAATGTTGACTCCAAAACCTATAATGCCTCAGTGCTGCCAGTGAGAGTCGAGGTG
GACATGGTGCGAGTGATGGAGGTGTTCCTGGCACAGTTGCGGTTGCTCTTTGGGATTGCT
CAGCCCCAGCTGCCTCCAAAATGCCTGCTTTCAGGGCCTACGAGTGAAGGGCTAATGACC
TGGGAGCTAGACCGGCTGCTCTGGGCTCGGTCAGTGGAGAACCTGGCCACAGCCACCACC
ACCCTTACCTCCCTGGCGCAGCTTCTGGGCAAGATCAGCAACATTGTCATTAAGGACGAC
GTGGCATCTGAGGTGTACAAGGCTGTAGCTGCCGTCCAGAAGTCGGCAGAAGAGTTGGCG
TCTGGGCACCTGGCATCTGCCTTTGTCGCCAGCCAGGAAGCTGTGACATCCTCTGAGCTT
GCCTTCTTTGACCCGTCACTCCTCCACCTCCTTTATTTCCCTGATGACCAGAAGTTTGCC
ATCTACATCCCACTCTTCCTGCCTATGGCTGTGCCCATCCTCCTGTCCCTGGTCAAGATC
TTCCTGGAGACCCGCAAGTCCTGGAGAAAGCCTGAGAAGACAGACTGA
|
| Enzyme 32 GenBank Gene ID |
AB057723  |
| Enzyme 32 GeneCard ID |
PIGS  |
| Enzyme 32 GenAtlas ID |
PIGS  |
| Enzyme 32 HGNC ID |
HGNC:14937  |
| Enzyme 32 Chromosome Location |
1 |
| Enzyme 32 Locus |
17p13.2 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [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
]
- 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 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
12953 |
| Enzyme 33 Name |
GPI transamidase component PIG-T |
| Enzyme 33 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class T protein
|
| Enzyme 33 Gene Name |
PIGT |
| Enzyme 33 Protein Sequence |
>GPI transamidase component PIG-T
MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQR
EGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTV
TDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREV
VCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQ
TLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPP
TTTYQDVILGTRKTYAIYDLLDTAMINNSRNLNIQLKWKRPPENEAPPVPFLHAQRYVSG
YGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLYVHTLTITSKGKENKPSYIHYQPAQ
DRLQPHLLEMLIQLPANSVTKVSIQFERALLKWTEYTPDPNHGFYVSPSVLSALVPSMVA
AKPVDWEESPLFNSLFPVSDGSNYFVRLYTEPLLVNLPTPDFSMPYNVICLTCTVVAVCY
GSFYNLLTRTFHIEEPRTGGLAKRLANLIRRARGVPPL
|
| Enzyme 33 Number of Residues |
578 |
| Enzyme 33 Molecular Weight |
65699.0 |
| Enzyme 33 Theoretical pI |
8.49 |
| Enzyme 33 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
- GPI-anchor transamidase complex
- cell part
- integral to membrane
- intrinsic to membrane
- macromolecular complex
- membrane part
- protein complex
|
|
| Enzyme 33 General Function |
Involved in protein binding |
| Enzyme 33 Specific Function |
Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
14456615  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q969N2  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
PIGT_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1737 bp
ATGGCGGCGGCTATGCCGCTTGCTCTGCTCGTCCTGTTGCTCCTGGGGCCCGGCGGCTGG
TGCCTTGCAGAACCCCCACGCGACAGCCTGCGGGAGGAACTTGTCATCACCCCGCTGCCT
TCCGGGGACGTAGCCGCCACATTCCAGTTCCGCACGCGCTGGGATTCGGAGCTTCAGCGG
GAAGGAGTGTCCCATTACAGGCTCTTTCCCAAAGCCCTGGGGCAGCTGATCTCCAAGTAT
TCTCTACGGGAGCTGCACCTGTCATTCACACAAGGCTTTTGGAGGACCCGATACTGGGGG
CCACCCTTCCTGCAGGCCCCATCAGGTGCAGAGCTGTGGGTCTGGTTCCAAGACACTGTC
ACTGATGTGGATAAATCTTGGAAGGAGCTCAGTAATGTCCTCTCAGGGATCTTCTGCGCC
TCTCTCAACTTCATCGACTCCACCAACACAGTCACTCCCACTGCCTCCTTCAAACCCCTG
GGTCTGGCCAATGACACTGACCACTACTTTCTGCGCTATGCTGTGCTGCCGCGGGAGGTG
GTCTGCACCGAAAACCTCACCCCCTGGAAGAAGCTCTTGCCCTGTAGTTCCAAGGCAGGC
CTCTCTGTGCTGCTGAAGGCAGATCGCTTGTTCCACACCAGCTACCACTCCCAGGCAGTG
CATATCCGCCCTGTTTGCAGAAATGCACGCTGTACTAGCATCTCCTGGGAGCTGAGGCAG
ACCCTGTCAGTTGTATTTGATGCCTTCATCACGGGGCAGGGAAAGAAAGACTGGTCCCTC
TTCCGGATGTTCTCCCGAACCCTCACGGAGCCCTGCCCCCTGGCTTCAGAGAGCCGAGTC
TATGTGGACATCACCACCTACAACCAGGACAACGAGACATTAGAGGTGCACCCACCCCCG
ACCACTACATATCAGGACGTCATCCTAGGCACTCGGAAGACCTATGCCATCTATGACTTG
CTTGACACCGCCATGATCAACAACTCTCGAAACCTCAACATCCAGCTCAAGTGGAAGAGA
CCCCCAGAGAATGAGGCCCCCCCAGTGCCCTTCCTGCATGCCCAGCGGTACGTGAGTGGC
TATGGGCTGCAGAAGGGGGAGCTGAGCACACTGCTGTACAACACCCACCCATACCGGGCC
TTCCCGGTGCTGCTGCTGGACACCGTACCCTGGTATCTGCGGCTGTATGTGCACACCCTC
ACCATCACCTCCAAGGGCAAGGAGAACAAACCAAGTTACATCCACTACCAGCCTGCCCAG
GACCGGCTGCAACCCCACCTCCTGGAGATGCTGATTCAGCTGCCGGCCAACTCAGTCACC
AAGGTTTCCATCCAGTTTGAGCGGGCGCTGCTGAAGTGGACCGAGTACACGCCAGATCCT
AACCATGGCTTCTATGTCAGCCCATCTGTCCTCAGCGCCCTTGTGCCCAGCATGGTAGCA
GCCAAGCCAGTGGACTGGGAAGAGAGTCCCCTCTTCAACAGCCTGTTCCCAGTCTCTGAT
GGCTCTAACTACTTTGTGCGGCTCTACACGGAGCCGCTGCTGGTGAACCTGCCGACACCG
GACTTCAGCATGCCCTACAACGTGATCTGCCTCACGTGCACTGTGGTGGCCGTGTGCTAT
GGCTCCTTCTACAATCTCCTCACCCGAACCTTCCACATCGAGGAGCCCCGCACAGGTGGC
CTGGCCAAGCGGCTGGCCAACCTTATCCGGCGCGCCCGAGGTGTCCCCCCACTCTGA
|
| Enzyme 33 GenBank Gene ID |
AB057724  |
| Enzyme 33 GeneCard ID |
PIGT  |
| Enzyme 33 GenAtlas ID |
PIGT  |
| Enzyme 33 HGNC ID |
HGNC:14938  |
| Enzyme 33 Chromosome Location |
2 |
| Enzyme 33 Locus |
20q12-q13.12 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [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
]
- 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
]
- 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
]
- 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
]
- 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
]
- Lai CH, Chou CY, Ch'ang LY, Liu CS, Lin W: Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics. Genome Res. 2000 May;10(5):703-13. [PubMed
]
- Ohishi K, Nagamune K, Maeda Y, Kinoshita T: Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge. J Biol Chem. 2003 Apr 18;278(16):13959-67. Epub 2003 Feb 11. [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 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
12954 |
| Enzyme 34 Name |
Phosphatidylinositol glycan anchor biosynthesis class U protein |
| Enzyme 34 Synonyms |
- Cell division cycle protein 91-like 1
- Protein CDC91-like 1
- GPI transamidase component PIG-U
|
| Enzyme 34 Gene Name |
PIGU |
| Enzyme 34 Protein Sequence |
>Phosphatidylinositol glycan anchor biosynthesis class U protein
MAAPLVLVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSG
AVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYA
PDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSAF
LSAIFLALATYQSLYPLTLFVPGLLYLLQRQYIPVKMKSKAFWIFSWEYAMMYVGSLVVI
ICLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFY
TIPLAIKLKEHPIFFMFIQIAVIAIFKSYPTVGDVALYMAFFPVWNHLYRFLRNIFVLTC
IIIVCSLLFPVLWHLWIYAGSANSNFFYAITLTFNVGQILLISDYFYAFLRREYYLTHGL
YLTAKDGTEAMLVLK
|
| Enzyme 34 Number of Residues |
435 |
| Enzyme 34 Molecular Weight |
50051.2 |
| Enzyme 34 Theoretical pI |
7.82 |
| Enzyme 34 GO Classification |
| Function |
| — |
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
- organelle membrane
|
|
| Enzyme 34 General Function |
Involved in GPI anchor biosynthetic process |
| Enzyme 34 Specific Function |
Component of the GPI transamidase complex. May be involved in the recognition of either the GPI attachment signal or the lipid portion of GPI |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
- 66-86
166-186
188-208
237-257
259-279
286-306
313-333
355-375
386-406
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
27372217  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q9H490  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
PIGU_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>1308 bp
ATGGCGGCTCCCTTGGTCCTGGTGCTGGTGGTGGCTGTGACAGTGCGGGCGGCCTTGTTC
CGCTCCAGTCTGGCCGAGTTCATTTCCGAGCGGGTGGAGGTGGTGTCCCCACTGAGCTCT
TGGAAGAGAGTGGTTGAAGGCCTTTCACTGTTGGACTTGGGAGTATCTCCGTATTCTGGA
GCAGTATTTCATGAAACTCCATTAATAATATACCTCTTTCATTTCCTAATTGACTATGCT
GAATTGGTGTTTATGATAACTGATGCACTCACTGCTATTGCCCTGTATTTTGCAATCCAG
GACTTCAATAAAGTTGTGTTTAAAAAGCAGAAACTCCTCCTAGAACTGGACCAGTATGCC
CCAGATGTGGCCGAACTCATCCGGACCCCTATGGAAATGCGTTACATCCCTTTGAAAGTG
GCCCTGTTCTATCTCTTAAATCCTTACACGATTTTGTCTTGTGTTGCCAAGTCTACCTGT
GCCATCAACAACACCCTCATTGCTTTCTTCATTTTGACTACGATAAAAGGCAGTGCTTTC
CTCAGTGCTATTTTTCTTGCCTTAGCGACATACCAGTCTCTGTACCCACTCACCTTGTTT
GTCCCAGGACTCCTCTATCTCCTCCAGCGGCAGTACATACCTGTGAAAATGAAGAGCAAA
GCCTTCTGGATCTTTTCTTGGGAGTATGCCATGATGTATGTGGGAAGCCTAGTGGTAATC
ATTTGCCTCTCCTTCTTCCTTCTCAGCTCTTGGGATTTCATCCCCGCAGTCTATGGCTTT
ATACTTTCTGTTCCAGATCTCACTCCAAACATTGGTCTTTTCTGGTACTTCTTTGCAGAG
ATGTTTGAGCACTTCAGCCTCTTCTTTGTATGTGTGTTTCAGATCAACGTCTTCTTCTAC
ACCATCCCCTTAGCCATAAAGCTAAAGGAGCACCCCATCTTCTTCATGTTTATCCAGATC
GCTGTCATCGCCATCTTTAAGTCCTACCCGACAGTGGGGGACGTGGCGCTCTACATGGCC
TTCTTCCCCGTGTGGAACCATCTCTACAGATTCCTGAGAAACATCTTTGTCCTCACCTGC
ATCATCATCGTCTGTTCCCTGCTCTTCCCTGTCCTGTGGCACCTCTGGATTTATGCAGGA
AGTGCCAACTCTAATTTCTTTTATGCCATCACACTGACCTTCAACGTTGGGCAGATCCTG
CTCATCTCTGATTACTTCTATGCCTTCCTGCGGCGGGAGTACTACCTCACACATGGCCTC
TACTTGACCGCCAAGGATGGCACAGAGGCCATGCTCGTGCTCAAGTAG
|
| Enzyme 34 GenBank Gene ID |
AB086842  |
| Enzyme 34 GeneCard ID |
PIGU  |
| Enzyme 34 GenAtlas ID |
PIGU  |
| Enzyme 34 HGNC ID |
HGNC:15791  |
| Enzyme 34 Chromosome Location |
2 |
| Enzyme 34 Locus |
20q11.22 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Hong Y, Ohishi K, Kang JY, Tanaka S, Inoue N, Nishimura J, Maeda Y, Kinoshita T: Human PIG-U and yeast Cdc91p are the fifth subunit of GPI transamidase that attaches GPI-anchors to proteins. Mol Biol Cell. 2003 May;14(5):1780-9. Epub 2003 Jan 26. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- 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
]
- 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
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
12955 |
| Enzyme 35 Name |
GPI mannosyltransferase 2 |
| Enzyme 35 Synonyms |
- GPI mannosyltransferase II
- GPI-MT-II
- Phosphatidylinositol-glycan biosynthesis class V protein
- PIG-V
|
| Enzyme 35 Gene Name |
PIGV |
| Enzyme 35 Protein Sequence |
>GPI mannosyltransferase 2
MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVEGLL
GGLSHWDAEHFLFIAEHGYLYEHNFAFFPGFPLALLVGTELLRPLRGLLSLRSCLLISVA
SLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSA
MGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMAS
LFLSVFTLGLPFALFQYYAYTQFCLPGSARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDV
PLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQR
SKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLGSSTPIMYWFPAHL
LQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYHWKTCSPVTRYILGYFLTYWL
LGLLLHCNFLPWT
|
| Enzyme 35 Number of Residues |
493 |
| Enzyme 35 Molecular Weight |
55712.1 |
| Enzyme 35 Theoretical pI |
8.03 |
| Enzyme 35 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- GPI anchor biosynthetic process
- macromolecule metabolic process
- macromolecule modification
- metabolic process
- protein amino acid lipidation
- protein modification process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
- organelle membrane
|
|
| Enzyme 35 General Function |
Involved in transferase activity, transferring hexosyl groups |
| Enzyme 35 Specific Function |
Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
Not Available |
| Enzyme 35 Pfam Domain Function |
Not Available |
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
- 14-34
78-98
114-134
137-157
162-182
193-213
235-255
328-348
379-399
470-490
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
7020604  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
Q9NUD9  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
PIGV_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>1482 bp
ATGTGGCCCCAGGACCCATCCCGGAAGGAGGTGCTGAGGTTTGCAGTCAGCTGCCGTATC
CTGACTCTGATGCTGCAGGCCCTCTTCAATGCCATCACCCCAGATCACCATGCAGAAGCC
TTCTCTCCTCCTCGCCTGGCCCCCTCAGGCTTTGTGGACCAACTCGTGGAAGGTCTTCTG
GGCGGCCTGTCTCACTGGGATGCTGAACACTTCTTGTTCATTGCTGAGCATGGCTACCTG
TATGAGCACAACTTTGCCTTCTTTCCTGGTTTCCCCTTGGCCCTGCTGGTGGGGACTGAA
CTGTTGAGACCCTTACGGGGGTTACTGAGTCTACGCAGTTGCCTGCTGATTTCGGTAGCA
TCACTCAATTTCTTGTTCTTCATGTTGGCTGCAGTTGCACTTCATGACCTGGGTTGTCTG
GTTTTGCACTGTCCCCACCAGTCCTTTTATGCAGCTCTGCTTTTCTGTCTCAGCCCTGCC
AATGTCTTCCTGGCAGCTGGTTACTCAGAAGCTTTGTTTGCCCTCCTGACATTCAGTGCC
ATGGGGCAGCTGGAGAGGGGCCGAGTCTGGACTAGTGTACTCCTCTTTGCCTTTGCCACT
GGGGTACGCTCCAACGGGCTGGTCAGTGTTGGCTTCCTCATGCATTCTCAATGCCAAGGC
TTTTTCTCTTCTCTAACGATGCTGAATCCTCTGAGACAGCTCTTTAAGCTGATGGCCTCT
CTGTTTCTGTCGGTGTTCACACTTGGCCTTCCCTTTGCCCTCTTTCAGTATTATGCCTAC
ACCCAATTCTGTCTGCCAGGCTCAGCCCGCCCCATTCCTGAGCCTTTGGTACAGTTAGCT
GTAGACAAGGGCTACCGGATTGCAGAGGGAAATGAACCGCCTTGGTGCTTCTGGGATGTT
CCACTAATATACAGCTATATCCAGGATGTCTACTGGAATGTTGGCTTTTTGAAATACTAT
GAGCTCAAGCAGGTGCCCAATTTTCTACTGGCTGCACCAGTGGCTATACTGGTTGCCTGG
GCAACTTGGACATACGTGACCACTCACCCTTGGCTCTGCCTTACACTTGGGCTGCAAAGG
AGCAAGAACAATAAGACCCTAGAGAAGCCCGATCTTGGATTCCTCAGTCCTCAGGTGTTT
GTGTACGTGGTCCACGCTGCAGTGCTGCTGCTGTTTGGAGGTCTGTGCATGCATGTTCAG
GTTCTCACCAGGTTTTTGGGCTCCTCCACTCCTATTATGTACTGGTTTCCAGCTCACTTG
CTTCAGGATCAAGAGCCGCTGTTGAGATCCTTAAAGACTGTGCCTTGGAAGCCTCTTGCA
GAGGACTCCCCACCAGGACAAAAGGTCCCCAGAAATCCTATCATGGGACTTTTGTATCAC
TGGAAAACCTGTTCTCCAGTCACACGATACATTCTAGGCTACTTCCTGACTTACTGGCTC
CTGGGACTACTCCTACATTGCAACTTCCTGCCTTGGACATGA
|
| Enzyme 35 GenBank Gene ID |
AK000484  |
| Enzyme 35 GeneCard ID |
PIGV  |
| Enzyme 35 GenAtlas ID |
PIGV  |
| Enzyme 35 HGNC ID |
HGNC:26031  |
| Enzyme 35 Chromosome Location |
1 |
| Enzyme 35 Locus |
1p36.11 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 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
]
- Fabre AL, Orlean P, Taron CH: Saccharomyces cerevisiae Ybr004c and its human homologue are required for addition of the second mannose during glycosylphosphatidylinositol precursor assembly. FEBS J. 2005 Mar;272(5):1160-8. [PubMed
]
- Kang JY, Hong Y, Ashida H, Shishioh N, Murakami Y, Morita YS, Maeda Y, Kinoshita T: PIG-V involved in transferring the second mannose in glycosylphosphatidylinositol. J Biol Chem. 2005 Mar 11;280(10):9489-97. Epub 2004 Dec 28. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
12956 |
| Enzyme 36 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y |
| Enzyme 36 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class Y protein
- PIG-Y
|
| Enzyme 36 Gene Name |
PIGY |
| Enzyme 36 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
MFLSLPTLTVLIPLVSLAGLFYSASVEENFPQGCTSTASLCFYSLLLPITIPVYVFFHLW
TWMGIKLFRHN
|
| Enzyme 36 Number of Residues |
71 |
| Enzyme 36 Molecular Weight |
8057.5 |
| Enzyme 36 Theoretical pI |
7.41 |
| Enzyme 36 GO Classification |
Not Available |
| Enzyme 36 General Function |
Involved in GPI anchor biosynthetic process |
| Enzyme 36 Specific Function |
Component of the GPI-GlcNAc transferase (GPI-GnT) complex in the endoplasmic reticulum, a complex that catalyzes transfer of GlcNAc from UDP-GlcNAc to an acceptor phosphatidylinositol, the first step in the production of GPI- anchors for cell surface proteins. May act by regulating the catalytic subunit PIGA |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
Not Available |
| Enzyme 36 Pfam Domain Function |
Not Available |
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
75674192  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q3MUY2  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
PIGY_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>216 bp
ATGTTTCTGTCTCTTCCTACGTTGACTGTTCTTATTCCACTGGTTTCTTTAGCAGGACTG
TTCTACTCAGCCTCTGTGGAAGAAAACTTCCCACAGGGCTGCACTAGCACAGCCAGCCTT
TGCTTTTACAGCCTGCTCTTGCCTATTACCATACCAGTGTATGTATTCTTCCACCTTTGG
ACTTGGATGGGTATTAAACTCTTCAGGCATAATTGA
|
| Enzyme 36 GenBank Gene ID |
AB206972  |
| Enzyme 36 GeneCard ID |
PIGY  |
| Enzyme 36 GenAtlas ID |
PIGY  |
| Enzyme 36 HGNC ID |
HGNC:28213  |
| Enzyme 36 Chromosome Location |
4 |
| Enzyme 36 Locus |
4q22.1 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Murakami Y, Siripanyaphinyo U, Hong Y, Tashima Y, Maeda Y, Kinoshita T: The initial enzyme for glycosylphosphatidylinositol biosynthesis requires PIG-Y, a seventh component. Mol Biol Cell. 2005 Nov;16(11):5236-46. Epub 2005 Sep 14. [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 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
12961 |
| Enzyme 37 Name |
Pleckstrin homology domain-containing family A member 8 |
| Enzyme 37 Synonyms |
- PH domain-containing family A member 8
- Phosphatidylinositol-four-phosphate adapter protein 2
- FAPP-2
- Phosphoinositol 4-phosphate adapter protein 2
- hFAPP2
- Serologically defined breast cancer antigen NY-BR-86
|
| Enzyme 37 Gene Name |
PLEKHA8 |
| Enzyme 37 Protein Sequence |
>Pleckstrin homology domain-containing family A member 8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGDHRKE
AFSIGMQRDLSLYLPAMKKQMAILDALYEVHGLESDEVV
|
| Enzyme 37 Number of Residues |
519 |
| Enzyme 37 Molecular Weight |
58306.0 |
| Enzyme 37 Theoretical pI |
4.89 |
| Enzyme 37 GO Classification |
| Function |
- binding
- glycolipid binding
- glycolipid transporter activity
- lipid binding
- lipid transporter activity
- substrate-specific transporter activity
- transporter activity
|
| Process |
- establishment of localization
- glycolipid transport
- lipid transport
- transport
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 37 General Function |
Involved in glycolipid transporter activity |
| Enzyme 37 Specific Function |
Involved in TGN-to-plasma membrane transport and in the formation of post-Golgi constitutive carriers. May play a role in ensuring the coordination of the budding and the fission reactions |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
Not Available |
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
308153327  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q96JA3  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
PKHA8_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>1560 bp
ATGGAGGGGGTGCTGTACAAGTGGACCAACTATCTGAGCGGTTGGCAGCCTCGATGGTTC
CTTCTCTGTGGGGGAATATTGTCCTATTATGATTCTCCTGAAGATGCCTGGAAAGGTTGC
AAAGGGAGCATACAAATGGCAGTCTGTGAAATTCAAGTTCATTCTGTAGATAATACACGC
ATGGACCTGATAATCCCTGGGGAACAGTATTTCTACCTGAAGGCCAGAAGTGTGGCTGAA
AGACAGCGGTGGCTGGTGGCCCTGGGATCAGCCAAGGCTTGCCTGACTGACAGTAGGACC
CAGAAGGAGAAAGAGTTTGCTGAAAACACTGAAAACTTGAAAACCAAAATGTCAGAACTA
AGACTCTACTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAAGTGACCACAACT
GGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAATCAACCTGTAAT
ACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATCGCAAATGCAGCCTTCACCTCTGAG
CTGCTCTACCGCACTCCACCAGGATCACCTCAGCTGGCCATGCTCAAGTCCAGCAAGATG
AAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAATGGAGTTGAGCACTTGT
GAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTAATGAAAAATAAG
AATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGTGAGGAAAATACA
GATGATAATATAACAGTCCAAGGTGAAATAAGGAAGGAAGATGGAATGGAAAACCTGAAA
AATCATGACAATAACTTGACTCAGTCTGGATCAGACTCAAGTTGCTCTCCGGAATGCCTC
TGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAACACAAGCTTTAGT
GACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTGGCATCATGTTAT
GCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCTGTTAAGATGGAT
CTTGTTGGAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAAGAAGAGTTTACC
ACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAGGTTAGGAACTCA
GCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAGGGATTTTTGACA
GAAGTGAAAAATGGGGAGAAGGATATCCAGACAGCCCTAAATAATGCATATGGTAAAACA
TTGCGGCAACACCATGGCTGGGTAGTTCGAGGGGTTTTTGCGTTAGCTTTAAGGGCAGCT
CCATCCTATGAAGATTTTGTGGCCGCGTTAACCGTAAAGGAAGGTGACCACCAGAAAGAA
GCTTTCAGTATTGGGATGCAGAGGGACCTCAGCCTTTACCTCCCTGCCATGGAGAAGCAG
CTGGCCATACTGGACACTTTATATGAGGTCCACGGGCTGGAATCTGATGAGGTGGTATGA
|
| Enzyme 37 GenBank Gene ID |
NM_001197026.1  |
| Enzyme 37 GeneCard ID |
PLEKHA8  |
| Enzyme 37 GenAtlas ID |
PLEKHA8  |
| Enzyme 37 HGNC ID |
HGNC:30037  |
| Enzyme 37 Chromosome Location |
7 |
| Enzyme 37 Locus |
7p21-p11.2 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Dowler S, Currie RA, Campbell DG, Deak M, Kular G, Downes CP, Alessi DR: Identification of pleckstrin-homology-domain-containing proteins with novel phosphoinositide-binding specificities. Biochem J. 2000 Oct 1;351(Pt 1):19-31. [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
]
- Scanlan MJ, Gout I, Gordon CM, Williamson B, Stockert E, Gure AO, Jager D, Chen YT, Mackay A, O'Hare MJ, Old LJ: Humoral immunity to human breast cancer: antigen definition and quantitative analysis of mRNA expression. Cancer Immun. 2001 Mar 30;1:4. [PubMed
]
- Godi A, Di Campli A, Konstantakopoulos A, Di Tullio G, Alessi DR, Kular GS, Daniele T, Marra P, Lucocq JM, De Matteis MA: FAPPs control Golgi-to-cell-surface membrane traffic by binding to ARF and PtdIns(4)P. Nat Cell Biol. 2004 May;6(5):393-404. Epub 2004 Apr 25. [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 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
14494 |
| Enzyme 38 Name |
Sphingomyelin phosphodiesterase 4 |
| Enzyme 38 Synonyms |
- Neutral sphingomyelinase 3
- nSMase-3
- nSMase3
- Neutral sphingomyelinase III
|
| Enzyme 38 Gene Name |
SMPD4 |
| Enzyme 38 Protein Sequence |
>Sphingomyelin phosphodiesterase 4
MAFPHLQQPSFLLASLKADSINKPFAQQCQDLVKVIEDFPAKELHTIFPWLVESIFGSLD
GVLVGWNLRCLQGRVNPVEYSIVMEFLDPGGPMMKLVYKLQAEDYKFDFPVSYLPGPVKA
SIQECILPDSPLYHNKVQFTPTGGLGLNLALNPFEYYIFFFALSLITQKPLPVSLHVRTS
DCAYFILVDRYLSWFLPTEGSVPPPLSSSPGGTSPSPPPRTPAIPFASYGLHHTSLLKRH
ISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQKMQSPHAKLEVLHYRLSVSS
ALYSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPEQASPSAHSHATSP
LEEFKRAAVPRFVQQKLYLFLQHCFGHWPLDASFRAVLEMWLSYLQPWRYAPDKQAPGSD
SQPRCVSEKWAPFVQENLLMYTKLFVGFLNRALRTDLVSPKHALMVFRVAKVFAQPNLAE
MIQKGEQLFLEPELVIPHRQHRLFTAPTFTGSFLSPWPPAVTDASFKVKSHVYSLEGQDC
KYTPMFGPEARTLVLRLAQLITQAKHTAKSISDQCAESPAGHSFLSWLGFSSMDTNGSYT
ANDLDEMGQDSVRKTDEYLEKALEYLRQIFRLSEAQLRQFTLALGTTQDENGKKQLPDCI
VGEDGLILTPLGRYQIINGLRRFEIEYQGDPELQPIRSYEIASLVRTLFRLSSAINHRFA
GQMAALCSRDDFLGSFCRYHLTEPGLASRHLLSPVGRRQVAGHTRGPRLSLRFLGSYRTL
VSLLLAFFVASLFCVGPLPCTLLLTLGYVLYASAMTLLTERGKLHQP
|
| Enzyme 38 Number of Residues |
827 |
| Enzyme 38 Molecular Weight |
93350.8 |
| Enzyme 38 Theoretical pI |
8.04 |
| Enzyme 38 GO Classification |
Not Available |
| Enzyme 38 General Function |
Involved in metal ion binding |
| Enzyme 38 Specific Function |
Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide |
| Enzyme 38 Pathways |
|
| Enzyme 38 Reactions |
- sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
|
| Enzyme 38 Pfam Domain Function |
Not Available |
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
102467481  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q9NXE4  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
NSMA3_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>2601 bp
ATGACGACTTTCGGCGCCGTGGCGGAATGGCGGCTTCCATCTCTGAGGCGAGCGACGCTA
TGGATCCCACAGTGGTTTGCTAAGAAGGCCATTTTCAACTCTCCACTGGAGGCTGCTATG
GCGTTCCCTCACCTGCAGCAGCCCAGCTTTCTACTGGCTAGCCTGAAAGCTGACTCTATA
AATAAGCCCTTTGCACAGCAGTGCCAAGACTTGGTTAAAGTCATTGAGGACTTTCCAGCA
AAGGAGCTGCACACCATCTTCCCATGGCTGGTAGAAAGCATTTTTGGCAGCCTAGATGGT
GTCCTCGTTGGCTGGAACCTCCGCTGCTTACAGGGGCGCGTGAATCCTGTGGAGTACAGC
ATCGTGATGGAATTTCTCGACCCTGGTGGCCCAATGATGAAGTTGGTTTATAAGCTTCAA
GCTGAAGACTATAAGTTCGACTTTCCTGTCTCCTACTTGCCTGGTCCTGTGAAGGCGTCC
ATCCAGGAGTGCATCCTCCCTGACAGTCCTCTGTACCACAACAAGGTCCAGTTCACCCCT
ACTGGGGGCCTTGGTCTGAACTTGGCCCTGAATCCGTTCGAGTATTACATATTCTTCTTT
GCCTTGAGCCTCATCACTCAGAAGCCACTTCCTGTGTCCCTCCACGTCCGTACTTCAGAC
TGTGCCTATTTCATCCTGGTGGACAGGTACCTGTCATGGTTCCTGCCCACCGAAGGCAGT
GTGCCCCCACCACTCTCCTCCAGCCCAGGGGGGACCAGCCCCTCACCACCTCCCAGGACA
CCAGCCATACCCTTTGCTTCCTATGGCCTCCACCACACTAGCCTCCTAAAGCGACACATC
TCTCATCAGACGTCTGTGAATGCAGACCCCGCCTCCCACGAGATCTGGAGGTCAGAAACT
CTGCTCCAGGTTTTTGTTGAAATGTGGCTTCATCACTATTCCTTGGAGATGTATCAAAAA
ATGCAGTCCCCTCATGCCAAGCTGGAGGTTCTGCACTACCGACTCAGTGTCTCCAGCGCC
CTCTACAGCCCCGCCCAACCCAGCCTCCAGGCCCTCCACGCCTACCAAGAGTCGTTCACG
CCTACTGAGGAGCATGTGTTGGTGGTGCGCCTGCTGCTGAAGCACCTGCACGCCTTTGCC
AACAGCCTGAAGCCAGAGCAGGCCTCACCCTCCGCCCACTCCCACGCCACCAGCCCCCTG
GAGGAGTTCAAACGGGCTGCTGTCCCGAGGTTCGTCCAGCAGAAACTCTACCTCTTCTTG
CAGCATTGCTTTGGCCACTGGCCCCTGGACGCATCGTTCAGAGCTGTCCTGGAGATGTGG
CTGAGCTACCTGCAGCCGTGGCGGTACGCGCCTGACAAGCAGGCTCCGGGCAGCGACTCC
CAGCCCCGGTGTGTGTCGGAGAAATGGGCACCCTTTGTCCAGGAGAACCTGCTGATGTAC
ACCAAGTTGTTTGTGGGCTTTCTGAACCGCGCGCTCCGCACAGACCTGGTCAGCCCCAAG
CACGCGCTCATGGTGTTCCGAGTGGCCAAAGTCTTTGCCCAGCCCAACCTGGCTGAGATG
ATTCAGAAAGGTGAGCAGCTATTCCTGGAGCCAGAGCTGGTCATCCCCCACCGCCAGCAC
CGACTCTTCACGGCCCCCACATTCACTGGGAGCTTCCTGTCACCCTGGCCACCAGCGGTC
ACTGATGCCTCCTTCAAGGTGAAGAGCCACGTCTACAGCCTGGAGGGCCAGGACTGCAAG
TACACCCCGATGTTTGGGCCCGAGGCCCGCACCCTGGTCCTGCGCCTCGCTCAGCTCATC
ACACAGGCCAAACACACAGCCAAGTCCATCTCCGACCAGTGTGCGGAGAGCCCGGCTGGC
CACTCCTTCCTCTCATGGCTGGGCTTTAGCTCCATGGACACCAATGGCTCCTACACAGCC
AACGACCTGGACGAGATGGGGCAAGACAGTGTCCGGAAGACAGATGAATACCTGGAGAAG
GCCCTGGAGTACCTGCGCCAGATATTCCGGCTCAGCGAAGCGCAGCTCAGGCAGTTCACA
CTCGCCTTGGGCACCACCCAGGATGAGAATGGAAAAAAGCAACTCCCCGACTGCATCGTG
GGTGAGGACGGACTCATCCTTACGCCCCTGGGGCGGTACCAGATCATCAATGGGCTGCGA
AGGTTTGAAATTGAGTACCAGGGGGACCCGGAGCTGCAGCCCATCCGGAGCTATGAGATC
GCCAGCTTGGTCCGCACACTCTTTAGGCTGTCGTCTGCCATCAACCACAGATTTGCAGGA
CAGATGGCGGCTCTGTGTTCCCGGGATGACTTCCTCGGCAGCTTCTGTCGCTACCACCTC
ACAGAACCTGGGCTGGCCAGCAGGCACCTGCTGAGCCCTGTGGGGCGGAGGCAGGTGGCC
GGCCACACCCGCGGCCCCAGGCTCAGCCTGCGCTTCCTGGGCAGTTACCGGACGCTGGTC
TCGCTGCTGCTGGCCTTCTTCGTGGCCTCTCTGTTCTGCGTCGGGCCCCTCCCATGCACG
CTGCTGCTCACCCTGGGCTATGTCCTCTACGCCTCTGCCATGACACTGCTGACCGAGCGG
GGGAAGCTGCACCAGCCCTGA
|
| Enzyme 38 GenBank Gene ID |
Not Available |
| Enzyme 38 GeneCard ID |
SMPD4  |
| Enzyme 38 GenAtlas ID |
SMPD4  |
| Enzyme 38 HGNC ID |
HGNC:32949  |
| Enzyme 38 Chromosome Location |
2 |
| Enzyme 38 Locus |
2q21.1 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Krut O, Wiegmann K, Kashkar H, Yazdanpanah B, Kronke M: Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein. J Biol Chem. 2006 May 12;281(19):13784-93. Epub 2006 Mar 3. [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
]
- 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
]
- 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 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
14925 |
| Enzyme 39 Name |
Non-lysosomal glucosylceramidase |
| Enzyme 39 Synonyms |
- NLGase
- Beta-glucocerebrosidase 2
- Beta-glucosidase 2
- Glucosylceramidase 2
|
| Enzyme 39 Gene Name |
GBA2 |
| Enzyme 39 Protein Sequence |
>Non-lysosomal glucosylceramidase
MGTQDPGNMGTGVPASEQISCAKEDPQVYCPEETGGTKDVQVTDCKSPEDSRPPKETDCC
NPEDSGQLMVSYEGKAMGYQVPPFGWRICLAHEFTEKRKPFQANNVSLSNMIKHIGMGLR
YLQWWYRKTHVEKKTPFIDMINSVPLRQIYGCPLGGIGGGTITRGWRGQFCRWQLNPGMY
QHRTVIADQFTVCLRREGQTVYQQVLSLERPSVLRSWNWGLCGYFAFYHALYPRAWTVYQ
LPGQNVTLTCRQITPILPHDYQDSSLPVGVFVWDVENEGDEALDVSIMFSMRNGLGGGDD
APGGLWNEPFCLERSGETVRGLLLHHPTLPNPYTMAVAARVTAATTVTHITAFDPDSTGQ
QVWQDLLQDGQLDSPTGQSTPTQKGVGIAGAVCVSSKLRPRGQCRLEFSLAWDMPRIMFG
AKGQVHYRRYTRFFGQDGDAAPALSHYALCRYAEWEERISAWQSPVLDDRSLPAWYKSAL
FNELYFLADGGTVWLEVLEDSLPEELGRNMCHLRPTLRDYGRFGYLEGQEYRMYNTYDVH
FYASFALIMLWPKLELSLQYDMALATLREDLTRRRYLMSGVMAPVKRRNVIPHDIGDPDD
EPWLRVNAYLIHDTADWKDLNLKFVLQVYRDYYLTGDQNFLKDMWPVCLAVMESEMKFDK
DHDGLIENGGYADQTYDGWVTTGPSAYCGGLWLAAVAVMVQMAALCGAQDIQDKFSSILS
RGQEAYERLLWNGRYYNYDSSSRPQSRSVMSDQCAGQWFLKACGLGEGDTEVFPTQHVVR
ALQTIFELNVQAFAGGAMGAVNGMQPHGVPDKSSVQSDEVWVGVVYGLAATMIQEGLTWE
GFQTAEGCYRTVWERLGLAFQTPEAYCQQRVFRSLAYMRPLSIWAMQLALQQQQHKKASW
PKVKQGTGLRTGPMFGPKEAMANLSPE
|
| Enzyme 39 Number of Residues |
927 |
| Enzyme 39 Molecular Weight |
104648.1 |
| Enzyme 39 Theoretical pI |
5.74 |
| Enzyme 39 GO Classification |
| Function |
- catalytic activity
- glucosylceramidase activity
- hydrolase activity
- hydrolase activity, acting on glycosyl bonds
- hydrolase activity, hydrolyzing O-glycosyl compounds
|
| Process |
- cellular lipid metabolic process
- glucosylceramide catabolic process
- glucosylceramide metabolic process
- glycolipid metabolic process
- glycosylceramide metabolic process
- lipid metabolic process
- membrane lipid metabolic process
- metabolic process
- primary metabolic process
- sphingolipid metabolic process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 39 General Function |
Involved in catalytic activity |
| Enzyme 39 Specific Function |
Non-lysosomal glucosylceramidase that catalyzes the conversion of glucosylceramide to free glucose and ceramide. Involved in sphingomyelin generation and prevention of glycolipid accumulation. May also catalyze the hydrolysis of bile acid 3-O- glucosides, however, the relevance of such activity is unclear in vivo |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
- D-glucosyl-N-acylsphingosine + H2O = D-glucose + N-acylsphingosine [RN:R01498]
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
24308251  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q9HCG7  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
GBA2_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>2784 bp
ATGGGGACCCAGGATCCAGGGAACATGGGAACCGGCGTCCCAGCCTCGGAGCAGATAAGC
TGTGCCAAAGAGGATCCACAAGTTTATTGCCCTGAAGAGACTGGCGGCACCAAGGATGTG
CAGGTTACAGACTGTAAGAGTCCCGAAGACAGCCGACCCCCAAAAGAGACGGACTGCTGC
AATCCGGAGGACTCTGGGCAGCTGATGGTTTCCTATGAGGGTAAAGCTATGGGCTACCAG
GTGCCTCCCTTTGGCTGGCGCATCTGTCTGGCTCATGAGTTTACAGAGAAGAGGAAACCC
TTTCAAGCTAACAACGTCTCCCTAAGCAACATGATAAAGCATATAGGCATGGGCTTGAGG
TACCTGCAGTGGTGGTACCGGAAGACCCATGTGGAAAAGAAGACACCTTTCATCGACATG
ATCAATTCTGTACCCCTAAGACAGATTTATGGTTGTCCCTTGGGTGGCATCGGGGGAGGC
ACTATTACCCGTGGCTGGAGAGGCCAGTTCTGTCGTTGGCAGCTTAACCCTGGAATGTAT
CAGCACCGGACAGTCATCGCTGACCAATTCACAGTGTGCCTGCGTCGGGAAGGGCAGACT
GTGTACCAGCAAGTCCTGTCCCTGGAGCGCCCAAGTGTCCTCCGCAGCTGGAACTGGGGC
CTGTGTGGGTACTTTGCTTTCTACCATGCCCTCTATCCCCGAGCCTGGACTGTCTATCAG
CTTCCTGGCCAGAATGTCACCCTCACCTGCCGTCAGATCACACCCATCTTGCCCCATGAC
TACCAGGACAGCAGCCTGCCTGTAGGAGTCTTTGTGTGGGATGTGGAAAATGAAGGGGAC
GAAGCTCTAGATGTGTCCATCATGTTCTCCATGCGGAATGGACTGGGTGGTGGAGACGAT
GCCCCAGGGGGTTTGTGGAATGAGCCCTTCTGTCTGGAGCGTAGCGGGGAAACTGTCCGG
GGGCTGCTCCTGCATCATCCAACCCTTCCAAACCCCTACACGATGGCTGTGGCTGCACGA
GTCACGGCAGCTACCACGGTAACCCACATCACAGCCTTTGACCCTGACAGCACGGGGCAG
CAGGTGTGGCAGGATCTACTTCAGGATGGACAGCTGGACTCTCCCACTGGCCAAAGCACC
CCTACGCAGAAAGGAGTAGGCATTGCTGGAGCTGTGTGTGTTTCCAGCAAGTTGCGACCT
CGAGGCCAGTGCCGCCTGGAGTTTTCACTGGCTTGGGACATGCCCAGGATCATGTTTGGA
GCTAAAGGCCAAGTCCACTACAGGCGGTATACAAGGTTCTTTGGCCAGGATGGAGATGCA
GCACCTGCCCTCAGCCACTATGCACTGTGCCGATACGCAGAGTGGGAAGAGAGGATCTCA
GCTTGGCAGAGCCCGGTATTGGATGACAGATCACTGCCTGCCTGGTACAAATCTGCGCTG
TTCAATGAACTATACTTCCTGGCTGATGGAGGCACAGTGTGGCTGGAAGTTCTTGAGGAC
TCCCTACCAGAGGAGCTGGGCAGAAACATGTGTCACCTCCGCCCCACCCTACGGGACTAC
GGTCGATTTGGCTACCTTGAGGGCCAGGAGTACCGCATGTACAACACATATGATGTCCAC
TTTTATGCTTCCTTTGCCCTCATCATGCTCTGGCCCAAACTTGAGCTCAGCCTACAGTAT
GACATGGCTCTGGCCACTCTCAGGGAGGACCTGACACGGCGACGGTACCTGATGAGTGGG
GTGATGGCACCTGTGAAAAGGAGGAACGTCATCCCCCATGATATTGGGGACCCAGATGAT
GAACCATGGCTCCGCGTCAATGCATATTTAATCCATGATACTGCTGATTGGAAGGACCTG
AACCTGAAGTTTGTGCTGCAGGTTTATCGGGACTATTACCTCACGGGTGATCAAAACTTC
CTGAAGGACATGTGGCCTGTGTGTCTAGCTGTGATGGAATCTGAAATGAAGTTTGACAAG
GACCATGATGGACTCATTGAAAATGGAGGCTATGCAGACCAGACCTATGATGGATGGGTG
ACCACAGGCCCCAGTGCTTACTGTGGAGGGCTGTGGCTGGCAGCTGTGGCTGTGATGGTC
CAGATGGCTGCTCTGTGTGGGGCACAGGACATCCAGGATAAGTTTTCTTCTATCCTCAGC
CGGGGCCAAGAAGCCTATGAGAGACTGCTGTGGAATGGCCGCTATTACAACTATGACAGC
AGCTCTCGGCCTCAGTCTCGTAGTGTTATGTCTGACCAGTGTGCTGGACAGTGGTTCCTG
AAGGCCTGTGGCCTAGGAGAAGGAGACACTGAGGTGTTTCCTACCCAACATGTGGTCCGT
GCTCTCCAAACTATCTTTGAGCTGAACGTCCAGGCCTTTGCAGGAGGGGCCATGGGGGCT
GTGAATGGGATGCAGCCCCATGGTGTCCCTGATAAATCCAGTGTGCAGTCTGATGAAGTC
TGGGTGGGTGTGGTCTACGGGCTGGCAGCTACCATGATCCAAGAGGGCCTGACTTGGGAG
GGCTTCCAGACAGCTGAAGGCTGCTACCGTACCGTGTGGGAGCGCCTGGGTCTGGCCTTC
CAGACCCCAGAGGCATACTGCCAGCAGCGAGTGTTCCGCTCACTGGCCTACATGCGGCCA
CTGAGCATATGGGCCATGCAGCTAGCCCTGCAACAGCAGCAGCACAAAAAGGCCTCCTGG
CCAAAAGTCAAACAGGGCACAGGACTAAGGACAGGGCCTATGTTTGGACCAAAGGAAGCC
ATGGCAAACCTGAGCCCAGAGTGA
|
| Enzyme 39 GenBank Gene ID |
NM_020944.2  |
| Enzyme 39 GeneCard ID |
GBA2  |
| Enzyme 39 GenAtlas ID |
GBA2  |
| Enzyme 39 HGNC ID |
HGNC:18986  |
| Enzyme 39 Chromosome Location |
9 |
| Enzyme 39 Locus |
9p13.3 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Matern H, Boermans H, Lottspeich F, Matern S: Molecular cloning and expression of human bile acid beta-glucosidase. J Biol Chem. 2001 Oct 12;276(41):37929-33. Epub 2001 Aug 6. [PubMed
]
- Nagase T, Kikuno R, Nakayama M, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Aug 31;7(4):273-81. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Matern H, Heinemann H, Legler G, Matern S: Purification and characterization of a microsomal bile acid beta-glucosidase from human liver. J Biol Chem. 1997 Apr 25;272(17):11261-7. [PubMed
]
- Boot RG, Verhoek M, Donker-Koopman W, Strijland A, van Marle J, Overkleeft HS, Wennekes T, Aerts JM: Identification of the non-lysosomal glucosylceramidase as beta-glucosidase 2. J Biol Chem. 2007 Jan 12;282(2):1305-12. Epub 2006 Nov 14. [PubMed
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
16484 |
| Enzyme 40 Name |
cDNA, FLJ94713 (Putative uncharacterized protein MGC26963) |
| Enzyme 40 Synonyms |
Not Available |
| Enzyme 40 Gene Name |
MGC26963 |
| Enzyme 40 Protein Sequence |
>cDNA, FLJ94713 (Putative uncharacterized protein MGC26963)
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYI
QIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDY
IDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLP
VPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFI
KEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNL
KVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGED
NEKST
|
| Enzyme 40 Number of Residues |
365 |
| Enzyme 40 Molecular Weight |
42281 |
| Enzyme 40 Theoretical pI |
9.00 |
| Enzyme 40 GO Classification |
Not Available |
| Enzyme 40 General Function |
Not Available |
| Enzyme 40 Specific Function |
Not Available |
| Enzyme 40 Pathways |
Not Available |
| Enzyme 40 Reactions |
Not Available |
| Enzyme 40 Pfam Domain Function |
Not Available |
| Enzyme 40 Signals |
|
| Enzyme 40 Transmembrane Regions |
|
| Enzyme 40 Essentiality |
Not Available |
| Enzyme 40 GenBank ID Protein |
Not Available |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
B2RA61  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
B2RA61_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
Not Available |
| Enzyme 40 GenBank Gene ID |
AK314049  |
| Enzyme 40 GeneCard ID |
B2RA61  |
| Enzyme 40 GenAtlas ID |
Not Available |
| Enzyme 40 HGNC ID |
Not Available |
| Enzyme 40 Chromosome Location |
Not Available |
| Enzyme 40 Locus |
Not Available |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
Not Available |
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
17301 |
| Enzyme 41 Name |
Sphingomyelin synthase-related protein 1 |
| Enzyme 41 Synonyms |
- SMSr
- Sterile alpha motif domain-containing protein 8
- SAM domain-containing protein 8
|
| Enzyme 41 Gene Name |
SAMD8 |
| Enzyme 41 Protein Sequence |
>Sphingomyelin synthase-related protein 1
MAGPNQLCIRRWTTKHVAVWLKDEGFFEYVDILCNKHRLDGITLLTLTEYDLRSPPLEIK
VLGDIKRLMLSVRKLQKIHIDVLEEMGYNSDSPMGSMTPFISALQSTDWLCNGELSHDCD
GPITDLNSDQYQYMNGKNKHSVRRLDPEYWKTILSCIYVFIVFGFTSFIMVIVHERVPDM
QTYPPLPDIFLDSVPRIPWAFAMTEVCGMILCYIWLLVLLLHKHRSILLRRLCSLMGTVF
LLRCFTMFVTSLSVPGQHLQCTGKIYGSVWEKLHRAFAIWSGFGMTLTGVHTCGDYMFSG
HTVVLTMLNFFVTEYTPRSWNFLHTLSWVLNLFGIFFILAAHEHYSIDVFIAFYITTRLF
LYYHTLANTRAYQQSRRARIWFPMFSFFECNVNGTVPNEYCWPFSKPAIMKRLIG
|
| Enzyme 41 Number of Residues |
415 |
| Enzyme 41 Molecular Weight |
48320.2 |
| Enzyme 41 Theoretical pI |
8.13 |
| Enzyme 41 GO Classification |
Not Available |
| Enzyme 41 General Function |
Involved in sphingomyelin biosynthetic process |
| Enzyme 41 Specific Function |
Not Available |
| Enzyme 41 Pathways |
Not Available |
| Enzyme 41 Reactions |
Not Available |
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
- 153-173
201-221
232-252
277-297
322-342
347-367
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
292658773  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
Q96LT4  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
SAMD8_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>1248 bp
ATGGCAGGTCCTAATCAACTCTGCATTCGCCGCTGGACTACCAAGCATGTAGCTGTGTGG
CTGAAGGATGAAGGCTTTTTTGAATATGTGGACATTTTATGCAATAAGCACCGACTTGAT
GGAATCACATTGCTAACATTGACTGAATATGATCTCCGGTCTCCTCCTCTGGAAATCAAA
GTCTTAGGGGACATTAAAAGGTTAATGCTCTCAGTCCGAAAATTGCAGAAAATACATATT
GATGTTTTAGAAGAGATGGGCTACAACAGTGACAGTCCCATGGGTTCCATGACCCCTTTC
ATCAGTGCTCTTCAGAGTACAGACTGGCTCTGTAATGGGGAGCTTTCCCATGACTGTGAC
GGACCCATAACTGACTTGAATTCTGATCAGTACCAGTACATGAATGGTAAAAACAAACAT
TCTGTTCGAAGATTGGACCCAGAATACTGGAAGACTATACTGAGTTGTATATATGTTTTT
ATAGTATTTGGATTTACATCTTTCATTATGGTTATAGTCCATGAGCGAGTGCCTGACATG
CAGACCTATCCACCACTCCCAGATATATTCTTAGACAGCGTTCCTAGAATCCCATGGGCC
TTTGCCATGACGGAAGTATGTGGCATGATTCTGTGCTATATTTGGCTCCTGGTTCTTCTT
CTTCACAAGCACAGGTCAATACTTCTGCGAAGGCTCTGTAGTCTGATGGGAACTGTATTC
TTGCTTCGCTGCTTTACCATGTTTGTGACCTCCCTCTCCGTGCCAGGACAACACCTGCAG
TGTACTGGAAAGATATATGGCAGTGTATGGGAGAAATTACATCGAGCCTTTGCCATTTGG
AGTGGCTTTGGTATGACCCTGACTGGCGTTCACACATGTGGAGATTACATGTTTAGTGGC
CACACAGTCGTCCTAACTATGCTGAATTTCTTTGTCACCGAATATACACCAAGAAGCTGG
AATTTCTTGCACACTTTATCCTGGGTTCTCAACCTCTTTGGAATCTTCTTCATCTTGGCT
GCCCATGAACATTATTCTATTGATGTGTTTATTGCTTTTTATATAACAACAAGACTCTTT
TTGTACTACCATACTCTGGCCAATACCAGAGCATATCAGCAGAGTAGGAGAGCAAGGATT
TGGTTTCCCATGTTCTCTTTTTTTGAATGCAATGTTAATGGCACAGTACCTAATGAATAT
TGTTGGCCATTTTCAAAACCAGCAATAATGAAAAGACTAATTGGATGA
|
| Enzyme 41 GenBank Gene ID |
NM_001174156.1  |
| Enzyme 41 GeneCard ID |
SAMD8  |
| Enzyme 41 GenAtlas ID |
SAMD8  |
| Enzyme 41 HGNC ID |
HGNC:26320  |
| Enzyme 41 Chromosome Location |
1 |
| Enzyme 41 Locus |
10q22.2 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 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, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
17337 |
| Enzyme 42 Name |
GPI-anchor transamidase |
| Enzyme 42 Synonyms |
- GPI transamidase
- GPI8 homolog
- hGPI8
- Phosphatidylinositol-glycan biosynthesis class K protein
- PIG-K
|
| Enzyme 42 Gene Name |
PIGK |
| Enzyme 42 Protein Sequence |
>GPI-anchor transamidase
MAVTDSLSRAATVLATVLLLSFGSVAASHIEDQAEQFFRSGHTNNWAVLVCTSRFWFNYR
HVANTLSVYRSVKRLGIPDSHIVLMLADDMACNPRNPKPATVFSHKNMELNVYGDDVEVD
YRSYEVTVENFLRVLTGRIPPSTPRSKRLLSDDRSNILIYMTGHGGNGFLKFQDSEEITN
IELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDPA
IGVHLMDRYTFYVLEFLEEINPASQTNMNDLFQVCPKSLCVSTPGHRTDLFQRDPKNVLI
TDFFGSVRKVEITTETIKLQQDSEIMESSYKEDQMDEKLMEPLKYAEQLPVAQIIHQKPK
LKDWHPPGGFILGLWALIIMVFFKTYGIKHMKFIF
|
| Enzyme 42 Number of Residues |
395 |
| Enzyme 42 Molecular Weight |
45251.4 |
| Enzyme 42 Theoretical pI |
6.09 |
| Enzyme 42 GO Classification |
| Function |
- catalytic activity
- cysteine-type endopeptidase activity
- endopeptidase activity
- hydrolase activity
- peptidase activity
- peptidase activity, acting on L-amino acid peptides
|
| Process |
- macromolecule metabolic process
- metabolic process
- protein metabolic process
- proteolysis
|
| Component |
| — |
|
| Enzyme 42 General Function |
Involved in cysteine-type endopeptidase activity |
| Enzyme 42 Specific Function |
Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein |
| 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 |
2558891  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
Q92643  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
GPI8_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>1188 bp
ATGGCCGTCACCGACAGCCTCAGCCGGGCTGCGACTGTCTTGGCAACTGTGTTGCTCTTG
TCCTTCGGCAGCGTGGCCGCTAGTCATATCGAGGATCAAGCAGAACAATTCTTTAGAAGT
GGCCATACAAACAACTGGGCTGTTCTGGTGTGTACATCCCGATTCTGGTTTAATTATCGA
CATGTTGCAAATACCCTTTCTGTTTATAGAAGTGTCAAGAGGCTAGGTATTCCTGACAGT
CACATTGTCCTAATGCTTGCAGATGATATGGCCTGTAATCCTAGAAATCCCAAACCAGCT
ACAGTGTTTAGTCACAAGAATATGGAACTAAATGTGTATGGAGATGATGTGGAAGTGGAT
TATAGAAGTTATGAGGTAACTGTGGAGAATTTTTTACGGGTATTAACTGGGAGGATCCCA
CCTAGTACTCCTCGGTCAAAACGTCTTCTTTCTGATGACAGAAGCAATATTCTAATTTAT
ATGACAGGGCATGGTGGAAATGGTTTCTTAAAATTTCAAGATTCTGAAGAAATTACCAAC
ATAGAACTCGCGGATGCTTTTGAACAAATGTGGCAGAAAAGACGCTACAATGAGCTACTG
TTTATTATTGATACTTGCCAAGGAGCATCCATGTATGAACGATTTTATTCTCCTAACATA
ATGGCTCTAGCTAGTAGTCAAGTGGGAGAAGATTCACTCTCGCATCAACCTGATCCTGCA
ATTGGAGTCCATCTTATGGATAGATACACATTTTATGTCTTGGAATTTTTGGAAGAAATT
AACCCAGCTAGCCAAACTAATATGAATGACCTTTTTCAGGTATGTCCCAAAAGTCTGTGT
GTGTCTACTCCTGGACATCGCACTGATCTTTTTCAGAGGGATCCTAAAAATGTACTGATA
ACTGATTTCTTTGGAAGTGTACGGAAAGTGGAAATTACAACAGAGACTATTAAATTGCAA
CAGGATTCAGAAATCATGGAAAGCAGCTATAAGGAAGACCAGATGGATGAGAAACTAATG
GAACCTCTGAAATATGCTGAACAACTTCCTGTAGCTCAGATAATACACCAGAAACCGAAG
CTGAAAGACTGGCATCCTCCTGGGGGCTTTATTCTGGGATTATGGGCACTTATTATCATG
GTTTTCTTCAAAACTTATGGAATTAAGCATATGAAGTTCATTTTTTAG
|
| Enzyme 42 GenBank Gene ID |
AF022913  |
| Enzyme 42 GeneCard ID |
PIGK  |
| Enzyme 42 GenAtlas ID |
PIGK  |
| Enzyme 42 HGNC ID |
HGNC:8965  |
| Enzyme 42 Chromosome Location |
1 |
| Enzyme 42 Locus |
1p31.1 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Benghezal M, Benachour A, Rusconi S, Aebi M, Conzelmann A: Yeast Gpi8p is essential for GPI anchor attachment onto proteins. EMBO J. 1996 Dec 2;15(23):6575-83. [PubMed
]
- Yu J, Nagarajan S, Knez JJ, Udenfriend S, Chen R, Medof ME: The affected gene underlying the class K glycosylphosphatidylinositol (GPI) surface protein defect codes for the GPI transamidase. Proc Natl Acad Sci U S A. 1997 Nov 11;94(23):12580-5. [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
]
- 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
]
- Ohishi K, Inoue N, Maeda Y, Takeda J, Riezman H, Kinoshita T: Gaa1p and gpi8p are components of a glycosylphosphatidylinositol (GPI) transamidase that mediates attachment of GPI to proteins. Mol Biol Cell. 2000 May;11(5):1523-33. [PubMed
]
- Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [PubMed
]
- Ohishi K, Nagamune K, Maeda Y, Kinoshita T: Two subunits of glycosylphosphatidylinositol transamidase, GPI8 and PIG-T, form a functionally important intermolecular disulfide bridge. J Biol Chem. 2003 Apr 18;278(16):13959-67. Epub 2003 Feb 11. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
17782 |
| Enzyme 43 Name |
Glycosylphosphatidylinositol anchor attachment 1 protein |
| Enzyme 43 Synonyms |
- GPI anchor attachment protein 1
- GAA1 protein homolog
- hGAA1
|
| Enzyme 43 Gene Name |
GPAA1 |
| Enzyme 43 Protein Sequence |
>Glycosylphosphatidylinositol anchor attachment 1 protein
MGLLSDPVRRRALARLVLRLNAPLCVLSYVAGIAWFLALVFPPLTQRTYMSENAMGSTMV
EEQFAGGDRARAFARDFAAHRKKSGALPVAWLERTMRSVGLEVYTQSFSRKLPFPDETHE
RYMVSGTNVYGILRAPRAASTESLVLTVPCGSDSTNSQAVGLLLALAAHFRGQIYWAKDI
VFLVTEHDLLGTEAWLEAYHDVNVTGMQSSPLQGRAGAIQAAVALELSSDVVTSLDVAVE
GLNGQLPNLDLLNLFQTFCQKGGLLCTLQGKLQPEDWTSLDGPLQGLQTLLLMVLRQASG
RPHGSHGLFLRYRVEALTLRGINSFRQYKYDLVAVGKALEGMFRKLNHLLERLHQSFFLY
LLPGLSRFVSIGLYMPAVGFLLLVLGLKALELWMQLHEAGMGLEEPGGAPGPSVPLPPSQ
GVGLASLVAPLLISQAMGLALYVLPVLGQHVATQHFPVAEAEAVVLTLLAIYAAGLALPH
NTHRVVSTQAPDRGWMALKLVALIYLALQLGCIALTNFSLGFLLATTMVPTAALAKPHGP
RTLYAALLVLTSPAATLLGSLFLWRELQEAPLSLAEGWQLFLAALAQGVLEHHTYGALLF
PLLSLGLYPCWLLFWNVLFWK
|
| Enzyme 43 Number of Residues |
621 |
| Enzyme 43 Molecular Weight |
67622.5 |
| Enzyme 43 Theoretical pI |
8.16 |
| Enzyme 43 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
- GPI-anchor transamidase complex
- cell part
- integral to membrane
- intrinsic to membrane
- macromolecular complex
- membrane part
- protein complex
|
|
| Enzyme 43 General Function |
Involved in tubulin binding |
| Enzyme 43 Specific Function |
Essential for GPI-anchoring of precursor proteins but not for GPI synthesis. Acts before or during formation of the carbonyl intermediate |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
Not Available |
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
- 25-45
369-389
428-448
459-479
496-516
544-564
600-620
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
5572751  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
O43292  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
GPAA1_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>1866 bp
ATGGGCCTCCTGTCGGACCCGGTTCGCCGGCGCGCGCTCGCCCGCCTAGTGCTGCGCCTC
AACGCGCCGTTGTGCGTGCTGAGCTACGTGGCGGGCATCGCCTGGTTCTTGGCGCTGGTT
TTCCCGCCGCTGACCCAGCGCACTTACATGTCGGAGAACGCCATGGGCTCCACCATGGTG
GAGGAGCAGTTTGCGGGCGGAGACCGTGCCCGGGCTTTTGCCCGGGACTTCGCCGCCCAC
CGCAAGAAGTCGGGGGCTCTGCCAGTGGCCTGGCTTGAACGGACGATGCGGTCAGTAGGG
CTGGAGGTCTACACGCAGAGTTTCTCCCGGAAACTGCCCTTCCCAGATGAGACCCACGAG
CGCTATATGGTGTCGGGCACCAACGTGTACGGCATCCTGCGGGCCCCGCGTGCTGCCAGC
ACCGAGTCGCTTGTGCTCACCGTGCCCTGTGGCTCTGACTCTACCAACAGCCAGGCTGTG
GGGCTGCTGCTGGCACTGGCTGCCCACTTCCGGGGGCAGATTTATTGGGCCAAAGATATC
GTCTTCCTGGTAACAGAACATGACCTTCTGGGCACTGAGGCTTGGCTTGAAGCCTACCAC
GATGTCAATGTCACTGGCATGCAGTCGTCTCCCCTGCAGGGCCGAGCTGGGGCCATTCAG
GCAGCCGTGGCCCTGGAGCTGAGCAGTGATGTGGTCACCAGCCTCGATGTGGCCGTGGAG
GGGCTTAACGGGCAGCTGCCCAACCTTGACCTGCTCAATCTCTTCCAGACCTTCTGCCAG
AAAGGGGGCCTGTTGTGCACGCTTCAGGGCAAGCTGCAGCCCGAGGACTGGACATCATTG
GATGGACCGCTGCAGGGCCTGCAGACACTGCTGCTCATGGTTCTGCGGCAGGCCTCCGGC
CGCCCCCACGGCTCCCATGGCCTCTTCCTGCGCTACCGTGTGGAGGCCCTAACCCTGCGT
GGCATCAATAGCTTCCGCCAGTACAAGTATGACCTGGTGGCAGTGGGCAAGGCTTTGGAG
GGCATGTTCCGCAAGCTCAACCACCTCCTGGAGCGCCTGCACCAGTCCTTCTTCCTCTAC
TTGCTCCCCGGCCTCTCCCGCTTCGTCTCCATCGGCCTCTACATGCCCGCTGTCGGCTTC
TTGCTCCTGGTCCTTGGTCTCAAGGCTCTGGAACTGTGGATGCAGCTGCATGAGGCTGGA
ATGGGCCTTGAGGAGCCCGGGGGTGCCCCTGGCCCCAGTGTACCCCTTCCCCCATCACAG
GGTGTGGGGCTGGCCTCGCTCGTGGCACCTCTGCTGATCTCACAGGCCATGGGACTGGCC
CTCTATGTCCTGCCAGTGCTGGGCCAACACGTTGCCACCCAGCACTTCCCAGTGGCAGAG
GCTGAGGCTGTGGTGCTGACACTGCTGGCGATTTATGCAGCTGGCCTGGCCCTGCCCCAC
AATACCCACCGGGTGGTAAGCACACAGGCCCCAGACAGGGGCTGGATGGCACTGAAGCTG
GTAGCCCTGATCTACCTAGCACTGCAGCTGGGCTGCATCGCCCTCACCAACTTCTCACTG
GGCTTCCTGCTGGCCACCACCATGGTGCCCACTGCTGCGCTTGCCAAGCCTCATGGGCCC
CGGACCCTCTATGCTGCCCTGCTGGTGCTGACCAGCCCGGCAGCCACGCTCCTTGGCAGC
CTGTTCCTGTGGCGGGAGCTGCAGGAGGCGCCACTGTCACTGGCCGAGGGCTGGCAGCTC
TTCCTGGCAGCGCTAGCCCAGGGTGTGCTGGAGCACCACACCTACGGCGCCCTGCTCTTC
CCACTGCTGTCCCTGGGCCTCTACCCCTGCTGGCTGCTTTTCTGGAATGTGCTCTTCTGG
AAGTGA
|
| Enzyme 43 GenBank Gene ID |
AB002135  |
| Enzyme 43 GeneCard ID |
GPAA1  |
| Enzyme 43 GenAtlas ID |
GPAA1  |
| Enzyme 43 HGNC ID |
HGNC:4446  |
| Enzyme 43 Chromosome Location |
8 |
| Enzyme 43 Locus |
8q24.3 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
- Hiroi Y, Komuro I, Chen R, Hosoda T, Mizuno T, Kudoh S, Georgescu SP, Medof ME, Yazaki Y: Molecular cloning of human homolog of yeast GAA1 which is required for attachment of glycosylphosphatidylinositols to proteins. FEBS Lett. 1998 Jan 16;421(3):252-8. [PubMed
]
- Inoue N, Ohishi K, Endo Y, Fujita T, Takeda J, Kinoshita T: Human and mouse GPAA1 (Glycosylphosphatidylinositol anchor attachment 1) genes: genomic structures, chromosome loci and the presence of a minor class intron. Cytogenet Cell Genet. 1999;84(3-4):199-205. [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
]
- Ohishi K, Inoue N, Kinoshita T: PIG-S and PIG-T, essential for GPI anchor attachment to proteins, form a complex with GAA1 and GPI8. EMBO J. 2001 Aug 1;20(15):4088-98. [PubMed
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
17783 |
| Enzyme 44 Name |
Protein PLEKHA9 |
| Enzyme 44 Synonyms |
Not Available |
| Enzyme 44 Gene Name |
PLEKHA9 |
| Enzyme 44 Protein Sequence |
>Protein PLEKHA9
MSELRLCCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAA
FTSELLYHTPPGSPQLAMLKSSKMKHPIIPIHNSLERQTELSTCENGSLNMEINGEEEIL
MKNKNSLYLKSAEIDCSISSEENTDDNITVQGEIMKEDRMENLKNHDNNLSQSGSDSSCS
PECLWEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCCAVVPVLDKLGPTVFAP
VKMDLVENIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLK
GFLTEVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGD
HRKEAFSIGMQRDLSLYLPAMKKQMAILDAL
|
| Enzyme 44 Number of Residues |
391 |
| Enzyme 44 Molecular Weight |
43538.3 |
| Enzyme 44 Theoretical pI |
4.76 |
| Enzyme 44 GO Classification |
| Function |
- binding
- glycolipid binding
- glycolipid transporter activity
- lipid binding
- lipid transporter activity
- substrate-specific transporter activity
- transporter activity
|
| Process |
- establishment of localization
- glycolipid transport
- lipid transport
- transport
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 44 General Function |
Involved in glycolipid transporter activity |
| Enzyme 44 Specific Function |
Not Available |
| 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 |
4050073  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
O95397  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
PKHA9_HUMAN  |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>1176 bp
ATGTCAGAACTAAGACTCTGCTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAA
GTGACCACAACTGGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAA
TCAACCTGTAATACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATTGCAAATGCAGCC
TTCACCTCTGAGCTGCTCTACCACACTCCACCAGGATCACCACAGCTGGCCATGCTCAAG
TCCAGCAAGATGAAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAACGGAG
TTGAGCACTTGTGAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTA
ATGAAAAATAAGAATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGT
GAGGAAAATACAGATGATAATATAACCGTCCAAGGTGAAATAATGAAGGAAGATAGAATG
GAAAACCTGAAAAATCATGACAATAACTTGTCTCAGTCTGGATCAGACTCAAGTTGCTCT
CCAGAATGCCTCTGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAAC
ACAAGCTTTAGTGACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTG
GCATCATGTTGTGCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCT
GTTAAGATGGATCTTGTTGAAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAA
GAAGAGTTTACCACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAG
GTTAGGAACTCAGCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAG
GGATTTTTGACAGAAGTGAAAAATGGGGAAAAGGATATCCAGACAGCCCTGAATAACGCA
TATGGTAAAACATTGCGGCAACACCATGGCTGGGTAGTTCGAGGGGTTTTTGCGTTAGCT
TTAAGGGCAACTCCATCCTATGAAGATTTTGTGGCCGCGTTAACCGTAAAGGAAGGTGAC
CACCGGAAAGAAGCTTTCAGTATTGGGATGCAGAGGGACCTCAGCCTTTACCTCCCTGCC
ATGAAGAAGCAGATGGCCATACTGGACGCTTTATAA
|
| Enzyme 44 GenBank Gene ID |
AF103731  |
| Enzyme 44 GeneCard ID |
PLEKHA9  |
| Enzyme 44 GenAtlas ID |
PLEKHA9  |
| Enzyme 44 HGNC ID |
HGNC:30222  |
| Enzyme 44 Chromosome Location |
1 |
| Enzyme 44 Locus |
12q |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
- 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 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
17784 |
| Enzyme 45 Name |
Glycolipid transfer protein domain-containing protein 2 |
| Enzyme 45 Synonyms |
Not Available |
| Enzyme 45 Gene Name |
GLTPD2 |
| Enzyme 45 Protein Sequence |
>Glycolipid transfer protein domain-containing protein 2
MGVAARPPALRHWFSHSIPLAIFALLLLYLSVRSLGARSGCGPRAQPCVPGETAPFQVRQ
ESGTLEAPERKQPPCLGPRGMLGRMMRRFHASLKPEGDVGLSPYLAGWRALVEFLTPLGS
VFAFATREAFTKVTDLEARVHGPDAEHYWSLAAMAAWERRAGLLEQPGAAPRDPTRSSGS
RTLLLLHRALRWSQLCLHRVATGALGGPEAGVQCSDAYRAALGPHHPWLVRQTARLAFLA
FPGRRRLLELACPGATEAEARAALLRAAGTLEDVYNRTQSLLAERGLLQLA
|
| Enzyme 45 Number of Residues |
291 |
| Enzyme 45 Molecular Weight |
31641.2 |
| Enzyme 45 Theoretical pI |
10.54 |
| Enzyme 45 GO Classification |
| Function |
- binding
- glycolipid binding
- glycolipid transporter activity
- lipid binding
- lipid transporter activity
- substrate-specific transporter activity
- transporter activity
|
| Process |
- establishment of localization
- glycolipid transport
- lipid transport
- transport
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 45 General Function |
Involved in glycolipid transporter activity |
| Enzyme 45 Specific Function |
Not Available |
| 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 |
304571945  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
A6NH11  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
GLTD2_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>876 bp
ATGGGAGTGGCGGCGCGGCCCCCAGCCCTGCGGCACTGGTTCAGCCACTCAATTCCTCTC
GCTATCTTCGCGCTGCTGCTGCTTTATCTCAGTGTTCGGAGCCTAGGCGCCCGCTCGGGC
TGCGGACCCAGGGCGCAGCCCTGCGTTCCAGGGGAAACGGCGCCCTTCCAGGTCCGGCAG
GAGTCGGGAACCCTGGAGGCCCCGGAGAGGAAACAGCCTCCGTGTCTGGGCCCTCGGGGG
ATGCTGGGCCGCATGATGAGGCGGTTCCACGCCAGTCTGAAACCCGAAGGGGATGTGGGG
CTGTCGCCGTACCTGGCGGGATGGAGGGCACTCGTCGAGTTCCTGACTCCCCTCGGCTCC
GTCTTCGCCTTCGCCACTAGGGAGGCCTTCACCAAGGTGACAGACCTGGAGGCTCGGGTG
CACGGCCCGGACGCGGAGCACTACTGGTCGCTGGTGGCCATGGCGGCGTGGGAGCGGAGG
GCGGGACTGCTGGAGCAGCCGGGGGCGGCCCCCCGGGACCCGACCCGGAGCTCGGGCTCT
CGCACGCTGCTCCTGCTGCACCGCGCGCTGCGCTGGTCCCAGCTCTGCCTCCACCGGGTG
GCGACCGGCGCGCTGGGAGGCCCGGAAGCGGGCGTGCAGTGCAGCGACGCCTACCGTGCG
GCCCTGGGTCCGCATCACCCCTGGCTGGTCCGACAGACCGCCCGCCTCGCCTTCCTCGCC
TTCCCGGGTCGCCGCCGCCTGCTGGAGCTGGCGTGTCCCGGAGCCACCGAGGCGGAGGCG
CGGGCCGCGCTGCTCCGGGCCGCCGGCACCTTGGAGGATGTCTACAACCGCACCCAGAGC
CTGCTGGCCGAGCGCGGCCTGCTCCAGCTGGCCTAA
|
| Enzyme 45 GenBank Gene ID |
NM_001014985.2  |
| Enzyme 45 GeneCard ID |
GLTPD2  |
| Enzyme 45 GenAtlas ID |
GLTPD2  |
| Enzyme 45 HGNC ID |
HGNC:33756  |
| Enzyme 45 Chromosome Location |
1 |
| Enzyme 45 Locus |
17p13.2 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
- 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
]
- 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 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
17785 |
| Enzyme 46 Name |
Putative uncharacterized protein PLEKHA8 |
| Enzyme 46 Synonyms |
Not Available |
| Enzyme 46 Gene Name |
PLEKHA8 |
| Enzyme 46 Protein Sequence |
>Putative uncharacterized protein PLEKHA8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALSVGMWV
|
| Enzyme 46 Number of Residues |
439 |
| Enzyme 46 Molecular Weight |
49308.8 |
| Enzyme 46 Theoretical pI |
4.67 |
| Enzyme 46 GO Classification |
| Function |
- binding
- glycolipid binding
- glycolipid transporter activity
- lipid binding
- lipid transporter activity
- substrate-specific transporter activity
- transporter activity
|
| Process |
- establishment of localization
- glycolipid transport
- lipid transport
- transport
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 46 General Function |
Involved in glycolipid transporter activity |
| Enzyme 46 Specific Function |
Not Available |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
Not Available |
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
14249174  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
B5MDU3  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
B5MDU3_HUMAN  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>1323 bp
ATGGAGGGGGTGCTGTACAAGTGGACCAACTATCTGAGCGGTTGGCAGCCTCGATGGTTC
CTTCTCTGTGGGGGAATATTGTCCTATTATGATTCTCCTGAAGATGCCTGGAAAGGTTGC
AAAGGGAGCATACAAATGGCAGTCTGTGAAATTCAAGTTCATTCTGTAGATAATACACGC
ATGGACCTGATAATCCCTGGGGAACAGTATTTCTACCTGAAGGCCAGAAGTGTGGCTGAA
AGACAGCGGTGGCTGGTGGCCCTGGGATCAGCCAAGGCTTGCCTGACTGACAGTAGGACC
CAGAAGGAGAAAGAGTTTGCTGAAAACACTGAAAACTTGAAAACCAAAATGTCAGAACTA
AGACTCTACTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAAGTGACCACAACT
GGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAATCAACCTGTAAT
ACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATCGCAAATGCAGCCTTCACCTCTGAG
CTGCTCTACCGCACTCCACCAGGATCACCTCAGCTGGCCATGCTCAAGTCCAGCAAGATG
AAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAATGGAGTTGAGCACTTGT
GAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTAATGAAAAATAAG
AATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGTGAGGAAAATACA
GATGATAATATAACAGTCCAAGGTGAAATAAGGAAGGAAGATGGAATGGAAAACCTGAAA
AATCATGACAATAACTTGACTCAGTCTGGATCAGACTCAAGTTGCTCTCCGGAATGCCTC
TGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAACACAAGCTTTAGT
GACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTGGCATCATGTTAT
GCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCTGTTAAGATGGAT
CTTGTTGGAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAAGAAGAGTTTACC
ACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAGGTTAGGAACTCA
GCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAGGGATTTTTGACA
GAAGTGAAAAATGGGGAGAAGGATATCCAGACAGCCCTAAGAAATCCAACAGAAAACACT
TGA
|
| Enzyme 46 GenBank Gene ID |
NM_032639  |
| Enzyme 46 GeneCard ID |
PLEKHA8  |
| Enzyme 46 GenAtlas ID |
PLEKHA8  |
| Enzyme 46 HGNC ID |
HGNC:30037  |
| Enzyme 46 Chromosome Location |
7 |
| Enzyme 46 Locus |
7p21-p11.2 |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
17786 |
| Enzyme 47 Name |
Pleckstrin homology domain containing, family A (Phosphoinositide binding specific) member 8, isoform CRA_a |
| Enzyme 47 Synonyms |
- SubName: cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
|
| Enzyme 47 Gene Name |
PLEKHA8 |
| Enzyme 47 Protein Sequence |
>Pleckstrin homology domain containing, family A (Phosphoinositide binding specific) member 8, isoform CRA_a
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRAAPSYEDFVAALTVKEGDHQKE
AFSIGMQRDLSLYLPAMEKQLAILDTLYEVHGLESDEVV
|
| Enzyme 47 Number of Residues |
519 |
| Enzyme 47 Molecular Weight |
58260.9 |
| Enzyme 47 Theoretical pI |
4.76 |
| Enzyme 47 GO Classification |
| Function |
- binding
- glycolipid binding
- glycolipid transporter activity
- lipid binding
- lipid transporter activity
- substrate-specific transporter activity
- transporter activity
|
| Process |
- establishment of localization
- glycolipid transport
- lipid transport
- transport
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 47 General Function |
Involved in glycolipid transporter activity |
| Enzyme 47 Specific Function |
Not Available |
| Enzyme 47 Pathways |
Not Available |
| Enzyme 47 Reactions |
Not Available |
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
194378422  |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
B4DH00  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
B4DH00_HUMAN  |
| Enzyme 47 PDB ID |
Not Available |
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>1560 bp
ATGGAGGGGGTGCTGTACAAGTGGACCAACTATCTGAGCGGTTGGCAGCCTCGATGGTTC
CTTCTCTGTGGGGGAATATTGTCCTATTATGATTCTCCTGAAGATGCCTGGAAAGGTTGC
AAAGGGAGCATACAAATGGCAGTCTGTGAAATTCAAGTTCATTCTGTAGATAATACACGC
ATGGACCTGATAATCCCTGGGGAACAGTATTTCTACCTGAAGGCCAGAAGTGTGGCTGAA
AGACAGCGGTGGCTGGTGGCCCTGGGATCAGCCAAGGCTTGCCTGACTGACAGTAGGACC
CAGAAGGAGAAAGAGTTTGCTGAAAACACTGAAAACTTGAAAACCAAAATGTCAGAACTA
AGACTCTACTGTGACCTCCTTGTTCAGCAAGTAGATAAAACAAAAGAAGTGACCACAACT
GGTGTGTCCAATTCTGAGGAGGGAATTGATGTGGGAACTTTGCTGAAATCAACCTGTAAT
ACTTTTCTGAAGACCTTGGAAGAATGCATGCAGATCGCAAATGCAGCCTTCACCTCTGAG
CTGCTCTACCGCACTCCACCAGGATCACCTCAGCTGGCCATGCTCAAGTCCAGCAAGATG
AAACATCCTATTATACCAATTCATAATTCATTGGAAAGGCAAATGGAGTTGAGCACTTGT
GAAAATGGATCTTTAAATATGGAAATAAATGGTGAGGAAGAAATCCTAATGAAAAATAAG
AATTCCTTATATTTGAAATCTGCAGAGATAGACTGCAGCATATCAAGTGAGGAAAATACA
GATGATAATATAACAGTCCAAGGTGAAATAAGGAAGGAAGATGGAATGGAAAACCTGAAA
AATCATGACAATAACTTGACTCAGTCTGGATCAGACTCAAGTTGCTCTCCGGAATGCCTC
TGGGAGGAAGGCAAAGAAGTTATCCCAACTTTCTTTAGTACCATGAACACAAGCTTTAGT
GACATTGAACTTCTGGAAGACAGTGGCATTCCCACAGAAGCATTCTTGGCATCATGTTAT
GCTGTGGTTCCAGTATTAGACAAACTTGGCCCTACAGTGTTTGCTCCTGTTAAGATGGAT
CTTGTTGGAAATATTAAGAAAGTAAATCAGAAGTATATAACCAACAAAGAAGAGTTTACC
ACTCTCCAGAAGATAGTGCTGCACGAAGTGGAGGCGGATGTAGCCCAGGTTAGGAACTCA
GCGACTGAAGCCCTCTTGTGGCTGAAGAGAGGTCTCAAATTTTTGAAGGGATTTTTGACA
GAAGTGAAAAATGGGGAGAAGGATATCCAGACAGCCCTAAATAATGCATATGGTAAAACG
TTGCGGCAACACCATGGCTGGGTAGTTCGAGGGGTTTTTGCGTTAGCTTTAAGGGCAGCT
CCATCCTATGAAGATTTTGTGGCCGCGTTAACCGTAAAGGAAGGTGACCACCAGAAAGAA
GCTTTCAGTATTGGGATGCAGAGGGACCTCAGCCTTTACCTCCCTGCCATGGAGAAGCAG
CTGGCCATACTGGACACTTTATATGAGGTCCACGGGCTGGAATCTGATGAGGTGGTATGA
|
| Enzyme 47 GenBank Gene ID |
AK294857  |
| Enzyme 47 GeneCard ID |
PLEKHA8  |
| Enzyme 47 GenAtlas ID |
PLEKHA8  |
| Enzyme 47 HGNC ID |
HGNC:30037  |
| Enzyme 47 Chromosome Location |
7 |
| Enzyme 47 Locus |
7p21-p11.2 |
| Enzyme 47 SNPs |
SNPJam Report  |
| Enzyme 47 General References |
Not Available |
| Enzyme 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
17787 |
| Enzyme 48 Name |
T-cell surface glycoprotein CD1a |
| Enzyme 48 Synonyms |
- T-cell surface antigen T6/Leu-6
- hTa1 thymocyte antigen
- CD1a antigen
|
| Enzyme 48 Gene Name |
CD1A |
| Enzyme 48 Protein Sequence |
>T-cell surface glycoprotein CD1a
MLFLLLPLLAVLPGDGNADGLKEPLSFHVTWIASFYNHSWKQNLVSGWLSDLQTHTWDSN
SSTIVFLCPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCE
LHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLS
DTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRG
EQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSV
GFIILAVIVPLLLLIGLALWFRKRCFC
|
| Enzyme 48 Number of Residues |
327 |
| Enzyme 48 Molecular Weight |
37077.1 |
| Enzyme 48 Theoretical pI |
6.79 |
| Enzyme 48 GO Classification |
| Function |
| — |
| Process |
- antigen processing and presentation
- immune response
- immune system process
|
| Component |
- MHC class I protein complex
- MHC protein complex
- cell part
- macromolecular complex
- membrane
- protein complex
|
|
| Enzyme 48 General Function |
Involved in immune response |
| Enzyme 48 Specific Function |
Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells |
| Enzyme 48 Pathways |
Not Available |
| 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 |
180036  |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
P06126  |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
CD1A_HUMAN  |
| Enzyme 48 PDB ID |
1ONQ  |
| Enzyme 48 PDB File |
Show |
| Enzyme 48 3D Structure |
|
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>984 bp
ATGCTGTTTTTGCTACTTCCATTGTTAGCTGTTCTCCCAGGTGATGGCAATGCAGACGGG
CTCAAGGAGCCTCTCTCCTTCCATGTCATCTGGATCGCATCCTTTTACAACCATTCCTGG
AAACAAAATCTGGTCTCAGGTTGGCTGAGTGATTTGCAGACTCATACCTGGGACAGCAAT
TCCAGCACCATCGTTTTCCTGTGGCCCTGGTCCAGGGGAAACTTCAGCAATGAGGAGTGG
AAGGAACTGGAAACATTATTCCGTATACGCACCATTCGGTCATTTGAGGGAATTCGTAGA
TACGCCCATGAATTGCAGTTTGAATATCCTTTTGAGATACAGGTGACAGGAGGCTGTGAG
CTGCACTCTGGAAAGGTCTCAGGAAGCTTCTTGCAGTTAGCTTATCAAGGATCAGACTTT
GTGAGCTTCCAGAACAATTCATGGTTGCCATATCCAGTGGCTGGGAATATGGCCAAGCAT
TTCTGCAAAGTGCTCAATCAGAATCAGCATGAAAATGACATAACACACAATCTTCTCAGT
GACACCTGCCCACGTTTCATCTTGGGTCTTCTTGATGCAGGAAAGGCACATCTCCAGCGG
CAAGTGAAGCCCGAGGCCTGGCTGTCCCATGGCCCCAGTCCTGGCCCTGGCCATCTGCAG
CTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGGGGT
GAGCAGGAGCAGCAGGGCACTCAGCGAGGGGACATCTTGCCCAGTGCTGATGGGACATGG
TATCTCCGCGCAACCCTGGAGGTGGCCGCTGGGGAGGCAGCTGACCTGTCCTGTCGGGTG
AAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGAGCATCACAGTTCCGTG
GGCTTCATCATCTTGGCGGTGATAGTGCCTTTACTTCTTCTGATAGGTCTTGCGCTTTGG
TTCAGGAAACGCTGTTTCTGTTAA
|
| Enzyme 48 GenBank Gene ID |
M28825  |
| Enzyme 48 GeneCard ID |
CD1A  |
| Enzyme 48 GenAtlas ID |
CD1A  |
| Enzyme 48 HGNC ID |
HGNC:1634  |
| Enzyme 48 Chromosome Location |
1 |
| Enzyme 48 Locus |
1q22-q23 |
| Enzyme 48 SNPs |
SNPJam Report  |
| Enzyme 48 General References |
- Aruffo A, Seed B: Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts. J Immunol. 1989 Sep 1;143(5):1723-30. [PubMed
]
- Martin LH, Calabi F, Lefebvre FA, Bilsland CA, Milstein C: Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9189-93. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed
]
- Longley J, Kraus J, Alonso M, Edelson R: Molecular cloning of CD1a (T6), a human epidermal dendritic cell marker related to class I MHC molecules. J Invest Dermatol. 1989 Apr;92(4):628-31. [PubMed
]
- Calabi F, Milstein C: A novel family of human major histocompatibility complex-related genes not mapping to chromosome 6. Nature. 1986 Oct 9-15;323(6088):540-3. [PubMed
]
- Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed
]
- Salamero J, Bausinger H, Mommaas AM, Lipsker D, Proamer F, Cazenave JP, Goud B, de la Salle H, Hanau D: CD1a molecules traffic through the early recycling endosomal pathway in human Langerhans cells. J Invest Dermatol. 2001 Mar;116(3):401-8. [PubMed
]
- Vincent MS, Xiong X, Grant EP, Peng W, Brenner MB: CD1a-, b-, and c-restricted TCRs recognize both self and foreign antigens. J Immunol. 2005 Nov 15;175(10):6344-51. [PubMed
]
- Sloma I, Zilber MT, Vasselon T, Setterblad N, Cavallari M, Mori L, De Libero G, Charron D, Mooney N, Gelin C: Regulation of CD1a surface expression and antigen presentation by invariant chain and lipid rafts. J Immunol. 2008 Jan 15;180(2):980-7. [PubMed
]
- Zajonc DM, Elsliger MA, Teyton L, Wilson IA: Crystal structure of CD1a in complex with a sulfatide self antigen at a resolution of 2.15 A. Nat Immunol. 2003 Aug;4(8):808-15. Epub 2003 Jun 29. [PubMed
]
- Zajonc DM, Crispin MD, Bowden TA, Young DC, Cheng TY, Hu J, Costello CE, Rudd PM, Dwek RA, Miller MJ, Brenner MB, Moody DB, Wilson IA: Molecular mechanism of lipopeptide presentation by CD1a. Immunity. 2005 Feb;22(2):209-19. [PubMed
]
- Oteo M, Arribas P, Setien F, Parra JF, Mirones I, Gomez del Moral M, Martinez-Naves E: Structural characterization of two CD1A allelic variants. Hum Immunol. 2001 Oct;62(10):1137-41. [PubMed
]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
17788 |
| Enzyme 49 Name |
Glycolipid transfer protein domain-containing protein 1 |
| Enzyme 49 Synonyms |
Not Available |
| Enzyme 49 Gene Name |
GLTPD1 |
| Enzyme 49 Protein Sequence |
>Glycolipid transfer protein domain-containing protein 1
MDDSETGFNLKVVLVSFKQCLDEKEEVLLDPYIASWKGLVRFLNSLGTIFSFISKDVVSK
LRIMERLRGGPQSEHYRSLQAMVAHELSNRLVDLERRSHHPESGCRTVLRLHRALHWLQL
FLEGLRTSPEDARTSALCADSYNASLAAYHPWVVRRAVTVAFCTLPTREVFLEAMNVGPP
EQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
|
| Enzyme 49 Number of Residues |
214 |
| Enzyme 49 Molecular Weight |
24364.8 |
| Enzyme 49 Theoretical pI |
7.23 |
| Enzyme 49 GO Classification |
| Function |
- binding
- glycolipid binding
- glycolipid transporter activity
- lipid binding
- lipid transporter activity
- substrate-specific transporter activity
- transporter activity
|
| Process |
- establishment of localization
- glycolipid transport
- lipid transport
- transport
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 49 General Function |
Involved in glycolipid transporter activity |
| Enzyme 49 Specific Function |
Not Available |
| Enzyme 49 Pathways |
Not Available |
| Enzyme 49 Reactions |
Not Available |
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
56204961  |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q5TA50  |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
GLTD1_HUMAN  |
| Enzyme 49 PDB ID |
Not Available |
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>645 bp
ATGGATGACTCGGAGACAGGTTTCAATCTGAAAGTCGTCCTGGTCAGTTTCAAGCAGTGT
CTCGATGAGAAGGAAGAGGTCTTGCTGGACCCCTACATTGCCAGCTGGAAGGGCCTGGTC
AGGTTTCTGAACAGCCTGGGCACCATCTTCTCATTCATCTCCAAGGACGTGGTCTCCAAG
CTGCGGATCATGGAGCGCCTCAGGGGCGGCCCGCAGAGCGAGCACTACCGCAGCCTGCAG
GCCATGGTGGCCCACGAGCTGAGCAACCGGCTGGTGGACCTGGAGCGCCGCTCCCACCAC
CCGGAGTCTGGCTGCCGGACGGTGCTGCGCCTGCACCGCGCCCTGCACTGGCTGCAGCTG
TTCCTGGAGGGCCTGCGTACCAGCCCCGAGGACGCACGCACCTCCGCGCTCTGCGCCGAC
TCCTACAACGCCTCGCTGGCCGCCTACCACCCCTGGGTCGTGCGCCGCGCCGTCACCGTG
GCCTTCTGCACGCTGCCCACACGCGAGGTCTTCCTGGAGGCCATGAACGTGGGGCCCCCG
GAGCAGGCCGTGCAGATGCTAGGCGAGGCCCTCCCCTTCATCCAGCGTGTCTACAACGTC
TCCCAGAAGCTCTACGCCGAGCACTCCCTGCTGGACCTGCCCTAG
|
| Enzyme 49 GenBank Gene ID |
AL139287  |
| Enzyme 49 GeneCard ID |
GLTPD1  |
| Enzyme 49 GenAtlas ID |
GLTPD1  |
| Enzyme 49 HGNC ID |
HGNC:28116  |
| Enzyme 49 Chromosome Location |
1 |
| Enzyme 49 Locus |
1p36.33 |
| Enzyme 49 SNPs |
SNPJam Report  |
| Enzyme 49 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 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
17789 |
| Enzyme 50 Name |
T-cell surface glycoprotein CD1c |
| Enzyme 50 Synonyms |
- CD1c antigen
|
| Enzyme 50 Gene Name |
CD1C |
| Enzyme 50 Protein Sequence |
>T-cell surface glycoprotein CD1c
MLFLQFLLLALLLPGGDNADASQEHVSFHVIQIFSFVNQSWARGQGSGWLDELQTHGWDS
ESGTIIFLHNWSKGNFSNEELSDLELLFRFYLFGLTREIQDHASQDYSKYPFEVQVKAGC
ELHSGKSPEGFFQVAFNGLDLLSFQNTTWVPSPGCGSLAQSVCHLLNHQYEGVTETVYNL
IRSTCPRFLLGLLDAGKMYVHRQVRPEAWLSSRPSLGSGQLLLVCHASGFYPKPVWVTWM
RNEQEQLGTKHGDILPNADGTWYLQVILEVASEEPAGLSCRVRHSSLGGQDIILYWGHHF
SMNWIALVVIVPLVILIVLVLWFKKHCSYQDIL
|
| Enzyme 50 Number of Residues |
333 |
| Enzyme 50 Molecular Weight |
37653.7 |
| Enzyme 50 Theoretical pI |
6.09 |
| Enzyme 50 GO Classification |
| Function |
| — |
| Process |
- antigen processing and presentation
- immune response
- immune system process
|
| Component |
|
|
| Enzyme 50 General Function |
Involved in immune response |
| Enzyme 50 Specific Function |
Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells |
| Enzyme 50 Pathways |
Not Available |
| Enzyme 50 Reactions |
Not Available |
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
110618227  |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
P29017  |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
CD1C_HUMAN  |
| Enzyme 50 PDB ID |
Not Available |
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>1002 bp
ATGCTGTTTCTGCAGTTTCTGCTGCTAGCTCTTCTTCTCCCAGGTGGTGACAATGCAGAC
GCATCCCAGGAACACGTCTCCTTCCATGTCATCCAGATCTTCTCATTTGTCAACCAATCC
TGGGCACGAGGTCAGGGCTCAGGATGGCTGGACGAGTTGCAGACTCATGGCTGGGACAGT
GAATCAGGCACAATAATTTTCCTGCATAACTGGTCCAAGGGCAACTTCAGCAATGAAGAG
TTGTCAGACCTAGAGTTGTTATTTCGTTTCTACCTCTTTGGATTAACTCGGGAGATTCAA
GACCATGCAAGTCAAGATTACTCGAAATATCCCTTTGAAGTACAGGTGAAAGCGGGCTGT
GAGCTGCATTCTGGAAAGAGCCCAGAAGGCTTCTTTCAGGTAGCTTTCAACGGATTAGAT
TTACTGAGTTTCCAGAATACAACATGGGTGCCATCTCCAGGCTGTGGAAGTTTGGCCCAA
AGTGTCTGTCATCTACTCAATCATCAGTATGAAGGCGTCACAGAAACAGTGTATAATCTC
ATAAGAAGCACTTGCCCCCGATTTCTCTTGGGTCTCCTGGATGCAGGGAAGATGTATGTA
CACAGGCAAGTGAGGCCAGAAGCCTGGCTGTCCAGTCGCCCCAGCCTTGGGTCTGGCCAG
CTGTTGCTGGTTTGTCATGCCTCCGGCTTCTACCCAAAGCCTGTTTGGGTGACATGGATG
CGGAATGAACAGGAGCAACTGGGCACTAAACATGGTGATATTCTTCCTAATGCTGATGGG
ACATGGTATCTTCAGGTGATCCTGGAGGTGGCATCTGAGGAGCCTGCTGGCCTGTCTTGT
CGAGTGAGACACAGCAGTCTAGGAGGCCAGGACATCATCCTCTACTGGGGACACCACTTT
TCCATGAATTGGATTGCCTTGGTAGTGATAGTGCCCTTGGTGATTCTAATAGTCCTTGTG
TTATGGTTTAAGAAGCACTGCTCATATCAGGACATCCTGTGA
|
| Enzyme 50 GenBank Gene ID |
NM_001765.2  |
| Enzyme 50 GeneCard ID |
CD1C  |
| Enzyme 50 GenAtlas ID |
CD1C  |
| Enzyme 50 HGNC ID |
HGNC:1636  |
| Enzyme 50 Chromosome Location |
1 |
| Enzyme 50 Locus |
1q22-q23 |
| Enzyme 50 SNPs |
SNPJam Report  |
| Enzyme 50 General References |
- Martin LH, Calabi F, Lefebvre FA, Bilsland CA, Milstein C: Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9189-93. [PubMed
]
- Aruffo A, Seed B: Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts. J Immunol. 1989 Sep 1;143(5):1723-30. [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
]
- Han M, Hannick LI, DiBrino M, Robinson MA: Polymorphism of human CD1 genes. Tissue Antigens. 1999 Aug;54(2):122-7. [PubMed
]
- Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed
]
- Briken V, Jackman RM, Watts GF, Rogers RA, Porcelli SA: Human CD1b and CD1c isoforms survey different intracellular compartments for the presentation of microbial lipid antigens. J Exp Med. 2000 Jul 17;192(2):281-8. [PubMed
]
- Moody DB, Ulrichs T, Muhlecker W, Young DC, Gurcha SS, Grant E, Rosat JP, Brenner MB, Costello CE, Besra GS, Porcelli SA: CD1c-mediated T-cell recognition of isoprenoid glycolipids in Mycobacterium tuberculosis infection. Nature. 2000 Apr 20;404(6780):884-8. [PubMed
]
- Sugita M, van Der Wel N, Rogers RA, Peters PJ, Brenner MB: CD1c molecules broadly survey the endocytic system. Proc Natl Acad Sci U S A. 2000 Jul 18;97(15):8445-50. [PubMed
]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed
]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
17790 |
| Enzyme 51 Name |
Lipopolysaccharide-binding protein |
| Enzyme 51 Synonyms |
- LBP
|
| Enzyme 51 Gene Name |
LBP |
| Enzyme 51 Protein Sequence |
>Lipopolysaccharide-binding protein
MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLP
DFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRK
SFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNL
FHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATA
QMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLN
FSITDDMIPPDSNIRLTTKSFRPFVPRLARLYPNMNLELQGSVPSAPLLNFSPGNLSVDP
YMEIDAFVLLPSSSKEPVFRLSVATNVSATLTFNTSKITGFLKPGKVKVELKESKVGLFN
AELLEALLNYYILNTFYPKFNDKLAEGFPLPLLKRVQLYDLGLQIHKDFLFLGANVQYMR
V
|
| Enzyme 51 Number of Residues |
481 |
| Enzyme 51 Molecular Weight |
53383.0 |
| Enzyme 51 Theoretical pI |
6.68 |
| Enzyme 51 GO Classification |
| Function |
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 51 General Function |
Involved in lipid binding |
| Enzyme 51 Specific Function |
Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria. The LBP/LPS complex seems to interact with the CD14 receptor |
| Enzyme 51 Pathways |
Not Available |
| Enzyme 51 Reactions |
Not Available |
| Enzyme 51 Pfam Domain Function |
|
| Enzyme 51 Signals |
|
| Enzyme 51 Transmembrane Regions |
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
2653817  |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
P18428  |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
LBP_HUMAN  |
| Enzyme 51 PDB ID |
Not Available |
| Enzyme 51 Cellular Location |
Not Available |
| Enzyme 51 Gene Sequence |
>1446 bp
ATGGGGGCCTTGGCAAGAGCCCTGCCGTCCATACTGCTGGCATTGCTGCTTACGTCCACC
CCAGAGGCTCTGGGTGCCAACCCCGGCTTGGTCGCCAGGATCACCGACAAGGGACTGCAG
TATGCGGCCCAGGAGGGGCTATTGGCTCTGCAGAGTGAGCTGCTCAGGATCACGCTGCCT
GACTTCACCGGGGACTTGAGGATCCCCCACGTCGGCCGTGGGCGCTATGAGTTCCACAGC
CTGAAGATCCACAGCTGTGAGCTGCTTCACTCTGCGCTGAGGCCTGTCCCCGGCCAGGGC
CTGAGTCTCAGCATCTCCGACTCCTCCATCCGGGTCCAGGGCAGGTGGAAGGTGCGCAAG
TCATTCTTCAAACTACAGGGCTTCTTTGATGTCAGTGTCAAGGGCATCAGCATTTCGGTC
AACCTCCTGTTGGGCAGCGAGTCCTCCGGGAGGCCCACAGTTACTGCCTCCAGCTGCAGC
AGTGACATCGCTGACGTGGAGGTGGACATGTCGGGAGACTTGGGGTGGCTGTTGAACCTC
TTCCACAACCAGATTGAGTCCAAGTTCCAGAAAGTACTGGAGAGCAGGATTTGCGAAATG
ATCCAGAAATCGGTGTCCTCCGATCTACAGCCTTATCTCCAAACTCTGCCAGTTACAACA
GAGATTGACAGTTTCGCCGACATTGATTATAGCTTAGTGGAAGCCCCTCGGGCAACAGCC
CAGATGCTGGAGGTGATGTTTAAGGGTGAAATCTTTCATCGTAACCACAGTTCTCCAGTT
ACCCTCCTTGCTGCAGTCATGAGCCTTCCTGAGGAACACAACAAAATGGTCTACTTTGCC
ATCTCGGATTATGTCTTCAACACGGCCAGCCTGGTTTATCATGAGGAAGGATATCTGAAC
TTCTCCATCACAGATGACATGATACCGCCTGACTCTAATATCCGACTGACCACCAAGTCC
TTCCGACCCTTCGTCCCACGGTTAGCCAGGCTCTACCCCAACATGAACCTGGAACTCCAG
GGATCAGTGCCCTCTGCTCCGCTCCTGAACTTCAGCCCTGGGAATCTGTCTGTGGACCCC
TATATGGAGATAGATGCCTTTGTGCACCTGCCCAGCTCCAGCAAGGAGCCTGTCTTCCGG
CTCAGTGTGGCCACTAATGTGTCCGCCACCTTGACCTTCAATACCAGCAAGATCACTGGG
TTCCTGAAGCCAGGAAAGGTAAAAGTGGAACTGAAAGAATCCAAAGTTGGACTATTCAAT
GCAGAGCTGTTGGAAGCGCTCCTCAACTATTACATCCTTAACACCTTCTACCCCAAGTTC
AATGATAAGTTGGCCGAAGGCTTCCCCCTTCCTCTGCTGAAGCGTGTTCAGCTCTACGAC
CTTGGGCTGCAGATCCATAAGGACTTCCTGTTCTTGGGTGCCAATGTCCAATACATGAGA
GTTTGA
|
| Enzyme 51 GenBank Gene ID |
AF013512  |
| Enzyme 51 GeneCard ID |
LBP  |
| Enzyme 51 GenAtlas ID |
LBP  |
| Enzyme 51 HGNC ID |
HGNC:6517  |
| Enzyme 51 Chromosome Location |
2 |
| Enzyme 51 Locus |
20q11.23 |
| Enzyme 51 SNPs |
SNPJam Report  |
| Enzyme 51 General References |
- Schumann RR, Leong SR, Flaggs GW, Gray PW, Wright SD, Mathison JC, Tobias PS, Ulevitch RJ: Structure and function of lipopolysaccharide binding protein. Science. 1990 Sep 21;249(4975):1429-31. [PubMed
]
- Wilde CG, Seilhamer JJ, McGrogan M, Ashton N, Snable JL, Lane JC, Leong SR, Thornton MB, Miller KL, Scott RW, et al.: Bactericidal/permeability-increasing protein and lipopolysaccharide (LPS)-binding protein. LPS binding properties and effects on LPS-mediated cell activation. J Biol Chem. 1994 Jul 1;269(26):17411-6. [PubMed
]
- Hubacek JA, Buchler C, Aslanidis C, Schmitz G: The genomic organization of the genes for human lipopolysaccharide binding protein (LBP) and bactericidal permeability increasing protein (BPI) is highly conserved. Biochem Biophys Res Commun. 1997 Jul 18;236(2):427-30. [PubMed
]
- Kirschning CJ, Au-Young J, Lamping N, Reuter D, Pfeil D, Seilhamer JJ, Schumann RR: Similar organization of the lipopolysaccharide-binding protein (LBP) and phospholipid transfer protein (PLTP) genes suggests a common gene family of lipid-binding proteins. Genomics. 1997 Dec 15;46(3):416-25. [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
]
- 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
]
- Beamer LJ, Carroll SF, Eisenberg D: The BPI/LBP family of proteins: a structural analysis of conserved regions. Protein Sci. 1998 Apr;7(4):906-14. [PubMed
]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
17791 |
| Enzyme 52 Name |
Putative uncharacterized protein DKFZp434L0435 |
| Enzyme 52 Synonyms |
Not Available |
| Enzyme 52 Gene Name |
DKFZp434L0435 |
| Enzyme 52 Protein Sequence |
>Putative uncharacterized protein DKFZp434L0435
VAFCTLPTREVFLEAMNVGPPEQAVQMLGEALPFIQRVYNVSQKLYAEHSLLDLP
|
| Enzyme 52 Number of Residues |
55 |
| Enzyme 52 Molecular Weight |
6175.1 |
| Enzyme 52 Theoretical pI |
4.41 |
| Enzyme 52 GO Classification |
| Function |
- binding
- glycolipid binding
- glycolipid transporter activity
- lipid binding
- lipid transporter activity
- substrate-specific transporter activity
- transporter activity
|
| Process |
- establishment of localization
- glycolipid transport
- lipid transport
- transport
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 52 General Function |
Involved in glycolipid transporter activity |
| Enzyme 52 Specific Function |
Not Available |
| Enzyme 52 Pathways |
Not Available |
| Enzyme 52 Reactions |
Not Available |
| Enzyme 52 Pfam Domain Function |
Not Available |
| Enzyme 52 Signals |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
50978454  |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
Q9UFH6  |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
Q9UFH6_HUMAN  |
| Enzyme 52 PDB ID |
Not Available |
| Enzyme 52 Cellular Location |
Not Available |
| Enzyme 52 Gene Sequence |
>168 bp
GTGGCCTTCTGCACGCTGCCCACACGCGAGGTCTTCCTGGAGGCCATGAACGTGGGGCCC
CCGGAGCAGGCCGTGCAGATGCTAGGCGAGGCCCTCCCCTTCATCCAGCGTGTCTACAAC
GTCTCCCAGAAGCTCTACGCCGAGCACTCCCTGCTGGACCTGCCCTAG
|
| Enzyme 52 GenBank Gene ID |
AL122073  |
| Enzyme 52 GeneCard ID |
DKFZp434L0435  |
| Enzyme 52 GenAtlas ID |
DKFZp434L0435  |
| Enzyme 52 HGNC ID |
HGNC:28116  |
| Enzyme 52 Chromosome Location |
Not Available |
| Enzyme 52 Locus |
Not Available |
| Enzyme 52 SNPs |
SNPJam Report  |
| Enzyme 52 General References |
Not Available |
| Enzyme 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
17792 |
| Enzyme 53 Name |
T-cell surface glycoprotein CD1b |
| Enzyme 53 Synonyms |
- CD1b antigen
|
| Enzyme 53 Gene Name |
CD1B |
| Enzyme 53 Protein Sequence |
>T-cell surface glycoprotein CD1b
MLLLPFQLLAVLFPGGNSEHAFQGPTSFHVIQTSSFTNSTWAQTQGSGWLDDLQIHGWDS
DSGTAIFLKPWSKGNFSDKEVAELEEIFRVYIFGFAREVQDFAGDFQMKYPFEIQGIAGC
ELHSGGAIVSFLRGALGGLDFLSVKNASCVPSPEGGSRAQKFCALIIQYQGIMETVRILL
YETCPRYLLGVLNAGKADLQRQVKPEAWLSSGPSPGPGRLQLVCHVSGFYPKPVWVMWMR
GEQEQQGTQLGDILPNANWTWYLRATLDVADGEAAGLSCRVKHSSLEGQDIILYWRNPTS
IGSIVLAIIVPSLLLLLCLALWYMRRRSYQNIP
|
| Enzyme 53 Number of Residues |
333 |
| Enzyme 53 Molecular Weight |
36939.1 |
| Enzyme 53 Theoretical pI |
6.24 |
| Enzyme 53 GO Classification |
| Function |
| — |
| Process |
- antigen processing and presentation
- immune response
- immune system process
|
| Component |
|
|
| Enzyme 53 General Function |
Involved in immune response |
| Enzyme 53 Specific Function |
Antigen-presenting protein that binds self and non-self lipid and glycolipid antigens and presents them to T-cell receptors on natural killer T-cells |
| Enzyme 53 Pathways |
Not Available |
| Enzyme 53 Reactions |
Not Available |
| Enzyme 53 Pfam Domain Function |
|
| Enzyme 53 Signals |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
55859606  |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
P29016  |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
CD1B_HUMAN  |
| Enzyme 53 PDB ID |
1UQS  |
| Enzyme 53 PDB File |
Show |
| Enzyme 53 3D Structure |
|
| Enzyme 53 Cellular Location |
Not Available |
| Enzyme 53 Gene Sequence |
>1002 bp
ATGCTGTTTCTGCAGTTTCTGCTGCTAGCTCTTCTTCTCCCAGGTGGTGACAATGCAGAC
GCATCCCAGGAACACGTCTCCTTCCATGTCATCCAGATCTTCTCATTTGTCAACCAATCC
TGGGCACGAGGTCAGGGCTCAGGATGGCTGGACGAGTTGCAGACTCATGGCTGGGACAGT
GAATCAGGCACAATAATTTTCCTGCATAACTGGTCCAAGGGCAACTTCAGCAATGAAGAG
TTGTCAGACCTAGAGTTGTTATTTCGTTTCTACCTCTTTGGATTAACTCGGGAGATTCAA
GACCATGCAAGTCAAGATTACTCGAAATATCCCTTTGAAGTACAGGTGAAAGCGGGCTGT
GAGCTGCATTCTGGAAAGAGCCCAGAAGGCTTCTTTCAGGTAGCTTTCAACGGATTAGAT
TTACTGAGTTTCCAGAATACAACATGGGTGCCATCTCCAGGCTGTGGAAGTTTGGCCCAA
AGTGTCTGTCATCTACTCAATCATCAGTATGAAGGCGTCACAGAAACAGTGTATAATCTC
ATAAGAAGCACTTGCCCCCGATTTCTCTTGGGTCTCCTGGATGCAGGGAAGATGTATGTA
CACAGGCAAGTGAGGCCAGAAGCCTGGCTGTCCAGTCGCCCCAGCCTTGGGTCTGGCCAG
CTGTTGCTGGTTTGTCATGCCTCCGGCTTCTACCCAAAGCCTGTTTGGGTGACATGGATG
CGGAATGAACAGGAGCAACTGGGCACTAAACATGGTGATATTCTTCCTAATGCTGATGGG
ACATGGTATCTTCAGGTGATCCTGGAGGTGGCATCTGAGGAGCCTGCTGGCCTGTCTTGT
CGAGTGAGACACAGCAGTCTAGGAGGCCAGGACATCATCCTCTACTGGGGACACCACTTT
TCCATGAATTGGATTGCCTTGGTAGTGATAGTGCCCTTGGTGATTCTAATAGTCCTTGTG
TTATGGTTTAAGAAGCACTGCTCATATCAGGACATCCTGTGA
|
| Enzyme 53 GenBank Gene ID |
AL121986  |
| Enzyme 53 GeneCard ID |
CD1B  |
| Enzyme 53 GenAtlas ID |
CD1B  |
| Enzyme 53 HGNC ID |
HGNC:1635  |
| Enzyme 53 Chromosome Location |
1 |
| Enzyme 53 Locus |
1q22-q23 |
| Enzyme 53 SNPs |
SNPJam Report  |
| Enzyme 53 General References |
- Martin LH, Calabi F, Lefebvre FA, Bilsland CA, Milstein C: Structure and expression of the human thymocyte antigens CD1a, CD1b, and CD1c. Proc Natl Acad Sci U S A. 1987 Dec;84(24):9189-93. [PubMed
]
- Aruffo A, Seed B: Expression of cDNA clones encoding the thymocyte antigens CD1a, b, c demonstrates a hierarchy of exclusion in fibroblasts. J Immunol. 1989 Sep 1;143(5):1723-30. [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
]
- Martin LH, Calabi F, Milstein C: Isolation of CD1 genes: a family of major histocompatibility complex-related differentiation antigens. Proc Natl Acad Sci U S A. 1986 Dec;83(23):9154-8. [PubMed
]
- Shamshiev A, Donda A, Prigozy TI, Mori L, Chigorno V, Benedict CA, Kappos L, Sonnino S, Kronenberg M, De Libero G: The alphabeta T cell response to self-glycolipids shows a novel mechanism of CD1b loading and a requirement for complex oligosaccharides. Immunity. 2000 Aug;13(2):255-64. [PubMed
]
- Briken V, Jackman RM, Watts GF, Rogers RA, Porcelli SA: Human CD1b and CD1c isoforms survey different intracellular compartments for the presentation of microbial lipid antigens. J Exp Med. 2000 Jul 17;192(2):281-8. [PubMed
]
- Winau F, Schwierzeck V, Hurwitz R, Remmel N, Sieling PA, Modlin RL, Porcelli SA, Brinkmann V, Sugita M, Sandhoff K, Kaufmann SH, Schaible UE: Saposin C is required for lipid presentation by human CD1b. Nat Immunol. 2004 Feb;5(2):169-74. Epub 2004 Jan 11. [PubMed
]
- Wollscheid B, Bausch-Fluck D, Henderson C, O'Brien R, Bibel M, Schiess R, Aebersold R, Watts JD: Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins. Nat Biotechnol. 2009 Apr;27(4):378-86. Epub 2009 Apr 6. [PubMed
]
- Gadola SD, Zaccai NR, Harlos K, Shepherd D, Castro-Palomino JC, Ritter G, Schmidt RR, Jones EY, Cerundolo V: Structure of human CD1b with bound ligands at 2.3 A, a maze for alkyl chains. Nat Immunol. 2002 Aug;3(8):721-6. Epub 2002 Jul 15. [PubMed
]
- Batuwangala T, Shepherd D, Gadola SD, Gibson KJ, Zaccai NR, Fersht AR, Besra GS, Cerundolo V, Jones EY: The crystal structure of human CD1b with a bound bacterial glycolipid. J Immunol. 2004 Feb 15;172(4):2382-8. [PubMed
]
- Garcia-Alles LF, Versluis K, Maveyraud L, Vallina AT, Sansano S, Bello NF, Gober HJ, Guillet V, de la Salle H, Puzo G, Mori L, Heck AJ, De Libero G, Mourey L: Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid-binding groove of CD1b. EMBO J. 2006 Aug 9;25(15):3684-92. Epub 2006 Jul 27. [PubMed
]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
17793 |
| Enzyme 54 Name |
Glycolipid transfer protein |
| Enzyme 54 Synonyms |
- GLTP
|
| Enzyme 54 Gene Name |
GLTP |
| Enzyme 54 Protein Sequence |
>Glycolipid transfer protein
MALLAEHLLKPLPADKQIETGPFLEAVSHLPPFFDCLGSPVFTPIKADISGNITKIKAVY
DTNPAKFRTLQNILEVEKEMYGAEWPKVGATLALMWLKRGLRFIQVFLQSICDGERDENH
PNLIRVNATKAYEMALKKYHGWIVQKIFQAALYAAPYKSDFLKALSKGQNVTEEECLEKI
RLFLVNYTATIDVIYEMYTQMNAELNYKV
|
| Enzyme 54 Number of Residues |
209 |
| Enzyme 54 Molecular Weight |
23849.6 |
| Enzyme 54 Theoretical pI |
7.49 |
| Enzyme 54 GO Classification |
| Function |
- binding
- glycolipid binding
- glycolipid transporter activity
- lipid binding
- lipid transporter activity
- substrate-specific transporter activity
- transporter activity
|
| Process |
- establishment of localization
- glycolipid transport
- lipid transport
- transport
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 54 General Function |
Involved in glycolipid transporter activity |
| Enzyme 54 Specific Function |
Accelerates the intermembrane transfer of various glycolipids. Catalyzes the transfer of various glycosphingolipids between membranes but does not catalyze the transfer of phospholipids. May be involved in the intracellular translocation of glucosylceramides |
| Enzyme 54 Pathways |
Not Available |
| Enzyme 54 Reactions |
Not Available |
| Enzyme 54 Pfam Domain Function |
|
| Enzyme 54 Signals |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
Not Available |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
Q9NZD2  |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
GLTP_HUMAN  |
| Enzyme 54 PDB ID |
1SX6  |
| Enzyme 54 PDB File |
Show |
| Enzyme 54 3D Structure |
|
| Enzyme 54 Cellular Location |
Not Available |
| Enzyme 54 Gene Sequence |
>630 bp
ATGGCGCTGCTGGCGGAGCACTTGCTGAAGCCGCTGCCCGCGGACAAGCAGATCGAGACC
GGGCCCTTCCTCGAGGCGGTGTCCCACCTGCCGCCCTTCTTCGATTGCCTTGGGTCCCCA
GTGTTTACTCCCATCAAGGCAGACATAAGCGGCAACATCACGAAAATCAAAGCTGTGTAC
GACACCAACCCAGCCAAGTTCCGGACCCTGCAGAACATCCTGGAGGTGGAGAAAGAAATG
TATGGAGCAGAGTGGCCCAAAGTAGGGGCCACACTGGCGCTGATGTGGCTGAAAAGAGGC
CTCCGCTTCATCCAGGTCTTCCTCCAGAGCATCTGCGACGGGGAGCGGGACGAGAACCAC
CCCAACCTCATCCGTGTCAACGCCACCAAGGCCTACGAGATGGCCCTCAAGAAGTACCAT
GGCTGGATCGTGCAGAAGATCTTCCAGGCAGCACTGTACGCAGCACCCTATAAGTCTGAC
TTCCTGAAAGCGCTCTCCAAGGGGCAGAATGTTACGGAGGAGGAGTGCCTGGAGAAGATC
CGCCTCTTCCTAGTCAACTACACGGCGACCATCGATGTCATCTACGAGATGTACACCCAG
ATGAACGCTGAGCTCAACTACAAGGTGTAG
|
| Enzyme 54 GenBank Gene ID |
AF209704  |
| Enzyme 54 GeneCard ID |
GLTP  |
| Enzyme 54 GenAtlas ID |
GLTP  |
| Enzyme 54 HGNC ID |
HGNC:24867  |
| Enzyme 54 Chromosome Location |
1 |
| Enzyme 54 Locus |
12q24.11 |
| Enzyme 54 SNPs |
SNPJam Report  |
| Enzyme 54 General References |
- Li XM, Malakhova ML, Lin X, Pike HM, Chung T, Molotkovsky JG, Brown RE: Human glycolipid transfer protein: probing conformation using fluorescence spectroscopy. Biochemistry. 2004 Aug 10;43(31):10285-94. [PubMed
]
- Zou X, Chung T, Lin X, Malakhova ML, Pike HM, Brown RE: Human glycolipid transfer protein (GLTP) genes: organization, transcriptional status and evolution. BMC Genomics. 2008 Feb 8;9:72. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Rao CS, Lin X, Pike HM, Molotkovsky JG, Brown RE: Glycolipid transfer protein mediated transfer of glycosphingolipids between membranes: a model for action based on kinetic and thermodynamic analyses. Biochemistry. 2004 Nov 2;43(43):13805-15. [PubMed
]
- Tuuf J, Mattjus P: Human glycolipid transfer protein--intracellular localization and effects on the sphingolipid synthesis. Biochim Biophys Acta. 2007 Nov;1771(11):1353-63. Epub 2007 Sep 21. [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
]
- Malinina L, Malakhova ML, Teplov A, Brown RE, Patel DJ: Structural basis for glycosphingolipid transfer specificity. Nature. 2004 Aug 26;430(7003):1048-53. [PubMed
]
- Malinina L, Malakhova ML, Kanack AT, Lu M, Abagyan R, Brown RE, Patel DJ: The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure. PLoS Biol. 2006 Nov;4(11):e362. [PubMed
]
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| Enzyme 54 Metabolite References |
Not Available |