|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5463 |
| Enzyme 1 Name |
Lipid phosphate phosphohydrolase 2 |
| Enzyme 1 Synonyms |
- Phosphatidic acid phosphatase 2c
- Phosphatidate phosphohydrolase type 2c
- PAP2c
- PAP- 2c
- PAP2-gamma
- PAP2-G
|
| Enzyme 1 Gene Name |
PPAP2C |
| Enzyme 1 Protein Sequence |
>Lipid phosphate phosphohydrolase 2
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGV
TITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMI
GRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLA
LYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTV
CYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
|
| Enzyme 1 Number of Residues |
288 |
| Enzyme 1 Molecular Weight |
32574 |
| Enzyme 1 Theoretical pI |
8.44 |
| Enzyme 1 GO Classification |
Not Available |
| Enzyme 1 General Function |
Lipid transport and metabolism |
| Enzyme 1 Specific Function |
Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). In addition it hydrolyzes lysophosphatidic acid (LPA), ceramide-1-phosphate (C-1-P) and sphingosine-1- phosphate (S-1-P). The relative catalytic efficiency is PA > C-1-P > LPA > S-1-P |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
Not Available |
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
3123896  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O43688  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
LPP2_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>867 bp
ATGCAGCGGAGGTGGGTCTTCGTGCTGCTCGACGTGCTGTGCTTACTGGTCGCCTCCCTG
CCCTTCGCTATCCTGACGCTGGTGAACGCCCCGTACAAGCGAGGATTTTACTGCGGGGAT
GACTCCATCCGGTACCCCTACCGTCCAGATACCATCACCCACGGGCTCATGGCTGGGGTC
ACCATCACGGCCACCGTCATCCTTGTCTCGGCCGGGGAAGCCTACCTGGTGTACACAGAC
CGGCTCTATTCTCGCTCGGACTTCAACAACTACGTGGCTGCTGTATACAAGGTGCTGGGG
ACCTTCCTGTTTGGGGCTGCCGTGAGCCAGTCTCTGACAGACCTGGCCAAGTACATGATT
GGGCGTCTGAGGCCCAACTTCCTAGCCGTCTGCGACCCCGACTGGAGCCGGGTCAACTGC
TCGGTCTATGTGCAGCTGGAGAAGGTGTGCAGGGGAAACCCTGCTGATGTCACCGAGGCC
AGGTTGTCTTTCTACTCGGGACACTCTTCCTTTGGGATGTACTGCATGGTGTTCTTGGCG
CTGTATGTGCAGGCACGACTCTGTTGGAAGTGGGCACGGCTGCTGCGACCCACAGTCCAG
TTCTTCCTGGTGGCCTTTGCCCTCTACGTGGGCTACACCCGCGTGTCTGATTACAAACAC
CACTGGAGCGATGTCCTTGTTGGCCTCCTGCAGGGGGCACTGGTGGCTGCCCTCACTGTC
TGCTACATCTCAGACTTCTTCAAAGCCCGACCCCCACAGCACTGTCTGAAGGAGGAGGAG
CTGGAACGGAAGCCCAGCCTGTCACTGACGTTGACCCTGGGCGAGGCTGACCACAACCAC
TATGGATACCCGCACTCCTCCTCCTGA
|
| Enzyme 1 GenBank Gene ID |
AF035959  |
| Enzyme 1 GeneCard ID |
PPAP2C  |
| Enzyme 1 GenAtlas ID |
PPAP2C  |
| Enzyme 1 HGNC ID |
HGNC:9230  |
| Enzyme 1 Chromosome Location |
19 |
| Enzyme 1 Locus |
19p13 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed
]
- Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5469 |
| Enzyme 2 Name |
Lipid phosphate phosphohydrolase 1 |
| Enzyme 2 Synonyms |
- Phosphatidic acid phosphatase 2a
- Phosphatidate phosphohydrolase type 2a
- PAP2a
- PAP- 2a
- PAP2-alpha
|
| Enzyme 2 Gene Name |
PPAP2A |
| Enzyme 2 Protein Sequence |
>Lipid phosphate phosphohydrolase 1
MFDKTRLPYVALDVLCVLLAGLPFAILTSRHTPFQRGVFCNDESIKYPYKEDTIPYALLG
GIIIPFSIIVIILGETLSVYCNLLHSNSFIRNNYIATIYKAIGTFLFGAAASQSLTDIAK
YSIGRLRPHFLDVCDPDWSKINCSDGYIEYYICRGNAERVKEGRLSFYSGHSSFSMYCML
FVALYLQARMKGDWARLLRPTLQFGLVAVSIYVGLSRVSDYKHHWSDVLTGLIQGALVAI
LVAVYVSDFFKERTSFKERKEEDSHTTLHETPTTGNHYPSNHQP
|
| Enzyme 2 Number of Residues |
284 |
| Enzyme 2 Molecular Weight |
32156 |
| Enzyme 2 Theoretical pI |
8.06 |
| Enzyme 2 GO Classification |
Not Available |
| Enzyme 2 General Function |
Lipid transport and metabolism |
| Enzyme 2 Specific Function |
Broad-specificity phosphohydrolase that dephosphorylates exogenous bioactive glycerolipids and sphingolipids. Catalyzes the conversion of phosphatidic acid (PA) to diacylglycerol (DG). Pivotal regulator of lysophosphatidic acid (LPA) signaling in the cardiovascular system. Major enzyme responsible of dephosphorylating LPA in platelets, which terminates signaling actions of LPA. May control circulating, and possibly also regulate localized, LPA levels resulting from platelet activation. It has little activity towards ceramide-1-phosphate (C-1-P) and sphingosine-1-phosphate (S-1-P). The relative catalytic efficiency is LPA > PA > S-1-P > C-1-P. It's down-regulation may contribute to the development of colon adenocarcinoma |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- A 3-sn-phosphatidate + H2O = a 1,2-diacyl-sn-glycerol + phosphate
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
Not Available |
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
2467298  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
O14494  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
LPP1_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>855 bp
ATGTTCGACAAGACGCGGCTGCCGTACGTGGCCCTCGATGTGCTCTGCGTGTTGCTGGCT
GGATTGCCTTTTGCAATTCTTACTTCAAGGCATACCCCCTTCCAACGAGGAGTATTCTGT
AATGATGAGTCCATCAAGTACCCTTACAAAGAAGACACCATACCTTATGCGTTATTAGGT
GGAATAATCATTCCATTCAGTATTATCGTTATTATTCTTGGAGAAACCCTGTCTGTTTAC
TGTAACCTTTTGCACTCAAATTCCTTTATCAGGAATAACTACATAGCCACTATTTACAAA
GCCATTGGAACCTTTTTATTTGGTGCAGCTGCTAGTCAGTCCCTGACTGACATTGCCAAG
TATTCAATAGGCAGACTGCGGCCTCACTTCTTGGATGTTTGTGATCCAGATTGGTCAAAA
ATCAACTGCAGCGATGGTTACATTGAATACTACATATGTCGAGGGAATGCAGAAAGAGTT
AAGGAAGGCAGGTTGTCCTTCTATTCAGGCCACTCTTCGTTTTCCATGTACTGCATGCTG
TTTGTGGCACTTTATCTTCAAGCCAGGATGAAGGGAGACTGGGCAAGACTCTTACGCCCC
ACACTGCAATTTGGTCTTGTTGCCGTATCCATTTATGTGGGCCTTTCTCGAGTTTCTGAT
TATAAACACCACTGGAGCGATGTGTTGACTGGACTCATTCAGGGAGCTCTGGTTGCAATA
TTAGTTGCTGTATATGTATCGGATTTCTTCAAAGAAAGAACTTCTTTTAAAGAAAGAAAA
GAGGAGGACTCTCATACAACTCTGCATGAAACACCAACAACTGGGAATCACTATCCGAGC
AATCACCAGCCTTGA
|
| Enzyme 2 GenBank Gene ID |
AB000888  |
| Enzyme 2 GeneCard ID |
PPAP2A  |
| Enzyme 2 GenAtlas ID |
PPAP2A  |
| Enzyme 2 HGNC ID |
HGNC:9228  |
| Enzyme 2 Chromosome Location |
5 |
| Enzyme 2 Locus |
5q11 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Kai M, Wada I, Imai S, Sakane F, Kanoh H: Cloning and characterization of two human isozymes of Mg2+-independent phosphatidic acid phosphatase. J Biol Chem. 1997 Sep 26;272(39):24572-8. [PubMed
]
- Leung DW, Tompkins CK, White T: Molecular cloning of two alternatively spliced forms of human phosphatidic acid phosphatase cDNAs that are differentially expressed in normal and tumor cells. DNA Cell Biol. 1998 Apr;17(4):377-85. [PubMed
]
- Ulrix W, Swinnen JV, Heyns W, Verhoeven G: Identification of the phosphatidic acid phosphatase type 2a isozyme as an androgen-regulated gene in the human prostatic adenocarcinoma cell line LNCaP. J Biol Chem. 1998 Feb 20;273(8):4660-5. [PubMed
]
- Roberts R, Sciorra VA, Morris AJ: Human type 2 phosphatidic acid phosphohydrolases. Substrate specificity of the type 2a, 2b, and 2c enzymes and cell surface activity of the 2a isoform. J Biol Chem. 1998 Aug 21;273(34):22059-67. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5671 |
| Enzyme 3 Name |
Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1 |
| Enzyme 3 Synonyms |
- Forssman glycolipid synthetase-like protein
|
| Enzyme 3 Gene Name |
GBGT1 |
| Enzyme 3 Protein Sequence |
>Globoside alpha-1,3-N-acetylgalactosaminyltransferase 1
MHRRRLALGLGFCLLAGTSLSVLWVYLENWLPVSYVPYYLPCPEIFNMKLHYKREKPLQP
VVWSQYPQPKLLEHRPTQLLTLTPWLAPIVSEGTFNPELLQHIYQPLNLTIGVTVFAVGK
YTHFIQSFLESAEEFFMRGYRVHYYIFTDNPAAVPGVPLGPHRLLSSIPIQGHSHWEETS
MRRMETISQHIAKRAHREVDYLFCLDVDMVFRNPWGPETLGDLVAAIHPSYYAVPRQQFP
YERRRVSTAFVADSEGDFYYGGAVFGGQVARVYEFTRGCHMAILADKANGIMAAWREESH
LNRHFISNKPSKVLSPEYLWDDRKPQPPSLKLIRFSTLDKDISCLRS
|
| Enzyme 3 Number of Residues |
347 |
| Enzyme 3 Molecular Weight |
40128 |
| Enzyme 3 Theoretical pI |
8.63 |
| Enzyme 3 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- carbohydrate metabolism
- macromolecule metabolism
- metabolism
- physiological process
|
| Component |
|
|
| Enzyme 3 General Function |
Not Available |
| Enzyme 3 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 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
Not Available |
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
Not Available |
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
6272650  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q8N5D6  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
GBGT1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1044 bp
ATGCATCGCCGGAGACTGGCCCTGGGTCTGGGGTTCTGCCTGTTGGCGGGCACAAGCCTC
AGTGTCCTGTGGGTGTATCTTGAGAACTGGCTGCCAGTCTCCTATGTCCCCTATTATCTC
CCCTGCCCAGAGATCTTCAACATGAAGCTGCACTACAAGAGGGAGAAGCCACTCCAGCCC
GTGGTATGGTCACAGTACCCTCAGCCCAAGCTGCTGGAGCACAGGCCCACACAGCTGCTG
ACACTCACACCCTGGTTGGCGCCCATCGTCTCCGAGGGAACCTTCAACCCAGAGCTTCTG
CAGCACATCTACCAGCCACTGAACCTGACCATTGGGGTCACGGTGTTTGCCGTGGGGAAG
TACACTCATTTCATCCAGTCCTTCCTGGAGTCAGCCGAGGAGTTCTTCATGCGTGGGTAC
CGGGTGCACTACTACATCTTCACTGACAACCCTGCAGCCGTTCCCGGGGTCCCGCTGGGT
CCCCACCAGCTTCTCAGCTCCATCCCCATCCAGGGTCACTCCCACTGGGAGGAGACATCC
ATGCGCCGGATGGAGACCATCAGCCAGCACATTGCTAAGAGGGCTCACCGGGAGGTGGAC
TACTTTTTCTGCCTTGATGTGGACATGGTGTTTCGGAACCCGTGGGGCCCTGAGACCTTG
GGAGACCTGGTGGCTGCCATTCACCCAAGCTACTACGCCGTTCCCCGCCAGCAGTTCCCC
TATGAGCGCAGGCGTGTTTCCACTGCCTTTGTGGCAGACAGGGAAGGGGACTTCTATTAT
GGTGGGGCAGTCTTCGGGGGGCAGGTGGCCAGGGTATATGAGTTTACTAGGGGCTGCCAC
ATGGCCATCCTGGCGGACAAGGCCAATGGCATCATGGCTGCCTGGCGGGAGGAAAGCCAC
CTGAACCGTCACTTCATCTCAAACAAGCCGTCCAAGGTGCTGTCCCCCGAGTACCTCTGG
GACGACAGGAAGCCCCAGCCACCCAGCCTGAAGCTGATCCGCTTTTCTACACTGGACAAG
GATATCAGCTGCCTGAGGAGCTGA
|
| Enzyme 3 GenBank Gene ID |
AF163572  |
| Enzyme 3 GeneCard ID |
GBGT1  |
| Enzyme 3 GenAtlas ID |
GBGT1  |
| Enzyme 3 HGNC ID |
HGNC:20460  |
| Enzyme 3 Chromosome Location |
Not Available |
| Enzyme 3 Locus |
Not Available |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5829 |
| Enzyme 4 Name |
N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase |
| Enzyme 4 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class L protein
- PIG-L
|
| Enzyme 4 Gene Name |
PIGL |
| Enzyme 4 Protein Sequence |
>N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPT
VLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGM
QWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVL
TLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIF
SRYMRINSLSFL
|
| Enzyme 4 Number of Residues |
252 |
| Enzyme 4 Molecular Weight |
28532 |
| Enzyme 4 Theoretical pI |
8.23 |
| Enzyme 4 GO Classification |
Not Available |
| Enzyme 4 General Function |
Not Available |
| Enzyme 4 Specific Function |
Involved in the second step of GPI biosynthesis. De-N- acetylation of N-acetylglucosaminyl-phosphatidylinositol |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
- 6-(N-acetyl-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = 6-(alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + acetate
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
Not Available |
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
4239986  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q9Y2B2  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PIGL_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>759 bp
ATGGAAGCAATGTGGCTCCTGTGTGTGGCGTTGGCGGTCTTGGCATGGGGCTTCCTCTGG
GTTTGGGACTCCTCAGAACGAATGAAGAGTCGGGAGCAGGGAGGACGGCTGGGAGCCGAA
AGCCGGACCCTGCTGGTCATAGCGCACCCTGACGATGAAGCCATGTTTTTTGCTCCCACA
GTGCTAGGCTTGGCCCGCCTAAGGCACTGGGTGTACCTGCTTTGCTTCTCTGCAGGAAAT
TACTACAATCAAGGAGAGACTCGTAAGAAAGAACTTTTGCAGAGCTGTGATGTTTTGGGG
ATTCCACTCTCCAGTGTAATGATTATTGACAACAGGGATTTCCCAGATGACCCAGGCATG
CAGTGGGACACAGAGCACGTGGCCAGAGTCCTCCTTCAGCACATAGAAGTGAATGGCATC
AATCTGGTGGTGACTTTCGATGCAGGGGGAGTAAGTGGCCACAGCAATCACATTGCTCTG
TATGCAGCTGTGAGGGCCCTGCACTCAGAAGGGAAGTTACCTAAAGGGTGCTCTGTGCTC
ACGCTTCAGTCTGTGAATGTGCTGCGCAAGTACATCTCCCTTCTGGATCTGCCCTTGTCT
CTGCTTCATACGCAGGATGTCCTCTTCGTGCTCAACAGCAAAGAAGTGGCACAGGCCAAG
AAAGCCATGTCCTGCCACCGCAGCCAGCTCCTCTGGTTCCGCCGCCTCTACATTATCTTC
TCCCGGTACATGAGAATCAACTCACTGAGCTTCCTCTGA
|
| Enzyme 4 GenBank Gene ID |
AB017165  |
| Enzyme 4 GeneCard ID |
PIGL  |
| Enzyme 4 GenAtlas ID |
PIGL  |
| Enzyme 4 HGNC ID |
HGNC:8966  |
| Enzyme 4 Chromosome Location |
17 |
| Enzyme 4 Locus |
17p12-p11.2 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
6228 |
| Enzyme 5 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q |
| Enzyme 5 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class Q protein
- PIG-Q
- N-acetylglucosamyl transferase component GPI1
|
| Enzyme 5 Gene Name |
PIGQ |
| Enzyme 5 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit Q
MVLKAFFPTCCVSTDSGLLVGRWVPEQSSAVVLAVLHFPFIPIQVKQLLAQVRQASQVGV
AVLGTWCHCRQEPEESLGRFLESLGAVFPHEPWLRLCRERGGTFWSCEATHRQAPTAPGA
PGEDQVMLIFYDQRQVLLSQLHLPTVLPDRQAGATTASTGGLAAVFDTVARSEVLFRSDR
FDEGPVRLSHWQSEGVEASILAELARRASGPICLLLASLLSLVSAVSACRVFKLWPLSFL
GSKLSTCEQLRHRLEHLTLIFSTRKAENPAQLMRKANTVASVLLDVALGLMLLSWLHGRS
RIGHLADALVPVADHVAEELQHLLQWLMGAPAGLKMNRALDQVLGRFFLYHIHLWISYIH
LMSPFVEHILWHVGLSACLGLTVALSLLSDIIALLTFHIYCFYVYGARLYCLKIHGLSSL
WRLFRGKKWNVLRQRVDSCSYDLDQLFIGTLLFTILLFLLPTTALYYLVFTLLRLLVVAV
QGLIHLLVDLINSLPLYSLGLRLCRPYRLADKPTALQPRGAHLPPPQLWLPPQALLGRPV
PQAVPWGAHLPLEAERGQAGLRELLARLAPPHGHSQPSALPGWHQLSWRMSCALWTLLCA
PEHGRPCYHTLGLEVIGSEQMWGWPARLAALHHWHCLPWDPLPTCCGHHGGEHSNPRCPE
HCPMPTLCTQVQRVRPPQQPQVEGWSPWGLPSGSALAVGVEGPCQDEPPSPRHPLAPSAE
QHPASGGLKQSLTPVPSGPGPSLPEPHGVYLRMFPGEVAL
|
| Enzyme 5 Number of Residues |
760 |
| Enzyme 5 Molecular Weight |
84083 |
| Enzyme 5 Theoretical pI |
8.08 |
| Enzyme 5 GO Classification |
| Function |
- UDP-glycosyltransferase activity
- acetylglucosaminyltransferase activity
- catalytic activity
- phosphatidylinositol N-acetylglucosaminyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- GPI anchor biosynthesis
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid lipidation
- protein modification
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 5 General Function |
Not Available |
| Enzyme 5 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 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
- UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
- 278-298
349-371
378-400
446-468
475-497
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
2623158  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9BRB3  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PIGQ_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1746 bp
ATGGTGCTCAAGGCCTTCTTCCCCACGTGCTGCGTCTCGGCGGACAGCGGGCTGCTGGTG
GGACGGTGGGTGCCGGAGCAGAGCAGCGCCGTGGTCCTGGCGGTCCTGCACTTTCCCTTC
ATCCCCATCCAGGTCAAGCAGCTCCTGGCCCAGGTGCGGCAGGCCAGCCAGGTGGGCGTG
GCCGTGCTGGGCACCTGGTGCCACTGCCGGCAGGAGCCCGAGGAGAGCCTGGGCCGCTTC
CTGGAGAGCCTGGGTGCTGTCTTCCCCCATGAGCCCTGGCTGCGGCTGTGCCGGGAGAGA
GGCGGCACGTTCTGGAGCTGCGAGGCCACCCACCGGCAAGCGCCCACTGCCCCCGGTGCC
CCTGGTGAGGACCAGGTCATGCTCATCTTCTATGACCAGCGCCAGGTGTTGCTGTCACAG
CTACACCTGCCCACCGTCCTGCCCGACCGCCAGGCTGGAGCCACCACTGCCAGCACGGGG
GGCCTGGCTGCCGTCTTCGACACGGTAGCACGCAGTGAGGTGCTCTTCCGCAGTGACCGC
TTTGATGAGGGCCCCGTGCGGCTGAGCCACTGGCAGTCGGAGGGCGTGGAGGCCAGCATC
CTCGCGGAGCTGGCCAGGCGAGCCTCGGGACCCATTTGTCTGCTGTTGGCCAGCCTGCTG
TCGCTGGTCTCAGCTGTCAGTGCCTGCCGAGTGTTCAAGCTCTGGCCCCTGTCCTTCCTC
GGGAGCAAACTCTCCACGTGCGAACAGCTCCGGCACCGGCTGGAGCACCTCACGCTAATC
TTCAGTACACGGAAGGCGGAGAACCCTGCCCAGCTGATGAGGAAGGCCAACACGGTGGCC
TCTGTGCTGCTGGACGTGGCCCTGGGCCTCATGCTGCTGTCCTGGCTCCACGGGAGAAGC
CGCATCGGGCATCTGGCCGACGCCCTCGTTCCTGTGGCTGACCACGTGGCCGAGGAGCTC
CAGCATCTGCTGCAGTGGCTGATGGGTGCTCCCGCCGGGCTCAAGATGAACCGTGCACTG
GACCAGGTGCTGGGCCGCTTCTTCCTCTACCACATCCACCTGTGGATCAGCTACATCCAC
CTCATGTCCCCCTTCGTGGAGCACATCCTTTGGCACGTGGGCCTCTCGGCCTGCCTGGGC
CTGACGGTGGCCCTGTCCCTCCTCTCGGACATTATCGCCCTCCTCACCTTCCACATCTAC
TGCTTTTACGTCTATGGAGCCAGGCTGTACTGCCTGAAGATCCATGGCCTGTCCTCACTG
TGGCGTCTGTTCCGGGGGAAGAAGTGGAACGTTCTGCGCCAGCGCGTGGACTCCTGTTCC
TATGACCTGGACCAGCTGTTCATCGGGACTCTGCTCTTCACCATCCTGCTCTTCCTCCTG
CCTACCACAGCCCTGTACTACCTGGTGTTCACCCTGCTCCGGCTCCTGGTGGTCGCCGTG
CAGGGCCTGATCCATCTGCTGGTGGACCTCATCAACTCCCTGCCGCTGTACTCACTGGGT
CTTCGGCTCTGCCGGCCCTACAGGCTGGCGGCTGGCGTGAAGTTCCGTGTCCTCCGGCAC
GAGGCCAGCAGGCCCCTCCGCCTCCTGATGCAGATAAACCCACTGCCCTACAGCCGCGTG
GTGCACACCTACCGCCTCCCCAGCTGTGGCTGCCACCCCAAGCACTCCTGGGGCGCCCTG
TGCCGCAAGCTGTTCCTTGGGGAGCTCATCTACCCCTGGAGGCAGAGAGGGGACAAGCAG
GACTGA
|
| Enzyme 5 GenBank Gene ID |
AF030177  |
| Enzyme 5 GeneCard ID |
PIGQ  |
| Enzyme 5 GenAtlas ID |
PIGQ  |
| Enzyme 5 HGNC ID |
HGNC:14135  |
| Enzyme 5 Chromosome Location |
16 |
| Enzyme 5 Locus |
16p13.3 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 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
]
- 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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6229 |
| Enzyme 6 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit A |
| Enzyme 6 Synonyms |
- GlcNAc-PI synthesis protein
- Phosphatidylinositol- glycan biosynthesis class A protein
- PIG-A
|
| Enzyme 6 Gene Name |
PIGA |
| Enzyme 6 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit A
MACRGGAGNGHRASATLSRVSPGSLYTCRTRTHNICMVSDFFYPNMGGVESHIYQLSQCL
IERGHKVIIVTHAYGNRKGIRYLTSGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRE
RVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNH
IICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSITIVVVSRLVYRKGI
DLLSGIIPELCQKYPDLNFIIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLV
QGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPENLIILCEPSVKSLCEGLE
KAIFQLKSGTLPAPENIHNIVKTFYTWRNVAERTEKVYDRVSVEAVLPMDKRLDRLISHC
GPVTGYIFALLAVFNFLFLIFLRWMTPDSIIDVAIDATGPRGAWTNNYSHSKRGGENNEI
SETR
|
| Enzyme 6 Number of Residues |
484 |
| Enzyme 6 Molecular Weight |
54127 |
| Enzyme 6 Theoretical pI |
8.41 |
| Enzyme 6 GO Classification |
| Function |
| — |
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Cell wall/membrane/envelope biogenesis |
| Enzyme 6 Specific Function |
Necessary for the synthesis of N-acetylglucosaminyl- phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
- UDP-N-acetyl-D-glucosamine + 1-phosphatidyl-1D-myo-inositol = UDP + 6(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
219994  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P37287  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PIGA_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 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 6 GenBank Gene ID |
D11466  |
| Enzyme 6 GeneCard ID |
PIGA  |
| Enzyme 6 GenAtlas ID |
PIGA  |
| Enzyme 6 HGNC ID |
HGNC:8957  |
| Enzyme 6 Chromosome Location |
X |
| Enzyme 6 Locus |
Xp22.1 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 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
]
- 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
]
- 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 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6230 |
| Enzyme 7 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit H |
| Enzyme 7 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class H protein
- PIG-H
|
| Enzyme 7 Gene Name |
PIGH |
| Enzyme 7 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit H
MEDERSFSDICGGRLALQRRYYSPSCREFCLSCPRLSLRSLTAVTCTVWLAAYGLFTLCE
NSMILSAAIFITLLGLLGYLHFVKIDQETLLIIDSLGIQMTSSYASGKESTTFIEMGKVK
DIVINEAIYMQKVIYYLCILLKDPVEPHGISQVVPVFQSAKPRLDCLIEVYRSCQEILAH
QKATSTSP
|
| Enzyme 7 Number of Residues |
188 |
| Enzyme 7 Molecular Weight |
21081 |
| Enzyme 7 Theoretical pI |
6.72 |
| Enzyme 7 GO Classification |
Not Available |
| Enzyme 7 General Function |
Not Available |
| 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
|
| Enzyme 7 Pfam Domain Function |
Not Available |
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
404726  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q14442  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PIGH_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>567 bp
ATGGAGGATGAGCGGAGCTTTTCGGATATCTGCGGCGGCCGCCTGGCGCTGCAGCGCCGC
TACTACTCCCCGTCCTGCCGGGAATTCTGCCTCAGCTGCCCTCGGCTCTCGCTGCGTTCG
CTCACCGCTGTCACCTGCACGGTGTGGCTGGCGGCCTACGGACTCTTCACCCTCTGCGAG
AACAGCATGATCCTCTCTGCTGCCATCTTCATCACCCTCTTAGGTCTGCTTGGTTATCTC
CATTTTGTGAAGATTGATCAGGAGACTCTGTTAATCATTGATTCCCTTGGCATTCAGATG
ACTTCATCTTATGCTTCAGGCAAAGAAAGCACTACCTTCATAGAAATGGGCAAGGTCAAG
GATATTGTCATCAATGAGGCCATTTACATGCAGAAGGTGATTTACTACCTCTGCATCTTA
TTGAAAGATCCAGTGGAACCACATGGGATATCCCAAGTAGTACCCGTCTTCCAGAGTGCC
AAGCCCCGGCTGGACTGCTTGATTGAAGTATACAGGAGCTGCCAGGAGATCCTGGCACAC
CAGAAAGCCACATCAACAAGCCCATGA
|
| Enzyme 7 GenBank Gene ID |
L19783  |
| Enzyme 7 GeneCard ID |
PIGH  |
| Enzyme 7 GenAtlas ID |
PIGH  |
| Enzyme 7 HGNC ID |
HGNC:8964  |
| Enzyme 7 Chromosome Location |
14 |
| Enzyme 7 Locus |
14q11-q24 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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
]
- 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
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
6231 |
| Enzyme 8 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit P |
| Enzyme 8 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class P protein
- PIG-P
- Down syndrome critical region protein 5
- Down syndrome critical region protein C
|
| Enzyme 8 Gene Name |
PIGP |
| Enzyme 8 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit P
MVPRSTSLTLIVFLFHRLSKAPGKMVENSPSPLPERAIYGFVLFLSSQFGFILYLVWAFI
PESWLNSLGLTYWPQKYWAVALPVYLLIAIVIGYVLLFGINMMSTSPLDSIHTITDNYAK
NQQQKKYQEEAIPALRDISISEVNQMFFLAAKELYTKN
|
| Enzyme 8 Number of Residues |
158 |
| Enzyme 8 Molecular Weight |
18089 |
| Enzyme 8 Theoretical pI |
9.20 |
| Enzyme 8 GO Classification |
Not Available |
| Enzyme 8 General Function |
Not Available |
| Enzyme 8 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 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
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
8698815  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
P57054  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PIGP_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>405 bp
ATGGTGGAAAATTCACCGTCGCCATTGCCAGAAAGAGCGATTTATGGCTTTGTTCTTTTC
TTAAGCTCCCAATTTGGCTTCATACTTTACCTCGTGTGGGCCTTTATTCCTGAATCTTGG
CTAAACTCTTTAGGTTTAACCTATTGGCCTCAAAAATATTGGGCAGTTGCATTACCTGTC
TACCTCCTTATTGCTATAGTAATTGGCTACGTGCTCTTGTTTGGGATTAACATGATGAGT
ACCTCTCCACTCGACTCCATCCATACAATCACAGATAACTATGCAAAAAATCAACAGCAG
AAGAAATACCAAGAGGAGGCCATTCCAGCCTTAAGAGATATTTCTATTAGTGAAGTAAAC
CAAATGTTCTTTCTTGCAGCCAAAGAACTTTACACCAAAAACTGA
|
| Enzyme 8 GenBank Gene ID |
AB037162  |
| Enzyme 8 GeneCard ID |
PIGP  |
| Enzyme 8 GenAtlas ID |
PIGP  |
| Enzyme 8 HGNC ID |
HGNC:3046  |
| Enzyme 8 Chromosome Location |
21 |
| Enzyme 8 Locus |
21q22.2 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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
]
- 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
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
6232 |
| Enzyme 9 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit C |
| Enzyme 9 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class C protein
- PIG-C
|
| Enzyme 9 Gene Name |
PIGC |
| Enzyme 9 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit C
MYAQPVTNTKEVKWQKVLYERQPFPDNYVDRRFLEELRKNIHARKYQYWAVVFESSVVIQ
QLCSVCVFVVIWWYMDEGLLAPHWLLGTGLASSLIGYVLFDLIDGGEGRKKSGQTRWADL
KSALVFITFTYGFSPVLKTLTESVSTDTIYAMSVFMLLGHLIFFDYGANAAIVSSTLSLN
MAIFASVCLASRLPRSLHAFIMVTFAIQIFALWPMLQKKLKACTPRSYVGVTLLFAFSAV
GGLLSISAVGAVLFALLLMSISCLCPFYLIRLQLFKENIHGPWDEAEIKEDLSRFLS
|
| Enzyme 9 Number of Residues |
297 |
| Enzyme 9 Molecular Weight |
33583 |
| Enzyme 9 Theoretical pI |
8.55 |
| Enzyme 9 GO Classification |
| Function |
- UDP-glycosyltransferase activity
- acetylglucosaminyltransferase activity
- catalytic activity
- phosphatidylinositol N-acetylglucosaminyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
|
| Process |
- GPI anchor biosynthesis
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid lipidation
- protein modification
|
| Component |
- cell
- integral to membrane
- intrinsic to membrane
- membrane
|
|
| Enzyme 9 General Function |
Not Available |
| 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
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
- 51-71
80-100
154-174
239-259
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
1620890  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q92535  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PIGC_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>894 bp
ATGTATGCTCAACCTGTGACTAACACCAAGGAGGTCAAGTGGCAGAAGGTCTTGTATGAG
CGACAGCCCTTTCCTGATAACTATGTGGACCGGCGATTCCTGGAAGAGCTCCGGAAAAAC
ATCCATGCTCGGAAATACCAATATTGGGCTGTGGTATTTGAGTCCAGTGTGGTGATCCAG
CAGCTGTGCAGTGTTTGTGTTTTTGTGGTTATCTGGTGGTATATGGATGAGGGTCTTCTG
GCCCCCCATTGGCTTTTAGGGACTGGCCTGGCTTCTTCACTGATTGGGTATGTTTTGTTT
GATCTCATTGATGGAGGTGAAGGGCGGAAGAAGAGTGGGCAGACCCGGTGGGCTGACCTG
AAGAGTGCCCTAGTCTTCATTACTTTCACTTATGGGTTTTCACCAGTGCTGAAGACCCTT
ACAGAGTCTGTCAGCACTGACACCATCTATGCCATGTCAGTCTTCATGCTGTTAGGCCAT
CTCATCTTTTTTGACTATGGTGCCAATGCTGCCATTGTATCCAGCACACTATCCTTGAAC
ATGGCCATCTTTGCTTCTGTATGCTTGGCATCACGTCTTCCCCGGTCCCTGCATGCCTTC
ATCATGGTGACATTTGCCATTCAGATTTTTGCCCTGTGGCCCATGTTGCAGAAGAAACTA
AAGGCATGTACTCCCCGGAGCTATGTGGGGGTCACACTGCTTTTTGCATTTTCAGCCGTG
GGAGGCCTACTGTCCATTAGTGCTGTGGGAGCCGTACTCTTTGCCCTTCTGCTGATGTCT
ATCTCATGTCTGTGTCCATTCTACCTCATTCGCTTGCAGCTTTTTAAAGAAAACATTCAT
GGGCCTTGGGATGAAGCTGAAATCAAGGAAGACTTGTCCAGGTTCCTCAGTTAA
|
| Enzyme 9 GenBank Gene ID |
D85418  |
| Enzyme 9 GeneCard ID |
PIGC  |
| Enzyme 9 GenAtlas ID |
PIGC  |
| Enzyme 9 HGNC ID |
HGNC:8960  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1q23-q25 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 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
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
6371 |
| Enzyme 10 Name |
Sphingosine kinase 1 |
| Enzyme 10 Synonyms |
- SK 1
- SPK 1
|
| Enzyme 10 Gene Name |
SPHK1 |
| Enzyme 10 Protein Sequence |
>Sphingosine kinase 1
MDPAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAEISFTLMLTERRNHA
RELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLCSLPAGSGNALAASL
NHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSVLSLAWGFIADVDLE
SEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASPVVVQQGPVDAHLVP
LEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMHLFYVRAGVSRAMLL
RLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMVSEAVQGQVHPNYFW
MVSGCVEPPPSWKPQQMPPPEEPL
|
| Enzyme 10 Number of Residues |
384 |
| Enzyme 10 Molecular Weight |
42518 |
| Enzyme 10 Theoretical pI |
7.13 |
| Enzyme 10 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- protein kinase C activation
- signal transduction
|
| Component |
| — |
|
| Enzyme 10 General Function |
Lipid transport and metabolism |
| Enzyme 10 Specific Function |
Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-sphingosine and to a lesser extent sphinganine, but not other lipids, such as D,L-threo-dihydrosphingosine, N,N-dimethylsphingosine, diacylglycerol, ceramide, or phosphatidylinositol |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
8133100  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q9NYA1  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
SPHK1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1155 bp
ATGGATCCAGCGGGCGGCCCCCGGGGCGTGCTCCCGCGGCCCTGCCGCGTGCTGGTGCTG
CTGAACCCGCGCGGCGGCAAGGGCAAGGCCTTGCAGCTCTTCCGGAGTCACGTGCAGCCC
CTTTTGGCTGAGGCTGAAATCTCCTTCACGCTGATGCTCACTGAGCGGCGGAACCACGCG
CGGGAGCTGGTGCGGTCGGAGGAGCTGGGCCGCTGGGACGCTCTGGTGGTCATGTCTGGA
GACGGGCTGATGCACGAGGTGGTGAACGGGCTCATGGAGCGGCCTGACTGGGAGACCGCC
ATCCAGAAGCCCCTGTGTAGCCTCCCAGCAGGCTCTGGCAACGCGCTGGCAGCTTCCTTG
AACCATTATGCTGGCTATGAGCAGGTCACCAATGAAGACCTCCTGACCAACTGCACGCTA
TTGCTGTGCCGCCGGCTGCTGTCACCCATGAACCTGCTGTCTCTGCACACGGCTTCGGGG
CTGCGCCTCTTCTCTGTGCTCAGCCTGGCCTGGGGCTTCATTGCTGATGTGGACCTAGAG
AGTGAGAAGTATCGGCGTCTGGGGGAGATGCGCTTCACTCTGGGCACCTTCCTGCGTCTG
GCAGCCCTGCGCACCTACCGCGGCCGACTGGCCTACCTCCCTGTAGGAAGAGTGGGTTCC
AAGACACCTGCCTCCCCCGTTGTGGTCCAGCAGGGCCCGGTAGATGCACACCTTGTGCCA
CTGGAGGAGCCAGTGCCCTCTCACTGGACAGTGGTGCCCGACGAGGACTTTGTGCTAGTC
CTGGCACTGCTGCACTCGCACCTGGGCAGTGAGATGTTTGCTGCACCCATGGGCCGCTGT
GCAGCTGGCGTCATGCATCTGTTCTACGTGCGGGCGGGAGTGTCTCGTGCCATGCTGCTG
CGCCTCTTCCTGGCCATGGAGAAGGGCAGGCATATGGAGTATGAATGCCCCTACTTGGTA
TATGTGCCCGTGGTCGCCTTCCGCTTGGAGCCCAAGGATGGGAAAGGTGTGTTTGCAGTG
GATGGGGAATTGATGGTTAGCGAGGCCGTGCAGGGCCAGGTGCACCCAAACTACTTCTGG
ATGGTCAGCGGTTGCGTGGAGCCCCCGCCCAGCTGGAAGCCCCAGCAGATGCCACCGCCA
GAAGAGCCCTTATGA
|
| Enzyme 10 GenBank Gene ID |
AF266756  |
| Enzyme 10 GeneCard ID |
SPHK1  |
| Enzyme 10 GenAtlas ID |
SPHK1  |
| Enzyme 10 HGNC ID |
HGNC:11240  |
| Enzyme 10 Chromosome Location |
17 |
| Enzyme 10 Locus |
17q25.2 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Melendez AJ, Carlos-Dias E, Gosink M, Allen JM, Takacs L: Human sphingosine kinase: molecular cloning, functional characterization and tissue distribution. Gene. 2000 Jun 13;251(1):19-26. [PubMed
]
- Nava VE, Lacana E, Poulton S, Liu H, Sugiura M, Kono K, Milstien S, Kohama T, Spiegel S: Functional characterization of human sphingosine kinase-1. FEBS Lett. 2000 May 4;473(1):81-4. [PubMed
]
- Pitson SM, D'andrea RJ, Vandeleur L, Moretti PA, Xia P, Gamble JR, Vadas MA, Wattenberg BW: Human sphingosine kinase: purification, molecular cloning and characterization of the native and recombinant enzymes. Biochem J. 2000 Sep 1;350 Pt 2:429-41. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
6372 |
| Enzyme 11 Name |
Sphingosine kinase 2 |
| Enzyme 11 Synonyms |
- SK 2
- SPK 2
|
| Enzyme 11 Gene Name |
SPHK2 |
| Enzyme 11 Protein Sequence |
>Sphingosine kinase 2
MNGHLEAEEQQDQRPDQELTGSWGHGPRSTLVRAKAMAPPPPPLAASTPLLHGEFGSYPA
RGPRFALTLTSQALHIQRLRPKPEARPRGGLVPLAEVSGCCTLRSRSPSDSAAYFCIYTY
PRGRRGARRRATRTFRADGAATYEENRAEAQRWATALTCLLRGLPLPGDGEITPDLLPRP
PRLLLLVNPFGGRGLAWQWCKNHVLPMISEAGLSFNLIQTERQNHARELVQGLSLSEWDG
IVTVSGDGLLHEVLNGLLDRPDWEEAVKMPVGILPCGSGNALAGAVNQHGGFEPALGLDL
LLNCSLLLCRGGGHPLDLLSVTLASGSRCFSFLSVAWGFVSDVDIQSERFRALGSARFTL
GTVLGLATLHTYRGRLSYLPATVEPASPTPAHSLPRAKSELTLTPDPAPPMAHSPLHRSV
SDLPLPLPQPALASPGSPEPLPILSLNGGGPELAGDWGGAGDAPLSPDPLLSSPPGSPKA
ALHSPVSEGAPVIPPSSGLPLPTPDARVGASTCGPPDHLLPPLGTPLPPDWVTLEGDFVL
MLAISPSHLGADLVAAPHARFDDGLVHLCWVRSGISRAALLRLFLAMERGSHFSLGCPQL
GYAAARAFRLEPLTPRGVLTVDGEQVEYGPLQAQMHPGIGTLLTGPPGCPGREP
|
| Enzyme 11 Number of Residues |
654 |
| Enzyme 11 Molecular Weight |
69218 |
| Enzyme 11 Theoretical pI |
6.94 |
| Enzyme 11 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- protein kinase C activation
- signal transduction
|
| Component |
| — |
|
| Enzyme 11 General Function |
Lipid transport and metabolism |
| Enzyme 11 Specific Function |
Catalyzes the phosphorylation of sphingosine to form sphingosine 1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro- dihydrosphingosine, D-erythro-sphingosine and L-threo- dihydrosphingosine |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
8248285  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9NRA0  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
SPHK2_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>1857 bp
ATGGCCCCGCCCCCACCGCCACTGGCTGCCAGCACCCCGCTCCTCCATGGCGAGTTTGGC
TCCTACCCAGCCCGAGGCCCACGCTTTGCCCTCACCCTTACATCGCAGGCCCTGCACATA
CAGCGGCTGCGCCCCAAACCTGAAGCCAGGCCCCGGGGTGGCCTGGTCCCGTTGGCCGAG
GTCTCAGGCTGCTGCACCCTGCGAAGCCGCAGCCCCTCAGACTCAGCGGCCTACTTCTGC
ATCTACACCTACCCTCGGGGCCGGCGCGGGGCCCGGCGCAGAGCCACTCGCACCTTCCGG
GCAGATGGGGCCGCCACCTACGAAGAGAACCGTGCCGAGGCCCAGCGCTGGGCCACTGCC
CTCACCTGTCTGCTCCGAGGACTGCCACTGCCCGGGGATGGGGAGATCACCCCTGACCTG
CTACCTCGGCCGCCCCGGTTGCTTCTATTGGTCAATCCCTTTGGGGGTCGGGGCCTGGCC
TGGCAGTGGTGTAAGAACCACGTGCTTCCCATGATCTCTGAAGCTGGGCTGTCCTTCAAC
CTCATCCAGACAGAACGACAGAACCACGCCCGGGAGCTGGTCCAGGGGCTGAGCCTGAGT
GAGTGGGATGGCATCGTCACGGTCTCGGGAGACGGGCTGCTCCATGAGGTGCTGAACGGG
CTCCTAGATCGCCCTGACTGGGAGGAAGCTGTGAAGATGCCTGTGGGCATCCTCCCCTGC
GGCTCGGGCAACGCGCTGGCCGGAGCAGTGAACCAGCACGGGGGATTTGAGCCAGCCCTG
GGCCTCGACCTGTTGCTCAACTGCTCACTGTTGCTGTGCCGGGGTGGTGGCCACCCACTG
GACCTGCTCTCCGTGACGCTGGCCTCGGGCTCCCGCTGTTTCTCCTTCCTGTCTGTGGCC
TGGGGCTTCGTGTCAGATGTGGATATCCAGAGCGAGCGCTTCAGGGCCTTGGGCAGTGCC
CGCTTCACACTGGGCACGGTGCTGGGCCTCGCCACACTGCACACCTACCGCGGACGCCTC
TCCTACCTCCCCGCCACTGTGGAACCTGCCTCGCCCACCCCTGCCCATAGCCTGCCTCGT
GCCAAGTCGGAGCTGACCCTAACCCCAGACCCAGCCCCGCCCATGGCCCACTCACCCCTG
CATCGTTCTGTGTCTGACCTGCCTCTTCCCCTGCCCCAGCCTGCCCTGGCCTCTCCTGGC
TCGCCAGAACCCCTGCCCATCCTGTCCCTCAACGGTGGGGGCCCAGAGCTGGCTGGGGAC
TGGGGTGGGGCTGGGGATGCTCCGCTGTCCCCGGACCCACTGCTGTCTTCACCTCCTGGC
TCTCCCAAGGCAGCTCTACACTCACCCGTCTCCGAAGGGGCCCCCGTAATTCCCCCATCC
TCTGGGCTCCCACTTCCCACCCCTGATGCCCGGGTAGGGGCCTCCACCTGCGGCCCGCCC
GACCACCTGCTGCCTCCGCTGGGCACCCCGCTGCCCCCAGACTGGGTGACGCTGGAGGGG
GACTTTGTGCTCATGTTGGCCATCTCGCCCAGCCACCTAGGCGCTGACCTGGTGGCAGCT
CCGCATGCGCGCTTCGACGACGGCCTGGTGCACCTGTGCTGGGTGCGTAGCGGCATCTCG
CGGGCTGCGCTGCTGCGCCTTTTCTTGGCCATGGAGCGTGGTAGCCACTTCAGCCTGGGC
TGTCCGCAGCTGGGCTACGCCGCGGCCCGTGCCTTCCGCCTAGAGCCGCTCACACCACGC
GGCGTGCTCACAGTGGACGGGGAGCAGGTGGAGTATGGGCCGCTACAGGCACAGATGCAC
CCTGGCATCGGTACACTGCTCACTGGGCCTCCTGGCTGCCCGGGGCGGGAGCCCTGA
|
| Enzyme 11 GenBank Gene ID |
AF245447  |
| Enzyme 11 GeneCard ID |
SPHK2  |
| Enzyme 11 GenAtlas ID |
SPHK2  |
| Enzyme 11 HGNC ID |
HGNC:18859  |
| Enzyme 11 Chromosome Location |
19 |
| Enzyme 11 Locus |
19q13.2 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Liu H, Sugiura M, Nava VE, Edsall LC, Kono K, Poulton S, Milstien S, Kohama T, Spiegel S: Molecular cloning and functional characterization of a novel mammalian sphingosine kinase type 2 isoform. J Biol Chem. 2000 Jun 30;275(26):19513-20. [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
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
7061 |
| Enzyme 12 Name |
Ganglioside GM2 activator precursor |
| Enzyme 12 Synonyms |
- GM2-AP
- Cerebroside sulfate activator protein
- Shingolipid activator protein 3
- SAP-3[Contains: Ganglioside GM2 activator isoform short]
|
| Enzyme 12 Gene Name |
GM2A |
| Enzyme 12 Protein Sequence |
>Ganglioside GM2 activator precursor
MQSLMQAPLLIALGLLLATPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIVV
PGNVTLSVVGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIP
TGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKR
LGCIKIAASLKGI
|
| Enzyme 12 Number of Residues |
193 |
| Enzyme 12 Molecular Weight |
20822 |
| Enzyme 12 Theoretical pI |
4.96 |
| Enzyme 12 GO Classification |
Not Available |
| Enzyme 12 General Function |
Not Available |
| Enzyme 12 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 12 Pathways |
Not Available |
| Enzyme 12 Reactions |
Not Available |
| Enzyme 12 Pfam Domain Function |
Not Available |
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
Not Available |
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
183357  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P17900  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
SAP3_HUMAN  |
| Enzyme 12 PDB ID |
1PU5  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>582 bp
ATGCAGTCCCTGATGCAGGCTCCCCTCCTGATCGCCCTGGGCTTGCTTCTCGCGGCCCCT
GCGCAAGCCCACCTGAAAAAGCCATCCCAGCTCAGTAGCTTTTCCTGGGATAACTGTGAT
GAAGGGAAGGACCCTGCGGTGATCAGAAGCCTGACTCTGGAGCCTGACCCCATCGTCGTT
CCTGGAAATGTGACCCTCAGTGTCGTGGGCAGCACCAGTGTCCCCCTGAGTTCTCCTCTG
AAGGTGGATTTAGTTTTGGAGAAGGAGGTGGCTGGCCTCTGGATCAAGATCCCATGCACA
GACTACATTGGCAGCTGTACCTTTGAACACTTCTGTGATGTGCTTGACATGTTAATTCCT
ACTGGGGAGCCCTGCCCAGAGCCCCTGCGTACCTATGGGCTTCCTTGCCACTGTCCCTTC
AAAGAAGGAACCTACTCACTGCCCAAGAGCGAATTCGTTGTGCCTGACCTGGAGCTGCCC
AGTTGGCTCACCACCGGGAACTACCGCATAGAGAGCGTCCTGAGCAGCAGTGGGAAGCGT
CTGGGCTGCATCAAGATCGCTGCCTCTCTAAAGGGCATATAA
|
| Enzyme 12 GenBank Gene ID |
M76477  |
| Enzyme 12 GeneCard ID |
GM2A  |
| Enzyme 12 GenAtlas ID |
GM2A  |
| Enzyme 12 HGNC ID |
HGNC:4367  |
| Enzyme 12 Chromosome Location |
5 |
| Enzyme 12 Locus |
5q31.3-q33.1 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 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
]
- 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 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
7905 |
| Enzyme 13 Name |
T-cell surface glycoprotein CD1e precursor |
| Enzyme 13 Synonyms |
- CD1e antigen
- R2G1
|
| Enzyme 13 Gene Name |
CD1E |
| Enzyme 13 Protein Sequence |
>T-cell surface glycoprotein CD1e precursor
MLLLFLLFEGLCCPGENTAAAEEQLSFRMLQTSSFANHSWAHSEGSGWLGDLQTHGWDTV
LGTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEYPFEIQILAGCR
MNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKEILQSLLGHTC
PRFLAGLMEAGESELKRKVKPEAWLSCGPSPGPGRLQLVCHVSGFYPKPVWVMWMRGEQE
QRGTQRGDVLPNADETWYLRATLDVAAGEAAGLSCRVKHSSLGGHDLIIHWGGYSIFLIL
ICLTVIVTLVILVVVDSRLKKQ
|
| Enzyme 13 Number of Residues |
322 |
| Enzyme 13 Molecular Weight |
35986 |
| Enzyme 13 Theoretical pI |
7.25 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Not Available |
| Enzyme 13 Specific Function |
Not Available |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
296640  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
P15812  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
CD1E_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>972 bp
ATGCTGCTCCTGTTCCTCCTCTTCGAGGGTCTCTGCTGTCCTGGGGAAAATACAGCAGCA
GCAGAGGAGCAGCTGTCCTTCCGCATGCTCCAAACTTCCTCCTTTGCCAACCACAGCTGG
GCACACAGTGAGGGCTCAGGATGGCTGGGTGACCTGCAGACTCATGGCTGGGACACTGTC
TTGGGCACCATCCGCTTTCTGAAGCCCTGGTCCCATGGAAACTTCAGCAAGCAGGAGCTG
AAAAACTTACAGTCACTGTTCCAGTTATACTTCCATAGTTTTATCCAGATAGTGCAAGCT
TCTGCTGGTCAATTTCAGCTTGAATACCCCTTCGAGATCCAGATATTAGCTGGCTGTAGA
ATGAATGCCCCACAAATCTTCTTAAATATGGCATATCAAGGGTCAGATTTCCTGAGTTTC
CAAGGAATTTCCTGGGAGCCATCTCCAGGAGCAGGGATCCGGGCCCAGAACATCTGTAAA
GTGCTCAATCGCTACCTAGATATTAAGGAAATACTGCAAAGCCTTCTTGGTCACACCTGC
CCTCGATTTCTAGCGGGGCTCATGGAAGCAGGGGAGTCAGAACTGAAACGGAAAGTGAAG
CCAGAGGCCTGGCTGTCCTGTGGCCCCAGTCCTGGCCCTGGCCGTCTGCAGCTTGTGTGC
CATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGGGGTGAGCAGGAG
CAGCGGGGCACTCAGCGAGGGGACGTCCTGCCTAATGCTGACGAGACATGGTATCTCCGA
GCAACCCTGGATGTGGCGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGGGTGAAACACAGC
AGTCTAGGGGGCCATGATCTAATCATCCATTGGGGTGGATATTCCATCTTTCTCATCCTG
ATCTGTTTGACTGTGATAGTTACCCTGGTCATATTGGTTGTAGTTGACTCACGGTTAAAA
AAACAGAGGTGA
|
| Enzyme 13 GenBank Gene ID |
X14975  |
| Enzyme 13 GeneCard ID |
CD1E  |
| Enzyme 13 GenAtlas ID |
CD1E  |
| Enzyme 13 HGNC ID |
HGNC:1638  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
1q22-q23 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 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
]
- 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
]
- 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
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
8178 |
| Enzyme 14 Name |
Epididymal secretory protein E1 precursor |
| Enzyme 14 Synonyms |
- Niemann-Pick disease type C2 protein
- hE1
|
| Enzyme 14 Gene Name |
NPC2 |
| Enzyme 14 Protein Sequence |
>Epididymal secretory protein E1 precursor
MRFLAATFLLLALSTAAQAEPVQFKDCGSVDGVIKEVNVSPCPTQPCQLSKGQSYSVNVT
FTSNIQSKSSKAVVHGILMGVPVPFPIPEPDGCKSGINCPIQKDKTYSYLNKLPVKSEYP
SIKLVVEWQLQDDKNQSLFCWEIPVQIVSHL
|
| Enzyme 14 Number of Residues |
151 |
| Enzyme 14 Molecular Weight |
16570 |
| Enzyme 14 Theoretical pI |
7.77 |
| Enzyme 14 GO Classification |
Not Available |
| Enzyme 14 General Function |
Not Available |
| Enzyme 14 Specific Function |
May be involved in the regulation of the lipid composition of sperm membranes during the maturation in the epididymis |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
Not Available |
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
37477  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P61916  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
NPC2_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>456 bp
ATGCGTTTCCTGGCAGCTACATTCCTGCTCCTGGCGCTCAGCACCGCTGCCCAGGCCGAA
CCGGTGCAGTTCAAGGACTGCGGTTCTGTGGATGGAGTTATAAAGGAAGTGAATGTGAGC
CCATGCCCCACCCAACCCTGCCAGCTGAGCAAAGGACAGTCTTACAGCGTCAATGTCACC
TTCACCAGCAATATTCAGTCTAAAAGCAGCAAGGCCGTGGTGCATGGCATCCTGATGGGC
GTCCCAGTTCCCTTTCCCATTCCTGAGCCTGATGGTTGTAAGAGTGGAATTAACTGCCCT
ATCCAAAAAGACAAGACCTATAGCTACCTGAATAAACTACCAGTGAAAAGCGAATATCCC
TCTATAAAACTGGTGGTGGAGTGGCAACTTCAGGATGACAAAAACCAAAGTCTCTTCTGC
TGGGAAATCCCAGTACAGATCGTTTCTCATCTCTAA
|
| Enzyme 14 GenBank Gene ID |
X67698  |
| Enzyme 14 GeneCard ID |
NPC2  |
| Enzyme 14 GenAtlas ID |
NPC2  |
| Enzyme 14 HGNC ID |
HGNC:14537  |
| Enzyme 14 Chromosome Location |
14 |
| Enzyme 14 Locus |
14q24.3 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 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
]
- 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
]
- 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
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
8289 |
| Enzyme 15 Name |
T-cell surface glycoprotein CD1d precursor |
| Enzyme 15 Synonyms |
- CD1d antigen
- R3G1
|
| Enzyme 15 Gene Name |
CD1D |
| Enzyme 15 Protein Sequence |
>T-cell surface glycoprotein CD1d precursor
MGCLLFLLLWALLQAWGSAEVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSN
DSDTVRSLKPWSQGTFSDQQWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGC
EVHPGNASNNFFHVAFQGKDILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLL
NGTCPQFVSGLLESGKSELKKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMR
GEQEQQGTQPGDILPNADETWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGGSYT
SMGLIALAVLACLLFLLIVGFTSRFKRQTSYQGVL
|
| Enzyme 15 Number of Residues |
335 |
| Enzyme 15 Molecular Weight |
37718 |
| Enzyme 15 Theoretical pI |
8.28 |
| Enzyme 15 GO Classification |
Not Available |
| Enzyme 15 General Function |
Not Available |
| Enzyme 15 Specific Function |
Not known |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
Not Available |
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
619798  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P15813  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
CD1D_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1008 bp
ATGGGGTGCCTGCTGTTTCTGCTGCTCTGGGCGCTCCTCCAGGCTTGGGGAAGCGCTGAA
GTCCCGCAAAGGCTTTTCCCCCTCCGCTGCCTCCAGATCTCGTCCTTCGCCAATAGCAGC
TGGACGCGCACCGACGGCTTGGCGTGGCTGGGGGAGCTGCAGACGCACAGCTGGAGCAAC
GACTCGGACACCGTCCGCTCTCTGAAGCCTTGGTCCCAGGGCACGTTCAGCGACCAGCAG
TGGGAGACGCTGCAGCATATATTTCGGGTTTATCGAAGCAGCTTCACCAGGGACGTGAAG
GAATTCGCCAAAATGCTACGCTTATCCTATCCCTTGGAGCTCCAGGTGTCCGCTGGCTGT
GAGGTGCACCCTGGGAACGCCTCAAATAACTTCTTCCATGTAGCATTTCAAGGAAAAGAT
ATCCTGAGTTTCCAAGGAACTTCTTGGGAGCCAACCCAAGAGGCCCCACTTTGGGTAAAC
TTGGCCATTCAAGTGCTCAACCAGGACAAGTGGACGAGGGAAACAGTGCAGTGGCTCCTT
AATGGCACCTGCCCCCAATTTGTCAGTGGCCTCCTTGAGTCAGGGAAGTCGGAACTGAAG
AAGCAAGTGAAGCCCAAGGCCTGGCTGTCCCGTGGCCCCAGTCCTGGCCCTGGCCGTCTG
CTGCTGGTGTGCCATGTCTCAGGATTCTACCCAAAGCCTGTATGGGTGAAGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCCAGGGGACATCCTGCCCAATGCTGACGAGACA
TGGTATCTCCGAGCAACCCTGGATGTGGTGGCTGGGGAGGCAGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTCTAGAGGGCCAGGACATCGTCCTCTACTGGGGTGGGAGCTACACC
TCCATGGGCTTGATTGCCTTGGCAGTCCTGGCGTGCTTGCTGTTCCTCCTCATTGTGGGC
TTTACCTCCCGGTTTAAGAGGCAAACTTCCTATCAGGGCGTCCTGTGA
|
| Enzyme 15 GenBank Gene ID |
L38820  |
| Enzyme 15 GeneCard ID |
CD1D  |
| Enzyme 15 GenAtlas ID |
CD1D  |
| Enzyme 15 HGNC ID |
HGNC:1637  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
1q22-q23 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 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
]
- 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
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
8469 |
| Enzyme 16 Name |
GPI mannosyltransferase 1 |
| Enzyme 16 Synonyms |
- GPI mannosyltransferase I
- GPI-MT-I
- Phosphatidylinositol-glycan biosynthesis class M protein
- PIG-M
|
| Enzyme 16 Gene Name |
PIGM |
| Enzyme 16 Protein Sequence |
>GPI mannosyltransferase 1
MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAAR
FVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLG
RRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMK
IYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFA
LSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLI
LLSAVSFAYYRDLVFCCFLHTSIFVTFNKVCTSQYFLWYLCLLPLVMPLVRMPWKRAVVL
LMLWFIGQAMWLAPAYVLEFQGKNTFLFIWLAGLFFLLINCSILIQIISHYKEEPLTERI
KYD
|
| Enzyme 16 Number of Residues |
423 |
| Enzyme 16 Molecular Weight |
49460 |
| Enzyme 16 Theoretical pI |
9.31 |
| Enzyme 16 GO Classification |
Not Available |
| Enzyme 16 General Function |
Not Available |
| Enzyme 16 Specific Function |
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
Not Available |
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
- 18-38
80-100
139-161
170-190
226-246
288-308
315-337
339-350
358-378
385-405
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
11414879  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
Q9H3S5  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
PIGM_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 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 16 GenBank Gene ID |
AB028127  |
| Enzyme 16 GeneCard ID |
PIGM  |
| Enzyme 16 GenAtlas ID |
PIGM  |
| Enzyme 16 HGNC ID |
HGNC:18858  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
1q23.2 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 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
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
8495 |
| Enzyme 17 Name |
Phosphatidylinositol-glycan biosynthesis class W protein |
| Enzyme 17 Synonyms |
- PIG-W
|
| Enzyme 17 Gene Name |
PIGW |
| Enzyme 17 Protein Sequence |
>Phosphatidylinositol-glycan biosynthesis class W protein
MSEKQMKEAFVSNLNGTTVLEITQGLCFPAFCILCRGFLIIFSQYLCSFSPTWKTRFLTD
FVVLIVPMVATLTIWASFILLELLGVIIFGAGLLYQIYRRRTCYARLPFLKILEKFLNIS
LESEYNPAISCFRVITSAFTAIAILAVDFPLFPRRFAKTELYGTGAMDFGVGGFVFGSAM
VCLEVRRRKYMEGSKLHYFTNSLYSVWPLVFLGIGRLAIIKSIGYQEHLTEYGVHWNFFF
TIIVVKLITPLLLIIFPLNKSWIIALGITVLYQLALDFTSLKRLILYGTDGSGTRVGLLN
ANREGIISTLGYVAIHMAGVQTGLYMHKNRSHIKDLIKVACFLLLAAISLFISLYVVQVN
VEAVSRRMANLAFCIWIVASSLILLSSLLLGDIILSFAKFLIKGALVPCSWKLIQSPVTN
KKHSESLVPEAERMEPSLCLITALNRKQLIFFLLSNITTGLINLMVDTLHSSTLWALFVV
NLYMFSNCLIVYVLYLQDKTVQFW
|
| Enzyme 17 Number of Residues |
504 |
| Enzyme 17 Molecular Weight |
56883 |
| Enzyme 17 Theoretical pI |
9.44 |
| Enzyme 17 GO Classification |
| Function |
- acetyltransferase activity
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring groups other than amino-acyl groups
|
| Process |
- GPI anchor biosynthesis
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid lipidation
- protein modification
|
| Component |
- cell
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- organelle membrane
|
|
| Enzyme 17 General Function |
Not Available |
| Enzyme 17 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 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 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 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
Not Available |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q7Z7B1  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
PIGW_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
Not Available |
| Enzyme 17 GenBank Gene ID |
AB097818  |
| Enzyme 17 GeneCard ID |
PIGW  |
| Enzyme 17 GenAtlas ID |
PIGW  |
| Enzyme 17 HGNC ID |
HGNC:23213  |
| Enzyme 17 Chromosome Location |
17 |
| Enzyme 17 Locus |
17q12 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
Not Available |
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
8588 |
| Enzyme 18 Name |
3-ketodihydrosphingosine reductase precursor |
| Enzyme 18 Synonyms |
- 3- dehydrosphinganine reductase
- KDS reductase
- Follicular variant translocation protein 1
- FVT-1
|
| Enzyme 18 Gene Name |
FVT1 |
| Enzyme 18 Protein Sequence |
>3-ketodihydrosphingosine reductase precursor
MLLLAAAFLVAFVLLLYMVSPLISPKPLALPGAHVVVTGGSSGIGKCIAIECYKQGAFIT
LVARNEDKLLQAKKEIEMHSINDKQVVLCISVDVSQDYNQVENVIKQAQEKLGPVDMLVN
CAGMAVSGKFEDLEVSTFERLMSINYLGSVYPSRAVITTMKERRVGRIVFVSSQAGQLGL
FGFTAYSASKFAIRGLAEALQMEVKPYNVYITVAYPPDTDTPGFAEENRTKPLETRLISE
TTSVCKPEQVAKQIVKDAIQGNFNSSLGSDGYMLSALTCGMAPVTSITEGLQQVVTMGLF
RTIALFYLGSFDSIVRRCMMQREKSENADKTA
|
| Enzyme 18 Number of Residues |
332 |
| Enzyme 18 Molecular Weight |
36188 |
| Enzyme 18 Theoretical pI |
7.18 |
| Enzyme 18 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Lipid transport and metabolism |
| Enzyme 18 Specific Function |
Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS) |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- sphinganine + NADP+ = 3-dehydrosphinganine + NADPH + H+
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
296186  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q06136  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
FVT1_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>999 bp
ATGCTGCTGCTGGCTGCCGCCTTCCTCGTGGCCTTCGTGCTGCTGCTGTACATGGTGTCT
CCGCTCATCAGCCCCAAGCCCCTCGCCCTGCCCGGGGCGCATGTGGTGGTTACAGGAGGT
TCCAGTGGCATCGGGAAGTGCATTGCTATCGAGTGCTATAAACAAGGAGCTTTTATAACT
CTGGTTGCACGAAATGAGGATAAGCTGCTGCAGGCAAAGAAAGAAATTGAAATGCACTCT
ATTAATGACAAACAGGTGGTGCTTTGCATATCAGTTGATGTATCTCAAGACTATAACCAA
GTAGAGAATGTCATAAAACAAGCACAGGAGAAACTGGGTCCAGTGGACATGCTGGTAAAT
TGTGCAGGAATGGCAGTGTCAGGAAAATTTGAAGATCTTGAAGTTAGTACCTTTGAAAGG
TTAATGAGCATCAATTACCTGGGCAGCGTGTACCCCAGCCGGGCCGTGATCACCACCATG
AAGGAGCGCCGGGTGGGCAGGATCGTGTTTGTGTCCTCCCAGGCAGGACAGTTGGGATTA
TTCGGTTTCACAGCCTACTCTGCATCCAAGTTTGCCATAAGGGGATTGGCAGAAGCTTTG
CAGATGGAGGTGAAGCCATATAATGTCTACATCACAGTTGCTTACCCACCAGACACAGAC
ACACCTGGCTTTGCCGAAGAAAACAGAACAAAGCCTTTGGAGACTCGACTTATTTCAGAG
ACCACATCTGTGTGCAAACCAGAACAGGTGGCCAAACAAATTGTTAAAGATGCCATACAA
GGAAATTTCAACAGTTCCCTTGGCTCAGATGGGTACATGCTCTCGGCCCTGACCTGTGGG
ATGGCTCCAGTAACTTCTATTACTGAGGGGCTCCAGCAGGTGGTCACCATGGGCCTTTTC
CGCACTATTGCTTTGTTTTACCTTGGAAGTTTTGACAGCATAGTTCGTCGCTGCATGATG
CAGAGAGAAAAATCTGAAAATGCAGACAAAACTGCCTAA
|
| Enzyme 18 GenBank Gene ID |
X63657  |
| Enzyme 18 GeneCard ID |
FVT1  |
| Enzyme 18 GenAtlas ID |
FVT1  |
| Enzyme 18 HGNC ID |
HGNC:4021  |
| Enzyme 18 Chromosome Location |
18 |
| Enzyme 18 Locus |
18q21.3 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Rimokh R, Gadoux M, Bertheas MF, Berger F, Garoscio M, Deleage G, Germain D, Magaud JP: FVT-1, a novel human transcription unit affected by variant translocation t(2;18)(p11;q21) of follicular lymphoma. Blood. 1993 Jan 1;81(1):136-42. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
8621 |
| Enzyme 19 Name |
Phosphatidylinositol-glycan biosynthesis class X protein precursor |
| Enzyme 19 Synonyms |
- PIG-X
|
| Enzyme 19 Gene Name |
PIGX |
| Enzyme 19 Protein Sequence |
>Phosphatidylinositol-glycan biosynthesis class X protein precursor
MAARVAAVRAAAWLLLGAATGLTRGPATAFTAARSDAGIRAMCSEIILRQEVLKDGFHRD
LLIKVKFGESIEDLHTCRLLIKQDIPAGLYVDPYELASLRERNITEAVMVSENFDIEAPN
YLSKESEVLIYARRDSQCIDCFQAFLPVHCRYHRPHSEDGEASIVVNNPDLLMFCDQEFP
ILKCWAHSEVAAPCALDNEDICQWNKMKYKSVYKNVILQVPVGLTVHTSLVCSVTLLITI
LCSTLILVAVFKYGHFSL
|
| Enzyme 19 Number of Residues |
258 |
| Enzyme 19 Molecular Weight |
28805 |
| Enzyme 19 Theoretical pI |
6.30 |
| Enzyme 19 GO Classification |
Not Available |
| Enzyme 19 General Function |
Not Available |
| Enzyme 19 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 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
Not Available |
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
18490317  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q8TBF5  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
PIGX_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>654 bp
ATGTGTTCTGAAATTATTTTGAGGCAAGAAGTTTTGAAAGATGGTTTCCACAGAGACCTT
TTAATCAAAGTGAAGTTTGGGGAAAGCATTGAGGACTTGCACACGTGCCGTCTCTTAATT
AAACAGGACATTCCTGCAGGACTTTATGTGGATCCGTATGAGTTGGCTTCATTACGAGAG
AGAAACATAACAGAGGCAGTGATGGTTTCAGAAAATTTTGATATAGAGGCCCCTAACTAT
TTGTCCAAGGAGTCTGAAGTTCTCATTTATGCCAGACGAGATTCACAGTGCATTGACTGT
TTTCAAGCCTTTTTGCCTGTGCACTGCCGCTATCATCGGCCGCACAGTGAAGATGGAGAA
GCCTCGATTGTGGTCAATAACCCAGATTTGTTGATGTTTTGTGACCAAGAGTTCCCGATT
TTGAAATGCTGGGCTCACTCAGAAGTGGCAGCCCCTTGTGCTTTGGATAATGAGGATATA
TGCCAATGGAACAAGATGAAGTATAAATCAGTATATAAGAATGTGATTCTACAAGTTCCA
GTGGGACTGACTGTACATACCTCTCTAGTATGTTCTGTGACTCTGCTCATTACAATCCTG
TGCTCTACATTGATCCTTGTAGCAGTTTTCAAATATGGCCATTTTTCCCTATAA
|
| Enzyme 19 GenBank Gene ID |
BC022542  |
| Enzyme 19 GeneCard ID |
PIGX  |
| Enzyme 19 GenAtlas ID |
PIGX  |
| Enzyme 19 HGNC ID |
HGNC:26046  |
| Enzyme 19 Chromosome Location |
3 |
| Enzyme 19 Locus |
3q29 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
Not Available |
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
8625 |
| Enzyme 20 Name |
GPI mannosyltransferase 4 |
| Enzyme 20 Synonyms |
- GPI mannosyltransferase IV
- GPI-MT-IV
- Phosphatidylinositol-glycan biosynthesis class Z protein
- PIG-Z
- hSMP3
|
| Enzyme 20 Gene Name |
PIGZ |
| Enzyme 20 Protein Sequence |
>GPI mannosyltransferase 4
MAVRVLWGGLSLLRVLWCLLPQTGYVHPDEFFQSPEVMAEDILGVQAARPWEFYPSSSCR
SVLFPLLISGSTFWLLRLWEELGPWPGLVSGYALLVGPRLLLTALSFALDGAVYHLAPPM
GADRWNALALLSGSYVTLVFYTRTFSNTIEGLLFTWLLVLVSSHVTWGPTRKEPAPGPRW
RSWLLGGIVAAGFFNRPTFLAFAVVPLYLWGTRGATNPGLKSLTREALVLLPGATLTAAV
FVATDSWYFSSPATSRNLVLTPVNFLHYNLNPQNLARHGTHARLTHLAVNGFLLFGVLHA
QALQAAWQQLQVGLQASAQMGLLRALGARSLLSSPRSYLLLLYFMPLALLSAFSHQEARF
LIPLLVPLVLLCSPQTQPVPWKGTVVLFNALGALLFGCLHQGGLVPGLEYLEQVVHAPVL
PSTPTHYTLLFTHTYMPPRHLLHLPGLGAPVEVVDIGGTEDWALCQTLKSFTRQPACQVA
GGPWLCRLFVVTPGTTRRAVEKCSFPFKNETLLFPHLTLEDPPALSSLLSGAWRDHLSLH
IVELGEET
|
| Enzyme 20 Number of Residues |
548 |
| Enzyme 20 Molecular Weight |
60249 |
| Enzyme 20 Theoretical pI |
8.40 |
| Enzyme 20 GO Classification |
Not Available |
| Enzyme 20 General Function |
Not Available |
| Enzyme 20 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 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
- 100-120
125-142
149-169
185-205
227-247
338-358
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
Not Available |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q86VD9  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PIGZ_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
Not Available |
| Enzyme 20 GenBank Gene ID |
AK022830  |
| Enzyme 20 GeneCard ID |
PIGZ  |
| Enzyme 20 GenAtlas ID |
PIGZ  |
| Enzyme 20 HGNC ID |
HGNC:30596  |
| Enzyme 20 Chromosome Location |
3 |
| Enzyme 20 Locus |
3q29 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
Not Available |
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
11996 |
| Enzyme 21 Name |
UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5 |
| Enzyme 21 Synonyms |
- Beta3Gn-T5
- BGnT-5
- Beta-1,3-N- acetylglucosaminyltransferase-5
- Lactotriaosylceramide synthase
- Lc(3Cer synthase
- Lc3 synthase
|
| Enzyme 21 Gene Name |
B3GNT5 |
| Enzyme 21 Protein Sequence |
>UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 5
MRMLVSGRRVKKWQLIIQLFATCFLASLMFFWEPIDNHIVSHMKSYSYRYLINSYDFVND
TLSLKHTSAGPRYQYLINHKEKCQAQDVLLLLFVKTAPENYDRRSGIRRTWGNENYVRSQ
LNANIKTLFALGTPNPLEGEELQRKLAWEDQRYNDIIQQDFVDSFYNLTLKLLMQFSWAN
TYCPHAKFLMTADDDIFIHMPNLIEYLQSLEQIGVQDFWIGRVHRGAPPIRDKSSKYYVS
YEMYQWPAYPDYTAGAAYVISGDVAAKVYEASQTLNSSLYIDDVFMGLCANKIGIVPQDH
VFFSGEGKTPYHPCIYEKMMTSHGHLEDLQDLWKNATDPKVKTISKGFFGQIYCRLMKII
LLCKISYVDTYPCRAAFI
|
| Enzyme 21 Number of Residues |
378 |
| Enzyme 21 Molecular Weight |
44053 |
| Enzyme 21 Theoretical pI |
Not Available |
| Enzyme 21 GO Classification |
| Function |
- catalytic activity
- galactosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid glycosylation
- protein modification
|
| Component |
|
|
| Enzyme 21 General Function |
Not Available |
| Enzyme 21 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 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
- galactosyl glucosyl ceramide + UDP-N-acetyl-D-glucosamine --> (Gal)1 (Glc)1 (GlcNAc)1 (Cer)1 + H+ + UDP
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
13568434  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9BYG0  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
B3GN5_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
Not Available |
| Enzyme 21 GenBank Gene ID |
AB045278  |
| Enzyme 21 GeneCard ID |
Not Available |
| Enzyme 21 GenAtlas ID |
B3GNT5  |
| Enzyme 21 HGNC ID |
HGNC:15684  |
| Enzyme 21 Chromosome Location |
Not Available |
| Enzyme 21 Locus |
Not Available |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 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
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
12558 |
| Enzyme 22 Name |
Beta-1,3-galactosyltransferase 5 |
| Enzyme 22 Synonyms |
- Beta-1,3-GalTase 5
- Beta3Gal-T5
- b3Gal-T5
- UDP-galactose:beta-N-acetylglucosamine beta- 1,3-galactosyltransferase 5
- UDP-Gal:beta-GlcNAc beta-1,3- galactosyltransferase 5
- Beta-3-Gx-T5
|
| Enzyme 22 Gene Name |
B3GALT5 |
| Enzyme 22 Protein Sequence |
>Beta-1,3-galactosyltransferase 5
MAFPKMRLMYICLLVLGALCLYFSMYSLNPFKEQSFVYKKDGNFLKLPDTDCRQTPPFLV
LLVTSSHKQLAERMAIRQTWGKERMVKGKQLKTFFLLGTTSSAAETKEVDQESQRHGDII
QKDFLDVYYNLTLKTMMGIEWVHRFCPQAAFVMKTDSDMFINVDYLTELLLKKNRTTRFF
TGFLKLNEFPIRQPFSKWFVSKSEYPWDRYPPFCSGTGYVFSGDVASQVYNVSKSVPYIK
LEDVFVGLCLERLNIRLEELHSQPTFFPGGLRFSVCLFRRIVACHFIKPRTLLDYWQALE
NSRGEDCPPV
|
| Enzyme 22 Number of Residues |
310 |
| Enzyme 22 Molecular Weight |
36190 |
| Enzyme 22 Theoretical pI |
Not Available |
| Enzyme 22 GO Classification |
| Function |
- catalytic activity
- galactosyltransferase activity
- transferase activity
- transferase activity, transferring glycosyl groups
- transferase activity, transferring hexosyl groups
|
| Process |
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid glycosylation
- protein modification
|
| Component |
|
|
| Enzyme 22 General Function |
Not Available |
| Enzyme 22 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 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
- globoside (homo sapiens) + UDPgalactose --> galactosylgloboside (homo sapiens) + H+ + UDP
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
4835503  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q9Y2C3  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
B3GT5_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
Not Available |
| Enzyme 22 GenBank Gene ID |
AB020337  |
| Enzyme 22 GeneCard ID |
Not Available |
| Enzyme 22 GenAtlas ID |
B3GALT5  |
| Enzyme 22 HGNC ID |
HGNC:920  |
| Enzyme 22 Chromosome Location |
Not Available |
| Enzyme 22 Locus |
Not Available |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 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
]
- 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
]
- 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 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
12947 |
| Enzyme 23 Name |
GPI mannosyltransferase 3 |
| Enzyme 23 Synonyms |
- GPI mannosyltransferase III
- GPI-MT-III
- Phosphatidylinositol-glycan biosynthesis class B protein
- PIG-B
|
| Enzyme 23 Gene Name |
PIGB |
| Enzyme 23 Protein Sequence |
>GPI mannosyltransferase 3
MRRPLSKCGMEPGGGDASLTLHGLQNRSHGKIKLRKRKSTLYFNTQEKSARRRGDLLGEN
IYLLLFTIALRILNCFLVQTSFVPDEYWQSLEVSHHMVFNYGYLTWEWTERLRSYTYPLI
FASIYKILHLLGKDSVQLLIWIPRLAQALLSAVADVRLYSLMKQLENQEVARWVFFCQLC
SWFTWYCCTRTLTNTMETVLTIIALFYYPLEGSKSMNSVKYSSLVALAFIIRPTAVILWT
PLLFRHFCQEPRKLDLILHHFLPVGFVTLSLSLMIDRIFFGQWTLVQFNFLKFNVLQNWG
TFYGSHPWHWYFSQGFPVILGTHLPFFIHGCYLAPKRYRILLVTVLWTLLVYSMLSHKEF
RFIYPVLPFCMVFCGYSLTHLKTWKKPALSFLFLSNLFLALYTGLVHQRGTLDVMSHIQK
VCYNNPNKSSASIFIMMPCHSTPYYSHVHCPLPMRFLQCPPDLTGKSHYLDEADVFYLNP
LNWLHREFHDDASLPTHLITFSILEEEISAFLISSNYKRTAVFFHTHLPEGRIGSHIYVY
ERKLKGKFNMKMKF
|
| Enzyme 23 Number of Residues |
554 |
| Enzyme 23 Molecular Weight |
65057 |
| Enzyme 23 Theoretical pI |
9.57 |
| Enzyme 23 GO Classification |
Not Available |
| Enzyme 23 General Function |
Not Available |
| Enzyme 23 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 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
- 63-83
136-156
192-212
224-244
255-275
315-335
340-360
362-382
387-407
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
1552169  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q92521  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PIGB_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
Not Available |
| Enzyme 23 GenBank Gene ID |
D42138  |
| Enzyme 23 GeneCard ID |
Q92521  |
| Enzyme 23 GenAtlas ID |
PIGB  |
| Enzyme 23 HGNC ID |
HGNC:8959  |
| Enzyme 23 Chromosome Location |
Not Available |
| Enzyme 23 Locus |
Not Available |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 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
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
12948 |
| Enzyme 24 Name |
Phosphatidylinositol-glycan biosynthesis class F protein |
| Enzyme 24 Synonyms |
- PIG-F
- GPI11 homolog
|
| Enzyme 24 Gene Name |
PIGF |
| Enzyme 24 Protein Sequence |
>Phosphatidylinositol-glycan biosynthesis class F protein
MKDNDIKRLLYTHLLCIFSIILSVFIPSLFLENFSILETHLTWLCICSGFVTAVNLVLYL
VVKPNTSSKRSSLSHKVTGFLKCCIYFLMSCFSFHVIFVLYGAPLIELALETFLFAVILS
TFTTVPCLCLLGPNLKAWLRVFSRNGVTSIWENSLQITTISSFVGAWLGALPIPLDWERP
WQVWPISCTLGATFGYVAGLVISPLWIYWNRKQLTYKNN
|
| Enzyme 24 Number of Residues |
219 |
| Enzyme 24 Molecular Weight |
24890 |
| Enzyme 24 Theoretical pI |
8.64 |
| Enzyme 24 GO Classification |
| Function |
| — |
| Process |
- GPI anchor biosynthesis
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid lipidation
- protein modification
|
| Component |
- cell
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- organelle membrane
|
|
| Enzyme 24 General Function |
Not Available |
| Enzyme 24 Specific Function |
Involved in GPI-anchor biosynthesis through the transfer of ethanolamine phosphate to the third mannose of GPI |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
- 11-31
42-62
86-106
113-133
155-175
189-209
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
303616  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q07326  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
PIGF_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
Not Available |
| Enzyme 24 GenBank Gene ID |
D13435  |
| Enzyme 24 GeneCard ID |
Q07326  |
| Enzyme 24 GenAtlas ID |
PIGF  |
| Enzyme 24 HGNC ID |
HGNC:8962  |
| Enzyme 24 Chromosome Location |
Not Available |
| Enzyme 24 Locus |
Not Available |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 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
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
12949 |
| Enzyme 25 Name |
GPI ethanolamine phosphate transferase 2 |
| Enzyme 25 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class G protein
- PIG-G
- GPI7 homolog
- hGPI7
|
| Enzyme 25 Gene Name |
PIGG |
| Enzyme 25 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 25 Number of Residues |
983 |
| Enzyme 25 Molecular Weight |
108174 |
| Enzyme 25 Theoretical pI |
7.15 |
| Enzyme 25 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- sulfuric ester hydrolase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 25 General Function |
Not Available |
| Enzyme 25 Specific Function |
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 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 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
58430451  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
Q5H8A4  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
PIGG_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
Not Available |
| Enzyme 25 GenBank Gene ID |
AB162713  |
| Enzyme 25 GeneCard ID |
Q5H8A4  |
| Enzyme 25 GenAtlas ID |
PIGG  |
| Enzyme 25 HGNC ID |
HGNC:25985  |
| Enzyme 25 Chromosome Location |
Not Available |
| Enzyme 25 Locus |
Not Available |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
12950 |
| Enzyme 26 Name |
GPI ethanolamine phosphate transferase 1 |
| Enzyme 26 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class N protein
- PIG-N
- MCD4 homolog
|
| Enzyme 26 Gene Name |
PIGN |
| Enzyme 26 Protein Sequence |
>GPI ethanolamine phosphate transferase 1
MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALY
ELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENP
VEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFD
NVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKE
IVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQ
FDDAFLKEWRLENWKRLDVNQADIAPLMTSLIGVPFPLNSVGILPVDYLNNTDLFKAESM
FTNAVQILEQFKVKMTQKKEVTLPFLFTPFKLLSDSKQFNILRKARSYIKHRKFDEVVSL
CKELIHLALKGLSYYHTYDRFFLGVNVVIGFVGWISYASLLIIKSHSNLIKGVSKEVKKP
SHLLPCSFVAIGILVAFFLLIQACPWTYYVYGLLPLPIWYAVLREFQVIQDLVVSVLTYP
LSHFVGYLLAFTLGIEVLVLSFFYRYMLTAGLTAFAAWPFLTRLWTRAKMTSLSWTFFSL
LLAVFPLMPVVGRKPDISLVMGAGLLVLLLSLCVVTSLMKRKDSFIKEELLVHLLQVLST
VLSMYVVYSTQSSLLRKQGLPLMNQIISWATLASSLVVPLLSSPVLFQRLFSILLSLMST
YLLLSTGYEALFPLVLSCLMFVWINIEQETLQQSGVCCKQKLTSIQFSYNTDITQFRQLY
LDDIRRAFFLVFFLVTAFFGTGNIASINSFDLASVYCFLTVFSPFMMGALMMWKILIPFV
LVMCAFEAVQLTTQLSSKSLFLIVLVISDIMALHFFFLVKDYGSWLDIGTSISHYVIVMS
MTIFLVFLNGLAQLLTTKKLRLCGKPKSHFM
|
| Enzyme 26 Number of Residues |
931 |
| Enzyme 26 Molecular Weight |
105811 |
| Enzyme 26 Theoretical pI |
8.87 |
| Enzyme 26 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 26 General Function |
Not Available |
| Enzyme 26 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 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
Not Available |
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 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 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
4206155  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
O95427  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
PIGN_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
Not Available |
| Enzyme 26 GenBank Gene ID |
AF109219  |
| Enzyme 26 GeneCard ID |
O95427  |
| Enzyme 26 GenAtlas ID |
PIGN  |
| Enzyme 26 HGNC ID |
HGNC:8967  |
| Enzyme 26 Chromosome Location |
Not Available |
| Enzyme 26 Locus |
Not Available |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 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
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
12951 |
| Enzyme 27 Name |
GPI ethanolamine phosphate transferase 3 |
| Enzyme 27 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class O protein
- PIG-O
|
| Enzyme 27 Gene Name |
PIGO |
| Enzyme 27 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 27 Number of Residues |
1089 |
| Enzyme 27 Molecular Weight |
118700 |
| Enzyme 27 Theoretical pI |
8.18 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
|
| Process |
- cellular metabolism
- metabolism
- nucleobase, nucleoside, nucleotide and nucleic acid metabolism
- nucleotide metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 27 General Function |
Not Available |
| Enzyme 27 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 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 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 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
21739535  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q8TEQ8  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
PIGO_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
Not Available |
| Enzyme 27 GenBank Gene ID |
AL833956  |
| Enzyme 27 GeneCard ID |
Q8TEQ8  |
| Enzyme 27 GenAtlas ID |
PIGO  |
| Enzyme 27 HGNC ID |
HGNC:23215  |
| Enzyme 27 Chromosome Location |
Not Available |
| Enzyme 27 Locus |
Not Available |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- 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
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
12952 |
| Enzyme 28 Name |
GPI transamidase component PIG-S |
| Enzyme 28 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class S protein
|
| Enzyme 28 Gene Name |
PIGS |
| Enzyme 28 Protein Sequence |
>GPI transamidase component PIG-S
MAAAGAAATHLEVARGKRAALFFAAVAIVLGLPLWWKTTETYRASLPYSQISGLNALQLR
LMVPVTVVFTRESVPLDDQEKLPFTVVHEREIPLKYKMKIKCRFQKAYRRALDHEEEALS
SGSVQEAEAMLDEPQEQAEGSLTVYVISEHSSLLPQDMMSYIGPKRTAVVRGIMHREAFN
IIGRRIVQVAQAMSLTEDVLAAALADHLPEDKWSAEKRRPLKSSLGYEITFSLLNPDPKS
HDVYWDIEGAVRRYVQPFLNALGAAGNFSVDSQILYYAMLGVNPRFDSASSSYYLDMHSL
PHVINPVESRLGSSAASLYPVLNFLLYVPELAHSPLYIQDKDGAPVATNAFHSPRWGGIM
VYNVDSKTYNASVLPVRVEVDMVRVMEVFLAQLRLLFGIAQPQLPPKCLLSGPTSEGLMT
WELDRLLWARSVENLATATTTLTSLAQLLGKISNIVIKDDVASEVYKAVAAVQKSAEELA
SGHLASAFVASQEAVTSSELAFFDPSLLHLLYFPDDQKFAIYIPLFLPMAVPILLSLVKI
FLETRKSWRKPEKTD
|
| Enzyme 28 Number of Residues |
555 |
| Enzyme 28 Molecular Weight |
61657 |
| Enzyme 28 Theoretical pI |
6.46 |
| Enzyme 28 GO Classification |
Not Available |
| Enzyme 28 General Function |
Not Available |
| Enzyme 28 Specific Function |
Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates |
| Enzyme 28 Pathways |
Not Available |
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
Not Available |
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
14456613  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q96S52  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
PIGS_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
Not Available |
| Enzyme 28 GenBank Gene ID |
AB057723  |
| Enzyme 28 GeneCard ID |
Q96S52  |
| Enzyme 28 GenAtlas ID |
PIGS  |
| Enzyme 28 HGNC ID |
HGNC:14937  |
| Enzyme 28 Chromosome Location |
Not Available |
| Enzyme 28 Locus |
Not Available |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 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
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
12953 |
| Enzyme 29 Name |
GPI transamidase component PIG-T precursor |
| Enzyme 29 Synonyms |
- Phosphatidylinositol- glycan biosynthesis class T protein
|
| Enzyme 29 Gene Name |
PIGT |
| Enzyme 29 Protein Sequence |
>GPI transamidase component PIG-T precursor
MAAAMPLALLVLLLLGPGGWCLAEPPRDSLREELVITPLPSGDVAATFQFRTRWDSELQR
EGVSHYRLFPKALGQLISKYSLRELHLSFTQGFWRTRYWGPPFLQAPSGAELWVWFQDTV
TDVDKSWKELSNVLSGIFCASLNFIDSTNTVTPTASFKPLGLANDTDHYFLRYAVLPREV
VCTENLTPWKKLLPCSSKAGLSVLLKADRLFHTSYHSQAVHIRPVCRNARCTSISWELRQ
TLSVVFDAFITGQGKKDWSLFRMFSRTLTEPCPLASESRVYVDITTYNQDNETLEVHPPP
TTTYQDVILGTRKTYAIYDLLDTAMINNSRNLNIQLKWKRPPENEAPPVPFLHAQRYVSG
YGLQKGELSTLLYNTHPYRAFPVLLLDTVPWYLRLYVHTLTITSKGKENKPSYIHYQPAQ
DRLQPHLLEMLIQLPANSVTKVSIQFERALLKWTEYTPDPNHGFYVSPSVLSALVPSMVA
AKPVDWEESPLFNSLFPVSDGSNYFVRLYTEPLLVNLPTPDFSMPYNVICLTCTVVAVCY
GSFYNLLTRTFHIEEPRTGGLAKRLANLIRRARGVPPL
|
| Enzyme 29 Number of Residues |
578 |
| Enzyme 29 Molecular Weight |
65700 |
| Enzyme 29 Theoretical pI |
8.49 |
| Enzyme 29 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
- GPI-anchor transamidase complex
- cell
- integral to membrane
- intrinsic to membrane
- membrane
- protein complex
|
|
| Enzyme 29 General Function |
Not Available |
| Enzyme 29 Specific Function |
Component of the GPI transamidase complex. Essential for transfer of GPI to proteins, particularly for formation of carbonyl intermediates |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
14456615  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q969N2  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
PIGT_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
Not Available |
| Enzyme 29 GenBank Gene ID |
AB057724  |
| Enzyme 29 GeneCard ID |
Q969N2  |
| Enzyme 29 GenAtlas ID |
PIGT  |
| Enzyme 29 HGNC ID |
HGNC:14938  |
| Enzyme 29 Chromosome Location |
Not Available |
| Enzyme 29 Locus |
Not Available |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 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
]
- 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
]
- 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
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
12954 |
| Enzyme 30 Name |
Phosphatidylinositol glycan anchor biosynthesis class U protein |
| Enzyme 30 Synonyms |
- GPI transamidase component PIG-U
- Cell division cycle protein 91-like 1
- Protein CDC91-like 1
|
| Enzyme 30 Gene Name |
PIGU |
| Enzyme 30 Protein Sequence |
>Phosphatidylinositol glycan anchor biosynthesis class U protein
MAAPLVLVLVVAVTVRAALFRSSLAEFISERVEVVSPLSSWKRVVEGLSLLDLGVSPYSG
AVFHETPLIIYLFHFLIDYAELVFMITDALTAIALYFAIQDFNKVVFKKQKLLLELDQYA
PDVAELIRTPMEMRYIPLKVALFYLLNPYTILSCVAKSTCAINNTLIAFFILTTIKGSAF
LSAIFLALATYQSLYPLTLFVPGLLYLLQRQYIPVKMKSKAFWIFSWEYAMMYVGSLVVI
ICLSFFLLSSWDFIPAVYGFILSVPDLTPNIGLFWYFFAEMFEHFSLFFVCVFQINVFFY
TIPLAIKLKEHPIFFMFIQIAVIAIFKSYPTVGDVALYMAFFPVWNHLYRFLRNIFVLTC
IIIVCSLLFPVLWHLWIYAGSANSNFFYAITLTFNVGQILLISDYFYAFLRREYYLTHGL
YLTAKDGTEAMLVLK
|
| Enzyme 30 Number of Residues |
435 |
| Enzyme 30 Molecular Weight |
50052 |
| Enzyme 30 Theoretical pI |
7.82 |
| Enzyme 30 GO Classification |
| Function |
| — |
| Process |
- GPI anchor biosynthesis
- biopolymer metabolism
- biopolymer modification
- macromolecule metabolism
- metabolism
- physiological process
- protein amino acid lipidation
- protein modification
|
| Component |
- cell
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- organelle membrane
|
|
| Enzyme 30 General Function |
Not Available |
| Enzyme 30 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 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
- 66-86
166-186
188-208
237-257
259-279
286-306
313-333
355-375
386-406
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
27372217  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q9H490  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
PIGU_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
Not Available |
| Enzyme 30 GenBank Gene ID |
AB086842  |
| Enzyme 30 GeneCard ID |
Q9H490  |
| Enzyme 30 GenAtlas ID |
PIGU  |
| Enzyme 30 HGNC ID |
HGNC:15791  |
| Enzyme 30 Chromosome Location |
Not Available |
| Enzyme 30 Locus |
Not Available |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- 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
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
12955 |
| Enzyme 31 Name |
GPI mannosyltransferase 2 |
| Enzyme 31 Synonyms |
- GPI mannosyltransferase II
- GPI-MT-II
- Phosphatidylinositol-glycan biosynthesis class V protein
- PIG-V
|
| Enzyme 31 Gene Name |
PIGV |
| Enzyme 31 Protein Sequence |
>GPI mannosyltransferase 2
MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVEGLL
GGLSHWDAEHFLFIAEHGYLYEHNFAFFPGFPLALLVGTELLRPLRGLLSLRSCLLISVA
SLNFLFFMLAAVALHDLGCLVLHCPHQSFYAALLFCLSPANVFLAAGYSEALFALLTFSA
MGQLERGRVWTSVLLFAFATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMAS
LFLSVFTLGLPFALFQYYAYTQFCLPGSARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDV
PLIYSYIQDVYWNVGFLKYYELKQVPNFLLAAPVAILVAWATWTYVTTHPWLCLTLGLQR
SKNNKTLEKPDLGFLSPQVFVYVVHAAVLLLFGGLCMHVQVLTRFLGSSTPIMYWFPAHL
LQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYHWKTCSPVTRYILGYFLTYWL
LGLLLHCNFLPWT
|
| Enzyme 31 Number of Residues |
493 |
| Enzyme 31 Molecular Weight |
55713 |
| Enzyme 31 Theoretical pI |
8.03 |
| Enzyme 31 GO Classification |
Not Available |
| Enzyme 31 General Function |
Not Available |
| Enzyme 31 Specific Function |
Alpha-1,6-mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the second mannose to the glycosylphosphatidylinositol during GPI precursor assembly |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
- 14-34
78-98
114-134
137-157
162-182
193-213
235-255
328-348
379-399
470-490
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
7020604  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
Q9NUD9  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
PIGV_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
Not Available |
| Enzyme 31 GenBank Gene ID |
AK000484  |
| Enzyme 31 GeneCard ID |
Q9NUD9  |
| Enzyme 31 GenAtlas ID |
PIGV  |
| Enzyme 31 HGNC ID |
HGNC:26031  |
| Enzyme 31 Chromosome Location |
Not Available |
| Enzyme 31 Locus |
Not Available |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
Not Available |
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
12956 |
| Enzyme 32 Name |
Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y |
| Enzyme 32 Synonyms |
- Phosphatidylinositol-glycan biosynthesis class Y protein
- PIG-Y
|
| Enzyme 32 Gene Name |
PIGY |
| Enzyme 32 Protein Sequence |
>Phosphatidylinositol N-acetylglucosaminyltransferase subunit Y
MFLSLPTLTVLIPLVSLAGLFYSASVEENFPQGCTSTASLCFYSLLLPITIPVYVFFHLW
TWMGIKLFRHN
|
| Enzyme 32 Number of Residues |
71 |
| Enzyme 32 Molecular Weight |
8058 |
| Enzyme 32 Theoretical pI |
7.41 |
| Enzyme 32 GO Classification |
Not Available |
| Enzyme 32 General Function |
Not Available |
| Enzyme 32 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 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
Not Available |
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
75674192  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q3MUY2  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
PIGY_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
Not Available |
| Enzyme 32 GenBank Gene ID |
AB206972  |
| Enzyme 32 GeneCard ID |
Q3MUY2  |
| Enzyme 32 GenAtlas ID |
PIGY  |
| Enzyme 32 HGNC ID |
HGNC:28213  |
| Enzyme 32 Chromosome Location |
Not Available |
| Enzyme 32 Locus |
Not Available |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
Not Available |
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
12961 |
| Enzyme 33 Name |
Pleckstrin homology domain-containing family A member 8 |
| Enzyme 33 Synonyms |
- Phosphoinositol 4-phosphate adapter protein 2
- Phosphatidylinositol- four-phosphate adapter protein 2
- hFAPP2
- Serologically defined breast cancer antigen NY-BR-86
|
| Enzyme 33 Gene Name |
PLEKHA8 |
| Enzyme 33 Protein Sequence |
>Pleckstrin homology domain-containing family A member 8
MEGVLYKWTNYLSGWQPRWFLLCGGILSYYDSPEDAWKGCKGSIQMAVCEIQVHSVDNTR
MDLIIPGEQYFYLKARSVAERQRWLVALGSAKACLTDSRTQKEKEFAENTENLKTKMSEL
RLYCDLLVQQVDKTKEVTTTGVSNSEEGIDVGTLLKSTCNTFLKTLEECMQIANAAFTSE
LLYRTPPGSPQLAMLKSSKMKHPIIPIHNSLERQMELSTCENGSLNMEINGEEEILMKNK
NSLYLKSAEIDCSISSEENTDDNITVQGEIRKEDGMENLKNHDNNLTQSGSDSSCSPECL
WEEGKEVIPTFFSTMNTSFSDIELLEDSGIPTEAFLASCYAVVPVLDKLGPTVFAPVKMD
LVGNIKKVNQKYITNKEEFTTLQKIVLHEVEADVAQVRNSATEALLWLKRGLKFLKGFLT
EVKNGEKDIQTALNNAYGKTLRQHHGWVVRGVFALALRATPSYEDFVAALTVKEGDHRKE
AFSIGMQRDLSLYLPAMKKQMAILDALYEVHGLESDEVV
|
| Enzyme 33 Number of Residues |
519 |
| Enzyme 33 Molecular Weight |
58307 |
| Enzyme 33 Theoretical pI |
4.89 |
| Enzyme 33 GO Classification |
Not Available |
| Enzyme 33 General Function |
Not Available |
| Enzyme 33 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 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 |
14165198  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q96JA3  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
PKHA8_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
Not Available |
| Enzyme 33 GenBank Gene ID |
AF380162  |
| Enzyme 33 GeneCard ID |
Q96JA3  |
| Enzyme 33 GenAtlas ID |
PLEKHA8  |
| Enzyme 33 HGNC ID |
HGNC:30037  |
| Enzyme 33 Chromosome Location |
Not Available |
| Enzyme 33 Locus |
Not Available |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 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
]
- 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
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
13104 |
| Enzyme 34 Name |
Sphingosine-1-phosphate phosphotase 2 |
| Enzyme 34 Synonyms |
Not Available |
| Enzyme 34 Gene Name |
SGPP2 |
| Enzyme 34 Protein Sequence |
>Sphingosine-1-phosphate phosphotase 2
MAELLRSLQDSQLVARFQRRCGLFPAPDEGPRENGADPTERAARVPGVEHLPAANGKGGE
APANGLRRAAAPEAYVQKYVVKNYFYYYLFQFSAALGQEVFYITFLPFTHWNIDPYLSRR
LIIIWVLVMYIGQVAKDVLKWPRPSSPPVVKLEKRLIAEYGMPSTHAMAATAIAFTLLIS
TMDRYQYPFVLGLVMAVVFSTLVCLSRLYTGMHTVLDVLGGVLITALLIVLTYPAWTFID
CLDSASPLFPVCVIVVPFFLCYNYPVSDYYSPTRADTTTILAAGAGVTIGFWINHFFQLV
SKPAESLPVIQNIPPLTTYMLVLGLTKFAVGIVLILLVRQLVQNLSLQVLYSWFKVVTRN
KEARRRLEIEVPYKFVTYTSVGICATTFVPMLHRFLGLP
|
| Enzyme 34 Number of Residues |
399 |
| Enzyme 34 Molecular Weight |
44741 |
| Enzyme 34 Theoretical pI |
9.25 |
| Enzyme 34 GO Classification |
Not Available |
| Enzyme 34 General Function |
Lipid transport and metabolism |
| Enzyme 34 Specific Function |
Not Available |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
126632031  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
A3KPB4  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
A3KPB4_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
Not Available |
| Enzyme 34 GenBank Gene ID |
BC134342  |
| Enzyme 34 GeneCard ID |
A3KPB4  |
| Enzyme 34 GenAtlas ID |
Not Available |
| Enzyme 34 HGNC ID |
Not Available |
| Enzyme 34 Chromosome Location |
Not Available |
| Enzyme 34 Locus |
Not Available |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
13105 |
| Enzyme 35 Name |
N-acylsphingosine amidohydrolase 3-like |
| Enzyme 35 Synonyms |
Not Available |
| Enzyme 35 Gene Name |
Not Available |
| Enzyme 35 Protein Sequence |
>N-acylsphingosine amidohydrolase 3-like
MGAPHWWDQLQAGSSEVDWCEDNYTIVPAIAEFYNTISNVLFFILPPICMCLFRQYATCF
NSGIYLIWTLLVVVGIGSVYFHATLSFLGQMLDELAVLWVLMCALAMWFPRRYLPKIFRN
DRGRFKVVVSVLSAVTTCLAFVKPAINNISLMTLGVPCTALLIAELKRCDNMRVFKLGLF
SGLWWTLALFCWISDRAFCELLSSFNFPYLHCMWHILICLAAYLGCVCFAYFDAASEIPE
QGPVIKFWPNEKWAFIGVPYVSLLCANKKSSVKIT
|
| Enzyme 35 Number of Residues |
275 |
| Enzyme 35 Molecular Weight |
31309 |
| Enzyme 35 Theoretical pI |
7.71 |
| Enzyme 35 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- cellular lipid metabolism
- ceramide metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- physiological process
- primary metabolism
- sphingoid metabolism
- sphingolipid metabolism
|
| Component |
- Golgi membrane
- cell
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- organelle membrane
|
|
| Enzyme 35 General Function |
Not Available |
| Enzyme 35 Specific Function |
Not Available |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
Not Available |
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
Not Available |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
A2A3R8  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
A2A3R8_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
Not Available |
| Enzyme 35 GenBank Gene ID |
AL391834  |
| Enzyme 35 GeneCard ID |
A2A3R8  |
| Enzyme 35 GenAtlas ID |
Not Available |
| Enzyme 35 HGNC ID |
Not Available |
| Enzyme 35 Chromosome Location |
Not Available |
| Enzyme 35 Locus |
Not Available |
| Enzyme 35 SNPs |
Not Available |
| Enzyme 35 General References |
Not Available |
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
13106 |
| Enzyme 36 Name |
Alkaline phytoceramidase |
| Enzyme 36 Synonyms |
- aPHC
- Alkaline ceramidase
- Alkaline dihydroceramidase SB89
|
| Enzyme 36 Gene Name |
PHCA |
| Enzyme 36 Protein Sequence |
>Alkaline phytoceramidase
MAPAADREGYWGPTTSTLDWCEENYSVTWYIAEFWNTVSNLIMIIPPMFGAIQSVRDGLE
KRYIASYLALTVVGMGSWCFHMTLKYEMQLLDELPMIYSCCIFVYCMFECFKIKNSVNYH
LLFTLVLFSLIVTTVYLKVKEPIFHQVMYGMLVFTLVLRSIYIVTWVYPWLRGLGYTSLG
IFLLGFLFWNIDNIFCESLRNFRKKVPPIIGITTQFHAWWHILTGLGSYLHILFSLYTRT
LYLRYRPKVKFLFGIWPVILFEPLRKH
|
| Enzyme 36 Number of Residues |
267 |
| Enzyme 36 Molecular Weight |
31566 |
| Enzyme 36 Theoretical pI |
8.77 |
| Enzyme 36 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
- hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
|
| Process |
- cellular lipid metabolism
- ceramide metabolism
- lipid metabolism
- membrane lipid metabolism
- metabolism
- physiological process
- primary metabolism
- sphingoid metabolism
- sphingolipid metabolism
|
| Component |
- Golgi membrane
- cell
- endoplasmic reticulum membrane
- integral to membrane
- intrinsic to membrane
- membrane
- organelle membrane
|
|
| Enzyme 36 General Function |
Not Available |
| Enzyme 36 Specific Function |
Hydrolyzes only phytoceramide into phytosphingosine and free fatty acid. Does not have reverse activity |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
Not Available |
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
- 29-51
63-84
94-111
118-137
147-169
174-196
216-238
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
14669436  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
Q9NUN7  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
APHC_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
Not Available |
| Enzyme 36 GenBank Gene ID |
AF214454  |
| Enzyme 36 GeneCard ID |
Q9NUN7  |
| Enzyme 36 GenAtlas ID |
PHCA  |
| Enzyme 36 HGNC ID |
HGNC:16066  |
| Enzyme 36 Chromosome Location |
Not Available |
| Enzyme 36 Locus |
Not Available |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Mao C, Xu R, Szulc ZM, Bielawska A, Galadari SH, Obeid LM: Cloning and characterization of a novel human alkaline ceramidase. A mammalian enzyme that hydrolyzes phytoceramide. J Biol Chem. 2001 Jul 13;276(28):26577-88. Epub 2001 May 16. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
14925 |
| Enzyme 37 Name |
Non-lysosomal glucosylceramidase |
| Enzyme 37 Synonyms |
- NLGase
- Glucosylceramidase 2
- Beta-glucocerebrosidase 2
- Beta-glucosidase 2
|
| Enzyme 37 Gene Name |
GBA2 |
| Enzyme 37 Protein Sequence |
>Non-lysosomal glucosylceramidase
MGTQDPGNMGTGVPASEQISCAKEDPQVYCPEETGGTKDVQVTDCKSPEDSRPPKETDCC
NPEDSGQLMVSYEGKAMGYQVPPFGWRICLAHEFTEKRKPFQANNVSLSNMIKHIGMGLR
YLQWWYRKTHVEKKTPFIDMINSVPLRQIYGCPLGGIGGGTITRGWRGQFCRWQLNPGMY
QHRTVIADQFTVCLRREGQTVYQQVLSLERPSVLRSWNWGLCGYFAFYHALYPRAWTVYQ
LPGQNVTLTCRQITPILPHDYQDSSLPVGVFVWDVENEGDEALDVSIMFSMRNGLGGGDD
APGGLWNEPFCLERSGETVRGLLLHHPTLPNPYTMAVAARVTAATTVTHITAFDPDSTGQ
QVWQDLLQDGQLDSPTGQSTPTQKGVGIAGAVCVSSKLRPRGQCRLEFSLAWDMPRIMFG
AKGQVHYRRYTRFFGQDGDAAPALSHYALCRYAEWEERISAWQSPVLDDRSLPAWYKSAL
FNELYFLADGGTVWLEVLEDSLPEELGRNMCHLRPTLRDYGRFGYLEGQEYRMYNTYDVH
FYASFALIMLWPKLELSLQYDMALATLREDLTRRRYLMSGVMAPVKRRNVIPHDIGDPDD
EPWLRVNAYLIHDTADWKDLNLKFVLQVYRDYYLTGDQNFLKDMWPVCLAVMESEMKFDK
DHDGLIENGGYADQTYDGWVTTGPSAYCGGLWLAAVAVMVQMAALCGAQDIQDKFSSILS
RGQEAYERLLWNGRYYNYDSSSRPQSRSVMSDQCAGQWFLKACGLGEGDTEVFPTQHVVR
ALQTIFELNVQAFAGGAMGAVNGMQPHGVPDKSSVQSDEVWVGVVYGLAATMIQEGLTWE
GFQTAEGCYRTVWERLGLAFQTPEAYCQQRVFRSLAYMRPLSIWAMQLALQQQQHKKASW
PKVKQGTGLRTGPMFGPKEAMANLSPE
|
| Enzyme 37 Number of Residues |
927 |
| Enzyme 37 Molecular Weight |
104650 |
| Enzyme 37 Theoretical pI |
5.74 |
| Enzyme 37 GO Classification |
Not Available |
| Enzyme 37 General Function |
Not Available |
| Enzyme 37 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 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 |
16215453  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
Q9HCG7  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
GBA2_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 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 37 GenBank Gene ID |
AJ309567  |
| Enzyme 37 GeneCard ID |
Q9HCG7  |
| Enzyme 37 GenAtlas ID |
GBA2  |
| Enzyme 37 HGNC ID |
HGNC:18986  |
| Enzyme 37 Chromosome Location |
Not Available |
| Enzyme 37 Locus |
Not Available |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 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
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
15257 |
| Enzyme 38 Name |
Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c) |
| Enzyme 38 Synonyms |
Not Available |
| Enzyme 38 Gene Name |
SPHK1 |
| Enzyme 38 Protein Sequence |
>Sphingosine kinase 1 (Sphingosine kinase 1, isoform CRA_c)
MDPVVGCGRGLFGFVFSAGGPRGVLPRPCRVLVLLNPRGGKGKALQLFRSHVQPLLAEAE
ISFTLMLTERRNHARELVRSEELGRWDALVVMSGDGLMHEVVNGLMERPDWETAIQKPLC
SLPAGSGNALAASLNHYAGYEQVTNEDLLTNCTLLLCRRLLSPMNLLSLHTASGLRLFSV
LSLAWGFIADVDLESEKYRRLGEMRFTLGTFLRLAALRTYRGRLAYLPVGRVGSKTPASP
VVVQQGPVDAHLVPLEEPVPSHWTVVPDEDFVLVLALLHSHLGSEMFAAPMGRCAAGVMH
LFYVRAGVSRAMLLRLFLAMEKGRHMEYECPYLVYVPVVAFRLEPKDGKGVFAVDGELMV
SEAVQGQVHPNYFWMVSGCVEPPPSWKPQQMPPPEEPL
|
| Enzyme 38 Number of Residues |
398 |
| Enzyme 38 Molecular Weight |
43945 |
| Enzyme 38 Theoretical pI |
7.33 |
| Enzyme 38 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- G-protein signaling, coupled to IP3 second messenger (phospholipase C activating)
- cell communication
- cell surface receptor linked signal transduction
- cellular process
- protein kinase C activation
- signal transduction
|
| Component |
| — |
|
| Enzyme 38 General Function |
Lipid transport and metabolism |
| Enzyme 38 Specific Function |
Not Available |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
Not Available |
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
14495625  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q96GK1  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
Q96GK1_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>1197 bp
ATGGATCCAGTGGTCGGTTGCGGACGTGGCCTCTTTGGTTTTGTTTTCTCAGCGGGCGGC
CCCCGGGGCGTGCTCCCGCGGCCCTGCCGCGTGCTGGTGCTGCTGAACCCGCGCGGCGGC
AAGGGCAAGGCCTTGCAGCTCTTCCGGAGTCACGTGCAGCCCCTTTTGGCTGAGGCTGAA
ATCTCCTTCACGCTGATGCTCACTGAGCGGCGGAACCACGCGCGGGAGCTGGTGCGGTCG
GAGGAGCTGGGCCGCTGGGACGCTCTGGTGGTCATGTCTGGAGACGGGCTGATGCACGAG
GTGGTGAACGGGCTCATGGAGCGGCCTGACTGGGAGACCGCCATCCAGAAGCCCCTGTGT
AGCCTCCCAGCAGGCTCTGGCAACGCGCTGGCAGCTTCCTTGAACCATTATGCTGGCTAT
GAGCAGGTCACCAATGAAGACCTCCTGACCAACTGCACGCTATTGCTGTGCCGCCGGCTG
CTGTCACCCATGAACCTGCTGTCTCTGCACACGGCTTCGGGGCTGCGCCTCTTCTCTGTG
CTCAGCCTGGCCTGGGGCTTCATTGCTGATGTGGACCTAGAGAGTGAGAAGTATCGGCGT
CTGGGGGAGATGCGCTTCACTCTGGGCACCTTCCTGCGTCTGGCAGCCCTGCGCACCTAC
CGCGGCCGACTGGCCTACCTCCCTGTAGGAAGAGTGGGTTCCAAGACACCTGCCTCCCCC
GTTGTGGTCCAGCAGGGCCCGGTAGATGCACACCTTGTGCCACTGGAGGAGCCAGTGCCC
TCTCACTGGACAGTGGTGCCCGACGAGGACTTTGTGCTAGTCCTGGCACTGCTGCACTCG
CACCTGGGCAGTGAGATGTTTGCTGCACCCATGGGCCGCTGTGCAGCTGGCGTCATGCAT
CTGTTCTACGTGCGGGCGGGAGTGTCTCGTGCCATGCTGCTGCGCCTCTTCCTGGCCATG
GAGAAGGGCAGGCATATGGAGTATGAATGCCCCTACTTGGTATATGTGCCCGTGGTCGCC
TTCCGCTTGGAGCCCAAGGATGGGAAAGGTGTGTTTGCAGTGGATGGGGAATTGATGGTT
AGCGAGGCCGTGCAGGGCCAGGTGCACCCAAACTACTTCTGGATGGTCAGCGGTTGCGTG
GAGCCCCCGCCCAGCTGGAAGCCCCAGCAGATGCCACCGCCAGAAGAGCCCTTATGA
|
| Enzyme 38 GenBank Gene ID |
BC009419  |
| Enzyme 38 GeneCard ID |
Q96GK1  |
| Enzyme 38 GenAtlas ID |
SPHK1  |
| Enzyme 38 HGNC ID |
HGNC:11240  |
| Enzyme 38 Chromosome Location |
17 |
| Enzyme 38 Locus |
17q25.2 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
15258 |
| Enzyme 39 Name |
ASAH1 protein |
| Enzyme 39 Synonyms |
Not Available |
| Enzyme 39 Gene Name |
Not Available |
| Enzyme 39 Protein Sequence |
>ASAH1 protein
MNCCIGLGEKARGSHRASYPSLSALFTEASILGFGSFAVKAQWTEDCRKSTYPPSGPTVF
PAVIRYRGAVPWYTINLDLPPYKRWHELMLDKAPVPGLLGNFPGPFEEEMKGIAAVTDIP
LGEIISFNIFYELFTVCTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITEQLKPLT
VNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWILGKKDA
MWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKESLDVYE
LDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLSTKPVLNK
LTVYTTLIDVTKGQFETYLRDCPDPCIGW
|
| Enzyme 39 Number of Residues |
389 |
| Enzyme 39 Molecular Weight |
44004 |
| Enzyme 39 Theoretical pI |
7.70 |
| Enzyme 39 GO Classification |
Not Available |
| Enzyme 39 General Function |
Not Available |
| Enzyme 39 Specific Function |
Not Available |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
Not Available |
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
16877108  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q96AS2  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
Q96AS2_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1170 bp
ATGAACTGCTGCATCGGGCTGGGAGAGAAGGCTCGCGGGTCCCACCGGGCCTCCTACCCA
AGTCTCAGCGCGCTTTTCACCGAGGCCTCAATTCTGGGATTTGGCAGCTTTGCTGTGAAA
GCCCAATGGACAGAGGACTGCAGAAAATCAACCTATCCTCCTTCAGGACCAACTGTCTTC
CCTGCTGTTATAAGGTACAGAGGTGCAGTTCCATGGTACACCATAAATCTTGACTTACCA
CCCTACAAAAGATGGCATGAATTGATGCTTGACAAGGCACCAGTGCCTGGCCTACTTGGC
AACTTTCCTGGCCCTTTTGAAGAGGAAATGAAGGGTATTGCCGCTGTTACTGATATACCT
TTAGGAGAGATTATTTCATTCAATATTTTTTATGAATTATTTACCGTTTGTACTTCAATA
GTAGCAGAAGACAAAAAAGGTCATCTAATACATGGGAGAAACATGGATTTTGGAGTATTT
CTTGGGTGGAACATAAATAATGATACCTGGGTCATAACTGAGCAACTAAAACCTTTAACA
GTGAATTTGGATTTCCAAAGAAACAACAAAACTGTCTTCAAGGCTTCAAGCTTTGCTGGC
TATGTGGGCATGTTAACAGGATTCAAACCAGGACTGTTCAGTCTTACACTGAATGAACGT
TTCAGTATAAATGGTGGTTATCTGGGTATTCTAGAATGGATTCTGGGAAAGAAAGATGCC
ATGTGGATAGGGTTCCTCACTAGAACAGTTCTGGAAAATAGCACAAGTTATGAAGAAGCC
AAGAATTTATTGACCAAGACCAAGATATTGGCCCCAGCCTACTTTATCCTGGGAGGCAAC
CAGTCTGGGGAAGGTTGTGTGATTACACGAGACAGAAAGGAATCATTGGATGTATATGAA
CTCGATGCTAAGCAGGGTAGATGGTATGTGGTACAAACAAATTATGACCGTTGGAAACAT
CCCTTCTTCCTTGATGATCGCAGAACGCCTGCAAAGATGTGTTTGAACCGCACCAGCCAA
GAGAATATCTCATTTGAAACCATGTATGATGTCCTGTCAACAAAACCTGTCCTCAACAAG
CTGACCGTATACACAACCTTGATAGATGTTACCAAAGGTCAATTCGAAACTTACCTGCGG
GACTGCCCTGACCCTTGTATAGGTTGGTGA
|
| Enzyme 39 GenBank Gene ID |
BC016828  |
| Enzyme 39 GeneCard ID |
Q96AS2  |
| Enzyme 39 GenAtlas ID |
Not Available |
| Enzyme 39 HGNC ID |
HGNC:735  |
| Enzyme 39 Chromosome Location |
Not Available |
| Enzyme 39 Locus |
Not Available |
| Enzyme 39 SNPs |
Not Available |
| Enzyme 39 General References |
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
16519 |
| Enzyme 40 Name |
cDNA, FLJ92680, Homo sapiens follicular lymphoma variant translocation 1 (FVT1),mRNA (Follicular lymphoma variant translocation 1, isoform CRA_a) |
| Enzyme 40 Synonyms |
Not Available |
| Enzyme 40 Gene Name |
FVT1 |
| Enzyme 40 Protein Sequence |
>cDNA, FLJ92680, Homo sapiens follicular lymphoma variant translocation 1 (FVT1),mRNA (Follicular lymphoma variant translocation 1, isoform CRA_a)
MLLLAAAFLVAFVLLLYMVSPLISPKPLALPGAHVVVTGGSSGIGKCIAIECYKQGAFIT
LVARNEDKLLQAKKEIEMHSINDKQVVLCISVDVSQDYNQVENVIKQAQEKLGPVDMLVN
CAGMAVSGKFEDLEVSTFERLMSINYLGSVYPSRAVITTMKERRVGRIVFVSSQAGQLGL
FGFTAYSASKFAIRGLAEALQMEVKPYNVYITVAYPPDTDTPGFAEENRTKPLETRLISE
TTSVCKPEQVAKQIVKDAIQGNFNSSLGSDGYMLSALTCGMAPVTSITEGLQQVVTMGLF
RTIALFYLGSFDSIVRRCMMQREKSENADKTA
|
| Enzyme 40 Number of Residues |
332 |
| Enzyme 40 Molecular Weight |
36188 |
| Enzyme 40 Theoretical pI |
7.18 |
| Enzyme 40 GO Classification |
| Function |
- catalytic activity
- oxidoreductase activity
|
| Process |
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 40 General Function |
Lipid transport and metabolism |
| Enzyme 40 Specific Function |
Not Available |
| Enzyme 40 Pathways |
Not Available |
| Enzyme 40 Reactions |
Not Available |
| Enzyme 40 Pfam Domain Function |
|
| 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 |
B2R5Y1  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
B2R5Y1_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
Not Available |
| Enzyme 40 GenBank Gene ID |
AK312360  |
| Enzyme 40 GeneCard ID |
B2R5Y1  |
| Enzyme 40 GenAtlas ID |
Not Available |
| Enzyme 40 HGNC ID |
Not Available |
| Enzyme 40 Chromosome Location |
18 |
| Enzyme 40 Locus |
18q21.3 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
Not Available |
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
16543 |
| Enzyme 41 Name |
cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a) |
| Enzyme 41 Synonyms |
Not Available |
| Enzyme 41 Gene Name |
PPAP2B |
| Enzyme 41 Protein Sequence |
>cDNA, FLJ92787, highly similar to Homo sapiens phosphatidic acid phosphatase type 2B (PPAP2B), mRNA (Phosphatidic acid phosphatase type 2B, isoform CRA_a)
MQNYKYDKAIVPESKNGGSPALNNNPRRSGSKRVLLICLDLFCLFMAGLPFLIIETSTIK
PYHRGFYCNDESIKYPLKTGETINDAVLCAVGIVIAILAIITGEFYRIYYLKKSRSTIQN
PYVAALYKQVGCFLFGCAISQSFTDIAKVSIGRLRPHFLSVCNPDFSQINCSEGYIQNYR
CRGDDSKVQEARKSFFSGHASFSMYTMLYLVLYLQARFTWRGARLLRPLLQFTLIMMAFY
TGLSRVSDHKHHPSDVLAGFAQGALVACCIVFFVSDLFKTKTTLSLPAPAIRKEILSPVD
IIDRNNHHNMM
|
| Enzyme 41 Number of Residues |
311 |
| Enzyme 41 Molecular Weight |
35116 |
| Enzyme 41 Theoretical pI |
9.40 |
| Enzyme 41 GO Classification |
Not Available |
| Enzyme 41 General Function |
Lipid transport and metabolism |
| 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 |
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
Not Available |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
B2R651  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
B2R651_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
Not Available |
| Enzyme 41 GenBank Gene ID |
AK312439  |
| Enzyme 41 GeneCard ID |
B2R651  |
| Enzyme 41 GenAtlas ID |
Not Available |
| Enzyme 41 HGNC ID |
Not Available |
| Enzyme 41 Chromosome Location |
Not Available |
| Enzyme 41 Locus |
Not Available |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
Not Available |
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
17337 |
| Enzyme 42 Name |
GPI-anchor transamidase |
| Enzyme 42 Synonyms |
- GPI transamidase
- Phosphatidylinositol-glycan biosynthesis class K protein
- PIG-K
- hGPI8
|
| 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
- legumain activity
- peptidase activity
|
| Process |
- cellular protein metabolism
- macromolecule metabolism
- metabolism
- physiological process
- protein metabolism
- 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 |
1518259  |
| 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 |
Not Available |
| Enzyme 42 GenBank Gene ID |
Y07596  |
| Enzyme 42 GeneCard ID |
PIGK  |
| Enzyme 42 GenAtlas ID |
Not Available |
| 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
]
- 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
- integral to membrane
- intrinsic to membrane
- membrane
- 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 |
2706632  |
| 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
CGGACCCTTTATGCTGCCCTGCTGGTGCTGACCAGCCCGGCAGCCACGCTCCTTGGCAGC
CTGTTCCTGTGGCGGGAGCTGCAGGAGGCGCCACTGTCACTGGCCGAGGGCTGGCAGCTC
TTCCTGGCAGCGCTAGCCCAGGGTGTGCTGGAGCACCACACCTACGGCGCCCTGCTCTTC
CCACTGCTGTCCCTGGGCCTCTACCCCTGCTGGCTGCTTTTCTGGAATGTGCTCTTCTGG
AAGTGA
|
| Enzyme 43 GenBank Gene ID |
AB006969  |
| Enzyme 43 GeneCard ID |
GPAA1  |
| Enzyme 43 GenAtlas ID |
Not Available |
| 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 |
Not Available |
| Enzyme 44 General Function |
Involved in glycolipid binding |
| 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 |
Not Available |
| 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 |
Not Available |
| Enzyme 45 General Function |
Involved in glycolipid binding |
| 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 |
152061018  |
| 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 |
Not Available |
| Enzyme 45 GenBank Gene ID |
BC150536  |
| Enzyme 45 GeneCard ID |
GLTPD2  |
| Enzyme 45 GenAtlas ID |
Not Available |
| 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 |
Not Available |
| Enzyme 46 General Function |
Involved in glycolipid binding |
| 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 |
Not Available |
| 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 |
Not Available |
| Enzyme 46 GenBank Gene ID |
AC007285  |
| Enzyme 46 GeneCard ID |
PLEKHA8  |
| Enzyme 46 GenAtlas ID |
Not Available |
| 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 |
Not Available |
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
17786 |
| Enzyme 47 Name |
cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA |
| Enzyme 47 Synonyms |
- SubName: Pleckstrin homology domain containing, family A (Phosphoinositide binding specific) member 8, isoform CRA_a
|
| Enzyme 47 Gene Name |
PLEKHA8 |
| Enzyme 47 Protein Sequence |
>cDNA FLJ61247, highly similar to Mus musculus pleckstrin homology domain containing, family A member 8, mRNA
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 |
Not Available |
| Enzyme 47 General Function |
Involved in glycolipid binding |
| 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 |
Not Available |
| 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
MLFLLLPLLAVLPGDGNADGLKEPLSFHVIWIASFYNHSWKQNLVSGWLSDLQTHTWDSN
SSTIVFLWPWSRGNFSNEEWKELETLFRIRTIRSFEGIRRYAHELQFEYPFEIQVTGGCE
LHSGKVSGSFLQLAYQGSDFVSFQNNSWLPYPVAGNMAKHFCKVLNQNQHENDITHNLLS
DTCPRFILGLLDAGKAHLQRQVKPEAWLSHGPSPGPGHLQLVCHVSGFYPKPVWVMWMRG
EQEQQGTQRGDILPSADGTWYLRATLEVAAGEAADLSCRVKHSSLEGQDIVLYWEHHSSV
GFIILAVIVPLLLLIGLALWFRKRCFC
|
| Enzyme 48 Number of Residues |
327 |
| Enzyme 48 Molecular Weight |
37172.2 |
| Enzyme 48 Theoretical pI |
6.79 |
| Enzyme 48 GO Classification |
| Function |
- MHC class I receptor activity
- receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- antigen presentation
- defense response
- immune response
- response to biotic stimulus
- response to stimulus
|
| Component |
- MHC class I protein complex
- MHC protein complex
- protein complex
|
|
| Enzyme 48 General Function |
Involved in antigen processing and presentation |
| 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 |
Not Available |
| 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
]
- 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 |
Not Available |
| Enzyme 49 General Function |
Involved in glycolipid binding |
| 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 |
Not Available |
| 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 |
Not Available |
| Enzyme 49 GenBank Gene ID |
CR599582  |
| Enzyme 49 GeneCard ID |
GLTPD1  |
| Enzyme 49 GenAtlas ID |
Not Available |
| 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 |
- MHC class I receptor activity
- receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- antigen presentation
- defense response
- immune response
- response to biotic stimulus
- response to stimulus
|
| Component |
- MHC class I protein complex
- MHC protein complex
- protein complex
|
|
| Enzyme 50 General Function |
Involved in antigen processing and presentation |
| 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 |
180066  |
| 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
CGAGTGAGACACAGCAGTCTAGGAGGCCAGGACATCATCCTCTACTGGGGACACCACTCT
TCCATGAATTGGATTGCCTTGGTAGTGATAGTGCCCTTGGTGATTCTAATAGTCCTTGTG
TTATGGTTTAAGAAGCACTGCTCATATCAGGACATCCTGTGA
|
| Enzyme 50 GenBank Gene ID |
M28827  |
| Enzyme 50 GeneCard ID |
CD1C  |
| Enzyme 50 GenAtlas ID |
Not Available |
| 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 Gram-negative bacterial cell surface 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 |
186966  |
| 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 |
Not Available |
| Enzyme 51 GenBank Gene ID |
M35533  |
| Enzyme 51 GeneCard ID |
LBP  |
| Enzyme 51 GenAtlas ID |
Not Available |
| Enzyme 51 HGNC ID |
HGNC:6517  |
| Enzyme 51 Chromosome Location |
2 |
| Enzyme 51 Locus |
20q11.23-q12 |
| 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
]
- 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 |
Not Available |
| Enzyme 52 General Function |
Involved in glycolipid binding |
| 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 |
Not Available |
| Enzyme 52 GenBank Gene ID |
AL122073  |
| Enzyme 52 GeneCard ID |
DKFZp434L0435  |
| Enzyme 52 GenAtlas ID |
Not Available |
| 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 |
- MHC class I receptor activity
- receptor activity
- signal transducer activity
- transmembrane receptor activity
|
| Process |
- antigen presentation
- defense response
- immune response
- response to biotic stimulus
- response to stimulus
|
| Component |
- MHC class I protein complex
- MHC protein complex
- protein complex
|
|
| Enzyme 53 General Function |
Involved in protein binding |
| 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 |
180056  |
| 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
ATGCTGCTGCTGCCATTTCAACTGTTAGCTGTTCTCTTTCCTGGTGGTAACAGTGAACAT
GCCTTCCAGGGGCCGACCTCCTTTCATGTTATCCAGACCTCGTCCTTTACCAATAGTACC
TGGGCACAAACTCAAGGCTCAGGCTGGTTGGATGATTTGCAGATTCATGGCTGGGATAGC
GACTCAGGCACTGCCATATTCCTGAAGCCTTGGTCTAAAGGTAACTTTAGTGATAAGGAG
GTTGCTGAGTTAGAGGAGATATTCCGAGTCTACATCTTTGGATTCGCTCGAGAAGTACAA
GACTTTGCCGGTGATTTCCAGATGAAATACCCCTTTGAGATCCAGGGCATAGCAGGCTGT
GAGCTACATTCTGGAGGTGCCATAGTAAGCTTCCTGAGGGGAGCTCTAGGAGGATTGGAT
TTCCTGAGTGTCAAGAATGCTTCATGTGTGCCTTCCCCAGAAGGTGGCAGCAGGGCACAG
AAATTCTGTGCACTAATCATACAATATCAAGGTATCATGGAAACTGTGAGAATTCTCCTC
TATGAAACCTGCCCCCGATATCTCTTGGGCGTCCTCAATGCAGGAAAAGCAGATCTGCAA
AGACAAGTGAAGCCTGAGGCCTGGCTGTCCAGTGGCCCCAGTCCTGGACCTGGCCGTCTG
CAGCTTGTGTGCCATGTCTCAGGATTCTACCCAAAGCCCGTGTGGGTGATGTGGATGCGG
GGTGAGCAGGAGCAGCAGGGCACTCAGCTAGGGGACATCCTGCCCAATGCTAACTGGACA
TGGTATCTCCGAGCAACCCTGGATGTGGCAGATGGGGAGGCGGCTGGCCTGTCCTGTCGG
GTGAAGCACAGCAGTTTAGAGGGCCAGGACATCATCCTCTACTGGAGAAACCCCACCTCC
ATTGGCTCAATTGTTTTGGCAATAATAGTGCCTTCCTTGCTCCTTTTGCTATGCCTTGCA
TTATGGTATATGAGGCGCCGGTCATATCAGAATATCCCATGA
|
| Enzyme 53 GenBank Gene ID |
M28826  |
| Enzyme 53 GeneCard ID |
CD1B  |
| Enzyme 53 GenAtlas ID |
Not Available |
| 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 |
Not Available |
| Enzyme 54 General Function |
Involved in glycolipid binding |
| 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 |
6959686  |
| 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 |
Not Available |
| 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
]
- 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
]
|
| Enzyme 54 Metabolite References |
Not Available |