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Enzyme 1
[top]
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| Enzyme 1 ID |
5264 |
| Enzyme 1 Name |
Fatty acid synthase |
| Enzyme 1 Synonyms |
- [Acyl-carrier-protein] S-acetyltransferase
- [Acyl-carrier-protein] S-malonyltransferase
- 3-oxoacyl-[acyl-carrier-protein] synthase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase
- Enoyl-[acyl-carrier-protein] reductase
- Oleoyl-[acyl-carrier-protein] hydrolase
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| Enzyme 1 Gene Name |
FASN |
| Enzyme 1 Protein Sequence |
>Fatty acid synthase
MEEVVIAGMSGKLPESENLQEFWDNLIGGVDMVTDDDRRWKAGLYGLPRRSGKLKDLSRF
DASFFGVHPKQAHTMDPQLRLLLEVTYEAIVDGGINPDSLRGTHTGVWVGVSGSETSEAL
SRDPETLVGYSMVGCQRAMMANRLSFFFDFRGPSIALDTACSSSLMALQNAYQAIHSGQC
PAAIVGGINVLLKPNTSVQFLRLGMLSPEGTCKAFDTAGNGYCRSEGVVAVLLTKKSLAR
RVYATILNAGTNTDGFKEQGVTFPSGDIQEQLIRSLYQSAGVAPESFEYIEAHGTGTKVG
DPQELNGITRALCATRQEPLLIGSTKSNMGHPEPASGLAALAKVLLSLEHGLWAPNLHFH
SPNPEIPALLDGRLQVVDQPLPVRGGNVGINSFGFGGSNVHIILRPNTQPPPAPAPHATL
PRLLRASGRTPEAVQKLLEQGLRHSQDLAFLSMLNDIAAVPATAMPFRGYAVLGGERGGP
EVQQVPAGERPLWFICSGMGTQWRGMGLSLMRLDRFRDSILRSDEAVKPFGLKVSQLLLS
TDESTFDDIVHSFVSLTAIQIGLIDLLSCMGLRPDGIVGHSLGEVACGYADGCLSQEEAV
LAAYWRGQCIKEAHLPPGAMAAVGLSWEECKQRCPPGVVPACHNSKDTVTISGPQAPVFE
FVEQLRKEGVFAKEVRTGGMAFHSYFMEAIAPPLLQELKKVIREPKPRSARWLSTSIPEA
QWHSSLARTSSAEYNVNNLVSPVLFQEALWHVPEHAVVLEIAPHALLQAVLKRGLKPSCT
IIPLMKKDHRDNLEFFLAGIGRLHLSGIDANPNALFPPVEFPAPRGTPLISPLIKWDHSL
AWDVPAAEDFPNGSGSPSAAIYNIDTSSESPDHYLVDHTLDGRVLFPATGYLSIVWKTLA
RALGLGVEQLPVVFEDVVLHQATILPKTGTVSLEVRLLEASRAFEVSENGNLVVSGKVYQ
WDDPDPRLFDHPESPTPNPTEPLFLAQAEVYKELRLRGYDYGPHFQGILEASLEGDSGRL
LWKDNWVSFMDTMLQMSILGSAKHGLYLPTRVTAIHIDPATHRQKLYTLQDKAQVADVVV
SRWLRVTVAGGVHISGLHTESAPRRQQEQQVPILEKFCFTPHTEEGCLSERAALQEELQL
CKGLVQALQTKVTQQGLKMVVPGLDGAQIPRDPSQQELPRLLSAACRLQLNGNLQLELAQ
VLAQERPKLPEDPLLSGLLDSPALKACLDTAVENMPSLKMKVVEVLAGHGHLYSRIPGLL
SPHPLLQLSYTATDRHPQALEAAQAELQQHDVAQGQWDPADPAPSALGSADLLVCNCAVA
ALGDPASALSNMVAALREGGFLLLHTLLRGHPLGDIVAFLTSTEPQYGQGILSQDAWESL
FSRVSLRLVGLKKSFYGSTLFLCRRPTPQDSPIFLPVDDTSFRWVESLKGILADEDSSRP
VWLKAINCATSGVVGLVNCLRREPGGNRLRCVLLSNLSSTSHVPEVDPGSAELQKVLQGD
LVMNVYRDGAWGAFRHFLLEEDKPEEPTAHAFVSTLTRGDLSSIRWVCSSLRHAQPTCPG
AQLCTVYYASLNFRDIMLATGKLSPDAIPGKWTSQDSLLGMEFSGRDASGKRVMGLVPAK
GLATSVLLSPDFLWDVPSNWTLEEAASVPVVYSTAYYALVVRGRVRPGETLLIHSGSGGV
GQAAIAIALSLGCRVFTTVGSAEKRAYLQARFPQLDSTSFANSRDTSFEQHVLWHTGGKG
VDLVLNSLAEEKLQASVRCLATHGRFLEIGKFDLSQNHPLGMAIFLKNVTFHGVLLDAFF
NESSADWREVWALVQAGIRDGVVRPLKCTVFHGAQVEDAFRYMAQGKHIGKVVVQVLAEE
PEAVLKGAKPKLMSAISKTFCPAHKSYIIAGGLGGFGLELAQWLIQRGVQKLVLTSRSGI
RTGYQAKQVRRWRRQGVQVQVSTSNISSLEGARGLIAEAAQLGPVGGVFNLAVVLRDGLL
ENQTPEFFQDVCKPKYSGTLNLDRVTREACPELDYFVVFSSVSCGRGNAGQSNYGFANSA
MERICEKRRHEGLPGLAVQWGAIGDVGILVETMSTNDTIVSGTLPQRMASCLEVLDLFLN
QPHMVLSSFVLAEKAAAYRDRDSQRDLVEAVAHILGIRDLAAVNLDSSLADLGLDSLMSV
EVRQTLERELNLVLSVREVRQLTLRKLQELSSKADEASELACPTPKEDGLAQQQTQLNLR
SLLVNPEGPTLMRLNSVQSSERPLFLVHPIEGSTTVFHSLASRLSIPTYGLQCTRAAPLD
SIHSLAAYYIDCIRQVQPEGPYRVAGYSYGACVAFEMCSQLQAQQSPAPTHNSLFLFDGS
PTYVLAYTQSYRAKLTPGCEAEAETEAICFFVQQFTDMEHNRVLEALLPLKGLEERVAAA
VDLIIKSHQGLDRQELSFAARSFYYKLRAAEQYTPKAKYHGNVMLLRAKTGGAYGEDLGA
DYNLSQVCDGKVSVHVIEGDHRTLLEGSGLESIISIIHSSLAEPRVSVREG
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| Enzyme 1 Number of Residues |
2511 |
| Enzyme 1 Molecular Weight |
273424.1 |
| Enzyme 1 Theoretical pI |
6.41 |
| Enzyme 1 GO Classification |
| Function |
- acyl carrier activity
- amino acid binding
- binding
- carboxylic acid binding
- catalytic activity
- cation binding
- cofactor binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- oxidoreductase activity
- phosphopantetheine binding
- substrate-specific transporter activity
- transferase activity
- transition metal ion binding
- transporter activity
- zinc ion binding
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| Process |
- biosynthetic process
- metabolic process
- oxidation reduction
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| Component |
| — |
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| Enzyme 1 General Function |
Involved in transferase activity |
| Enzyme 1 Specific Function |
Fatty acid synthetase catalyzes the formation of long- chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. This multifunctional protein has 7 catalytic activities and an acyl carrier protein |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- a (3R)-3-hydroxypalmitoyl-[acyl-carrier protein] = a hexadec-2-enoyl-[acyl-carrier protein] + H2O [RN:R04462]
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| Enzyme 1 Pfam Domain Function |
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| Enzyme 1 Signals |
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| Enzyme 1 Transmembrane Regions |
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| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
41872631  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P49327  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
FAS_HUMAN  |
| Enzyme 1 PDB ID |
1XKT  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>7536 bp
ATGGAGGAGGTGGTGATTGCCGGCATGTCCGGGAAGCTGCCAGAGTCGGAGAACTTGCAG
GAGTTCTGGGACAACCTCATCGGCGGTGTGGACATGGTCACGGACGATGACCGTCGCTGG
AAGGCGGGGCTCTACGGCCTGCCCCGGCGGTCCGGCAAGCTGAAGGACCTGTCTAGGTTT
GATGCCTCCTTCTTCGGAGTCCACCCCAAGCAGGCACACACGATGGACCCTCAGCTGCGG
CTGCTGCTGGAAGTCACCTATGAAGCCATCGTGGACGGAGGCATCAACCCAGATTCACTC
CGAGGAACACACACTGGCGTCTGGGTGGGCGTGAGCGGCTCTGAGACCTCGGAGGCCCTG
AGCCGAGACCCCGAGACACTCGTGGGCTACAGCATGGTGGGCTGCCAGCGAGCGATGATG
GCCAACCGGCTCTCCTTCTTCTTCGACTTCAGAGGGCCCAGCATCGCACTGGACACAGCC
TGCTCCTCCAGCCTGATGGCCCTGCAGAACGCCTACCAGGCCATCCACAGCGGGCAGTGC
CCTGCCGCCATCGTGGGGGGCATCAATGTCCTGCTGAAGCCCAACACCTCCGTGCAGTTC
TTGAGGCTGGGGATGCTCAGCCCCGAGGGCACCTGCAAGGCCTTCGACACAGCGGGGAAT
GGGTACTGCCGCTCGGAGGGTGTGGTGGCCGTCCTGCTGACCAAGAAGTCCCTGGCCCGG
CGGGTGTACGCCACCATCCTGAACGCCGGCACCAATACAGATGGCTTCAAGGAGCAAGGC
GTGACCTTCCCCTCAGGGGATATCCAGGAGCAGCTCATCCGCTCGTTGTACCAGTCGGCC
GGAGTGGCCCCTGAGTCATTTGAATACATCGAAGCCCACGGCACAGGCACCAAGGTGGGC
GACCCCCAGGAGCTGAATGGCATCACCCGAGCCCTGTGCGCCACCCGCCAGGAGCCGCTG
CTCATCGGCTCCACCAAGTCCAACATGGGGCACCCGGAGCCAGCCTCGGGGCTGGCAGCC
CTGGCCAAGGTGCTGCTGTCCCTGGAGCACGGGCTCTGGGCCCCCAACCTGCACTTCCAT
AGCCCCAACCCTGAGATCCCAGCGCTGTTGGATGGGCGGCTGCAGGTGGTGGACCAGCCC
CTGCCCGTCCGTGGCGGCAACGTGGGCATCAACTCCTTTGGCTTCGGGGGCTCCAACGTG
CACATCATCCTGAGGCCCAACACGCAGCCGCCCCCCGCACCCGCCCCACATGCCACCCTG
CCCCGTCTGCTGCGGGCCAGCGGACGCACCCCTGAGGCCGTGCAGAAGCTGCTGGAGCAG
GGCCTCCGGCACAGCCAGGACCTGGCTTTCCTGAGCATGCTGAACGACATCGCGGCTGTC
CCCGCCACCGCCATGCCCTTCCGTGGCTACGCTGTGCTGGGTGGTGAGCGCGGTGGCCCA
GAGGTGCAGCAGGTGCCCGCTGGCGAGCGCCCGCTCTGGTTCATCTGCTCTGGGATGGGC
ACACAGTGGCGCGGGATGGGGCTGAGCCTCATGCGCCTGGACCGCTTCCGAGATTCCATC
CTACGCTCCGATGAGGCTGTGAAGCCATTCGGCCTGAAGGTGTCACAGCTGCTGCTGAGC
ACAGACGAGAGCACCTTTGATGACATCGTCCATTCGTTTGTGAGCCTGACTGCCATCCAG
ATAGGCCTCATAGACCTGCTGAGCTGCATGGGGCTGAGGCCAGATGGCATCGTCGGCCAC
TCCCTGGGGGAGGTGGCCTGTGGCTACGCCGACGGCTGCCTGTCCCAGGAGGAGGCCGTC
CTCGCTGCCTACTGGAGGGGACAGTGCATCAAAGAAGCCCATCTCCCGCCGGGCGCCATG
GCAGCCGTGGGCTTGTCCTGGGAGGAGTGTAAACAGCGCTGCCCCCCGGGCGTGGTGCCC
GCCTGCCACAACTCCAAGGACACAGTCACCATCTCGGGACCTCAGGCCCCGGTGTTTGAG
TTCGTGGAGCAGCTGAGGAAGGAGGGTGTGTTTGCCAAGGAGGTGCGGACCGGCGGTATG
GCCTTCCACTCCTACTTCATGGAGGCCATCGCACCCCCACTGCTGCAGGAGCTCAAGAAG
GTGATCCGGGAGCCGAAGCCACGTTCAGCCCGCTGGCTCAGCACCTCTATCCCCGAGGCC
CAGTGGCACAGCAGCCTGGCACGCACGTCCTCCGCCGAGTACAATGTCAACAACCTGGTG
AGCCCTGTGCTGTTCCAGGAGGCCCTGTGGCACGTGCCTGAGCACGCGGTGGTGCTGGAG
ATCGCGCCCCACGCCCTGCTGCAGGCTGTCCTGAAGCGTGGCCTGAAGCCGAGCTGCACC
ATCATCCCCCTGATGAAGAAGGATCACAGGGACAACCTGGAGTTCTTCCTGGCCGGCATC
GGCAGGCTGCACCTCTCAGGCATCGACGCCAACCCCAATGCCTTGTTCCCACCTGTGGAG
TTCCCAGCTCCCCGAGGAACTCCCCTCATCTCCCCACTCATCAAGTGGGACCACAGCCTG
GCCTGGGACGTGCCGGCCGCCGAGGACTTCCCCAACGGTTCAGGTTCCCCCTCAGCCGCC
ATCTACAACATCGACACCAGCTCCGAGTCTCCTGACCACTACCTGGTGGACCACACCCTC
GACGGTCGCGTCCTCTTCCCCGCCACTGGCTACCTGAGCATAGTGTGGAAGACGCTGGCC
CGCGCCCTGGGCCTGGGCGTCGAGCAGCTGCCTGTGGTGTTTGAGGATGTGGTGCTGCAC
CAGGCCACCATCCTGCCCAAGACTGGGACAGTGTCCCTGGAGGTACGGCTCCTGGAGGCC
TCCCGTGCCTTCGAGGTGTCAGAGAACGGCAACCTGGTAGTGAGTGGGAAGGTGTACCAG
TGGGATGACCCTGACCCCAGGCTCTTCGACCACCCGGAAAGCCCCACCCCCAACCCCACG
GAGCCCCTCTTCCTGGCCCAGGCTGAAGTTTACAAGGAGCTGCGTCTGCGTGGCTACGAC
TACGGCCCTCATTTCCAGGGCATCCTGGAGGCCAGCCTGGAAGGTGACTCGGGGAGGCTG
CTGTGGAAGGATAACTGGGTGAGCTTCATGGACACCATGCTGCAGATGTCCATCCTGGGC
TCGGCCAAGCACGGCCTGTACCTGCCCACCCGTGTCACCGCCATCCACATCGACCCTGCC
ACCCACAGGCAGAAGCTGTACACACTGCAGGACAAGGCCCAAGTGGCTGACGTGGTGGTG
AGCAGGTGGCTGAGGGTCACAGTGGCCGGAGGCGTCCACATCTCCGGGCTCCACACTGAG
TCGGCCCCGCGGCGGCAGCAGGAGCAGCAGGTGCCCATCCTGGAGAAGTTTTGCTTCACT
CCCCACACGGAGGAGGGGTGCCTGTCTGAGCGCGCTGCCCTGCAGGAGGAGCTGCAACTG
TGCAAGGGGCTGGTGCAGGCACTGCAGACCAAGGTGACCCAGCAGGGGCTGAAGATGGTG
GTGCCCGGACTGGATGGGGCCCAGATCCCCCGGGACCCCTCACAGCAGGAACTGCCCCGG
CTGTTGTCGGCTGCCTGCAGGCTTCAGCTCAACGGGAACCTGCAGCTGGAGCTGGCGCAG
GTGCTGGCCCAGGAGAGGCCCAAGCTGCCAGAGGACCCTCTGCTCAGCGGCCTCCTGGAC
TCCCCGGCACTCAAGGCCTGCCTGGACACTGCCGTGGAGAACATGCCCAGCCTGAAGATG
AAGGTGGTGGAGGTGCTGGCTGGCCACGGTCACCTGTATTCCCGCATCCCAGGCCTGCTC
AGCCCCCATCCCCTGCTGCAGCTGAGCTACACGGCCACCGACCGCCACCCCCAGGCCCTG
GAGGCTGCCCAGGCCGAGCTGCAGCAGCACGACGTTGCCCAGGGCCAGTGGGATCCCGCA
GACCCTGCCCCCAGCGCCCTGGGCAGCGCCGACCTCCTGGTGTGCAACTGTGCTGTGGCT
GCCCTCGGGGACCCGGCCTCAGCTCTCAGCAACATGGTGGCTGCCCTGAGAGAAGGGGGC
TTTCTGCTCCTGCACACACTGCTCCGGGGGCACCCCCTCGGGGACATCGTGGCCTTCCTC
ACCTCCACTGAGCCGCAGTATGGCCAGGGCATCCTGAGCCAGGACGCGTGGGAGAGCCTC
TTCTCCAGGGTGTCGCTGCGCCTGGTGGGCCTGAAGAAGTCCTTCTACGGCTCCACGCTC
TTCCTGTGCCGCCGGCCCACCCCGCAGGACAGCCCCATCTTCCTGCCGGTGGACGATACC
AGCTTCCGCTGGGTGGAGTCTCTGAAGGGCATCCTGGCTGACGAAGACTCTTCCCGGCCT
GTGTGGCTGAAGGCCATCAACTGTGCCACCTCGGGCGTGGTGGGCTTGGTGAACTGTCTC
CGCCGAGAGCCCGGCGGGAACCGCCTCCGGTGTGTGCTGCTCTCCAACCTCAGCAGCACC
TCCCACGTCCCGGAGGTGGACCCGGGCTCCGCAGAACTGCAGAAGGTGTTGCAGGGAGAC
CTGGTGATGAACGTCTACCGCGACGGGGCCTGGGGGGCTTTCCGCCACTTCCTGCTGGAG
GAGGACAAGCCTGAGGAGCCGACGGCACATGCCTTTGTGAGCACCCTCACCCGGGGGGAC
CTGTCCTCCATCCGCTGGGTCTGCTCCTCGCTGCGCCATGCCCAGCCCACCTGCCCTGGC
GCCCAGCTCTGCACGGTCTACTACGCCTCCCTCAACTTCCGCGACATCATGCTGGCCACT
GGCAAGCTGTCCCCTGATGCCATCCCAGGGAAGTGGACCTCCCAGGACAGCCTGCTAGGT
ATGGAGTTCTCGGGCCGAGACGCCAGCGGCAAGCGTGTGATGGGACTGGTGCCTGCCAAG
GGCCTGGCCACCTCTGTCCTGCTGTCACCGGACTTCCTCTGGGATGTGCCTTCCAACTGG
ACGCTGGAGGAGGCGGCCTCGGTGCCTGTCGTCTACAGCACGGCCTACTACGCGCTGGTG
GTGCGTGGGCGGGTGCGCCCCGGGGAGACGCTGCTCATCCACTCGGGCTCGGGCGGCGTG
GGCCAGGCCGCCATCGCCATCGCCCTCAGTCTGGGCTGCCGCGTCTTCACCACCGTGGGG
TCGGCTGAGAAGCGGGCGTACCTCCAGGCCAGGTTCCCCCAGCTCGACAGCACCAGCTTC
GCCAACTCCCGGGACACATCCTTCGAGCAGCATGTGCTGTGGCACACGGGCGGGAAGGGC
GTTGACCTGGTCTTGAACTCCTTGGCGGAAGAGAAGCTGCAGGCCAGCGTGAGGTGCTTG
GCTACGCACGGTCGCTTCCTGGAAATTGGCAAATTCGACCTTTCTCAGAACCACCCGCTC
GGCATGGCTATCTTCCTGAAGAACGTGACATTCCACGGGGTCCTACTGGATGCGTTCTTC
AACGAGAGCAGTGCTGACTGGCGGGAGGTGTGGGCGCTTGTGCAGGCCGGCATCCGGGAT
GGGGTGGTACGGCCCCTCAAGTGCACGGTGTTCCATGGGGCCCAGGTGGAGGACGCCTTC
CGCTACATGGCCCAAGGGAAGCACATTGGCAAAGTCGTCGTGCAGGTGCTTGCGGAGGAG
CCGGAGGCAGTGCTGAAGGGGGCCAAACCCAAGCTGATGTCGGCCATCTCCAAGACCTTC
TGCCCGGCCCACAAGAGCTACATCATCGCTGGTGGTCTGGGTGGCTTCGGCCTGGAGTTG
GCGCAGTGGCTGATACAGCGTGGGGTGCAGAAGCTCGTGTTGACTTCTCGCTCCGGGATC
CGGACAGGCTACCAGGCCAAGCAGGTCCGCCGGTGGAGGCGCCAGGGCGTACAGGTGCAG
GTGTCCACCAGCAACATCAGCTCACTGGAGGGGGCCCGGGGCCTCATTGCCGAGGCGGCG
CAGCTTGGGCCCGTGGGCGGCGTCTTCAACCTGGCCGTGGTCTTGAGAGATGGCTTGCTG
GAGAACCAGACCCCAGAGTTCTTCCAGGACGTCTGCAAGCCCAAGTACAGCGGCACCCTG
AACCTGGACAGGGTGACCCGAGAGGCGTGCCCTGAGCTGGACTACTTTGTGGTCTTCTCC
TCTGTGAGCTGCGGGCGTGGCAATGCGGGACAGAGCAACTACGGCTTTGCCAATTCCGCC
ATGGAGCGTATCTGTGAGAAACGCCGGCACGAAGGCCTCCCAGGCCTGGCCGTGCAGTGG
GGCGCCATCGGCGACGTGGGCATTTTGGTGGAGACGATGAGCACCAACGACACGATCGTC
AGTGGCACGCTGCCCCAGCGCATGGCGTCCTGCCTGGAGGTGCTGGACCTCTTCCTGAAC
CAGCCCCACATGGTCCTGAGCAGCTTTGTGCTGGCTGAGAAGGCTGCGGCCTATAGGGAC
AGGGACAGCCAGCGGGACCTGGTGGAGGCCGTGGCACACATCCTGGGCATCCGCGACTTG
GCTGCTGTCAACCTGGACAGCTCACTGGCGGACCTGGGCCTGGACTCGCTCATGAGCGTG
GAGGTGCGCCAGACGCTGGAGCGTGAGCTCAACCTGGTGCTGTCCGTGCGCGAGGTGCGG
CAACTCACGCTCCGGAAACTGCAGGAGCTGTCCTCAAAGGCGGATGAGGCCAGCGAGCTG
GCATGCCCCACGCCCAAGGAGGATGGTCTGGCCCAGCAGCAGACTCAGCTGAACCTGCGC
TCCCTGCTGGTGAACCCGGAGGGCCCCACCCTGATGCGGCTCAACTCCGTGCAGAGCTCG
GAGCGGCCCCTGTTCCTGGTGCACCCAATCGAGGGCTCCACCACCGTGTTCCACAGCCTG
GCCTCCCGGCTCAGCATCCCCACCTATGGCCTGCAGTGCACCCGAGCTGCGCCCCTTGAC
AGCATCCACAGCCTGGCTGCCTACTACATCGACTGCATCAGGCAGGTGCAGCCCGAGGGC
CCCTACCGCGTGGCCGGCTACTCCTACGGGGCCTGCGTGGCCTTTGAAATGTGCTCCCAG
CTGCAGGCCCAGCAGAGCCCAGCCCCCACCCACAACAGCCTCTTCCTGTTCGACGGCTCG
CCCACCTACGTACTGGCCTACACCCAGAGCTACCGGGCAAAGCTGACCCCAGGCTGTGAG
GCTGAGGCTGAGACGGAGGCCATATGCTTCTTCGTGCAGCAGTTCACGGACATGGAGCAC
AACAGGGTGCTGGAGGCGCTGCTGCCGCTGAAGGGCCTAGAGGAGCGTGTGGCAGCCGCC
GTGGACCTGATCATCAAGAGCCACCAGGGCCTGGACCGCCAGGAGCTGAGCTTTGCGGCC
CGGTCCTTCTACTACAAGCTGCGTGCCGCTGAGCAGTACACACCCAAGGCCAAGTACCAT
GGCAACGTGATGCTACTGCGCGCCAAGACGGGTGGCGCCTACGGCGAGGACCTGGGCGCG
GACTACAACCTCTCCCAGGTATGCGACGGGAAAGTATCCGTCCACGTCATCGAGGGTGAC
CACCGCACGCTGCTGGAGGGCAGCGGCCTGGAGTCCATCATCAGCATCATCCACAGCTCC
CTGGCTGAGCCACGCGTGAGCGTGCGGGAGGGCTAG
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| Enzyme 1 GenBank Gene ID |
NM_004104.4  |
| Enzyme 1 GeneCard ID |
FASN  |
| Enzyme 1 GenAtlas ID |
FASN  |
| Enzyme 1 HGNC ID |
HGNC:3594  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
17q25 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Jayakumar A, Tai MH, Huang WY, al-Feel W, Hsu M, Abu-Elheiga L, Chirala SS, Wakil SJ: Human fatty acid synthase: properties and molecular cloning. Proc Natl Acad Sci U S A. 1995 Sep 12;92(19):8695-9. [PubMed
]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Kuhajda FP, Jenner K, Wood FD, Hennigar RA, Jacobs LB, Dick JD, Pasternack GR: Fatty acid synthesis: a potential selective target for antineoplastic therapy. Proc Natl Acad Sci U S A. 1994 Jul 5;91(14):6379-83. [PubMed
]
- Semenkovich CF, Coleman T, Fiedorek FT Jr: Human fatty acid synthase mRNA: tissue distribution, genetic mapping, and kinetics of decay after glucose deprivation. J Lipid Res. 1995 Jul;36(7):1507-21. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Chi A, Valencia JC, Hu ZZ, Watabe H, Yamaguchi H, Mangini NJ, Huang H, Canfield VA, Cheng KC, Yang F, Abe R, Yamagishi S, Shabanowitz J, Hearing VJ, Wu C, Appella E, Hunt DF: Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes. J Proteome Res. 2006 Nov;5(11):3135-44. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Brink J, Ludtke SJ, Yang CY, Gu ZW, Wakil SJ, Chiu W: Quaternary structure of human fatty acid synthase by electron cryomicroscopy. Proc Natl Acad Sci U S A. 2002 Jan 8;99(1):138-43. Epub 2001 Dec 26. [PubMed
]
- Chakravarty B, Gu Z, Chirala SS, Wakil SJ, Quiocho FA: Human fatty acid synthase: structure and substrate selectivity of the thioesterase domain. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15567-72. Epub 2004 Oct 26. [PubMed
]
- Bunkoczi G, Pasta S, Joshi A, Wu X, Kavanagh KL, Smith S, Oppermann U: Mechanism and substrate recognition of human holo ACP synthase. Chem Biol. 2007 Nov;14(11):1243-53. [PubMed
]
- Pemble CW 4th, Johnson LC, Kridel SJ, Lowther WT: Crystal structure of the thioesterase domain of human fatty acid synthase inhibited by Orlistat. Nat Struct Mol Biol. 2007 Aug;14(8):704-9. Epub 2007 Jul 8. [PubMed
]
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| Enzyme 1 Metabolite References |
Not Available |
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Enzyme 2
[top]
|
| Enzyme 2 ID |
5287 |
| Enzyme 2 Name |
Calcium-dependent phospholipase A2 |
| Enzyme 2 Synonyms |
- Group V phospholipase A2
- PLA2-10
- Phosphatidylcholine 2-acylhydrolase 5
|
| Enzyme 2 Gene Name |
PLA2G5 |
| Enzyme 2 Protein Sequence |
>Calcium-dependent phospholipase A2
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
|
| Enzyme 2 Number of Residues |
138 |
| Enzyme 2 Molecular Weight |
15674.1 |
| Enzyme 2 Theoretical pI |
8.48 |
| Enzyme 2 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in phospholipase A2 activity |
| Enzyme 2 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. This isozyme hydrolyzes more efficiently L-alpha-1-palmitoyl-2-oleoyl phosphatidylcholine than L-alpha-1-palmitoyl-2-arachidonyl phosphatidylcholine, L- alpha-1-palmitoyl-2-arachidonyl phosphatidylethanolamine, or L- alpha-1-stearoyl-2-arachidonyl phosphatidylinositol. May be involved in the production of lung surfactant, the remodeling or regulation of cardiac muscle |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
10862735  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P39877  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PA2G5_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>417 bp
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
|
| Enzyme 2 GenBank Gene ID |
AL158172  |
| Enzyme 2 GeneCard ID |
PLA2G5  |
| Enzyme 2 GenAtlas ID |
PLA2G5  |
| Enzyme 2 HGNC ID |
HGNC:9038  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p36-p34 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Chen J, Engle SJ, Seilhamer JJ, Tischfield JA: Cloning and recombinant expression of a novel human low molecular weight Ca(2+)-dependent phospholipase A2. J Biol Chem. 1994 Jan 28;269(4):2365-8. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5288 |
| Enzyme 3 Name |
Group IIF secretory phospholipase A2 |
| Enzyme 3 Synonyms |
- GIIF sPLA2
- sPLA2-IIF
- Phosphatidylcholine 2-acylhydrolase 2F
|
| Enzyme 3 Gene Name |
PLA2G2F |
| Enzyme 3 Protein Sequence |
>Group IIF secretory phospholipase A2
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
|
| Enzyme 3 Number of Residues |
168 |
| Enzyme 3 Molecular Weight |
18658.0 |
| Enzyme 3 Theoretical pI |
4.94 |
| Enzyme 3 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in phospholipase A2 activity |
| Enzyme 3 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference |
| Enzyme 3 Pathways |
|
| Enzyme 3 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
12276060  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
Q9BZM2  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PA2GF_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>507 bp
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
|
| Enzyme 3 GenBank Gene ID |
AF306566  |
| Enzyme 3 GeneCard ID |
PLA2G2F  |
| Enzyme 3 GenAtlas ID |
PLA2G2F  |
| Enzyme 3 HGNC ID |
HGNC:30040  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1p35 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Valentin E, Singer AG, Ghomashchi F, Lazdunski M, Gelb MH, Lambeau G: Cloning and recombinant expression of human group IIF-secreted phospholipase A(2). Biochem Biophys Res Commun. 2000 Dec 9;279(1):223-8. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5289 |
| Enzyme 4 Name |
Cytosolic phospholipase A2 |
| Enzyme 4 Synonyms |
- cPLA2
- Phospholipase A2 group IVA
- Phospholipase A2
- Phosphatidylcholine 2-acylhydrolase
- Lysophospholipase
|
| Enzyme 4 Gene Name |
PLA2G4A |
| Enzyme 4 Protein Sequence |
>Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
|
| Enzyme 4 Number of Residues |
749 |
| Enzyme 4 Molecular Weight |
85210.2 |
| Enzyme 4 Theoretical pI |
5.03 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- phospholipase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in metabolic process |
| Enzyme 4 Specific Function |
Selectively hydrolyzes arachidonyl phospholipids in the sn-2 position releasing arachidonic acid. Together with its lysophospholipid activity, it is implicated in the initiation of the inflammatory response |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P47712  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PA24A_HUMAN  |
| Enzyme 4 PDB ID |
1CJY  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>2250 bp
ATGTCATTTATAGATCCTTACCAGCACATTATAGTGGAGCACCAGTATTCCCACAAGTTT
ACGGTAGTGGTGTTACGTGCCACCAAAGTGACAAAGGGGGCCTTTGGTGACATGCTTGAT
ACTCCAGATCCCTATGTGGAACTTTTTATCTCTACAACCCCTGACAGCAGGAAGAGAACA
AGACATTTCAATAATGACATAAACCCTGTGTGGAATGAGACCTTTGAATTTATTTTGGAT
CCTAATCAGGAAAATGTTTTGGAGATTACGTTAATGGATGCCAATTATGTCATGGATGAA
ACTCTAGGGACAGCAACATTTACTGTATCTTCTATGAAGGTGGGAGAAAAGAAAGAAGTT
CCTTTTATTTTCAACCAAGTCACTGAAATGGTTCTAGAAATGTCTCTTGAAGTTTGCTCA
TGCCCAGACCTACGATTTAGTATGGCTCTGTGTGATCAGGAGAAGACTTTCAGACAACAG
AGAAAAGAACACATAAGGGAGAGCATGAAGAAACTCTTGGGTCCAAAGAATAGTGAAGGA
TTGCATTCTGCACGTGATGTGCCTGTGGTAGCCATATTGGGTTCAGGTGGGGGTTTCCGA
GCCATGGTGGGATTCTCTGGTGTGATGAAGGCATTATACGAATCAGGAATTCTGGATTGT
GCTACCTACGTTGCTGGTCTTTCTGGCTCCACCTGGTATATGTCAACCTTGTATTCTCAC
CCTGATTTTCCAGAGAAAGGGCCAGAGGAGATTAATGAAGAACTAATGAAAAATGTTAGC
CACAATCCCCTTTTACTTCTCACACCACAGAAAGTTAAAAGATATGTTGAGTCTTTATGG
AAGAAGAAAAGCTCTGGACAACCTGTCACCTTTACTGATATCTTTGGGATGTTAATAGGA
GAAACACTAATTCATAATAGAATGAATACTACTCTGAGCAGTTTGAAGGAAAAAGTTAAT
ACTGCACAATGCCCTTTACCTCTTTTCACCTGTCTTCATGTCAAACCTGACGTTTCAGAG
CTGATGTTTGCAGATTGGGTTGAATTTAGTCCATACGAAATTGGCATGGCTAAATATGGT
ACTTTTATGGCTCCCGACTTATTTGGAAGCAAATTTTTTATGGGAACAGTCGTTAAGAAG
TATGAAGAAAACCCCTTGCATTTCTTAATGGGTGTCTGGGGCAGTGCCTTTTCCATATTG
TTCAACAGAGTTTTGGGCGTTTCTGGTTCACAAAGCAGAGGCTCCACAATGGAGGAAGAA
TTAGAAAATATTACCACAAAGCATATTGTGAGTAATGATAGCTCGGACAGTGATGATGAA
TCACACGAACCCAAAGGCACTGAAAATGAAGATGCTGGAAGTGACTATCAAAGTGATAAT
CAAGCAAGTTGGATTCATCGTATGATAATGGCCTTGGTGAGTGATTCAGCTTTATTCAAT
ACCAGAGAAGGACGTGCTGGGAAGGTACACAACTTCATGCTGGGCTTGAATCTCAATACA
TCTTATCCACTGTCTCCTTTGAGTGACTTTGCCACACAGGACTCCTTTGATGATGATGAA
CTGGATGCAGCTGTAGCAGATCCTGATGAATTTGAGCGAATATATGAGCCTCTGGATGTC
AAAAGTAAAAAGATTCATGTAGTGGACAGTGGGCTCACATTTAACCTGCCGTATCCCTTG
ATACTGAGACCTCAGAGAGGGGTTGATCTCATAATCTCCTTTGACTTTTCTGCAAGGCCA
AGTGACTCTAGTCCTCCGTTCAAGGAACTTCTACTTGCAGAAAAGTGGGCTAAAATGAAC
AAGCTCCCCTTTCCAAAGATTGATCCTTATGTGTTTGATCGGGAAGGGCTGAAGGAGTGC
TATGTCTTTAAACCCAAGAATCCTGATATGGAGAAAGATTGCCCAACCATCATCCACTTT
GTTCTGGCCAACATCAACTTCAGAAAGTACAAGGCTCCAGGTGTTCCAAGGGAAACTGAG
GAAGAGAAAGAAATCGCTGACTTTGATATTTTTGATGACCCAGAATCACCATTTTCAACC
TTCAATTTTCAATATCCAAATCAAGCATTCAAAAGACTACATGATCTTATGCACTTCAAT
ACTCTGAACAACATTGATGTGATAAAAGAAGCCATGGTTGAAAGCATTGAATATAGAAGA
CAGAATCCATCTCGTTGCTCTGTTTCCCTTAGTAATGTTGAGGCAAGAAGATTTTTCAAC
AAGGAGTTTCTAAGTAAACCCAAAGCATAG
|
| Enzyme 4 GenBank Gene ID |
M72393  |
| Enzyme 4 GeneCard ID |
PLA2G4A  |
| Enzyme 4 GenAtlas ID |
PLA2G4A  |
| Enzyme 4 HGNC ID |
HGNC:9035  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
1q25 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Clark JD, Lin LL, Kriz RW, Ramesha CS, Sultzman LA, Lin AY, Milona N, Knopf JL: A novel arachidonic acid-selective cytosolic PLA2 contains a Ca(2+)-dependent translocation domain with homology to PKC and GAP. Cell. 1991 Jun 14;65(6):1043-51. [PubMed
]
- Sharp JD, White DL, Chiou XG, Goodson T, Gamboa GC, McClure D, Burgett S, Hoskins J, Skatrud PL, Sportsman JR, et al.: Molecular cloning and expression of human Ca(2+)-sensitive cytosolic phospholipase A2. J Biol Chem. 1991 Aug 15;266(23):14850-3. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lin LL, Wartmann M, Lin AY, Knopf JL, Seth A, Davis RJ: cPLA2 is phosphorylated and activated by MAP kinase. Cell. 1993 Jan 29;72(2):269-78. [PubMed
]
- Sharp JD, Pickard RT, Chiou XG, Manetta JV, Kovacevic S, Miller JR, Varshavsky AD, Roberts EF, Strifler BA, Brems DN, et al.: Serine 228 is essential for catalytic activities of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1994 Sep 16;269(37):23250-4. [PubMed
]
- Borsch-Haubold AG, Bartoli F, Asselin J, Dudler T, Kramer RM, Apitz-Castro R, Watson SP, Gelb MH: Identification of the phosphorylation sites of cytosolic phospholipase A2 in agonist-stimulated human platelets and HeLa cells. J Biol Chem. 1998 Feb 20;273(8):4449-58. [PubMed
]
- Sheridan AM, Force T, Yoon HJ, O'Leary E, Choukroun G, Taheri MR, Bonventre JV: PLIP, a novel splice variant of Tip60, interacts with group IV cytosolic phospholipase A(2), induces apoptosis, and potentiates prostaglandin production. Mol Cell Biol. 2001 Jul;21(14):4470-81. [PubMed
]
- Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Perisic O, Fong S, Lynch DE, Bycroft M, Williams RL: Crystal structure of a calcium-phospholipid binding domain from cytosolic phospholipase A2. J Biol Chem. 1998 Jan 16;273(3):1596-604. [PubMed
]
- Xu GY, McDonagh T, Yu HA, Nalefski EA, Clark JD, Cumming DA: Solution structure and membrane interactions of the C2 domain of cytosolic phospholipase A2. J Mol Biol. 1998 Jul 17;280(3):485-500. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5290 |
| Enzyme 5 Name |
Phospholipase A2 |
| Enzyme 5 Synonyms |
- Group IB phospholipase A2
- Phosphatidylcholine 2-acylhydrolase 1B
|
| Enzyme 5 Gene Name |
PLA2G1B |
| Enzyme 5 Protein Sequence |
>Phospholipase A2
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
|
| Enzyme 5 Number of Residues |
148 |
| Enzyme 5 Molecular Weight |
16359.5 |
| Enzyme 5 Theoretical pI |
7.91 |
| Enzyme 5 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in phospholipase A2 activity |
| Enzyme 5 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides |
| Enzyme 5 Pathways |
|
| Enzyme 5 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
P04054  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PA21B_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>447 bp
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTATGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
|
| Enzyme 5 GenBank Gene ID |
M21054  |
| Enzyme 5 GeneCard ID |
PLA2G1B  |
| Enzyme 5 GenAtlas ID |
PLA2G1B  |
| Enzyme 5 HGNC ID |
HGNC:9030  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
12q23-q24.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Seilhamer JJ, Randall TL, Yamanaka M, Johnson LK: Pancreatic phospholipase A2: isolation of the human gene and cDNAs from porcine pancreas and human lung. DNA. 1986 Dec;5(6):519-27. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Scherer SE, Muzny DM, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Montgomery KT, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Lovering RC, Wheeler DA, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clerc-Blankenburg KP, Davis C, Delgado O, Dinh HH, Draper H, Gonzalez-Garay ML, Havlak P, Jackson LR, Jacob LS, Kelly SH, Li L, Li Z, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Pasternak S, Perez LM, Plopper FJ, Santibanez J, Shen H, Tabor PE, Verduzco D, Waldron L, Wang Q, Williams GA, Zhang J, Zhou J, Allen CC, Amin AG, Anyalebechi V, Bailey M, Barbaria JA, Bimage KE, Bryant NP, Burch PE, Burkett CE, Burrell KL, Calderon E, Cardenas V, Carter K, Casias K, Cavazos I, Cavazos SR, Ceasar H, Chacko J, Chan SN, Chavez D, Christopoulos C, Chu J, Cockrell R, Cox CD, Dang M, Dathorne SR, David R, Davis CM, Davy-Carroll L, Deshazo DR, Donlin JE, D'Souza L, Eaves KA, Egan A, Emery-Cohen AJ, Escotto M, Flagg N, Forbes LD, Gabisi AM, Garza M, Hamilton C, Henderson N, Hernandez O, Hines S, Hogues ME, Huang M, Idlebird DG, Johnson R, Jolivet A, Jones S, Kagan R, King LM, Leal B, Lebow H, Lee S, LeVan JM, Lewis LC, London P, Lorensuhewa LM, Loulseged H, Lovett DA, Lucier A, Lucier RL, Ma J, Madu RC, Mapua P, Martindale AD, Martinez E, Massey E, Mawhiney S, Meador MG, Mendez S, Mercado C, Mercado IC, Merritt CE, Miner ZL, Minja E, Mitchell T, Mohabbat F, Mohabbat K, Montgomery B, Moore N, Morris S, Munidasa M, Ngo RN, Nguyen NB, Nickerson E, Nwaokelemeh OO, Nwokenkwo S, Obregon M, Oguh M, Oragunye N, Oviedo RJ, Parish BJ, Parker DN, Parrish J, Parks KL, Paul HA, Payton BA, Perez A, Perrin W, Pickens A, Primus EL, Pu LL, Puazo M, Quiles MM, Quiroz JB, Rabata D, Reeves K, Ruiz SJ, Shao H, Sisson I, Sonaike T, Sorelle RP, Sutton AE, Svatek AF, Svetz LA, Tamerisa KS, Taylor TR, Teague B, Thomas N, Thorn RD, Trejos ZY, Trevino BK, Ukegbu ON, Urban JB, Vasquez LI, Vera VA, Villasana DM, Wang L, Ward-Moore S, Warren JT, Wei X, White F, Williamson AL, Wleczyk R, Wooden HS, Wooden SH, Yen J, Yoon L, Yoon V, Zorrilla SE, Nelson D, Kucherlapati R, Weinstock G, Gibbs RA: The finished DNA sequence of human chromosome 12. Nature. 2006 Mar 16;440(7082):346-51. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Grataroli R, Dijkman R, Dutilh CE, van der Ouderaa F, De Haas GH, Figarella C: Studies on prophospholipase A2 and its enzyme from human pancreatic juice. Catalytic properties and sequence of the N-terminal region. Eur J Biochem. 1982 Feb;122(1):111-7. [PubMed
]
- Verheij HM, Westerman J, Sternby B, De Haas GH: The complete primary structure of phospholipase A2 from human pancreas. Biochim Biophys Acta. 1983 Sep 14;747(1-2):93-9. [PubMed
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
5292 |
| Enzyme 6 Name |
Group 10 secretory phospholipase A2 |
| Enzyme 6 Synonyms |
- Group X secretory phospholipase A2
- GX sPLA2
- sPLA2-X
- Phosphatidylcholine 2-acylhydrolase 10
|
| Enzyme 6 Gene Name |
PLA2G10 |
| Enzyme 6 Protein Sequence |
>Group 10 secretory phospholipase A2
MGPLPVCLPIMLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPI
AYMKYGCFCGLGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGP
AENKCQELLCKCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
|
| Enzyme 6 Number of Residues |
165 |
| Enzyme 6 Molecular Weight |
18153.0 |
| Enzyme 6 Theoretical pI |
6.46 |
| Enzyme 6 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in phospholipase A2 activity |
| Enzyme 6 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine |
| Enzyme 6 Pathways |
|
| Enzyme 6 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
O15496  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
PA2GX_HUMAN  |
| Enzyme 6 PDB ID |
1LE7  |
| Enzyme 6 PDB File |
Show |
| Enzyme 6 3D Structure |
|
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>498 bp
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
|
| Enzyme 6 GenBank Gene ID |
U95301  |
| Enzyme 6 GeneCard ID |
PLA2G10  |
| Enzyme 6 GenAtlas ID |
PLA2G10  |
| Enzyme 6 HGNC ID |
HGNC:9029  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
16p13.1-p12 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Cupillard L, Koumanov K, Mattei MG, Lazdunski M, Lambeau G: Cloning, chromosomal mapping, and expression of a novel human secretory phospholipase A2. J Biol Chem. 1997 Jun 20;272(25):15745-52. [PubMed
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5293 |
| Enzyme 7 Name |
Galactoside-binding soluble lectin 13 |
| Enzyme 7 Synonyms |
- Galectin-13
- Gal-13
- Placental tissue protein 13
- PP13
- Placental protein 13
|
| Enzyme 7 Gene Name |
LGALS13 |
| Enzyme 7 Protein Sequence |
>Galactoside-binding soluble lectin 13
MSSLPVPYKLPVSLSVGSCVIIKGTPIHSFINDPQLQVDFYTDMDEDSDIAFRFRVHFGN
HVVMNRREFGIWMLEETTDYVPFEDGKQFELCIYVHYNEYEIKVNGIRIYGFVHRIPPSF
VKMVQVSRDISLTSVCVCN
|
| Enzyme 7 Number of Residues |
139 |
| Enzyme 7 Molecular Weight |
16118.4 |
| Enzyme 7 Theoretical pI |
5.53 |
| Enzyme 7 GO Classification |
| Function |
- binding
- carbohydrate binding
- sugar binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in sugar binding |
| Enzyme 7 Specific Function |
Has lysophospholipase activity |
| Enzyme 7 Pathways |
|
| Enzyme 7 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
6650760  |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9UHV8  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PP13_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>420 bp
ATGTCTTCTTTACCCGTGCCATACAAACTGCCTGTGTCTTTGTCTGTTGGTTCCTGCGTG
ATAATCAAAGGGACACCAATCCACTCTTTTATCAATGACCCACAGCTGCAGGTGGATTTC
TACACTGACATGGATGAGGATTCAGATATTGCCTTCCGTTTCCGAGTGCACTTTGGCAAT
CATGTGGTCATGAACAGGCGTGAGTTTGGGATATGGATGTTGGAGGAGACAACAGACTAC
GTGCCCTTTGAGGATGGCAAACAATTTGAGCTGTGCATCTACGTACATTACAATGAGTAT
GAGATAAAGGTCAATGGCATACGCATTTACGGCTTTGTCCATCGAATCCCGCCATCATTT
GTGAAGATGGTGCAAGTGTCGAGAGATATCTCCCTGACCTCAGTGTGTGTCTGCAATTGA
|
| Enzyme 7 GenBank Gene ID |
AF117383  |
| Enzyme 7 GeneCard ID |
LGALS13  |
| Enzyme 7 GenAtlas ID |
LGALS13  |
| Enzyme 7 HGNC ID |
HGNC:15449  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
19q13.1 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 General References |
- Than NG, Sumegi B, Than GN, Berente Z, Bohn H: Isolation and sequence analysis of a cDNA encoding human placental tissue protein 13 (PP13), a new lysophospholipase, homologue of human eosinophil Charcot-Leyden Crystal protein. Placenta. 1999 Nov;20(8):703-10. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bohn H, Kraus W, Winckler W: Purification and characterization of two new soluble placental tissue proteins (PP13 and PP17). Oncodev Biol Med. 1983;4(5):343-50. [PubMed
]
- Visegrady B, Than NG, Kilar F, Sumegi B, Than GN, Bohn H: Homology modelling and molecular dynamics studies of human placental tissue protein 13 (galectin-13). Protein Eng. 2001 Nov;14(11):875-80. [PubMed
]
|
| Enzyme 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5294 |
| Enzyme 8 Name |
Group IIE secretory phospholipase A2 |
| Enzyme 8 Synonyms |
- GIIE sPLA2
- sPLA2-IIE
- Phosphatidylcholine 2-acylhydrolase 2E
|
| Enzyme 8 Gene Name |
PLA2G2E |
| Enzyme 8 Protein Sequence |
>Group IIE secretory phospholipase A2
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
|
| Enzyme 8 Number of Residues |
142 |
| Enzyme 8 Molecular Weight |
15988.5 |
| Enzyme 8 Theoretical pI |
8.28 |
| Enzyme 8 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in phospholipase A2 activity |
| Enzyme 8 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Has a preference for arachidonic-containing phospholipids |
| Enzyme 8 Pathways |
|
| Enzyme 8 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
Not Available |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
Q9NZK7  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PA2GE_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>429 bp
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
|
| Enzyme 8 GenBank Gene ID |
AF189279  |
| Enzyme 8 GeneCard ID |
PLA2G2E  |
| Enzyme 8 GenAtlas ID |
PLA2G2E  |
| Enzyme 8 HGNC ID |
HGNC:13414  |
| Enzyme 8 Chromosome Location |
1 |
| Enzyme 8 Locus |
1p36.13 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 General References |
- Suzuki N, Ishizaki J, Yokota Y, Higashino K, Ono T, Ikeda M, Fujii N, Kawamoto K, Hanasaki K: Structures, enzymatic properties, and expression of novel human and mouse secretory phospholipase A(2)s. J Biol Chem. 2000 Feb 25;275(8):5785-93. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
|
| Enzyme 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5296 |
| Enzyme 9 Name |
Group XIIA secretory phospholipase A2 |
| Enzyme 9 Synonyms |
- GXII sPLA2
- sPLA2-XII
- Phosphatidylcholine 2-acylhydrolase 12A
|
| Enzyme 9 Gene Name |
PLA2G12A |
| Enzyme 9 Protein Sequence |
>Group XIIA secretory phospholipase A2
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
|
| Enzyme 9 Number of Residues |
189 |
| Enzyme 9 Molecular Weight |
21067.0 |
| Enzyme 9 Theoretical pI |
7.27 |
| Enzyme 9 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
|
|
| Enzyme 9 General Function |
Involved in phospholipase A2 activity |
| Enzyme 9 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Does not exhibit detectable activity toward sn-2-arachidonoyl- or linoleoyl- phosphatidylcholine or -phosphatidylethanolamine |
| Enzyme 9 Pathways |
|
| Enzyme 9 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
12276062  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q9BZM1  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PG12A_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>570 bp
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTGGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
|
| Enzyme 9 GenBank Gene ID |
AF306567  |
| Enzyme 9 GeneCard ID |
PLA2G12A  |
| Enzyme 9 GenAtlas ID |
PLA2G12A  |
| Enzyme 9 HGNC ID |
HGNC:18554  |
| Enzyme 9 Chromosome Location |
4 |
| Enzyme 9 Locus |
4q25 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Gelb MH, Valentin E, Ghomashchi F, Lazdunski M, Lambeau G: Cloning and recombinant expression of a structurally novel human secreted phospholipase A2. J Biol Chem. 2000 Dec 22;275(51):39823-6. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Murakami M, Masuda S, Shimbara S, Bezzine S, Lazdunski M, Lambeau G, Gelb MH, Matsukura S, Kokubu F, Adachi M, Kudo I: Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII). J Biol Chem. 2003 Mar 21;278(12):10657-67. Epub 2003 Jan 8. [PubMed
]
|
| Enzyme 9 Metabolite References |
Not Available |
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5297 |
| Enzyme 10 Name |
85 kDa calcium-independent phospholipase A2 |
| Enzyme 10 Synonyms |
- CaI-PLA2
- iPLA2
- Group VI phospholipase A2
- GVI PLA2
|
| Enzyme 10 Gene Name |
PLA2G6 |
| Enzyme 10 Protein Sequence |
>85 kDa calcium-independent phospholipase A2
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHG
VPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHL
LCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGM
YFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFR
NYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNP
TLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKT
VFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVN
ALWETEVYIYEHREEFQKLIQLLLSP
|
| Enzyme 10 Number of Residues |
806 |
| Enzyme 10 Molecular Weight |
89902.3 |
| Enzyme 10 Theoretical pI |
7.28 |
| Enzyme 10 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in metabolic process |
| Enzyme 10 Specific Function |
Isoform ankyrin-iPLA2-1 and isoform ankyrin-iPLA2-2, which lack the catalytic domain, are probably involved in the negative regulation of iPLA2 activity |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
3142700  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
O60733  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PA2G6_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>2421 bp
ATGCAGTTCTTTGGCCGCCTGGTCAATACCTTCAGTGGCGTCACCAACTTGTTCTCTAAC
CCATTCCGGGTGAAGGAGGTGGCTGTGGCCGACTACACCTCGAGTGACCGAGTTCGGGAG
GAAGGGCAGCTGATTCTGTTCCAGAACACTCCCAACCGCACCTGGGACTGCGTCCTGGTC
AACCCCAGGAACTCACAGAGTGGATTCCGACTCTTCCAGCTGGAGTTGGAGGCTGACGCC
CTAGTGAATTTCCATCAGTATTCTTCCCAGCTGCTACCCTTCTATGAGAGCTCCCCTCAG
GTCCTGCACACTGAGGTCCTGCAGCACCTGACCGACCTCATCCGTAACCACCCCAGCTGG
TCAGTGGCCCACCTGGCTGTGGAGCTAGGGATCCGCGAGTGCTTCCATCACAGCCGTATC
ATCAGCTGTGCCAATTGCGCGGAGAACGAGGAGGGCTGCACACCCCTGCACCTGGCCTGC
CGCAAGGGTGATGGGGAGATCCTGGTGGAGCTGGTGCAGTACTGCCACACTCAGATGGAT
GTCACCGACTACAAGGGAGAGACCGTCTTCCATTATGCTGTCCAGGGTGACAATTCTCAG
GTGCTGCAGCTCCTTGGAAGGAACGCAGTGGCTGGCCTGAACCAGGTGAATAACCAAGGG
CTGACCCCGCTGCACCTGGCCTGCCAGCTGGGGAAGCAGGAGATGGTCCGCGTGCTGCTG
CTGTGCAATGCTCGGTGCAACATCATGGGCCCCAACGGCTACCCCATCCACTCGGCCATG
AAGTTCTCTCAGAAGGGGTGTGCGGAGATGATCATCAGCATGGACAGCAGCCAGATCCAC
AGCAAAGACCCCCGTTACGGAGCCAGCCCCCTCCACTGGGCCAAGAACGCAGAGATGGCC
CGCATGCTGCTGAAACGGGGCTGCAACGTGAACAGCACCAGCTCCGCGGGGAACACGGCC
CTGCACGTGGCGGTGATGCGCAACCGCTTCGACTGTGCCATAGTGCTGCTGACCCACGGG
GCCAACGCGGATGCCCGCGGAGAGCACGGCAACACCCCGCTGCACCTGGCCATGTCGAAA
GACAACGTGGAGATGATCAAGGCCCTCATCGTGTTCGGAGCAGAAGTGGACACCCCGAAT
GACTTTGGGGAGACTCCTACATTCCTAGCCTCCAAAATCGGCAGACTTGTCACCAGGAAG
GCGATCTTGACTCTGCTGAGAACCGTGGGGGCCGAATACTGCTTCCCACCCATCCACGGG
GTCCCCGCGGAGCAGGGCTCTGCAGCGCCACATCATCCCTTCTCCCTGGAAAGAGCTCAG
CCCCCACCGATCAGCCTAAACAACCTAGAACTACAGGATCTCATGCACATCTCACGGGCC
CGGAAGCCAGCGTTCATCCTGGGCTCCATGAGGGACGAGAAGCGGACCCACGACCACCTG
CTGTGCCTGGATGGAGGAGGAGTGAAAGGCCTCATCATCATCCAGCTCCTCATCGCCATC
GAGAAGGCCTCGGGTGTGGCCACCAAGGACCTGTTTGACTGGGTGGCGGGCACCAGCACT
GGAGGCATCCTGGCCCTGGCCATTCTGCACAGTAAGTCCATGGCCTACATGCGCGGCATG
TACTTTCGCATGAAGGATGAGGTGTTCCGGGGCTCCAGGCCCTACGAGTCGGGGCCCCTG
GAGGAGTTCCTGAAGCGGGAGTTTGGGGAGCACACCAAGATGACGGACGTCAGGAAACCC
AAGGTGATGCTGACAGGGACACTGTCTGACCGGCAGCCGGCTGAACTCCACCTCTTCCGG
AACTACGATGCTCCAGAAACTGTCCGGGAGCCTCGTTTCAACCAGAACGTTAACCTCAGG
CCTCCAGCTCAGCCCTCAGACCAGCTGGTGTGGCGGGCGGCCCGAAGCAGCGGGGCAGCT
CCTACTTACTTCCGACCCAATGGGCGCTTCCTGGACGGTGGGCTGCTGGCCAACAACCCC
ACGCTGGATGCCATGACCGAGATCCATGAGTACAATCAGGACCTGATCCGCAAGGGTCAG
GCCAACAAGGTGAAGAAACTCTCCATCGTTGTCTCCCTGGGGACAGGGAGGTCCCCACAA
GTGCCTGTGACCTGTGTGGATGTCTTCCGTCCCAGCAACCCCTGGGAGCTGGCCAAGACT
GTTTTTGGGGCCAAGGAACTGGGCAAGATGGTGGTGGACTGTTGCACGGATCCAGACGGG
CGGGCTGTGGACCGGGCACGGGCCTGGTGCGAGATGGTCGGCATCCAGTACTTCAGATTG
AACCCCCAGCTGGGGACGGACATCATGCTGGATGAGGTCAGTGACACAGTGCTGGTCAAC
GCCCTCTGGGAGACCGAGGTCTACATCTATGAGCACCGCGAGGAGTTCCAGAAGCTCATC
CACCTGCTGCTCTCACCCTGA
|
| Enzyme 10 GenBank Gene ID |
AF064594  |
| Enzyme 10 GeneCard ID |
PLA2G6  |
| Enzyme 10 GenAtlas ID |
PLA2G6  |
| Enzyme 10 HGNC ID |
HGNC:9039  |
| Enzyme 10 Chromosome Location |
2 |
| Enzyme 10 Locus |
22q13.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Larsson PK, Claesson HE, Kennedy BP: Multiple splice variants of the human calcium-independent phospholipase A2 and their effect on enzyme activity. J Biol Chem. 1998 Jan 2;273(1):207-14. [PubMed
]
- Ma Z, Wang X, Nowatzke W, Ramanadham S, Turk J: Human pancreatic islets express mRNA species encoding two distinct catalytically active isoforms of group VI phospholipase A2 (iPLA2) that arise from an exon-skipping mechanism of alternative splicing of the transcript from the iPLA2 gene on chromosome 22q13.1. J Biol Chem. 1999 Apr 2;274(14):9607-16. [PubMed
]
- Larsson Forsell PK, Kennedy BP, Claesson HE: The human calcium-independent phospholipase A2 gene multiple enzymes with distinct properties from a single gene. Eur J Biochem. 1999 Jun;262(2):575-85. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Malhotra A, Edelman-Novemsky I, Xu Y, Plesken H, Ma J, Schlame M, Ren M: Role of calcium-independent phospholipase A2 in the pathogenesis of Barth syndrome. Proc Natl Acad Sci U S A. 2009 Feb 17;106(7):2337-41. Epub 2009 Jan 21. [PubMed
]
- Khateeb S, Flusser H, Ofir R, Shelef I, Narkis G, Vardi G, Shorer Z, Levy R, Galil A, Elbedour K, Birk OS: PLA2G6 mutation underlies infantile neuroaxonal dystrophy. Am J Hum Genet. 2006 Nov;79(5):942-8. Epub 2006 Sep 19. [PubMed
]
- Morgan NV, Westaway SK, Morton JE, Gregory A, Gissen P, Sonek S, Cangul H, Coryell J, Canham N, Nardocci N, Zorzi G, Pasha S, Rodriguez D, Desguerre I, Mubaidin A, Bertini E, Trembath RC, Simonati A, Schanen C, Johnson CA, Levinson B, Woods CG, Wilmot B, Kramer P, Gitschier J, Maher ER, Hayflick SJ: PLA2G6, encoding a phospholipase A2, is mutated in neurodegenerative disorders with high brain iron. Nat Genet. 2006 Jul;38(7):752-4. Epub 2006 Jun 18. [PubMed
]
- Paisan-Ruiz C, Bhatia KP, Li A, Hernandez D, Davis M, Wood NW, Hardy J, Houlden H, Singleton A, Schneider SA: Characterization of PLA2G6 as a locus for dystonia-parkinsonism. Ann Neurol. 2009 Jan;65(1):19-23. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5299 |
| Enzyme 11 Name |
Eosinophil lysophospholipase |
| Enzyme 11 Synonyms |
- Charcot-Leyden crystal protein
- CLC
- Galectin-10
- Gal-10
- Lysolecithin acylhydrolase
|
| Enzyme 11 Gene Name |
CLC |
| Enzyme 11 Protein Sequence |
>Eosinophil lysophospholipase
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR
|
| Enzyme 11 Number of Residues |
142 |
| Enzyme 11 Molecular Weight |
16480.8 |
| Enzyme 11 Theoretical pI |
7.50 |
| Enzyme 11 GO Classification |
| Function |
- binding
- carbohydrate binding
- sugar binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in sugar binding |
| Enzyme 11 Specific Function |
May have both lysophospholipase and carbohydrate-binding activities |
| Enzyme 11 Pathways |
|
| Enzyme 11 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
3399666  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q05315  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
LPPL_HUMAN  |
| Enzyme 11 PDB ID |
1QKQ  |
| Enzyme 11 PDB File |
Show |
| Enzyme 11 3D Structure |
|
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>429 bp
ATGTCCCTGCTACCCGTGCCATACACAGAGGCTGCCTCTTTGTCTACTGGTTCTACTGTG
ACAATCAAAGGGCGACCACTTGTCTGTTTCTTGAATGAACCATATCTGCAGGTGGATTTC
CACACTGAGATGAAGGAGGAATCAGACATTGTCTTCCATTTCCAAGTGTGCTTTGGTCGT
CGTGTGGTCATGAACAGCCGTGAGTATGGGGCCTGGAAGCAGCAGGTGGAATCCAAGAAC
ATGCCCTTTCAGGATGGCCAAGAATTTGAACTGAGCATCTCAGTGCTGCCAGATAAGTAC
CAGGTAATGGTCAATGGCCAATCCTCTTACACCTTTGACCATAGAATCAAGCCTGAGGCT
GTGAAGATGGTGCAAGTGTGGAGAGATATCTCCCTGACCAAATTTAATGTCAGCTATTTA
AAGAGATAA
|
| Enzyme 11 GenBank Gene ID |
AC005393  |
| Enzyme 11 GeneCard ID |
CLC  |
| Enzyme 11 GenAtlas ID |
CLC  |
| Enzyme 11 HGNC ID |
HGNC:2014  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
19q13.1 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Ackerman SJ, Corrette SE, Rosenberg HF, Bennett JC, Mastrianni DM, Nicholson-Weller A, Weller PF, Chin DT, Tenen DG: Molecular cloning and characterization of human eosinophil Charcot-Leyden crystal protein (lysophospholipase). Similarities to IgE binding proteins and the S-type animal lectin superfamily. J Immunol. 1993 Jan 15;150(2):456-68. [PubMed
]
- Mastrianni DM, Eddy RL, Rosenberg HF, Corrette SE, Shows TB, Tenen DG, Ackerman SJ: Localization of the human eosinophil Charcot-Leyden crystal protein (lysophospholipase) gene (CLC) to chromosome 19 and the human ribonuclease 2 (eosinophil-derived neurotoxin) and ribonuclease 3 (eosinophil cationic protein) genes (RNS2 and RNS3) to chromosome 14. Genomics. 1992 May;13(1):240-2. [PubMed
]
- Dyer KD, Handen JS, Rosenberg HF: The genomic structure of the human Charcot-Leyden crystal protein gene is analogous to those of the galectin genes. Genomics. 1997 Mar 1;40(2):217-21. [PubMed
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ghafouri B, Irander K, Lindbom J, Tagesson C, Lindahl M: Comparative proteomics of nasal fluid in seasonal allergic rhinitis. J Proteome Res. 2006 Feb;5(2):330-8. [PubMed
]
- Leonidas DD, Elbert BL, Zhou Z, Leffler H, Ackerman SJ, Acharya KR: Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins. Structure. 1995 Dec 15;3(12):1379-93. [PubMed
]
- Swaminathan GJ, Leonidas DD, Savage MP, Ackerman SJ, Acharya KR: Selective recognition of mannose by the human eosinophil Charcot-Leyden crystal protein (galectin-10): a crystallographic study at 1.8 A resolution. Biochemistry. 1999 Oct 19;38(42):13837-43. [PubMed
]
|
| Enzyme 11 Metabolite References |
Not Available |
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5301 |
| Enzyme 12 Name |
Phospholipase A2, membrane associated |
| Enzyme 12 Synonyms |
- GIIC sPLA2
- Group IIA phospholipase A2
- Non-pancreatic secretory phospholipase A2
- NPS-PLA2
- Phosphatidylcholine 2-acylhydrolase 2A
|
| Enzyme 12 Gene Name |
PLA2G2A |
| Enzyme 12 Protein Sequence |
>Phospholipase A2, membrane associated
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
|
| Enzyme 12 Number of Residues |
144 |
| Enzyme 12 Molecular Weight |
16082.5 |
| Enzyme 12 Theoretical pI |
9.51 |
| Enzyme 12 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in phospholipase A2 activity |
| Enzyme 12 Specific Function |
Thought to participate in the regulation of the phospholipid metabolism in biomembranes including eicosanoid biosynthesis. Catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
Not Available |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
P14555  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PA2GA_HUMAN  |
| Enzyme 12 PDB ID |
1DB4  |
| Enzyme 12 PDB File |
Show |
| Enzyme 12 3D Structure |
|
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
|
| Enzyme 12 GenBank Gene ID |
M22430  |
| Enzyme 12 GeneCard ID |
PLA2G2A  |
| Enzyme 12 GenAtlas ID |
PLA2G2A  |
| Enzyme 12 HGNC ID |
HGNC:9031  |
| Enzyme 12 Chromosome Location |
1 |
| Enzyme 12 Locus |
1p35 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Seilhamer JJ, Pruzanski W, Vadas P, Plant S, Miller JA, Kloss J, Johnson LK: Cloning and recombinant expression of phospholipase A2 present in rheumatoid arthritic synovial fluid. J Biol Chem. 1989 Apr 5;264(10):5335-8. [PubMed
]
- Kramer RM, Hession C, Johansen B, Hayes G, McGray P, Chow EP, Tizard R, Pepinsky RB: Structure and properties of a human non-pancreatic phospholipase A2. J Biol Chem. 1989 Apr 5;264(10):5768-75. [PubMed
]
- Kramer RM, Johansen B, Hession C, Pepinsky RB: Structure and properties of a secretable phospholipase A2 from human platelets. Adv Exp Med Biol. 1990;275:35-53. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Kanda A, Ono T, Yoshida N, Tojo H, Okamoto M: The primary structure of a membrane-associated phospholipase A2 from human spleen. Biochem Biophys Res Commun. 1989 Aug 30;163(1):42-8. [PubMed
]
- Hara S, Kudo I, Matsuta K, Miyamoto T, Inoue K: Amino acid composition and NH2-terminal amino acid sequence of human phospholipase A2 purified from rheumatoid synovial fluid. J Biochem (Tokyo). 1988 Sep;104(3):326-8. [PubMed
]
- Lai CY, Wada K: Phospholipase A2 from human synovial fluid: purification and structural homology to the placental enzyme. Biochem Biophys Res Commun. 1988 Dec 15;157(2):488-93. [PubMed
]
- Minami T, Tojo H, Shinomura Y, Matsuzawa Y, Okamoto M: Purification and characterization of a phospholipase A2 from human ileal mucosa. Biochim Biophys Acta. 1993 Oct 13;1170(2):125-30. [PubMed
]
- Wery JP, Schevitz RW, Clawson DK, Bobbitt JL, Dow ER, Gamboa G, Goodson T Jr, Hermann RB, Kramer RM, McClure DB, et al.: Structure of recombinant human rheumatoid arthritic synovial fluid phospholipase A2 at 2.2 A resolution. Nature. 1991 Jul 4;352(6330):79-82. [PubMed
]
- Scott DL, White SP, Browning JL, Rosa JJ, Gelb MH, Sigler PB: Structures of free and inhibited human secretory phospholipase A2 from inflammatory exudate. Science. 1991 Nov 15;254(5034):1007-10. [PubMed
]
- Schevitz RW, Bach NJ, Carlson DG, Chirgadze NY, Clawson DK, Dillard RD, Draheim SE, Hartley LW, Jones ND, Mihelich ED, et al.: Structure-based design of the first potent and selective inhibitor of human non-pancreatic secretory phospholipase A2. Nat Struct Biol. 1995 Jun;2(6):458-65. [PubMed
]
- Kitadokoro K, Hagishita S, Sato T, Ohtani M, Miki K: Crystal structure of human secretory phospholipase A2-IIA complex with the potent indolizine inhibitor 120-1032. J Biochem (Tokyo). 1998 Apr;123(4):619-23. [PubMed
]
|
| Enzyme 12 Metabolite References |
Not Available |
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5302 |
| Enzyme 13 Name |
Group IID secretory phospholipase A2 |
| Enzyme 13 Synonyms |
- GIID sPLA2
- sPLA2-IID
- PLA2IID
- Phosphatidylcholine 2-acylhydrolase 2D
- Secretory-type PLA, stroma-associated homolog
|
| Enzyme 13 Gene Name |
PLA2G2D |
| Enzyme 13 Protein Sequence |
>Group IID secretory phospholipase A2
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
|
| Enzyme 13 Number of Residues |
145 |
| Enzyme 13 Molecular Weight |
16546.1 |
| Enzyme 13 Theoretical pI |
8.28 |
| Enzyme 13 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 13 General Function |
Involved in phospholipase A2 activity |
| Enzyme 13 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined |
| Enzyme 13 Pathways |
|
| Enzyme 13 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
5771420  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9UNK4  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PA2GD_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>438 bp
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
|
| Enzyme 13 GenBank Gene ID |
AF112982  |
| Enzyme 13 GeneCard ID |
PLA2G2D  |
| Enzyme 13 GenAtlas ID |
PLA2G2D  |
| Enzyme 13 HGNC ID |
HGNC:9033  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
1p36.12 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- Ishizaki J, Suzuki N, Higashino K, Yokota Y, Ono T, Kawamoto K, Fujii N, Arita H, Hanasaki K: Cloning and characterization of novel mouse and human secretory phospholipase A(2)s. J Biol Chem. 1999 Aug 27;274(35):24973-9. [PubMed
]
- Shakhov AN, Rubtsov AV, Lyakhov IG, Tumanov AV, Nedospasov SA: SPLASH (PLA2IID), a novel member of phospholipase A2 family, is associated with lymphotoxin deficiency. Genes Immun. 2000 Feb;1(3):191-9. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 13 Metabolite References |
Not Available |
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
5453 |
| Enzyme 14 Name |
Pancreatic triacylglycerol lipase |
| Enzyme 14 Synonyms |
- PL
- Pancreatic lipase
|
| Enzyme 14 Gene Name |
PNLIP |
| Enzyme 14 Protein Sequence |
>Pancreatic triacylglycerol lipase
MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTN
ENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCIC
VDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGR
RTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGH
LDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGF
PCASYNVFTANKCFPCPSGGCPQMGHYADRYPGKTNDVGQKFYLDTGDASNFARWRYKVS
VTLSGKKVTGHILVSLFGNKGNSKQYEIFKGTLKPDSTHSNEFDSDVDVGDLQMVKFIWY
NNVINPTLPRVGASKIIVETNVGKQFNFCSPETVREEVLLTLTPC
|
| Enzyme 14 Number of Residues |
465 |
| Enzyme 14 Molecular Weight |
51156.5 |
| Enzyme 14 Theoretical pI |
6.72 |
| Enzyme 14 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in catalytic activity |
| Enzyme 14 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 14 Pathways |
|
| Enzyme 14 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
Not Available |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
P16233  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
LIPP_HUMAN  |
| Enzyme 14 PDB ID |
1N8S  |
| Enzyme 14 PDB File |
Show |
| Enzyme 14 3D Structure |
|
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1398 bp
ATGCTGCCACTTTGGACTCTTTCACTGCTGCTGGGAGCAGTAGCAGGAAAAGAAGTTTGC
TACGAAAGACTCGGCTGCTTCAGTGATGACTCCCCATGGTCAGGAATTACGGAAAGACCC
CTCCATATATTGCCTTGGTCTCCAAAAGATGTCAACACCCGCTTCCTCCTATATACTAAT
GAGAACCCAAACAACTTTCAAGAAGTTGCCGCAGATTCATCAAGCATCAGTGGCTCCAAT
TTCAAAACAAATAGAAAAACTCGCTTTATTATTCATGGATTCATAGACAAGGGAGAAGAA
AACTGGCTGGCCAATGTGTGCAAGAATCTGTTCAAGGTGGAAAGTGTGAACTGTATCTGT
GTGGACTGGAAAGGTGGCTCCCGAACTGGATACACACAAGCCTCGCAGAACATCAGGATC
GTGGGAGCAGAAGTGGCATATTTTGTTGAATTTCTTCAGTCGGCGTTCGGTTACTCACCT
TCCAACGTGCATGTCATTGGCCACAGCCTGGGTGCCCACGCTGCTGGGGAGGCTGGAAGG
AGAACCAATGGGACCATTGGACGCATCACAGGGTTGGACCCAGCAGAACCTTGCTTTCAG
GGCACACCTGAATTAGTCCGATTGGACCCCAGCGATGCCAAATTTGTGGATGTAATTCAC
ACGGATGGTGCCCCCATAGTCCCCAATTTGGGGTTTGGAATGAGCCAAGTCGTGGGCCAC
CTAGATTTCTTTCCAAATGGAGGAGTGGAAATGCCTGGATGTAAAAAGAACATTCTCTCT
CAGATTGTGGACATAGACGGAATCTGGGAAGGGACTCGAGACTTTGCGGCCTGTAATCAC
TTAAGAAGCTACAAATATTACACTGATAGCATCGTCAACCCTGATGGCTTTGCTGGATTC
CCCTGTGCCTCTTACAACGTCTTCACTGCAAACAAGTGTTTCCCTTGTCCAAGTGGAGGC
TGCCCACAGATGGGTCACTATGCTGATAGATATCCTGGGAAAACAAATGATGTGGGCCAG
AAATTTTATCTAGACACTGGTGATGCCAGTAATTTTGCACGTTGGAGGTATAAGGTATCT
GTCACACTGTCTGGAAAAAAGGTTACAGGACACATACTAGTTTCTTTGTTCGGAAATAAA
GGAAACTCTAAGCAGTATGAAATTTTCAAGGGCACTCTCAAACCAGATAGTACTCATTCC
AATGAATTTGACTCAGATGTGGATGTTGGGGACTTGCAGATGGTTAAATTTATTTGGTAT
AACAATGTGATCAACCCAACTTTACCTAGAGTGGGAGCATCCAAGATTATAGTGGAGACA
AATGTTGGAAAACAGTTCAACTTCTGTAGTCCAGAAACCGTCAGGGAGGAAGTTCTGCTC
ACCCTCACACCGTGTTAG
|
| Enzyme 14 GenBank Gene ID |
J05125  |
| Enzyme 14 GeneCard ID |
PNLIP  |
| Enzyme 14 GenAtlas ID |
PNLIP  |
| Enzyme 14 HGNC ID |
HGNC:9155  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
10q26.1 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Lowe ME, Rosenblum JL, Strauss AW: Cloning and characterization of human pancreatic lipase cDNA. J Biol Chem. 1989 Nov 25;264(33):20042-8. [PubMed
]
- Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed
]
- Sims HF, Jennens ML, Lowe ME: The human pancreatic lipase-encoding gene: structure and conservation of an Alu sequence in the lipase gene family. Gene. 1993 Sep 15;131(2):281-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Winkler FK, D'Arcy A, Hunziker W: Structure of human pancreatic lipase. Nature. 1990 Feb 22;343(6260):771-4. [PubMed
]
- van Tilbeurgh H, Sarda L, Verger R, Cambillau C: Structure of the pancreatic lipase-procolipase complex. Nature. 1992 Sep 10;359(6391):159-62. [PubMed
]
- van Tilbeurgh H, Egloff MP, Martinez C, Rugani N, Verger R, Cambillau C: Interfacial activation of the lipase-procolipase complex by mixed micelles revealed by X-ray crystallography. Nature. 1993 Apr 29;362(6423):814-20. [PubMed
]
- Carriere F, Thirstrup K, Boel E, Verger R, Thim L: Structure-function relationships in naturally occurring mutants of pancreatic lipase. Protein Eng. 1994 Apr;7(4):563-9. [PubMed
]
|
| Enzyme 14 Metabolite References |
Not Available |
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
5458 |
| Enzyme 15 Name |
Hepatic triacylglycerol lipase |
| Enzyme 15 Synonyms |
- HL
- Hepatic lipase
- Lipase member C
|
| Enzyme 15 Gene Name |
LIPC |
| Enzyme 15 Protein Sequence |
>Hepatic triacylglycerol lipase
MDTSPLCFSILLVLCIFIQSSALGQSLKPEPFGRRAQAVETNKTLHEMKTRFLLFGETNQ
GCQIRINHPDTLQECGFNSSLPLVMIIHGWSVDGVLENWIWQMVAALKSQPAQPVNVGLV
DWITLAHDHYTIAVRNTRLVGKEVAALLRWLEESVQLSRSHVHLIGYSLGAHVSGFAGSS
IGGTHKIGRITGLDAAGPLFEGSAPSNRLSPDDANFVDAIHTFTREHMGLSVGIKQPIGH
YDFYPNGGSFQPGCHFLELYRHIAQHGFNAITQTIKCSHERSVHLFIDSLLHAGTQSMAY
PCGDMNSFSQGLCLSCKKGRCNTLGYHVRQEPRSKSKRLFLVTRAQSPFKVYHYQLKIQF
INQTETPIQTTFTMSLLGTKEKMQKIPITLGKGIASNKTYSFLITLDVDIGELIMIKFKW
ENSAVWANVWDTVQTIIPWSTGPRHSGLVLKTIRVKAGETQQRMTFCSENTDDLLLRPTQ
EKIFVKCEIKSKTSKRKIR
|
| Enzyme 15 Number of Residues |
499 |
| Enzyme 15 Molecular Weight |
55880.1 |
| Enzyme 15 Theoretical pI |
9.37 |
| Enzyme 15 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in catalytic activity |
| Enzyme 15 Specific Function |
Hepatic lipase has the capacity to catalyze hydrolysis of phospholipids, mono-, di-, and triglycerides, and acyl-CoA thioesters. It is an important enzyme in HDL metabolism. Hepatic lipase binds heparin |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
194097335  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P11150  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
LIPC_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1500 bp
ATGGACACAAGTCCCCTGTGTTTCTCCATTCTGTTGGTTTTATGCATCTTTATCCAATCA
AGTGCCCTTGGACAAAGCCTGAAACCAGAGCCATTTGGAAGAAGAGCTCAAGCTGTTGAA
ACAAACAAAACGCTGCATGAGATGAAGACCAGATTCCTGCTCTTTGGAGAAACCAATCAG
GGCTGTCAGATTCGAATCAATCATCCGGACACGTTACAGGAGTGCGGCTTCAACTCCTCC
CTGCCTCTGGTGATGATAATCCACGGGTGGTCGGTGGACGGCGTGCTAGAAAACTGGATC
TGGCAGATGGTGGCCGCGCTGAAGTCTCAGCCGGCCCAGCCAGTGAACGTGGGGCTGGTG
GACTGGATCACCCTGGCCCACGACCACTACACCATCGCCGTCCGCAACACCCGCCTTGTG
GGCAAGGAGGTCGCGGCTCTTCTCCGGTGGCTGGAGGAATCTGTGCAACTCTCTCGAAGC
CATGTTCACCTAATTGGGTACAGCCTGGGTGCACACGTGTCAGGATTTGCCGGCAGTTCC
ATCGGTGGAACGCACAAGATTGGGAGAATCACAGGGCTGGATGCCGCGGGACCTTTGTTT
GAGGGAAGTGCCCCCAGCAATCGTCTTTCTCCAGATGATGCCAATTTTGTGGATGCCATT
CATACCTTTACCCGGGAGCACATGGGCCTGAGCGTGGGCATCAAACAGCCCATAGGACAC
TATGACTTCTATCCCAACGGGGGCTCCTTCCAGCCTGGCTGCCACTTCCTAGAGCTCTAC
AGACATATTGCCCAGCACGGCTTCAATGCCATCACCCAGACCATAAAATGCTCCCACGAG
CGATCGGTGCACCTTTTCATCGACTCCTTGCTGCACGCCGGCACGCAGAGCATGGCCTAC
CCGTGTGGTGACATGAACAGCTTCAGCCAGGGCCTGTGCCTGAGCTGCAAGAAGGGCCGC
TGCAACACGCTGGGCTACCACGTCCGCCAGGAGCCGCGGAGCAAGAGCAAGAGGCTCTTC
CTCGTAACGCGAGCCCAGTCCCCCTTCAAAGTTTATCATTACCAGTTCAAGATCCAGTTC
ATCAACCAAACTGAGACACCAATACAAACAACTTTTACCATGTCACTACTCGGAACAAAA
GAGAAAATGCAGAAAATTCCCATCACTCTGGGCAAAGGAATTGCTAGTAATAAAACGTAT
TCCTTTCTTATCACGCTGGATGTGGATATCGGCGAGCTGATCATGATCAAGTTCAAGTGG
GAAAACAGTGCAGTGTGGGCCAATGTCTGGGACACGGTCCAGACCATCATCCCATGGAGC
ACAGGGCCGCGCCACTCAGGCCTCGTTCTGAAGACGATCAGAGTCAAAGCAGGAGAAACC
CAGCAAAGAATGACATTTTGTTCAGAAAACACAGATGACCTACTACTTCGCCCAACCCAG
GAAAAAATCTTCGTGAAATGTGAAATAAAGTCTAAAACATCAAAGCGAAAGATCAGATGA
|
| Enzyme 15 GenBank Gene ID |
NM_000236.2  |
| Enzyme 15 GeneCard ID |
LIPC  |
| Enzyme 15 GenAtlas ID |
LIPC  |
| Enzyme 15 HGNC ID |
HGNC:6619  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
15q21-q23 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Martin GA, Busch SJ, Meredith GD, Cardin AD, Blankenship DT, Mao SJ, Rechtin AE, Woods CW, Racke MM, Schafer MP, et al.: Isolation and cDNA sequence of human postheparin plasma hepatic triglyceride lipase. J Biol Chem. 1988 Aug 5;263(22):10907-14. [PubMed
]
- Stahnke G, Sprengel R, Augustin J, Will H: Human hepatic triglyceride lipase: cDNA cloning, amino acid sequence and expression in a cultured cell line. Differentiation. 1987;35(1):45-52. [PubMed
]
- Datta S, Luo CC, Li WH, VanTuinen P, Ledbetter DH, Brown MA, Chen SH, Liu SW, Chan L: Human hepatic lipase. Cloned cDNA sequence, restriction fragment length polymorphisms, chromosomal localization, and evolutionary relationships with lipoprotein lipase and pancreatic lipase. J Biol Chem. 1988 Jan 25;263(3):1107-10. [PubMed
]
- Cai SJ, Wong DM, Chen SH, Chan L: Structure of the human hepatic triglyceride lipase gene. Biochemistry. 1989 Nov 14;28(23):8966-71. [PubMed
]
- Ameis D, Stahnke G, Kobayashi J, McLean J, Lee G, Buscher M, Schotz MC, Will H: Isolation and characterization of the human hepatic lipase gene. J Biol Chem. 1990 Apr 25;265(12):6552-5. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Tiebel O, Gehrisch S, Pietzsch J, Gromeier S, Jaross W: 18 bp insertion/duplication with internal missense mutation in human hepatic lipase gene exon 3. Mutations in brief no. 181. Online. Hum Mutat. 1998;12(3):216. [PubMed
]
- Takagi A, Ikeda Y, Mori A, Ashida Y, Yamamoto A: Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene. Mol Cell Probes. 1996 Aug;10(4):313-4. [PubMed
]
- Todorova B, Kubaszek A, Pihlajamaki J, Lindstrom J, Eriksson J, Valle TT, Hamalainen H, Ilanne-Parikka P, Keinanen-Kiukaanniemi S, Tuomilehto J, Uusitupa M, Laakso M: The G-250A promoter polymorphism of the hepatic lipase gene predicts the conversion from impaired glucose tolerance to type 2 diabetes mellitus: the Finnish Diabetes Prevention Study. J Clin Endocrinol Metab. 2004 May;89(5):2019-23. [PubMed
]
- Grarup N, Andreasen CH, Andersen MK, Albrechtsen A, Sandbaek A, Lauritzen T, Borch-Johnsen K, Jorgensen T, Schmitz O, Hansen T, Pedersen O: The -250G>A promoter variant in hepatic lipase associates with elevated fasting serum high-density lipoprotein cholesterol modulated by interaction with physical activity in a study of 16,156 Danish subjects. J Clin Endocrinol Metab. 2008 Jun;93(6):2294-9. Epub 2008 Mar 25. [PubMed
]
- Hegele RA, Tu L, Connelly PW: Human hepatic lipase mutations and polymorphisms. Hum Mutat. 1992;1(4):320-4. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
5461 |
| Enzyme 16 Name |
Pancreatic lipase-related protein 1 |
| Enzyme 16 Synonyms |
- PL-RP1
|
| Enzyme 16 Gene Name |
PNLIPRP1 |
| Enzyme 16 Protein Sequence |
>Pancreatic lipase-related protein 1
MLIFWTITLFLLGAAKGKEVCYEDLGCFSDTEPWGGTAIRPLKILPWSPEKIGTRFLLYT
NENPNNFQILLLSDPSTIEASNFQMDRKTRFIIHGFIDKGDESWVTDMCKKLFEVEEVNC
ICVDWKKGSQATYTQAANNVRVVGAQVAQMLDILLTEYSYPPSKVHLIGHSLGAHVAGEA
GSKTPGLSRITGLDPVEASFESTPEEVRLDPSDADFVDVIHTDAAPLIPFLGFGTNQQMG
HLDFFPNGGESMPGCKKNALSQIVDLDGIWAGTRDFVACNHLRSYKYYLESILNPDGFAA
YPCTSYKSFESDKCFPCPDQGCPQMGHYADKFAGRTSEEQQKFFLNTGEASNFARWRYGV
SITLSGRTATGQIKVALFGNKGNTHQYSIFRGILKPGSTHSYEFDAKLDVGTIEKVKFLW
NNNVINPTLPKVGATKITVQKGEEKTVYNFCSEDTVREDTLLTLTPC
|
| Enzyme 16 Number of Residues |
467 |
| Enzyme 16 Molecular Weight |
51847.4 |
| Enzyme 16 Theoretical pI |
5.47 |
| Enzyme 16 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 16 General Function |
Involved in catalytic activity |
| Enzyme 16 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 16 Pathways |
|
| Enzyme 16 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
5453920  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
P54315  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
LIPR1_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>1404 bp
ATGCTGATCTTCTGGACAATCACACTTTTCCTGCTGGGAGCAGCCAAAGGAAAAGAAGTT
TGCTATGAGGACCTCGGGTGCTTTTCTGACACTGAGCCCTGGGGCGGGACAGCAATCAGG
CCCCTGAAAATTCTCCCCTGGAGCCCTGAGAAGATCGGCACCCGCTTCCTGCTGTACACC
AATGAAAACCCAAACAACTTTCAAATTCTCCTCCTCTCTGATCCATCAACAATTGAGGCA
TCAAATTTTCAAATGGACAGAAAGACCCGGTTCATCATCCATGGCTTCATAGACAAAGGA
GATGAGAGCTGGGTGACAGACATGTGCAAGAAACTGTTCGAGGTGGAGGAGGTGAACTGC
ATCTGCGTGGACTGGAAGAAGGGCTCCCAAGCCACCTACACACAGGCTGCCAACAACGTG
CGAGTGGTGGGCGCCCAGGTGGCCCAGATGCTCGACATCCTCTTGACAGAGTATAGCTAC
CCCCCTTCCAAAGTTCACCTCATTGGCCACAGCCTGGGAGCCCACGTGGCTGGAGAGGCA
GGAAGCAAGACTCCAGGCCTGAGCAGGATTACAGGGTTGGATCCTGTAGAAGCAAGTTTC
GAGAGTACTCCTGAAGAGGTGCGACTTGATCCCTCTGATGCTGACTTTGTTGATGTGATT
CACACGGATGCAGCTCCCCTGATCCCATTCTTGGGTTTTGGAACGAACCAACAGATGGGT
CATCTTGACTTCTTCCCCAATGGAGGAGAGAGCATGCCGGGATGCAAGAAGAATGCCCTG
TCTCAGATCGTGGATCTAGATGGCATCTGGGCGGGAACCCGGGACTTTGTGGCTTGCAAT
CACCTAAGAAGCTACAAGTATTACTTGGAAAGCATCCTCAATCCCGATGGGTTTGCTGCA
TATCCCTGCACTTCCTACAAGTCCTTTGAGTCTGACAAGTGCTTCCCGTGTCCAGATCAA
GGATGCCCACAGATGGGTCACTATGCTGATAAATTTGCTGGCAGGACAAGTGAAGAGCAG
CAGAAATTCTTCTTGAACACAGGAGAGGCTAGCAATTTCGCTCGCTGGAGATATGGGGTT
TCCATCACACTGTCTGGAAGAACAGCCACTGGTCAGATCAAAGTTGCTTTGTTTGGAAAT
AAGGGAAACACTCACCAGTACAGCATCTTCAGGGGGATTCTCAAACCAGGCTCAACCCAT
TCCTATGAGTTTGATGCAAAGCTGGATGTTGGAACAATTGAGAAAGTCAAGTTTCTTTGG
AATAACAATGTGATAAATCCAACCCTCCCCAAAGTGGGTGCCACCAAGATCACTGTGCAA
AAGGGAGAAGAGAAGACAGTGTACAACTTCTGTAGCGAAGACACAGTGCGGGAAGACACG
CTGCTCACCCTCACGCCCTGCTAA
|
| Enzyme 16 GenBank Gene ID |
NM_006229.2  |
| Enzyme 16 GeneCard ID |
PNLIPRP1  |
| Enzyme 16 GenAtlas ID |
PNLIPRP1  |
| Enzyme 16 HGNC ID |
HGNC:9156  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
10q25.3 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
5464 |
| Enzyme 17 Name |
Patatin-like phospholipase domain-containing protein 3 |
| Enzyme 17 Synonyms |
- Acylglycerol O-acyltransferase
- Adiponutrin
- Calcium-independent phospholipase A2-epsilon
- iPLA2-epsilon
|
| Enzyme 17 Gene Name |
PNPLA3 |
| Enzyme 17 Protein Sequence |
>Patatin-like phospholipase domain-containing protein 3
MYDAERGWSLSFAGCGFLGFYHVGATRCLSEHAPHLLRDARMLFGASAGALHCVGVLSGI
PLEQTLQVLSDLVRKARSRNIGIFHPSFNLSKFLRQGLCKCLPANVHQLISGKIGISLTR
VSDGENVLVSDFRSKDEVVDALVCSCFIPFYSGLIPPSFRGVRYVDGGVSDNVPFIDAKT
TITVSPFYGEYDICPKVKSTNFLHVDITKLSLRLCTGNLYLLSRAFVPPDLKVLGEICLR
GYLDAFRFLEEKGICNRPQPGLKSSSEGMDPEVAMPSWANMSLDSSPESAALAVRLEGDE
LLDHLRLSILPWDESILDTLSPRLATALSEEMKDKGGYMSKICNLLPIRIMSYVMLPCTL
PVESAIAIVQRLVTWLPDMPDDVLWLQWVTSQVFTRVLMCLLPASRSQMPVSSQQASPCT
PEQDWPCWTPCSPKGCPAETKAEATPRSILRSSLNFFLGNKVPAGAEGLSTFPSFSLEKS
L
|
| Enzyme 17 Number of Residues |
481 |
| Enzyme 17 Molecular Weight |
52864.6 |
| Enzyme 17 Theoretical pI |
6.68 |
| Enzyme 17 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in metabolic process |
| Enzyme 17 Specific Function |
Multifunctional enzyme which has both triacylglycerol lipase and acylglycerol O-acyltransferase activities |
| Enzyme 17 Pathways |
|
| Enzyme 17 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
17059636  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
Q9NST1  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
PLPL3_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>1446 bp
ATGTACGACGCAGAGCGCGGCTGGAGCTTGTCCTTCGCGGGCTGCGGCTTCCTGGGCTTC
TACCACGTCGGGGCGACCCGCTGCCTGAGCGAGCACGCCCCGCACCTCCTCCGCGACGCG
CGCATGTTGTTCGGCGCTTCGGCCGGGGCGTTGCACTGCGTCGGCGTCCTCTCCGGTATC
CCGCTGGAGCAGACTCTGCAGGTCCTCTCAGATCTTGTGCGGAAGGCCAGGAGTCGGAAC
ATTGGCATCTTCCATCCATCCTTCAACTTAAGCAAGTTCCTCCGACAGGGTCTCTGCAAA
TGCCTCCCGGCCAATGTCCACCAGCTCATCTCCGGCAAAATAGGCATCTCTCTTACCAGA
GTGTCTGATGGGGAAAACGTTCTGGTGTCTGACTTTCGGTCCAAAGACGAAGTCGTGGAT
GCCTTGGTATGTTCCTGCTTCATCCCCTTCTACAGTGGCCTTATCCCTCCTTCCTTCAGA
GGCGTGCGATATGTGGATGGAGGAGTGAGTGACAACGTACCCTTCATTGATGCCAAAACA
ACCATCACCGTGTCCCCCTTCTATGGGGAGTACGACATCTGCCCTAAAGTCAAGTCCACG
AACTTTCTTCATGTGGACATCACCAAGCTCAGTCTACGCCTCTGCACAGGGAACCTCTAC
CTTCTCTCGAGAGCTTTTGTCCCCCCGGATCTCAAGGTGCTGGGAGAGATATGCCTTCGA
GGATATTTGGATGCATTCAGGTTCTTGGAAGAGAAGGGCATCTGCAACAGGCCCCAGCCA
GGCCTGAAGTCATCCTCAGAAGGGATGGATCCTGAGGTCGCCATGCCCAGCTGGGCAAAC
ATGAGTCTGGATTCTTCCCCGGAGTCGGCTGCCTTGGCTGTGAGGCTGGAGGGAGATGAG
CTGCTAGACCACCTGCGTCTCAGCATCCTGCCCTGGGATGAGAGCATCCTGGACACCCTC
TCGCCCAGGCTCGCTACAGCACTGAGTGAAGAAATGAAAGACAAAGGTGGATACATGAGC
AAGATTTGCAACTTGCTACCCATTAGGATAATGTCTTATGTAATGCTGCCCTGTACCCTG
CCTGTGGAATCTGCCATTGCGATTGTCCAGAGACTGGTGACATGGCTTCCAGATATGCCC
GACGATGTCCTGTGGTTGCAGTGGGTGACCTCACAGGTGTTCACTCGAGTGCTGATGTGT
CTGCTCCCCGCCTCCAGGTCCCAAATGCCAGTGAGCAGCCAACAGGCCTCCCCATGCACA
CCTGAGCAGGACTGGCCCTGCTGGACTCCCTGCTCCCCCAAGGGCTGTCCAGCAGAGACC
AAAGCAGAGGCCACCCCGCGGTCCATCCTCAGGTCCAGCCTGAACTTCTTCTTGGGCAAT
AAAGTACCTGCTGGTGCTGAGGGGCTCTCCACCTTTCCCAGTTTTTCACTAGAGAAGAGT
CTGTGA
|
| Enzyme 17 GenBank Gene ID |
AL138578  |
| Enzyme 17 GeneCard ID |
PNPLA3  |
| Enzyme 17 GenAtlas ID |
PNPLA3  |
| Enzyme 17 HGNC ID |
HGNC:18590  |
| Enzyme 17 Chromosome Location |
2 |
| Enzyme 17 Locus |
22q13.31 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Collins JE, Goward ME, Cole CG, Smink LJ, Huckle EJ, Knowles S, Bye JM, Beare DM, Dunham I: Reevaluating human gene annotation: a second-generation analysis of chromosome 22. Genome Res. 2003 Jan;13(1):27-36. [PubMed
]
- Collins JE, Wright CL, Edwards CA, Davis MP, Grinham JA, Cole CG, Goward ME, Aguado B, Mallya M, Mokrab Y, Huckle EJ, Beare DM, Dunham I: A genome annotation-driven approach to cloning the human ORFeome. Genome Biol. 2004;5(10):R84. Epub 2004 Sep 30. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed
]
- Liu YM, Moldes M, Bastard JP, Bruckert E, Viguerie N, Hainque B, Basdevant A, Langin D, Pairault J, Clement K: Adiponutrin: A new gene regulated by energy balance in human adipose tissue. J Clin Endocrinol Metab. 2004 Jun;89(6):2684-9. [PubMed
]
- Johansson LE, Lindblad U, Larsson CA, Rastam L, Ridderstrale M: Polymorphisms in the adiponutrin gene are associated with increased insulin secretion and obesity. Eur J Endocrinol. 2008 Nov;159(5):577-83. Epub 2008 Aug 26. [PubMed
]
- Romeo S, Kozlitina J, Xing C, Pertsemlidis A, Cox D, Pennacchio LA, Boerwinkle E, Cohen JC, Hobbs HH: Genetic variation in PNPLA3 confers susceptibility to nonalcoholic fatty liver disease. Nat Genet. 2008 Dec;40(12):1461-5. Epub 2008 Sep 25. [PubMed
]
- Kotronen A, Johansson LE, Johansson LM, Roos C, Westerbacka J, Hamsten A, Bergholm R, Arkkila P, Arola J, Kiviluoto T, Fisher RM, Ehrenborg E, Orho-Melander M, Ridderstrale M, Groop L, Yki-Jarvinen H: A common variant in PNPLA3, which encodes adiponutrin, is associated with liver fat content in humans. Diabetologia. 2009 Jun;52(6):1056-60. Epub 2009 Feb 18. [PubMed
]
- He S, McPhaul C, Li JZ, Garuti R, Kinch L, Grishin NV, Cohen JC, Hobbs HH: A sequence variation (I148M) in PNPLA3 associated with nonalcoholic fatty liver disease disrupts triglyceride hydrolysis. J Biol Chem. 2010 Feb 26;285(9):6706-15. Epub 2009 Dec 23. [PubMed
]
- Sookoian S, Castano GO, Burgueno AL, Gianotti TF, Rosselli MS, Pirola CJ: A nonsynonymous gene variant in the adiponutrin gene is associated with nonalcoholic fatty liver disease severity. J Lipid Res. 2009 Oct;50(10):2111-6. [PubMed
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
5468 |
| Enzyme 18 Name |
Gastric triacylglycerol lipase |
| Enzyme 18 Synonyms |
- GL
- Gastric lipase
|
| Enzyme 18 Gene Name |
LIPF |
| Enzyme 18 Protein Sequence |
>Gastric triacylglycerol lipase
MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILE
VNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRG
NTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFI
AFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQF
LATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKS
GKFQAYDWGSPVQNRMHYDQSQPPYYNVTAMNVPIAVWNGGKDLLADPQDVGLLLPKLPN
LIYHKEIPFYNHLDFIWAMDAPQEVYNDIVSMISEDKK
|
| Enzyme 18 Number of Residues |
398 |
| Enzyme 18 Molecular Weight |
45237.4 |
| Enzyme 18 Theoretical pI |
7.37 |
| Enzyme 18 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in lipid metabolic process |
| Enzyme 18 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
758063  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
P07098  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
LIPG_HUMAN  |
| Enzyme 18 PDB ID |
1HLG  |
| Enzyme 18 PDB File |
Show |
| Enzyme 18 3D Structure |
|
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>1197 bp
ATGTGGCTGCTTTTAACAATGGCAAGTTTGATATCTGTACTGGGGACTACACATGGTTTG
TTTGGAAAATTACATCCTGGAAGCCCTGAAGTGACTATGAACATTAGTCAGATGATTACT
TATTGGGGATACCCAAATGAAGAATATGAAGTTGTGACTGAAGATGGTTATATTCTTGAA
GTCAATAGAATTCCTTATGGGAAGAAAAATTCAGGGAATACAGGCCAGAGACCTGTTGTG
TTTTTGCAGCATGGTTTGCTTGCATCAGCCACAAACTGGATTTCCAACCTGCCGAACAAC
AGCCTTGCCTTCATTCTGGCAGATGCTGGTTATGATGTGTGGCTGGGCAACAGCAGAGGA
AACACCTGGGCCAGAAGAAACTTGTACTATTCACCAGATTCAGTTGAATTCTGGGCTTTC
AGCTTTGATGAAATGGCTAAATATGACCTTCCAGCCACAATCGACTTCATTGTAAAGAAA
ACTGGACAGAAGCAGCTACACTATGTTGGCCATTCCCAGGGCACCACCATTGGTTTTATT
GCCTTTTCCACCAATCCCAGCCTGGCTAAAAGAATCAAAACCTTCTATGCTCTAGCTCCT
GTTGCCACTGTGAAGTATACAAAAAGCCTTATAAACAAACTTAGATTTGTTCCTCAATCC
CTCTTCAAGTTTATATTTGGTGACAAAATATTCTACCCACACAACTTCTTTGATCAATTT
CTTGCTACTGAAGTGTGCTCCCGTGAGATGCTGAATCTCCTTTGCAGCAATGCCTTATTT
ATAATTTGTGGATTTGACAGTAAGAACTTTAACACGAGTCGCTTGGATGTGTATCTATCA
CATAATCCAGCAGGAACTTCTGTTCAAAACATGTTCCATTGGACCCAGGCTGTTAAGTCT
GGGAAATTCCAAGCTTATGACTGGGGAAGCCCAGTTCAGAATAGGATGCACTATGATCAG
TCCCAACCTCCCTACTACAATGTGACAGCCATGAATGTACCAATTGCAGTGTGGAACGGT
GGCAAGGACCTGTTGGCTGACCCCCAAGATGTTGGCCTTTTGCTTCCAAAACTCCCCAAT
CTTATTTACCACAAGGAGATTCCTTTTTACAATCACTTGGACTTTATCTGGGCAATGGAT
GCCCCTCAAGAAGTTTACAATGACATTGTTTCTATGATATCAGAAGATAAAAAGTAG
|
| Enzyme 18 GenBank Gene ID |
X05997  |
| Enzyme 18 GeneCard ID |
LIPF  |
| Enzyme 18 GenAtlas ID |
LIPF  |
| Enzyme 18 HGNC ID |
HGNC:6622  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
10q23.31 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Bodmer MW, Angal S, Yarranton GT, Harris TJ, Lyons A, King DJ, Pieroni G, Riviere C, Verger R, Lowe PA: Molecular cloning of a human gastric lipase and expression of the enzyme in yeast. Biochim Biophys Acta. 1987 Aug 25;909(3):237-44. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bernback S, Blackberg L: Human gastric lipase. The N-terminal tetrapeptide is essential for lipid binding and lipase activity. Eur J Biochem. 1989 Jul 1;182(3):495-9. [PubMed
]
- Roussel A, Canaan S, Egloff MP, Riviere M, Dupuis L, Verger R, Cambillau C: Crystal structure of human gastric lipase and model of lysosomal acid lipase, two lipolytic enzymes of medical interest. J Biol Chem. 1999 Jun 11;274(24):16995-7002. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
5471 |
| Enzyme 19 Name |
Endothelial lipase |
| Enzyme 19 Synonyms |
- Endothelial cell-derived lipase
- EDL
- EL
|
| Enzyme 19 Gene Name |
LIPG |
| Enzyme 19 Protein Sequence |
>Endothelial lipase
MSNSVPLLCFWSLCYCFAAGSPVPFGPEGRLEDKLHKPKATQTEVKPSVRFNLRTSKDPE
HEGCYLSVGHSQPLEDCSFNMTAKTFFIIHGWTMSGIFENWLHKLVSALHTREKDANVVV
VDWLPLAHQLYTDAVNNTRVVGHSIARMLDWLQEKDDFSLGNVHLIGYSLGAHVAGYAGN
FVKGTVGRITGLDPAGPMFEGADIHKRLSPDDADFVDVLHTYTRSFGLSIGIQMPVGHID
IYPNGGDFQPGCGLNDVLGSIAYGTITEVVKCEHERAVHLFVDSLVNQDKPSFAFQCTDS
NRFKKGICLSCRKNRCNSIGYNAKKMRNKRNSKMYLKTRAGMPFRVYHYQMKIHVFSYKN
MGEIEPTFYVTLYGTNADSQTLPLEIVERIEQNATNTFLVYTEEDLGDLLKIQLTWEGAS
QSWYNLWKEFRSYLSQPRNPGRELNIRRIRVKSGETQRKLTFCTEDPENTSISPGRELWF
RKCRDGWRMKNETSPTVELP
|
| Enzyme 19 Number of Residues |
500 |
| Enzyme 19 Molecular Weight |
56794.3 |
| Enzyme 19 Theoretical pI |
8.00 |
| Enzyme 19 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipoprotein lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 19 General Function |
Involved in catalytic activity |
| Enzyme 19 Specific Function |
Has phospholipase and triglyceride lipase activities. Hydrolyzes high density lipoproteins (HDL) more efficiently than other lipoproteins. Binds heparin |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
4836419  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9Y5X9  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
LIPE_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1503 bp
ATGAGCAACTCCGTTCCTCTGCTCTGTTTCTGGAGCCTCTGCTATTGCTTTGCTGCGGGG
AGCCCCGTACCTTTTGGTCCAGAGGGACGGCTGGAAGATAAGCTCCACAAACCCAAAGCT
ACACAGACTGAGGTCAAACCATCTGTGAGGTTTAACCTCCGCACCTCCAAGGACCCAGAG
CATGAAGGATGCTACCTCTCCGTCGGCCACAGCCAGCCCTTAGAAGACTGCAGTTTCAAC
ATGACAGCTAAAACCTTTTTCATCATTCACGGATGGACGATGAGCGGTATCTTTGAAAAC
TGGCTGCACAAACTCGTGTCAGCCCTGCACACAAGAGAGAAAGACGCCAATGTAGTTGTG
GTTGACTGGCTCCCCCTGGCCCACCAGCTTTACACGGATGCGGTCAATAATACCAGGGTG
GTGGGACACAGCATTGCCAGGATGCTCGACTGGCTGCAGGAGAAGGACGATTTTTCTCTC
GGGAATGTCCACTTGATCGGCTACAGCCTCGGAGCGCACGTGGCCGGGTATGCAGGCAAC
TTCGTGAAAGGAACGGTGGGCCGAATCACAGGTTTGGATCCTGCCGGGCCCATGTTTGAA
GGGGCCGACATCCACAAGAGGCTCTCTCCGGACGATGCAGATTTTGTGGATGTCCTCCAC
ACCTACACGCGTTCCTTCGGCTTGAGCATTGGTATTCAGATGCCTGTGGGCCACATTGAC
ATCTACCCCAATGGGGGTGACTTCCAGCCAGGCTGTGGACTCAACGATGTCTTGGGATCA
ATTGCATATGGAACAATCACAGAGGTGGTAAAATGTGAGCATGAGCGAGCCGTCCACCTC
TTTGTTGACTCTCTGGTGAATCAGGACAAGCCGAGTTTTGCCTTCCAGTGCACTGACTCC
AATCGCTTCAAAAAGGGGATCTGTCTGAGCTGCCGCAAGAACCGTTGTAATAGCATTGGC
TACAATGCCAAGAAAATGAGGAACAAGAGGAACAGCAAAATGTACCTAAAAACCCGGGCA
GGCATGCCTTTCAGAGTTTACCATTATCAGATGAAAATCCATGTCTTCAGTTACAAGAAC
ATGGGAGAAATTGAGCCCACCTTTTACGTCACCCTTTATGGCACTAATGCAGATTCCCAG
ACTCTGCCACTGGAAATAGTGGAGCGGATCGAGCAGAATGCCACCAACACCTTCCTGGTC
TACACCGAGGAGGACTTGGGAGACCTCTTGAAGATCCAGCTCACCTGGGAGGGGGCCTCT
CAGTCTTGGTACAACCTGTGGAAGGAGTTTCGCAGCTACCTGTCTCAACCCCGCAACCCC
GGACGGGAGCTGAATATCAGGCGCATCCGGGTGAAGTCTGGGGAAACCCAGCGGAAACTG
ACATTTTGTACAGAAGACCCTGAGAACACCAGCATATCCCCAGGCCGGGAGCTCTGGTTT
CGCAAGTGTCGGGATGGCTGGAGGATGAAAAACGAAACCAGTCCCACTGTGGAGCTTCCC
TGA
|
| Enzyme 19 GenBank Gene ID |
AF118767  |
| Enzyme 19 GeneCard ID |
LIPG  |
| Enzyme 19 GenAtlas ID |
LIPG  |
| Enzyme 19 HGNC ID |
HGNC:6623  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
18q21.1 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Hirata K, Dichek HL, Cioffi JA, Choi SY, Leeper NJ, Quintana L, Kronmal GS, Cooper AD, Quertermous T: Cloning of a unique lipase from endothelial cells extends the lipase gene family. J Biol Chem. 1999 May 14;274(20):14170-5. [PubMed
]
- Jaye M, Lynch KJ, Krawiec J, Marchadier D, Maugeais C, Doan K, South V, Amin D, Perrone M, Rader DJ: A novel endothelial-derived lipase that modulates HDL metabolism. Nat Genet. 1999 Apr;21(4):424-8. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- McCoy MG, Sun GS, Marchadier D, Maugeais C, Glick JM, Rader DJ: Characterization of the lipolytic activity of endothelial lipase. J Lipid Res. 2002 Jun;43(6):921-9. [PubMed
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
5473 |
| Enzyme 20 Name |
Bile salt-activated lipase |
| Enzyme 20 Synonyms |
- BAL
- Bile salt-stimulated lipase
- BSSL
- Bucelipase
- Carboxyl ester lipase
- Cholesterol esterase
- Pancreatic lysophospholipase
- Sterol esterase
|
| Enzyme 20 Gene Name |
CEL |
| Enzyme 20 Protein Sequence |
>Bile salt-activated lipase
MGRLQLVVLGLTCCWAVASAAKLGAVYTEGGFVEGVNKKLGLLGDSVDIFKGIPFAAPTK
ALENPQPHPGWQGTLKAKNFKKRCLQATITQDSTYGDEDCLYLNIWVPQGRKQVSRDLPV
MIWIYGGAFLMGSGHGANFLNNYLYDGEEIATRGNVIVVTFNYRVGPLGFLSTGDANLPG
NYGLRDQHMAIAWVKRNIAAFGGDPNNITLFGESAGGASVSLQTLSPYNKGLIRRAISQS
GVALSPWVIQKNPLFWAKKVAEKVGCPVGDAARMAQCLKVTDPRALTLAYKVPLAGLEYP
MLHYVGFVPVIDGDFIPADPINLYANAADIDYIAGTNNMDGHIFASIDMPAINKGNKKVT
EEDFYKLVSEFTITKGLRGAKTTFDVYTESWAQDPSQENKKKTVVDFETDVLFLVPTEIA
LAQHRANAKSAKTYAYLFSHPSRMPVYPKWVGADHADDIQYVFGKPFATPTGYRPQDRTV
SKAMIAYWTNFAKTGDPNMGDSAVPTHWEPYTTENSGYLEITKKMGSSSMKRSLRTNFLR
YWTLTYLALPTVTDQEATPVPPTGDSEATPVPPTGDSETAPVPPTGDSGAPPVPPTGDSG
APPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVPPTGDSGAPPVP
PTGDSGAPPVPPTGDAGPPPVPPTGDSGAPPVPPTGDSGAPPVTPTGDSETAPVPPTGDS
GAPPVPPTGDSEAAPVPPTDDSKEAQMPAVIRF
|
| Enzyme 20 Number of Residues |
753 |
| Enzyme 20 Molecular Weight |
79320.9 |
| Enzyme 20 Theoretical pI |
4.94 |
| Enzyme 20 GO Classification |
Not Available |
| Enzyme 20 General Function |
Lipid transport and metabolism |
| Enzyme 20 Specific Function |
Catalyzes fat and vitamin absorption. Acts in concert with pancreatic lipase and colipase for the complete digestion of dietary triglycerides |
| Enzyme 20 Pathways |
|
| Enzyme 20 Reactions |
- a steryl ester + H2O = a sterol + a fatty acid [RN:R02115]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
148536848  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
P19835  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
CEL_HUMAN  |
| Enzyme 20 PDB ID |
1F6W  |
| Enzyme 20 PDB File |
Show |
| Enzyme 20 3D Structure |
|
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>2271 bp
ATGCTCACCATGGGGCGCCTGCAACTGGTTGTGTTGGGCCTCACCTGCTGCTGGGCAGTG
GCGAGTGCCGCGAAGCTGGGCGCCGTGTACACAGAAGGTGGGTTCGTGGAAGGCGTCAAT
AAGAAGCTCGGCCTCCTGGGTGACTCTGTGGACATCTTCAAGGGCATCCCCTTCGCAGCT
CCCACCAAGGCCCTGGAAAATCCTCAGCCACATCCTGGCTGGCAAGGGACCCTGAAGGCC
AAGAACTTCAAGAAGAGATGCCTGCAGGCCACCATCACCCAGGACAGCACCTACGGGGAT
GAAGACTGCCTGTACCTCAACATTTGGGTGCCCCAGGGCAGGAAGCAAGTCTCCCGGGAC
CTGCCCGTTATGATCTGGATCTATGGAGGCGCCTTCCTCATGGGGTCCGGCCATGGGGCC
AACTTCCTCAACAACTACCTGTATGACGGCGAGGAGATCGCCACACGCGGAAACGTCATC
GTGGTCACCTTCAACTACCGTGTCGGCCCCCTTGGGTTCCTCAGCACTGGGGACGCCAAT
CTGCCAGGTAACTATGGCCTTCGGGATCAGCACATGGCCATTGCTTGGGTGAAGAGGAAT
ATCGCGGCCTTCGGGGGGGACCCCAACAACATCACGCTCTTCGGGGAGTCTGCTGGAGGT
GCCAGCGTCTCTCTGCAGACCCTCTCCCCCTACAACAAGGGCCTCATCCGGCGAGCCATC
AGCCAGAGCGGCGTGGCCCTGAGTCCCTGGGTCATCCAGAAAAACCCACTCTTCTGGGCC
AAAAAGGTGGCTGAGAAGGTGGGTTGCCCTGTGGGTGATGCCGCCAGGATGGCCCAGTGT
CTGAAGGTTACTGATCCCCGAGCCCTGACGCTGGCCTATAAGGTGCCGCTGGCAGGCCTG
GAGTACCCCATGCTGCACTATGTGGGCTTCGTCCCTGTCATTGATGGAGACTTCATCCCC
GCTGACCCGATCAACCTGTACGCCAACGCCGCCGACATCGACTATATAGCAGGCACCAAC
AACATGGACGGCCACATCTTCGCCAGCATCGACATGCCTGCCATCAACAAGGGCAACAAG
AAAGTCACGGAGGAGGACTTCTACAAGCTGGTCAGTGAGTTCACAATCACCAAGGGGCTC
AGAGGCGCCAAGACGACCTTTGATGTCTACACCGAGTCCTGGGCCCAGGACCCATCCCAG
GAGAATAAGAAGAAGACTGTGGTGGACTTTGAGACCGATGTCCTCTTCCTGGTGCCCACC
GAGATTGCCCTAGCCCAGCACAGAGCCAATGCCAAGAGTGCCAAGACCTACGCCTACCTG
TTTTCCCATCCCTCTCGGATGCCCGTCTACCCCAAATGGGTGGGGGCCGACCATGCAGAT
GACATTCAGTACGTTTTCGGGAAGCCCTTCGCCACCCCCACGGGCTACCGGCCCCAAGAC
AGGACAGTCTCTAAGGCCATGATCGCCTACTGGACCAACTTTGCCAAAACAGGGGACCCC
AACATGGGCGACTCGGCTGTGCCCACACACTGGGAACCCTACACTACGGAAAACAGCGGC
TACCTGGAGATCACCAAGAAGATGGGCAGCAGCTCCATGAAGCGGAGCCTGAGAACCAAC
TTCCTGCGCTACTGGACCCTCACCTATCTGGCGCTGCCCACAGTGACCGACCAGGAGGCC
ACCCCTGTGCCCCCCACAGGGGACTCCGAGGCCACTCCCGTGCCCCCCACGGGTGACTCC
GAGACCGCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGT
GACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCC
ACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCCCCCGTG
CCGCCCACGGGTGACTCCGGGGCCCCCCCCGTGCCGCCCACGGGTGACTCCGGGGCCCCC
CCCGTGCCGCCCACGGGTGACTCCGGCGCCCCCCCCGTGCCGCCCACGGGTGACGCCGGG
CCCCCCCCCGTGCCGCCCACGGGTGACTCCGGCGCCCCCCCCGTGCCGCCCACGGGTGAC
TCCGGGGCCCCCCCCGTGACCCCCACGGGTGACTCCGAGACCGCCCCCGTGCCGCCCACG
GGTGACTCCGGGGCCCCCCCTGTGCCCCCCACGGGTGACTCTGAGGCTGCCCCTGTGCCC
CCCACAGATGACTCCAAGGAAGCTCAGATGCCTGCAGTCATTAGGTTTTAG
|
| Enzyme 20 GenBank Gene ID |
Not Available |
| Enzyme 20 GeneCard ID |
CEL  |
| Enzyme 20 GenAtlas ID |
CEL  |
| Enzyme 20 HGNC ID |
HGNC:1848  |
| Enzyme 20 Chromosome Location |
9 |
| Enzyme 20 Locus |
9q34.3 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Nilsson J, Blackberg L, Carlsson P, Enerback S, Hernell O, Bjursell G: cDNA cloning of human-milk bile-salt-stimulated lipase and evidence for its identity to pancreatic carboxylic ester hydrolase. Eur J Biochem. 1990 Sep 11;192(2):543-50. [PubMed
]
- Hui DY, Kissel JA: Sequence identity between human pancreatic cholesterol esterase and bile salt-stimulated milk lipase. FEBS Lett. 1990 Dec 10;276(1-2):131-4. [PubMed
]
- Baba T, Downs D, Jackson KW, Tang J, Wang CS: Structure of human milk bile salt activated lipase. Biochemistry. 1991 Jan 15;30(2):500-10. [PubMed
]
- Lidberg U, Nilsson J, Stromberg K, Stenman G, Sahlin P, Enerback S, Bjursell G: Genomic organization, sequence analysis, and chromosomal localization of the human carboxyl ester lipase (CEL) gene and a CEL-like (CELL) gene. Genomics. 1992 Jul;13(3):630-40. [PubMed
]
- Roudani S, Miralles F, Margotat A, Escribano MJ, Lombardo D: Bile salt-dependent lipase transcripts in human fetal tissues. Biochim Biophys Acta. 1995 Oct 17;1264(1):141-50. [PubMed
]
- Madeyski K, Lidberg U, Bjursell G, Nilsson J: Structure and organization of the human carboxyl ester lipase locus. Mamm Genome. 1998 Apr;9(4):334-8. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Hui DY, Hayakawa K, Oizumi J: Lipoamidase activity in normal and mutagenized pancreatic cholesterol esterase (bile salt-stimulated lipase). Biochem J. 1993 Apr 1;291 ( Pt 1):65-9. [PubMed
]
- Christie DL, Cleverly DR, O'Connor CJ: Human milk bile-salt stimulated lipase. Sequence similarity with rat lysophospholipase and homology with the active site region of cholinesterases. FEBS Lett. 1991 Jan 28;278(2):190-4. [PubMed
]
- Wang CS, Dashti A, Jackson KW, Yeh JC, Cummings RD, Tang J: Isolation and characterization of human milk bile salt-activated lipase C-tail fragment. Biochemistry. 1995 Aug 22;34(33):10639-44. [PubMed
]
- Mechref Y, Chen P, Novotny MV: Structural characterization of the N-linked oligosaccharides in bile salt-stimulated lipase originated from human breast milk. Glycobiology. 1999 Mar;9(3):227-34. [PubMed
]
- Terzyan S, Wang CS, Downs D, Hunter B, Zhang XC: Crystal structure of the catalytic domain of human bile salt activated lipase. Protein Sci. 2000 Sep;9(9):1783-90. [PubMed
]
- Raeder H, Johansson S, Holm PI, Haldorsen IS, Mas E, Sbarra V, Nermoen I, Eide SA, Grevle L, Bjorkhaug L, Sagen JV, Aksnes L, Sovik O, Lombardo D, Molven A, Njolstad PR: Mutations in the CEL VNTR cause a syndrome of diabetes and pancreatic exocrine dysfunction. Nat Genet. 2006 Jan;38(1):54-62. Epub 2005 Dec 20. [PubMed
]
|
| Enzyme 20 Metabolite References |
Not Available |
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
5477 |
| Enzyme 21 Name |
Pancreatic lipase-related protein 2 |
| Enzyme 21 Synonyms |
- PL-RP2
|
| Enzyme 21 Gene Name |
PNLIPRP2 |
| Enzyme 21 Protein Sequence |
>Pancreatic lipase-related protein 2
MLPPWTLGLLLLATVRGKEVCYGQLGCFSDEKPWAGTLQRPVKLLPWSPEDIDTRFLLYT
NENPNNFQLITGTEPDTIEASNFQLDRKTRFIIHGFLDKAEDSWPSDMCKKMFEVEKVNC
ICVDWRHGSRAMYTQAVQNIRVVGAETAFLIQALSTQLGYSLEDVHVIGHSLGAHTAAEA
GRRLGGRVGRITGLDPAGPCFQDEPEEVRLDPSDAVFVDVIHTDSSPIVPSLGFGMSQKV
GHLDFFPNGGKEMPGCKKNVLSTITDIDGIWEGIGGFVSCNHLRSFEYYSSSVLNPDGFL
GYPCASYDEFQESKCFPCPAEGCPKMGHYADQFKGKTSAVEQTFFLNTGESGNFTSWRYK
VSVTLSGKEKVNGYIRIALYGSNENSKQYEIFKGSLKPDASHTCAIDVDFNVGKIQKVKF
LWNKRGINLSEPKLGASQITVQSGEDGTEYNFCSSDTVEENVLQSLYPC
|
| Enzyme 21 Number of Residues |
469 |
| Enzyme 21 Molecular Weight |
51946.3 |
| Enzyme 21 Theoretical pI |
5.11 |
| Enzyme 21 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 21 General Function |
Involved in catalytic activity |
| Enzyme 21 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 21 Pathways |
|
| Enzyme 21 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
Not Available |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
P54317  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
LIPR2_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>1410 bp
ATGCTGCCCCCTTGGACCCTCGGCCTTCTCCTGCTGGCCACAGTCAGAGGAAAAGAGGTC
TGCTACGGACAACTTGGCTGCTTTTCTGATGAAAAACCATGGGCAGGAACCCTTCAGCGA
CCTGTAAAATTACTTCCCTGGTCCCCCGAGGACATTGACACCCGCTTTCTTCTGTACACA
AATGAAAATCCAAACAACTTCCAACTAATCACTGGCACGGAACCAGACACCATTGAGGCT
TCAAACTTCCAACTGGACCGCAAGACACGCTTCATCATCCATGGCTTCTTAGACAAGGCG
GAGGACAGCTGGCCATCGGACATGTGCAAGAAAATGTTTGAAGTGGAGAAGGTGAACTGC
ATCTGTGTGGACTGGAGGCACGGGTCCCGGGCAATGTACACCCAAGCCGTGCAAAACATT
CGGGTTGTTGGGGCGGAGACAGCTTTCTTAATACAAGCACTGTCGACGCAGCTAGGGTAC
AGCCTTGAGGACGTGCATGTCATCGGCCACAGCCTGGGCGCGCACACGGCCGCGGAGGCG
GGCAGGAGGCTGGGGGGCCGCGTGGGCAGGATCACAGGGCTGGATCCAGCAGGGCCGTGC
TTCCAGGATGAACCTGAGGAGGTTCGGTTGGATCCATCTGACGCCGTGTTTGTGGATGTG
ATTCACACAGATTCTTCTCCCATAGTTCCTTCCCTAGGTTTCGGAATGAGCCAAAAGGTG
GGCCATCTGGATTTCTTTCCAAATGGAGGAAAGGAAATGCCCGGATGTAAGAAAAATGTC
CTTTCAACCATTACTGATATTGATGGAATATGGGAAGGAATTGGTGGCTTTGTGTCTTGC
AATCACCTAAGAAGCTTCGAGTATTACTCAAGCAGCGTCCTCAACCCTGATGGCTTCCTG
GGCTATCCCTGTGCCTCCTACGATGAGTTTCAGGAGAGTAAGTGTTTCCCTTGTCCAGCT
GAAGGATGCCCCAAAATGGGGCACTATGCTGACCAATTTAAGGGGAAAACAAGTGCTGTG
GAACAAACCTTTTTCCTGAACACAGGAGAGAGTGGTAACTTTACTAGTTGGAGATATAAG
GTATCAGTCACACTTTCTGGAAAAGAGAAAGTGAATGGGTACATCAGGATTGCTTTGTAT
GGAAGTAATGAAAACTCGAAACAATATGAGATTTTCAAAGGATCCCTCAAACCAGATGCA
AGTCACACGTGTGCTATTGATGTGGATTTTAATGTTGGAAAAATACAGAAAGTTAAATTC
CTCTGGAACAAACGTGGGATAAATCTATCTGAGCCCAAACTGGGGGCTTCCCAAATCACA
GTGCAAAGTGGTGAAGATGGGACTGAGTATAATTTTTGTAGCAGCGACACTGTGGAAGAA
AACGTCTTGCAATCTCTTTACCCTTGTTAA
|
| Enzyme 21 GenBank Gene ID |
M93284  |
| Enzyme 21 GeneCard ID |
PNLIPRP2  |
| Enzyme 21 GenAtlas ID |
PNLIPRP2  |
| Enzyme 21 HGNC ID |
HGNC:9157  |
| Enzyme 21 Chromosome Location |
1 |
| Enzyme 21 Locus |
10q25.3 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Giller T, Buchwald P, Blum-Kaelin D, Hunziker W: Two novel human pancreatic lipase related proteins, hPLRP1 and hPLRP2. Differences in colipase dependence and in lipase activity. J Biol Chem. 1992 Aug 15;267(23):16509-16. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Eydoux C, Spinelli S, Davis TL, Walker JR, Seitova A, Dhe-Paganon S, De Caro A, Cambillau C, Carriere F: Structure of human pancreatic lipase-related protein 2 with the lid in an open conformation. Biochemistry. 2008 Sep 9;47(36):9553-64. Epub 2008 Aug 15. [PubMed
]
|
| Enzyme 21 Metabolite References |
Not Available |
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
5545 |
| Enzyme 22 Name |
Lipoprotein lipase |
| Enzyme 22 Synonyms |
- LPL
|
| Enzyme 22 Gene Name |
LPL |
| Enzyme 22 Protein Sequence |
>Lipoprotein lipase
MESKALLVLTLAVWLQSLTASRGGVAAADQRRDFIDIESKFALRTPEDTAEDTCHLIPGV
AESVATCHFNHSSKTFMVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLSRAQEH
YPVSAGYTKLVGQDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGIAGSLTNKKVNRIT
GLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQ
PGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCSSKEAFEKG
LCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTESETHTNQ
AFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMLKLKWKSDSYFSWSDW
WSSPGFAIQKIRVKAGETQKKVIFCSREKVSHLQKGKAPAVFVKCHDKSLNKKSG
|
| Enzyme 22 Number of Residues |
475 |
| Enzyme 22 Molecular Weight |
53162.1 |
| Enzyme 22 Theoretical pI |
8.26 |
| Enzyme 22 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipoprotein lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 22 General Function |
Involved in catalytic activity |
| Enzyme 22 Specific Function |
The primary function of this lipase is the hydrolysis of triglycerides of circulating chylomicrons and very low density lipoproteins (VLDL). Binding to heparin sulfate proteogylcans at the cell surface is vital to the function. The apolipoprotein, APOC2, acts as a coactivator of LPL activity in the presence of lipids on the luminal surface of vascular endothelium |
| Enzyme 22 Pathways |
|
| Enzyme 22 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
189065397  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
P06858  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
LIPL_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>1428 bp
ATGGAGAGCAAAGCCCTGCTCGTGCTGACTCTGGCCGTGTGGCTCCAGAGTCTGACCGCC
TCCCGCGGAGGGGTGGCCGCCGCCGACCAAAGAAGAGATTTTATCGACATCGAAAGTAAA
TTTGCCCTAAGGACCCCTGAAGACACAGCTGAGGACACTTGCCACCTCATTCCCGGAGTA
GCAGAGTCCGTGGCTACCTGTCATTTCAATCACAGCAGCAAAACCTTCATGGTGATCCAT
GGCTGGACGGTAACAGGAATGTATGAGAGTTGGGTGCCAAAACTTGTGGCCGCCCTGTAC
AAGAGAGAACCAGACTCCAATGTCATTGTGGTGGACTGGCTGTCACGGGCTCAGGAGCAT
TACCCAGTGTCCGCGGGCTACACCAAACTGGTGGGACAGGATGTGGCCCGGTTTATCAAC
TGGATGGAGGAGGAGTTTAACTACCCTCTGGACAATGTCCATCTCTTGGGATACAGCCTT
GGAGCCCATGCTGCTGGCATTGCAGGAAGTCTGACCAATAAGAAAGTCAACAGAATTACT
GGCCTCGATCCAGCTGGACCTAACTTTGAGTATGCAGAAGCCCCGAGTCGTCTTTCTCCT
GATGATGCAGATTTTGTAGACGTCTTACACACATTCACCAGAGGGTCCCCTGGTCGAAGC
ATTGGAATCCAGAAACCAGTTGGGCATGTTGACATTTACCCGAATGGAGGTACTTTTCAG
CCAGGATGTAACATTGGAGAAGCTATCCGCGTGATTGCAGAGAGAGGACTTGGAGATGTG
GACCAGCTAGTGAAGTGCTCCCACGAGCGCTCCATTCATCTCTTCATCGACTCTCTGTTG
AATGAAGAAAATCCAAGTAAGGCCTACAGGTGCAGTTCCAAGGAAGCCTTTGAGAAAGGG
CTCTGCTTGAGTTGTAGAAAGAACCGCTGCAACAATCTGGGCTATGAGATCAATAAAGTC
AGAGCCAAAAGAAGCAGCAAAATGTACCTGAAGACTCGTTCTCAGATGCCCTACAAAGTC
TTCCATTACCAAGTAAAGATTCATTTTTCTGGGACTGAGAGTGAAACCCATACCAATCAG
GCCTTTGAGATTTCTCTGTATGGCACCGTGGCCGAGAGTGAGAACATCCCATTCACTCTG
CCTGAAGTTTCCACAAATAAGACCTACTCCTTCCTAATTTACACAGAGGTAGATATTGGA
GAACTACTCATGTTGAAGCTCAAATGGAAGAGTGATTCATACTTTAGCTGGTCAGACTGG
TGGAGCAGTCCCGGCTTCGCCATTCAGAAGATCAGAGTAAAAGCAGGAGAGACTCAGAAA
AAGGTGATCTTCTGTTCTAGGGAGAAAGTGTCTCATTTGCAGAAAGGAAAGGCACCTGCG
GTATTTGTGAAATGCCATGACAAGTCTCTGAATAAGAAGTCAGGCTGA
|
| Enzyme 22 GenBank Gene ID |
AK312311  |
| Enzyme 22 GeneCard ID |
LPL  |
| Enzyme 22 GenAtlas ID |
LPL  |
| Enzyme 22 HGNC ID |
HGNC:6677  |
| Enzyme 22 Chromosome Location |
8 |
| Enzyme 22 Locus |
8p22 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Wion KL, Kirchgessner TG, Lusis AJ, Schotz MC, Lawn RM: Human lipoprotein lipase complementary DNA sequence. Science. 1987 Mar 27;235(4796):1638-41. [PubMed
]
- Gotoda T, Senda M, Gamou T, Furuichi Y, Oka K: Nucleotide sequence of human cDNA coding for a lipoprotein lipase (LPL) cloned from placental cDNA library. Nucleic Acids Res. 1989 Mar 25;17(6):2351. [PubMed
]
- Takagi A, Ikeda Y, Yamamoto A: DNA sequence of lipoprotein lipase cDNA cloned from human monocytic leukemia THP-1 cells. Nucleic Acids Res. 1990 Nov 11;18(21):6436. [PubMed
]
- Chuat JC, Raisonnier A, Etienne J, Galibert F: The lipoprotein lipase-encoding human gene: sequence from intron-6 to intron-9 and presence in intron-7 of a 40-million-year-old Alu sequence. Gene. 1992 Jan 15;110(2):257-61. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Enerback S, Ohlsson BG, Samuelsson L, Bjursell G: Characterization of the human lipoprotein lipase (LPL) promoter: evidence of two cis-regulatory regions, LP-alpha and LP-beta, of importance for the differentiation-linked induction of the LPL gene during adipogenesis. Mol Cell Biol. 1992 Oct;12(10):4622-33. [PubMed
]
- Zechner R: Rapid and simple isolation procedure for lipoprotein lipase from human milk. Biochim Biophys Acta. 1990 May 1;1044(1):20-5. [PubMed
]
- Lutz EP, Merkel M, Kako Y, Melford K, Radner H, Breslow JL, Bensadoun A, Goldberg IJ: Heparin-binding defective lipoprotein lipase is unstable and causes abnormalities in lipid delivery to tissues. J Clin Invest. 2001 May;107(9):1183-92. [PubMed
]
- Gin P, Beigneux AP, Davies B, Young MF, Ryan RO, Bensadoun A, Fong LG, Young SG: Normal binding of lipoprotein lipase, chylomicrons, and apo-AV to GPIHBP1 containing a G56R amino acid substitution. Biochim Biophys Acta. 2007 Dec;1771(12):1464-8. Epub 2007 Oct 22. [PubMed
]
- Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed
]
- van Tilbeurgh H, Roussel A, Lalouel JM, Cambillau C: Lipoprotein lipase. Molecular model based on the pancreatic lipase x-ray structure: consequences for heparin binding and catalysis. J Biol Chem. 1994 Feb 11;269(6):4626-33. [PubMed
]
- Hata A, Emi M, Luc G, Basdevant A, Gambert P, Iverius PH, Lalouel JM: Compound heterozygote for lipoprotein lipase deficiency: Ser----Thr244 and transition in 3' splice site of intron 2 (AG----AA) in the lipoprotein lipase gene. Am J Hum Genet. 1990 Oct;47(4):721-6. [PubMed
]
- Emi M, Wilson DE, Iverius PH, Wu L, Hata A, Hegele R, Williams RR, Lalouel JM: Missense mutation (Gly----Glu188) of human lipoprotein lipase imparting functional deficiency. J Biol Chem. 1990 Apr 5;265(10):5910-6. [PubMed
]
- Monsalve MV, Henderson H, Roederer G, Julien P, Deeb S, Kastelein JJ, Peritz L, Devlin R, Bruin T, Murthy MR, et al.: A missense mutation at codon 188 of the human lipoprotein lipase gene is a frequent cause of lipoprotein lipase deficiency in persons of different ancestries. J Clin Invest. 1990 Sep;86(3):728-34. [PubMed
]
- Beg OU, Meng MS, Skarlatos SI, Previato L, Brunzell JD, Brewer HB Jr, Fojo SS: Lipoprotein lipaseBethesda: a single amino acid substitution (Ala-176----Thr) leads to abnormal heparin binding and loss of enzymic activity. Proc Natl Acad Sci U S A. 1990 May;87(9):3474-8. [PubMed
]
- Dichek HL, Fojo SS, Beg OU, Skarlatos SI, Brunzell JD, Cutler GB Jr, Brewer HB Jr: Identification of two separate allelic mutations in the lipoprotein lipase gene of a patient with the familial hyperchylomicronemia syndrome. J Biol Chem. 1991 Jan 5;266(1):473-7. [PubMed
]
- Faustinella F, Chang A, Van Biervliet JP, Rosseneu M, Vinaimont N, Smith LC, Chen SH, Chan L: Catalytic triad residue mutation (Asp156----Gly) causing familial lipoprotein lipase deficiency. Co-inheritance with a nonsense mutation (Ser447----Ter) in a Turkish family. J Biol Chem. 1991 Aug 5;266(22):14418-24. [PubMed
]
- Ameis D, Kobayashi J, Davis RC, Ben-Zeev O, Malloy MJ, Kane JP, Lee G, Wong H, Havel RJ, Schotz MC: Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene. J Clin Invest. 1991 Apr;87(4):1165-70. [PubMed
]
- Henderson HE, Ma Y, Hassan MF, Monsalve MV, Marais AD, Winkler F, Gubernator K, Peterson J, Brunzell JD, Hayden MR: Amino acid substitution (Ile194----Thr) in exon 5 of the lipoprotein lipase gene causes lipoprotein lipase deficiency in three unrelated probands. Support for a multicentric origin. J Clin Invest. 1991 Jun;87(6):2005-11. [PubMed
]
- Gotoda T, Yamada N, Kawamura M, Kozaki K, Mori N, Ishibashi S, Shimano H, Takaku F, Yazaki Y, Furuichi Y, et al.: Heterogeneous mutations in the human lipoprotein lipase gene in patients with familial lipoprotein lipase deficiency. J Clin Invest. 1991 Dec;88(6):1856-64. [PubMed
]
- Ma Y, Henderson HE, Murthy V, Roederer G, Monsalve MV, Clarke LA, Normand T, Julien P, Gagne C, Lambert M, et al.: A mutation in the human lipoprotein lipase gene as the most common cause of familial chylomicronemia in French Canadians. N Engl J Med. 1991 Jun 20;324(25):1761-6. [PubMed
]
- Ishimura-Oka K, Faustinella F, Kihara S, Smith LC, Oka K, Chan L: A missense mutation (Trp86----Arg) in exon 3 of the lipoprotein lipase gene: a cause of familial chylomicronemia. Am J Hum Genet. 1992 Jun;50(6):1275-80. [PubMed
]
- Bruin T, Kastelein JJ, Van Diermen DE, Ma Y, Henderson HE, Stuyt PM, Stalenhoef AF, Sturk A, Brunzell JD, Hayden MR: A missense mutation Pro157 Arg in lipoprotein lipase (LPLNijmegen) resulting in loss of catalytic activity. Eur J Biochem. 1992 Sep 1;208(2):267-72. [PubMed
]
- Ma Y, Wilson BI, Bijvoet S, Henderson HE, Cramb E, Roederer G, Ven Murthy MR, Julien P, Bakker HD, Kastelein JJ, et al.: A missense mutation (Asp250----Asn) in exon 6 of the human lipoprotein lipase gene causes chylomicronemia in patients of different ancestries. Genomics. 1992 Jul;13(3):649-53. [PubMed
]
- Ma YH, Bruin T, Tuzgol S, Wilson BI, Roederer G, Liu MS, Davignon J, Kastelein JJ, Brunzell JD, Hayden MR: Two naturally occurring mutations at the first and second bases of codon aspartic acid 156 in the proposed catalytic triad of human lipoprotein lipase. In vivo evidence that aspartic acid 156 is essential for catalysis. J Biol Chem. 1992 Jan 25;267(3):1918-23. [PubMed
]
- Emmerich J, Beg OU, Peterson J, Previato L, Brunzell JD, Brewer HB Jr, Santamarina-Fojo S: Human lipoprotein lipase. Analysis of the catalytic triad by site-directed mutagenesis of Ser-132, Asp-156, and His-241. J Biol Chem. 1992 Feb 25;267(6):4161-5. [PubMed
]
- Hata A, Ridinger DN, Sutherland SD, Emi M, Kwong LK, Shuhua J, Lubbers A, Guy-Grand B, Basdevant A, Iverius PH, et al.: Missense mutations in exon 5 of the human lipoprotein lipase gene. Inactivation correlates with loss of dimerization. J Biol Chem. 1992 Oct 5;267(28):20132-9. [PubMed
]
- Ishimura-Oka K, Semenkovich CF, Faustinella F, Goldberg IJ, Shachter N, Smith LC, Coleman T, Hide WA, Brown WV, Oka K, et al.: A missense (Asp250----Asn) mutation in the lipoprotein lipase gene in two unrelated families with familial lipoprotein lipase deficiency. J Lipid Res. 1992 May;33(5):745-54. [PubMed
]
- Reina M, Brunzell JD, Deeb SS: Molecular basis of familial chylomicronemia: mutations in the lipoprotein lipase and apolipoprotein C-II genes. J Lipid Res. 1992 Dec;33(12):1823-32. [PubMed
]
- Kobayashi J, Sasaki N, Tashiro J, Inadera H, Saito Y, Yoshida S: A missense mutation (Ala334-->Thr) in exon 7 of the lipoprotein lipase gene in a case with type I hyperlipidemia. Biochem Biophys Res Commun. 1993 Mar 31;191(3):1046-54. [PubMed
]
- Haubenwallner S, Horl G, Shachter NS, Presta E, Fried SK, Hofler G, Kostner GM, Breslow JL, Zechner R: A novel missense mutation in the gene for lipoprotein lipase resulting in a highly conservative amino acid substitution (Asp180-->Glu) causes familial chylomicronemia (type I hyperlipoproteinemia). Genomics. 1993 Nov;18(2):392-6. [PubMed
]
- Ma Y, Liu MS, Ginzinger D, Frohlich J, Brunzell JD, Hayden MR: Gene-environment interaction in the conversion of a mild-to-severe phenotype in a patient homozygous for a Ser172-->Cys mutation in the lipoprotein lipase gene. J Clin Invest. 1993 May;91(5):1953-8. [PubMed
]
- Wilson DE, Hata A, Kwong LK, Lingam A, Shuhua J, Ridinger DN, Yeager C, Kaltenborn KC, Iverius PH, Lalouel JM: Mutations in exon 3 of the lipoprotein lipase gene segregating in a family with hypertriglyceridemia, pancreatitis, and non-insulin-dependent diabetes. J Clin Invest. 1993 Jul;92(1):203-11. [PubMed
]
- Bruin T, Tuzgol S, van Diermen DE, Hoogerbrugge-van der Linden N, Brunzell JD, Hayden MR, Kastelein JJ: Recurrent pancreatitis and chylomicronemia in an extended Dutch kindred is caused by a Gly154-->Ser substitution in lipoprotein lipase. J Lipid Res. 1993 Dec;34(12):2109-19. [PubMed
]
- Pepe G, Chimienti G, Resta F, Di Perna V, Tarricone C, Lovecchio M, Colacicco AM, Capurso A: A new Italian case of lipoprotein lipase deficiency: a Leu365- > Val change resulting in loss of enzyme activity. Biochem Biophys Res Commun. 1994 Mar 15;199(2):570-6. [PubMed
]
- Kobayashi J, Inadera H, Fujita Y, Talley G, Morisaki N, Yoshida S, Saito Y, Fojo SS, Brewer HB Jr: A naturally occurring mutation at the second base of codon asparagine 43 in the proposed N-linked glycosylation site of human lipoprotein lipase: in vivo evidence that asparagine 43 is essential for catalysis and secretion. Biochem Biophys Res Commun. 1994 Nov 30;205(1):506-15. [PubMed
]
- Ma Y, Liu MS, Chitayat D, Bruin T, Beisiegel U, Benlian P, Foubert L, De Gennes JL, Funke H, Forsythe I, et al.: Recurrent missense mutations at the first and second base of codon Arg243 in human lipoprotein lipase in patients of different ancestries. Hum Mutat. 1994;3(1):52-8. [PubMed
]
- Bruin T, Tuzgol S, Mulder WJ, van den Ende AE, Jansen H, Hayden MR, Kastelein JJ: A compound heterozygote for lipoprotein lipase deficiency, Val69-->Leu and Gly188-->Glu: correlation between in vitro LPL activity and clinical expression. J Lipid Res. 1994 Mar;35(3):438-45. [PubMed
]
- Ma Y, Ooi TC, Liu MS, Zhang H, McPherson R, Edwards AL, Forsythe IJ, Frohlich J, Brunzell JD, Hayden MR: High frequency of mutations in the human lipoprotein lipase gene in pregnancy-induced chylomicronemia: possible association with apolipoprotein E2 isoform. J Lipid Res. 1994 Jun;35(6):1066-75. [PubMed
]
- Previato L, Guardamagna O, Dugi KA, Ronan R, Talley GD, Santamarina-Fojo S, Brewer HB Jr: A novel missense mutation in the C-terminal domain of lipoprotein lipase (Glu410-->Val) leads to enzyme inactivation and familial chylomicronemia. J Lipid Res. 1994 Sep;35(9):1552-60. [PubMed
]
- Reymer PW, Gagne E, Groenemeyer BE, Zhang H, Forsyth I, Jansen H, Seidell JC, Kromhout D, Lie KE, Kastelein J, et al.: A lipoprotein lipase mutation (Asn291Ser) is associated with reduced HDL cholesterol levels in premature atherosclerosis. Nat Genet. 1995 May;10(1):28-34. [PubMed
]
- Henderson HE, Hassan F, Marais D, Hayden MR: A new mutation destroying disulphide bridging in the C-terminal domain of lipoprotein lipase. Biochem Biophys Res Commun. 1996 Oct 3;227(1):189-94. [PubMed
]
- de Bruin TW, Mailly F, van Barlingen HH, Fisher R, Castro Cabezas M, Talmud P, Dallinga-Thie GM, Humphries SE: Lipoprotein lipase gene mutations D9N and N291S in four pedigrees with familial combined hyperlipidaemia. Eur J Clin Invest. 1996 Aug;26(8):631-9. [PubMed
]
- Wiebusch H, Funke H, Bruin T, Bucher H, von Eckardstein A, Kastelein JJ, Assmann G: Compound heterozygosity for a known (D250N) and a novel (E410K) missense mutation in the C-terminal domain of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):381-3. [PubMed
]
- Wiebusch H, Funke H, Santer R, Richter W, Assmann G: A novel missense (E163G) mutation in the catalytic subunit of lipoprotein lipase causes familial chylomicronemia. Hum Mutat. 1996;8(4):392. [PubMed
]
- Rouis M, Lohse P, Dugi KA, Lohse P, Beg OU, Ronan R, Talley GD, Brunzell JD, Santamarina-Fojo S: Homozygosity for two point mutations in the lipoprotein lipase (LPL) gene in a patient with familial LPL deficiency: LPL(Asp9-->Asn, Tyr262-->His). J Lipid Res. 1996 Mar;37(3):651-61. [PubMed
]
- Benlian P, De Gennes JL, Foubert L, Zhang H, Gagne SE, Hayden M: Premature atherosclerosis in patients with familial chylomicronemia caused by mutations in the lipoprotein lipase gene. N Engl J Med. 1996 Sep 19;335(12):848-54. [PubMed
]
- Foubert L, Bruin T, De Gennes JL, Ehrenborg E, Furioli J, Kastelein J, Benlian P, Hayden M: A single Ser259Arg mutation in the gene for lipoprotein lipase causes chylomicronemia in Moroccans of Berber ancestry. Hum Mutat. 1997;10(3):179-85. [PubMed
]
- Mailly F, Palmen J, Muller DP, Gibbs T, Lloyd J, Brunzell J, Durrington P, Mitropoulos K, Betteridge J, Watts G, Lithell H, Angelico F, Humphries SE, Talmud PJ: Familial lipoprotein lipase (LPL) deficiency: a catalogue of LPL gene mutations identified in 20 patients from the UK, Sweden, and Italy. Hum Mutat. 1997;10(6):465-73. [PubMed
]
- Foubert L, De Gennes JL, Lagarde JP, Ehrenborg E, Raisonnier A, Girardet JP, Hayden MR, Benlian P: Assessment of French patients with LPL deficiency for French Canadian mutations. J Med Genet. 1997 Aug;34(8):672-5. [PubMed
]
- Henderson HE, Bijvoet SM, Mannens MA, Bruin T, Erkelens DW, Hayden MR, Kastelein JJ: Ile225Thr loop mutation in the lipoprotein lipase (LPL) gene is a de novo event. Am J Med Genet. 1998 Jul 24;78(4):313-6. [PubMed
]
- Henderson H, Leisegang F, Hassan F, Hayden M, Marais D: A novel Glu421Lys substitution in the lipoprotein lipase gene in pregnancy-induced hypertriglyceridemic pancreatitis. Clin Chim Acta. 1998 Jan 12;269(1):1-12. [PubMed
]
- Evans D, Wendt D, Ahle S, Guerra A, Beisiegel U: Compound heterozygosity for a new (S259G) and a previously described (G188E) mutation in lipoprotein lipase (LpL) as a cause of chylomicronemia. Mutations in brief no. 183. Online. Hum Mutat. 1998;12(3):217. [PubMed
]
- Zhang Q, Liu Y, Liu BW, Fan P, Cavanna J, Galton DJ: Common genetic variants of lipoprotein lipase and apolipoproteins AI-CIII that relate to coronary artery disease: a study in Chinese and European subjects. Mol Genet Metab. 1998 Jul;64(3):177-83. [PubMed
]
- Nickerson DA, Taylor SL, Weiss KM, Clark AG, Hutchinson RG, Stengard J, Salomaa V, Vartiainen E, Boerwinkle E, Sing CF: DNA sequence diversity in a 9.7-kb region of the human lipoprotein lipase gene. Nat Genet. 1998 Jul;19(3):233-40. [PubMed
]
- Cargill M, Altshuler D, Ireland J, Sklar P, Ardlie K, Patil N, Shaw N, Lane CR, Lim EP, Kalyanaraman N, Nemesh J, Ziaugra L, Friedland L, Rolfe A, Warrington J, Lipshutz R, Daley GQ, Lander ES: Characterization of single-nucleotide polymorphisms in coding regions of human genes. Nat Genet. 1999 Jul;22(3):231-8. [PubMed
]
- Takagi A, Ikeda Y, Takeda E, Yamamoto A: A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a Japanese patient with familial LPL deficiency. Biochim Biophys Acta. 2000 Nov 15;1502(3):433-46. [PubMed
]
- Ikeda Y, Goji K, Takagi A: A compound heterozygote for a novel missense mutation (G105R) in exon 3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in a Japanese infant with hyperchylomicronaemia. Clin Sci (Lond). 2000 Dec;99(6):569-78. [PubMed
]
- Hoffmann MM, Jacob S, Luft D, Schmulling RM, Rett K, Marz W, Haring HU, Matthaei S: Type I hyperlipoproteinemia due to a novel loss of function mutation of lipoprotein lipase, Cys(239)-->Trp, associated with recurrent severe pancreatitis. J Clin Endocrinol Metab. 2000 Dec;85(12):4795-8. [PubMed
]
- Holzl B, Kraft HG, Wiebusch H, Sandhofer A, Patsch J, Sandhofer F, Paulweber B: Two novel mutations in the lipoprotein lipase gene in a family with marked hypertriglyceridemia in heterozygous carriers. Potential interaction with the polymorphic marker D1S104 on chromosome 1q21-q23. J Lipid Res. 2000 May;41(5):734-41. [PubMed
]
- Ikeda Y, Takagi A, Nakata Y, Sera Y, Hyoudou S, Hamamoto K, Nishi Y, Yamamoto A: Novel compound heterozygous mutations for lipoprotein lipase deficiency. A G-to-T transversion at the first position of exon 5 causing G154V missense mutation and a 5' splice site mutation of intron 8. J Lipid Res. 2001 Jul;42(7):1072-81. [PubMed
]
- Chan LY, Lam CW, Mak YT, Tomlinson B, Tsang MW, Baum L, Masarei JR, Pang CP: Genotype-phenotype studies of six novel LPL mutations in Chinese patients with hypertriglyceridemia. Hum Mutat. 2002 Sep;20(3):232-3. [PubMed
]
- Saika Y, Sakai N, Takahashi M, Maruyama T, Kihara S, Ouchi N, Ishigami M, Hiraoka H, Nakamura T, Yamashita S, Matsuzawa Y: Novel LPL mutation (L303F) found in a patient associated with coronary artery disease and severe systemic atherosclerosis. Eur J Clin Invest. 2003 Mar;33(3):216-22. [PubMed
]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed
]
- Abifadel M, Jambart S, Allard D, Rabes JP, Varret M, Derre A, Chouery E, Salem N, Junien C, Aydenian H, Boileau C: Identification of the first Lebanese mutation in the LPL gene and description of a rapid detection method. Clin Genet. 2004 Feb;65(2):158-61. [PubMed
]
- Kavazarakis E, Stabouli S, Gourgiotis D, Roumeliotou K, Traeger-Synodinos J, Bossios A, Fretzayas A, Kanavakis E: Severe hypertriglyceridaemia in a Greek infant: a clinical, biochemical and genetic study. Eur J Pediatr. 2004 Aug;163(8):462-6. Epub 2004 Jun 5. [PubMed
]
- Maruyama T, Yamashita S, Matsuzawa Y, Bujo H, Takahashi K, Saito Y, Ishibashi S, Ohashi K, Shionoiri F, Gotoda T, Yamada N, Kita T: Mutations in Japanese subjects with primary hyperlipidemia--results from the Research Committee of the Ministry of Health and Welfare of Japan since 1996--. J Atheroscler Thromb. 2004;11(3):131-45. [PubMed
]
- Santer R, Gokcay G, Demirkol M, Gal A, Lukacs Z: Hyperchylomicronaemia due to lipoprotein lipase deficiency as a cause of false-positive newborn screening for biotinidase deficiency. J Inherit Metab Dis. 2005;28(2):137-40. [PubMed
]
|
| Enzyme 22 Metabolite References |
Not Available |
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
5744 |
| Enzyme 23 Name |
Liver carboxylesterase 1 |
| Enzyme 23 Synonyms |
- Acyl-coenzyme A:cholesterol acyltransferase
- ACAT
- Brain carboxylesterase hBr1
- Cocaine carboxylesterase
- Egasyn
- HMSE
- Monocyte/macrophage serine esterase
- Retinyl ester hydrolase
- REH
- Serine esterase 1
- Triacylglycerol hydrolase
- TGH
|
| Enzyme 23 Gene Name |
CES1 |
| Enzyme 23 Protein Sequence |
>Liver carboxylesterase 1
MWLRAFILATLSASAAWGHPSSPPVVDTVHGKVLGKFVSLEGFAQPVAIFLGIPFAKPPL
GPLRFTPPQPAEPWSFVKNATSYPPMCTQDPKAGQLLSELFTNRKENIPLKLSEDCLYLN
IYTPADLTKKNRLPVMVWIHGGGLMVGAASTYDGLALAAHENVVVVTIQYRLGIWGFFST
GDEHSRGNWGHLDQVAALRWVQDNIASFGGNPGSVTIFGESAGGESVSVLVLSPLAKNLF
HRAISESGVALTSVLVKKGDVKPLAEQIAITAGCKTTTSAVMVHCLRQKTEEELLETTLK
MKFLSLDLQGDPRESQPLLGTVIDGMLLLKTPEELQAERNFHTVPYMVGINKQEFGWLIP
MQLMSYPLSEGQLDQKTAMSLLWKSYPLVCIAKELIPEATEKYLGGTDDTVKKKDLFLDL
IADVMFGVPSVIVARNHRDAGAPTYMYEFQYRPSFSSDMKPKTVIGDHGDELFSVFGAPF
LKEGASEEEIRLSKMVMKFWANFARNGNPNGEGLPHWPEYNQKEGYLQIGANTQAAQKLK
DKEVAFWTNLFAKKAVEKPPQTEHIEL
|
| Enzyme 23 Number of Residues |
567 |
| Enzyme 23 Molecular Weight |
62520.6 |
| Enzyme 23 Theoretical pI |
6.58 |
| Enzyme 23 GO Classification |
Not Available |
| Enzyme 23 General Function |
Lipid transport and metabolism |
| Enzyme 23 Specific Function |
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Hydrolyzes aromatic and aliphatic esters, but has no catalytic activity toward amides or a fatty acyl-CoA ester. Hydrolyzes the methyl ester group of cocaine to form benzoylecgonine. Catalyzes the transesterification of cocaine to form cocaethylene. Displays fatty acid ethyl ester synthase activity, catalyzing the ethyl esterification of oleic acid to ethyloleate |
| Enzyme 23 Pathways |
|
| Enzyme 23 Reactions |
- a carboxylic ester + H2O = an alcohol + a carboxylate [RN:R00630]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
Not Available |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
P23141  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
EST1_HUMAN  |
| Enzyme 23 PDB ID |
1MX1  |
| Enzyme 23 PDB File |
Show |
| Enzyme 23 3D Structure |
|
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>1704 bp
ATGTGGCTCCGTGCCTTTATCCTGGCCACTCTCTCTGCTTCCGCGGCTTGGGGGCATCCG
TCCTCGCCACCTGTGGTGGACACCGTGCATGGCAAAGTGCTGGGGAAGTTCGTCAGCTTA
GAAGGATTTGCACAGCCTGTGGCCATTTTCCTGGGAATCCCTTTTGCCAAGCCGCCTCTT
GGACCCCTGAGGTTTACTCCACCGCAGCCTGCAGAACCATGGAGCTTTGTGAAGAATGCC
ACCTCGTACCCTCCTATGTGCACCCAAGATCCCAAGGCGGGGCAGTTACTCTCAGAGCTA
TTTACAAACCGAAAGGAGAACATTCCTCTCAAGCTTTCTGAAGACTGTCTTTACCTCAAT
ATTTACACTCCTGCTGACTTGACCAAGAAAAACAGGCTGCCGGTGATGGTGTGGATCCAC
GGAGGGGGGCTGATGGTGGGTGCGGCATCAACCTATGATGGGCTGGCCCTTGCTGCCCAT
GAAAACGTGGTGGTGGTGACCATTCAATATCGCCTGGGCATCTGGGGATTCTTCAGCACA
GGGGATGAACACAGCCGGGGGAACTGGGGTCACCTGGACCAGGTGGCTGCCCTGCGCTGG
GTCCAGGACAACATTGCCAGCTTTGGAGGGAACCCAGGCTCTGTGACCATCTTTGGAGAG
TCAGCGGGAGGAGAAAGTGTCTCTGTTCTTGTTTTGTCTCCATTGGCCAAGAACCTCTTC
CACCGGGCCATTTCTGAGAGTGGCGTGGCCCTCACTTCTGTTCTGGTGAAGAAAGGTGAT
GTCAAGCCCTTGGCTGAGCAAATTGCTATCACTGCTGGGTGCAAAACCACCACCTCTGCT
GTCATGGTTCACTGCCTGCGACAGAAGACGGAAGAGGAGCTCTTGGAGACGACATTGAAA
ATGAAATTCTTATCTCTGGACTTACAGGGAGACCCCAGAGAGAGTCAACCCCTTCTGGGC
ACTGTGATTGATGGGATGCTGCTGCTGAAAACACCTGAAGAGCTTCAAGCTGAAAGGAAT
TTCCACACTGTCCCCTACATGGTCGGAATTAACAAGCAGGAGTTTGGCTGGTTGATTCCA
ATGCAGTTGATGAGCTATCCACTCTCCGAAGGGCAACTGGACCAGAAGACAGCCATGTCA
CTCCTGTGGAAGTCCTATCCCCTTGTTTGCATTGCTAAGGAACTGATTCCAGAAGCCACT
GAGAAATACTTAGGAGGAACAGACGACACTGTCAAAAAGAAAGACCTGTTCCTGGACTTG
ATAGCAGATGTGATGTTTGGTGTCCCATCTGTGATTGTGGCCCGGAACCACAGAGATGCT
GGAGCACCCACCTACATGTATGAGTTTCAGTACCGTCCAAGCTTCTCATCAGACATGAAA
CCCAAGACGGTGATAGGAGACCACGGGGATGAGCTCTTCTCCGTCTTTGGGGCCCCATTT
TTAAAAGAGGGTGCCTCAGAAGAGGAGATCAGACTTAGCAAGATGGTGATGAAATTCTGG
GCCAACTTTGCTCGCAATGGAAACCCCAATGGGGAAGGGCTGCCCCACTGGCCAGAGTAC
AACCAGAAGGAAGGGTATCTGCAGATTGGTGCCAACACCCAGGCGGCCCAGAAGCTGAAG
GACAAAGAAGTAGCTTTCTGGACCAACCTCTTTGCCAAGAAGGCAGTGGAGAAGCCACCC
CAGACAGAACACATAGAGCTGTGA
|
| Enzyme 23 GenBank Gene ID |
M73499  |
| Enzyme 23 GeneCard ID |
CES1  |
| Enzyme 23 GenAtlas ID |
CES1  |
| Enzyme 23 HGNC ID |
HGNC:1863  |
| Enzyme 23 Chromosome Location |
1 |
| Enzyme 23 Locus |
16q22.2 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Munger JS, Shi GP, Mark EA, Chin DT, Gerard C, Chapman HA: A serine esterase released by human alveolar macrophages is closely related to liver microsomal carboxylesterases. J Biol Chem. 1991 Oct 5;266(28):18832-8. [PubMed
]
- Kroetz DL, McBride OW, Gonzalez FJ: Glycosylation-dependent activity of baculovirus-expressed human liver carboxylesterases: cDNA cloning and characterization of two highly similar enzyme forms. Biochemistry. 1993 Nov 2;32(43):11606-17. [PubMed
]
- Shibata F, Takagi Y, Kitajima M, Kuroda T, Omura T: Molecular cloning and characterization of a human carboxylesterase gene. Genomics. 1993 Jul;17(1):76-82. [PubMed
]
- Becker A, Bottcher A, Lackner KJ, Fehringer P, Notka F, Aslanidis C, Schmitz G: Purification, cloning, and expression of a human enzyme with acyl coenzyme A: cholesterol acyltransferase activity, which is identical to liver carboxylesterase. Arterioscler Thromb. 1994 Aug;14(8):1346-55. [PubMed
]
- Islam MR, Waheed A, Shah GN, Tomatsu S, Sly WS: Human egasyn binds beta-glucuronidase but neither the esterase active site of egasyn nor the C terminus of beta-glucuronidase is involved in their interaction. Arch Biochem Biophys. 1999 Dec 1;372(1):53-61. [PubMed
]
- Ghosh S: Cholesteryl ester hydrolase in human monocyte/macrophage: cloning, sequencing, and expression of full-length cDNA. Physiol Genomics. 2000 Jan 24;2(1):1-8. [PubMed
]
- Alam M, Ho S, Vance DE, Lehner R: Heterologous expression, purification, and characterization of human triacylglycerol hydrolase. Protein Expr Purif. 2002 Feb;24(1):33-42. [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
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Mori M, Hosokawa M, Ogasawara Y, Tsukada E, Chiba K: cDNA cloning, characterization and stable expression of novel human brain carboxylesterase. FEBS Lett. 1999 Sep 10;458(1):17-22. [PubMed
]
- Brzezinski MR, Abraham TL, Stone CL, Dean RA, Bosron WF: Purification and characterization of a human liver cocaine carboxylesterase that catalyzes the production of benzoylecgonine and the formation of cocaethylene from alcohol and cocaine. Biochem Pharmacol. 1994 Nov 1;48(9):1747-55. [PubMed
]
- Schindler R, Mentlein R, Feldheim W: Purification and characterization of retinyl ester hydrolase as a member of the non-specific carboxylesterase supergene family. Eur J Biochem. 1998 Feb 1;251(3):863-73. [PubMed
]
- Satoh T, Hosokawa M: Molecular aspects of carboxylesterase isoforms in comparison with other esterases. Toxicol Lett. 1995 Dec;82-83:439-45. [PubMed
]
- Alam M, Vance DE, Lehner R: Structure-function analysis of human triacylglycerol hydrolase by site-directed mutagenesis: identification of the catalytic triad and a glycosylation site. Biochemistry. 2002 May 28;41(21):6679-87. [PubMed
]
- Long RM, Calabrese MR, Martin BM, Pohl LR: Cloning and sequencing of a human liver carboxylesterase isoenzyme. Life Sci. 1991;48(11):PL43-9. [PubMed
]
- Zschunke F, Salmassi A, Kreipe H, Buck F, Parwaresch MR, Radzun HJ: cDNA cloning and characterization of human monocyte/macrophage serine esterase-1. Blood. 1991 Jul 15;78(2):506-12. [PubMed
]
- Riddles PW, Richards LJ, Bowles MR, Pond SM: Cloning and analysis of a cDNA encoding a human liver carboxylesterase. Gene. 1991 Dec 15;108(2):289-92. [PubMed
]
- Zhu HJ, Patrick KS, Yuan HJ, Wang JS, Donovan JL, DeVane CL, Malcolm R, Johnson JA, Youngblood GL, Sweet DH, Langaee TY, Markowitz JS: Two CES1 gene mutations lead to dysfunctional carboxylesterase 1 activity in man: clinical significance and molecular basis. Am J Hum Genet. 2008 Jun;82(6):1241-8. Epub 2008 May 15. [PubMed
]
- Bencharit S, Morton CL, Hyatt JL, Kuhn P, Danks MK, Potter PM, Redinbo MR: Crystal structure of human carboxylesterase 1 complexed with the Alzheimer's drug tacrine: from binding promiscuity to selective inhibition. Chem Biol. 2003 Apr;10(4):341-9. [PubMed
]
- Bencharit S, Morton CL, Xue Y, Potter PM, Redinbo MR: Structural basis of heroin and cocaine metabolism by a promiscuous human drug-processing enzyme. Nat Struct Biol. 2003 May;10(5):349-56. [PubMed
]
|
| Enzyme 23 Metabolite References |
Not Available |
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
5745 |
| Enzyme 24 Name |
Carboxylesterase 2 |
| Enzyme 24 Synonyms |
- CE-2
- hCE-2
|
| Enzyme 24 Gene Name |
CES2 |
| Enzyme 24 Protein Sequence |
>Carboxylesterase 2
MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLG
IPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMS
EDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLG
VLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVS
PISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEI
LAINKPFKMIPGVVDGVFLPRHPQELLASADFQPVPSIVGVNNNEFGWLIPKVMRIYDTQ
KEMDREASQAALQKMLTLLMLPPTFGDLLREEYIGDNGDPQTLQAQFQEMMADSMFVIPA
LQVAHFQCSRAPVYFYEFQHQPSWLKNIRPPHMKADHGDELPFVFRSFFGGNYIKFTEEE
EQLSRKMMKYWANFARNGNPNGEGLPHWPLFDQEEQYLQLNLQPAVGRALKAHRLQFWKK
ALPQKIQELEEPEERHTEL
|
| Enzyme 24 Number of Residues |
559 |
| Enzyme 24 Molecular Weight |
61806.4 |
| Enzyme 24 Theoretical pI |
6.03 |
| Enzyme 24 GO Classification |
Not Available |
| Enzyme 24 General Function |
Lipid transport and metabolism |
| Enzyme 24 Specific Function |
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows high catalytic efficiency for hydrolysis of 4-methyumbelliferyl acetate, heroin and 6-monoacetylmorphine |
| Enzyme 24 Pathways |
|
| Enzyme 24 Reactions |
- a carboxylic ester + H2O = an alcohol + a carboxylate [RN:R00630]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
2058318  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
O00748  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
EST2_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1680 bp
ATGCGGCTGCACAGACTTCGTGCGCGGCTGAGCGCGGTGGCCTGTGGGCTTCTGCTGCTT
CTTGTCCGGGGCCAGGGCCAGGACTCAGCCAGTCCCATCCGGACCACACACACGGGGCAG
GTGCTGGGGAGTCTTGTCCATGTGAAGGGCGCCAATGCCGGGGTCCAAACCTTCCTGGGA
ATTCCATTTGCCAAGCCACCTCTAGGTCCGCTGCGATTTGCACCCCCTGAGCCCCCTGAA
TCTTGGAGTGGTGTGAGGGATGGAACCACCCATCCGGCCATGTGTCTACAGGACCTCACC
GCAGTGGAGTCAGAGTTTCTTAGCCAGTTCAACATGACCTTCCCTTCCGACTCCATGTCT
GAGGACTGCCTGTACCTCAGCATCTACACGCCGGCCCATAGCCATGAAGGCTCTAACCTG
CCGGTGATGGTGTGGATCCACGGTGGTGCGCTTGTTTTTGGCATGGCTTCCTTGTATGAT
GGTTCCATGCTGGCTGCCTTGGAGAACGTGGTGGTGGTCATCATCCAGTACCGCCTGGGT
GTCCTGGGCTTCTTCAGCACTGGAGACAAGCACGCAACCGGCAACTGGGGCTACCTGGAC
CAAGTGGCTGCACTACGCTGGGTCCAGCAGAATATCGCCCACTTTGGAGGCAACCCTGAC
CGTGTCACCATTTTTGGCGAGTCTGCGGGTGGCACGAGTGTGTCTTCGCTTGTTGTGTCC
CCCATATCCCAAGGACTCTTCCACGGAGCCATCATGGAGAGTGGCGTGGCCCTCCTGCCC
GGCCTCATTGCCAGCTCAGCTGATGTCATCTCCACGGTGGTGGCCAACCTGTCTGCCTGT
GACCAAGTTGACTCTGAGGCCCTGGTGGGCTGCCTGCGGGGCAAGAGTAAAGAGGAGATT
CTTGCAATTAACAAGCCTTTCAAGATGATCCCCGGAGTGGTGGATGGGGTCTTCCTGCCC
AGGCACCCCCAGGAGCTGCTGGCCTCTGCCGACTTTCAGCCTGTCCCTAGCATTGTTGGT
GTCAACAACAATGAATTCGGCTGGCTCATCCCCAAGGTCATGAGGATCTATGATACCCAG
AAGGAAATGGACAGAGAGGCCTCCCAGGCTGCTCTGCAGAAAATGTTAACGCTGCTGATG
TTGCCTCCTACATTTGGTGACCTGCTGAGGGAGGAGTACATTGGGGACAATGGGGATCCC
CAGACCCTCCAAGCGCAGTTCCAGGAGATGATGGCGGACTCCATGTTTGTGATCCCTGCA
CTCCAAGTAGCACATTTTCAGTGTTCCCGGGCCCCTGTGTACTTCTACGAGTTCCAGCAT
CAGCCCAGCTGGCTCAAGAACATCAGGCCACCGCACATGAAGGCAGACCATGGTGATGAG
CTTCCTTTTGTTTTCAGAAGTTTCTTTGGGGGCAACTACATTAAATTCACTGAGGAAGAG
GAGCAGCTAAGCAGGAAGATGATGAAGTACTGGGCCAACTTTGCGAGAAATGGGAACCCC
AATGGCGAGGGTCTGCCACACTGGCCGCTGTTCGACCAGGAGGAGCAATACCTGCAGCTG
AACCTACAGCCTGCGGTGGGCCGGGCTCTGAAGGCCCACAGGCTCCAGTTCTGGAAGAAG
GCGCTGCCCCAAAAGATCCAGGAGCTCGAGGAGCCTGAAGAGAGACACACAGAGCTGTAG
|
| Enzyme 24 GenBank Gene ID |
Y09616  |
| Enzyme 24 GeneCard ID |
CES2  |
| Enzyme 24 GenAtlas ID |
CES2  |
| Enzyme 24 HGNC ID |
HGNC:1864  |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
16q22.1 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Schwer H, Langmann T, Daig R, Becker A, Aslanidis C, Schmitz G: Molecular cloning and characterization of a novel putative carboxylesterase, present in human intestine and liver. Biochem Biophys Res Commun. 1997 Apr 7;233(1):117-20. [PubMed
]
- Pindel EV, Kedishvili NY, Abraham TL, Brzezinski MR, Zhang J, Dean RA, Bosron WF: Purification and cloning of a broad substrate specificity human liver carboxylesterase that catalyzes the hydrolysis of cocaine and heroin. J Biol Chem. 1997 Jun 6;272(23):14769-75. [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
]
- Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- Saito S, Iida A, Sekine A, Kawauchi S, Higuchi S, Ogawa C, Nakamura Y: Catalog of 680 variations among eight cytochrome p450 ( CYP) genes, nine esterase genes, and two other genes in the Japanese population. J Hum Genet. 2003;48(5):249-70. Epub 2003 Apr 29. [PubMed
]
- Kim SR, Nakamura T, Saito Y, Sai K, Nakajima T, Saito H, Shirao K, Minami H, Ohtsu A, Yoshida T, Saijo N, Ozawa S, Sawada J: Twelve novel single nucleotide polymorphisms in the CES2 gene encoding human carboxylesterase 2 (hCE-2). Drug Metab Pharmacokinet. 2003;18(5):327-32. [PubMed
]
|
| Enzyme 24 Metabolite References |
Not Available |
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
5774 |
| Enzyme 25 Name |
Cholinesterase |
| Enzyme 25 Synonyms |
- Acylcholine acylhydrolase
- Butyrylcholine esterase
- Choline esterase II
- Pseudocholinesterase
|
| Enzyme 25 Gene Name |
BCHE |
| Enzyme 25 Protein Sequence |
>Cholinesterase
MHSKVTIICIRFLFWFLLLCMLIGKSHTEDDIIIATKNGKVRGMNLTVFGGTVTAFLGIP
YAQPPLGRLRFKKPQSLTKWSDIWNATKYANSCCQNIDQSFPGFHGSEMWNPNTDLSEDC
LYLNVWIPAPKPKNATVLIWIYGGGFQTGTSSLHVYDGKFLARVERVIVVSMNYRVGALG
FLALPGNPEAPGNMGLFDQQLALQWVQKNIAAFGGNPKSVTLFGESAGAASVSLHLLSPG
SHSLFTRAILQSGSFNAPWAVTSLYEARNRTLNLAKLTGCSRENETEIIKCLRNKDPQEI
LLNEAFVVPYGTPLSVNFGPTVDGDFLTDMPDILLELGQFKKTQILVGVNKDEGTAFLVY
GAPGFSKDNNSIITRKEFQEGLKIFFPGVSEFGKESILFHYTDWVDDQRPENYREALGDV
VGDYNFICPALEFTKKFSEWGNNAFFYYFEHRSSKLPWPEWMGVMHGYEIEFVFGLPLER
RDNYTKAEEILSRSIVKRWANFAKYGNPNETQNNSTSWPVFKSTEQKYLTLNTESTRIMT
KLRAQQCRFWTSFFPKVLEMTGNIDEAEWEWKAGFHRWNNYMMDWKNQFNDYTSKKESCV
GL
|
| Enzyme 25 Number of Residues |
602 |
| Enzyme 25 Molecular Weight |
68417.6 |
| Enzyme 25 Theoretical pI |
7.47 |
| Enzyme 25 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- cholinesterase activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
| — |
| Component |
|
|
| Enzyme 25 General Function |
Involved in carboxylesterase activity |
| Enzyme 25 Specific Function |
Esterase with broad substrate specificity. Contributes to the inactivation of the neurotransmitter acetylcholine. Can degrade neurotoxic organophosphate esters |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
- an acylcholine + H2O = choline + a carboxylate [RN:R01029]
|
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
180484  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
P06276  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
CHLE_HUMAN  |
| Enzyme 25 PDB ID |
1P0Q  |
| Enzyme 25 PDB File |
Show |
| Enzyme 25 3D Structure |
|
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1809 bp
ATGCATAGCAAAGTCACAATCATATGCATCAGATTTCTCTTTTGGTTTCTTTTGCTCTGC
ATGCTTATTGGGAAGTCACATACTGAAGATGACATCATAATTGCAACAAAGAATGGAAAA
GTCAGAGGGATGAACTTGACAGTTTTTGGTGGCACGGTAACAGCCTTTCTTGGAATTCCC
TATGCACAGCCACCTCTTGGTAGACTTCGATTCAAAAAGCCACAGTCTCTGACCAAGTGG
TCTGATATTTGGAATGCCACAAAATATGCAAATTCTTGCTGTCAGAACATAGATCAAAGT
TTTCCAGGCTTCCATGGATCAGAGATGTGGAACCCAAACACTGACCTCAGTGAAGACTGT
TTATATCTAAATGTATGGATTCCAGCACCTAAACCAAAAAATGCCACTGTATTGATATGG
ATTTATGGTGGTGGTTTTCAAACTGGAACATCATCTTTACATGTTTATGATGGCAAGTTT
CTGGCTCGGGTTGAAAGAGTTATTGTAGTGTCAATGAACTATAGGGTGGGTGCCCTAGGA
TTCTTAGCTTTGCCAGGAAATCCTGAGGCTCCAGGGAACATGGGTTTATTTGATCAACAG
TTGGCTCTTCAGTGGGTTCAAAAAAATATAGCAGCCTTTGGTGGAAATCCTAAAAGTGTA
ACTCTCTTTGGAGAAAGTGCAGGAGCAGCTTCAGTTAGCCTGCATTTGCTTTCTCCTGGA
AGCCATTCATTGTTCACCAGAGCCATTCTGCAAAGTGGATCCTTTAATGCTCCTTGGGCG
GTAACATCTCTTTATGAAGCTAGGAACAGAACGTTGAACTTAGCTAAATTGACTGGTTGC
TCTAGAGAGAATGAGACTGAAATAATCAAGTGTCTTAGAAATAAAGATCCCCAAGAAATT
CTTCTGAATGAAGCATTTGTTGTCCCCTATGGGACTCCTTTGTCAGTAAACTTTGGTCCG
ACCGTGGATGGTGATTTTCTCACTGACATGCCAGACATATTACTTGAACTTGGACAATTT
AAAAAAACCCAGATTTTGGTGGGTGTTAATAAAGATGAAGGGACAGCTTTTTTAGTCTAT
GGTGCTCCTGGCTTCAGCAAAGATAACAATAGTATCATAACTAGAAAAGAATTTCAGGAA
GGTTTAAAAATATTTTTTCCAGGAGTGAGTGAGTTTGGAAAGGAATCCATCCTTTTTCAT
TACACAGACTGGGTAGATGATCAGAGACCTGAAAACTACCGTGAGGCCTTGGGTGATGTT
GTTGGGGATTATAATTTCATATGCCCTGCCTTGGAGTTCACCAAGAAGTTCTCAGAATGG
GGAAATAATGCCTTTTTCTACTATTTTGAACACCGATCCTCCAAACTTCCGTGGCCAGAA
TGGATGGGAGTGATGCATGGCTATGAAATTGAATTTGTCTTTGGTTTACCTCTGGAAAGA
AGAGATAATTACACAAAAGCCGAGGAAATTTTGAGTAGATCCATAGTGAAACGGTGGGCA
AATTTTGCAAAATATGGGAATCCAAATGAGACTCAGAACAATAGCACAAGCTGGCCTGTC
TTCAAAAGCACTGAACAAAAATATCTAACCTTGAATACAGAGTCAACAAGAATAATGACG
AAACTACGTGCTCAACAATGTCGATTCTGGACATCATTTTTTCCAAAAGTCTTGGAAATG
ACAGGAAATATTGATGAAGCAGAATGGGAGTGGAAAGCAGGATTCCATCGCTGGAACAAT
TACATGATGGACTGGAAAAATCAATTTAACGATTACACTAGCAAGAAAGAAAGTTGTGTG
GGTCTCTAA
|
| Enzyme 25 GenBank Gene ID |
M16541  |
| Enzyme 25 GeneCard ID |
BCHE  |
| Enzyme 25 GenAtlas ID |
BCHE  |
| Enzyme 25 HGNC ID |
HGNC:983  |
| Enzyme 25 Chromosome Location |
3 |
| Enzyme 25 Locus |
3q26.1-q26.2 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Arpagaus M, Kott M, Vatsis KP, Bartels CF, La Du BN, Lockridge O: Structure of the gene for human butyrylcholinesterase. Evidence for a single copy. Biochemistry. 1990 Jan 9;29(1):124-31. [PubMed
]
- Prody CA, Zevin-Sonkin D, Gnatt A, Goldberg O, Soreq H: Isolation and characterization of full-length cDNA clones coding for cholinesterase from fetal human tissues. Proc Natl Acad Sci U S A. 1987 Jun;84(11):3555-9. [PubMed
]
- McTiernan C, Adkins S, Chatonnet A, Vaughan TA, Bartels CF, Kott M, Rosenberry TL, La Du BN, Lockridge O: Brain cDNA clone for human cholinesterase. Proc Natl Acad Sci U S A. 1987 Oct;84(19):6682-6. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lockridge O, Bartels CF, Vaughan TA, Wong CK, Norton SE, Johnson LL: Complete amino acid sequence of human serum cholinesterase. J Biol Chem. 1987 Jan 15;262(2):549-57. [PubMed
]
- Lockridge O, Adkins S, La Du BN: Location of disulfide bonds within the sequence of human serum cholinesterase. J Biol Chem. 1987 Sep 25;262(27):12945-52. [PubMed
]
- Bunkenborg J, Pilch BJ, Podtelejnikov AV, Wisniewski JR: Screening for N-glycosylated proteins by liquid chromatography mass spectrometry. Proteomics. 2004 Feb;4(2):454-65. [PubMed
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
- Chilukuri N, Duysen EG, Parikh K, diTargiani R, Doctor BP, Lockridge O, Saxena A: Adenovirus-transduced human butyrylcholinesterase in mouse blood functions as a bioscavenger of chemical warfare nerve agents. Mol Pharmacol. 2009 Sep;76(3):612-7. Epub 2009 Jun 19. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Amitay M, Shurki A: The structure of G117H mutant of butyrylcholinesterase: nerve agents scavenger. Proteins. 2009 Nov 1;77(2):370-7. [PubMed
]
- Nicolet Y, Lockridge O, Masson P, Fontecilla-Camps JC, Nachon F: Crystal structure of human butyrylcholinesterase and of its complexes with substrate and products. J Biol Chem. 2003 Oct 17;278(42):41141-7. Epub 2003 Jul 17. [PubMed
]
- Nachon F, Asojo OA, Borgstahl GE, Masson P, Lockridge O: Role of water in aging of human butyrylcholinesterase inhibited by echothiophate: the crystal structure suggests two alternative mechanisms of aging. Biochemistry. 2005 Feb 1;44(4):1154-62. [PubMed
]
- Ngamelue MN, Homma K, Lockridge O, Asojo OA: Crystallization and X-ray structure of full-length recombinant human butyrylcholinesterase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Sep 1;63(Pt 9):723-7. Epub 2007 Aug 10. [PubMed
]
- Frasco MF, Colletier JP, Weik M, Carvalho F, Guilhermino L, Stojan J, Fournier D: Mechanisms of cholinesterase inhibition by inorganic mercury. FEBS J. 2007 Apr;274(7):1849-61. Epub 2007 Mar 12. [PubMed
]
- Carletti E, Li H, Li B, Ekstrom F, Nicolet Y, Loiodice M, Gillon E, Froment MT, Lockridge O, Schopfer LM, Masson P, Nachon F: Aging of cholinesterases phosphylated by tabun proceeds through O-dealkylation. J Am Chem Soc. 2008 Nov 26;130(47):16011-20. [PubMed
]
- Carletti E, Aurbek N, Gillon E, Loiodice M, Nicolet Y, Fontecilla-Camps JC, Masson P, Thiermann H, Nachon F, Worek F: Structure-activity analysis of aging and reactivation of human butyrylcholinesterase inhibited by analogues of tabun. Biochem J. 2009 Jun 12;421(1):97-106. [PubMed
]
- McGuire MC, Nogueira CP, Bartels CF, Lightstone H, Hajra A, Van der Spek AF, Lockridge O, La Du BN: Identification of the structural mutation responsible for the dibucaine-resistant (atypical) variant form of human serum cholinesterase. Proc Natl Acad Sci U S A. 1989 Feb;86(3):953-7. [PubMed
]
- Bartels CF, James K, La Du BN: DNA mutations associated with the human butyrylcholinesterase J-variant. Am J Hum Genet. 1992 May;50(5):1104-14. [PubMed
]
- Nogueira CP, Bartels CF, McGuire MC, Adkins S, Lubrano T, Rubinstein HM, Lightstone H, Van der Spek AF, Lockridge O, La Du BN: Identification of two different point mutations associated with the fluoride-resistant phenotype for human butyrylcholinesterase. Am J Hum Genet. 1992 Oct;51(4):821-8. [PubMed
]
- Hada T, Muratani K, Ohue T, Imanishi H, Moriwaki Y, Itoh M, Amuro Y, Higashino K: A variant serum cholinesterase and a confirmed point mutation at Gly-365 to Arg found in a patient with liver cirrhosis. Intern Med. 1992 Mar;31(3):357-62. [PubMed
]
- Jensen FS, Bartels CF, La Du BN: Structural basis of the butyrylcholinesterase H-variant segregating in two Danish families. Pharmacogenetics. 1992 Oct;2(5):234-40. [PubMed
]
- Maekawa M, Sudo K, Kanno T, Kotani K, Dey DC, Ishikawa J, Izumi M, Etoh K: Genetic basis of the silent phenotype of serum butyrylcholinesterase in three compound heterozygotes. Clin Chim Acta. 1995 Feb 28;235(1):41-57. [PubMed
]
- Iida S, Kinoshita M, Fujii H, Moriyama Y, Nakamura Y, Yura N, Moriwaki K: Mutations of human butyrylcholinesterase gene in a family with hypocholinesterasemia. Hum Mutat. 1995;6(4):349-51. [PubMed
]
- Primo-Parmo SL, Bartels CF, Wiersema B, van der Spek AF, Innis JW, La Du BN: Characterization of 12 silent alleles of the human butyrylcholinesterase (BCHE) gene. Am J Hum Genet. 1996 Jan;58(1):52-64. [PubMed
]
- Hidaka K, Iuchi I, Tomita M, Watanabe Y, Minatogawa Y, Iwasaki K, Gotoh K, Shimizu C: Genetic analysis of a Japanese patient with butyrylcholinesterase deficiency. Ann Hum Genet. 1997 Nov;61(Pt 6):491-6. [PubMed
]
- Sudo K, Maekawa M, Akizuki S, Magara T, Ogasawara H, Tanaka T: Human butyrylcholinesterase L330I mutation belongs to a fluoride-resistant gene, by expression in human fetal kidney cells. Biochem Biophys Res Commun. 1997 Nov 17;240(2):372-5. [PubMed
]
- Maekawa M, Sudo K, Dey DC, Ishikawa J, Izumi M, Kotani K, Kanno T: Genetic mutations of butyrylcholine esterase identified from phenotypic abnormalities in Japan. Clin Chem. 1997 Jun;43(6 Pt 1):924-9. [PubMed
]
- Primo-Parmo SL, Lightstone H, La Du BN: Characterization of an unstable variant (BChE115D) of human butyrylcholinesterase. Pharmacogenetics. 1997 Feb;7(1):27-34. [PubMed
]
- Sakamoto N, Hidaka K, Fujisawa T, Maeda M, Iuchi I: Identification of a point mutation associated with a silent phenotype of human serum butyrylcholinesterase--a case of familial cholinesterasemia. Clin Chim Acta. 1998 Jun 22;274(2):159-66. [PubMed
]
- Asanuma K, Yagihashi A, Uehara N, Kida T, Watanabe N: Three point mutations of human butyrylcholinesterase in a Japanese family and the alterations of three-dimensional structure. Clin Chim Acta. 1999 May;283(1-2):33-42. [PubMed
]
- Boeck AT, Fry DL, Sastre A, Lockridge O: Naturally occurring mutation, Asp70his, in human butyrylcholinesterase. Ann Clin Biochem. 2002 Mar;39(Pt 2):154-6. [PubMed
]
- Yen T, Nightingale BN, Burns JC, Sullivan DR, Stewart PM: Butyrylcholinesterase (BCHE) genotyping for post-succinylcholine apnea in an Australian population. Clin Chem. 2003 Aug;49(8):1297-308. [PubMed
]
- On-Kei Chan A, Lam CW, Tong SF, Man Tung C, Yung K, Chan YW, Au KM, Yuen YP, Hung CT, Ng KP, Shek CC: Novel mutations in the BCHE gene in patients with no butyrylcholinesterase activity. Clin Chim Acta. 2005 Jan;351(1-2):155-9. [PubMed
]
- Manoharan I, Wieseler S, Layer PG, Lockridge O, Boopathy R: Naturally occurring mutation Leu307Pro of human butyrylcholinesterase in the Vysya community of India. Pharmacogenet Genomics. 2006 Jul;16(7):461-8. [PubMed
]
- Gatke MR, Bundgaard JR, Viby-Mogensen J: Two novel mutations in the BCHE gene in patients with prolonged duration of action of mivacurium or succinylcholine during anaesthesia. Pharmacogenet Genomics. 2007 Nov;17(11):995-9. [PubMed
]
|
| Enzyme 25 Metabolite References |
Not Available |
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
5778 |
| Enzyme 26 Name |
Cytosolic phospholipase A2 gamma |
| Enzyme 26 Synonyms |
- cPLA2-gamma
- Phospholipase A2 group IVC
|
| Enzyme 26 Gene Name |
PLA2G4C |
| Enzyme 26 Protein Sequence |
>Cytosolic phospholipase A2 gamma
MGSSEVSIIPGLQKEEKAAVERRRLHVLKALKKLRIEADEAPVVAVLGSGGGLRAHIACL
GVLSEMKEQGLLDAVTYLAGVSGSTWAISSLYTNDGDMEALEADLKHRFTRQEWDLAKSL
QKTIQAARSENYSLTDFWAYMVISKQTRELPESHLSNMKKPVEEGTLPYPIFAAIDNDLQ
PSWQEARAPETWFEFTPHHAGFPALGAFVSITHFGSKFKKGRLVRTHPERDLTFLRGLWG
SALGNTEVIREYIFDQLRNLTLKGLWRRAVANAKSIGHLIFARLLRLQESSQGEHPPPED
EGGEPEHTWLTEMLENWTRTSLEKQEQPHEDPERKGSLSNLMDFVKKTGICASKWEWGTT
HNFLYKHGGIRDKIMSSRKHLHLVDAGLAINTPFPLVLPPTREVHLILSFDFSAGDPFET
IRATTDYCRRHKIPFPQVEEAELDLWSKAPASCYILKGETGPVVMHFPLFNIDACGGDIE
AWSDTYDTFKLADTYTLDVVVLLLALAKKNVRENKKKILRELMNVAGLYYPKDSARSCCL
A
|
| Enzyme 26 Number of Residues |
541 |
| Enzyme 26 Molecular Weight |
60948.1 |
| Enzyme 26 Theoretical pI |
6.93 |
| Enzyme 26 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- phospholipase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in metabolic process |
| Enzyme 26 Specific Function |
Has a preference for arachidonic acid at the sn-2 position of phosphatidylcholine as compared with palmitic acid |
| Enzyme 26 Pathways |
|
| Enzyme 26 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
226693354  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q9UP65  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
PA24C_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1626 bp
ATGGGAAGCTCTGAAGTTTCCATAATTCCTGGGCTCCAGAAAGAAGAAAAGGCGGCCGTG
GAGAGACGAAGACTTCATGTGCTGAAAGCTCTGAAGAAGCTAAGGATTGAGGCTGATGAG
GCCCCAGTTGTTGCTGTGCTGGGCTCAGGCGGAGGACTGCGGGCTCACATTGCCTGCCTT
GGGGTCCTGAGTGAGATGAAAGAACAGGGCCTGTTGGATGCCGTCACGTACCTCGCAGGG
GTCTCTGGATCCACTTGGGCAATATCTTCTCTCTACACCAATGATGGTGACATGGAAGCT
CTCGAGGCTGACCTGAAACATCGATTTACCCGACAGGAGTGGGACTTGGCTAAGAGCCTA
CAGAAAACCATCCAAGCAGCGAGGTCTGAGAATTACTCTCTGACCGACTTCTGGGCCTAC
ATGGTTATCTCTAAGCAAACCAGAGAACTGCCGGAGTCTCATTTGTCCAATATGAAGAAG
CCCGTGGAAGAAGGGACACTACCCTACCCAATATTTGCAGCCATTGACAATGACCTGCAA
CCTTCCTGGCAGGAGGCAAGAGCACCAGAGACCTGGTTCGAGTTCACCCCTCACCACGCT
GGCTTCTCTGCACTGGGGGCCTTTGTTTCCATAACCCACTTCGGAAGCAAATTCAAGAAG
GGAAGACTGGTCAGAACTCACCCTGAGAGAGACCTGACTTTCCTGAGAGGTTTATGGGGA
AGTGCTCTTGGTAACACTGAAGTCATTAGGGAATACATTTTTGACCAGTTAAGGAATCTG
ACCCTGAAAGGTTTATGGAGAAGGGCTGTTGCTAATGCTAAAAGCATTGGACACCTTATT
TTTGCCCGATTACTGAGGCTGCAAGAAAGTTCACAAGGGGAACATCCTCCCCCAGAAGAT
GAAGGCGGTGAGCCTGAACACACCTGGCTGACTGAGATGCTCGAGAATTGGACCAGGACC
TCCCTGGAAAAGCAGGAGCAGCCCCATGAGGACCCCGAAAGGAAAGGCTCACTCAGTAAC
TTGATGGATTTTGTGAAGAAAACAGGCATTTGCGCTTCAAAGTGGGAATGGGGGACCACT
CACAACTTCCTGTACAAACACGGTGGCATCCGGGACAAGATAATGAGCAGCCGGAAGCAC
CTCCACCTGGTGGATGCTGGTTTAGCCATCAACACTCCCTTCCCACTCGTGCTGCCCCCG
ACGCGGGAGGTTCACCTCATCCTCTCCTTCGACTTCAGTGCCGGAGATCCTTTCGAGACC
ATCCGGGCTACCACTGACTACTGCCGCCGCCACAAGATCCCCTTTCCCCAAGTAGAAGAG
GCTGAGCTGGATTTGTGGTCCAAGGCCCCCGCCAGCTGCTACATCCTGAAAGGAGAAACT
GGACCAGTGGTGATGCATTTTCCCCTGTTCAACATAGATGCCTGTGGAGGTGATATTGAG
GCATGGAGTGACACATACGACACATTCAAGCTTGCTGACACCTACACTCTAGATGTGGTG
GTGCTACTCTTGGCATTAGCCAAGAAGAATGTCAGGGAAAACAAGAAGAAGATCCTTAGA
GAGTTGATGAACGTGGCCGGGCTCTACTACCCGAAGGATAGTGCCCGAAGTTGCTGCTTG
GCATAG
|
| Enzyme 26 GenBank Gene ID |
NM_003706.2  |
| Enzyme 26 GeneCard ID |
PLA2G4C  |
| Enzyme 26 GenAtlas ID |
PLA2G4C  |
| Enzyme 26 HGNC ID |
HGNC:9037  |
| Enzyme 26 Chromosome Location |
1 |
| Enzyme 26 Locus |
19q13.3 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Underwood KW, Song C, Kriz RW, Chang XJ, Knopf JL, Lin LL: A novel calcium-independent phospholipase A2, cPLA2-gamma, that is prenylated and contains homology to cPLA2. J Biol Chem. 1998 Aug 21;273(34):21926-32. [PubMed
]
- Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Jenkins CM, Han X, Yang J, Mancuso DJ, Sims HF, Muslin AJ, Gross RW: Purification of recombinant human cPLA2 gamma and identification of C-terminal farnesylation, proteolytic processing, and carboxymethylation by MALDI-TOF-TOF analysis. Biochemistry. 2003 Oct 14;42(40):11798-807. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
5781 |
| Enzyme 27 Name |
Hormone-sensitive lipase |
| Enzyme 27 Synonyms |
- HSL
|
| Enzyme 27 Gene Name |
LIPE |
| Enzyme 27 Protein Sequence |
>Hormone-sensitive lipase
MEPGSKSVSRSDWQPEPHQRPITPLEPGPEKTPIAQPESKTLQGSNTQQKPASNQRPLTQ
QETPAQHDAESQKEPRAQQKSASQEEFLAPQKPAPQQSPYIQRVLLTQQEAASQQGPGLG
KESITQQEPALRQRHVAQPGPGPGEPPPAQQEAESTPAAQAKPGAKREPSAPTESTSQET
PEQSDKQTTPVQGAKSKQGSLTELGFLTKLQELSIQRSALEWKALSEWVTDSESESDVGS
SSDTDSPATMGGMVAQGVKLGFKGKSGYKVMSGYSGTSPHEKTSARNHRHYQDTASRLIH
NMDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAH
LFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALT
QLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPAIRP
FLQTISIGLVSFGEHYKRNETGLSVAASSLFTSGRFAIDPELRGAEFERITQNLDVHFWK
AFWNITEMEVLSSLANMASATVRVSRLLSLPPEAFEMPLTADPTLTVTISPPLAHTGPGP
VLVRLISYDLREGQDSEELSSLIKSNGQRSLELWPRPQQAPRSRSLIVHFHGGGFVAQTS
RSHEPYLKSWAQELGAPIISIDYSLAPEAPFPRALEECFFAYCWAIKHCALLGSTGERIC
LAGDSAGGNLCFTVALRAAAYGVRVPDGIMAAYPATMLQPAASPSRLLSLMDPLLPLSVL
SKCVSAYAGAKTEDHSNSDQKALGMMGLVRRDTALLLRDFRLGASSWLNSFLELSGRKSQ
KMSEPIAEPMRRSVSEAALAQPQGPLGTDSLKNLTLRDLSLRGNSETSSDTPEMSLSAET
LSPSTPSDVNFLLPPEDAGEEAEAKNELSPMDRGLGVRAAFPEGFHPRRSSQGATQMPLY
SSPIVKNPFMSPLLAPDSMLKSLPPVHIVACALDPMLDDSVMLARRLRNLGQPVTLRVVE
DLPHGFLTLAALCRETRQAAELCVERIRLVLTPPAGAGPSGETGAAGVDGGCGGRH
|
| Enzyme 27 Number of Residues |
1076 |
| Enzyme 27 Molecular Weight |
116596.7 |
| Enzyme 27 Theoretical pI |
6.68 |
| Enzyme 27 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
|
| Process |
- alcohol metabolic process
- cholesterol metabolic process
- lipid catabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
- small molecule metabolic process
- sterol metabolic process
|
| Component |
| — |
|
| Enzyme 27 General Function |
Involved in hydrolase activity |
| Enzyme 27 Specific Function |
In adipose tissue and heart, it primarily hydrolyzes stored triglycerides to free fatty acids, while in steroidogenic tissues, it principally converts cholesteryl esters to free cholesterol for steroid hormone production |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
- (1) diacylglycerol + H2O = monoacylglycerol + a carboxylate [RN:R05209]
- (2) triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
- (3) monoacylglycerol + H2O = glycerol + a carboxylate [RN:R07293]
|
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
47124456  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q05469  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
LIPS_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>3231 bp
ATGGAGCCAGGTTCTAAGTCAGTGTCTAGGTCAGACTGGCAACCTGAACCACACCAGAGG
CCTATAACCCCGCTAGAGCCTGGGCCAGAAAAGACACCCATAGCCCAGCCAGAATCGAAG
ACTCTGCAGGGATCCAATACCCAACAGAAGCCTGCTTCAAACCAAAGACCCCTCACCCAG
CAGGAGACCCCTGCACAACATGATGCTGAATCCCAGAAGGAACCTAGAGCCCAACAAAAA
TCTGCTTCACAAGAGGAATTTCTTGCCCCACAGAAGCCCGCACCACAGCAATCACCTTAC
ATCCAAAGGGTGCTGCTCACTCAACAGGAAGCTGCCTCCCAGCAGGGACCTGGGCTAGGA
AAAGAATCTATAACTCAACAGGAGCCAGCATTGAGACAAAGACATGTAGCCCAGCCAGGG
CCTGGGCCAGGAGAGCCACCTCCAGCTCAACAAGAAGCTGAATCAACACCTGCGGCCCAG
GCTAAACCTGGAGCCAAAAGGGAGCCATCTGCCCCGACTGAATCTACGTCCCAAGAGACA
CCTGAACAGTCAGACAAGCAAACAACGCCAGTCCAGGGAGCCAAATCCAAGCAGGGATCT
TTGACAGAGCTGGGATTTCTAACAAAACTTCAGGAACTATCCATACAGCGATCAGCCCTA
GAGTGGAAGGCACTTTCTGAGTGGGTCACAGATTCTGAGTCAGAATCAGATGTGGGATCA
TCTTCAGACACAGATTCTCCAGCCACGATGGGTGGAATGGTGGCCCAGGGAGTGAAGCTA
GGCTTCAAAGGAAAATCTGGTTATAAAGTGATGTCAGGATACAGTGGGACGTCGCCACAT
GAGAAAACCAGTGCTCGGAATCACAGACACTACCAGGATACAGCCTCAAGGCTCATCCAC
AACATGGACCTGCGCACAATGACACAGTCGCTGGTGACTCTGGCGGAGGACAACATAGCC
TTCTTCTCGAGCCAGGGTCCTGGGGAAACGGCCCAGCGGCTGTCAGGCGTTTTTGCCGGT
GTACGGGAGCAGGCGCTGGGGCTGGAGCCGGCCCTGGGCCGCCTGCTGGGTGTGGCGCAC
CTCTTTGACCTGGACCCAGAGACACCGGCCAACGGGTACCGCAGCCTAGTGCACACAGCC
CGCTGCTGCCTGGCGCACCTCCTGCACAAATCCCGCTATGTGGCCTCCAACCGCCGCAGC
ATCTTCTTCCGCACCAGCCACAACCTGGCCGAGCTGGAGGCCTACCTGGCTGCCCTCACC
CAGCTCCGCGCTCTGGTCTACTACGCCCAGCGCCTGCTGGTTACCAATCGGCCGGGGGTA
CTCTTCTTTGAGGGCGACGAGGGGCTCACCGCCGACTTCCTCCGGGAGTATGTCACGCTG
CATAAGGGATGCTTCTATGGCCGCTGCCTGGGCTTCCAGTTCACGCCTGCCATCCGGCCA
TTCCTGCAGACCATCTACATTGGGCTGGTGTCCTTCGGGGAGCACTACAAACGCAACGAG
ACAGGCCTCAGTGTGGCCGCCAGCTCTCTCTTCACCAGCGGCCGCTTTGCCATCGACCCC
GAGCTGCGTGGGGCTGAGTTTGAGCGGATCACACAGAACCTGGACGTGCACTTCTGGAAA
GCCTTCTGGAACATCACCGAGATGGAAGTGCTATCGTCTCTGGCCAACATGGCATCGGCC
ACCGTGAGGGTAAGCCGCCTGCTCAGCCTGCCACCCGAAGCCTTTGAGATGCCACTGACT
GCCGACCCCACGCTCACGGTCACCATCTCACCCCCACTGGCCCACACAGGCCCTGGGCCC
GTCCTCGTCAGGCTCATCTCCTGTGACCTGCGTGAAGGACAGGACAGTGAGGAGCTCAGC
AGCCTGATAAAGTCCAACGGCCAACGGAGCCTGGAGCTGTGGCCGCGCCCCCAGCAGGCA
CCCCGCTCGCGGTCCCTGATAGTGCACTTCCACGGCGGTGGCTTTGTGGCCCAGACCTCC
AGATCCCACGAGCCCTACCTCAAGAGCTGGGCCCAGGAGCTGGGCGCCCCCATCATCTCC
ATCGACTACTCCCTGGCCCCTGAGGCCCCCTTCCCCCGTGCGCTGGAGGAGTGCTTCTTC
GCCTACTGCTGGGCCATCAAGCACTGCGCCCTCCTTGGCTCAACAGGGGAACGAATCTGC
CTTGCGGGGGACAGTGCAGGCGGGAACCTCTGCTTCACCGTGGCTCTTCGGGCAGCAGCC
TACGGGGTGCGGGTGCCAGATGGCATCATGGCAGCCTACCCGGCCACAATGCTGCAGCCT
GCCGCCTCTCCCTCCCGCCTGCTGAGCCTCATGGACCCCTTGCTGCCCCTCAGTGTGCTC
TCCAAGTGTGTCAGCGCCTATGCTGGTGCAAAGACGGAGGACCACTCCAACTCAGACCAG
AAAGCCCTCGGCATGATGGGGCTGGTGCGGCGGGACACAGCCCTGCTCCTCCGAGACTTC
CGCCTGGGTGCCTCCTCATGGCTCAACTCCTTCCTGGAGTTAAGTGGGCGCAAGTCCCAG
AAGATGTCGGAGCCCATAGCAGAGCCGATGCGCCGCAGTGTGTCTGAAGCAGCACTGGCC
CAGCCCCAGGGCCCACTGGGCACGGATTCCCTCAAGAACCTGACCCTGAGGGACTTGAGC
CTGAGGGGAAACTCCGAGACGTCGTCGGACACCCCCGAGATGTCGCTGTCAGCTGAGACA
CTTAGCCCCTCCACACCCTCCGATGTCAACTTCTTATTACCACCTGAGGATGCAGGGGAA
GAGGCTGAGGCCAAAAATGAGCTGAGCCCCATGGACAGAGGCCTGGGCGTCCGTGCCGCC
TTCCCCGAGGGTTTCCACCCCCGACGCTCCAGCCAGGGTGCCACACAGATGCCCCTCTAC
TCCTCACCCATAGTCAAGAACCCCTTCATGTCGCCGCTGCTGGCACCCGACAGCATGCTC
AAGAGCCTGCCACCTGTGCACATCGTGGCGTGCGCGCTGGACCCCATGCTGGACGACTCG
GTCATGCTCGCGCGGCGACTGCGCAACCTGGGCCAGCCGGTGACGCTGCGCGTGGTGGAG
GACCTGCCGCACGGCTTCCTGACCCTAGCGGCGCTGTGCCGCGAGACGCGCCAGGCCGCA
GAGCTGTGCGTGGAGCGCATCCGCCTCGTCCTCACTCCTCCCGCCGGAGCCGGGCCGAGC
GGGGAGACGGGGGCTGCGGGGGTAGACGGGGGCTGCGGGGGGCGACACTAA
|
| Enzyme 27 GenBank Gene ID |
BC070041  |
| Enzyme 27 GeneCard ID |
LIPE  |
| Enzyme 27 GenAtlas ID |
LIPE  |
| Enzyme 27 HGNC ID |
HGNC:6621  |
| Enzyme 27 Chromosome Location |
1 |
| Enzyme 27 Locus |
19q13.2 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Langin D, Laurell H, Holst LS, Belfrage P, Holm C: Gene organization and primary structure of human hormone-sensitive lipase: possible significance of a sequence homology with a lipase of Moraxella TA144, an antarctic bacterium. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):4897-901. [PubMed
]
- Holst LS, Langin D, Mulder H, Laurell H, Grober J, Bergh A, Mohrenweiser HW, Edgren G, Holm C: Molecular cloning, genomic organization, and expression of a testicular isoform of hormone-sensitive lipase. Genomics. 1996 Aug 1;35(3):441-7. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Aboulaich N, Ortegren U, Vener AV, Stralfors P: Association and insulin regulated translocation of hormone-sensitive lipase with PTRF. Biochem Biophys Res Commun. 2006 Nov 24;350(3):657-61. Epub 2006 Sep 28. [PubMed
]
- Ortegren U, Yin L, Ost A, Karlsson H, Nystrom FH, Stralfors P: Separation and characterization of caveolae subclasses in the plasma membrane of primary adipocytes; segregation of specific proteins and functions. FEBS J. 2006 Jul;273(14):3381-92. Epub 2006 Jun 26. [PubMed
]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
5783 |
| Enzyme 28 Name |
Group 3 secretory phospholipase A2 |
| Enzyme 28 Synonyms |
- Group III secretory phospholipase A2
- GIII sPLA2
- sPLA2-III
- Phosphatidylcholine 2-acylhydrolase 3
|
| Enzyme 28 Gene Name |
PLA2G3 |
| Enzyme 28 Protein Sequence |
>Group 3 secretory phospholipase A2
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ
|
| Enzyme 28 Number of Residues |
509 |
| Enzyme 28 Molecular Weight |
57150.5 |
| Enzyme 28 Theoretical pI |
9.23 |
| Enzyme 28 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 28 General Function |
Involved in phospholipase A2 activity |
| Enzyme 28 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. Shows an 11-fold preference for phosphatidylglycerol over phosphatidylcholine (PC). Preferential cleavage:1-palmitoyl-2-linoleoyl- phosphatidylethanolamine (PE) > 1-palmitoyl-2-linoleoyl-PC > 1- palmitoyl-2-arachidonoyl-PC > 1-palmitoyl-2-arachidonoyl-PE |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
142976884  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q9NZ20  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
PA2G3_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>1530 bp
ATGGGGGTTCAGGCAGGGCTGTTTGGGATGCTGGGCTTCCTGGGGGTGGCCCTGGGGGGC
TCCCCTGCCCTCCGCTGGTACAGGACCTCCTGCCACTTGACCAAGGCCGTCCCTGGCAAC
CCACTGGGGTACCTGAGCTTCCTGGCCAAGGATGCTCAGGGACTGGCCCTGATCCATGCC
CGCTGGGATGCGCATAGGAGGCTGCAGTCATGTAGCTGGGAGGATGAGCCGGAGCTCACC
GCAGCCTACGGTGCTCTCTGTGCTCATGAGACTGCCTGGGGCTCCTTCATCCACACCCCC
GGACCCGAGCTGCAGAGAGCACTGGCCACTCTTCAGAGTCAGTGGGAGGCATGCCGAGCG
CTTGAGGAGAGTCCAGCAGGGGCCAGGAAGAAGCGAGCAGCAGGGCAGAGTGGAGTCCCT
GGTGGAGGGCACCAGCGAGAGAAGAGAGGATGGACCATGCCTGGCACACTGTGGTGTGGA
GTTGGAGATTCTGCTGGGAACTCCTCGGAGCTGGGGGTCTTCCAGGGACCTGATCTCTGT
TGCCGGGAACATGACCGCTGCCCACAGAACATCTCACCCTTGCAGTACAACTATGGCATC
CGAAACTACCGATTCCACACCATCTCCCACTGTGACTGTGACACCAGGTTTCAGCAATGC
CTACAGAATCAGCACGACTCCATCTCGGACATCGTGGGCGTGGCCTTCTTCAACGTGCTG
GAGATCCCCTGCTTTGTGCTGGAGGAGCAGGAGGCGTGTGTGGCGTGGTACTGGTGGGGC
GGGTGTAGGATGTACGGCACAGTGCCCCTCGCTCGCCTGCAGCCCAGGACCTTCTACAAT
GCCTCCTGGAGCTCCCGGGCCACCTCCCCAACTCCCAGCTCCCGGAGCCCAGCCCCTCCC
AAGCCTCGACAGAAGCAGCACCTTCGGAAGGGGCCACCACATCAGAAAGGGTCCAAGCGC
CCCAGCAAAGCCAACACCACAGCCCTCCAGGACCCTATGGTCTCTCCCAGGCTTGATGTG
GCCCCCACAGGCCTCCAGGGCCCACAGGGTGGCCTAAAACCTCAGGGTGCCCGCTGGGTC
TGCCGCAGCTTCCGCCGCCACCTGGACCAGTGTGAGCACCAGATTGGGCCCCGGGAAATC
GAGTTCCAGCTGCTCAACAGCGCCCAAGAGCCCCTCTTCCACTGCAACTGCACGCGCCGT
CTGGCACGCTTCCTGAGGCTCCACAGCCCACCCGAGGTTACCAACATGCTTTGGGAGCTG
CTGGGCACAACCTGCTTCAAGCTGGCCCCTCCACTGGACTGTGTGGAAGGCAAAAACTGT
TCCAGAGACCCTAGGGCCATCAGGGTGTCAGCCCGGCACTTGCGGAGGCTTCAGCAGAGG
CGACACCAGCTCCAGGATAAAGGCACAGATGAGAGGCAGCCATGGCCTTCAGAGCCCCTG
AGAGGCCCCATGTCATTCTACAACCAGTGCCTGCAGCTAACCCAGGCAGCCAGGAGACCC
GACAGGCAGCAGAAGTCCTGGAGCCAGTGA
|
| Enzyme 28 GenBank Gene ID |
NM_015715.3  |
| Enzyme 28 GeneCard ID |
PLA2G3  |
| Enzyme 28 GenAtlas ID |
PLA2G3  |
| Enzyme 28 HGNC ID |
HGNC:17934  |
| Enzyme 28 Chromosome Location |
2 |
| Enzyme 28 Locus |
22q12.2 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Valentin E, Ghomashchi F, Gelb MH, Lazdunski M, Lambeau G: Novel human secreted phospholipase A(2) with homology to the group III bee venom enzyme. J Biol Chem. 2000 Mar 17;275(11):7492-6. [PubMed
]
- Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP, et al.: The DNA sequence of human chromosome 22. Nature. 1999 Dec 2;402(6761):489-95. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Murakami M, Masuda S, Shimbara S, Bezzine S, Lazdunski M, Lambeau G, Gelb MH, Matsukura S, Kokubu F, Adachi M, Kudo I: Cellular arachidonate-releasing function of novel classes of secretory phospholipase A2s (groups III and XII). J Biol Chem. 2003 Mar 21;278(12):10657-67. Epub 2003 Jan 8. [PubMed
]
- Murakami M, Masuda S, Shimbara S, Ishikawa Y, Ishii T, Kudo I: Cellular distribution, post-translational modification, and tumorigenic potential of human group III secreted phospholipase A(2). J Biol Chem. 2005 Jul 1;280(26):24987-98. Epub 2005 Apr 29. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
5821 |
| Enzyme 29 Name |
Bile acid-CoA:amino acid N-acyltransferase |
| Enzyme 29 Synonyms |
- BACAT
- BAT
- Glycine N-choloyltransferase
- Long-chain fatty-acyl-CoA hydrolase
|
| Enzyme 29 Gene Name |
BAAT |
| Enzyme 29 Protein Sequence |
>Bile acid-CoA:amino acid N-acyltransferase
MIQLTATPVSALVDEPVHIRATGLIPFQMVSFQASLEDENGDMFYSQAHYRANEFGEVDL
NHASSLGGDYMGVHPMGLFWSLKPEKLLTRLLKRDVMNRPFQVQVKLYDLELIVNNKVAS
APKASLTLERWYVAPGVTRIKVREGRLRGALFLPPGEGLFPGVIDLFGGLGGLLEFRASL
LASRGFASLALAYHNYEDLPRKPEVTDLEYFEEAANFLLRHPKVFGSGVGVVSVCQGVQI
GLSMAIYLKQVTATVLINGTNFPFGIPQVYHGQIHQPLPHSAQLISTNALGLLELYRTFE
TTQVGASQYLFPIEEAQGQFLFIVGEGDKTINSKAHAEQAIGQLKRHGKNNWTLLSYPGA
GHLIEPPYSPLCCASTTHDLRLHWGGEVIPHAAAQEHAWKEIQRFLRKHLIPDVTSQL
|
| Enzyme 29 Number of Residues |
418 |
| Enzyme 29 Molecular Weight |
46298.9 |
| Enzyme 29 Theoretical pI |
7.00 |
| Enzyme 29 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 29 General Function |
Involved in thiolester hydrolase activity |
| Enzyme 29 Specific Function |
Involved in bile acid metabolism. In liver hepatocytes catalyzes the second step in the conjugation of C24 bile acids (choloneates) to glycine and taurine before excretion into bile canaliculi. The major components of bile are cholic acid and chenodeoxycholic acid. In a first step the bile acids are converted to an acyl-CoA thioester, either in peroxisomes (primary bile acids deriving from the cholesterol pathway), or cytoplasmic at the endoplasmic reticulum (secondary bile acids). May catalyze the conjugation of primary or secondary bile acids, or both. The conjugation increases the detergent properties of bile acids in the intestine, which facilitates lipid and fat-soluble vitamin absorption. In turn, bile acids are deconjugated by bacteria in the intestine and are recycled back to the liver for reconjugation (secondary bile acids). May also act as an acyl-CoA thioesterase that regulates intracellular levels of free fatty acids. In vitro, catalyzes the hydrolysis of long- and very long-chain saturated acyl-CoAs to the free fatty acid and coenzyme A (CoASH), and conjugates glycine to these acyl-CoAs |
| Enzyme 29 Pathways |
- Bile Acid Biosynthesis (map00120
)
- Taurine and Hypotaurine Metabolism (map00430
)
|
| Enzyme 29 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
Not Available |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q14032  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
BAAT_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1257 bp
ATGATCCAGTTGACAGCTACCCCTGTGAGTGCACTTGTTGATGAGCCAGTGCATATCCGA
GCTACAGGCCTGATTCCCTTTCAGATGGTGAGTTTTCAGGCATCACTGGAAGATGAAAAC
GGAGACATGTTTTATTCTCAAGCCCACTATAGGGCCAATGAATTCGGTGAGGTGGACCTG
AATCATGCTTCTTCACTTGGAGGGGATTATATGGGAGTCCACCCCATGGGTCTCTTCTGG
TCTCTGAAACCTGAAAAGCTATTAACAAGACTGTTGAAAAGAGATGTGATGAATAGGCCT
TTCCAGGTCCAAGTAAAACTTTATGACTTAGAGTTAATAGTGAACAATAAAGTTGCCAGT
GCTCCAAAGGCCAGCCTGACTTTGGAGAGGTGGTATGTGGCACCTGGTGTCACACGAATT
AAGGTTCGAGAAGGCCGCCTTCGAGGAGCTCTCTTTCTCCCTCCAGGAGAGGGTCTCTTC
CCAGGGGTAATTGATTTGTTTGGTGGTTTGGGTGGGCTGCTTGAATTTCGGGCCAGCCTC
CTAGCCAGTCGTGGCTTCGCCTCCTTGGCCTTGGCTTACCATAACTATGAAGACCTGCCC
CGCAAACCAGAAGTAACAGATTTGGAATATTTTGAGGAGGCTGCCAACTTTCTCCTGAGA
CATCCAAAGGTCTTTGGCTCAGGCGTTGGGGTAGTCTCTGTATGTCAAGGAGTACAGATT
GGACTATCTATGGCTATTTACCTAAAGCAAGTCACAGCCACGGTACTTATTAATGGGACC
AACTTTCCTTTTGGCATTCCACAGGTATATCATGGTCAGATCCATCAGCCCCTTCCCCAT
TCTGCACAATTAATATCCACCAATGCCTTGGGGTTACTAGAGCTCTATCGCACTTTTGAG
ACAACTCAAGTTGGGGCCAGTCAATATTTGTTTCCTATTGAAGAGGCCCAGGGGCAATTC
CTCTTCATTGTAGGAGAAGGTGATAAGACTATCAACAGCAAAGCACACGCTGAACAAGCC
ATAGGACAGCTGAAGAGACATGGGAAGAACAACTGGACCCTGCTATCTTACCCTGGGGCA
GGCCACCTGATAGAACCTCCCTATTCTCCTCTGTGCTGTGCCTCAACGACCCACGATTTG
AGGTTACACTGGGGAGGAGAGGTGATCCCACACGCAGCTGCACAGGAACATGCTTGGAAG
GAGATCCAGAGATTTCTCAGGAAGCACCTCATTCCAGATGTGACCAGTCAACTCTAA
|
| Enzyme 29 GenBank Gene ID |
L34081  |
| Enzyme 29 GeneCard ID |
BAAT  |
| Enzyme 29 GenAtlas ID |
BAAT  |
| Enzyme 29 HGNC ID |
HGNC:932  |
| Enzyme 29 Chromosome Location |
9 |
| Enzyme 29 Locus |
9q22.3 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Falany CN, Johnson MR, Barnes S, Diasio RB: Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase. J Biol Chem. 1994 Jul 29;269(30):19375-9. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Johnson MR, Barnes S, Kwakye JB, Diasio RB: Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver. J Biol Chem. 1991 Jun 5;266(16):10227-33. [PubMed
]
- Sfakianos MK, Wilson L, Sakalian M, Falany CN, Barnes S: Conserved residues in the putative catalytic triad of human bile acid Coenzyme A:amino acid N-acyltransferase. J Biol Chem. 2002 Dec 6;277(49):47270-5. Epub 2002 Sep 17. [PubMed
]
- O'Byrne J, Hunt MC, Rai DK, Saeki M, Alexson SE: The human bile acid-CoA:amino acid N-acyltransferase functions in the conjugation of fatty acids to glycine. J Biol Chem. 2003 Sep 5;278(36):34237-44. Epub 2003 Jun 16. [PubMed
]
- Carlton VE, Harris BZ, Puffenberger EG, Batta AK, Knisely AS, Robinson DL, Strauss KA, Shneider BL, Lim WA, Salen G, Morton DH, Bull LN: Complex inheritance of familial hypercholanemia with associated mutations in TJP2 and BAAT. Nat Genet. 2003 May;34(1):91-6. [PubMed
]
|
| Enzyme 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
5824 |
| Enzyme 30 Name |
Acylphosphatase-2 |
| Enzyme 30 Synonyms |
- Acylphosphatase, muscle type isozyme
- Acylphosphate phosphohydrolase 2
|
| Enzyme 30 Gene Name |
ACYP2 |
| Enzyme 30 Protein Sequence |
>Acylphosphatase-2
MSTAQSLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTGQVQGPEDKVN
SMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY
|
| Enzyme 30 Number of Residues |
99 |
| Enzyme 30 Molecular Weight |
11139.5 |
| Enzyme 30 Theoretical pI |
10.01 |
| Enzyme 30 GO Classification |
| Function |
- acylphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 30 General Function |
Involved in acylphosphatase activity |
| Enzyme 30 Specific Function |
Its physiological role is not yet clear |
| Enzyme 30 Pathways |
|
| Enzyme 30 Reactions |
- an acylphosphate + H2O = a carboxylate + phosphate [RN:R00539]
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
15341747  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
P14621  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
ACYP2_HUMAN  |
| Enzyme 30 PDB ID |
1APS  |
| Enzyme 30 PDB File |
Show |
| Enzyme 30 3D Structure |
|
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>300 bp
ATGTCTACCGCCCAGTCACTCAAATCCGTGGACTACGAGGTGTTCGGAAGAGTGCAGGGT
GTTTGCTTCAGAATGTATACAGAAGATGAAGCTAGGAAAATAGGAGTGGTTGGCTGGGTG
AAGAATACCAGCAAAGGCACCGTGACAGGCCAAGTGCAGGGGCCAGAAGACAAAGTCAAT
TCCATGAAGTCCTGGCTGAGCAAGGTTGGAAGCCCTAGTTCTCGCATTGACCGCACAAAC
TTTTCTAATGAAAAAACCATCTCTAAGCTTGAATACTCTAATTTTAGTATTAGATACTAA
|
| Enzyme 30 GenBank Gene ID |
BC012290  |
| Enzyme 30 GeneCard ID |
ACYP2  |
| Enzyme 30 GenAtlas ID |
ACYP2  |
| Enzyme 30 HGNC ID |
HGNC:180  |
| Enzyme 30 Chromosome Location |
2 |
| Enzyme 30 Locus |
2p16.2 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 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
]
- Manao G, Camici G, Modesti A, Liguri G, Berti A, Stefani M, Cappugi G, Ramponi G: Human skeletal muscle acylphosphatase: the primary structure. Mol Biol Med. 1984 Dec;2(6):369-78. [PubMed
]
- Chiarugi P, Raugei G, Marzocchini R, Fiaschi T, Ciccarelli C, Berti A, Ramponi G: Differential modulation of expression of the two acylphosphatase isoenzymes by thyroid hormone. Biochem J. 1995 Oct 15;311 ( Pt 2):567-73. [PubMed
]
|
| Enzyme 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
5825 |
| Enzyme 31 Name |
Acylphosphatase-1 |
| Enzyme 31 Synonyms |
- Acylphosphatase, erythrocyte isozyme
- Acylphosphatase, organ-common type isozyme
- Acylphosphate phosphohydrolase 1
|
| Enzyme 31 Gene Name |
ACYP1 |
| Enzyme 31 Protein Sequence |
>Acylphosphatase-1
MAEGNTLISVDYEIFGKVQGVFFRKHTQAEGKKLGLVGWVQNTDRGTVQGQLQGPISKVR
HMQEWLETRGSPKSHIDKANFNNEKVILKLDYSDFQIVK
|
| Enzyme 31 Number of Residues |
99 |
| Enzyme 31 Molecular Weight |
11260.8 |
| Enzyme 31 Theoretical pI |
9.94 |
| Enzyme 31 GO Classification |
| Function |
- acylphosphatase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 31 General Function |
Involved in acylphosphatase activity |
| Enzyme 31 Specific Function |
Its physiological role is not yet clear |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- an acylphosphate + H2O = a carboxylate + phosphate [RN:R00539]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
4885693  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
P07311  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
ACYP1_HUMAN  |
| Enzyme 31 PDB ID |
2ACY  |
| Enzyme 31 PDB File |
Show |
| Enzyme 31 3D Structure |
|
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>300 bp
ATGGCAGAAGGAAACACCCTGATATCAGTGGATTATGAAATTTTTGGGAAGGTGCAAGGG
GTGTTTTTCCGTAAGCATACTCAGGCTGAGGGTAAAAAGCTGGGATTGGTAGGCTGGGTC
CAGAACACTGACCGGGGCACAGTGCAAGGACAATTGCAAGGTCCCATCTCCAAGGTGCGT
CATATGCAGGAATGGCTTGAAACAAGAGGAAGTCCTAAATCACACATCGACAAAGCAAAC
TTCAACAATGAAAAAGTCATCTTGAAGTTGGATTACTCAGACTTCCAAATTGTAAAATAA
|
| Enzyme 31 GenBank Gene ID |
AC007055  |
| Enzyme 31 GeneCard ID |
ACYP1  |
| Enzyme 31 GenAtlas ID |
ACYP1  |
| Enzyme 31 HGNC ID |
HGNC:179  |
| Enzyme 31 Chromosome Location |
1 |
| Enzyme 31 Locus |
14q24.3 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- 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
]
- Liguri G, Camici G, Manao G, Cappugi G, Nassi P, Modesti A, Ramponi G: A new acylphosphatase isoenzyme from human erythrocytes: purification, characterization, and primary structure. Biochemistry. 1986 Dec 2;25(24):8089-94. [PubMed
]
- Fiaschi T, Raugei G, Marzocchini R, Chiarugi P, Cirri P, Ramponi G: Cloning and expression of the cDNA coding for the erythrocyte isoenzyme of human acylphosphatase. FEBS Lett. 1995 Jun 26;367(2):145-8. [PubMed
]
- Yeung RC, Lam SY, Wong KB: Crystallization and preliminary crystallographic analysis of human common-type acylphosphatase. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jan 1;62(Pt 1):80-2. Epub 2005 Dec 23. [PubMed
]
- Gribenko AV, Patel MM, Liu J, McCallum SA, Wang C, Makhatadze GI: Rational stabilization of enzymes by computational redesign of surface charge-charge interactions. Proc Natl Acad Sci U S A. 2009 Feb 24;106(8):2601-6. Epub 2009 Feb 5. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
5826 |
| Enzyme 32 Name |
Aminoacylase-1 |
| Enzyme 32 Synonyms |
- ACY-1
- N-acyl-L-amino-acid amidohydrolase
|
| Enzyme 32 Gene Name |
ACY1 |
| Enzyme 32 Protein Sequence |
>Aminoacylase-1
MTSKGPEEEHPSVTLFRQYLRIRTVQPKPDYGAAVAFFEETARQLGLGCQKVEVAPGYVV
TVLTWPGTNPTLSSILLNSHTDVVPVFKEHWSHDPFEAFKDSEGYIYARGAQDMKCVSIQ
YLEAVRRLKVEGHRFPRTIHMTFVPDEEVGGHQGMELFVQRPEFHALRAGFALDEGIANP
TDAFTVFYSERSPWWVRVTSTGRPGHASRFMEDTAAEKLHKVVNSILAFREKEWQRLQSN
PHLKEGSVTSVNLTKLEGGVAYNVIPATMSASFDFRVAPDVDFKAFEEQLQSWCQAAGEG
VTLEFAQKWMHPQVTPTDDSNPWWAAFSRVCKDMNLTLEPEIMPAATDNRYIRAVGVPAL
GFSPMNRTPVLLHDHDERLHEAVFLRGVDIYTRLLPALASVPALPSDS
|
| Enzyme 32 Number of Residues |
408 |
| Enzyme 32 Molecular Weight |
45884.7 |
| Enzyme 32 Theoretical pI |
6.12 |
| Enzyme 32 GO Classification |
| Function |
- aminoacylase activity
- binding
- 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
- metallopeptidase activity
- peptidase activity
- peptidase activity, acting on L-amino acid peptides
- protein binding
|
| Process |
- cellular amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- macromolecule metabolic process
- metabolic process
- protein metabolic process
- proteolysis
|
| Component |
- cell part
- cytoplasm
- intracellular part
|
|
| Enzyme 32 General Function |
Involved in metallopeptidase activity |
| Enzyme 32 Specific Function |
Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
- an N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid [RN:R01263]
|
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
178071  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q03154  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
ACY1_HUMAN  |
| Enzyme 32 PDB ID |
1Q7L  |
| Enzyme 32 PDB File |
Show |
| Enzyme 32 3D Structure |
|
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>1227 bp
ATGACCAGCAAGGGTCCCGAGGAGGAGCACCCATCGGTGACGCTCTTCCGCCAGTACCTG
CGTATCCGCACTGTCCAGCCCAAGCCTGACTATGGAGCTGCTGTGGCTTTCTTTGAGGAG
ACAGCCCGCCAGCTGGGCCTGGGCTGTCAGAAAGTAGAGGTGGCACCTGGCTATGTGGTG
ACCGTGTTGACCTGGCCAGGCACCAACCCTACACTCTCCTCCATCTTGCTCAACTCCCAC
ACGGATGTGGTGCCTGTCTTCAAGGAACATTGGAGTCACGACCCCTTTGAGGCCTTCAAG
GATTCTGAGGGCTACATCTATGCCAGGGGTGCCCAGGACATGAAGTGCGTCAGCATCCAG
TACCTGGAAGCTGTGAGGAGGCTGAAGGTGGAGGGCCACCGGTTCCCCAGAACCATCCAC
ATGACCTTTGTGCCTGATGAGGAGGTTGGGGGTCACCAAGGCATGGAGCTGTTCGTGCAG
CGGCCTGAGTTCCACGCCCTGAGGGCAGGCTTTGCCCTGGATGAGGGCATAGCCAATCCC
ACTGATGCCTTCACTGTCTTTTATAGTGAGCGGAGTCCCTGGTGGGTGCGGGTTACCAGC
ACTGGGAGGCCAGGCCATGCCTCACGCTTCATGGAGGACACAGCAGCAGAGAAGCTGCAC
AAGGTTGTAAACTCCATCCTGGCATTCCGGGAGAAGGAATGGCAGAGGCTGCAGTCAAAC
CCCCACCTGAAAGAGGGGTCCGTGACCTCCGTGAACCTGACTAAGCTAGAGGGTGGCGTG
GCCTATAACGTGATACCTGCCACCATGAGCGCCAGCTTTGACTTCCGTGTGGCACCGGAT
GTGGACTTCAAGGCTTTTGAGGAGCAGCTGCAGAGCTGGTGCCAGGCAGCTGGCGAGGGG
GTCACCCTAGAGTTTGCTCAGAAGTGGATGCACCCCCAAGTGACACCTACTGATGACTCA
AACCCTTGGTGGGCAGCTTTTAGCCGGGTCTGCAAGGATATGAACCTCACTCTGGAGCCT
GAGATCATGCCTGCTGCCACTGACAACCGCTATATCCGCGCGGTGGGGGTCCCAGCTCTA
GGCTTCTCACCCATGAACCGCACACCTGTGCTGCTGCACGACCACGATGAACGGCTGCAT
GAGGCTGTGTTCCTCCGTGGGGTGGACATATATACACGCCTGCTGCCTGCCCTTGCCAGT
GTGCCTGCCCTGCCCAGTGACAGCTGA
|
| Enzyme 32 GenBank Gene ID |
L07548  |
| Enzyme 32 GeneCard ID |
ACY1  |
| Enzyme 32 GenAtlas ID |
ACY1  |
| Enzyme 32 HGNC ID |
HGNC:177  |
| Enzyme 32 Chromosome Location |
3 |
| Enzyme 32 Locus |
3p21.1 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Mitta M, Kato I, Tsunasawa S: The nucleotide sequence of human aminoacylase-1. Biochim Biophys Acta. 1993 Aug 19;1174(2):201-3. [PubMed
]
- Cook RM, Burke BJ, Buchhagen DL, Minna JD, Miller YE: Human aminoacylase-1. Cloning, sequence, and expression analysis of a chromosome 3p21 gene inactivated in small cell lung cancer. J Biol Chem. 1993 Aug 15;268(23):17010-7. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Van Coster RN, Gerlo EA, Giardina TG, Engelke UF, Smet JE, De Praeter CM, Meersschaut VA, De Meirleir LJ, Seneca SH, Devreese B, Leroy JG, Herga S, Perrier JP, Wevers RA, Lissens W: Aminoacylase I deficiency: a novel inborn error of metabolism. Biochem Biophys Res Commun. 2005 Dec 23;338(3):1322-6. Epub 2005 Nov 2. [PubMed
]
- Sass JO, Mohr V, Olbrich H, Engelke U, Horvath J, Fliegauf M, Loges NT, Schweitzer-Krantz S, Moebus R, Weiler P, Kispert A, Superti-Furga A, Wevers RA, Omran H: Mutations in ACY1, the gene encoding aminoacylase 1, cause a novel inborn error of metabolism. Am J Hum Genet. 2006 Mar;78(3):401-9. Epub 2006 Jan 18. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
- Sass JO, Olbrich H, Mohr V, Hart C, Woldseth B, Krywawych S, Bjurulf B, Lakhani PK, Buchdahl RM, Omran H: Neurological findings in aminoacylase 1 deficiency. Neurology. 2007 Jun 12;68(24):2151-3. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
5827 |
| Enzyme 33 Name |
Aspartoacylase |
| Enzyme 33 Synonyms |
- Aminoacylase-2
- ACY-2
|
| Enzyme 33 Gene Name |
ASPA |
| Enzyme 33 Protein Sequence |
>Aspartoacylase
MTSCHIAEEHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVKK
CTRYIDCDLNRIFDLENLGKKMSEDLPYEVRRAQEINHLFGPKDSEDSYDIIFDLHNTTS
NMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEHPSLKYATTRSIAKYPVGIEVG
PQPQGVLRADILDQMRKMIKHALDFIHHFNEGKEFPPCAIEVYKIIEKVDYPRDENGEIA
AIIHPNLQDQDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTK
LTLNAKSIRCCLH
|
| Enzyme 33 Number of Residues |
313 |
| Enzyme 33 Molecular Weight |
35734.8 |
| Enzyme 33 Theoretical pI |
6.51 |
| Enzyme 33 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
|
| Component |
| — |
|
| Enzyme 33 General Function |
Involved in hydrolase activity, acting on ester bonds |
| Enzyme 33 Specific Function |
Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate and L-aspartate. NAA occurs in high concentration in brain and its hydrolysis NAA plays a significant part in the maintenance of intact white matter. In other tissues it act as a scavenger of NAA from body fluids |
| Enzyme 33 Pathways |
|
| Enzyme 33 Reactions |
- N-acyl-L-aspartate + H2O = a carboxylate + L-aspartate [RN:R00546]
|
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
Not Available |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
P45381  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
ACY2_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>942 bp
ATGACTTCTTGTCACATTGCTGAAGAACATATACAAAAGGTTGCTATCTTTGGAGGAACC
CATGGGAATGAGCTAACCGGAGTATTTCTGGTTAAGCATTGGCTAGAGAATGGCGCTGAG
ATTCAGAGAACAGGGCTGGAGGTAAAACCATTTATTACTAACCCCAGAGCAGTGAAGAAG
TGTACCAGATATATTGACTGTGACCTGAATCGCATTTTTGACCTTGAAAATCTTGGCAAA
AAAATGTCAGAAGATTTGCCATATGAAGTGAGAAGGGCTCAAGAAATAAATCATTTATTT
GGTCCAAAAGACAGTGAAGATTCCTATGACATTATTTTTGACCTTCACAACACCACCTCT
AACATGGGGTGCACTCTTATTCTTGAGGATTCCAGGAATAACTTTTTAATTCAGATGTTT
CATTACATTAAGACTTCTCTGGCTCCACTACCCTGCTACGTTTATCTGATTGAGCATCCT
TCCCTCAAATATGCGACCACTCGTTCCATAGCCAAGTATCCTGTGGGTATAGAAGTTGGT
CCTCAGCCTCAAGGGGTTCTGAGAGCTGATATCTTGGATCAAATGAGAAAAATGATTAAA
CATGCTCTTGATTTTATACATCATTTCAATGAAGGAAAAGAATTTCCTCCCTGCGCCATT
GAGGTCTATAAAATTATAGAGAAAGTTGATTACCCCCGGGATGAAAATGGAGAAATTGCT
GCTATCATCCATCCTAATCTGCAGGATCAAGACTGGAAACCACTGCATCCTGGGGATCCC
ATGTTTTTAACTCTTGATGGGAAGACGATCCCACTGGGCGGAGACTGTACCGTGTACCCC
GTGTTTGTGAATGAGGCCGCATATTACGAAAAGAAAGAAGCTTTTGCAAAGACAACTAAA
CTAACGCTCAATGCAAAAAGTATTCGCTGCTGTTTACATTAG
|
| Enzyme 33 GenBank Gene ID |
S67156  |
| Enzyme 33 GeneCard ID |
ASPA  |
| Enzyme 33 GenAtlas ID |
ASPA  |
| Enzyme 33 HGNC ID |
HGNC:756  |
| Enzyme 33 Chromosome Location |
1 |
| Enzyme 33 Locus |
17p13.3 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Kaul R, Gao GP, Balamurugan K, Matalon R: Cloning of the human aspartoacylase cDNA and a common missense mutation in Canavan disease. Nat Genet. 1993 Oct;5(2):118-23. [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
]
- Moore RA, Le Coq J, Faehnle CR, Viola RE: Purification and preliminary characterization of brain aspartoacylase. Arch Biochem Biophys. 2003 May 1;413(1):1-8. [PubMed
]
- Le Coq J, Pavlovsky A, Malik R, Sanishvili R, Xu C, Viola RE: Examination of the mechanism of human brain aspartoacylase through the binding of an intermediate analogue. Biochemistry. 2008 Mar 18;47(11):3484-92. Epub 2008 Feb 23. [PubMed
]
- Bitto E, Bingman CA, Wesenberg GE, McCoy JG, Phillips GN Jr: Structure of aspartoacylase, the brain enzyme impaired in Canavan disease. Proc Natl Acad Sci U S A. 2007 Jan 9;104(2):456-61. Epub 2006 Dec 28. [PubMed
]
- Kaul R, Gao GP, Aloya M, Balamurugan K, Petrosky A, Michals K, Matalon R: Canavan disease: mutations among Jewish and non-jewish patients. Am J Hum Genet. 1994 Jul;55(1):34-41. [PubMed
]
- Shaag A, Anikster Y, Christensen E, Glustein JZ, Fois A, Michelakakis H, Nigro F, Pronicka E, Ribes A, Zabot MT, et al.: The molecular basis of canavan (aspartoacylase deficiency) disease in European non-Jewish patients. Am J Hum Genet. 1995 Sep;57(3):572-80. [PubMed
]
- Kaul R, Gao GP, Michals K, Whelan DT, Levin S, Matalon R: Novel (cys152 > arg) missense mutation in an Arab patient with Canavan disease. Hum Mutat. 1995;5(3):269-71. [PubMed
]
- Kaul R, Gao GP, Matalon R, Aloya M, Su Q, Jin M, Johnson AB, Schutgens RB, Clarke JT: Identification and expression of eight novel mutations among non-Jewish patients with Canavan disease. Am J Hum Genet. 1996 Jul;59(1):95-102. [PubMed
]
- Kobayashi K, Tsujino S, Ezoe T, Hamaguchi H, Nihei K, Sakuragawa N: Missense mutation (I143T) in a Japanese patient with Canavan disease. Hum Mutat. 1998;Suppl 1:S308-9. [PubMed
]
- Rady PL, Vargas T, Tyring SK, Matalon R, Langenbeck U: Novel missense mutation (Y231C) in a turkish patient with canavan disease. Am J Med Genet. 1999 Nov 26;87(3):273-5. [PubMed
]
- Elpeleg ON, Shaag A: The spectrum of mutations of the aspartoacylase gene in Canavan disease in non-Jewish patients. J Inherit Metab Dis. 1999 Jun;22(4):531-4. [PubMed
]
- Sistermans EA, de Coo RF, van Beerendonk HM, Poll-The BT, Kleijer WJ, van Oost BA: Mutation detection in the aspartoacylase gene in 17 patients with Canavan disease: four new mutations in the non-Jewish population. Eur J Hum Genet. 2000 Jul;8(7):557-60. [PubMed
]
- Zeng BJ, Wang ZH, Ribeiro LA, Leone P, De Gasperi R, Kim SJ, Raghavan S, Ong E, Pastores GM, Kolodny EH: Identification and characterization of novel mutations of the aspartoacylase gene in non-Jewish patients with Canavan disease. J Inherit Metab Dis. 2002 Nov;25(7):557-70. [PubMed
]
- Olsen TR, Tranebjaerg L, Kvittingen EA, Hagenfeldt L, Moller C, Nilssen O: Two novel aspartoacylase gene (ASPA) missense mutations specific to Norwegian and Swedish patients with Canavan disease. J Med Genet. 2002 Sep;39(9):e55. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
5830 |
| Enzyme 34 Name |
Aspartoacylase-2 |
| Enzyme 34 Synonyms |
- Acylase III
- Aminoacylase-3
- ACY-3
- Hepatitis C virus core-binding protein 1
- HCBP1
|
| Enzyme 34 Gene Name |
ACY3 |
| Enzyme 34 Protein Sequence |
>Aspartoacylase-2
MCSLPVPREPLRRVAVTGGTHGNEMSGVYLARHWLHAPAELQRASFSAVPVLANPAATSG
CRRYVDHDLNRTFTSSFLNSRPTPDDPYEVTRARELNQLLGPKASGQAFDFVLDLHNTTA
NMGTCLIAKSSHEVFAMHLCRHLQLQYPELSCQVFLYQRSGEESYNLDSVAKNGLGLELG
PQPQGVLRADIFSRMRTLVATVLDFIELFNQGTAFPAFEMEAYRPVGVVDFPRTEAGHLA
GTVHPQLQDRDFQPLQPGAPIFQMFSGEDLLYEGESTVYPVFINEAAYYEKGVAFVQTEK
FTFTVPAMPALTPAPSPAS
|
| Enzyme 34 Number of Residues |
319 |
| Enzyme 34 Molecular Weight |
35240.7 |
| Enzyme 34 Theoretical pI |
5.77 |
| Enzyme 34 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
|
| Component |
| — |
|
| Enzyme 34 General Function |
Involved in hydrolase activity, acting on ester bonds |
| Enzyme 34 Specific Function |
Plays an important role in deacetylating mercapturic acids in kidney proximal tubules |
| Enzyme 34 Pathways |
|
| 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 |
Not Available |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q96HD9  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
ACY3_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>960 bp
ATGTGCTCACTGCCTGTGCCCCGGGAGCCCCTGCGTCGCGTGGCTGTGACTGGGGGCACG
CATGGCAACGAGATGTCGGGCGTCTACCTGGCCCGGCACTGGCTGCATGCCCCCGCAGAG
CTGCAGAGAGCCAGCTTCTCCGCTGTGCCTGTGCTGGCCAACCCGGCAGCCACATCCGGC
TGCCGCCGCTACGTGGACCATGACCTCAACCGCACCTTCACCAGCAGCTTCCTCAATTCC
AGGCCCACCCCGGACGACCCATATGAGGTGACAAGAGCCCGAGAGCTGAACCAGCTGCTG
GGGCCCAAGGCCTCGGGCCAGGCCTTTGACTTTGTCCTTGACCTGCACAACACCACGGCC
AACATGGGCACCTGCTTAATCGCGAAGTCCTCCCACGAAGTCTTTGCCATGCACCTGTGC
CGCCATCTGCAGCTGCAGTACCCCGAGCTGTCCTGCCAGGTCTTCCTGTACCAGCGGTCT
GGGGAGGAGAGCTACAACCTGGACTCTGTGGCCAAAAATGGACTGGGTCTGGAGCTGGGC
CCCCAGCCACAGGGTGTGCTGCGGGCTGACATTTTCTCAAGGATGAGGACCCTGGTGGCC
ACAGTTCTGGACTTCATCGAACTCTTCAACCAGGGTACGGCCTTTCCTGCCTTTGAGATG
GAAGCCTATAGACCCGTGGGCGTCGTGGACTTCCCCCGCACCGAGGCCGGGCACCTGGCA
GGCACTGTGCATCCTCAGCTGCAGGACCGAGACTTCCAGCCACTGCAGCCTGGTGCTCCC
ATCTTCCAGATGTTCAGTGGGGAGGACCTGCTCTATGAGGGAGAGTCCACGGTGTACCCC
GTGTTCATTAACGAGGCTGCCTACTATGAGAAGGGCGTTGCCTTTGTCCAGACTGAGAAG
TTCACATTCACCGTGCCTGCCATGCCCGCGCTGACCCCTGCCCCGAGCCCAGCTTCCTAA
|
| Enzyme 34 GenBank Gene ID |
AY040761  |
| Enzyme 34 GeneCard ID |
ACY3  |
| Enzyme 34 GenAtlas ID |
ACY3  |
| Enzyme 34 HGNC ID |
HGNC:24104  |
| Enzyme 34 Chromosome Location |
1 |
| Enzyme 34 Locus |
11q13.2 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 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
]
- Chen YR, Chen TY, Zhang SL, Lin SM, Zhao YR, Ye F, Zhang X, Shi L, Dang SS, Liu M: Identification of a novel protein binding to hepatitis C virus core protein. J Gastroenterol Hepatol. 2009 Jul;24(7):1300-4. Epub 2009 Apr 13. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
6335 |
| Enzyme 35 Name |
Cytosolic acyl coenzyme A thioester hydrolase |
| Enzyme 35 Synonyms |
- Acyl-CoA thioesterase 7
- Brain acyl-CoA hydrolase
- CTE-IIa
- CTE-II
- Long chain acyl-CoA thioester hydrolase
|
| Enzyme 35 Gene Name |
ACOT7 |
| Enzyme 35 Protein Sequence |
>Cytosolic acyl coenzyme A thioester hydrolase
MKLLARALRLCEFGRQASSRRLVAGQGCVGPRRGCCAPVQVVGPRADLPPCGACITGRIM
RPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGE
VAHVSAEITYTSKHSVEVQVNVMSENILTGAKKLTNKATLWYVPLSLKNVDKVLEVPPVV
YSRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCT
LHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTS
NKSMEIEVLVDADPVVDSSQKRYRAASAFFTYVSLSQEGRSLPVPQLVPETEDEKKRFEE
GKGRYLQMKAKRQGHAEPQP
|
| Enzyme 35 Number of Residues |
380 |
| Enzyme 35 Molecular Weight |
41795.8 |
| Enzyme 35 Theoretical pI |
8.66 |
| Enzyme 35 GO Classification |
Not Available |
| Enzyme 35 General Function |
Lipid transport and metabolism |
| Enzyme 35 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May play an important physiological function in brain. May play a regulatory role by modulating the cellular levels of fatty acyl- CoA ligands for certain transcription factors as well as the substrates for fatty acid metabolizing enzymes, contributing to lipid homeostasis. Has broad specificity, active towards fatty acyl-CoAs with chain-lengths of C8-C18. Has a maximal activity toward palmitoyl-CoA |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
|
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
32528282  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
O00154  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
BACH_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>1143 bp
ATGAAGCTGCTTGCCAGGGCTCTCCGGCTCTGTGAGTTTGGGAGGCAGGCATCTTCCAGG
AGGCTGGTGGCTGGCCAGGGATGTGTGGGGCCCCGGCGAGGGTGCTGCGCTCCCGTCCAG
GTGGTTGGGCCCAGGGCTGATCTCCCACCCTGTGGAGCCTGCATTACTGGAAGGATCATG
CGGCCAGATGATGCCAACGTGGCCGGCAATGTCCACGGGGGGACCATCCTGAAGATGATC
GAGGAGGCAGGCGCCATCATCAGCACCCGGCATTGCAACAGCCAGAACGGGGAGCGCTGT
GTGGCCGCCCTGGCTCGTGTCGAGCGCACCGACTTCCTGTCTCCCATGTGCATCGGTGAG
GTGGCGCATGTCAGCGCGGAGATCACCTACACCTCCAAGCACTCTGTGGAGGTGCAGGTC
AACGTGATGTCCGAAAACATCCTCACAGGTGCCAAAAAGCTGACCAATAAGGCCACCCTG
TGGTATGTGCCCCTGTCGCTGAAGAATGTGGACAAGGTCCTCGAGGTGCCTCCTGTTGTG
TATTCCCGGCAGGAGCAGGAGGAGGAGGGCCGGAAGCGGTATGAAGCCCAGAAGCTGGAG
CGCATGGAGACCAAGTGGAGGAACGGGGACATCGTCCAGCCAGTCCTCAACCCAGAGCCG
AACACTGTCAGCTACAGCCAGTCCAGCTTGATCCACCTGGTGGGGCCTTCAGACTGCACC
CTGCACGGCTTTGTGCACGGAGGTGTGACCATGAAGCTCATGGATGAGGTCGCCGGGATC
GTGGCTGCACGCCACTGCAAGACCAACATCGTCACAGCTTCCGTGGACGCCATTAATTTT
CATGACAAGATCAGAAAAGGCTGCGTCATCACCATCTCGGGACGCATGACCTTCACGAGC
AATAAGTCCATGGAGATCGAGGTGTTGGTGGACGCCGACCCTGTTGTGGACAGCTCTCAG
AAGCGCTACCGGGCCGCCAGTGCCTTCTTCACCTACGTGTCGCTGAGCCAGGAAGGCAGG
TCGCTGCCTGTGCCCCAGCTGGTGCCCGAGACCGAGGACGAGAAGAAGCGCTTTGAGGAA
GGCAAAGGGCGGTACCTGCAGATGAAGGCGAAGCGACAGGGCCACGCGGAGCCTCAGCCC
TAG
|
| Enzyme 35 GenBank Gene ID |
NM_181864.2  |
| Enzyme 35 GeneCard ID |
ACOT7  |
| Enzyme 35 GenAtlas ID |
ACOT7  |
| Enzyme 35 HGNC ID |
HGNC:24157  |
| Enzyme 35 Chromosome Location |
1 |
| Enzyme 35 Locus |
1p36 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Yamada J, Kurata A, Hirata M, Taniguchi T, Takama H, Furihata T, Shiratori K, Iida N, Takagi-Sakuma M, Watanabe T, Kurosaki K, Endo T, Suga T: Purification, molecular cloning, and genomic organization of human brain long-chain acyl-CoA hydrolase. J Biochem (Tokyo). 1999 Dec;126(6):1013-9. [PubMed
]
- Yamada J, Kuramochi Y, Takagi M, Watanabe T, Suga T: Human brain acyl-CoA hydrolase isoforms encoded by a single gene. Biochem Biophys Res Commun. 2002 Nov 22;299(1):49-56. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
6336 |
| Enzyme 36 Name |
Acyl-coenzyme A thioesterase 2, mitochondrial |
| Enzyme 36 Synonyms |
- Acyl-CoA thioesterase 2
- Acyl-coenzyme A thioester hydrolase 2a
- CTE-Ia
- Long-chain acyl-CoA thioesterase 2
- ZAP128
|
| Enzyme 36 Gene Name |
ACOT2 |
| Enzyme 36 Protein Sequence |
>Acyl-coenzyme A thioesterase 2, mitochondrial
MSNKLLSPHPHSVVLRSEFKMASSPAVLRASRLYQWSLKSSAQFLGSPQLRQVGQIIRVP
ARMAATLILEPAGRCCWDEPVRIAVRGLAPEQPVTLRASLRDEKGALFQAHARYRADTLG
ELDLERAPALGGSFAGLEPMGLLWALEPEKPLVRLVKRDVRTPLAVELEVLDGHDPDPGR
LLCQTRHERYFLPPGVRREPVRVGRVRGTLFLPPEPGPFPGIVDMFGTGGGLLEYRASLL
AGKGFAVMALAYYNYEDLPKTMETLHLEYFEEAMNYLLSHPEVKGPGVGLLGISKGGELC
LSMASFLKGITAAVVINGSVANVGGTLHYKGETLPPVGVNRNRIKVTKDGYADIVDVLNS
PLEGPDQKSFIPVERAESTFLFLVGQDDHNWKSEFYANEACKRLQAHGRRKPQIICYPET
GHYIEPPYFPLCRASLHALVGSPIIWGGEPRAHAMAQVDAWKQLQTFFHKHLGGHEGTIP
SKV
|
| Enzyme 36 Number of Residues |
483 |
| Enzyme 36 Molecular Weight |
53218.0 |
| Enzyme 36 Theoretical pI |
8.62 |
| Enzyme 36 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 36 General Function |
Involved in thiolester hydrolase activity |
| Enzyme 36 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Displays high levels of activity on medium- and long chain acyl CoAs |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
- palmitoyl-CoA + H2O = CoA + palmitate [RN:R01274]
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
7023514  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
P49753  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
ACOT2_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>1452 bp
ATGTCTAACAAGCTTCTTTCTCCCCACCCCCATTCAGTTGTTCTCAGGTCTGAATTCAAA
ATGGCCTCATCTCCTGCTGTCCTTCGAGCGTCCCGGCTGTACCAATGGAGCCTGAAGAGT
TCGGCGCAGTTCCTGGGGTCTCCACAGCTGAGGCAGGTTGGTCAGATCATTAGGGTTCCT
GCTCGGATGGCGGCGACGCTGATCCTGGAGCCTGCGGGCCGCTGCTGCTGGGACGAACCG
GTGCGAATCGCCGTGCGCGGCCTAGCCCCGGAGCAGCCGGTCACGCTGCGCGCGTCCCTG
CGCGACGAGAAGGGCGCGCTTTTCCAGGCCCACGCGCGCTACCGCGCCGACACTCTTGGC
GAGCTGGACCTGGAGCGCGCGCCCGCGCTGGGCGGCAGCTTCGCGGGGCTTGAGCCCATG
GGGCTGCTCTGGGCCTTGGAGCCCGAGAAACCTTTGGTGCGGCTGGTGAAGCGCGACGTG
CGAACGCCCTTGGCCGTGGTGCTGGAGGTGCTGGATGGCCACGACCCCGACCCCGGGCGG
CTGCTGTGCCAGACGCGGCACGAGCGCTACTTCCTCCCGCCCGGGGTGCGGCGCGAGCCG
GTGCGCGTGGGCCGGGTGCGAGGCACGCTCTTCCTGCCGCCAGAACCTGGGCCCTTTCCT
GGGATTGTGGACATGTTCGGAACTGGAGGTGGCCTGCTGGAGTATCGGGCTAGTCTGCTG
GCTGGGAAGGGTTTTGCTGTGATGGCTCTGGCTTATTATAACTATGAAGACCTCCCCAAG
ACCATGGAGACGCTCCATCTGGAGTACTTTGAAGAAGCCATGAACTACTTGCTCAGTCAT
CCCGAGGTAAAAGGTCCAGGAGTTGGGCTGCTTGGAATTTCCAAAGGGGGTGAGCTCTGC
CTTTCCATGGCCTCTTTCCTGAAGGGCATCACGGCTGCTGTCGTCATCAACGGCTCTGTG
GCCAATGTTGGGGGAACCTTACGCTACAAGGGCGAGACCCTGCCCCCTGTGGGCGTCAAC
AGAAATCGCATCAAGGTGACCAAAGATGGCTATGCAGACATTGTGGATGTCCTGAACAGC
CCTTTGGAAGGACCTGACCAGAAGAGCTTCATTCCTGTGGAAAGGGCAGAGAGCACCTTC
CTGTTCCTGGTAGGTCAGGATGACCACAACTGGAAGAGTGAGTTCTATGCTAATGAGGCC
TGTAAACGCTTGCAGGCCCATGGGAGGAGAAAGCCCCAGATCATCTGTTACCCAGAGACA
GGGCACTATATTGAGCCTCCTTACTTCCCCCTGTGTCGGGCTTCCCTGCATGCCTTGGTG
GGCAGTCCTATTATCTGGGGAGGGGAGCCCAGGGCTCATGCCATGGCTCAGGTGGATGCT
TGGAAACAACTCCAGACTTTCTTCCACAAACACTTGGGTGGCCGCGAGGGGACAATCCCA
TCAAAAGTGTAA
|
| Enzyme 36 GenBank Gene ID |
AK001939  |
| Enzyme 36 GeneCard ID |
ACOT2  |
| Enzyme 36 GenAtlas ID |
ACOT2  |
| Enzyme 36 HGNC ID |
HGNC:18431  |
| Enzyme 36 Chromosome Location |
1 |
| Enzyme 36 Locus |
14q24.3 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Sherrington R, Rogaev EI, Liang Y, Rogaeva EA, Levesque G, Ikeda M, Chi H, Lin C, Li G, Holman K, et al.: Cloning of a gene bearing missense mutations in early-onset familial Alzheimer's disease. Nature. 1995 Jun 29;375(6534):754-60. [PubMed
]
- Hunt MC, Rautanen A, Westin MA, Svensson LT, Alexson SE: Analysis of the mouse and human acyl-CoA thioesterase (ACOT) gene clusters shows that convergent, functional evolution results in a reduced number of human peroxisomal ACOTs. FASEB J. 2006 Sep;20(11):1855-64. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Jones JM, Gould SJ: Identification of PTE2, a human peroxisomal long-chain acyl-CoA thioesterase. Biochem Biophys Res Commun. 2000 Aug 18;275(1):233-40. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
6338 |
| Enzyme 37 Name |
Acyl-coenzyme A thioesterase 8 |
| Enzyme 37 Synonyms |
- Acyl-CoA thioesterase 8
- Choloyl-coenzyme A thioesterase
- HIV-Nef-associated acyl-CoA thioesterase
- PTE-2
- Peroxisomal acyl-coenzyme A thioester hydrolase 1
- PTE-1
- Peroxisomal long-chain acyl-CoA thioesterase 1
- Thioesterase II
- hACTE-III
- hACTEIII
- hTE
|
| Enzyme 37 Gene Name |
ACOT8 |
| Enzyme 37 Protein Sequence |
>Acyl-coenzyme A thioesterase 8
MSSPQAPEDGQGCGDRGDPPGDLRSVLVTTVLNLEPLDEDLFRGRHYWVPAKRLFGGQIV
GQALVAAAKSVSEDVHVHSLHCYFVRAGDPKLPVLYQVERTRTGSSFSVRSVKAVQHGKP
IFICQASFQQAQPSPMQHQFSMPTVPPPEELLDCETLIDQYLRDPNLQKRYPLALNRIAA
QEVPIEIKPVNPSPLSQLQRMEPKQMFWVRARGYIGEGDMKMHCCVAAYISDYAFLGTAL
LPHQWQHKVHFMVSLDHSMWFHAPFRADHWMLYECESPWAGGSRGLVHGRLWRQDGVLAV
TCAQEGVIRVKPQVSESKL
|
| Enzyme 37 Number of Residues |
319 |
| Enzyme 37 Molecular Weight |
35914.0 |
| Enzyme 37 Theoretical pI |
7.60 |
| Enzyme 37 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- thiolester hydrolase activity
|
| Process |
- acyl-CoA metabolic process
- cellular metabolic process
- coenzyme metabolic process
- cofactor metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 37 General Function |
Involved in acyl-CoA thioesterase activity |
| Enzyme 37 Specific Function |
Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. May mediate Nef-induced down-regulation of CD4. Major thioesterase in peroxisomes. Competes with BAAT (Bile acid CoA:amino acid N- acyltransferase) for bile acid-CoA substrate (such as chenodeoxycholoyl-CoA). Shows a preference for medium-length fatty acyl-CoAs. May be involved in the metabolic regulation of peroxisome proliferation |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
- choloyl-CoA + H2O = cholate + CoA [RN:R07296]
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
Not Available |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
O14734  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
ACOT8_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>960 bp
ATGTCGTCCCCGCAGGCCCCAGAAGATGGGCAGGGCTGTGGCGACCGCGGCGATCCCCCT
GGGGACCTCCGTAGCGTCTTGGTCACGACCGTGCTCAACCTCGAGCCGCTGGACGAGGAT
CTCTTCAGAGGAAGGCATTACTGGGTACCGGCCAAGAGGCTGTTTGGTGGTCAGATCGTG
GGCCAGGCCCTGGTGGCTGCAGCCAAGTCTGTGAGTGAAGACGTCCACGTGCACTCCCTG
CACTGCTACTTTGTTCGGGCAGGGGACCCGAAGCTGCCAGTACTGTACCAAGTGGAGCGG
ACACGAACAGGGTCGAGCTTCTCGGTGCGCTCTGTGAAGGCCGTGCAACATGGGAAGCCC
ATCTTCATCTGCCAGGCCTCCTTCCAGCAGGCCCAGCCCAGCCCCATGCAGCACCAGTTC
TCCATGCCCACTGTGCCACCACCAGAAGAGCTGCTTGACTGTGAGACCCTCATTGACCAG
TATTTAAGGGACCCTAACCTCCAAAAGAGGTACCCATTGGCGCTCAACCGAATTGCTGCT
CAGGAGGTCCCCATTGAGATCAAGCCAGTAAACCCATCCCCCCTGAGCCAGCTGCAGAGA
ATGGAGCCCAAACAGATGTTCTGGGTGCGAGCCCGGGGCTATATTGGCGAGGGCGACATG
AAGATGCACTGCTGCGTGGCCGCCTATATCTCCGACTATGCCTTCTTGGGCACTGCACTG
CTGCCTCACCAGTGGCAGCACAAGGTGCACTTCATGGTCTCACTGGACCATTCCATGTGG
TTCCACGCCCCCTTCCGAGCTGACCACTGGATGCTCTATGAATGCGAGAGCCCCTGGGCC
GGTGGCTCTCGGGGGCTGGTCCATGGGCGGCTGTGGCGTCAGGATGGAGTCCTAGCTGTG
ACCTGTGCCCAGGAGGGCGTGATCCGAGTGAAGCCCCAGGTCTCAGAGAGCAAGCTGTAG
|
| Enzyme 37 GenBank Gene ID |
AF014404  |
| Enzyme 37 GeneCard ID |
ACOT8  |
| Enzyme 37 GenAtlas ID |
ACOT8  |
| Enzyme 37 HGNC ID |
HGNC:15919  |
| Enzyme 37 Chromosome Location |
2 |
| Enzyme 37 Locus |
20q13.12 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Watanabe H, Shiratori T, Shoji H, Miyatake S, Okazaki Y, Ikuta K, Sato T, Saito T: A novel acyl-CoA thioesterase enhances its enzymatic activity by direct binding with HIV Nef. Biochem Biophys Res Commun. 1997 Sep 8;238(1):234-9. [PubMed
]
- Liu LX, Margottin F, Le Gall S, Schwartz O, Selig L, Benarous R, Benichou S: Binding of HIV-1 Nef to a novel thioesterase enzyme correlates with Nef-mediated CD4 down-regulation. J Biol Chem. 1997 May 23;272(21):13779-85. [PubMed
]
- Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ: Identification of peroxisomal acyl-CoA thioesterases in yeast and humans. J Biol Chem. 1999 Apr 2;274(14):9216-23. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ishizuka M, Toyama Y, Watanabe H, Fujiki Y, Takeuchi A, Yamasaki S, Yuasa S, Miyazaki M, Nakajima N, Taki S, Saito T: Overexpression of human acyl-CoA thioesterase upregulates peroxisome biogenesis. Exp Cell Res. 2004 Jul 1;297(1):127-41. [PubMed
]
- Hunt MC, Alexson SE: The role Acyl-CoA thioesterases play in mediating intracellular lipid metabolism. Prog Lipid Res. 2002 Mar;41(2):99-130. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
6373 |
| Enzyme 38 Name |
Acid ceramidase |
| Enzyme 38 Synonyms |
- AC
- Acylsphingosine deacylase
- N-acylsphingosine amidohydrolase
- Putative 32 kDa heart protein
- PHP32
- Acid ceramidase subunit alpha
- Acid ceramidase subunit beta
|
| Enzyme 38 Gene Name |
ASAH1 |
| Enzyme 38 Protein Sequence |
>Acid ceramidase
MPGRSCVALVLLAAAVSCAVAQHAPPWTEDCRKSTYPPSGPTYRGAVPWYTINLDLPPYK
RWHELMLDKAPVLKVIVNSLKNMINTFVPSGKIMQVVDEKLPGLLGNFPGPFEEEMKGIA
AVTDIPLGEIISFNIFYELFTICTSIVAEDKKGHLIHGRNMDFGVFLGWNINNDTWVITE
QLKPLTVNLDFQRNNKTVFKASSFAGYVGMLTGFKPGLFSLTLNERFSINGGYLGILEWI
LGKKDVMWIGFLTRTVLENSTSYEEAKNLLTKTKILAPAYFILGGNQSGEGCVITRDRKE
SLDVYELDAKQGRWYVVQTNYDRWKHPFFLDDRRTPAKMCLNRTSQENISFETMYDVLST
KPVLNKLTVYTTLIDVTKGQFETYLRDCPDPCIGW
|
| Enzyme 38 Number of Residues |
395 |
| Enzyme 38 Molecular Weight |
44659.3 |
| Enzyme 38 Theoretical pI |
7.70 |
| Enzyme 38 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
- intracellular membrane-bounded organelle
- lysosome
- lytic vacuole
- membrane-bounded organelle
- organelle
- vacuole
|
|
| Enzyme 38 General Function |
Involved in lipid metabolic process |
| Enzyme 38 Specific Function |
Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid |
| Enzyme 38 Pathways |
|
| Enzyme 38 Reactions |
- N-acylsphingosine + H2O = a carboxylate + sphingosine [RN:R01493]
|
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
189011548  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q13510  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
ASAH1_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>1188 bp
ATGCCGGGCCGGAGTTGCGTCGCCTTAGTCCTCCTGGCTGCCGCCGTCAGCTGTGCCGTC
GCGCAGCACGCGCCGCCGTGGACAGAGGACTGCAGAAAATCAACCTATCCTCCTTCAGGA
CCAACGTACAGAGGTGCAGTTCCATGGTACACCATAAATCTTGACTTACCACCCTACAAA
AGATGGCATGAATTGATGCTTGACAAGGCACCAGTGCTAAAGGTTATAGTGAATTCTCTG
AAGAATATGATAAATACATTCGTGCCAAGTGGAAAAATTATGCAGGTGGTGGATGAAAAA
TTGCCTGGCCTACTTGGCAACTTTCCTGGCCCTTTTGAAGAGGAAATGAAGGGTATTGCC
GCTGTTACTGATATACCTTTAGGAGAGATTATTTCATTCAATATTTTTTATGAATTATTT
ACCATTTGTACTTCAATAGTAGCAGAAGACAAAAAAGGTCATCTAATACATGGGAGAAAC
ATGGATTTTGGAGTATTTCTTGGGTGGAACATAAATAATGATACCTGGGTCATAACTGAG
CAACTAAAACCTTTAACAGTGAATTTGGATTTCCAAAGAAACAACAAAACTGTCTTCAAG
GCTTCAAGCTTTGCTGGCTATGTGGGCATGTTAACAGGATTCAAACCAGGACTGTTCAGT
CTTACACTGAATGAACGTTTCAGTATAAATGGTGGTTATCTGGGTATTCTAGAATGGATT
CTGGGAAAGAAAGATGTCATGTGGATAGGGTTCCTCACTAGAACAGTTCTGGAAAATAGC
ACAAGTTATGAAGAAGCCAAGAATTTATTGACCAAGACCAAGATATTGGCCCCAGCCTAC
TTTATCCTGGGAGGCAACCAGTCTGGGGAAGGTTGTGTGATTACACGAGACAGAAAGGAA
TCATTGGATGTATATGAACTCGATGCTAAGCAGGGTAGATGGTATGTGGTACAAACAAAT
TATGACCGTTGGAAACATCCCTTCTTCCTTGATGATCGCAGAACGCCTGCAAAGATGTGT
CTGAACCGCACCAGCCAAGAGAATATCTCATTTGAAACCATGTATGATGTCCTGTCAACA
AAACCTGTCCTCAACAAGCTGACCGTATACACAACCTTGATAGATGTTACCAAAGGTCAA
TTCGAAACTTACCTGCGGGACTGCCCTGACCCTTGTATAGGTTGGTGA
|
| Enzyme 38 GenBank Gene ID |
NM_177924.3  |
| Enzyme 38 GeneCard ID |
ASAH1  |
| Enzyme 38 GenAtlas ID |
ASAH1  |
| Enzyme 38 HGNC ID |
HGNC:735  |
| Enzyme 38 Chromosome Location |
8 |
| Enzyme 38 Locus |
8p22 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
- Koch J, Gartner S, Li CM, Quintern LE, Bernardo K, Levran O, Schnabel D, Desnick RJ, Schuchman EH, Sandhoff K: Molecular cloning and characterization of a full-length complementary DNA encoding human acid ceramidase. Identification Of the first molecular lesion causing Farber disease. J Biol Chem. 1996 Dec 20;271(51):33110-5. [PubMed
]
- Zhang Z, Mandal AK, Mital A, Popescu N, Zimonjic D, Moser A, Moser H, Mukherjee AB: Human acid ceramidase gene: novel mutations in Farber disease. Mol Genet Metab. 2000 Aug;70(4):301-9. [PubMed
]
- Li CM, Park JH, He X, Levy B, Chen F, Arai K, Adler DA, Disteche CM, Koch J, Sandhoff K, Schuchman EH: The human acid ceramidase gene (ASAH): structure, chromosomal location, mutation analysis, and expression. Genomics. 1999 Dec 1;62(2):223-31. [PubMed
]
- Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bernardo K, Hurwitz R, Zenk T, Desnick RJ, Ferlinz K, Schuchman EH, Sandhoff K: Purification, characterization, and biosynthesis of human acid ceramidase. J Biol Chem. 1995 May 12;270(19):11098-102. [PubMed
]
- Zhang H, Li XJ, Martin DB, Aebersold R: Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry. Nat Biotechnol. 2003 Jun;21(6):660-6. Epub 2003 May 18. [PubMed
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
- Lewandrowski U, Moebius J, Walter U, Sickmann A: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol Cell Proteomics. 2006 Feb;5(2):226-33. Epub 2005 Oct 31. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Bar J, Linke T, Ferlinz K, Neumann U, Schuchman EH, Sandhoff K: Molecular analysis of acid ceramidase deficiency in patients with Farber disease. Hum Mutat. 2001 Mar;17(3):199-209. [PubMed
]
- Muramatsu T, Sakai N, Yanagihara I, Yamada M, Nishigaki T, Kokubu C, Tsukamoto H, Ito M, Inui K: Mutation analysis of the acid ceramidase gene in Japanese patients with Farber disease. J Inherit Metab Dis. 2002 Nov;25(7):585-92. [PubMed
]
- Devi AR, Gopikrishna M, Ratheesh R, Savithri G, Swarnalata G, Bashyam M: Farber lipogranulomatosis: clinical and molecular genetic analysis reveals a novel mutation in an Indian family. J Hum Genet. 2006;51(9):811-4. Epub 2006 Sep 2. [PubMed
]
|
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
6700 |
| Enzyme 39 Name |
Homeodomain-interacting protein kinase 1 |
| Enzyme 39 Synonyms |
Not Available |
| Enzyme 39 Gene Name |
HIPK1 |
| Enzyme 39 Protein Sequence |
>Homeodomain-interacting protein kinase 1
MASQLQVFSPPSVSSSAFCSAKKLKIEPSGWDVSGQSSNDKYYTHSKTLPATQGQANSSH
QVANFNIPAYDQGLLLPAPAVEHIVVTAADSSGSAATSTFQSSQTLTHRSNVSLLEPYQK
CGLKRKSEEVDSNGSVQIIEEHPPLMLQNRTVVGAAATTTTVTTKSSSSSGEGDYQLVQH
EILCSMTNSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQGQIEVSILSR
LSSENADEYNFVRSYECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILQQVA
TALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKAVCSTYLQSRYYRA
PEIILGLPFCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLPAEYLLSAGT
KTTRFFNRDPNLGYPLWRLKTPEEHELETGIKSKEARKYIFNCLDDMAQVNMSTDLEGTD
MLAEKADRREYIDLLKKMLTIDADKRITPLKTLNHQFVTMTHLLDFPHSNHVKSCFQNME
ICKRRVHMYDTVSQIKSPFTTHVAPNTSTNLTMSFSNQLNTVHNQASVLASSSTAAAATL
SLANSDVSLLNYQSALYPSSAAPVPGVAQQGVSLQPGTTQICTQTDPFQQTFIVCPPAFQ
TGLQATTKHSGFPVRMDNAVPIVPQAPAAQPLQIQSGVLTQGSCTPLMVATLHPQVATIT
PQYAVPFTLSCAAGRPALVEQTAAVLQAWPGGTQQILLPSTWQQLPGVALHNSVQPTAMI
PEAMGSGQQLADWRNAHSHGNQYSTIMQQPSLLTNHVTLATAQPLNVGVAHVVRQQQSSS
LPSKKNKQSAPVSSKSSLDVLPSQVYSLVGSSPLRTTSSYNSLVPVQDQHQPIIIPDTPS
PPVSVITIRSDTDEEEDNKYKPSSSGLKPRSNVISYVTVNDSPDSDSSLSSPYSTDTLSA
LRGNSGSVLEGPGRVVADGTGTRTIIVPPLKTQLGDCTVATQASGLLSNKTKPVASVSGQ
SSGCCITPTGYRAQRGGTSAAQPLNLSQNQQSSAAPTSQERSSNPAPRRQQAFVAPLSQA
PYTFQHGSPLHSTGHPHLAPAPAHLPSQAHLYTYAAPTSAAALGSTSSIAHLFSPQGSSR
HAAAYTTHPSTLVHQVPVSVGPSLLTSASVAPAQYQHQFATQSYIGSSRGSTIYTGYPLS
PTKISQYSYL
|
| Enzyme 39 Number of Residues |
1210 |
| Enzyme 39 Molecular Weight |
130841.6 |
| Enzyme 39 Theoretical pI |
8.31 |
| Enzyme 39 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- kinase activity
- nucleoside binding
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- cellular metabolic process
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
|
| Component |
| — |
|
| Enzyme 39 General Function |
Involved in protein kinase activity |
| Enzyme 39 Specific Function |
May play a role as a corepressor for homeodomain transcription factors. Phosphorylates DAXX in response to stress, and mediates its translocation from the nucleus to the cytoplasm. May be involved in malignant squamous cell tumor formation |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
28411264  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q86Z02  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
HIPK1_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>3633 bp
ATGGCATCACAGCTGCAAGTGTTTTCGCCCCCATCAGTGTCGTCGAGTGCCTTCTGCAGT
GCGAAGAAACTGAAAATAGAGCCCTCTGGCTGGGATGTTTCAGGACAGAGTAGCAACGAC
AAATATTATACCCACAGCAAAACCCTCCCAGCCACACAAGGGCAAGCCAACTCCTCTCAC
CAGGTAGCAAATTTCAACATCCCTGCTTACGACCAGGGCCTCCTCCTCCCAGCTCCTGCA
GTGGAGCATATTGTTGTAACAGCCGCTGATAGCTCGGGCAGTGCTGCTACATCAACCTTC
CAAAGCAGCCAGACCCTGACTCACAGAAGCAACGTTTCTTTGCTTGAGCCATATCAAAAA
TGTGGATTGAAACGAAAAAGTGAGGAAGTTGACAGCAACGGTAGTGTGCAGATCATAGAA
GAACATCCCCCTCTCATGCTGCAAAACAGGACTGTGGTGGGTGCTGCTGCCACAACCACC
ACTGTGACCACAAAGAGTAGCAGTTCCAGCGGAGAAGGGGATTACCAGCTGGTCCAGCAT
GAGATCCTTTGCTCTATGACCAATAGCTATGAAGTCTTGGAGTTCCTAGGCCGGGGGACA
TTTGGACAGGTGGCTAAGTGCTGGAAGAGGAGCACCAAGGAAATTGTGGCTATTAAAATC
TTGAAGAACCACCCCTCCTATGCCAGACAAGGACAGATTGAAGTGAGCATCCTTTCCCGC
CTAAGCAGTGAAAATGCTGATGAGTATAATTTTGTCCGTTCATACGAGTGCTTTCAGCAT
AAGAATCACACCTGCCTTGTTTTTGAAATGTTGGAGCAGAACTTATATGATTTTCTAAAG
CAAAACAAATTTAGCCCACTGCCACTCAAGTACATCAGACCAATCTTGCAGCAGGTGGCC
ACAGCCTTGATGAAGCTCAAGAGTCTTGGTCTGATCCACGCTGACCTTAAGCCTGAAAAC
ATCATGCTGGTTGATCCAGTTCGCCAGCCCTACCGAGTGAAGGTCATTGACTTTGGTTCT
GCTAGTCACGTTTCCAAAGCTGTGTGCTCAACCTACTTACAGTCACGTTACTACAGAGCT
CCTGAAATTATTCTTGGGTTACCATTTTGTGAAGCTATTGATATGTGGTCACTGGGCTGT
GTGATAGCTGAGCTGTTCCTGGGATGGCCTCTTTATCCTGGTGCTTCAGAATATGATCAG
ATTCGTTATATTTCACAAACACAAGGCTTGCCAGCTGAATATCTTCTCAGTGCCGGAACA
AAAACAACCAGGTTTTTCAACAGAGATCCTAATTTGGGGTACCCACTGTGGAGGCTTAAG
ACACCTGAAGAACATGAACTGGAGACTGGAATAAAATCAAAAGAAGCTCGGAAGTACATT
TTTAATTGCTTAGATGACATGGCTCAGGTGAATATGTCTACAGACCTGGAGGGAACAGAC
ATGTTGGCAGAGAAGGCAGACCGAAGAGAATACATTGATCTGTTAAAGAAAATGCTCACA
ATTGATGCAGATAAGAGAATTACCCCTCTAAAAACTCTTAACCATCAGTTTGTGACAATG
ACTCACCTTTTGGATTTTCCACATAGCAATCATGTTAAGTCTTGTTTTCAGAACATGGAG
ATCTGCAAGCGGAGGGTTCACATGTATGATACAGTGAGTCAGATCAAGAGTCCCTTCACT
ACACATGTTGCCCCAAATACAAGCACAAATCTAACCATGAGCTTCAGCAATCAGCTCAAT
ACAGTGCACAATCAGGCCAGTGTTCTAGCTTCCAGTTCTACTGCAGCAGCTGCTACTCTT
TCTCTGGCTAATTCAGATGTCTCACTACTAAACTACCAGTCAGCTTTGTACCCATCATCT
GCTGCACCAGTTCCTGGAGTTGCCCAGCAGGGTGTTTCCTTGCAGCCTGGAACCACCCAG
ATTTGCACTCAGACAGATCCATTCCAACAGACATTTATAGTATGTCCACCTGCGTTTCAA
ACTGGACTACAAGCAACAACAAAGCATTCTGGATTCCCTGTGAGGATGGATAATGCTGTA
CCGATTGTACCCCAGGCACCAGCTGCTCAGCCACTACAGATTCAGTCAGGAGTTCTCACG
CAGGGAAGCTGTACACCACTAATGGTAGCAACTCTCCACCCTCAAGTAGCCACCATCACA
CCGCAGTATGCGGTGCCCTTTACTCTGAGCTGCGCAGCCGGCCGGCCGGCGCTGGTTGAA
CAGACTGCCGCTGTACTGCAGGCGTGGCCTGGAGGGACTCAGCAAATTCTCCTGCCTTCA
ACTTGGCAACAGTTGCCTGGGGTAGCTCTACACAACTCTGTCCAGCCCACAGCAATGATT
CCAGAGGCCATGGGGAGTGGACAGCAGCTAGCTGACTGGAGGAATGCCCACTCTCATGGC
AACCAGTACAGCACTATCATGCAGCAGCCATCCTTGCTGACTAACCATGTGACATTGGCC
ACTGCTCAGCCTCTGAATGTTGGTGTTGCCCATGTTGTCAGACAACAACAATCCAGTTCC
CTCCCTTCGAAGAAGAATAAGCAGTCAGCTCCAGTCTCTTCCAAGTCCTCTCTAGATGTT
CTGCCTTCCCAAGTCTATTCTCTGGTTGGGAGCAGTCCCCTCCGCACCACATCTTCTTAT
AATTCCTTGGTCCCTGTCCAAGATCAGCATCAGCCCATCATCATTCCAGATACTCCCAGC
CCTCCTGTGAGTGTCATCACTATCCGAAGTGACACTGATGAGGAAGAGGACAACAAATAC
AAGCCCAGTAGCTCTGGACTGAAGCCAAGGTCTAATGTCATCAGTTATGTCACTGTCAAT
GATTCTCCAGACTCTGACTCTTCTTTGAGCAGCCCTTATTCCACTGATACCCTGAGTGCT
CTCCGAGGCAATAGTGGATCCGTTTTGGAGGGGCCTGGCAGAGTTGTGGCAGATGGCACT
GGCACCCGCACTATCATTGTGCCTCCACTGAAAACTCAGCTTGGTGACTGCACTGTAGCA
ACCCAGGCCTCAGGTCTCCTGAGCAATAAGACTAAGCCAGTCGCTTCAGTGAGTGGGCAG
TCATCTGGATGCTGTATCACCCCCACAGGGTATCGAGCTCAACGCGGGGGGACCAGTGCA
GCACAACCACTCAATCTTAGCCAGAACCAGCAGTCATCGGCGGCTCCAACCTCACAGGAG
AGAAGCAGCAACCCAGCCCCCCGCAGGCAGCAGGCATTTGTGGCCCCTCTCTCCCAAGCC
CCCTACACCTTCCAGCATGGCAGCCCGCTACACTCGACAGGGCACCCACACCTTGCCCCG
GCCCCTGCTCACCTGCCAAGCCAGGCTCATCTGTATACGTATGCTGCCCCGACTTCTGCT
GCTGCACTGGGCTCAACCAGCTCCATTGCTCATCTTTTCTCCCCACAGGGTTCCTCAAGG
CATGCTGCAGCCTATACCACTCACCCTAGCACTTTGGTGCACCAGGTCCCTGTCAGTGTT
GGGCCCAGCCTCCTCACTTCTGCCAGCGTGGCCCCTGCTCAGTACCAACACCAGTTTGCC
ACCCAATCCTACATTGGGTCTTCCCGAGGCTCAACAATTTACACTGGATACCCGCTGAGT
CCTACCAAGATCAGCCAGTATTCCTACTTATAG
|
| Enzyme 39 GenBank Gene ID |
AB089957  |
| Enzyme 39 GeneCard ID |
HIPK1  |
| Enzyme 39 GenAtlas ID |
HIPK1  |
| Enzyme 39 HGNC ID |
HGNC:19006  |
| Enzyme 39 Chromosome Location |
1 |
| Enzyme 39 Locus |
1p13.2 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 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
]
- 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
]
- Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed
]
- Song JJ, Lee YJ: Role of the ASK1-SEK1-JNK1-HIPK1 signal in Daxx trafficking and ASK1 oligomerization. J Biol Chem. 2003 Nov 21;278(47):47245-52. Epub 2003 Sep 10. [PubMed
]
- Ecsedy JA, Michaelson JS, Leder P: Homeodomain-interacting protein kinase 1 modulates Daxx localization, phosphorylation, and transcriptional activity. Mol Cell Biol. 2003 Feb;23(3):950-60. [PubMed
]
- Kondo S, Lu Y, Debbas M, Lin AW, Sarosi I, Itie A, Wakeham A, Tuan J, Saris C, Elliott G, Ma W, Benchimol S, Lowe SW, Mak TW, Thukral SK: Characterization of cells and gene-targeted mice deficient for the p53-binding kinase homeodomain-interacting protein kinase 1 (HIPK1). Proc Natl Acad Sci U S A. 2003 Apr 29;100(9):5431-6. Epub 2003 Apr 17. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
7657 |
| Enzyme 40 Name |
Peroxisome proliferator-activated receptor gamma |
| Enzyme 40 Synonyms |
- PPAR-gamma
- Nuclear receptor subfamily 1 group C member 3
|
| Enzyme 40 Gene Name |
PPARG |
| Enzyme 40 Protein Sequence |
>Peroxisome proliferator-activated receptor gamma
MGETLGDSPIDPESDSFTDTLSANISQEMTMVDTEMPFWPTNFGISSVDLSVMEDHSHSF
DIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKT
QLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNC
RIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLR
ALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQE
QSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLAS
LMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVKFNALELDDSDLAIFIAVII
LSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQL
LQVIKKTETDMSLHPLLQEIYKDLY
|
| Enzyme 40 Number of Residues |
505 |
| Enzyme 40 Molecular Weight |
57619.6 |
| Enzyme 40 Theoretical pI |
5.77 |
| Enzyme 40 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- ligand-dependent nuclear receptor activity
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- receptor activity
- sequence-specific DNA binding
- sequence-specific DNA binding transcription factor activity
- signal transducer activity
- steroid hormone receptor activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 40 General Function |
Involved in DNA binding |
| Enzyme 40 Specific Function |
Receptor that binds peroxisome proliferators such as hypolipidemic drugs and fatty acids. Once activated by a ligand, the receptor binds to a promoter element in the gene for acyl-CoA oxidase and activates its transcription. It therefore controls the peroxisomal beta-oxidation pathway of fatty acids. Key regulator of adipocyte differentiation and glucose homeostasis |
| 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 |
P37231  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
PPARG_HUMAN  |
| Enzyme 40 PDB ID |
1I7I  |
| Enzyme 40 PDB File |
Show |
| Enzyme 40 3D Structure |
|
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>1518 bp
ATGGGTGAAACTCTGGGAGATTCTCCTATTGACCCAGAAAGCGATTCCTTCACTGATACA
CTGTCTGCAAACATATCACAAGAAATGACCATGGTTGACACAGAGATGCCATTCTGGCCC
ACCAACTTTGGGATCAGCTCCGTGGATCTCTCCGTAATGGAAGACCACTCCCACTCCTTT
GATATCAAGCCCTTCACTACTGTTGACTTCTCCAGCATTTCTACTCCACATTACGAAGAC
ATTCCATTCACAAGAACAGATCCAGTGGTTGCAGATTACAAGTATGACCTGAAACTTCAA
GAGTACCAAAGTGCAATCAAAGTGGAGCCTGCATCTCCACCTTATTATTCTGAGAAGACT
CAGCTCTACAATAAGCCTCATGAAGAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGT
GTCTGTGGAGATAAAGCTTCTGGATTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAG
GGTTTCTTCCGGAGAACAATCAGATTGAAGCTTATCTATGACAGATGTGATCTTAACTGT
CGGATCCACAAAAAAAGTAGAAATAAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCA
GTGGGGATGTCTCATAATGCCATCAGGTTTGGGCGGATGCCACAGGCCGAGAAGGAGAAG
CTGTTGGCGGAGATCTCCAGTGATATCGACCAGCTGAATCCAGAGTCCGCTGACCTCCGG
GCCCTGGCAAAACATTTGTATGACTCATACATAAAGTCCTTCCCGCTGACCAAAGCAAAG
GCGAGGGCGATCTTGACAGGAAAGACAACAGACAAATCACCATTCGTTATCTATGACATG
AATTCCTTAATGATGGGAGAAGATAAAATCAAGTTCAAACACATCACCCCCCTGCAGGAG
CAGAGCAAAGAGGTGGCCATCCGCATCTTTCAGGGCTGCCAGTTTCGCTCCGTGGAGGCT
GTGCAGGAGATCACAGAGTATGCCAAAAGCATTCCTGGTTTTGTAAATCTTGACTTGAAC
GACCAAGTAACTCTCCTCAAATATGGAGTCCACGAGATCATTTACACAATGCTGGCCTCC
TTGATGAATAAAGATGGGGTTCTCATATCCGAGGGCCAAGGCTTCATGACAAGGGAGTTT
CTAAAGAGCCTGCGAAAGCCTTTTGGTGACTTTATGGAGCCCAAGTTTGAGTTTGCTGTG
AAGTTCAATGCACTGGAATTAGATGACAGCGACTTGGCAATATTTATTGCTGTCATTATT
CTCAGTGGAGACCGCCCAGGTTTGCTGAATGTGAAGCCCATTGAAGACATTCAAGACAAC
CTGCTACAAGCCCTGGAGCTCCAGCTGAAGCTGAACCACCCTGAGTCCTCACAGCTGTTT
GCCAAGCTGCTCCAGAAAATGACAGACCTCAGACAGATTGTCACGGAACACGTGCAGCTA
CTGCAGGTGATCAAGAAGACGGAGACAGACATGAGTCTTCACCCGCTCCTGCAGGAGATC
TACAAGGACTTGTACTAG
|
| Enzyme 40 GenBank Gene ID |
U79012  |
| Enzyme 40 GeneCard ID |
PPARG  |
| Enzyme 40 GenAtlas ID |
PPARG  |
| Enzyme 40 HGNC ID |
HGNC:9236  |
| Enzyme 40 Chromosome Location |
3 |
| Enzyme 40 Locus |
3p25 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- Mukherjee R, Jow L, Croston GE, Paterniti JR Jr: Identification, characterization, and tissue distribution of human peroxisome proliferator-activated receptor (PPAR) isoforms PPARgamma2 versus PPARgamma1 and activation with retinoid X receptor agonists and antagonists. J Biol Chem. 1997 Mar 21;272(12):8071-6. [PubMed
]
- Elbrecht A, Chen Y, Cullinan CA, Hayes N, Leibowitz M, Moller DE, Berger J: Molecular cloning, expression and characterization of human peroxisome proliferator activated receptors gamma 1 and gamma 2. Biochem Biophys Res Commun. 1996 Jul 16;224(2):431-7. [PubMed
]
- Yanase T, Yashiro T, Takitani K, Kato S, Taniguchi S, Takayanagi R, Nawata H: Differential expression of PPAR gamma1 and gamma2 isoforms in human adipose tissue. Biochem Biophys Res Commun. 1997 Apr 17;233(2):320-4. [PubMed
]
- Greene ME, Blumberg B, McBride OW, Yi HF, Kronquist K, Kwan K, Hsieh L, Greene G, Nimer SD: Isolation of the human peroxisome proliferator activated receptor gamma cDNA: expression in hematopoietic cells and chromosomal mapping. Gene Expr. 1995;4(4-5):281-99. [PubMed
]
- Okazawa H, Mori H, Tamori Y, Araki S, Niki T, Masugi J, Kawanishi M, Kubota T, Shinoda H, Kasuga M: No coding mutations are detected in the peroxisome proliferator-activated receptor-gamma gene in Japanese patients with lipoatrophic diabetes. Diabetes. 1997 Nov;46(11):1904-6. [PubMed
]
- Lambe KG, Tugwood JD: A human peroxisome-proliferator-activated receptor-gamma is activated by inducers of adipogenesis, including thiazolidinedione drugs. Eur J Biochem. 1996 Jul 1;239(1):1-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
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- Drori S, Girnun GD, Tou L, Szwaya JD, Mueller E, Xia K, Shivdasani RA, Spiegelman BM: Hic-5 regulates an epithelial program mediated by PPARgamma. Genes Dev. 2005 Feb 1;19(3):362-75. [PubMed
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- Uppenberg J, Svensson C, Jaki M, Bertilsson G, Jendeberg L, Berkenstam A: Crystal structure of the ligand binding domain of the human nuclear receptor PPARgamma. J Biol Chem. 1998 Nov 20;273(47):31108-12. [PubMed
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- Nolte RT, Wisely GB, Westin S, Cobb JE, Lambert MH, Kurokawa R, Rosenfeld MG, Willson TM, Glass CK, Milburn MV: Ligand binding and co-activator assembly of the peroxisome proliferator-activated receptor-gamma. Nature. 1998 Sep 10;395(6698):137-43. [PubMed
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- Gampe RT Jr, Montana VG, Lambert MH, Miller AB, Bledsoe RK, Milburn MV, Kliewer SA, Willson TM, Xu HE: Asymmetry in the PPARgamma/RXRalpha crystal structure reveals the molecular basis of heterodimerization among nuclear receptors. Mol Cell. 2000 Mar;5(3):545-55. [PubMed
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- Xu HE, Lambert MH, Montana VG, Plunket KD, Moore LB, Collins JL, Oplinger JA, Kliewer SA, Gampe RT Jr, McKee DD, Moore JT, Willson TM: Structural determinants of ligand binding selectivity between the peroxisome proliferator-activated receptors. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13919-24. Epub 2001 Nov 6. [PubMed
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- Cronet P, Petersen JF, Folmer R, Blomberg N, Sjoblom K, Karlsson U, Lindstedt EL, Bamberg K: Structure of the PPARalpha and -gamma ligand binding domain in complex with AZ 242; ligand selectivity and agonist activation in the PPAR family. Structure. 2001 Aug;9(8):699-706. [PubMed
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- Ebdrup S, Pettersson I, Rasmussen HB, Deussen HJ, Frost Jensen A, Mortensen SB, Fleckner J, Pridal L, Nygaard L, Sauerberg P: Synthesis and biological and structural characterization of the dual-acting peroxisome proliferator-activated receptor alpha/gamma agonist ragaglitazar. J Med Chem. 2003 Apr 10;46(8):1306-17. [PubMed
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- Ostberg T, Svensson S, Selen G, Uppenberg J, Thor M, Sundbom M, Sydow-Backman M, Gustavsson AL, Jendeberg L: A new class of peroxisome proliferator-activated receptor agonists with a novel binding epitope shows antidiabetic effects. J Biol Chem. 2004 Sep 24;279(39):41124-30. Epub 2004 Jul 15. [PubMed
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- Haffner CD, Lenhard JM, Miller AB, McDougald DL, Dwornik K, Ittoop OR, Gampe RT Jr, Xu HE, Blanchard S, Montana VG, Consler TG, Bledsoe RK, Ayscue A, Croom D: Structure-based design of potent retinoid X receptor alpha agonists. J Med Chem. 2004 Apr 8;47(8):2010-29. [PubMed
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- Shi GQ, Dropinski JF, McKeever BM, Xu S, Becker JW, Berger JP, MacNaul KL, Elbrecht A, Zhou G, Doebber TW, Wang P, Chao YS, Forrest M, Heck JV, Moller DE, Jones AB: Design and synthesis of alpha-aryloxyphenylacetic acid derivatives: a novel class of PPARalpha/gamma dual agonists with potent antihyperglycemic and lipid modulating activity. J Med Chem. 2005 Jun 30;48(13):4457-68. [PubMed
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- Hopkins CR, O'neil SV, Laufersweiler MC, Wang Y, Pokross M, Mekel M, Evdokimov A, Walter R, Kontoyianni M, Petrey ME, Sabatakos G, Roesgen JT, Richardson E, Demuth TP Jr: Design and synthesis of novel N-sulfonyl-2-indole carboxamides as potent PPAR-gamma binding agents with potential application to the treatment of osteoporosis. Bioorg Med Chem Lett. 2006 Nov 1;16(21):5659-63. Epub 2006 Aug 21. [PubMed
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- Lu IL, Huang CF, Peng YH, Lin YT, Hsieh HP, Chen CT, Lien TW, Lee HJ, Mahindroo N, Prakash E, Yueh A, Chen HY, Goparaju CM, Chen X, Liao CC, Chao YS, Hsu JT, Wu SY: Structure-based drug design of a novel family of PPARgamma partial agonists: virtual screening, X-ray crystallography, and in vitro/in vivo biological activities. J Med Chem. 2006 May 4;49(9):2703-12. [PubMed
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- Yen CJ, Beamer BA, Negri C, Silver K, Brown KA, Yarnall DP, Burns DK, Roth J, Shuldiner AR: Molecular scanning of the human peroxisome proliferator activated receptor gamma (hPPAR gamma) gene in diabetic Caucasians: identification of a Pro12Ala PPAR gamma 2 missense mutation. Biochem Biophys Res Commun. 1997 Dec 18;241(2):270-4. [PubMed
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- Ristow M, Muller-Wieland D, Pfeiffer A, Krone W, Kahn CR: Obesity associated with a mutation in a genetic regulator of adipocyte differentiation. N Engl J Med. 1998 Oct 1;339(14):953-9. [PubMed
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]
|
| Enzyme 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
8375 |
| Enzyme 41 Name |
Long-chain fatty acid transport protein 6 |
| Enzyme 41 Synonyms |
- FATP-6
- Fatty acid transport protein 6
- Fatty-acid-coenzyme A ligase, very long-chain 2
- Solute carrier family 27 member 6
- Very long-chain acyl-CoA synthetase homolog 1
- VLCSH1
- hVLCS-H1
|
| Enzyme 41 Gene Name |
SLC27A6 |
| Enzyme 41 Protein Sequence |
>Long-chain fatty acid transport protein 6
MLLSWLTVLGAGMVVLHFLQKLLFPYFWDDFWFVLKVVLIIIRLKKYEKRGELVTVLDKF
LSHAKRQPRKPFIIYEGDIYTYQDVDKRSSRVAHVFLNHSSLKKGDTVALLMSNEPDFVH
VWFGLAKLGCVVAFLNTNIRSNSLLNCIRACGPRALVVGADLLGTVEEILPSLSENISVW
GMKDSVPQGVISLKEKLSTSPDEPVPRSHHVVSLLKSTCLYIFTSGTTGLPKAAVISQLQ
VLRGSAVLWAFGCTAHDIVYITLPLYHSSAAILGISGCVELGATCVLKKKFSASQFWSDC
KKYDVTVFQYIGELCRYLCKQSKREGEKDHKVRLAIGNGIRSDVWREFLDRFGNIKVCEL
YAATESSISFMNYTGRIGAIGRTNLFYKLLSTFDLIKYDFQKDEPMRNEQGWCIHVKKGE
PGLLISRVNAKNPFFGYAGPYKHTKDKLLCDVFKKGDVYLNTGDLIVQDQDNFLYFWDRT
GDTFRWKGENVATTEVADVIGMLDFIQEANVYGVAISGYEGRAGMASIILKPNTSLDLEK
VYEQVVTFLPAYACPRFLRIQEKMEATGTFKLLKHQLVEDGFNPLKISEPLYFMDNLKKS
YVLLTRELYDQIMLGEIKL
|
| Enzyme 41 Number of Residues |
619 |
| Enzyme 41 Molecular Weight |
70111.0 |
| Enzyme 41 Theoretical pI |
8.66 |
| Enzyme 41 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 41 General Function |
Involved in catalytic activity |
| Enzyme 41 Specific Function |
Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Thought to function as the predominant fatty acid protein transporter in heart |
| 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 |
4768275  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
Q9Y2P4  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
S27A6_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>1860 bp
ATGCTGCTGTCATGGCTAACAGTTCTAGGGGCTGGAATGGTCGTCCTGCACTTCTTGCAG
AAACTCCTGTTCCCTTACTTTTGGGATGACTTCTGGTTCGTGTTGAAGGTGGTGCTCATT
ATAATTCGGCTGAAGAAGTATGAAAAGAGAGGGGAGCTGGTGACTGTGCTGGATAAATTC
TTGAGTCATGCCAAAAGACAACCTCGGAAACCTTTCATCATCTATGAGGGAGACATCTAC
ACCTATCAGGATGTAGACAAAAGGAGCAGCAGAGTGGCCCATGTCTTCCTGAACCATTCC
TCTCTGAAAAAGGGGGACACGGTGGCTCTGCTGATGAGCAATGAGCCGGACTTCGTTCAC
GTGTGGTTCGGCCTCGCCAAGCTGGGCTGCGTGGTGGCCTTTCTCAACACCAACATTCGC
TCCAACTCCCTCCTGAATTGCATCCGCGCCTGTGGGCCCAGAGCCCTAGTGGTGGGCGCA
GATTTGCTTGGAACGGTAGAAGAAATCCTTCCAAGCCTCTCAGAAAATATCAGTGTTTGG
GGGATGAAAGATTCTGTTCCACAAGGTGTAATTTCACTCAAAGAAAAACTGAGCACCTCA
CCTGATGAGCCCGTGCCACGCAGCCACCATGTTGTCTCACTCCTCAAGTCTACTTGTCTT
TACATTTTTACCTCTGGAACAACAGGTCTACCAAAAGCAGCTGTGATTAGTCAGCTGCAG
GTTTTAAGGGGTTCTGCTGTCCTGTGGGCTTTTGGTTGTACTGCTCATGACATTGTTTAT
ATAACCCTTCCTCTGTATCATAGTTCAGCAGCTATCCTGGGAATTTCTGGATGTGTTGAG
TTGGGTGCCACTTGTGTGTTAAAGAAGAAATTTTCAGCAAGCCAGTTTTGGAGTGACTGC
AAGAAGTATGATGTGACTGTGTTTCAGTATATTGGAGAACTTTGTCGCTACCTTTGCAAA
CAATCTAAGAGAGAAGGAGAAAAGGATCATAAGGTGCGTTTGGCAATTGGAAATGGCATA
CGGAGTGATGTATGGAGAGAATTTTTAGACAGATTTGGAAATATAAAGGTGTGTGAACTT
TATGCAGCTACCGAATCAAGCATATCTTTCATGAACTACACTGGGAGAATTGGAGCAATT
GGGAGAACAAATTTGTTTTACAAACTTCTTTCCACTTTTGACTTAATAAAGTATGACTTT
CAGAAAGATGAACCCATGAGAAATGAGCAGGGTTGGTGTATTCATGTGAAAAAAGGAGAA
CCTGGACTTCTCATTTCTCGAGTGAATGCAAAAAATCCCTTCTTTGGCTATGCTGGGCCT
TATAAGCACACAAAAGACAAATTGCTTTGTGATGTTTTTAAGAAGGGAGATGTTTACCTT
AATACTGGAGACTTAATAGTCCAGGATCAGGACAATTTCCTTTATTTTTGGGACCGTACT
GGAGACACTTTCAGATGGAAAGGAGAAAATGTCGCAACCACTGAGGTTGCTGATGTTATT
GGAATGTTGGATTTCATACAGGAAGCAAACGTCTATGGTGTGGCTATATCAGGTTATGAA
GGAAGAGCAGGAATGGCTTCTATTATTTTAAAACCAAATACATCTTTAGATTTGGAAAAA
GTTTATGAACAAGTTGTAACATTTCTACCAGCTTATGCTTGTCCACGATTTTTAAGAATT
CAGGAAAAAATGGAAGCAACAGGAACATTCAAACTATTGAAGCATCAGTTGGTGGAAGAT
GGATTTAATCCACTGAAAATTTCTGAACCACTTTACTTCATGGATAACTTGAAAAAGTCT
TATGTTCTACTGACCAGGGAACTTTATGATCAAATAATGTTAGGGGAAATAAAACTTTAA
|
| Enzyme 41 GenBank Gene ID |
AF064254  |
| Enzyme 41 GeneCard ID |
SLC27A6  |
| Enzyme 41 GenAtlas ID |
SLC27A6  |
| Enzyme 41 HGNC ID |
HGNC:11000  |
| Enzyme 41 Chromosome Location |
5 |
| Enzyme 41 Locus |
5q23.3 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Gimeno RE, Ortegon AM, Patel S, Punreddy S, Ge P, Sun Y, Lodish HF, Stahl A: Characterization of a heart-specific fatty acid transport protein. J Biol Chem. 2003 May 2;278(18):16039-44. Epub 2003 Jan 28. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
8493 |
| Enzyme 42 Name |
Thioesterase domain containing 1 |
| Enzyme 42 Synonyms |
Not Available |
| Enzyme 42 Gene Name |
THEDC1 |
| Enzyme 42 Protein Sequence |
>Thioesterase domain containing 1
MERGDQPKRTRNENIFNCLYKNPEATFKLICFPWMGGGSTHFAKWGQDTHDLLEVHSLRL
PGRESRVEEPLENDISQLVDEVVCALQPVIQDKPFAFFGHSMGSYIAFRTALGLKENNQP
EPLHLFLSSATPVHSKAWHRIPKDDELSEEQISHYLMEFGGTPKHFAEAKEFVKQCSPII
RADLNIVRSCTSNVPSKAVLSCDLTCFVGSEDIAKDMEAWKDVTSGNAKIYQLPGGHFYL
LDPANEKLIKNYIIKCLEVSSISNF
|
| Enzyme 42 Number of Residues |
265 |
| Enzyme 42 Molecular Weight |
29931 |
| Enzyme 42 Theoretical pI |
6.17 |
| Enzyme 42 GO Classification |
| Function |
- CoA hydrolase activity
- acyl-CoA thioesterase II activity
- acyl-CoA thioesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- thiolester hydrolase activity
|
| Process |
- biosynthesis
- metabolism
- physiological process
|
| Component |
| — |
|
| Enzyme 42 General Function |
Secondary metabolites biosynthesis, transport and catabolism |
| Enzyme 42 Specific Function |
Not Available |
| Enzyme 42 Pathways |
Not Available |
| Enzyme 42 Reactions |
Not Available |
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
Not Available |
| Enzyme 42 Transmembrane Regions |
Not Available |
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
Not Available |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
Q5VUB6  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
Q5VUB6_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
Not Available |
| Enzyme 42 GenBank Gene ID |
AL590365  |
| Enzyme 42 GeneCard ID |
OLAH  |
| Enzyme 42 GenAtlas ID |
OLAH  |
| Enzyme 42 HGNC ID |
HGNC:25625  |
| Enzyme 42 Chromosome Location |
10 |
| Enzyme 42 Locus |
10p13 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
Not Available |
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
8676 |
| Enzyme 43 Name |
Long-chain fatty acid transport protein 3 |
| Enzyme 43 Synonyms |
- FATP-3
- Fatty acid transport protein 3
- Solute carrier family 27 member 3
- Very long-chain acyl-CoA synthetase homolog 3
- VLCS-3
|
| Enzyme 43 Gene Name |
SLC27A3 |
| Enzyme 43 Protein Sequence |
>Long-chain fatty acid transport protein 3
MGVCQRTRAPWKEKSQLERAALGFRKGGSGMFASGWNQTVPIEEAGSMAALLLLPLLLLL
PLLLLKLHLWPQLRWLPADLAFAVRALCCKRALRARALAAAAADPEGPEGGCSLAWRLAE
LAQQRAAHTFLIHGSRRFSYSEAERESNRAARAFLRALGWDWGPDGGDSGEGSAGEGERA
APGAGDAAAGSGAEFAGGDGAARGGGAAAPLSPGATVALLLPAGPEFLWLWFGLAKAGLR
TAFVPTALRRGPLLHCLRSCGARALVLAPEFLESLEPDLPALRAMGLHLWAAGPGTHPAG
ISDLLAEVSAEVDGPVPGYLSSPQSITDTCLYIFTSGTTGLPKAARISHLKILQCQGFYQ
LCGVHQEDVIYLALPLYHMSGSLLGIVGCMGIGATVVLKSKFSAGQFWEDCQQHRVTVFQ
YIGELCRYLVNQPPSKAERGHKVRLAVGSGLRPDTWERFVRRFGPLQVLETYGLTEGNVA
TINYTGQRGAVGRASWLYKHIFPFSLIRYDVTTGEPIRDPQGHCMATSPGEPGLLVAPVS
QQSPFLGYAGGPELAQGKLLKDVFRPGDVFFNTGDLLVCDDQGFLRFHDRTGDTFRWKGE
NVATTEVAEVFEALDFLQEVNVYGVTVPGHEGRAGMAALVLRPPHALDLMQLYTHVSENL
PPYARPRFLRLQESLATTETFKQQKVRMANEGFDPSTLSDPLYVLDQAVGAYLPLTTARY
SALLAGNLRI
|
| Enzyme 43 Number of Residues |
730 |
| Enzyme 43 Molecular Weight |
78643.4 |
| Enzyme 43 Theoretical pI |
7.53 |
| Enzyme 43 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 43 General Function |
Involved in catalytic activity |
| Enzyme 43 Specific Function |
Has acyl-CoA ligase activity for long-chain and very- long-chain fatty acids. Does not exhibit fatty acid transport activity |
| Enzyme 43 Pathways |
Not Available |
| Enzyme 43 Reactions |
Not Available |
| Enzyme 43 Pfam Domain Function |
|
| Enzyme 43 Signals |
|
| Enzyme 43 Transmembrane Regions |
|
| Enzyme 43 Essentiality |
Not Available |
| Enzyme 43 GenBank ID Protein |
13236579  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
Q5K4L6  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
S27A3_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>2193 bp
ATGGGCGTGTGCCAGCGCACGCGCGCTCCCTGGAAGGAGAAGTCTCAGCTAGAACGAGCG
GCCCTAGGTTTTCGGAAGGGAGGATCAGGGATGTTTGCGAGCGGCTGGAACCAGACGGTG
CCGATAGAGGAAGCGGGCTCCATGGCTGCCCTCCTGCTGCTGCCCCTGCTGCTGTTGCTA
CCGCTGCTGCTGCTGAAGCTACACCTCTGGCCGCAGTTGCGCTGGCTTCCGGCGGACTTG
GCCTTTGCGGTGCGAGCTCTGTGCTGCAAAAGGGCTCTTCGAGCTCGCGCCCTGGCCGCG
GCTGCCGCCGACCCGGAAGGTCCCGAGGGGGGCTGCAGCCTGGCCTGGCGCCTCGCGGAA
CTGGCCCAGCAGCGCGCCGCGCACACCTTTCTCATTCACGGCTCGCGGCGCTTTAGCTAC
TCAGAGGCGGAGCGCGAGAGTAACAGGGCTGCACGCGCCTTCCTACGTGCGCTAGGCTGG
GACTGGGGACCCGACGGCGGCGACAGCGGCGAGGGGAGCGCTGGAGAAGGCGAGCGGGCA
GCGCCGGGAGCCGGAGATGCAGCGGCCGGAAGCGGCGCGGAGTTTGCCGGAGGGGACGGT
GCCGCCAGAGGTGGAGGAGCCGCCGCCCCTCTGTCACCTGGAGCAACTGTGGCGCTGCTC
CTCCCCGCTGGCCCAGAGTTTCTGTGGCTCTGGTTCGGGCTGGCCAAGGCCGGCCTGCGC
ACTGCCTTTGTGCCCACCGCCCTGCGCCGGGGCCCCCTGCTGCACTGCCTCCGCAGCTGC
GGCGCGCGCGCGCTGGTGCTGGCGCCAGAGTTTCTGGAGTCCCTGGAGCCGGACCTGCCC
GCCCTGAGAGCCATGGGGCTCCACCTGTGGGCTGCAGGCCCAGGAACCCACCCTGCTGGA
ATTAGCGATTTGCTGGCTGAAGTGTCCGCTGAAGTGGATGGGCCAGTGCCAGGATACCTC
TCTTCCCCCCAGAGCATAACAGACACGTGCCTGTACATCTTCACCTCTGGCACCACGGGC
CTCCCCAAGGCTGCTCGGATCAGTCATCTGAAGATCCTGCAATGCCAGGGCTTCTATCAG
CTGTGTGGTGTCCACCAGGAAGATGTGATCTACCTCGCCCTCCCACTCTACCACATGTCC
GGTTCCCTGCTGGGCATCGTGGGCTGCATGGGCATTGGGGCCACAGTGGTGCTGAAATCC
AAGTTCTCGGCTGGTCAGTTCTGGGAAGATTGCCAGCAGCACAGGGTGACGGTGTTCCAG
TACATTGGGGAGCTGTGCCGATACCTTGTCAACCAGCCCCCGAGCAAGGCAGAACGTGGC
CATAAGGTCCGGCTGGCAGTGGGCAGCGGGCTGCGCCCAGATACCTGGGAGCGTTTTGTG
CGGCGCTTCGGGCCCCTGCAGGTGCTGGAGACATATGGACTGACAGAGGGCAACGTGGCC
ACCATCAACTACACAGGACAGCGGGGCGCTGTGGGGCGTGCTTCCTGGCTTTACAAGCAT
ATCTTCCCCTTCTCCTTGATTCGCTATGATGTCACCACAGGAGAGCCAATTCGGGACCCC
CAGGGGCACTGTATGGCCACATCTCCAGGTGAGCCAGGGCTGCTGGTGGCCCCGGTAAGC
CAGCAGTCCCCATTCCTGGGCTATGCTGGCGGGCCAGAGCTGGCCCAGGGGAAGTTGCTA
AAGGATGTCTTCCGGCCTGGGGATGTTTTCTTCAACACTGGGGACCTGCTGGTCTGCGAT
GACCAAGGTTTTCTCCGCTTCCATGATCGTACTGGAGACACCTTCAGGTGGAAGGGGGAG
AATGTGGCCACAACCGAGGTGGCAGAGGTCTTCGAGGCCCTAGATTTTCTTCAGGAGGTG
AACGTCTATGGAGTCACTGTGCCAGGGCATGAAGGCAGGGCTGGAATGGCAGCCCTAGTT
CTGCGTCCCCCCCACGCTTTGGACCTTATGCAGCTCTACACCCACGTGTCTGAGAACTTG
CCACCTTATGCCCGGCCCCGATTCCTCAGGCTCCAGGAGTCTTTGGCCACCACAGAGACC
TTCAAACAGCAGAAAGTTCGGATGGCAAATGAGGGCTTCGACCCCAGCACCCTGTCTGAC
CCACTGTACGTTCTGGACCAGGCTGTAGGTGCCTACCTGCCCCTCACAACTGCCCGGTAC
AGCGCCCTCCTGGCAGGAAACCTTCGAATCTGA
|
| Enzyme 43 GenBank Gene ID |
NM_024330.1  |
| Enzyme 43 GeneCard ID |
SLC27A3  |
| Enzyme 43 GenAtlas ID |
SLC27A3  |
| Enzyme 43 HGNC ID |
HGNC:10997  |
| Enzyme 43 Chromosome Location |
1 |
| Enzyme 43 Locus |
1q21.3 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
8715 |
| Enzyme 44 Name |
Patatin-like phospholipase domain-containing protein 4 |
| Enzyme 44 Synonyms |
- Protein GS2
|
| Enzyme 44 Gene Name |
PNPLA4 |
| Enzyme 44 Protein Sequence |
>Patatin-like phospholipase domain-containing protein 4
MKHINLSFAACGFLGIYHLGAASALCRHGKKLVKDVKAFAGASAGSLVASVLLTAPEKIE
ECNQFTYKFAEEIRRQSFGAVTPGYDFMARLRSGMESILPPSAHELAQNRLHVSITNAKT
RENHLVSTFSSREDLIKVLLASSFVPIYAGLKLVEYKGQKWVDGGLTNALPILPVGRTVT
ISPFSGRLDISPQDKGQLDLYVNIAKQDIMLSLANLVRLNQALFPPSKRKMESLYQCGFD
DTVKFLLKENWFE
|
| Enzyme 44 Number of Residues |
253 |
| Enzyme 44 Molecular Weight |
27980.2 |
| Enzyme 44 Theoretical pI |
9.54 |
| Enzyme 44 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 44 General Function |
Involved in metabolic process |
| Enzyme 44 Specific Function |
Lipid hydrolase |
| Enzyme 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
158260799  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
P41247  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
PLPL4_HUMAN  |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>762 bp
ATGAAGCACATCAACCTATCATTTGCAGCGTGTGGATTTCTGGGCATTTACCACTTGGGG
GCAGCATCTGCACTTTGCAGACATGGCAAAAAACTTGTGAAGGATGTCAAAGCCTTCGCT
GGGGCGTCTGCGGGATCGTTGGTTGCTTCTGTTCTGCTAACAGCACCAGAAAAAATAGAG
GAATGTAACCAATTTACCTACAAGTTTGCCGAAGAAATCAGAAGGCAGTCTTTCGGGGCA
GTAACGCCCGGTTATGACTTCATGGCCCGACTAAGAAGTGGGATGGAGTCGATTCTTCCT
CCCAGCGCTCACGAGCTGGCCCAGAACCGACTGCACGTATCCATCACCAACGCCAAAACC
AGAGAAAATCACTTAGTCTCCACTTTTTCCTCCAGGGAGGACCTCATTAAGGTCCTCCTA
GCCAGCAGTTTTGTGCCCATTTATGCAGGACTGAAGCTAGTGGAATACAAAGGGCAGAAG
TGGGTGGACGGAGGCCTCACCAACGCTCTTCCCATCCTGCCCGTCGGCCGGACAGTAACC
ATCTCCCCCTTCAGTGGACGACTGGACATCTCCCCGCAGGACAAAGGGCAGCTAGATCTG
TATGTTAATATCGCCAAGCAGGATATCATGTTGTCCCTGGCAAACCTGGTGAGACTCAAC
CAAGCCCTTTTTCCCCCAAGCAAGAGGAAAATGGAATCTTTGTATCAGTGTGGTTTTGAT
GACACTGTTAAGTTTTTACTTAAAGAAAATTGGTTTGAATAA
|
| Enzyme 44 GenBank Gene ID |
AK289888  |
| Enzyme 44 GeneCard ID |
PNPLA4  |
| Enzyme 44 GenAtlas ID |
PNPLA4  |
| Enzyme 44 HGNC ID |
HGNC:24887  |
| Enzyme 44 Chromosome Location |
Not Available |
| Enzyme 44 Locus |
Not Available |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 General References |
- Lee WC, Salido E, Yen PH: Isolation of a new gene GS2 (DXS1283E) from a CpG island between STS and KAL1 on Xp22.3. Genomics. 1994 Jul 15;22(2):372-6. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
|
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
8735 |
| Enzyme 45 Name |
Long-chain fatty acid transport protein 1 |
| Enzyme 45 Synonyms |
- FATP-1
- Fatty acid transport protein 1
- Solute carrier family 27 member 1
|
| Enzyme 45 Gene Name |
SLC27A1 |
| Enzyme 45 Protein Sequence |
>Long-chain fatty acid transport protein 1
MRAPGAGAASVVSLALLWLLGLPWTWSAAAALGVYVGSGGWRFLRIVCKTARRDLFGLSV
LIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLF
RQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI
FGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKGM
DDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIG
VGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRL
AVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIR
LVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSV
FSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVY
GVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQ
KTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAFAL
|
| Enzyme 45 Number of Residues |
646 |
| Enzyme 45 Molecular Weight |
71107.5 |
| Enzyme 45 Theoretical pI |
8.63 |
| Enzyme 45 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 45 General Function |
Lipid transport and metabolism |
| Enzyme 45 Specific Function |
Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. The LFCA import appears to be hormone-regulated in a tissue-specific manner. In adipocytes, but not myocytes, insulin induces a rapid translocation of FATP1 from intracellular compartments to the plasma membrane, paralleled by increased LFCA uptake. May act directly as a bona fide transporter, or alternatively, in a cytoplasmic or membrane- associated multimeric protein complex to trap and draw fatty acids towards accumulation. Plays a pivotal role in regulating available LFCA substrates from exogenous sources in tissues undergoing high levels of beta-oxidation or triglyceride synthesis. May be involved in regulation of cholesterol metabolism. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids |
| 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 |
38524616  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
Q6PCB7  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
S27A1_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>1941 bp
ATGCGGGCTCCGGGTGCGGGCGCGGCCTCGGTGGTCTCGCTGGCGCTGTTGTGGCTGCTG
GGGCTGCCGTGGACCTGGAGCGCGGCAGCGGCGCTCGGCGTGTACGTGGGCAGCGGCGGC
TGGCGCTTCCTGCGCATCGTCTGCAAGACCGCGAGGCGAGACCTCTTCGGTCTCTCTGTG
CTGATCCGCGTGCGCCTGGAGCTGCGGCGGCACCAGCGTGCCGGCCACACCATCCCGCGC
ATCTTTCAGGCGGTAGTGCAGCGACAGCCCGAGCGCCTGGCGCTGGTGGATGCCGGGACC
GGCGAGTGCTGGACCTTTGCGCAGCTGGACGCCTACTCCAATGCGGTAGCCAACCTCTTC
CGCCAGCTGGGCTTCGCGCCGGGCGACGTGGTGGCCATCTTCCTGGAGGGCCGGCCGGAG
TTCGTGGGGCTGTGGCTGGGCCTGGCCAAGGCGGGCATGGAGGCCGCGCTGCTCAACGTG
AACCTGCGGCGCGAGCCCCTGGCCTTCTGCCTGGGCACCTCGGGCGCTAAGGCCCTGATC
TTTGGAGGAGAAATGGTGGCGGCGGTGGCCGAAGTGAGCGGGCATCTGGGGAAAAGTTTG
ATCAAGTTCTGCTCTGGAGACTTGGGGCCCGAGGGCATCTTGCCGGACACCCACCTCCTG
GACCCGCTGCTGAAGGAGGCCTCTACTGCCCCCTTGGCACAGATCCCCAGCAAGGGCATG
GACGATCGTCTTTTCTACATCTACACGTCGGGGACCACCGGGCTGCCCAAGGCTGCCATT
GTCGTGCACAGCAGGTACTACCGCATGGCAGCCTTCGGCCACCACGCCTACCGCATGCAG
GCGGCTGACGTGCTCTATGACTGCCTGCCCCTGTACCACTCGGCAGGAAACATCATCGGC
GTGGGGCAGTGTCTCATCTATGGGCTGACAGTCGTCCTCCGCAAGAAATTCTCGGCCAGC
CGCTTCTGGGACGACTGCATCAAGTACAACTGCACGGTGGTTCAGTACATCGGGGAGATC
TGCCGCTACCTGCTGAAGCAGCCGGTGCGCGAGGCGGAGAGGCGACACCGCGTGCGCCTG
GCGGTGGGGAACGGGCTGCGTCCTGCCATCTGGGAGGAGTTCACGGAGCGCTTCGGCGTA
CGCCAAATCGGGGAGTTCTACGGCGCCACCGAGTGCAACTGCAGCATTGCCAACATGGAC
GGCAAGGTCGGCTCCTGTGGTTTCAACAGCCGCATCCTGCCCCACGTGTACCCCATCCGG
CTGGTGAAGGTCAATGAGGACACAATGGAGCTGCTGCGGGATGCCCAGGGCCTCTGCATC
CCCTGCCAGGCCGGGGAGCCTGGCCTCCTTGTGGGTCAGATCAACCAACAGGACCCGCTG
CGCCGCTTCGATGGCTATGTCAGCGAGAGCGCCACCAGCAAGAAGATCGCCCACAGCGTC
TTCAGCAAGGGCGACAGCGCCTACCTCTCAGGTGACGTGCTAGTGATGGATGAGCTGGGC
TACATGTACTTCCGGGACCGTAGCGGGGACACCTTCCGCTGGCGAGGGGAGAACGTCTCC
ACCACCGAGGTGGAGGGCGTGCTGAGCCGCCTGCTGGGCCAGACAGACGTGGCCGTCTAT
GGGGTGGCTGTTCCAGGAGTGGAGGGTAAGGCAGGGATGGCGGCCGTCGCAGACCCCCAC
AGCCTGCTGGACCCCAACGCGATATACCAGGAGCTGCAGAAGGTGCTGGCACCCTATGCC
CGGCCCATCTTCCTGCGCCTCCTGCCCCAGGTGGACACCACAGGCACCTTCAAGATCCAG
AAGACGAGGCTGCAGCGAGAGGGCTTTGACCCACGCCAGACCTCAGACCGGCTCTTCTTC
CTGGACCTGAAGCAGGGCCACTACCTGCCCTTAAATGAGGCAGTCTACACTCGCATCTGC
TCGGGCGCCTTCGCCCTCTGA
|
| Enzyme 45 GenBank Gene ID |
NM_198580.1  |
| Enzyme 45 GeneCard ID |
SLC27A1  |
| Enzyme 45 GenAtlas ID |
Not Available |
| Enzyme 45 HGNC ID |
Not Available |
| Enzyme 45 Chromosome Location |
1 |
| Enzyme 45 Locus |
19p13.11 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 General References |
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Martin G, Nemoto M, Gelman L, Geffroy S, Najib J, Fruchart JC, Roevens P, de Martinville B, Deeb S, Auwerx J: The human fatty acid transport protein-1 (SLC27A1; FATP-1) cDNA and gene: organization, chromosomal localization, and expression. Genomics. 2000 Jun 15;66(3):296-304. [PubMed
]
- Hatch GM, Smith AJ, Xu FY, Hall AM, Bernlohr DA: FATP1 channels exogenous FA into 1,2,3-triacyl-sn-glycerol and down-regulates sphingomyelin and cholesterol metabolism in growing 293 cells. J Lipid Res. 2002 Sep;43(9):1380-9. [PubMed
]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
12492 |
| Enzyme 46 Name |
Long-chain fatty acid transport protein 4 |
| Enzyme 46 Synonyms |
- FATP-4
- Fatty acid transport protein 4
- Solute carrier family 27 member 4
|
| Enzyme 46 Gene Name |
SLC27A4 |
| Enzyme 46 Protein Sequence |
>Long-chain fatty acid transport protein 4
MLLGASLVGVLLFSKLVLKLPWTQVGFSLLFLYLGSGGWRFIRVFIKTIRRDIFGGLVLL
KVKAKVRQCLQERRTVPILFASTVRRHPDKTALIFEGTDTHWTFRQLDEYSSSVANFLQA
RGLASGDVAAIFMENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFG
SEMASAICEVHASLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDK
LFYIYTSGTTGLPKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQ
CLLHGMTVVIRKKFSASRFWDDCIKYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALG
NGLRQSIWTNFSSRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVR
VNEDTMELIRGPDGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKK
GDQAYLTGDVLVMDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVE
VPGTEGRAGMAAVASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTE
LRKEGFDPAIVKDPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL
|
| Enzyme 46 Number of Residues |
643 |
| Enzyme 46 Molecular Weight |
72063.6 |
| Enzyme 46 Theoretical pI |
8.58 |
| Enzyme 46 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 46 General Function |
Involved in catalytic activity |
| Enzyme 46 Specific Function |
Involved in translocation of long-chain fatty acids (LFCA) across the plasma membrane. Appears to be the principal fatty acid transporter in small intestinal enterocytes. Plays a role in the formation of the epidermal barrier. Required for fat absorption in early embryogenesis. Has acyl-CoA ligase activity for long-chain and very-long-chain fatty acids |
| 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 |
40807357  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
Q6P1M0  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
S27A4_HUMAN  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>1932 bp
ATGCTGCTTGGAGCCTCTCTGGTGGGGGTGCTGCTGTTCTCCAAGCTGGTGCTGAAACTG
CCCTGGACCCAGGTGGGATTCTCCCTGTTGTTCCTCTACTTGGGATCTGGCGGCTGGCGC
TTCATCCGGGTCTTCATCAAGACCATCAGGCGCGATATCTTTGGCGGCCTGGTCCTCCTG
AAGGTGAAGGCAAAGGTGCGACAGTGCCTGCAGGAGCGGCGGACAGTGCCCATTTTGTTT
GCCTCTACCGTTCGGCGCCACCCCGACAAGACGGCCCTGATCTTCGAGGGCACAGATACC
CACTGGACCTTCCGCCAGCTGGATGAGTACTCAAGCAGTGTAGCCAACTTCCTGCAGGCC
CGGGGCCTGGCCTCGGGCGATGTGGCTGCCATCTTCATGGAGAACCGCAATGAGTTCGTG
GGCCTATGGCTGGGCATGGCCAAGCTCGGTGTGGAGGCAGCCCTCATCAACACCAACCTG
CGGCGGGATGCTCTGCTCCACTGCCTCACCACCTCGCGCGCACGGGCCCTTGTCTTTGGC
AGCGAAATGGCCTCAGCCATCTGTGAGGTCCATGCCAGCCTGGACCCCTCGCTCAGCCTC
TTCTGCTCTGGCTCCTGGGAGCCCGGTGCGGTGCCTCCAAGCACAGAACACCTGGACCCT
CTGCTGAAAGATGCTCCCAAGCACCTTCCCAGTTGCCCTGACAAGGGCTTCACAGATAAA
CTGTTCTACATCTACACATCCGGCACCACAGGGCTGCCCAAGGCCGCCATCGTGGTGCAC
AGCAGGTATTACCGCATGGCTGCCCTGGTGTACTATGGATTCCGCATGCGGCCCAACGAC
ATCGTCTATGACTGCCTCCCCCTCTACCACTCAGCAGGAAACATCGTGGGAATCGGCCAG
TGCCTGCTGCATGGCATGACGGTGGTGATTCGGAAGAAGTTCTCAGCCTCCCGGTTCTGG
GACGATTGTATCAAGTACAACTGCACGATTGTGCAGTACATTGGTGAACTGTGCCGCTAC
CTCCTGAACCAGCCACCGCGGGAGGCAGAAAACCAGCACCAGGTTCGCATGGCACTAGGC
AATGGCCTCCGGCAGTCCATCTGGACCAACTTTTCCAGCCGCTTCCACATACCCCAGGTG
GCTGAGTTCTACGGGGCCACAGAGTGCAACTGTAGCCTGGGCAACTTCGACAGCCAGGTG
GGGGCCTGTGGTTTCAATAGCCGCATCCTGTCCTTCGTGTACCCCATCCGGTTGGTACGT
GTCAACGAGGACACCATGGAGCTGATCCGGGGGCCCGACGGCGTCTGCATTCCCTGCCAG
CCAGGTGAGCCGGGCCAGCTGGTGGGCCGCATCATCCAGAAAGACCCCCTGCGCCGCTTC
GATGGCTACCTCAACCAGGGCGCCAACAACAAGAAGATTGCCAAGGATGTCTTCAAGAAG
GGGGACCAGGCCTACCTTACTGGTGATGTGCTGGTGATGGACGAGCTGGGCTACCTGTAC
TTCCGAGACCGCACTGGGGACACGTTCCGCTGGAAAGGTGAGAACGTGTCCACCACCGAG
GTGGAAGGCACACTCAGCCGCCTGCTGGACATGGCTGACGTGGCCGTGTATGGTGTCGAG
GTGCCAGGAACCGAGGGCCGGGCCGGAATGGCTGCTGTGGCCAGCCCCACTGGCAACTGT
GACCTGGAGCGCTTTGCTCAGGTCTTGGAGAAGGAACTGCCCCTGTATGCGCGCCCCATC
TTCCTGCGCCTCCTGCCTGAGCTGCACAAAACAGGAACCTACAAGTTCCAGAAGACAGAG
CTACGGAAGGAGGGCTTTGACCCGGCTATTGTGAAAGACCCGCTGTTCTATCTAGATGCC
CAGAAGGGCCGCTACGTCCCGCTGGACCAAGAGGCCTACAGCCGCATCCAGGCAGGCGAG
GAGAAGCTGTGA
|
| Enzyme 46 GenBank Gene ID |
NM_005094.3  |
| Enzyme 46 GeneCard ID |
SLC27A4  |
| Enzyme 46 GenAtlas ID |
SLC27A4  |
| Enzyme 46 HGNC ID |
HGNC:10998  |
| Enzyme 46 Chromosome Location |
9 |
| Enzyme 46 Locus |
9q34.11 |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- Fitscher BA, Riedel HD, Young KC, Stremmel W: Tissue distribution and cDNA cloning of a human fatty acid transport protein (hsFATP4). Biochim Biophys Acta. 1998 Dec 22;1443(3):381-5. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Gertow K, Bellanda M, Eriksson P, Boquist S, Hamsten A, Sunnerhagen M, Fisher RM: Genetic and structural evaluation of fatty acid transport protein-4 in relation to markers of the insulin resistance syndrome. J Clin Endocrinol Metab. 2004 Jan;89(1):392-9. [PubMed
]
- Klar J, Schweiger M, Zimmerman R, Zechner R, Li H, Torma H, Vahlquist A, Bouadjar B, Dahl N, Fischer J: Mutations in the fatty acid transport protein 4 gene cause the ichthyosis prematurity syndrome. Am J Hum Genet. 2009 Aug;85(2):248-53. Epub 2009 Jul 23. [PubMed
]
|
| Enzyme 46 Metabolite References |
Not Available |
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
12921 |
| Enzyme 47 Name |
60 kDa lysophospholipase |
| Enzyme 47 Synonyms |
- L-asparaginase
- L-asparagine amidohydrolase
- Platelet-activating factor acetylhydrolase
- PAF acetylhydrolase
|
| Enzyme 47 Gene Name |
ASPG |
| Enzyme 47 Protein Sequence |
>60 kDa lysophospholipase
MARAVGPERRLLAVYTGGTIGMRSELGVLVPGTGLAAILRTLPMFHDEEHARARGLSEDT
LVLPPASRNQRILYTVLECQPLFDSSDMTIAEWVCLAQTIKRHYEQYHGFVVIHGTDTMA
FAASMLSFMLENLQKTVILTGAQVPIHALWSDGRENLLGALLMAGQYVIPEVCLFFQNQL
FRGNRATKVDARRFAAFCSPNLLPLATVGADITINRELVRKVDGKAGLVVHSSMEQDVGL
LRLYPGIPAALVRAFLQPPLKGVVMETFGSGNGPTKPDLLQELRVATERGLVIVNCTHCL
QGAVTTDYAAGMAMAGAGVISGFDMTSEAALAKLSYVLGQPGLSLDVRKELLTKDLRGEM
TPPSVEERRPSLQGNTLGGGVSWLLSLSGSQEADALRNALVPSLACAAAHAGDVEALQAL
VELGSDLGLVDFNGQTPLHAAARGGHTEAVTMLLQRGVDVNTRDTDGFSPLLLAVRGRHP
GVIGLLREAGASLSTQELEEAGTELCRLAYRADLEGLQVWWQAGADLGQPGYDGHSALHV
AEAAGNLAVVAFLQSLEGAVGAQAPCP
|
| Enzyme 47 Number of Residues |
567 |
| Enzyme 47 Molecular Weight |
60287.7 |
| Enzyme 47 Theoretical pI |
5.59 |
| Enzyme 47 GO Classification |
| Function |
- asparaginase activity
- 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 amino acid and derivative metabolic process
- cellular amino acid metabolic process
- cellular metabolic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 47 General Function |
Involved in asparaginase activity |
| Enzyme 47 Specific Function |
Exhibits lysophospholipase, transacylase, PAF acetylhydrolase and asparaginase activities |
| Enzyme 47 Pathways |
Not Available |
| Enzyme 47 Reactions |
- L-asparagine + H2O = L-aspartate + NH3 [RN:R00485]
|
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
122937331  |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
Q86U10  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
LPP60_HUMAN  |
| Enzyme 47 PDB ID |
Not Available |
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
>1740 bp
ATGGCGCGCGCGGTGGGGCCCGAGCGGAGGCTGCTGGCCGTCTACACCGGCGGCACCATT
GGCATGCGGAGTGAGCTCGGCGTGCTTGTGCCCGGGACGGGCCTGGCTGCCATCCTGAGG
ACACTGCCCATGTTCCATGACGAGGAGCACGCCCGAGCCCGCGGCCTCTCTGAGGACACC
CTGGTGCTACCCCCGGCCAGCCGCAACCAGAGGATTCTCTACACCGTGCTGGAGTGCCAG
CCCCTCTTCGACTCCAGTGACATGACCATCGCTGAGTGGGTTTGCCTTGCCCAGACCATC
AAGAGGCACTACGAGCAGTACCACGGCTTTGTGGTCATCCACGGCACCGACACCATGGCC
TTTGCTGCCTCGATGCTGTCCTTCATGCTGGAGAACCTGCAGAAGACTGTCATCCTCACT
GGGGCCCAGGTGCCCATCCATGCCCTGTGGAGCGACGGCCGTGAGAACCTGCTGGGGGCA
CTGCTCATGGCTGGCCAGTATGTGATCCCAGAGGTCTGCCTTTTCTTCCAGAATCAGCTG
TTTCGGGGCAACCGGGCAACCAAGGTAGACGCTCGGAGGTTCGCAGCTTTCTGCTCCCCG
AACCTGCTGCCTCTGGCCACAGTGGGTGCTGACATCACAATCAACAGGGAGCTGGTGCGG
AAGGTGGACGGGAAGGCTGGGCTGGTGGTGCACAGCAGCATGGAGCAGGACGTGGGCCTG
CTGCGCCTCTACCCTGGGATCCCTGCCGCCCTGGTTCGGGCCTTCTTGCAGCCTCCCCTG
AAGGGCGTGGTCATGGAGACCTTCGGTTCAGGGAACGGACCCACCAAGCCCGACCTGCTG
CAGGAGCTGCGGGTGGCCACCGAGCGCGGCCTGGTCATCGTCAACTGTACCCACTGCCTC
CAGGGGGCTGTGACCACAGACTATGCAGCTGGCATGGCCATGGCGGGAGCCGGCGTCATC
TCAGGCTTCGACATGACATCGGAGGCCGCCCTGGCCAAGCTATCGTATGTGCTGGGCCAG
CCAGGGCTGAGCCTGGATGTCAGGAAGGAGCTGCTGACCAAGGACCTTCGGGGGGAGATG
ACGCCACCCTCGGTGGAAGAGCGCCGGCCCTCACTGCAGGGCAACACGCTGGGCGGTGGG
GTCTCCTGGCTCCTCAGTCTGAGCGGCAGCCAGGAGGCAGATGCCCTGCGGAATGCCCTG
GTGCCCAGCCTGGCCTGTGCTGCTGCCCACGCCGGTGACGTGGAGGCGCTGCAGGCGCTT
GTGGAGCTGGGCAGTGACCTGGGCCTGGTGGACTTTAACGGCCAAACCCCACTGCACGCG
GCCGCCCGGGGAGGCCACACAGAGGCAGTCACCATGCTGCTGCAGAGAGGTGTGGACGTG
AACACCCGGGACACGGATGGCTTCAGCCCGCTGCTGCTGGCCGTGCGGGGCAGGCATCCG
GGTGTCATTGGGTTGCTGCGGGAAGCCGGGGCCTCCCTGTCCACCCAGGAGCTGGAGGAA
GCAGGGACGGAGCTGTGCAGGCTGGCATACAGGGCCGACCTCGAAGGCCTGCAGGTGTGG
TGGCAGGCAGGGGCTGACCTGGGGCAGCCGGGCTATGACGGGCACAGCGCCCTGCACGTC
GCAGAGGCAGCCGGGAACCTGGCAGTGGTGGCCTTTCTACAGAGCCTGGAGGGTGCGGTT
GGTGCCCAGGCCCCATGCCCAGAGCCCTCATGTTTTCAGGAAGTGCTGCCTGGTGTCTAA
|
| Enzyme 47 GenBank Gene ID |
NM_001080464  |
| Enzyme 47 GeneCard ID |
ASPG  |
| Enzyme 47 GenAtlas ID |
ASPG  |
| Enzyme 47 HGNC ID |
HGNC:20123  |
| Enzyme 47 Chromosome Location |
1 |
| Enzyme 47 Locus |
14q32.33 |
| Enzyme 47 SNPs |
SNPJam Report  |
| Enzyme 47 General References |
- Heilig R, Eckenberg R, Petit JL, Fonknechten N, Da Silva C, Cattolico L, Levy M, Barbe V, de Berardinis V, Ureta-Vidal A, Pelletier E, Vico V, Anthouard V, Rowen L, Madan A, Qin S, Sun H, Du H, Pepin K, Artiguenave F, Robert C, Cruaud C, Bruls T, Jaillon O, Friedlander L, Samson G, Brottier P, Cure S, Segurens B, Aniere F, Samain S, Crespeau H, Abbasi N, Aiach N, Boscus D, Dickhoff R, Dors M, Dubois I, Friedman C, Gouyvenoux M, James R, Madan A, Mairey-Estrada B, Mangenot S, Martins N, Menard M, Oztas S, Ratcliffe A, Shaffer T, Trask B, Vacherie B, Bellemere C, Belser C, Besnard-Gonnet M, Bartol-Mavel D, Boutard M, Briez-Silla S, Combette S, Dufosse-Laurent V, Ferron C, Lechaplais C, Louesse C, Muselet D, Magdelenat G, Pateau E, Petit E, Sirvain-Trukniewicz P, Trybou A, Vega-Czarny N, Bataille E, Bluet E, Bordelais I, Dubois M, Dumont C, Guerin T, Haffray S, Hammadi R, Muanga J, Pellouin V, Robert D, Wunderle E, Gauguet G, Roy A, Sainte-Marthe L, Verdier J, Verdier-Discala C, Hillier L, Fulton L, McPherson J, Matsuda F, Wilson R, Scarpelli C, Gyapay G, Wincker P, Saurin W, Quetier F, Waterston R, Hood L, Weissenbach J: The DNA sequence and analysis of human chromosome 14. Nature. 2003 Feb 6;421(6923):601-7. Epub 2003 Jan 1. [PubMed
]
- 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 47 Metabolite References |
Not Available |
|
Enzyme 48
[top]
|
| Enzyme 48 ID |
12922 |
| Enzyme 48 Name |
Phospholipase B1, membrane-associated |
| Enzyme 48 Synonyms |
- Phospholipase B
- hPLB
- Phospholipase B/lipase
- PLB/LIP
- Phospholipase A2
- Lysophospholipase
|
| Enzyme 48 Gene Name |
PLB1 |
| Enzyme 48 Protein Sequence |
>Phospholipase B1, membrane-associated
MGLRPGIFLLELLLLLGQGTPQIHTSPRKSTLEGQLWPETLKNSPFPCNPNKLGVNMPSK
SVHSLKPSDIKFVAAIGNLEIPPDPGTGDLEKQDWTERPQQVCMGVMTVLSDIIRYFSPS
VPMPVCHTGKRVIPHDGAEDLWIQAQELVRNMKENLQLDFQFDWKLINVFFSNASQCYLC
PSAQQNGLAAGGVDELMGVLDYLQQEVPRAFVNLVDLSEVAEVSRQYHGTWLSPAPEPCN
CSEETTRLAKVVMQWSYQEAWNSLLASSRYSEQESFTVVFQPFFYETTPSLHSEDPRLQD
STTLAWHLWNRMMEPAGEKDEPLSVKHGRPMKCPSQESPYLFSYRNSNYLTRLQKPQDKL
EVREGAEIRCPDKDPSDTVPTSVHRLKPADINVIGALGDSLTAGNGAGSTPGNVLDVLTQ
YRGLSWSVGGDENIGTVTTLANILREFNPSLKGFSVGTGKETSPNAFLNQAVAGGRAEDL
PVQARRLVDLMKNDTRIHFQEDWKIITLFIGGNDLCDFCNDLVHYSPQNFTDNIGKALDI
LHAEVPRAFVNLVTVLEIVNLRELYQEKKVYCPRMILRSLCPCVLKFDDNSTELATLIEF
NKKFQEKTHQLIESGRYDTREDFTVVVQPFFENVDMPKTSEGLPDNSFFAPDCFHFSSKS
HSRAASALWNNMLEPVGQKTTRHKFENKINITCPNQVQPFLRTYKNSMQGHGTWLPCRDR
APSALHPTSVHALRPADIQVVAALGDSLTAGNGIGSKPDDLPDVTTQYRGLSYSAGGDGS
LENVTTLPNILREFNRNLTGYAVGTGDANDTNAFLNQAVPGAKAEDLMSQVQTLMQKMKD
DHRVNFHEDWKVITVLIGGSDLCDYCTDSNLYSAANFVHHLRNALDVLHREVPRVLVNLV
DFLNPTIMRQVFLGNPDKCPVQQASVLCNCVLTLRENSQELARLEAFSRAYRSSMRELVG
SGRYDTQEDFSVVLQPFFQNIQLPVLADGLPDTSFFAPDCIHPNQKFHSQLARALWTNML
EPLGSKTETLDLRAEMPITCPTQNEPFLRTPRNSNYTYPIKPAIENWGSDFLCTEWKASN
SVPTSVHQLRPADIKVVAALGDSLTTAVGARPNNSSDLPTSWRGLSWSIGGDGNLETHTT
LPNILKKFNPYLLGFSTSTWEGTAGLNVAAEGARARDMPAQAWDLVERMKNSPDINLEKD
WKLVTLFIGVNDLCHYCENPEAHLATEYVQHIQQALDILSEELPRAFVNVVEVMELASLY
QGQGGKCAMLAAQNNCTCLRHSQSSLEKQELKKVNWNLQHGISSFSYWHQYTQREDFAVV
VQPFFQNTLTPLNERGDTDLTFFSEDCFHFSDRGHAEMAIALWNNMLEPVGRKTTSNNFT
HSRAKLKCPSPESPYLYTLRNSRLLPDQAEEAPEVLYWAVPVAAGVGLVVGIIGTVVWRC
RRGGRREDPPMSLRTVAL
|
| Enzyme 48 Number of Residues |
1458 |
| Enzyme 48 Molecular Weight |
163079.3 |
| Enzyme 48 Theoretical pI |
5.72 |
| Enzyme 48 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 48 General Function |
Involved in hydrolase activity |
| Enzyme 48 Specific Function |
Membrane-associated phospholipase. Exhibits a calcium- independent broad substrate specificity including phospholipase A2/lysophospholipase activity. Preferential hydrolysis at the sn-2 position of diacylphospholipids and diacyglycerol, whereas it shows no positional specificity toward triacylglycerol. Exhibits also esterase activity toward p-nitrophenyl. May act on the brush border membrane to facilitate the absorption of digested lipids |
| Enzyme 48 Pathways |
Not Available |
| Enzyme 48 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 48 Pfam Domain Function |
|
| Enzyme 48 Signals |
|
| Enzyme 48 Transmembrane Regions |
|
| Enzyme 48 Essentiality |
Not Available |
| Enzyme 48 GenBank ID Protein |
283436112  |
| Enzyme 48 UniProtKB/Swiss-Prot ID |
Q6P1J6  |
| Enzyme 48 UniProtKB/Swiss-Prot Entry Name |
PLB1_HUMAN  |
| Enzyme 48 PDB ID |
Not Available |
| Enzyme 48 Cellular Location |
Not Available |
| Enzyme 48 Gene Sequence |
>4377 bp
ATGGGGCTGCGGCCAGGCATTTTCCTCCTGGAGCTGCTGCTGCTTCTGGGGCAAGGGACC
CCTCAGATCCATACCTCTCCTAGAAAGAGTACATTGGAAGGGCAGCTATGGCCAGAGACC
CTGAAGAATTCTCCATTCCCATGCAACCCAAATAAATTAGGAGTGAATATGCCTTCTAAA
TCAGTTCACTCTCTGAAGCCTTCTGATATTAAATTTGTGGCAGCCATTGGCAATCTGGAA
ATTCCTCCAGACCCAGGGACGGGCGATCTGGAGAAGCAAGACTGGACTGAAAGGCCACAG
CAGGTGTGCATGGGAGTGATGACAGTCCTTTCAGACATCATCAGATATTTCAGTCCTTCT
GTTCCAATGCCTGTGTGCCACACTGGAAAGAGAGTCATACCCCACGATGGTGCTGAAGAC
TTGTGGATTCAGGCTCAAGAACTGGTGAGAAACATGAAAGAGAACCTGCAACTTGACTTT
CAATTTGACTGGAAGCTCATCAATGTGTTCTTCAGTAATGCAAGCCAGTGTTACCTGTGC
CCCTCTGCTCAACAGAATGGGCTTGCGGCGGGCGGCGTGGATGAGCTGATGGGGGTGCTG
GACTACCTGCAGCAGGAGGTCCCCAGAGCATTTGTAAACCTGGTGGACCTCTCTGAGGTT
GCAGAGGTCTCTCGTCAGTATCACGGCACTTGGCTCAGCCCTGCACCAGAGCCCTGTAAT
TGCTCAGAGGAGACCACCCGGCTGGCCAAGGTGGTGATGCAGTGGTCTTATCAGGAAGCC
TGGAACAGCCTCCTGGCCTCCAGCAGGTACAGTGAGCAGGAGTCCTTCACCGTGGTTTTC
CAGCCTTTCTTCTATGAGACCACCCCATCTCTACACTCGGAGGACCCCCGACTCCAGGAT
TCTACCACGCTGGCCTGGCATCTCTGGAATAGGATGATGGAGCCAGCAGGAGAGAAAGAT
GAGCCATTGAGTGTAAAACACGGGAGGCCAATGAAGTGTCCCTCTCAGGAGAGCCCCTAT
CTGTTCAGCTACAGAAACAGCAACTACCTGACCAGACTGCAGAAACCCCAAGACAAGCTT
GAGGTAAGAGAAGGAGCGGAAATCAGATGTCCTGACAAAGACCCCTCCGATACGGTTCCC
ACCTCAGTTCATAGGCTGAAGCCGGCTGACATCAACGTAATTGGAGCCCTGGGTGACTCT
CTCACGGCAGGCAATGGGGCCGGGTCCACACCTGGGAACGTCTTGGACGTCTTGACTCAG
TACCGAGGCCTGTCCTGGAGCGTCGGCGGAGATGAGAACATCGGCACCGTTACCACCCTG
GCGAACATCCTCCGGGAATTCAACCCTTCCCTGAAGGGCTTCTCTGTTGGCACTGGGAAA
GAAACCAGTCCTAATGCCTTCTTAAACCAGGCTGTGGCAGGAGGCCGAGCTGAGGATCTA
CCTGTCCAGGCCAGGAGGCTGGTGGACCTGATGAAGAATGACACGAGGATACACTTTCAG
GAAGACTGGAAGATAATAACCCTGTTTATAGGCGGCAATGACCTCTGTGATTTCTGCAAT
GATCTGGTCCACTATTCTCCCCAGAACTTCACAGACAACATTGGAAAGGCCCTGGACATC
CTCCATGCTGAGGTTCCTCGGGCATTTGTGAACCTGGTGACGGTGCTTGAGATCGTCAAC
CTGAGGGAGCTGTACCAGGAGAAAAAAGTCTACTGCCCAAGGATGATCCTCAGGTCTCTG
TGTCCCTGTGTCCTGAAGTTTGATGATAACTCAACAGAACTTGCTACCCTCATCGAATTC
AACAAGAAGTTTCAGGAGAAGACCCACCAACTGATTGAGAGTGGGCGATATGACACAAGG
GAAGATTTTACTGTGGTTGTGCAGCCGTTCTTTGAAAACGTGGACATGCCAAAGACCTCG
GAAGGATTGCCTGACAACTCTTTCTTCGCTCCTGACTGTTTCCACTTCAGCAGCAAGTCT
CACTCCCGAGCAGCCAGTGCTCTCTGGAACAATATGCTGGAGCCTGTTGGCCAGAAGACG
ACTCGTCATAAGTTTGAAAACAAGATCAATATCACATGTCCGAACCAGGTCCAGCCGTTT
CTGAGGACCTACAAGAACAGCATGCAGGGTCATGGGACCTGGCTGCCATGCAGGGACAGA
GCCCCTTCTGCCTTGCACCCTACCTCAGTGCATGCCCTGAGACCTGCAGACATCCAAGTT
GTGGCTGCTCTGGGGGATTCTCTGACCGCTGGCAATGGAATTGGCTCCAAACCAGACGAC
CTCCCCGATGTCACCACACAGTATCGGGGACTGTCATACAGTGCAGGAGGGGACGGCTCC
CTGGAGAATGTGACCACCTTACCTAATATCCTTCGGGAGTTTAACAGAAACCTCACAGGC
TACGCCGTGGGCACGGGTGATGCCAATGACACGAATGCATTCCTCAATCAAGCTGTTCCC
GGAGCAAAGGCTGAGGATCTTATGAGCCAAGTCCAAACTCTGATGCAGAAGATGAAAGAT
GATCATAGAGTAAATTTCCATGAAGACTGGAAGGTCATCACAGTGCTGATCGGAGGCAGC
GATTTATGTGACTACTGCACAGATTCGAATCTGTATTCTGCAGCCAACTTTGTTCACCAT
CTCCGCAATGCCTTGGACGTCCTGCATAGAGAGGTGCCCAGAGTCCTGGTCAACCTCGTG
GACTTCCTGAACCCCACTATCATGCGGCAGGTGTTCCTGGGAAACCCAGACAAGTGCCCA
GTGCAGCAGGCCAGCGTTTTGTGTAACTGCGTTCTGACCCTGCGGGAGAACTCCCAAGAG
CTAGCCAGGCTGGAGGCCTTCAGCCGAGCCTACCGGAGCAGCATGCGCGAGCTGGTGGGG
TCAGGCCGCTATGACACGCAGGAGGACTTCTCTGTGGTGCTGCAGCCCTTCTTCCAGAAC
ATCCAGCTCCCTGTCCTGGCGGATGGGCTCCCAGATACGTCCTTCTTTGCCCCAGACTGC
ATCCACCCAAATCAGAAATTCCACTCCCAGCTGGCCAGAGCCCTTTGGACCAATATGCTT
GAACCACTTGGAAGCAAAACAGAGACCCTGGACCTGAGAGCAGAGATGCCCATCACCTGT
CCCACTCAGAATGAGCCCTTCCTGAGAACCCCTCGGAATAGTAACTACACGTACCCCATC
AAGCCAGCCATTGAGAACTGGGGCAGTGACTTCCTGTGTACAGAGTGGAAGGCTTCCAAT
AGTGTTCCAACCTCTGTCCACCAGCTCCGACCAGCAGACATCAAAGTGGTGGCCGCCCTG
GGTGACTCTCTGACTACAGCAGTGGGAGCTCGACCAAACAACTCCAGTGACCTACCCACA
TCTTGGAGGGGACTCTCTTGGAGCATTGGAGGGGATGGGAACTTGGAGACTCACACCACA
CTGCCCAACATTCTGAAGAAGTTCAACCCTTACCTCCTTGGCTTCTCTACCAGCACCTGG
GAGGGGACAGCAGGACTAAATGTGGCAGCGGAAGGGGCCAGAGCTAGGGACATGCCAGCC
CAGGCCTGGGACCTGGTAGAGCGAATGAAAAACAGCCCCGACATCAACCTGGAGAAAGAC
TGGAAGCTGGTCACACTCTTCATTGGGGTCAACGACTTGTGTCATTACTGTGAGAATCCG
GAGGCCCACTTGGCCACGGAATATGTTCAGCACATCCAACAGGCCCTGGACATCCTCTCT
GAGGAGCTCCCAAGGGCTTTCGTCAACGTGGTGGAGGTCATGGAGCTGGCTAGCCTGTAC
CAGGGCCAAGGCGGGAAATGTGCCATGCTGGCAGCTCAGAACAACTGCACTTGCCTCAGA
CACTCGCAAAGCTCCCTGGAGAAGCAAGAACTGAAGAAAGTGAACTGGAACCTCCAGCAT
GGCATCTCCAGTTTCTCCTACTGGCACCAATACACACAGCGTGAGGACTTTGCGGTTGTG
GTGCAGCCTTTCTTCCAAAACACACTCACCCCACTGAACGAGAGAGGGGACACTGACCTC
ACCTTCTTCTCCGAGGACTGTTTTCACTTCTCAGACCGCGGGCATGCCGAGATGGCCATC
GCACTCTGGAACAACATGCTGGAACCAGTGGGCCGCAAGACTACCTCCAACAACTTCACC
CACAGCCGAGCCAAACTCAAGTGCCCCTCTCCTGAGAGCCCTTACCTCTACACCCTGCGG
AACAGCCGATTGCTCCCAGACCAGGCTGAAGAAGCCCCCGAGGTGCTCTACTGGGCTGTC
CCAGTGGCAGCGGGAGTCGGCCTTGTGGTGGGCATCATCGGGACAGTGGTCTGGAGGTGC
AGGAGAGGTGGCCGGAGGGAAGATCCTCCAATGAGCCTGCGCACTGTGGCCCTCTAG
|
| Enzyme 48 GenBank Gene ID |
NM_153021.4  |
| Enzyme 48 GeneCard ID |
PLB1  |
| Enzyme 48 GenAtlas ID |
PLB1  |
| Enzyme 48 HGNC ID |
HGNC:30041  |
| Enzyme 48 Chromosome Location |
2 |
| Enzyme 48 Locus |
2p23.2 |
| Enzyme 48 SNPs |
SNPJam Report  |
| Enzyme 48 General References |
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Maury E, Prevost MC, Nauze M, Redoules D, Tarroux R, Charveron M, Salles JP, Perret B, Chap H, Gassama-Diagne A: Human epidermis is a novel site of phospholipase B expression. Biochem Biophys Res Commun. 2002 Jul 12;295(2):362-9. [PubMed
]
|
| Enzyme 48 Metabolite References |
Not Available |
|
Enzyme 49
[top]
|
| Enzyme 49 ID |
12969 |
| Enzyme 49 Name |
Patatin-like phospholipase domain-containing protein 2 |
| Enzyme 49 Synonyms |
- Adipose triglyceride lipase
- Calcium-independent phospholipase A2
- Desnutrin
- IPLA2-zeta
- Pigment epithelium-derived factor
- TTS2.2
- Transport-secretion protein 2
- TTS2
|
| Enzyme 49 Gene Name |
PNPLA2 |
| Enzyme 49 Protein Sequence |
>Patatin-like phospholipase domain-containing protein 2
MFPREKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGV
CLGEAGAKFIEVSKEARKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTR
VSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGGISDNLPLYELKN
TITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPLVLREMCKQ
GYRDGLRFLQRNGLLNRPNPLLALPPARPHGPEDKDQAVESAQAEDYSQLPGEDHILEHL
PARLNEALLEACVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTIRLLEWLPDVP
EDIRWMKEQTGSICQYLVMRAKRKLGRHLPSRLPEQVELRRVQSLPSVPLSCAAYREALP
GWMRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPEALRMRAPADPAPAPADPASPQHQ
LAGPAPLLSTPAPEARPVIGALGL
|
| Enzyme 49 Number of Residues |
504 |
| Enzyme 49 Molecular Weight |
55315.2 |
| Enzyme 49 Theoretical pI |
7.09 |
| Enzyme 49 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 49 General Function |
Involved in metabolic process |
| Enzyme 49 Specific Function |
Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Also has acylglycerol transacylase activity. May act coordinately with LIPE/HLS within the lipolytic cascade. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion |
| Enzyme 49 Pathways |
|
| Enzyme 49 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 49 Pfam Domain Function |
|
| Enzyme 49 Signals |
|
| Enzyme 49 Transmembrane Regions |
|
| Enzyme 49 Essentiality |
Not Available |
| Enzyme 49 GenBank ID Protein |
32698724  |
| Enzyme 49 UniProtKB/Swiss-Prot ID |
Q96AD5  |
| Enzyme 49 UniProtKB/Swiss-Prot Entry Name |
PLPL2_HUMAN  |
| Enzyme 49 PDB ID |
Not Available |
| Enzyme 49 Cellular Location |
Not Available |
| Enzyme 49 Gene Sequence |
>1515 bp
ATGTTTCCCCGCGAGAAGACGTGGAACATCTCGTTCGCGGGCTGCGGCTTCCTCGGCGTC
TACTACGTCGGCGTGGCCTCCTGCCTCCGCGAGCACGCGCCCTTCCTGGTGGCCAACGCC
ACGCACATCTACGGCGCCTCGGCCGGGGCGCTCACGGCCACGGCGCTGGTCACCGGGGTC
TGCCTGGGTGAGGCTGGTGCCAAGTTCATTGAGGTATCTAAAGAGGCCCGGAAGCGGTTC
CTGGGCCCCCTGCACCCCTCCTTCAACCTGGTAAAGATCATCCGCAGTTTCCTGCTGAAG
GTCCTGCCTGCTGATAGCCATGAGCATGCCAGTGGGCGCCTGGGCATCTCCCTGACCCGC
GTGTCAGACGGCGAGAATGTCATTATATCCCACTTCAACTCCAAGGACGAGCTCATCCAG
GCCAATGTCTGCAGCGGTTTCATCCCCGTGTACTGTGGGCTCATCCCTCCCTCCCTCCAG
GGGGTGCGCTACGTGGATGGTGGCATTTCAGACAACCTGCCACTCTATGAGCTTAAGAAC
ACCATCACAGTGTCCCCCTTCTCGGGCGAGAGTGACATCTGTCCGCAGGACAGCTCCACC
AACATCCACGAGCTGCGGGTCACCAACACCAGCATCCAGTTCAACCTGCGCAACCTCTAC
CGCCTCTCCAAGGCCCTCTTCCCGCCGGAGCCCCTGGTGCTGCGAGAGATGTGCAAGCAG
GGATACCGGGATGGCCTGCGCTTTCTGCAGCGGAACGGCCTCCTGAACCGGCCCAACCCC
TTGCTGGCGTTGCCCCCCGCCCGCCCCCACGGCCCAGAGGACAAGGACCAGGCAGTGGAG
AGCGCCCAAGCGGAGGATTACTCGCAGCTGCCCGGAGAAGATCACATCCTGGAGCACCTG
CCCGCCCGGCTCAATGAGGCCCTGCTGGAGGCCTGCGTGGAGCCCACGGACCTGCTGACC
ACCCTCTCCAACATGCTGCCTGTGCGTCTGGCCACGGCCATGATGGTGCCCTACACGCTG
CCGCTGGAGAGCGCTCTGTCCTTCACCATCCGCTTGCTGGAGTGGCTGCCCGACGTTCCC
GAGGACATCCGGTGGATGAAGGAGCAGACGGGCAGCATCTGCCAGTACCTGGTGATGCGC
GCCAAGAGGAAGCTGGGCAGGCACCTGCCCTCCAGGCTGCCGGAGCAGGTGGAGCTGCGC
CGCGTCCAGTCGCTGCCGTCCGTGCCGCTGTCCTGCGCCGCCTACAGAGAGGCACTGCCC
GGCTGGATGCGCAACAACCTCTCGCTGGGGGACGCGCTGGCCAAGTGGGAGGAGTGCCAG
CGCCAGCTGCTGCTCGGCCTCTTCTGCACCAACGTGGCCTTCCCGCCCGAAGCTCTGCGC
ATGCGCGCACCCGCCGACCCGGCTCCCGCCCCCGCGGACCCAGCATCCCCGCAGCACCAG
CTGGCCGGGCCTGCCCCCTTGCTGAGCACCCCTGCTCCCGAGGCCCGGCCCGTGATCGGG
GCCCTGGGGCTGTGA
|
| Enzyme 49 GenBank Gene ID |
NM_020376.3  |
| Enzyme 49 GeneCard ID |
PNPLA2  |
| Enzyme 49 GenAtlas ID |
PNPLA2  |
| Enzyme 49 HGNC ID |
HGNC:30802  |
| Enzyme 49 Chromosome Location |
1 |
| Enzyme 49 Locus |
11p15.5 |
| Enzyme 49 SNPs |
SNPJam Report  |
| Enzyme 49 General References |
- Zimmermann R, Strauss JG, Haemmerle G, Schoiswohl G, Birner-Gruenberger R, Riederer M, Lass A, Neuberger G, Eisenhaber F, Hermetter A, Zechner R: Fat mobilization in adipose tissue is promoted by adipose triglyceride lipase. Science. 2004 Nov 19;306(5700):1383-6. [PubMed
]
- Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J: Large-scale cDNA transfection screening for genes related to cancer development and progression. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15724-9. Epub 2004 Oct 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Jenkins CM, Mancuso DJ, Yan W, Sims HF, Gibson B, Gross RW: Identification, cloning, expression, and purification of three novel human calcium-independent phospholipase A2 family members possessing triacylglycerol lipase and acylglycerol transacylase activities. J Biol Chem. 2004 Nov 19;279(47):48968-75. Epub 2004 Sep 10. [PubMed
]
- Langin D, Dicker A, Tavernier G, Hoffstedt J, Mairal A, Ryden M, Arner E, Sicard A, Jenkins CM, Viguerie N, van Harmelen V, Gross RW, Holm C, Arner P: Adipocyte lipases and defect of lipolysis in human obesity. Diabetes. 2005 Nov;54(11):3190-7. [PubMed
]
- Lake AC, Sun Y, Li JL, Kim JE, Johnson JW, Li D, Revett T, Shih HH, Liu W, Paulsen JE, Gimeno RE: Expression, regulation, and triglyceride hydrolase activity of Adiponutrin family members. J Lipid Res. 2005 Nov;46(11):2477-87. Epub 2005 Sep 8. [PubMed
]
- Kim JY, Tillison K, Lee JH, Rearick DA, Smas CM: The adipose tissue triglyceride lipase ATGL/PNPLA2 is downregulated by insulin and TNF-alpha in 3T3-L1 adipocytes and is a target for transactivation by PPARgamma. Am J Physiol Endocrinol Metab. 2006 Jul;291(1):E115-27. Epub 2006 May 16. [PubMed
]
- Smirnova E, Goldberg EB, Makarova KS, Lin L, Brown WJ, Jackson CL: ATGL has a key role in lipid droplet/adiposome degradation in mammalian cells. EMBO Rep. 2006 Jan;7(1):106-13. [PubMed
]
- Notari L, Baladron V, Aroca-Aguilar JD, Balko N, Heredia R, Meyer C, Notario PM, Saravanamuthu S, Nueda ML, Sanchez-Sanchez F, Escribano J, Laborda J, Becerra SP: Identification of a lipase-linked cell membrane receptor for pigment epithelium-derived factor. J Biol Chem. 2006 Dec 8;281(49):38022-37. Epub 2006 Oct 10. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Schoenborn V, Heid IM, Vollmert C, Lingenhel A, Adams TD, Hopkins PN, Illig T, Zimmermann R, Zechner R, Hunt SC, Kronenberg F: The ATGL gene is associated with free fatty acids, triglycerides, and type 2 diabetes. Diabetes. 2006 May;55(5):1270-5. [PubMed
]
- Fischer J, Lefevre C, Morava E, Mussini JM, Laforet P, Negre-Salvayre A, Lathrop M, Salvayre R: The gene encoding adipose triglyceride lipase (PNPLA2) is mutated in neutral lipid storage disease with myopathy. Nat Genet. 2007 Jan;39(1):28-30. Epub 2006 Dec 24. [PubMed
]
|
| Enzyme 49 Metabolite References |
Not Available |
|
Enzyme 50
[top]
|
| Enzyme 50 ID |
13574 |
| Enzyme 50 Name |
Cytosolic phospholipase A2 delta |
| Enzyme 50 Synonyms |
- cPLA2-delta
- Phospholipase A2 group IVD
|
| Enzyme 50 Gene Name |
PLA2G4D |
| Enzyme 50 Protein Sequence |
>Cytosolic phospholipase A2 delta
MESLSPGGPPGHPYQGEASTCWQLTVRVLEARNLRWADLLSEADPYVILQLSTAPGMKFK
TKTLTDTSHPVWNEAFRFLIQSQVKNVLELSIYDEDSVTEDDICFKVLYDISEVLPGKLL
RKTFSQSPQGEEELDVEFLMEETSDRPENLITNKVIVARELSCLDVHLDSTGSTAVVADQ
DKLELELVLKGSYEDTQTSFLGTASAFRFHYMAALETELSGRLRSSRSNGWNGDNSAGYL
TVPLRPLTIGKEVTMDVPAPNAPGVRLQLKAEGCPEELAVHLGFNLCAEEQAFLSRRKQV
VAKALKQALQLDRDLQEDEVPVVGIMATGGGARAMTSLYGHLLALQKLGLLDCVTYFSGI
SGSTWTMAHLYGDPEWSQRDLEGPIRYAREHLAKSKLEVFSPERLASYRRELELRAEQGH
PTTFVDLWALVLESMLHGQVMDQKLSGQRAALERGQNPLPLYLSLNVKENNLETLDFKEW
VEFSPYEVGFLKYGAFVPPELFGSEFFMGRLMRRIPEPRICFLEAIWSNIFSLNLLDAWY
DLTSSGESWKQHIKDKTRSLEKEPLTTSGTSSRLEASWLQPGTALAQAFKGFLTGRPLHQ
RSPNFLQGLQLHQDYCSHKDFSTWADYQLDSMPSQLTPKEPRLCLVDAAYFINTSSPSMF
RPGRRLDLILSFDYSLSAPFEALQQTELYCRARGLPFPRVEPSPQDQHQPRECHLFSDPA
CPEAPILLHFPLVNASFKDHSAPGVQRSPAELQGGQVDLTGATCPYTLSNMTYKEEDFER
LLRLSDYNVQTSQGAILQALRTALKHRTLEARPPRAQT
|
| Enzyme 50 Number of Residues |
818 |
| Enzyme 50 Molecular Weight |
91951.4 |
| Enzyme 50 Theoretical pI |
5.19 |
| Enzyme 50 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- phospholipase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 50 General Function |
Involved in metabolic process |
| Enzyme 50 Specific Function |
Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Not arachidonic acid-specific but has linoleic acid-specific activity. May play a role in inflammation in psoriatic lesions |
| Enzyme 50 Pathways |
|
| Enzyme 50 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 50 Pfam Domain Function |
|
| Enzyme 50 Signals |
|
| Enzyme 50 Transmembrane Regions |
|
| Enzyme 50 Essentiality |
Not Available |
| Enzyme 50 GenBank ID Protein |
29467442  |
| Enzyme 50 UniProtKB/Swiss-Prot ID |
Q86XP0  |
| Enzyme 50 UniProtKB/Swiss-Prot Entry Name |
PA24D_HUMAN  |
| Enzyme 50 PDB ID |
Not Available |
| Enzyme 50 Cellular Location |
Not Available |
| Enzyme 50 Gene Sequence |
>2457 bp
ATGGAGAGCCTGTCACCTGGGGGACCAACTGGCCACCCTTACCAGGGGGAGGCCTCTACC
TGCTGGCAGCTCACAGTGAGGGTCCTGGAGGCGCGGAACCTGCGCTGGGCTGACCTGTTG
AGTGAGGCCGACCCTTACGTGATCCTACAGCTGTCGACCGCACCTGGAATGAAGTTTAAG
ACCAAGACGCTCACCGACACCAGTCATCCTGTGTGGAATGAGGCCTTCCGTTTCCTTATC
CAAAGTCAGGTCAAGAATGTTCTGGAGCTTAGCATCTATGATGAGGACTCAGTCACGGAG
GATGACATCTGCTTCAAGGTTCTCTATGACATCTCAGAAGTCCTCCCTGGCAAGCTGCTC
CGGAAAACCTTCTCCCAGAGTCCCCAGGGAGAGGAGGAGCTGGATGTGGAGTTCCTGATG
GAAGAAACGTCAGATCGCCCAGAAAACCTCATCACCAACAAAGTCATTGTGGCCCGAGAG
CTGTCATGCCTGGATGTGCATCTGGACAGCACAGGGAGCACCGCTGTGGTTGCAGATCAG
GACAAGCTGGAGCTGGAGCTGGTGCTGAAGGGGTCCTATGAGGACACACAGACATCCTTC
CTGGGCACAGCCTCTGCCTTCCGCTTCCACTACATGGCAGCCCTAGAGACAGAGCTGAGC
GGGCGCCTGAGGAGCTCCAGAAGCAATGGCTGGAATGGGGACAACTCAGCTGGGTACCTC
ACTGTGCCCCTGAGGCCCTTGACCATTGGGAAGGAGGTGACTATGGATGTTCCTGCTCCA
AATGCCCCAGGAGTGAGGCTGCAGCTCAAGGCAGAGGGCTGCCCTGAGGAGCTGGCCGTG
CACCTGGGCTTCAATCTCTGTGCAGAGGAGCAGGCCTTCCTGAGCAGGAGGAAGCAGGTG
GTGGCCAAGGCCCTGAAGCAGGCCCTGCAGCTGGACAGAGACCTGCAGGAGGATGAGGTA
CCCGTTGTGGGCATCATGGCCACAGGAGGAGGTGCCCGGGCCATGACCTCACTCTACGGC
CACCTATTGGCCTTGCAGAAGCTGGGCCTCCTAGACTGTGTGACCTACTTCAGTGGCATC
TCTGGCTCTACGTGGACAATGGCCCACCTGTACGGGGACCCTGAGTGGTCGCAGAGGGAC
CTGGAGGGACCTATCAGATACGCCCGGGAGCACCTGGCCAAGAGCAAGCTGGAGGTCTTT
TCCCCAGAGCGCCTGGCGAGCTACCGCCGGGAGCTGGAGCTGCGGGCTGAGCAGGGCCAC
CCCACGACCTTTGTGGACCTGTGGGCGCTAGTGCTGGAGTCCATGCTGCACGGCCAGGTG
ATGGATCAGAAGCTGTCAGGACAGAGAGCCGCCCTGGAACGGGGTCAGAACCCTCTGCCC
CTCTACTTGAGCCTCAATGTCAAAGAGAACAATCTGGAGACACTGGACTTCAAGGAGTGG
GTTGAGTTCTCCCCCTATGAGGTCGGTTTCCTGAAGTACGGGGCCTTCGTCCCTCCTGAG
CTCTTCGGCTCCGAGTTCTTCATGGGACGGCTGATGAGGAGGATCCCGGAGCCCCGGATC
TGCTTTCTGGAAGCCATCTGGAGCAACATTTTCTCCCTGAACCTGCTGGATGCCTGGTAT
GACCTCACCAGTTCTGGGGAGTCCTGGAAACAGCACATCAAGGACAAGACCAGGAGCTTA
GAGAAGGAGCCCCTGACCACCTCGGGGACCTCCTCGCGGCTGGAGGCCTCGTGGCTGCAG
CCAGGCACGGCGCTGGCCCAGGCATTTAAAGGCTTCCTGACAGGCAGGCCCCTCCACCAG
CGCAGCCCCAACTTCCTCCAGGGCCTCCAGCTGCACCAGGACTACTGTAGCCACAAAGAC
TTCTCCACCTGGGCAGACTACCAGCTTGACTCCATGCCCAGCCAGCTGACCCCCAAGGAG
CCCCGGCTCTGCCTGGTGGACGCCGCCTACTTCATCAACACCAGCTCTCCCTCCATGTTC
CGGCCAGGCCGCAGGCTGGACCTCATCCTCTCCTTCGACTACTCCCTATCTGCGCCCTTC
GAGGCACTGCAGCAGACGGAGCTGTACTGCCGGGCCCGGGGGCTGCCCTTCCCCCGGGTG
GAACCCAGCCCTCAGGACCAGCACCAGCCAAGGGAATGCCACCTCTTCTCAGACCCCGCC
TGCCCCGAGGCCCCGATCCTGCTGCACTTCCCGCTGGTCAATGCCTCCTTCAAGGACCAC
TCAGCCCCCGGTGTCCAGCGCAGCCCCGCAGAGCTCCAGGGTGGCCAAGTGGATCTCACC
GGGGCCACCTGCCCCTACACCCTGTCCAACATGACCTACAAGGAGGAAGACTTCGAGCGC
CTGCTGCGGCTCAGTGACTACAACGTGCAGACCAGCCAGGGTGCCATCCTGCAGGCCCTG
AGGACCGCGCTGAAGCACCGGACTCTAGAGGCGAGGCCTCCAAGGGCACAGACCTGA
|
| Enzyme 50 GenBank Gene ID |
AB090876  |
| Enzyme 50 GeneCard ID |
PLA2G4D  |
| Enzyme 50 GenAtlas ID |
PLA2G4D  |
| Enzyme 50 HGNC ID |
HGNC:30038  |
| Enzyme 50 Chromosome Location |
1 |
| Enzyme 50 Locus |
15q15.1 |
| Enzyme 50 SNPs |
SNPJam Report  |
| Enzyme 50 General References |
- Chiba H, Michibata H, Wakimoto K, Seishima M, Kawasaki S, Okubo K, Mitsui H, Torii H, Imai Y: Cloning of a gene for a novel epithelium-specific cytosolic phospholipase A2, cPLA2delta, induced in psoriatic skin. J Biol Chem. 2004 Mar 26;279(13):12890-7. Epub 2004 Jan 6. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Tao R, Yu Y, Zhang X, Shi J, Guo Y, Wang C, Han B, Xu Q, Shang H, Zhang X, Xie L, Liu S, Ju G, Shen Y, Wei J: A family based study of the genetic association between the PLA2G4D gene and schizophrenia. Prostaglandins Leukot Essent Fatty Acids. 2005 Dec;73(6):419-22. Epub 2005 Oct 6. [PubMed
]
|
| Enzyme 50 Metabolite References |
Not Available |
|
Enzyme 51
[top]
|
| Enzyme 51 ID |
13575 |
| Enzyme 51 Name |
Cytosolic phospholipase A2 epsilon |
| Enzyme 51 Synonyms |
- cPLA2-epsilon
- Phospholipase A2 group IVE
|
| Enzyme 51 Gene Name |
PLA2G4E |
| Enzyme 51 Protein Sequence |
>Cytosolic phospholipase A2 epsilon
MLLRQMHARVSHSLPDPCQAEDSRPSATCALKAPQTSWDGLLREGLSPCHLLTVRVIRMK
NVRQADMLSQTDCFVSLWLPTASQKKLRTRTISNCPNPEWNESFNFQIQSRVKNVLELSV
CDEDTVTPDDHLLTVLYDLTKLCFRKKTHVKFPLNPQGMEELEVEFLLEESPSPPETLVT
NGVLVSRGHGWLLLSGEQDQGRKQWAKDLLVMVNESFENTQRVRPCLEPCCPTSACFHYP
KYFQSQVHVEVPKSHWSCGLCCRSRKKGPISQPLDCLSDGQVMTLPVGGGESLGSPETLD
VRLGFSLCPAELEFLQKRKVVVAKALKQVLQLEEDLQEDEVPLIAIMATGGGTRSMTSMY
GHLLGLQKLNLLDCASYITGLSGATWTMATLYRDPDWSSKNLEPAIFEARRHVVKDKLPS
LFPDQLRKFQEELRQRSQEGYRVTFTDFWGLLIETCLGDERNECKLSDQRAALSCGQNPL
PIYLTINVKDDVSNQDFREWFEFSPYEVGLQKYGAFIPSELFGSEFFMGRLVKRIPESRI
CYMLGLWSSIFSLNLLDAWNLSHTSEEFFHRWTREKVQDIEDEPILPEIPKCDANILETT
VVIPGSWLSNSFREILTHRSFVSEFHNFLSGLQLHTNYLQNGQFSRWKDTVLDGFPNQLT
ESANHLCLLDTAFFVNSSYPPLLRPERKADLIIHLNYCAGSQTKPLKQTCEYCTVQNIPF
PKYELPDENENLKECYLMENPQEPDAPIVTFFPLINDTFRKYKAPGVERSPEELEQGQVD
IYGPKTPYATKELTYTEATFDKLVKLSEYNILNNKDTLLQALRLAVEKKKRLKGQCPS
|
| Enzyme 51 Number of Residues |
838 |
| Enzyme 51 Molecular Weight |
95686.5 |
| Enzyme 51 Theoretical pI |
5.78 |
| Enzyme 51 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- phospholipase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 51 General Function |
Involved in metabolic process |
| Enzyme 51 Specific Function |
Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position |
| Enzyme 51 Pathways |
|
| Enzyme 51 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 51 Pfam Domain Function |
|
| Enzyme 51 Signals |
|
| Enzyme 51 Transmembrane Regions |
|
| Enzyme 51 Essentiality |
Not Available |
| Enzyme 51 GenBank ID Protein |
Not Available |
| Enzyme 51 UniProtKB/Swiss-Prot ID |
Q3MJ16  |
| Enzyme 51 UniProtKB/Swiss-Prot Entry Name |
PA24E_HUMAN  |
| Enzyme 51 PDB ID |
Not Available |
| Enzyme 51 Cellular Location |
Not Available |
| Enzyme 51 Gene Sequence |
Not Available |
| Enzyme 51 GenBank Gene ID |
Not Available |
| Enzyme 51 GeneCard ID |
PLA2G4E  |
| Enzyme 51 GenAtlas ID |
PLA2G4E  |
| Enzyme 51 HGNC ID |
HGNC:24791  |
| Enzyme 51 Chromosome Location |
1 |
| Enzyme 51 Locus |
15q15.1 |
| Enzyme 51 SNPs |
SNPJam Report  |
| Enzyme 51 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Tang LY, Deng N, Wang LS, Dai J, Wang ZL, Jiang XS, Li SJ, Li L, Sheng QH, Wu DQ, Li L, Zeng R: Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction. Mol Cell Proteomics. 2007 Nov;6(11):1952-67. Epub 2007 Aug 12. [PubMed
]
|
| Enzyme 51 Metabolite References |
Not Available |
|
Enzyme 52
[top]
|
| Enzyme 52 ID |
13576 |
| Enzyme 52 Name |
Cytosolic phospholipase A2 zeta |
| Enzyme 52 Synonyms |
- cPLA2-zeta
- Phospholipase A2 group IVF
|
| Enzyme 52 Gene Name |
PLA2G4F |
| Enzyme 52 Protein Sequence |
>Cytosolic phospholipase A2 zeta
MLWALWPRWLADKMLPLLGAVLLQKREKRGPLWRHWRRETYPYYDLQVKVLRATNIRGTD
LLSKADCYVQLWLPTASPSPAQTRIVANCSDPEWNETFHYQIHGAVKNVLELTLYDKDIL
GSDQLSLLLFDLRSLKCGQPHKHTFPLNHQDSQELQVEFVLEKSQVPASEVITNGVLVAH
PCLRIQGTLRGDGTAPREEYGSRQLQLAVPGAYEKPQLLPLQPPTEPGLPPTFTFHVNPV
LSSRLHVELMELLAAVQSGPSAELEAQTSKLGEGGILLSSLPLGQEEQCSVALGEGQEVA
LSMKVEMSSGDLDLRLGFDLSDGEQEFLDRRKQVVSKALQQVLGLSEALDSGQVPVVAVL
GSGGGTRAMSSLYGSLAGLQELGLLDTVTYLSGVSGSTWCISTLYRDPAWSQVALQGPIE
RAQVHVCSSKMGALSTERLQYYTQELGVRERSGHSVSLIDLWGLLVEYLLYQEENPAKLS
DQQEAVRQGQNPYPIYTSVNVRTNLSGEDFAEWCEFTPYEVGFPKYGAYVPTELFGSELF
MGRLLQLQPEPRICYLQGMWGSAFATSLDEIFLKTAGSGLSFLEWYRGSVNITDDCQKPQ
LHNPSRLRTRLLTPQGPFSQAVLDIFTSRFTSAQSFNFTRGLCLHKDYVAGREFVAWKDT
HPDAFPNQLTPMRDCLYLVDGGFAINSPFPLALLPQRAVDLILSFDYSLEAPFEVLKMTE
KYCLDRGIPFPSIEVGPEDVEEARECYLFAKAEDPRSPIVLHFPLVNRTFRTHLAPGVER
QTAEEKAFGDFVINRPDTPYGMMNFTYEPQDFYRLVALSRYNVLNNVETLKCALQLALDR
HQARERAGA
|
| Enzyme 52 Number of Residues |
849 |
| Enzyme 52 Molecular Weight |
95049.4 |
| Enzyme 52 Theoretical pI |
5.11 |
| Enzyme 52 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- phospholipase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 52 General Function |
Involved in metabolic process |
| Enzyme 52 Specific Function |
Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Has higher enzyme activity for phosphatidylethanolamine than phosphatidylcholine |
| Enzyme 52 Pathways |
|
| Enzyme 52 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 52 Pfam Domain Function |
|
| Enzyme 52 Signals |
|
| Enzyme 52 Transmembrane Regions |
|
| Enzyme 52 Essentiality |
Not Available |
| Enzyme 52 GenBank ID Protein |
281371376  |
| Enzyme 52 UniProtKB/Swiss-Prot ID |
Q68DD2  |
| Enzyme 52 UniProtKB/Swiss-Prot Entry Name |
PA24F_HUMAN  |
| Enzyme 52 PDB ID |
Not Available |
| Enzyme 52 Cellular Location |
Not Available |
| Enzyme 52 Gene Sequence |
>2550 bp
ATGCTTTGGGCACTCTGGCCAAGGTGGCTGGCAGACAAGATGCTGCCCCTCCTGGGGGCA
GTGCTGCTTCAGAAGAGAGAGAAGAGGGGCCCTCTGTGGAGGCACTGGCGGCGGGAAACC
TACCCATACTATGACCTCCAGGTGAAGGTGCTGAGGGCCACAAACATCCGGGGCACAGAC
CTGCTGTCCAAAGCCGACTGCTATGTGCAACTGTGGCTGCCCACGGCGTCCCCAAGCCCT
GCCCAGACTAGGATAGTGGCCAACTGCAGTGACCCCGAGTGGAATGAGACCTTCCACTAC
CAGATCCATGGTGCTGTGAAGAACGTCCTGGAGCTCACCCTCTATGACAAGGACATCCTG
GGCAGCGACCAGCTCTCTCTGCTCCTGTTTGACCTGAGAAGCCTCAAGTGTGGCCAACCT
CACAAACACACCTTCCCACTCAACCACCAGGATTCACAAGAGCTGCAGGTGGAATTTGTT
CTGGAGAAGAGCCAGGTGCCTGCATCTGAAGTCATCACCAACGGGGTTCTGGTGGCTCAC
CCCTGTCTGAGAATCCAGGGCACGCTCCGGGGAGATGGGACAGCCCCACGGGAAGAGTAC
GGCTCTAGGCAGCTCCAGCTGGCAGTGCCTGGAGCCTACGAGAAGCCACAGCTCTTGCCC
CTGCAGCCTCCCACAGAGCCAGGCCTCCCACCCACCTTTACCTTCCACGTGAACCCAGTG
CTGAGCTCCAGGCTACACGTGGAGCTGATGGAGCTGCTGGCAGCTGTGCAGAGTGGCCCC
AGCGCAGAGTTGGAGGCTCAGACCAGCAAGCTGGGCGAGGGGGGCATCCTGCTCTCCTCT
CTGCCCCTAGGCCAGGAGGAACAGTGTTCTGTGGCCCTGGGGGAGGGCCAGGAGGTGGCT
CTGAGCATGAAGGTGGAAATGAGCTCCGGGGACCTAGACCTACGCCTTGGCTTTGACCTC
TCTGACGGGGAGCAGGAGTTTCTGGACAGGAGGAAGCAGGTCGTGTCCAAGGCCCTGCAG
CAAGTGCTGGGATTGAGTGAGGCTCTGGACAGTGGCCAGGTGCCTGTAGTGGCTGTGTTG
GGTTCCGGGGGTGGAACCCGAGCCATGTCTTCTCTGTACGGCAGCCTGGCAGGGTTGCAG
GAGCTCGGCCTTCTAGACACTGTGACCTACCTGAGTGGGGTCTCTGGGTCTACCTGGTGC
ATCTCCACACTCTACAGGGACCCAGCCTGGTCCCAGGTGGCCTTGCAGGGCCCCATTGAG
CGTGCCCAGGTTCACGTCTGCAGCAGTAAGATGGGAGCTTTGTCCACGGAGCGGCTACAG
TACTACACTCAGGAACTGGGGGTCCGGGAGCGCAGTGGCCACAGCGTGTCCCTCATCGAC
CTCTGGGGCCTCCTTGTTGAGTATCTCCTGTACCAGGAGGAGAACCCTGCCAAGCTGTCT
GACCAACAGGAGGCGGTCCGCCAGGGTCAGAACCCTTACCCCATTTACACCAGTGTCAAC
GTCCGCACCAACTTGAGTGGGGAAGATTTTGCAGAGTGGTGCGAGTTCACGCCCTATGAG
GTTGGCTTCCCCAAGTACGGGGCTTATGTTCCCACCGAGCTCTTCGGCTCAGAACTCTTC
ATGGGACGATTGCTGCAGCTCCAGCCTGAACCCCGGATCTGTTACCTGCAAGGTATGTGG
GGCAGCGCCTTTGCCACCAGCCTGGATGAGATCTTCCTAAAGACCGCCGGCTCGGGCCTC
AGCTTCCTGGAGTGGTACAGAGGCAGTGTGAATATCACAGACGACTGCCAGAAGCCTCAG
CTGCACAACCCCTCGAGGCTGCGAACGAGGCTCCTCACCCCACAGGGGCCCTTCTCCCAG
GCTGTGCTGGACATATTCACCTCCCGCTTCACTTCCGCCCAGAGCTTTAACTTCACCCGG
GGTCTCTGCTTGCACAAGGACTATGTGGCTGGCAGGGAGTTCGTGGCCTGGAAAGACACA
CACCCGGACGCCTTCCCCAACCAGCTCACCCCCATGCGGGACTGCCTGTACCTGGTGGAC
GGAGGCTTTGCCATCAACTCTCCGTTCCCACTGGCTCTGCTGCCTCAGAGAGCAGTGGAC
CTCATTCTGTCCTTTGACTATTCCTTGGAAGCCCCTTTTGAGGTCTTGAAGATGACAGAG
AAGTACTGCCTGGACCGAGGAATCCCCTTCCCTAGCATCGAGGTGGGCCCTGAGGACATG
GAGGAGGCCCGTGAGTGCTATCTGTTTGCCAAGGCTGAGGACCCCCGCTCCCCCATTGTG
CTGCACTTCCCCCTGGTTAACCGTACCTTCCGCACACACCTGGCCCCAGGTGTGGAGCGA
CAAACAGCTGAGGAGAAGGCCTTTGGGGACTTTGTCATCAACAGGCCAGACACCCCCTAT
GGCATGATGAACTTCACCTATGAGCCCCAGGACTTTTATCGGCTGGTGGCCCTCAGTCGA
TACAACGTCCTGAACAACGTGGAGACCTTGAAGTGCGCCCTCCAGCTGGCTCTGGACCGG
CACCAGGCTCGGGAGAGGGCAGGGGCCTGA
|
| Enzyme 52 GenBank Gene ID |
NM_213600.3  |
| Enzyme 52 GeneCard ID |
PLA2G4F  |
| Enzyme 52 GenAtlas ID |
PLA2G4F  |
| Enzyme 52 HGNC ID |
HGNC:27396  |
| Enzyme 52 Chromosome Location |
1 |
| Enzyme 52 Locus |
15q15.1 |
| Enzyme 52 SNPs |
SNPJam Report  |
| Enzyme 52 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
|
| Enzyme 52 Metabolite References |
Not Available |
|
Enzyme 53
[top]
|
| Enzyme 53 ID |
13656 |
| Enzyme 53 Name |
Calcium-independent phospholipase A2-gamma |
| Enzyme 53 Synonyms |
- Intracellular membrane-associated calcium-independent phospholipase A2 gamma
- iPLA2-gamma
- PNPLA-gamma
- Patatin-like phospholipase domain-containing protein 8
- iPLA2-2
|
| Enzyme 53 Gene Name |
PNPLA8 |
| Enzyme 53 Protein Sequence |
>Calcium-independent phospholipase A2-gamma
MSINLTVDIYIYLLSNARSVCGKQRSKQLYFLFSPKHYWRISHISLQRGFHTNIIRCKWT
KSEAHSCSKHCYSPSNHGLHIGILKLSTSAPKGLTKVNICMSRIKSTLNSVSKAVFGNQN
EMISRLAQFKPSSQILRKVSDSGWLKQKNIKQAIKSLKKYSDKSAEKSPFPEEKSHIIDK
EEDIGKRSLFHYTSSITTKFGDSFYFLSNHINSYFKRKEKMSQQKENEHFRDKSELEDKK
VEEGKLRSPDPGILAYKPGSESVHTVDKPTSPSAIPDVLQVSTKQSIANFLSRPTEGVQA
LVGGYIGGLVPKLKYDSKSQSEEQEEPAKTDQAVSKDRNAEEKKRLSLQREKIIARVSID
NRTRALVQALRRTTDPKLCITRVEELTFHLLEFPEGKGVAVKERIIPYLLRLRQIKDETL
QAAVREILALIGYVDPVKGRGIRILSIDGGGTRGVVALQTLRKLVELTQKPVHQLFDYIC
GVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFSQNVIVGTVKMSWSHAFYDSQTWENI
LKDRMGSALMIETARNPTCPKVAAVSTIVNRGITPKAFVFRNYGHFPGINSHYLGGCQYK
MWQAIRASSAAPGYFAEYALGNDLHQDGGLLLNNPSALAMHECKCLWPDVPLECIVSLGT
GRYESDVRNTVTYTSLKTKLSNVINSATDTEEVHIMLDGLLPPDTYFRFNPVMCENIPLD
ESRNEKLDQLQLEGLKYIERNEQKMKKVAKILSQEKTTLQKINDWIKLKTDMYEGLPFFS
KL
|
| Enzyme 53 Number of Residues |
782 |
| Enzyme 53 Molecular Weight |
88476.1 |
| Enzyme 53 Theoretical pI |
9.70 |
| Enzyme 53 GO Classification |
| Function |
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 53 General Function |
Involved in metabolic process |
| Enzyme 53 Specific Function |
Calcium-independent phospholipase A2, which catalyzes the hydrolysis of the sn-2 position of glycerophospholipids, PtdSer and to a lower extent PtdCho. Cleaves membrane phospholipids |
| Enzyme 53 Pathways |
|
| Enzyme 53 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 53 Pfam Domain Function |
|
| Enzyme 53 Signals |
|
| Enzyme 53 Transmembrane Regions |
|
| Enzyme 53 Essentiality |
Not Available |
| Enzyme 53 GenBank ID Protein |
7670058  |
| Enzyme 53 UniProtKB/Swiss-Prot ID |
Q9NP80  |
| Enzyme 53 UniProtKB/Swiss-Prot Entry Name |
PLPL8_HUMAN  |
| Enzyme 53 PDB ID |
Not Available |
| Enzyme 53 Cellular Location |
Not Available |
| Enzyme 53 Gene Sequence |
>2349 bp
ATGTCTATTAATCTGACTGTAGATATATATATTTACCTCCTTAGTAATGCAAGAAGTGTT
TGTGGGAAGCAGAGAAGCAAGCAACTGTATTTCTTGTTCTCACCTAAGCATTACTGGAGG
ATAAGCCACATCAGTCTACAAAGAGGTTTTCATACAAACATAATAAGATGTAAATGGACC
AAAAGTGAAGCACATTCTTGCAGTAAGCACTGTTACTCTCCAAGCAACCATGGTTTACAT
ATTGGGATTTTGAAACTTAGCACTTCTGCTCCCAAGGGACTTACAAAAGTGAACATTTGT
ATGTCCCGTATTAAAAGTACTTTGAACTCTGTTTCAAAGGCTGTTTTTGGCAATCAAAAT
GAAATGATTTCACGTTTAGCTCAATTTAAGCCAAGTTCCCAAATTTTAAGAAAAGTATCG
GATAGTGGCTGGTTAAAACAGAAAAACATCAAACAAGCCATCAAATCTCTGAAAAAATAT
AGTGACAAATCAGCAGAAAAGAGTCCTTTTCCAGAAGAGAAAAGTCACATTATAGACAAA
GAAGAAGATATAGGTAAACGCAGTCTTTTTCATTACACAAGTTCTATAACCACAAAATTT
GGAGACTCATTCTACTTTTTATCAAATCATATTAATTCATATTTCAAACGTAAGGAAAAA
ATGTCTCAACAAAAGGAAAATGAACATTTCCGGGACAAATCAGAACTTGAAGATAAAAAG
GTAGAAGAGGGGAAATTAAGATCTCCAGATCCTGGCATCCTGGCTTATAAGCCAGGCTCA
GAATCTGTACATACGGTGGACAAGCCTACAAGTCCTTCTGCGATACCTGATGTTCTTCAA
GTTTCAACTAAACAAAGTATTGCTAACTTTCTTTCTCGTCCCACGGAAGGTGTACAAGCT
TTAGTAGGTGGTTATATTGGTGGACTTGTCCCCAAATTAAAGTATGATTCAAAGAGTCAG
TCAGAAGAACAGGAAGAGCCTGCTAAAACTGATCAGGCTGTCAGCAAAGACAGAAATGCA
GAGGAGAAAAAGCGTTTATCTCTTCAGCGAGAAAAGATTATCGCAAGGGTGAGTATTGAT
AACAGGACCCGGGCATTAGTTCAGGCATTAAGAAGAACAACTGACCCAAAGCTCTGCATT
ACTAGGGTTGAAGAACTGACTTTTCATCTTCTAGAATTTCCTGAAGGAAAAGGAGTGGCT
GTCAAGGAAAGAATTATTCCATATTTATTACGACTGAGACAAATTAAGGATGAAACTCTT
CAGGCTGCAGTTAGAGAAATTTTGGCCCTAATTGGCTATGTGGATCCAGTGAAAGGGAGA
GGAATCCGAATTCTCTCAATTGATGGTGGAGGAACAAGGGGCGTGGTTGCTCTCCAGACC
CTACGAAAATTAGTTGAACTTACTCAGAAGCCAGTTCATCAGCTCTTTGATTACATTTGT
GGTGTAAGCACAGGTGCCATATTAGCTTTCATGTTGGGGTTGTTTCATATGCCCTTGGAT
GAATGTGAGGAACTTTATCGAAAATTAGGATCAGATGTATTTTCACAAAATGTCATTGTT
GGAACAGTAAAAATGAGTTGGAGCCATGCATTTTATGACAGTCAAACATGGGAAAACATT
CTTAAGGATAGGATGGGATCTGCACTGATGATTGAAACAGCAAGAAACCCCACATGTCCT
AAGGTAGCTGCTGTAAGTACCATAGTAAATAGAGGGATAACACCCAAAGCTTTTGTGTTC
AGAAACTATGGTCATTTTCCTGGAATCAACTCTCATTATTTGGGAGGCTGTCAGTATAAA
ATGTGGCAGGCCATTAGAGCCTCATCTGCTGCTCCAGGCTACTTTGCAGAATATGCATTG
GGAAATGATCTTCATCAAGATGGAGGTTTGCTTCTGAATAACCCTTCGGCATTAGCTATG
CATGAGTGTAAATGTCTTTGGCCAGATGTGCCGTTAGAGTGCATAGTATCCCTGGGCACT
GGACGTTATGAGAGTGATGTGAGAAACACGGTAACATACACAAGCTTGAAAACTAAACTT
TCTAATGTTATCAACAGTGCTACAGATACAGAAGAAGTCCATATAATGCTTGATGGCCTG
TTACCTCCTGACACCTATTTTAGATTCAATCCTGTAATGTGTGAAAACATACCTCTAGAT
GAAAGTCGAAATGAAAAGCTGGATCAGCTGCAGTTGGAAGGGTTGAAATACATAGAAAGA
AATGAACAAAAAATGAAAAAAGTTGCAAAAATATTAAGTCAAGAAAAAACAACTCTGCAG
AAAATTAATGATTGGATAAAATTAAAAACTGATATGTATGAAGGACTTCCATTCTTTTCA
AAATTGTGA
|
| Enzyme 53 GenBank Gene ID |
AB041261  |
| Enzyme 53 GeneCard ID |
PNPLA8  |
| Enzyme 53 GenAtlas ID |
PNPLA8  |
| Enzyme 53 HGNC ID |
HGNC:28900  |
| Enzyme 53 Chromosome Location |
7 |
| Enzyme 53 Locus |
7q31 |
| Enzyme 53 SNPs |
SNPJam Report  |
| Enzyme 53 General References |
- Tanaka H, Takeya R, Sumimoto H: A novel intracellular membrane-bound calcium-independent phospholipase A(2). Biochem Biophys Res Commun. 2000 Jun 7;272(2):320-6. [PubMed
]
- Mancuso DJ, Jenkins CM, Gross RW: The genomic organization, complete mRNA sequence, cloning, and expression of a novel human intracellular membrane-associated calcium-independent phospholipase A(2). J Biol Chem. 2000 Apr 7;275(14):9937-45. [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
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- Kinsey GR, Cummings BS, Beckett CS, Saavedra G, Zhang W, McHowat J, Schnellmann RG: Identification and distribution of endoplasmic reticulum iPLA2. Biochem Biophys Res Commun. 2005 Feb 4;327(1):287-93. [PubMed
]
- Murakami M, Masuda S, Ueda-Semmyo K, Yoda E, Kuwata H, Takanezawa Y, Aoki J, Arai H, Sumimoto H, Ishikawa Y, Ishii T, Nakatani Y, Kudo I: Group VIB Ca2+-independent phospholipase A2gamma promotes cellular membrane hydrolysis and prostaglandin production in a manner distinct from other intracellular phospholipases A2. J Biol Chem. 2005 Apr 8;280(14):14028-41. Epub 2005 Feb 4. [PubMed
]
|
| Enzyme 53 Metabolite References |
Not Available |
|
Enzyme 54
[top]
|
| Enzyme 54 ID |
14866 |
| Enzyme 54 Name |
Cytosolic phospholipase A2 beta |
| Enzyme 54 Synonyms |
- cPLA2-beta
- Phospholipase A2 group IVB
|
| Enzyme 54 Gene Name |
PLA2G4B |
| Enzyme 54 Protein Sequence |
>Cytosolic phospholipase A2 beta
MAVAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVW
NQSFHFRIHRQLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEG
RLEVEFRLQSLADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGP
QEASVGTGTFRFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMR
VELKKEAGLRELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIM
ATGGGIRAMTSLYGQLAGLKELGLLDCVSYITGASGSTWALANLYEDPEWSQKDLAGPTE
LLKTQVTKNKLGVLAPSQLQRYRQELAERARLGYPSCFTNLWALINEALLHDEPHDHKLS
DQREALSHGQNPLPIYCALNTKGQSLTTFEFGEWCEFSPYEVGFPKYGAFIPSELFGSEF
FMGQLMKRLPESRICFLEGIWSNLYAANLQDSLYWASEPSQFWDRWVRNQANLDKEQVPL
LKIEEPPSTAGRIAEFFTDLLTWRPLAQATHNFLRGLHFHKDYFQHPHFSTWKATTLDGL
PNQLTPSEPHLCLLDVGYLINTSCLPLLQPTRDVDLILSLDYNLHGAFQQLQLLGRFCQE
QGIPFPPISPSPEEQLQPRECHTFSDPTCPGAPAVLHFPLVSDSFREYSAPGVRRTPEEA
AAGEVNLSSSDSPYHYTKVTYSQEDVDKLLHLTHYNVCNNQEQLLEALRQAVQRRRQRRP
H
|
| Enzyme 54 Number of Residues |
781 |
| Enzyme 54 Molecular Weight |
87977.0 |
| Enzyme 54 Theoretical pI |
5.85 |
| Enzyme 54 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lipase activity
- phospholipase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid catabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 54 General Function |
Involved in metabolic process |
| Enzyme 54 Specific Function |
Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position with a preference for arachidonoyl phospholipids. Has a much weaker activity than PLA2G4A. Isoform 3 has calcium-dependent activity against palmitoyl-arachidonyl-phosphatidylethanolamine and low level lysophospholipase activity but no activity against phosphatidylcholine |
| Enzyme 54 Pathways |
Not Available |
| Enzyme 54 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 54 Pfam Domain Function |
|
| Enzyme 54 Signals |
|
| Enzyme 54 Transmembrane Regions |
|
| Enzyme 54 Essentiality |
Not Available |
| Enzyme 54 GenBank ID Protein |
194387976  |
| Enzyme 54 UniProtKB/Swiss-Prot ID |
P0C869  |
| Enzyme 54 UniProtKB/Swiss-Prot Entry Name |
PA24B_HUMAN  |
| Enzyme 54 PDB ID |
Not Available |
| Enzyme 54 Cellular Location |
Not Available |
| Enzyme 54 Gene Sequence |
>2346 bp
ATGGCTGTGGCAGAGGTGTCCAGGACCTGCCTGCTCACGGTTCGTGTCCTGCAGGCCCAT
CGCCTACCCTCTAAGGACCTAGTGACCCCCTCTGACTGCTACGTGACTCTCTGGCTGCCC
ACGGCCTGCAGCCACAGGCTCCAGACACGCACGGTCAAGAACAGCAGTAGCCCTGTCTGG
AACCAGAGCTTTCACTTCAGGATCCACAGGCAGCTCAAGAATGTCATGGAACTGAAAGTC
TTTGACCAGGACCTGGTGACCGGAGATGACCCTGTGTTGTCAGTACTGTTTGATGCGGGG
ACTCTGCGGGCTGGGGAGTTCCGGCGCGAGAGCTTCTCACTGAGCCCTCAGGGTGAGGGG
CGCCTGGAAGTTGAATTTCGCCTGCAGAGTCTGGCTGACCGTGGCGAGTGGCTCGTCAGC
AATGGCGTTCTGGTGGCCCGGGAGCTCTCCTGCTTGCACGTTCAACTGGAGGAGACAGGA
GACCAGAAGTCCTCAGAGCACAGAGTTCAGCTTGTGGTTCCTGGGTCCTGTGAGGGTCCG
CAGGAGGCCTCTGTGGGCACTGGCACCTTCTGCTTCCACTGCCCAGCCTGCTGGGAGCAG
GAGCTGAGTATTCGCCTGCAGGATGCCCCCGAGGAGCAACTAAAGGCGCCACTGAGTGCC
CTGCCCTCTGGTCAAGTGGTGAGGCTTGTCTTCCCCACGTCCCAGGAGCCCCTGATGAGA
GTGGAGCTGAAAAAAGAAGCAGGACTGAGGGAGCTGGCCGTGCGACTGGGCTTCGGGCCC
TGTGCAGAGGAGCAGGCCTTCCTGAGCAGGAGGAAGCAGGTGGTGGCCGCGGCCTTGAGG
CAGGCCCTGCAGCTGGATGGAGACCTGCAGGAGGATGAGATCCCAGTGGTAGCTATTATG
GCCACTGGTGGTGGGATCCGGGCAATGACTTCCCTGTATGGGCAGCTGGCTGGCCTGAAG
GAGCTGGGCCTCTTGGATTGCGTCTCCTACATCACCGGGGCCTCGGGCTCCACCTGGGCC
TTGGCCAACCTTTATGAGGACCCAGAGTGGTCTCAGAAGGACCTGGCAGGGCCCACTGAG
TTGCTGAAGACCCAGGTGACCAAGAACAAGCTGGGTGTGCTGGCCCCCAGCCAGCTGCAG
CGGTACCGGCAGGAGCTGGCCGAGCGTGCCCGCTTGGGCTACCCAAGCTGCTTCACCAAC
CTGTGGGCCCTCATCAACGAGGCGCTGCTGCATGATGAGCCCCATGATCACAAGCTCTCA
GATCAACGGGAGGCCCTGAGTCATGGCCAGAACCCTCTGCCCATCTACTGTGCCCTCAAC
ACCAAAGGGCAGAGCCTGACCACTTTTGAATTTGGGGAGTGGTGCGAGTTCTCTCCCTAC
GAGGTCGGCTTCCCCAAGTACGGGGCCTTCATCCCCTCTGAGCTCTTTGGCTCCGAGTTC
TTTATGGGGCAGCTGATGAAGAGGCTTCCTGAGTCCCGCATCTGCTTCTTAGAAGGTATC
TGGAGCAACCTGTATGCAGCCAACCTCCAGGACAGCTTATACTGGGCCTCAGAGCCCAGC
CAGTTCTGGGACCGCTGGGTCAGGAACCAGGCCAACCTGGACAAGGAGCAGGTCCCCCTT
CTGAAGATAGAAGAACCACCCTCAACAGCCGGCAGGATAGCTGAGTTTTTCACCGATCTT
CTGACGTGGCGTCCACTGGCCCAGGCCACACATAATTTCCTGTGTGGCCTCCATTTCCAC
AAAGACTACTTTCAGCATCCTCACTTCTCCACATGGAAAGCTACCACTCTGGATGGGCTC
CCCAACCAGCTGACACCCTCGGAGCCCCACCTGTGCCTGCTGGATGTTGGCTACCTCATC
AATACCAGCTGCCTGCCCCTCCTGCAGCCCACTCGGGACGTGGACCTCATCCTGTCATTG
GACTACAACCTCCACGGAGCCTTCCAGCAGTTGCAGCTCCTGGGCCGGTTCTGCCAGGAG
CAGGGGATCCCGTTCCCACCCATCTCGCCCAGCCCCGAAGAGCAGCTCCAGCCTCGGGAG
TGCCACACCTTCTCTGACCCCACCTGCCCCGGAGCCCCTGCGGTGCTGCACTTTCCTCTG
GTCAGCGACTCCTTCCGGGAGTACTCGGCCCCTGGGGTCCGGCGGACACCCGAGGAGGCG
GCAGCTGAGGAGGTGAACCTGTCTTCATCGGACTCTCCCTACCACTACACGAAGGTGACC
TACAGCCAGGAGGACGTGGACAAGCTGCTGCACCTGACACATTACAATGTCTGCAACAAC
CAGGAGCAGCTGCTGGAGGCTCTGCGCCAGGCAGTGCAGCGGAGGCGGCAGCGCAGGCCC
CACTGA
|
| Enzyme 54 GenBank Gene ID |
AK299419  |
| Enzyme 54 GeneCard ID |
PLA2G4B  |
| Enzyme 54 GenAtlas ID |
PLA2G4B  |
| Enzyme 54 HGNC ID |
HGNC:9036  |
| Enzyme 54 Chromosome Location |
1 |
| Enzyme 54 Locus |
15q11.2-q21.3 |
| Enzyme 54 SNPs |
SNPJam Report  |
| Enzyme 54 General References |
- Pickard RT, Strifler BA, Kramer RM, Sharp JD: Molecular cloning of two new human paralogs of 85-kDa cytosolic phospholipase A2. J Biol Chem. 1999 Mar 26;274(13):8823-31. [PubMed
]
- Song C, Chang XJ, Bean KM, Proia MS, Knopf JL, Kriz RW: Molecular characterization of cytosolic phospholipase A2-beta. J Biol Chem. 1999 Jun 11;274(24):17063-7. [PubMed
]
- Ghosh M, Loper R, Gelb MH, Leslie CC: Identification of the expressed form of human cytosolic phospholipase A2beta (cPLA2beta): cPLA2beta3 is a novel variant localized to mitochondria and early endosomes. J Biol Chem. 2006 Jun 16;281(24):16615-24. Epub 2006 Apr 14. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
|
| Enzyme 54 Metabolite References |
Not Available |
|
Enzyme 55
[top]
|
| Enzyme 55 ID |
14918 |
| Enzyme 55 Name |
Putative neutral ceramidase C |
| Enzyme 55 Synonyms |
- N-acylsphingosine amidohydrolase 2C
- Non-lysosomal ceramidase C
|
| Enzyme 55 Gene Name |
ASAH2C |
| Enzyme 55 Protein Sequence |
>Putative neutral ceramidase C
MDSEKSSEWRSDVLNRLQSKYGSLYRRDNVILSGTHTHSGPAGYFQYTVFVIASEGFSNQ
TFQHMVTGILKSIDIAHTNMKPGKIFINKGNVDGVQINRSPYSYLQNPQSERARYSSNTD
KEMIVLKMVDLNGDDLGLISWFAIHPVSMNNSNHLVNSDNVGYASYLLEQEKNKGYLPGQ
GPFVAAFSSSNLGDVSPNILGPRCINTGESCDNANSTCPIGGPSMCIAKGPGQDMFDSTQ
IIGRAMYQRAKELYASASQEVTGPLASAHQWVDMTDVTVWLNSTHASKTCKPALGYSFAA
GTIDGVGGLNFTQGKTEGDPFWDTIRDQILGKPSEEIKECHKPKPILLHTGELSKPHPWH
PDIVDVQIITLGSLAITAIPGEFTTMSGRRLREAVQAEFASHGMQNMTVVISGLCNVYTH
YITTYEEYQAQRYEAASTIYGPHTLSAYIQLFRNLAKAIATDTVANLSRGPEPPFFKQLI
VPLIPSIVDRAPKGRTFGDVLQPAKPEYRVGEVAEVIFVGANPKNSVQNQNHQTFLTVEK
YEATSTSWQIVCNDASWETRFYWHKGLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQD
ILKPAVILSFEGTSPAFEVVTI
|
| Enzyme 55 Number of Residues |
622 |
| Enzyme 55 Molecular Weight |
68748.1 |
| Enzyme 55 Theoretical pI |
6.82 |
| Enzyme 55 GO Classification |
Not Available |
| Enzyme 55 General Function |
Involved in ceramidase activity |
| Enzyme 55 Specific Function |
May hydrolyze the sphingolipid ceramide into sphingosine and free fatty acid |
| Enzyme 55 Pathways |
Not Available |
| Enzyme 55 Reactions |
- N-acylsphingosine + H2O = a carboxylate + sphingosine [RN:R01493]
|
| Enzyme 55 Pfam Domain Function |
Not Available |
| Enzyme 55 Signals |
|
| Enzyme 55 Transmembrane Regions |
|
| Enzyme 55 Essentiality |
Not Available |
| Enzyme 55 GenBank ID Protein |
55962226  |
| Enzyme 55 UniProtKB/Swiss-Prot ID |
P0C7U2  |
| Enzyme 55 UniProtKB/Swiss-Prot Entry Name |
ASA2C_HUMAN  |
| Enzyme 55 PDB ID |
Not Available |
| Enzyme 55 Cellular Location |
Not Available |
| Enzyme 55 Gene Sequence |
>1833 bp
GTCCTGAACAGACTGCAGAGTAAATATGGCTCCCTGTACAGAAGAGATAATGTCATCCTG
AGTGGCACTCACACTCATTCAGGTCCTGCAGGATATTTCCAGTATACCGTGTTTGTAATT
GCCAGTGAAGGATTTAGCAATCAAACTTTTCAGCACATGGTCACTGGTATCTTGAAGAGC
ATTGACATAGCACACACAAATATGAAACCAGGCAAAATCTTCATCAATAAAGGAAATGTG
GATGGTGTGCAGATCAACAGAAGTCCGTATTCTTACCTTCAAAATCCGCAGTCAGAGAGA
GCAAGGTATTCTTCAAATACAGACAAGGAAATGATAGTTTTGAAAATGGTAGATTTGAAT
GGAGATGACTTGGGCCTTATCAGCTGGTTTGCCATCCACCCGGTCAGCATGAACAACAGT
AACCATCTTGTAAACAGTGACAATGTGGGCTATGCATCTTACCTGCTTGAGCAAGAGAAG
AACAAAGGATATCTACCTGGACAGGGGCCATTTGTAGCAGCCTTTTCTTCATCAAACCTA
GGAGATGTGTCCCCCAACATTCTTGGACCACGTTGCATCAACACAGGAGAGTCCTGTGAT
AACGCCAATAGCACTTGTCCCATTGGTGGGCCTAGCATGTGCATTGCTAAGGGACCTGGA
CAGGATATGTTTGACAGCACACAAATTATAGGACGGGCCATGTATCAGAGAGCAAAGGAA
CTCTATGCCTCTGCCTCCCAGGAGGTAACAGGACCACTGGCTTCAGCACACCAGTGGGTG
GATATGACAGATGTGACTGTCTGGCTCAATTCCACACATGCATCAAAAACATGTAAACCA
GCATTGGGCTACAGTTTTGCGGCTGGCACTATTGATGGAGTTGGAGGCCTCAATTTTACA
CAGGGGAAAACAGAAGGGGATCCATTTTGGGACACCATTCGGGACCAGATCCTGGGAAAG
CCATCTGAAGAAATTAAAGAATGTCATAAACCAAAGCCCATCCTTCTTCACACCGGAGAA
CTATCAAAACCTCACCCCTGGCATCCAGACATTGTTGATGTTCAGATTATTACCCTTGGG
TCCTTGGCCATAACTGCCATCCCCGGGGAGTTTACGACCATGTCTGGACGAAGACTTCGA
GAGGCAGTTCAAGCAGAATTTGCATCTCATGGGATGCAGAACATGACTGTTGTTATTTCA
GGTCTATGCAACGTCTATACACATTACATTACCACTTATGAAGAATACCAGGCTCAGCGA
TATGAGGCAGCATCGACAATTTATGGACCGCACACATTATCTGCTTACATTCAGCTCTTC
AGAAACCTTGCTAAGGCTATTGCTACGGACACGGTAGCCAACCTGAGCAGAGGTCCAGAA
CCTCCCTTTTTCAAACAATTAATAGTTCCATTAATTCCTAGTATTGTGGATAGAGCACCA
AAAGGCAGAACTTTCGGGGATGTCCTGCAGCCAGCAAAACCTGAATACAGAGTGGGGGAA
GTTGCTGAAGTTATATTTGTAGGTGCTAACCCGAAGAATTCAGTACAAAACCAGAACCAT
CAGACCTTCCTCACTGTGGAGAAATATGAGGCTACTTCAACATCGTGGCAGATAGTGTGT
AATGATGCCTCCTGGGAGACTCGTTTTTATTGGCACAAGGGACTCCTGGGTCTGAGTAAT
GCAACAGTGGAATGGCATATTCCAGACACTGCCCAGCCTGGAATCTACAGAATAAGATAT
TTTGGACACAATCGGAAGCAGGACATTCTGAAGCCTGCTGTCATACTTTCATTTGAAGGC
ACTTCCCCGGCTTTTGAAGTTGTAACTATTTAG
|
| Enzyme 55 GenBank Gene ID |
AL954360  |
| Enzyme 55 GeneCard ID |
ASAH2C  |
| Enzyme 55 GenAtlas ID |
ASAH2C  |
| Enzyme 55 HGNC ID |
HGNC:23457  |
| Enzyme 55 Chromosome Location |
1 |
| Enzyme 55 Locus |
10q11.22 |
| Enzyme 55 SNPs |
SNPJam Report  |
| Enzyme 55 General References |
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
|
| Enzyme 55 Metabolite References |
Not Available |
|
Enzyme 56
[top]
|
| Enzyme 56 ID |
14919 |
| Enzyme 56 Name |
Alkaline ceramidase 2 |
| Enzyme 56 Synonyms |
- AlkCDase 2
- Alkaline CDase 2
- haCER2
- Acylsphingosine deacylase 3-like
- N-acylsphingosine amidohydrolase 3-like
|
| Enzyme 56 Gene Name |
ACER2 |
| Enzyme 56 Protein Sequence |
>Alkaline ceramidase 2
MGAPHWWDQLQAGSSEVDWCEDNYTIVPAIAEFYNTISNVLFFILPPICMCLFRQYATCF
NSGIYLIWTLLVVVGIGSVYFHATLSFLGQMLDELAVLWVLMCALAMWFPRRYLPKIFRN
DRGRFKVVVSVLSAVTTCLAFVKPAINNISLMTLGVPCTALLIAELKRCDNMRVFKLGLF
SGLWWTLALFCWISDRAFCELLSSFNFPYLHCMWHILICLAAYLGCVCFAYFDAASEIPE
QGPVIKFWPNEKWAFIGVPYVSLLCANKKSSVKIT
|
| Enzyme 56 Number of Residues |
275 |
| Enzyme 56 Molecular Weight |
31308.9 |
| Enzyme 56 Theoretical pI |
7.71 |
| Enzyme 56 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 metabolic process
- ceramide metabolic process
- lipid metabolic process
- membrane lipid metabolic process
- metabolic process
- primary metabolic process
- sphingoid metabolic process
- sphingolipid metabolic process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 56 General Function |
Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| Enzyme 56 Specific Function |
Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Regulates the maturation of integrin beta-1 (ITGB1) by controlling the generation of sphingosine in the Golgi complex. Inhibits cell adhesion by reducing the level of ITGB1 in the cell surface. May have a role in cell proliferation and apoptosis that seems to depend on the balance between sphingosine and sphingosine-1-phosphate |
| Enzyme 56 Pathways |
Not Available |
| Enzyme 56 Reactions |
- N-acylsphingosine + H2O = a carboxylate + sphingosine [RN:R01493]
|
| Enzyme 56 Pfam Domain Function |
|
| Enzyme 56 Signals |
|
| Enzyme 56 Transmembrane Regions |
- 33-53
63-83
87-107
125-142
144-164
174-194
212-232
|
| Enzyme 56 Essentiality |
Not Available |
| Enzyme 56 GenBank ID Protein |
36304156  |
| Enzyme 56 UniProtKB/Swiss-Prot ID |
Q5QJU3  |
| Enzyme 56 UniProtKB/Swiss-Prot Entry Name |
ACER2_HUMAN  |
| Enzyme 56 PDB ID |
Not Available |
| Enzyme 56 Cellular Location |
Not Available |
| Enzyme 56 Gene Sequence |
>828 bp
ATGGGCGCCCCGCACTGGTGGGACCAGCTGCAGGCTGGTAGCTCGGAGGTGGACTGGTGC
GAGGACAACTACACCATCGTGCCTGCTATCGCCGAGTTCTACAACACGATCAGCAATGTC
TTATTTTTCATTTTACCGCCCATCTGCATGTGCTTGTTTCGTCAGTATGCAACATGCTTC
AACAGTGGCATCTACTTAATCTGGACTCTTTTGGTTGTAGTGGGAATTGGATCCGTCTAC
TTCCATGCAACCCTTAGTTTCTTGGGTCAGATGCTTGATGAACTTGCAGTCCTTTGGGTT
CTGATGTGTGCTTTGGCCATGTGGTTCCCCAGAAGGTATCTACCAAAGATCTTTCGGAAT
GACCGGGGTAGGTTCAAGGTGGTGGTCAGTGTCCTGTCTGCGGTTACGACGTGCCTGGCA
TTTGTCAAGCCTGCCATCAACAACATCTCTCTGATGACCCTGGGAGTTCCTTGCACTGCA
CTGCTCATCGCAGAGCTAAAGAGGTGTGACAACATGCGTGTGTTTAAGCTGGGCCTCTTC
TCGGGCCTCTGGTGGACCCTGGCCCTGTTCTGCTGGATCAGTGACCGAGCTTTCTGCGAG
CTGCTGTCATCCTTCAACTTCCCCTACCTGCACTGCATGTGGCACATCCTCATCTGCCTT
GCTGCCTACCTGGGCTGTGTATGCTTTGCCTACTTTGATGCTGCCTCAGAGATTCCTGAG
CAAGGCCCTGTCATCAAGTTCTGGCCCAATGAGAAATGGGCCTTCATTGGTGTCCCCTAT
GTGTCCCTCCTGTGTGCCAACAAGAAATCATCAGTCAAGACCACGTGA
|
| Enzyme 56 GenBank Gene ID |
AY312516  |
| Enzyme 56 GeneCard ID |
ACER2  |
| Enzyme 56 GenAtlas ID |
ACER2  |
| Enzyme 56 HGNC ID |
HGNC:23675  |
| Enzyme 56 Chromosome Location |
9 |
| Enzyme 56 Locus |
9p22.1 |
| Enzyme 56 SNPs |
SNPJam Report  |
| Enzyme 56 General References |
- Xu R, Jin J, Hu W, Sun W, Bielawski J, Szulc Z, Taha T, Obeid LM, Mao C: Golgi alkaline ceramidase regulates cell proliferation and survival by controlling levels of sphingosine and S1P. FASEB J. 2006 Sep;20(11):1813-25. [PubMed
]
- Wan D, Gong Y, Qin W, Zhang P, Li J, Wei L, Zhou X, Li H, Qiu X, Zhong F, He L, Yu J, Yao G, Jiang H, Qian L, Yu Y, Shu H, Chen X, Xu H, Guo M, Pan Z, Chen Y, Ge C, Yang S, Gu J: Large-scale cDNA transfection screening for genes related to cancer development and progression. Proc Natl Acad Sci U S A. 2004 Nov 2;101(44):15724-9. Epub 2004 Oct 21. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Sun W, Hu W, Xu R, Jin J, Szulc ZM, Zhang G, Galadari SH, Obeid LM, Mao C: Alkaline ceramidase 2 regulates beta1 integrin maturation and cell adhesion. FASEB J. 2009 Feb;23(2):656-66. Epub 2008 Oct 22. [PubMed
]
|
| Enzyme 56 Metabolite References |
Not Available |
|
Enzyme 57
[top]
|
| Enzyme 57 ID |
14920 |
| Enzyme 57 Name |
Alkaline ceramidase 2 |
| Enzyme 57 Synonyms |
- AlkCDase 2
- Alkaline CDase 2
- maCER2
- Acylsphingosine deacylase 3-like
- Cancer-related gene liver 1 protein
- CRG-L1
- N-acylsphingosine amidohydrolase 3-like
|
| Enzyme 57 Gene Name |
Acer2 |
| Enzyme 57 Protein Sequence |
>Alkaline ceramidase 2
MGAPHWWDHLRAGSSEVDWCEDNYTIVPAIAEFYNTISNVLFFILPPICMCLFRQYATCF
NSGIYLIWTLLVVVGIGSVYFHATLSFLGQMLDELAILWVLMCALAMWFPRRYLPKIFRN
DRGRFKAVVCVLSAITTCLAFIKPAINNISLMILGLPCTALLVAELKRCDNVRVFKLGLF
SGLWWTLALFCWISDQAFCELLSSFHFPYLHCVWHILICLASYLGCVCFAYFDAASEIPE
QGPVIRFWPSEKWAFIGVPYVSLLCAHKKSPVKIT
|
| Enzyme 57 Number of Residues |
275 |
| Enzyme 57 Molecular Weight |
31368.9 |
| Enzyme 57 Theoretical pI |
7.71 |
| Enzyme 57 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 metabolic process
- ceramide metabolic process
- lipid metabolic process
- membrane lipid metabolic process
- metabolic process
- primary metabolic process
- sphingoid metabolic process
- sphingolipid metabolic process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 57 General Function |
Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| Enzyme 57 Specific Function |
Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid. Regulates the maturation of integrin beta-1 (ITGB1) by controlling the generation of sphingosine in the Golgi complex. Inhibits cell adhesion by reducing the level of ITGB1 in the cell surface. May have a role in cell proliferation and apoptosis that seems to depend on the balance between sphingosine and sphingosine-1-phosphate |
| Enzyme 57 Pathways |
Not Available |
| Enzyme 57 Reactions |
- N-acylsphingosine + H2O = a carboxylate + sphingosine [RN:R01493]
|
| Enzyme 57 Pfam Domain Function |
|
| Enzyme 57 Signals |
|
| Enzyme 57 Transmembrane Regions |
- 33-53
63-83
87-107
128-143
144-164
174-194
212-232
|
| Enzyme 57 Essentiality |
Not Available |
| Enzyme 57 GenBank ID Protein |
17529684  |
| Enzyme 57 UniProtKB/Swiss-Prot ID |
Q8VD53  |
| Enzyme 57 UniProtKB/Swiss-Prot Entry Name |
ACER2_MOUSE  |
| Enzyme 57 PDB ID |
Not Available |
| Enzyme 57 Cellular Location |
Not Available |
| Enzyme 57 Gene Sequence |
>828 bp
ATGGGCGCCCCGCACTGGTGGGACCACCTGCGGGCTGGCAGTTCGGAGGTGGATTGGTGC
GAGGACAACTACACTATCGTGCCTGCCATTGCCGAGTTCTACAACACGATCAGCAACGTC
TTGTTTTTCATTTTACCTCCCATCTGCATGTGCTTGTTCCGCCAGTACGCAACGTGCTTC
AACAGCGGCATCTACTTAATATGGACGCTCCTAGTTGTAGTGGGGATTGGATCTGTCTAC
TTCCATGCAACGCTGAGTTTCCTGGGTCAGATGCTTGATGAACTTGCCATTCTGTGGGTT
CTGATGTGTGCTTTGGCCATGTGGTTTCCCAGGAGGTATTTACCAAAGATCTTTCGGAAT
GACAGGGGCAGGTTCAAGGCAGTGGTGTGTGTCCTGTCTGCAATTACAACGTGCTTGGCG
TTTATCAAGCCCGCCATCAACAATATTTCCCTGATGATTCTGGGACTTCCATGCACTGCG
CTGCTTGTTGCAGAGCTGAAGAGGTGTGACAATGTGCGTGTGTTTAAGCTGGGCCTCTTC
TCTGGCCTCTGGTGGACTCTGGCTCTCTTCTGCTGGATCAGCGACCAAGCCTTCTGTGAG
CTGCTCTCCTCCTTTCACTTCCCCTACCTGCACTGTGTGTGGCATATTCTCATCTGCCTT
GCTTCGTACCTGGGCTGTGTGTGCTTCGCCTACTTTGATGCTGCCTCAGAGATACCTGAG
CAAGGTCCAGTCATCAGATTCTGGCCCAGCGAGAAATGGGCTTTTATTGGTGTCCCTTAT
GTGTCCCTTCTGTGTGCCCACAAGAAGTCGCCAGTCAAGATCACGTGA
|
| Enzyme 57 GenBank Gene ID |
AF282864  |
| Enzyme 57 GeneCard ID |
Acer2  |
| Enzyme 57 GenAtlas ID |
Not Available |
| Enzyme 57 HGNC ID |
Not Available |
| Enzyme 57 Chromosome Location |
9 |
| Enzyme 57 Locus |
9p22.1 |
| Enzyme 57 SNPs |
SNPJam Report  |
| Enzyme 57 General References |
- Graveel CR, Jatkoe T, Madore SJ, Holt AL, Farnham PJ: Expression profiling and identification of novel genes in hepatocellular carcinomas. Oncogene. 2001 May 10;20(21):2704-12. [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
]
- Carninci P, Kasukawa T, Katayama S, Gough J, Frith MC, Maeda N, Oyama R, Ravasi T, Lenhard B, Wells C, Kodzius R, Shimokawa K, Bajic VB, Brenner SE, Batalov S, Forrest AR, Zavolan M, Davis MJ, Wilming LG, Aidinis V, Allen JE, Ambesi-Impiombato A, Apweiler R, Aturaliya RN, Bailey TL, Bansal M, Baxter L, Beisel KW, Bersano T, Bono H, Chalk AM, Chiu KP, Choudhary V, Christoffels A, Clutterbuck DR, Crowe ML, Dalla E, Dalrymple BP, de Bono B, Della Gatta G, di Bernardo D, Down T, Engstrom P, Fagiolini M, Faulkner G, Fletcher CF, Fukushima T, Furuno M, Futaki S, Gariboldi M, Georgii-Hemming P, Gingeras TR, Gojobori T, Green RE, Gustincich S, Harbers M, Hayashi Y, Hensch TK, Hirokawa N, Hill D, Huminiecki L, Iacono M, Ikeo K, Iwama A, Ishikawa T, Jakt M, Kanapin A, Katoh M, Kawasawa Y, Kelso J, Kitamura H, Kitano H, Kollias G, Krishnan SP, Kruger A, Kummerfeld SK, Kurochkin IV, Lareau LF, Lazarevic D, Lipovich L, Liu J, Liuni S, McWilliam S, Madan Babu M, Madera M, Marchionni L, Matsuda H, Matsuzawa S, Miki H, Mignone F, Miyake S, Morris K, Mottagui-Tabar S, Mulder N, Nakano N, Nakauchi H, Ng P, Nilsson R, Nishiguchi S, Nishikawa S, Nori F, Ohara O, Okazaki Y, Orlando V, Pang KC, Pavan WJ, Pavesi G, Pesole G, Petrovsky N, Piazza S, Reed J, Reid JF, Ring BZ, Ringwald M, Rost B, Ruan Y, Salzberg SL, Sandelin A, Schneider C, Schonbach C, Sekiguchi K, Semple CA, Seno S, Sessa L, Sheng Y, Shibata Y, Shimada H, Shimada K, Silva D, Sinclair B, Sperling S, Stupka E, Sugiura K, Sultana R, Takenaka Y, Taki K, Tammoja K, Tan SL, Tang S, Taylor MS, Tegner J, Teichmann SA, Ueda HR, van Nimwegen E, Verardo R, Wei CL, Yagi K, Yamanishi H, Zabarovsky E, Zhu S, Zimmer A, Hide W, Bult C, Grimmond SM, Teasdale RD, Liu ET, Brusic V, Quackenbush J, Wahlestedt C, Mattick JS, Hume DA, Kai C, Sasaki D, Tomaru Y, Fukuda S, Kanamori-Katayama M, Suzuki M, Aoki J, Arakawa T, Iida J, Imamura K, Itoh M, Kato T, Kawaji H, Kawagashira N, Kawashima T, Kojima M, Kondo S, Konno H, Nakano K, Ninomiya N, Nishio T, Okada M, Plessy C, Shibata K, Shiraki T, Suzuki S, Tagami M, Waki K, Watahiki A, Okamura-Oho Y, Suzuki H, Kawai J, Hayashizaki Y: The transcriptional landscape of the mammalian genome. Science. 2005 Sep 2;309(5740):1559-63. [PubMed
]
|
| Enzyme 57 Metabolite References |
Not Available |
|
Enzyme 58
[top]
|
| Enzyme 58 ID |
14921 |
| Enzyme 58 Name |
Neutral ceramidase |
| Enzyme 58 Synonyms |
- N-CDase
- NCDase
- Acylsphingosine deacylase 2
- BCDase
- LCDase
- hCD
- N-acylsphingosine amidohydrolase 2
- Non-lysosomal ceramidase
- Neutral ceramidase soluble form
|
| Enzyme 58 Gene Name |
ASAH2 |
| Enzyme 58 Protein Sequence |
>Neutral ceramidase
MAKRTFSNLETFLIFLLVMMSAITVALLSLLFITSGTIENHKDLGGHFFSTTQSPPATQG
STAAQRSTATQHSTATQSSTATQTSPVPLTPESPLFQNFSGYHIGVGRADCTGQVADINL
MGYGKSGQNAQGILTRLYSRAFIMAEPDGSNRTVFVSIDIGMVSQRLRLEVLNRLQSKYG
SLYRRDNVILSGTHTHSGPAGYFQYTVFVIASEGFSNQTFQHMVTGILKSIDIAHTNMKP
GKIFINKGNVDGVQINRSPYSYLQNPQSERARYSSNTDKEMIVLKMVDLNGDDLGLISWF
AIHPVSMNNSNHLVNSDNVGYASYLLEQEKNKGYLPGQGPFVAAFASSNLGDVSPNILGP
RCINTGESCDNANSTCPIGGPSMCIAKGPGQDMFDSTQIIGRAMYQRAKELYASASQEVT
GPLASAHQWVDMTDVTVWLNSTHASKTCKPALGYSFAAGTIDGVGGLNFTQGKTEGDPFW
DTIRDQILGKPSEEIKECHKPKPILLHTGELSKPHPWHPDIVDVQIITLGSLAITAIPGE
FTTMSGRRLREAVQAEFASHGMQNMTVVISGLCNVYTHYITTYEEYQAQRYEAASTIYGP
HTLSAYIQLFRNLAKAIATDTVANLSRGPEPPFFKQLIVPLIPSIVDRAPKGRTFGDVLQ
PAKPEYRVGEVAEVIFVGANPKNSVQNQTHQTFLTVEKYEATSTSWQIVCNDASWETRFY
WHKGLLGLSNATVEWHIPDTAQPGIYRIRYFGHNRKQDILKPAVILSFEGTSPAFEVVTI
|
| Enzyme 58 Number of Residues |
780 |
| Enzyme 58 Molecular Weight |
85515.2 |
| Enzyme 58 Theoretical pI |
7.24 |
| Enzyme 58 GO Classification |
Not Available |
| Enzyme 58 General Function |
Involved in ceramidase activity |
| Enzyme 58 Specific Function |
Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 6.5-8.5. Acts as a key regulator of sphingolipid signaling metabolites by generating sphingosine at the cell surface. Acts as a repressor of apoptosis both by reducing C16-ceramide, thereby preventing ceramide-induced apoptosis, and generating sphingosine, a precursor of the antiapoptotic factor sphingosine 1-phosphate. Probably involved in the digestion of dietary sphingolipids in intestine by acting as a key enzyme for the catabolism of dietary sphingolipids and regulating the levels of bioactive sphingolipid metabolites in the intestinal tract |
| Enzyme 58 Pathways |
Not Available |
| Enzyme 58 Reactions |
- N-acylsphingosine + H2O = a carboxylate + sphingosine [RN:R01493]
|
| Enzyme 58 Pfam Domain Function |
Not Available |
| Enzyme 58 Signals |
|
| Enzyme 58 Transmembrane Regions |
|
| Enzyme 58 Essentiality |
Not Available |
| Enzyme 58 GenBank ID Protein |
77862360  |
| Enzyme 58 UniProtKB/Swiss-Prot ID |
Q9NR71  |
| Enzyme 58 UniProtKB/Swiss-Prot Entry Name |
ASAH2_HUMAN  |
| Enzyme 58 PDB ID |
Not Available |
| Enzyme 58 Cellular Location |
Not Available |
| Enzyme 58 Gene Sequence |
>2343 bp
ATGGCCAAACGCACCTTCTCTAACTTGGAGACATTCCTGATTTTCCTCCTTGTAATGATG
AGTGCCATCACAGTGGCCCTTCTCAGCCTCTTGTTTATCACCAGTGGGACCATTGAAAAC
CACAAAGATTTAGGAGGCCATTTTTTTTCAACCACCCAAAGCCCTCCAGCCACCCAGGGC
TCCACAGCTGCCCAACGCTCCACAGCCACCCAGCATTCCACAGCCACCCAGAGCTCCACA
GCCACTCAAACTTCTCCAGTGCCTTTAACCCCAGAGTCTCCTCTATTTCAGAACTTCAGT
GGCTACCATATTGGTGTTGGACGAGCTGACTGCACAGGACAAGTAGCAGATATCAATTTG
ATGGGCTATGGCAAATCCGGCCAGAATGCACAGGGCATCCTCACCAGGCTATACAGTCGT
GCCTTCATCATGGCAGAACCTGATGGGTCCAATCGAACAGTGTTTGTCAGCATCGACATA
GGCATGGTATCACAAAGGCTCAGGCTGGAGGTCCTGAACAGACTGCAGAGTAAATATGGC
TCCCTGTACAGAAGAGATAATGTCATCCTGAGTGGCACTCACACTCATTCAGGTCCTGCA
GGATATTTCCAGTATACCGTGTTTGTAATTGCCAGTGAAGGATTTAGCAATCAAACTTTT
CAGCACATGGTCACTGGTATCTTGAAGAGCATTGACATAGCACACACAAATATGAAACCA
GGCAAAATCTTCATCAATAAAGGAAATGTGGATGGTGTGCAGATCAACAGAAGTCCGTAT
TCTTACCTTCAAAATCCGCAGTCAGAGAGAGCAAGGTATTCTTCAAATACAGACAAGGAA
ATGATAGTTTTGAAAATGGTAGATTTGAATGGAGATGACTTGGGCCTTATCAGCTGGTTT
GCCATCCACCCGGTCAGCATGAACAACAGTAACCATCTTGTAAACAGTGACAATGTGGGC
TATGCATCTTACCTGCTTGAGCAAGAGAAGAACAAAGGATATCTACCTGGACAGGGGCCA
TTTGTAGCAGCCTTTGCTTCATCAAACCTAGGAGATGTGTCCCCCAACATTCTTGGACCA
CGTTGCATCAACACAGGAGAGTCCTGTGATAACGCCAATAGCACTTGTCCCATTGGTGGG
CCTAGCATGTGCATTGCTAAGGGACCTGGACAGGATATGTTTGACAGCACACAAATTATA
GGACGGGCCATGTATCAGAGAGCAAAGGAACTCTATGCCTCTGCCTCCCAGGAGGTAACA
GGACCACTGGCTTCAGCACACCAGTGGGTGGATATGACAGATGTGACTGTCTGGCTCAAT
TCCACACATGCATCAAAAACATGTAAACCAGCATTGGGCTACAGTTTTGCGGCTGGCACT
ATTGATGGAGTTGGAGGCCTCAATTTTACACAGGGGAAAACAGAAGGGGATCCATTTTGG
GACACCATTCGGGACCAGATCCTGGGAAAGCCATCTGAAGAAATTAAAGAATGTCATAAA
CCAAAGCCCATCCTTCTTCACACCGGAGAACTATCAAAACCTCACCCCTGGCATCCAGAC
ATTGTTGATGTTCAGATTATTACCCTTGGGTCCTTGGCCATAACTGCCATCCCCGGGGAG
TTTACGACCATGTCTGGACGAAGACTTCGAGAGGCAGTTCAAGCAGAATTTGCATCTCAT
GGGATGCAGAACATGACTGTTGTTATTTCAGGTCTATGCAACGTCTATACACATTACATT
ACCACTTATGAAGAATACCAGGCTCAGCGATATGAGGCAGCATCGACAATTTATGGACCG
CACACATTATCTGCTTACATTCAGCTCTTCAGAAACCTTGCTAAGGCTATTGCTACGGAC
ACGGTAGCCAACCTGAGCAGAGGTCCAGAACCTCCCTTTTTCAAACAATTAATAGTTCCA
TTAATTCCTAGTATTGTGGATAGAGCACCAAAAGGCAGAACTTTCGGGGATGTCCTGCAG
CCAGCAAAACCTGAATACAGAGTGGGGGAAGTTGCTGAAGTTATATTTGTAGGTGCTAAC
CCGAAGAATTCAGTACAAAACCAGACCCATCAGACCTTCCTCACTGTGGAGAAATATGAG
GCTACTTCAACATCGTGGCAGATAGTGTGTAATGATGCCTCCTGGGAGACTCGTTTTTAT
TGGCACAAGGGACTCCTGGGTCTGAGTAATGCAACAGTGGAATGGCATATTCCAGACACT
GCCCAGCCTGGAATCTACAGAATAAGATATTTTGGACACAATCGGAAGCAGGACATTCTG
AAGCCTGCTGTCATACTTTCATTTGAAGGCACTTCCCCGGCTTTTGAAGTTGTAACTATT
TAG
|
| Enzyme 58 GenBank Gene ID |
AF449759  |
| Enzyme 58 GeneCard ID |
ASAH2  |
| Enzyme 58 GenAtlas ID |
ASAH2  |
| Enzyme 58 HGNC ID |
HGNC:18860  |
| Enzyme 58 Chromosome Location |
1 |
| Enzyme 58 Locus |
10q11.21 |
| Enzyme 58 SNPs |
SNPJam Report  |
| Enzyme 58 General References |
- Choi MS, Anderson MA, Zhang Z, Zimonjic DB, Popescu N, Mukherjee AB: Neutral ceramidase gene: role in regulating ceramide-induced apoptosis. Gene. 2003 Oct 2;315:113-22. [PubMed
]
- Osawa Y, Uchinami H, Bielawski J, Schwabe RF, Hannun YA, Brenner DA: Roles for C16-ceramide and sphingosine 1-phosphate in regulating hepatocyte apoptosis in response to tumor necrosis factor-alpha. J Biol Chem. 2005 Jul 29;280(30):27879-87. Epub 2005 Jun 9. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- El Bawab S, Roddy P, Qian T, Bielawska A, Lemasters JJ, Hannun YA: Molecular cloning and characterization of a human mitochondrial ceramidase. J Biol Chem. 2000 Jul 14;275(28):21508-13. [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
]
- Hwang YH, Tani M, Nakagawa T, Okino N, Ito M: Subcellular localization of human neutral ceramidase expressed in HEK293 cells. Biochem Biophys Res Commun. 2005 May 27;331(1):37-42. [PubMed
]
- Tani M, Sano T, Ito M, Igarashi Y: Mechanisms of sphingosine and sphingosine 1-phosphate generation in human platelets. J Lipid Res. 2005 Nov;46(11):2458-67. Epub 2005 Aug 1. [PubMed
]
- Galadari S, Wu BX, Mao C, Roddy P, El Bawab S, Hannun YA: Identification of a novel amidase motif in neutral ceramidase. Biochem J. 2006 Feb 1;393(Pt 3):687-95. [PubMed
]
- Avramopoulos D, Wang R, Valle D, Fallin MD, Bassett SS: A novel gene derived from a segmental duplication shows perturbed expression in Alzheimer's disease. Neurogenetics. 2007 Apr;8(2):111-20. Epub 2007 Feb 16. [PubMed
]
|
| Enzyme 58 Metabolite References |
Not Available |
|
Enzyme 59
[top]
|
| Enzyme 59 ID |
15234 |
| Enzyme 59 Name |
Acyl-CoA thioesterase 4 |
| Enzyme 59 Synonyms |
Not Available |
| Enzyme 59 Gene Name |
ACOT4 |
| Enzyme 59 Protein Sequence |
>Acyl-CoA thioesterase 4
MSATLILEPPGRCCWNEPVRIAVRGLAPEQRVTLRASLRDEKGALFRAHARYCADACGEL
DLERAPALGGSFAGLEPMGLLWALEPEKPFWRFLKRDVQIPFVVELEVLDGHDPEPGRLL
CQAQHERHFLPPGVRRQSVRAGRVRATLFLPPGPGPFPGIIDIFGIGGGLLEYRASLLAG
HGFATLALAYYNFEDLPNNMDNISLEYFEEAVCYMLQHPQVKGPGIGLLGISLGADICLS
MASFLKNVSATVSINGSGISGNTAINYKHSSIPPLGYDLRRIKVAFSGLVDIVDIRNALV
GGYKNPSMIPIEKAQGPILLIVGQDDHNWRSELYAQTVSERLQAHGKEKPQIICYPGTGH
YIEPPYFPLCPASLHRLLNKHVIWGGEPRAHSKAQEDAWKQILAFFCKHLGGTQKTAVPK
L
|
| Enzyme 59 Number of Residues |
421 |
| Enzyme 59 Molecular Weight |
46274 |
| Enzyme 59 Theoretical pI |
7.95 |
| Enzyme 59 GO Classification |
| Function |
- CoA hydrolase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- palmitoyl-CoA hydrolase activity
- thiolester hydrolase activity
|
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 59 General Function |
Not Available |
| Enzyme 59 Specific Function |
Not Available |
| Enzyme 59 Pathways |
Not Available |
| Enzyme 59 Reactions |
Not Available |
| Enzyme 59 Pfam Domain Function |
|
| Enzyme 59 Signals |
|
| Enzyme 59 Transmembrane Regions |
|
| Enzyme 59 Essentiality |
Not Available |
| Enzyme 59 GenBank ID Protein |
60551129  |
| Enzyme 59 UniProtKB/Swiss-Prot ID |
Q5BKT6  |
| Enzyme 59 UniProtKB/Swiss-Prot Entry Name |
Q5BKT6_HUMAN  |
| Enzyme 59 PDB ID |
Not Available |
| Enzyme 59 Cellular Location |
Not Available |
| Enzyme 59 Gene Sequence |
>1266 bp
ATGTCAGCAACGCTGATCCTGGAGCCCCCAGGCCGCTGCTGCTGGAACGAGCCGGTGCGC
ATTGCCGTGCGCGGCCTGGCCCCGGAGCAGCGGGTTACGCTGCGCGCGTCCCTGCGCGAC
GAGAAGGGCGCGCTCTTCCGGGCCCACGCGCGCTACTGCGCCGACGCCTGCGGCGAGCTG
GACCTGGAGCGCGCACCCGCGCTGGGCGGCAGCTTCGCGGGACTCGAGCCCATGGGGCTG
CTCTGGGCCCTGGAACCCGAGAAGCCTTTTTGGCGCTTCCTGAAGCGGGACGTACAGATT
CCTTTTGTCGTGGAGTTGGAGGTGCTGGACGGCCACGACCCCGAGCCTGGACGGCTGCTG
TGCCAGGCGCAGCACGAGCGCCACTTCCTCCCGCCAGGGGTGCGGCGCCAGTCGGTGCGA
GCGGGCCGGGTGCGCGCCACGCTCTTCCTGCCGCCAGGACCTGGACCCTTCCCAGGGATC
ATTGACATCTTTGGTATTGGAGGGGGCCTCTTGGAATATCGAGCCAGCCTCCTTGCTGGC
CATGGCTTTGCCACGTTGGCTCTAGCTTATTATAACTTTGAAGATCTCCCCAATAACATG
GACAACATATCCCTGGAGTACTTCGAAGAAGCCGTATGCTACATGCTTCAACATCCCCAG
GTAAAAGGCCCAGGCATTGGGCTTTTGGGCATTTCTCTAGGAGCTGATATTTGTCTCTCA
ATGGCCTCATTCTTGAAGAATGTCTCAGCCACAGTTTCCATCAATGGATCTGGGATCAGT
GGGAACACAGCCATCAACTATAAGCACAGTAGCATTCCACCATTGGGCTATGACCTGAGG
AGAATCAAGGTAGCTTTCTCAGGCCTCGTGGACATCGTGGATATAAGGAATGCTCTCGTA
GGAGGGTACAAGAACCCCAGCATGATTCCAATAGAGAAGGCCCAGGGGCCCATCCTGCTC
ATTGTTGGTCAGGATGACCATAACTGGAGAAGTGAGTTGTATGCCCAAACAGTCTCTGAA
CGGTTACAGGCCCATGGAAAGGAAAAACCCCAGATCATCTGTTACCCTGGGACTGGGCAT
TACATCGAGCCTCCTTACTTCCCCCTGTGCCCAGCTTCCCTTCACAGATTACTGAACAAA
CATGTTATATGGGGTGGGGAGCCCAGGGCTCATTCTAAGGCCCAGGAAGATGCCTGGAAG
CAAATTCTAGCCTTCTTCTGCAAACACCTGGGAGGTACCCAGAAAACAGCTGTCCCTAAA
TTGTAA
|
| Enzyme 59 GenBank Gene ID |
BC090945  |
| Enzyme 59 GeneCard ID |
Q5BKT6  |
| Enzyme 59 GenAtlas ID |
ACOT4  |
| Enzyme 59 HGNC ID |
HGNC:19748  |
| Enzyme 59 Chromosome Location |
14 |
| Enzyme 59 Locus |
14q24.3 |
| Enzyme 59 SNPs |
SNPJam Report  |
| Enzyme 59 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 59 Metabolite References |
Not Available |
|
Enzyme 60
[top]
|
| Enzyme 60 ID |
16056 |
| Enzyme 60 Name |
Carboxylesterase 7 |
| Enzyme 60 Synonyms |
- Carboxylesterase-like urinary excreted protein homolog
- Cauxin
|
| Enzyme 60 Gene Name |
CES7 |
| Enzyme 60 Protein Sequence |
>Carboxylesterase 7
MSGNWVHPGQILIWAIWVLAAPTKGPSAEGPQRNTRLGWIQGKQVTVLGSPVPVNVFLGV
PFAAPPLGSLRFTNPQPASPWDNLREATSYPNLCLQNSEWLLLDQHMLKVHYPKFGVSED
CLYLNIYAPAHADTGSKLPVLVWFPGGAFKTGSASIFDGSALAAYEDVLVVVVQYRLGIF
GFFTTWDQHAPGNWAFKDQVAALSWVQKNIEFFGGDPSSVTIFGESAGAISVSSLILSPM
AKGLFHKAIMESGVAIIPYLEAHDYEKSEDLQVVAHFCGNNASDSEALLRCLRTKPSKEL
LTLSQKTKSFTRVVDGAFFPNEPLDLLSQKAFKAIPSIIGVNNHECGFLLPMKEAPEILS
GSNKSLALHLIQNILHIPPQYLHLVANEYFHDKHSLTEIRDSLLDLLGDVFFVVPALITA
RYHRDAGAPVYFYEFRHRPQCFEDTKPAFVKADHADEVRFVFGGAFLKGDIVMFEGATEE
EKLLSRKMMKYWATFARTGNPNGNDLSLWPAYNLTEQYLQLDLNMSLGQRLKEPRVDFWT
STIPLILSASDMLHSPLSSLTFLSLLQPFFFFCAP
|
| Enzyme 60 Number of Residues |
575 |
| Enzyme 60 Molecular Weight |
63925.8 |
| Enzyme 60 Theoretical pI |
6.42 |
| Enzyme 60 GO Classification |
Not Available |
| Enzyme 60 General Function |
Lipid transport and metabolism |
| Enzyme 60 Specific Function |
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs |
| Enzyme 60 Pathways |
Not Available |
| Enzyme 60 Reactions |
- a carboxylic ester + H2O = an alcohol + a carboxylate [RN:R00630]
|
| Enzyme 60 Pfam Domain Function |
|
| Enzyme 60 Signals |
|
| Enzyme 60 Transmembrane Regions |
|
| Enzyme 60 Essentiality |
Not Available |
| Enzyme 60 GenBank ID Protein |
219521907  |
| Enzyme 60 UniProtKB/Swiss-Prot ID |
Q6NT32  |
| Enzyme 60 UniProtKB/Swiss-Prot Entry Name |
EST7_HUMAN  |
| Enzyme 60 PDB ID |
Not Available |
| Enzyme 60 Cellular Location |
Not Available |
| Enzyme 60 Gene Sequence |
>1728 bp
ATGAGTGGGAATTGGGTGCACCCAGGCCAGATCCTAATTTGGGCTATCTGGGTCCTTGCA
GCCCCCACCAAAGGGCCTTCTGCTGAAGGGCCACAGAGGAACACCAGGCTGGGATGGATT
CAGGGCAAGCAAGTCACTGTGCTGGGAAGCCCTGTGCCTGTGAACGTGTTCCTCGGAGTC
CCCTTTGCTGCTCCCCCGCTGGGATCCCTGCGATTTACGAACCCGCAGCCTGCATCGCCC
TGGGATAACTTGCGAGAAGCCACCTCCTACCCTAATTTGTGCCTCCAGAACTCAGAGTGG
CTGCTCTTAGATCAACATATGCTCAAGGTGCATTACCCGAAATTCGGAGTGTCAGAAGAC
TGCCTCTACCTGAACATCTATGCGCCTGCCCACGCCGATACAGGCTCCAAGCTCCCCGTC
TTGGTGTGGTTCCCAGGAGGTGCCTTCAAGACTGGCTCAGCCTCCATCTTTGATGGGTCC
GCCCTGGCTGCCTATGAGGACGTGCTGGTTGTGGTCGTCCAGTACCGGCTAGGAATATTT
GGTTTCTTCACCACATGGGATCAGCATGCTCCGGGGAACTGGGCCTTCAAGGACCAGGTG
GCTGCTCTGTCCTGGGTCCAGAAGAACATCGAGTTCTTCGGTGGGGACCCCAGCTCTGTG
ACCATCTTTGGCGAGTCCGCGGGAGCCATAAGTGTTTCTAGTCTTATACTGTCTCCCATG
GCCAAAGGCTTATTCCACAAAGCCATCATGGAGAGTGGGGTGGCCATCATCCCTTACCTG
GAGGCCCATGATTATGAGAAGAGTGAGGACCTGCAGGTGGTTGCACATTTCTGTGGTAAC
AATGCGTCAGACTCTGAGGCCCTGCTGAGGTGCCTGAGGACAAAACCCTCCAAGGAGCTG
CTGACCCTCAGCCAGAAAACAAAGTCTTTCACTCGAGTGGTTGATGGTGCTTTCTTTCCT
AATGAGCCTCTAGATCTATTGTCTCAGAAAGCATTTAAAGCAATTCCTTCCATCATCGGA
GTCAATAACCACGAGTGTGGCTTCCTGCTGCCTATGAAGGAGGCTCCTGAGATCCTCAGT
GGCTCCAACAAGTCCCTTGCCCTCCATCTGATACAAAACATCCTGCACATCCCGCCTCAG
TATTTGCACCTTGTGGCTAATGAATACTTCCATGACAAGCACTCCCTGACTGAAATCCGA
GACAGTCTTCTGGACTTGCTTGGAGATGTGTTCTTTGTGGTCCCTGCACTGATCACAGCT
CGATATCACAGAGATGCTGGTGCACCTGTCTACTTCTATGAGTTTCGGCACCGGCCTCAG
TGCTTTGAAGACACGAAGCCAGCTTTTGTCAAAGCCGACCACGCTGATGAAGTCCGCTTT
GTGTTCGGTGGTGCCTTCCTGAAGGGGGACATTGTTATGTTCGAAGGAGCCACGGAGGAG
GAGAAGTTACTGAGCCGGAAGATGATGAAATACTGGGCTACCTTTGCTCGAACCGGGAAT
CCTAATGGGAACGACCTGTCTCTGTGGCCAGCTTATAATCTGACTGAGCAGTACCTCCAG
CTGGACTTGAACATGAGCCTCGGACAGAGACTCAAAGAACCGCGGGTGGATTTTTGGACC
AGCACCATCCCCCTGATCCTGTCTGCCTCCGACATGCTCCACAGTCCTCTTTCTTCCTTA
ACTTTCCTCTCTCTCCTCCAGCCTTTCTTTTTCTTTTGTGCTCCTTGA
|
| Enzyme 60 GenBank Gene ID |
NM_001143685.1  |
| Enzyme 60 GeneCard ID |
CES7  |
| Enzyme 60 GenAtlas ID |
CES7  |
| Enzyme 60 HGNC ID |
HGNC:26459  |
| Enzyme 60 Chromosome Location |
1 |
| Enzyme 60 Locus |
16q12.2 |
| Enzyme 60 SNPs |
SNPJam Report  |
| Enzyme 60 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 60 Metabolite References |
Not Available |
|
Enzyme 61
[top]
|
| Enzyme 61 ID |
16867 |
| Enzyme 61 Name |
Alkaline ceramidase 1 |
| Enzyme 61 Synonyms |
- AlkCDase 1
- Alkaline CDase 1
- Acylsphingosine deacylase 3
- N-acylsphingosine amidohydrolase 3
|
| Enzyme 61 Gene Name |
ACER1 |
| Enzyme 61 Protein Sequence |
>Alkaline ceramidase 1
MPSIFAYQSSEVDWCESNFQYSELVAEFYNTFSNIPFFIFGPLMMLLMHPYAQKRSRYIY
VVWVLFMIIGLFSMYFHMTLSFLGQLLDEIAILWLLGSGYSIWMPRCYFPSFLGGNRSQF
IRLVFITTVVSTLLSFLRPTVNAYALNSIALHILYIVCQEYRKTSNKELRHLIEVSVVLW
AVALTSWISDRLLCSFWQRIHFFYLHSIWHVLISITFPYGMVTMALVDANYEMPGETLKV
RYWPRDSWPVGLPYVEIRGDDKDC
|
| Enzyme 61 Number of Residues |
264 |
| Enzyme 61 Molecular Weight |
31095.2 |
| Enzyme 61 Theoretical pI |
7.16 |
| Enzyme 61 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 metabolic process
- ceramide metabolic process
- lipid metabolic process
- membrane lipid metabolic process
- metabolic process
- primary metabolic process
- sphingoid metabolic process
- sphingolipid metabolic process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 61 General Function |
Involved in hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| Enzyme 61 Specific Function |
Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid at an optimal pH of 8.0. Has a highly restricted substrate specificity for the natural stereoisomer of ceramide with D-erythro-sphingosine but not D-ribo- phytosphingosine or D-erythro-dihydrosphingosine as a backbone. May have a role in regulating the levels of bioactive lipids ceramide and sphingosine 1-phosphate, as well as complex sphingolipids |
| Enzyme 61 Pathways |
Not Available |
| Enzyme 61 Reactions |
- N-acylsphingosine + H2O = a carboxylate + sphingosine [RN:R01493]
|
| Enzyme 61 Pfam Domain Function |
|
| Enzyme 61 Signals |
|
| Enzyme 61 Transmembrane Regions |
- 28-48
58-78
82-102
120-137
139-159
177-197
207-227
|
| Enzyme 61 Essentiality |
Not Available |
| Enzyme 61 GenBank ID Protein |
19070367  |
| Enzyme 61 UniProtKB/Swiss-Prot ID |
Q8TDN7  |
| Enzyme 61 UniProtKB/Swiss-Prot Entry Name |
ACER1_HUMAN  |
| Enzyme 61 PDB ID |
Not Available |
| Enzyme 61 Cellular Location |
Not Available |
| Enzyme 61 Gene Sequence |
>795 bp
ATGCCTAGCATCTTCGCCTATCAGAGCTCCGAGGTGGACTGGTGTGAGAGCAACTTCCAG
TACTCGGAGCTGGTGGCCGAGTTCTACAACACGTTCTCCAATATCCCCTTCTTCATCTTC
GGGCCACTGATGATGCTCCTGATGCACCCGTATGCCCAGAAGCGCTCCCGCTACATTTAC
GTTGTCTGGGTCCTCTTCATGATCATAGGCCTGTTCTCCATGTATTTCCACATGACGCTC
AGCTTCCTGGGCCAGCTGCTGGACGAGATCGCCATCCTGTGGCTCCTGGGCAGTGGCTAT
AGCATATGGATGCCCCGCTGCTATTTCCCCTCCTTCCTTGGGGGGAACAGGTCCCAGTTC
ATCCGCCTGGTCTTCATCACCACTGTGGTCAGCACCCTTCTGTCCTTCCTGCGGCCCACG
GTCAACGCCTACGCCCTCAACAGCATTGCCCTGCACATTCTCTACATCGTGTGCCAGGAG
TACAGGAAGACCAGCAATAAGGAGCTTCGGCACCTGATTGAGGTCTCCGTGGTTTTATGG
GCTGTTGCTCTGACCAGCTGGATCAGTGACCGTCTGCTTTGCAGCTTCTGGCAGAGGATT
CATTTCTTCTATCTGCACAGCATCTGGCATGTGCTCATCAGCATCACCTTCCCTTATGGC
ATGGTCACCATGGCCTTGGTGGATGCCAACTATGAGATGCCAGGTGAAACCCTCAAAGTC
CGCTACTGGCCTCGGGACAGTTGGCCCGTGGGGCTGCCCTACGTGGAAATCCGGGGTGAT
GACAAGGACTGCTGA
|
| Enzyme 61 GenBank Gene ID |
AF347024  |
| Enzyme 61 GeneCard ID |
ACER1  |
| Enzyme 61 GenAtlas ID |
ACER1  |
| Enzyme 61 HGNC ID |
HGNC:18356  |
| Enzyme 61 Chromosome Location |
1 |
| Enzyme 61 Locus |
19p13.3 |
| Enzyme 61 SNPs |
SNPJam Report  |
| Enzyme 61 General References |
- Mao C, Xu R, Szulc ZM, Bielawski J, Becker KP, Bielawska A, Galadari SH, Hu W, Obeid LM: Cloning and characterization of a mouse endoplasmic reticulum alkaline ceramidase: an enzyme that preferentially regulates metabolism of very long chain ceramides. J Biol Chem. 2003 Aug 15;278(33):31184-91. Epub 2003 Jun 3. [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
]
- Houben E, Holleran WM, Yaginuma T, Mao C, Obeid LM, Rogiers V, Takagi Y, Elias PM, Uchida Y: Differentiation-associated expression of ceramidase isoforms in cultured keratinocytes and epidermis. J Lipid Res. 2006 May;47(5):1063-70. Epub 2006 Feb 13. [PubMed
]
|
| Enzyme 61 Metabolite References |
Not Available |
|
Enzyme 62
[top]
|
| Enzyme 62 ID |
16935 |
| Enzyme 62 Name |
Neuropathy target esterase |
| Enzyme 62 Synonyms |
- Patatin-like phospholipase domain-containing protein 6
|
| Enzyme 62 Gene Name |
PNPLA6 |
| Enzyme 62 Protein Sequence |
>Neuropathy target esterase
MGTSSHGLATNSSGAKVAERDGFQDVLAPGEGSAGRICGAQPVPFVPQVLGVMIGAGVAV
VVTAVLILLVVRRLRVPKTPAPDGPRYRFRKRDKVLFYGRKIMRKVSQSTSSLVDTSVSA
TSRPRMRKKLKMLNIAKKILRIQKETPTLQRKEPPPAVLEADLTEGDLANSHLPSEVLYM
LKNVRVLGHFEKPLFLELCRHMVFQRLGQGDYVFRPGQPDASIYVVQDGLLELCLPGPDG
KECVVKEVVPGDSVNSLLSILDVITGHQHPQRTVSARAARDSTVLRLPVEAFSAVFTKYP
ESLVRVVQIIMVRLQRVTFLALHNYLGLTNELFSHEIQPLRLFPSPGLPTRTSPVRGSKR
MVSTSATDEPRETPGRPPDPTGAPLPGPTGDPVKPTSLETPSAPLLSRCVSMPGDISGLQ
GGPRSDFDMAYERGRISVSLQEEASGGSLAAPARTPTQEPREQPAGACEYSYCEDESATG
GCPFGPYQGRQTSSIFEAAKQELAKLMRIEDPSLLNSRVLLHHAKAGTIIARQGDQDVSL
HFVLWGCLHVYQRMIDKAEDVCLFVAQPGELVGQLAVLTGEPLIFTLRAQRDCTFLRISK
SDFYEIMRAQPSVVLSAAHTVAARMSPFVRQMDFAIDWTAVEAGRALYRQGDRSDCTYIV
LNGRLRSVIQRGSGKKELVGEYGRGDLIGVVEALTRQPRATTVHAVRDTELAKLPEGTLG
HIKRRYPQVVTRLIHLLSQKILGNLQQLQGPFPAGSGLGVPPHSELTNPASNLATVAILP
VCAEVPMVAFTLELQHALQAIGPTLLLNSDIIRARLGASALDSIQEFRLSGWLAQQEDAH
RIVLYQTDASLTPWTVRCLRQADCILIVGLGDQEPTLGQLEQMLENTAVRALKQLVLLHR
EEGAGPTRTVEWLNMRSWCSGHLHLRCPRRLFSRRSPAKLHELYEKVFSRRADRHSDFSR
LARVLTGNTIALVLGGGGARGCSHIGVLKALEEAGVPVDLVGGTSIGSFIGALYAEERSA
SRTKQRAREWAKSMTSVLEPVLDLTYPVTSMFTGSAFNRSIHRVFQDKQIEDLWLPYFNV
TTDITASAMRVHKDGSLWRYVRASMTLSGYLPPLCDPKDGHLLMDGGYINNLPADIARSM
GAKTVIAIDVGSQDETDLSTYGDSLSGWWLLWKRLNPWADKVKVPDMAEIQSRLAYVSCV
RQLEVVKSSSYCEYLRPPIDCFKTMDFGKFDQIYDVGYQYGKAVFGGWSRGNVIEKMLTD
RRSTDLNESRRADVLAFPSSGFTDLAEIVSRIEPPTSYVSDGCADGEESDCLTEYEEDAG
PDCSRDEGGSPEGASPSTASEMEEEKSILRQRRCLPQEPPGSATDA
|
| Enzyme 62 Number of Residues |
1366 |
| Enzyme 62 Molecular Weight |
149993.3 |
| Enzyme 62 Theoretical pI |
7.85 |
| Enzyme 62 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- lysophospholipase activity
|
| Process |
- glycerophospholipid metabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylcholine metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
- cell part
- endoplasmic reticulum membrane
- membrane
- organelle membrane
|
|
| Enzyme 62 General Function |
Involved in metabolic process |
| Enzyme 62 Specific Function |
Phospholipase B that deacylates intracellular phosphatidylcholine (PtdCho), generating glycerophosphocholine (GroPtdCho). This deacylation occurs at both sn-2 and sn-1 positions of PtdCho. Its specific chemical modification by certain organophosphorus (OP) compounds leads to distal axonopathy |
| Enzyme 62 Pathways |
Not Available |
| Enzyme 62 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 62 Pfam Domain Function |
|
| Enzyme 62 Signals |
|
| Enzyme 62 Transmembrane Regions |
|
| Enzyme 62 Essentiality |
Not Available |
| Enzyme 62 GenBank ID Protein |
116256487  |
| Enzyme 62 UniProtKB/Swiss-Prot ID |
Q8IY17  |
| Enzyme 62 UniProtKB/Swiss-Prot Entry Name |
PLPL6_HUMAN  |
| Enzyme 62 PDB ID |
Not Available |
| Enzyme 62 Cellular Location |
Not Available |
| Enzyme 62 Gene Sequence |
>3984 bp
ATGGAGGCTCCGCTGCAAACTGGAATGGTGCTTGGCGTGATGATCGGGGCCGGAGTGGCG
GTGGTGGTCACGGCCGTGCTCATCCTCCTGGTGGTGCGGAGGCTGCGAGTGCCAAAAACC
CCAGCCCCGGATGGCCCCCGGTATCGGTTCCGGAAGAGGGACAAAGTGCTCTTCTATGGC
CGGAAGATTATGCGGAAGGTGTCACAATCCACCTCCTCCCTCGTGGATACCTCTGTCTCC
GCCACCTCCCGGCCACGCATGAGGAAGAAACTGAAGATGCTCAACATTGCCAAGAAGATC
CTGCGCATCCAGAAAGAGACGCCCACGCTGCAGCGGAAGGAGCCCCCGCCCGCAGTGCTA
GAAGCTGACCTGACCGAGGGCGACCTGGCTAACTCCCATCTGCCCTCTGAAGTGCTTTAT
ATGCTCAAGAACGTCCGGGTGCTGGGCCACTTCGAGAAGCCACTCTTCCTGGAGCTCTGC
CGCCACATGGTCTTCCAGCGGCTGGGCCAGGGTGACTACGTCTTCCGGCCGGGCCAGCCA
GATGCCAGCATCTACGTGGTGCAGGACGGGCTGCTGGAGCTCTGTCTGCCAGGGCCTGAC
GGGAAGGAGTGTGTGGTGAAGGAAGTGGTTCCTGGGGACAGCGTCAACAGCCTTCTCAGC
ATCCTGGATGTCATCACCGGTCACCAGCATCCCCAGCGGACCGTGTCTGCCCGGGCGGCC
CGGGACTCCACGGTGCTGCGCCTGCCGGTGGAAGCATTCTCCGCGGTCTTCACCAAGTAC
CCGGAGAGCTTGGTGCGGGTCGTGCAGATCATCATGGTGCGGCTGCAGCGAGTCACCTTC
CTGGCACTGCACAACTACCTGGGTCTGACCAATGAGCTCTTCAGCCACGAGATCCAGCCC
CTGCGTCTGTTCCCCAGCCCCGGCCTCCCAACTCGCACCAGCCCTGTGCGGGGCTCCAAG
AGAATGGTCAGCACCTCAGCTACAGACGAGCCCAGGGAGACCCCAGGGCGGCCACCCGAT
CCCACCGGGGCCCCGCTGCCTGGACCTACAGGGGACCCTGTGAAGCCCACATCCCTGGAA
ACCCCCTCGGCCCCTCTGCTGAGCCGCTGCGTCTCCATGCCAGGGGACATCTCAGGCTTG
CAGGGTGGCCCCCGCTCCGACTTCGACATGGCCTATGAGCGTGGCCGGATCTCCGTGTCC
CTGCAGGAAGAGGCCTCCGGGGGGTCCCTGGCAGCCCCCGCTCGGACCCCCACTCAGGAG
CCTCGTGAGCAGCCGGCAGGCGCCTGTGAATACAGCTACTGTGAGGATGAGTCGGCCACT
GGTGGCTGCCCTTTCGGGCCCTACCAGGGCCGCCAGACCAGCAGCATCTTCGAGGCAGCA
AAGCAGGAGCTGGCCAAGCTGATGCGGATTGAGGACCCCTCCCTCCTGAACAGCAGAGTC
TTGCTGCACCACGCCAAAGCTGGCACCATCATTGCCCGCCAGGGAGACCAGGACGTGAGC
CTGCACTTCGTGCTCTGGGGCTGCCTGCACGTGTACCAGCGCATGATCGACAAGGCGGAG
GACGTGTGCCTGTTCGTAGCGCAGCCCGGGGAACTGGTGGGGCAGCTGGCGGTGCTCACT
GGCGAACCTCTCATCTTCACACTGCGAGCCCAACGCGACTGCACCTTCCTGCGGATCTCC
AAGTCCGACTTCTATGAGATCATGCGCGCACAGCCCAGTGTGGTGCTGAGTGCGGCGCAC
ACGGTGGCAGCCAGGATGTCGCCCTTCGTGCGCCAGATGGACTTCGCCATCGACTGGACT
GCAGTGGAGGCGGGACGCGCGCTGTACAGGCAGGGCGACCGCTCCGACTGCACTTACATC
GTGCTCAATGGGCGGCTGCGTAGCGTGATCCAGCGAGGCAGTGGCAAGAAGGAGCTGGTG
GGCGAGTACGGCCGCGGCGACCTCATCGGCGTGGTGGAGGCACTGACCCGGCAGCCGCGA
GCCACGACGGTGCACGCGGTGCGCGACACGGAGCTGGCCAAGCTTCCCGAGGGCACCTTG
GGTCACATCAAACGCCGGTACCCGCAGGTCGTGACCCGCCTTATCCACCTACTGAGCCAG
AAAATTCTAGGGAATTTGCAGCAGCTGCAAGGACCCTTCCCAGCAGGCTCTGGGTTGGGT
GTGCCCCCACACTCGGAACTCACCAACCCAGCCAGCAACCTGGCAACTGTGGCAATCCTG
CCTGTGTGTGCTGAGGTCCCCATGGTGGCCTTCACGCTGGAGCTGCAGCACGCCCTGCAG
GCCATCGGTCCGACGCTACTCCTTAACAGTGACATCATCCGGGCACGCCTGGGGGCCTCC
GCACTGGATAGCATCCAAGAGTTCCGGCTGTCAGGGTGGCTGGCCCAGCAGGAGGATGCA
CACCGTATCGTACTCTACCAGACGGACGCCTCGCTGACGCCCTGGACCGTGCGCTGCCTG
CGACAGGCCGACTGCATCCTCATTGTGGGCCTGGGGGACCAGGAGCCTACCCTCGGCCAG
CTGGAGCAGATGCTGGAGAACACGGCTGTGCGCGCCCTTAAGCAGCTAGTCCTGCTCCAC
CGAGAGGAGGGCGCGGGCCCCACGCGCACCGTGGAGTGGCTAAATATGCGCAGCTGGTGC
TCGGGGCACCTGCACCTGCGCTGTCCGCGCCGCCTCTTTTCGCGCCGCAGCCCTGCCAAG
CTGCATGAGCTCTACGAGAAGGTTTTCTCCAGGCGCGCGGACCGGCACAGCGACTTCTCC
CGCTTGGCGAGGGTGCTCACGGGGAACACCATTGCCCTTGTGCTAGGCGGGGGCGGGGCC
AGGGGCTGCTCGCACATCGGAGTACTAAAGGCATTAGAGGAGGCGGGGGTCCCCGTGGAC
CTGGTGGGCGGCACGTCCATTGGCTCTTTCATCGGAGCGTTGTACGCGGAGGAGCGCAGC
GCCAGCCGCACGAAGCAGCGGGCCCGGGAGTGGGCCAAGAGCATGACTTCGGTGCTGGAA
CCTGTGTTGGACCTCACGTACCCAGTCACCTCCATGTTCACTGGGTCTGCCTTTAACCGC
AGCATCCATCGGGTCTTCCAGGATAAGCAGATTGAGGACCTGTGGCTGCCTTACTTCAAC
GTGACCACAGATATCACCGCCTCAGCCATGCGAGTCCACAAAGATGGCTCCCTGTGGCGG
TACGTGCGCGCCAGCATGACGCTGTCGGGCTACCTGCCCCCGCTGTGCGACCCCAAGGAC
GGGCACCTACTCATGGATGGCGGCTACATCAACAATCTGCCAGCGGACATCGCCCGCAGC
ATGGGTGCCAAAACGGTCATCGCCATTGACGTGGGGAGCCAGGATGAGACGGACCTCAGC
ACCTACGGGGACAGCCTGTCCGGCTGGTGGCTGCTGTGGAAGCGGCTGAATCCCTGGGCT
GACAAGGTAAAGGTTCCAGACATGGCTGAAATCCAGTCCCGCCTGGCCTACGTGTCCTGT
GTGCGGCAGCTAGAGGTTGTCAAGTCCAGCTCCTACTGCGAGTACCTGCGCCCGCCCATC
GACTGCTTCAAGACCATGGACTTTGGGAAGTTCGACCAGATCTATGATGTGGGCTACCAG
TACGGGAAGGCGGTGTTTGGAGGCTGGAGCCGTGGCAACGTCATTGAGAAAATGCTCACA
GACCGGCGGTCTACAGACCTTAATGAGAGCCGCCGTGCAGACGTGCTTGCCTTCCCAAGC
TCTGGCTTCACTGACTTGGCAGAGATTGTGTCCCGGATTGAGCCCCCCACGAGCTATGTC
TCTGATGGCTGTGCTGACGGAGAGGAGTCAGATTGTCTGACAGAGTATGAGGAGGACGCC
GGACCCGACTGCTCGAGGGATGAAGGGGGGTCCCCCGAGGGCGCAAGCCCCAGCACTGCC
TCCGAGATGGAGGAGGAGAAGTCGATTCTCCGGCAACGACGCTGTCTGCCCCAGGAGCCG
CCCGGCTCAGCCACAGATGCCTGA
|
| Enzyme 62 GenBank Gene ID |
Not Available |
| Enzyme 62 GeneCard ID |
PNPLA6  |
| Enzyme 62 GenAtlas ID |
PNPLA6  |
| Enzyme 62 HGNC ID |
HGNC:16268  |
| Enzyme 62 Chromosome Location |
1 |
| Enzyme 62 Locus |
19p13.2 |
| Enzyme 62 SNPs |
SNPJam Report  |
| Enzyme 62 General References |
- Lush MJ, Li Y, Read DJ, Willis AC, Glynn P: Neuropathy target esterase and a homologous Drosophila neurodegeneration-associated mutant protein contain a novel domain conserved from bacteria to man. Biochem J. 1998 May 15;332 ( Pt 1):1-4. [PubMed
]
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Lotti M: The pathogenesis of organophosphate polyneuropathy. Crit Rev Toxicol. 1991;21(6):465-87. [PubMed
]
- Zaccheo O, Dinsdale D, Meacock PA, Glynn P: Neuropathy target esterase and its yeast homologue degrade phosphatidylcholine to glycerophosphocholine in living cells. J Biol Chem. 2004 Jun 4;279(23):24024-33. Epub 2004 Mar 25. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Rainier S, Bui M, Mark E, Thomas D, Tokarz D, Ming L, Delaney C, Richardson RJ, Albers JW, Matsunami N, Stevens J, Coon H, Leppert M, Fink JK: Neuropathy target esterase gene mutations cause motor neuron disease. Am J Hum Genet. 2008 Mar;82(3):780-5. Epub 2008 Feb 28. [PubMed
]
|
| Enzyme 62 Metabolite References |
Not Available |
|
Enzyme 63
[top]
|
| Enzyme 63 ID |
17240 |
| Enzyme 63 Name |
Pancreatic lipase-related protein 3 |
| Enzyme 63 Synonyms |
- PL-RP3
|
| Enzyme 63 Gene Name |
PNLIPRP3 |
| Enzyme 63 Protein Sequence |
>Pancreatic lipase-related protein 3
MLGIWIVAFLFFGTSRGKEVCYERLGCFKDGLPWTRTFSTELVGLPWSPEKINTRFLLYT
IHNPNAYQEISAVNSSTIQASYFGTDKITRINIAGWKTDGKWQRDMCNVLLQLEDINCIN
LDWINGSREYIHAVNNLRVVGAEVAYFIDVLMKKFEYSPSKVHLIGHSLGAHLAGEAGSR
IPGLGRITGLDPAGPFFHNTPKEVRLDPSDANFVDVIHTNAARILFELGVGTIDACGHLD
FYPNGGKHMPGCEDLITPLLKFNFNAYKKEMASFFDCNHARSYQFYAESILNPDAFIAYP
CRSYTSFKAGNCFFCSKEGCPTMGHFADRFHFKNMKTNGSHYFLNTGSLSPFARWRHKLS
VKLSGSEVTQGTVFLRVGGAVRKTGEFAIVSGKLEPGMTYTKLIDADVNVGNITSVQFIW
KKHLFEDSQNKLGAEMVINTSGKYGYKSTFCSQDIMGPNILQNLKPC
|
| Enzyme 63 Number of Residues |
467 |
| Enzyme 63 Molecular Weight |
52253.4 |
| Enzyme 63 Theoretical pI |
8.36 |
| Enzyme 63 GO Classification |
| Function |
- carboxylesterase activity
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- triglyceride lipase activity
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 63 General Function |
Involved in catalytic activity |
| Enzyme 63 Specific Function |
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate |
| Enzyme 63 Pathways |
Not Available |
| Enzyme 63 Reactions |
- triacylglycerol + H2O = diacylglycerol + a carboxylate [RN:R01369]
|
| Enzyme 63 Pfam Domain Function |
|
| Enzyme 63 Signals |
|
| Enzyme 63 Transmembrane Regions |
|
| Enzyme 63 Essentiality |
Not Available |
| Enzyme 63 GenBank ID Protein |
190341077  |
| Enzyme 63 UniProtKB/Swiss-Prot ID |
Q17RR3  |
| Enzyme 63 UniProtKB/Swiss-Prot Entry Name |
LIPR3_HUMAN  |
| Enzyme 63 PDB ID |
Not Available |
| Enzyme 63 Cellular Location |
Not Available |
| Enzyme 63 Gene Sequence |
>1404 bp
ATGCTTGGAATTTGGATTGTTGCATTCTTGTTCTTTGGCACATCAAGAGGAAAAGAAGTT
TGCTATGAAAGGTTAGGGTGTTTCAAAGATGGTTTACCATGGACCAGGACTTTCTCAACA
GAGTTGGTAGGTTTACCCTGGTCTCCAGAGAAGATAAACACTCGTTTCCTGCTCTACACT
ATACACAATCCCAATGCCTATCAGGAGATCAGTGCGGTTAATTCTTCAACTATCCAAGCC
TCATATTTTGGAACAGACAAGATCACCCGTATCAACATAGCTGGATGGAAAACAGATGGC
AAATGGCAGAGAGACATGTGCAATGTGTTGCTACAGCTGGAAGATATAAATTGCATTAAT
TTAGATTGGATCAACGGTTCACGGGAATACATCCATGCTGTAAACAATCTCCGTGTTGTT
GGTGCTGAGGTGGCTTATTTTATTGATGTTCTCATGAAAAAATTTGAATATTCCCCTTCT
AAAGTGCACTTGATTGGCCACAGCTTGGGAGCACACCTGGCTGGGGAAGCTGGGTCAAGG
ATACCAGGCCTTGGAAGAATAACTGGGTTGGACCCAGCTGGGCCATTTTTCCACAACACT
CCAAAGGAAGTCAGGCTAGACCCCTCGGATGCCAACTTTGTTGACGTTATTCATACAAAT
GCAGCTCGCATCCTCTTTGAGCTTGGTGTTGGAACCATTGATGCTTGTGGTCATCTTGAC
TTTTACCCAAATGGAGGGAAGCACATGCCAGGATGTGAAGACTTAATTACACCTTTACTG
AAATTTAACTTCAATGCTTACAAAAAAGAAATGGCTTCCTTCTTTGACTGTAACCATGCC
CGAAGTTATCAATTTTATGCTGAAAGCATTCTTAATCCTGATGCATTTATTGCTTATCCT
TGTAGATCCTACACATCTTTTAAAGCAGGAAATTGCTTCTTTTGTTCCAAAGAAGGTTGC
CCAACAATGGGTCATTTTGCTGATAGATTTCACTTCAAAAATATGAAGACTAATGGATCA
CATTATTTTTTAAACACAGGGTCCCTTTCCCCATTTGCCCGTTGGAGGCACAAATTGTCT
GTTAAACTCAGTGGAAGCGAAGTCACTCAAGGAACTGTCTTTCTTCGTGTAGGCGGGGCA
GTTAGGAAAACTGGGGAGTTTGCCATTGTCAGTGGAAAACTTGAGCCAGGCATGACTTAC
ACAAAATTAATCGATGCAGATGTTAACGTTGGAAACATTACAAGTGTTCAGTTCATCTGG
AAAAAACATTTGTTTGAAGATTCTCAGAATAAGTTGGGAGCAGAAATGGTGATAAATACA
TCTGGGAAATATGGATATAAATCTACCTTCTGTAGCCAAGACATTATGGGACCTAATATT
CTCCAGAACCTGAAACCATGCTAA
|
| Enzyme 63 GenBank Gene ID |
NM_001011709.2  |
| Enzyme 63 GeneCard ID |
PNLIPRP3  |
| Enzyme 63 GenAtlas ID |
PNLIPRP3  |
| Enzyme 63 HGNC ID |
HGNC:23492  |
| Enzyme 63 Chromosome Location |
1 |
| Enzyme 63 Locus |
10q25.3 |
| Enzyme 63 SNPs |
SNPJam Report  |
| Enzyme 63 General References |
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Saelee P, Wongkham S, Puapairoj A, Khuntikeo N, Petmitr S, Chariyalertsak S, Sumethchotimaytha W, Karalak A: Novel PNLIPRP3 and DOCK8 gene expression and prognostic implications of DNA loss on chromosome 10q25.3 in hepatocellular carcinoma. Asian Pac J Cancer Prev. 2009 Jul-Sep;10(3):501-6. [PubMed
]
|
| Enzyme 63 Metabolite References |
Not Available |
|
Enzyme 64
[top]
|
| Enzyme 64 ID |
17334 |
| Enzyme 64 Name |
Carnitine palmitoyltransferase 1B isoform a variant |
| Enzyme 64 Synonyms |
Not Available |
| Enzyme 64 Gene Name |
Not Available |
| Enzyme 64 Protein Sequence |
>Carnitine palmitoyltransferase 1B isoform a variant
MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPT
SWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTG
IFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPR
VSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEE
YIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALG
IVPMCSYQMERMFNTTRIPGNDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDL
EMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVA
LDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPI
IGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIKSSYQVAKAL
ADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREG
RTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCL
YLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGY
GVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS
|
| Enzyme 64 Number of Residues |
772 |
| Enzyme 64 Molecular Weight |
87785.4 |
| Enzyme 64 Theoretical pI |
8.85 |
| Enzyme 64 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 64 General Function |
Involved in acyltransferase activity |
| Enzyme 64 Specific Function |
Not Available |
| Enzyme 64 Pathways |
Not Available |
| Enzyme 64 Reactions |
Not Available |
| Enzyme 64 Pfam Domain Function |
|
| Enzyme 64 Signals |
|
| Enzyme 64 Transmembrane Regions |
|
| Enzyme 64 Essentiality |
Not Available |
| Enzyme 64 GenBank ID Protein |
62897909  |
| Enzyme 64 UniProtKB/Swiss-Prot ID |
Q53FV7  |
| Enzyme 64 UniProtKB/Swiss-Prot Entry Name |
Q53FV7_HUMAN  |
| Enzyme 64 PDB ID |
Not Available |
| Enzyme 64 Cellular Location |
Not Available |
| Enzyme 64 Gene Sequence |
>2319 bp
ATGGCGGAAGCTCACCAGGCCGTGGCCTTCCAGTTCACGGTGACCCCAGACGGGGTCGAC
TTCCGGCTCAGTCGGGAGGCCCTGAAACACGTCTACCTGTCTGGGATCAACTCCTGGAAG
AAACGCCTGATCCGCATCAAGAATGGCATCCTCAGGGGCGTGTACCCTGGCAGCCCCACC
AGCTGGCTGGTCGTCATCATGGCAACAGTGGGTTCCTCCTTCTGCAACGTGGACATCTCC
TTGGGGCTGGTCAGTTGCATCCAGAGATGCCTCCCTCAGGGGTGTGGCCCCTACCAGACC
CCGCAGACCCGGGCACTTCTCAGCATGGCCATCTTCTCCACGGGCGTCTGGGTGACGGGC
ATCTTCTTCTTCCGCCAAACCCTGAAGCTGCTTCTCTGCTACCATGGGTGGATGTTTGAG
ATGCATGGCAAGACCAGCAACTTGACCAGGATCTGGGCTATGTGTATCCGCCTTCTATCC
AGCCGGCACCCTATGCTCTACAGCTTCCAGACATCTCTGCCCAAGCTTCCTGTGCCCAGG
GTGTCAGCCACAATTCAGCGGTACCTAGAGTCTGTGCGCCCCTTGTTGGATGATGAGGAA
TATTACCGCATGGAGTTGCTGGCCAAAGAATTCCAGGACAAGACTGCCCCCAGGCTGCAG
AAATACCTGGTGCTCAAGTCATGGTGGGCAAGTAACTATGTGAGTGACTGGTGGGAAGAG
TACATCTACCTTCGAGGCAGGAGCCCTCTCATGGTGAACAGCAACTATTATGTCATGGAC
CTTGTGCTCATCAAGAATACAGACGTGCAGGCAGCCCGCCTGGGAAACATCATCCACGCC
ATGATCATGTATCGCCGTAAACTGGACCGTGAAGAAATCAAGCCTGTGATGGCACTGGGC
ATAGTGCCTATGTGCTCCTACCAGATGGAGAGGATGTTCAACACCACTCGGATCCCGGGC
AACGACACAGATGTGCTACAGCACCTCTCAGACAGCCGGCACGTGGCTGTCTACCACAAG
GGACGCTTCTTCAAGCTGTGGCTCTATGAGGGCGCCCGTCTGCTCAAGCCTCAGGATCTG
GAGATGCAGTTCCAGAGGATCCTGGACGACCCCTCCCCACCTCAGCCTGGGGAGGAGAAG
CTGGCAGCCCTCACTGCAGGAGGAAGGGTGGAGTGGGCGCAGGCACGCCAGGCCTTCTTT
AGCTCTGGAAAGAATAAGGCTGCCTTGGAGGCCATCGAGCGTGCCGCTTTCTTCGTGGCC
CTGGATGAGGAATCCTACTCCTATGACCCCGAAGATGAGGCCAGCCTCAGCCTCTATGGC
AAGGCCCTGCTACATGGCAACTGCTACAACAGGTGGTTTGACAAATCCTTCACTCTCATT
TCCTTCAAGAATGGCCAGTTGGGTCTCAATGCAGAGCATGCGTGGGCAGATGCTCCCATC
ATTGGGCACCTCTGGGAGTTTGTCCTGGGCACAGACAGCTTCCACCTGGGCTACACGGAG
ACCGGGCACTGCCTGGGCAAACCGAACCCTGCGCTCGCACCTCCTACACGGCTGCAGTGG
GACATTCCAAAACAGTGCCAGGCGGTCATCAAGAGTTCCTACCAGGTGGCCAAGGCGTTG
GCAGACGACGTGGAGTTGTACTGCTTCCAGTTCCTGCCCTTTGGCAAAGGCCTCATCAAG
AAGTGCCGGACCAGCCCTGATGCCTTTGTGCAGATCGCGCTGCAGCTGGCTCACTTCCGG
GACAGGGGTAAGTTCTGCCTGACCTATGAGGCCTCAATGACCAGAATGTTCCGGGAGGGA
CGGACTGAGACTGTGCGTTCCTGTACCAGCGAGTCCACAGCCTTTGTGCAGGCCATGATG
GAGGGGTCCCACACAAAAGCAGACCTGCGAGATCTCTTCCAGAAGGCTGCTAAGAAGCAC
CAGAATATGTACCGCCTGGCCATGACCGGGGCAGGGATCGACAGGCACCTCTTCTGCCTT
TACTTGGTCTCCAAGTACCTAGGAGTCAGCTCTCCTTTCCTTGCTGAGGTGCTCTCGGAA
CCCTGGCGTCTCTCCACCAGCCAGATCCCCCAATCCCAGATCCGCATGTTCGACCCAGAG
CAGCACCCCAATCACCTGGGCGCTGGAGGTGGCTTTGGCCCTGTAGCAGATGATGGCTAT
GGAGTTTCCTACATGATTGCAGGCGAGAACACGATCTTCTTCCACATCTCCAGCAAGTTC
TCAAGCTCAGAGACGAACGCCCAGCGCTTTGGAAACCACATCCGCAAAGCCCTGCTGGAC
ATTGCTGATCTTTTCCAAGTTCCCAAGGCCTACAGCTGA
|
| Enzyme 64 GenBank Gene ID |
AK223174  |
| Enzyme 64 GeneCard ID |
Not Available |
| Enzyme 64 GenAtlas ID |
Not Available |
| Enzyme 64 HGNC ID |
HGNC:2329  |
| Enzyme 64 Chromosome Location |
Not Available |
| Enzyme 64 Locus |
Not Available |
| Enzyme 64 SNPs |
Not Available |
| Enzyme 64 General References |
- Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed
]
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed
]
|
| Enzyme 64 Metabolite References |
Not Available |
|
Enzyme 65
[top]
|
| Enzyme 65 ID |
17335 |
| Enzyme 65 Name |
cDNA FLJ76296, highly similar to Homo sapiens carnitine palmitoyltransferase 1B (muscle) (CPT1B), transcript variant 1, mRNA |
| Enzyme 65 Synonyms |
Not Available |
| Enzyme 65 Gene Name |
Not Available |
| Enzyme 65 Protein Sequence |
>cDNA FLJ76296, highly similar to Homo sapiens carnitine palmitoyltransferase 1B (muscle) (CPT1B), transcript variant 1, mRNA
MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPT
SWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFPTGVWVTG
IFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPR
VSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEE
YIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALG
IVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDL
EMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVA
LDEESYCYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPI
IGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKAL
ADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREG
RTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCL
YLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGY
GVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS
|
| Enzyme 65 Number of Residues |
772 |
| Enzyme 65 Molecular Weight |
87826.5 |
| Enzyme 65 Theoretical pI |
8.72 |
| Enzyme 65 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 65 General Function |
Involved in acyltransferase activity |
| Enzyme 65 Specific Function |
Not Available |
| Enzyme 65 Pathways |
Not Available |
| Enzyme 65 Reactions |
Not Available |
| Enzyme 65 Pfam Domain Function |
|
| Enzyme 65 Signals |
|
| Enzyme 65 Transmembrane Regions |
|
| Enzyme 65 Essentiality |
Not Available |
| Enzyme 65 GenBank ID Protein |
158256068  |
| Enzyme 65 UniProtKB/Swiss-Prot ID |
A8K5K1  |
| Enzyme 65 UniProtKB/Swiss-Prot Entry Name |
A8K5K1_HUMAN  |
| Enzyme 65 PDB ID |
Not Available |
| Enzyme 65 Cellular Location |
Not Available |
| Enzyme 65 Gene Sequence |
>2319 bp
ATGGCGGAAGCTCACCAGGCCGTGGCCTTCCAGTTCACGGTGACCCCAGACGGGGTCGAC
TTCCGGCTCAGTCGGGAGGCCCTGAAACACGTCTACCTGTCTGGGATCAACTCCTGGAAG
AAACGCCTGATCCGCATCAAGAATGGCATCCTCAGGGGCGTGTACCCTGGCAGCCCCACC
AGCTGGCTGGTCGTCATCATGGCAACAGTGGGTTCCTCCTTCTGCAACGTGGACATCTCC
TTGGGGCTGGTCAGTTGCATCCAGAGATGCCTCCCTCAGGGGTGTGGCCCCTACCAGACC
CCGCAGACCCGGGCACTTCTCAGCATGGCCATCTTCCCCACGGGCGTCTGGGTGACGGGC
ATCTTCTTCTTCCGCCAAACCCTGAAGCTTCTTCTCTGCTACCATGGGTGGATGTTTGAG
ATGCATGGCAAGACCAGCAACTTGACCAGGATCTGGGCTATGTGTATCCGCCTTCTATCC
AGCCGGCACCCTATGCTCTACAGCTTCCAGACATCTCTGCCCAAGCTTCCTGTGCCCAGG
GTGTCAGCCACAATTCAGCGGTACCTAGAGTCTGTGCGCCCCTTGTTGGATGATGAGGAA
TATTACCGCATGGAGTTGCTGGCCAAAGAATTCCAGGACAAGACTGCCCCCAGGCTGCAG
AAATACCTGGTGCTCAAGTCATGGTGGGCAAGTAACTATGTGAGTGACTGGTGGGAAGAG
TACATCTACCTTCGAGGCAGGAGCCCTCTCATGGTGAACAGCAACTATTATGTCATGGAC
CTTGTGCTCATCAAGAATACAGACGTGCAGGCAGCCCGCCTGGGAAACATCATCCACGCC
ATGATCATGTATCGCCGTAAACTGGACCGTGAAGAAATCAAGCCTGTGATGGCACTGGGC
ATAGTGCCTATGTGCTCCTACCAGATGGAGAGGATGTTCAACACCACTCGGATCCCGGGC
AAGGACACAGATGTGCTACAGCACCTCTCAGACAGCCGGCACGTGGCTGTCTACCACAAG
GGACGCTTCTTCAAGCTGTGGCTCTATGAGGGCGCCCGTCTGCTCAAGCCTCAGGATCTG
GAGATGCAGTTCCAGAGGATCCTGGACGACCCCTCCCCACCTCAGCCTGGGGAGGAGAAG
CTGGCAGCCCTCACTGCAGGAGGAAGGGTGGAGTGGGCGCAGGCACGCCAGGCCTTCTTT
AGCTCTGGAAAGAATAAGGCTGCCTTGGAGGCCATCGAGCGTGCCGCTTTCTTCGTGGCC
CTGGATGAGGAATCCTACTGCTATGACCCCGAAGATGAGGCCAGCCTCAGCCTCTATGGC
AAGGCCCTGCTACATGGCAACTGCTACAACAGGTGGTTTGACAAATCCTTCACTCTCATT
TCCTTCAAGAATGGCCAGTTGGGTCTCAATGCAGAGCATGCGTGGGCAGATGCTCCCATC
ATTGGGCACCTCTGGGAGTTTGTCCTGGGCACAGACAGCTTCCACCTGGGCTACACGGAG
ACCGGGCACTGCCTGGGCAAACCGAACCCTGCGCTCGCACCTCCTACACGGCTGCAGTGG
GACATTCCAAAACAGTGCCAGGCGGTCATCGAGAGTTCCTACCAGGTGGCCAAGGCGTTG
GCAGACGACGTGGAGTTGTACTGCTTCCAGTTCCTGCCCTTTGGCAAAGGCCTCATCAAG
AAGTGCCGGACCAGCCCTGATGCCTTTGTGCAGATCGCGCTGCAGCTGGCTCACTTCCGG
GACAGGGGTAAGTTCTGCCTGACCTATGAGGCCTCAATGACCAGAATGTTCCGGGAGGGA
CGGACTGAGACTGTGCGTTCCTGTACCAGCGAGTCCACAGCCTTTGTGCAGGCCATGATG
GAGGGGTCCCACACAAAAGCAGACCTGCGAGATCTCTTCCAGAAGGCTGCTAAGAAGCAC
CAGAATATGTACCGCCTGGCCATGACCGGGGCAGGGATCGACAGGCACCTCTTCTGCCTT
TACTTGGTCTCCAAGTACCTAGGAGTCAGCTCTCCTTTCCTTGCTGAGGTGCTCTCGGAA
CCCTGGCGTCTCTCCACCAGCCAGATCCCCCAATCCCAGATCCGCATGTTCGACCCAGAG
CAGCACCCCAATCACCTGGGCGCTGGAGGTGGCTTTGGCCCTGTAGCAGATGATGGCTAT
GGAGTTTCCTACATGATTGCAGGCGAGAACACGATCTTCTTCCACATCTCCAGCAAGTTC
TCAAGCTCAGAGACGAACGCCCAGCGCTTTGGAAACCACATCCGCAAAGCCCTGCTGGAC
ATTGCTGATCTTTTCCAAGTTCCCAAGGCCTACAGCTGA
|
| Enzyme 65 GenBank Gene ID |
AK291316  |
| Enzyme 65 GeneCard ID |
Not Available |
| Enzyme 65 GenAtlas ID |
Not Available |
| Enzyme 65 HGNC ID |
HGNC:2329  |
| Enzyme 65 Chromosome Location |
Not Available |
| Enzyme 65 Locus |
Not Available |
| Enzyme 65 SNPs |
Not Available |
| Enzyme 65 General References |
Not Available |
| Enzyme 65 Metabolite References |
Not Available |
|
Enzyme 66
[top]
|
| Enzyme 66 ID |
17336 |
| Enzyme 66 Name |
Carboxylesterase 3 |
| Enzyme 66 Synonyms |
- Liver carboxylesterase 31 homolog
|
| Enzyme 66 Gene Name |
CES3 |
| Enzyme 66 Protein Sequence |
>Carboxylesterase 3
MERAVRVESGVLVGVVCLLLACPATATGPEVAQPEVDTTLGRVRGRQVGVKGTDRLVNVF
LGIPFAQPPLGPDRFSAPHPAQPWEGVRDASTAPPMCLQDVESMNSSRFVLNGKQQIFSV
SEDCLVLNVYSPAEVPAGSGRPVMVWVHGGALITGAATSYDGSALAAYGDVVVVTVQYRL
GVLGFFSTGDEHAPGNQGFLDVVAALRWVQENIAPFGGDLNCVTVFGGSAGGSIISGLVL
SPVAAGLFHRAITQSGVITTPGIIDSHPWPLAQKIANTLACSSSSPAEMVQCLQQKEGEE
LVLSKKLKNTIYPLTVDGTVFPKSPKELLKEKPFHSVPFLMGVNNHEFSWLIPRGWGLLD
TMEQMSREDMLAISTPVLTSLDVPPEMMPTVIDEYLGSNSDAQAKCQAFQEFMGDVFINV
PTVSFSRYLRDSGSPVFFYEFQHRPSSFAKIKPAWVKADHGAEGAFVFGGPFLMDESSRL
AFPEATEEEKQLSLTMMAQWTHFARTGDPNSKALPPWPQFNQAEQYLEINPVPRAGQKFR
EAWMQFWSETLPSKIQQWHQKQKNRKAQEDL
|
| Enzyme 66 Number of Residues |
571 |
| Enzyme 66 Molecular Weight |
62281.7 |
| Enzyme 66 Theoretical pI |
5.34 |
| Enzyme 66 GO Classification |
Not Available |
| Enzyme 66 General Function |
Lipid transport and metabolism |
| Enzyme 66 Specific Function |
Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs. Shows low catalytic efficiency for hydrolysis of CPT-11 (7-ethyl-10-[4-(1-piperidino)- 1-piperidino]-carbonyloxycamptothecin), a prodrug for camptothecin used in cancer therapeutics |
| Enzyme 66 Pathways |
Not Available |
| Enzyme 66 Reactions |
- a carboxylic ester + H2O = an alcohol + a carboxylate [RN:R00630]
|
| Enzyme 66 Pfam Domain Function |
|
| Enzyme 66 Signals |
|
| Enzyme 66 Transmembrane Regions |
|
| Enzyme 66 Essentiality |
Not Available |
| Enzyme 66 GenBank ID Protein |
37182340  |
| Enzyme 66 UniProtKB/Swiss-Prot ID |
Q6UWW8  |
| Enzyme 66 UniProtKB/Swiss-Prot Entry Name |
EST3_HUMAN  |
| Enzyme 66 PDB ID |
Not Available |
| Enzyme 66 Cellular Location |
Not Available |
| Enzyme 66 Gene Sequence |
>1716 bp
ATGGAGAGAGCAGTGAGAGTGGAGTCCGGGGTCCTGGTCGGGGTGGTCTGTCTGCTCCTG
GCATGCCCTGCCACAGCCACTGGGCCCGAAGTTGCTCAGCCTGAAGTAGACACCACCCTG
GGTCGTGTGCGAGGCCGGCAGGTGGGCGTGAAGGGCACAGACCGCCTTGTGAATGTCTTT
CTGGGCATTCCATTTGCCCAGCCGCCACTGGGCCCTGACCGGTTCTCAGCCCCACACCCA
GCACAGCCCTGGGAGGGTGTGCGGGATGCCAGCACTGCGCCCCCAATGTGCCTACAAGAC
GTGGAGAGCATGAACAGCAGCAGATTTGTCCTCAACGGAAAACAGCAGATCTTCTCCGTT
TCAGAGGACTGCCTGGTCCTCAACGTCTATAGCCCAGCTGAGGTCCCCGCAGGGTCCGGT
AGGCCGGTCATGGTATGGGTCCATGGAGGCGCTCTGATAACTGGCGCTGCCACCTCCTAC
GATGGATCAGCTCTGGCTGCCTATGGGGATGTGGTCGTGGTTACAGTCCAGTACCGCCTT
GGGGTCCTTGGCTTCTTCAGCACTGGAGATGAGCATGCACCTGGCAACCAGGGCTTCCTA
GATGTGGTAGCTGCTTTGCGCTGGGTGCAAGAAAACATCGCCCCCTTCGGGGGTGACCTC
AACTGTGTCACTGTCTTTGGTGGATCTGCCGGTGGGAGCATCATCTCTGGCCTGGTCCTG
TCCCCAGTGGCTGCAGGGCTGTTCCACAGAGCCATCACACAGAGTGGGGTCATCACCACC
CCAGGGATCATCGACTCTCACCCTTGGCCCCTAGCTCAGAAAATCGCAAACACCTTGGCC
TGCAGCTCCAGCTCCCCGGCTGAGATGGTGCAGTGCCTTCAGCAGAAAGAAGGAGAAGAG
CTGGTCCTTAGCAAGAAGCTGAAAAATACTATCTATCCTCTCACCGTTGATGGCACTGTC
TTCCCCAAAAGCCCCAAGGAACTCCTGAAGGAGAAGCCCTTCCACTCTGTGCCCTTCCTC
ATGGGTGTCAACAACCATGAGTTCAGCTGGCTCATCCCCAGGGGCTGGGGTCTCCTGGAT
ACAATGGAGCAGATGAGCCGGGAGGACATGCTGGCCATCTCAACACCCGTCTTGACCAGT
CTGGATGTGCCCCCTGAGATGATGCCCACCGTCATAGATGAATACCTAGGAAGCAACTCG
GACGCACAAGCCAAATGCCAGGCGTTCCAGGAATTCATGGGTGACGTATTCATCAATGTT
CCCACCGTCAGTTTTTCAAGATACCTTCGAGATTCTGGAAGCCCTGTCTTTTTCTATGAG
TTCCAGCATCGACCCAGTTCTTTTGCGAAGATCAAACCTGCCTGGGTGAAGGCTGATCAT
GGGGCCGAGGGTGCTTTTGTGTTCGGAGGTCCCTTCCTCATGGACGAGAGCTCCCGCCTG
GCCTTTCCAGAGGCCACAGAGGAGGAGAAGCAGCTAAGCCTCACCATGATGGCCCAGTGG
ACCCACTTTGCCCGGACAGGGGACCCCAATAGCAAGGCTCTGCCTCCTTGGCCCCAATTC
AACCAGGCGGAACAATATCTGGAGATCAACCCAGTGCCACGGGCCGGACAGAAGTTCAGG
GAGGCCTGGATGCAGTTCTGGTCAGAGACGCTCCCCAGCAAGATACAACAGTGGCACCAG
AAGCAGAAGAACAGGAAGGCCCAGGAGGACCTCTGA
|
| Enzyme 66 GenBank Gene ID |
AY358609  |
| Enzyme 66 GeneCard ID |
CES3  |
| Enzyme 66 GenAtlas ID |
CES3  |
| Enzyme 66 HGNC ID |
HGNC:1865  |
| Enzyme 66 Chromosome Location |
1 |
| Enzyme 66 Locus |
16q22.1 |
| Enzyme 66 SNPs |
SNPJam Report  |
| Enzyme 66 General References |
- Sanghani SP, Quinney SK, Fredenburg TB, Davis WI, Murry DJ, Bosron WF: Hydrolysis of irinotecan and its oxidative metabolites, 7-ethyl-10-[4-N-(5-aminopentanoic acid)-1-piperidino] carbonyloxycamptothecin and 7-ethyl-10-[4-(1-piperidino)-1-amino]-carbonyloxycamptothecin, by human carboxylesterases CES1A1, CES2, and a newly expressed carboxylesterase isoenzyme, CES3. Drug Metab Dispos. 2004 May;32(5):505-11. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Sanghani SP, Quinney SK, Fredenburg TB, Sun Z, Davis WI, Murry DJ, Cummings OW, Seitz DE, Bosron WF: Carboxylesterases expressed in human colon tumor tissue and their role in CPT-11 hydrolysis. Clin Cancer Res. 2003 Oct 15;9(13):4983-91. [PubMed
]
- Quinney SK, Sanghani SP, Davis WI, Hurley TD, Sun Z, Murry DJ, Bosron WF: Hydrolysis of capecitabine to 5'-deoxy-5-fluorocytidine by human carboxylesterases and inhibition by loperamide. J Pharmacol Exp Ther. 2005 Jun;313(3):1011-6. Epub 2005 Feb 1. [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 66 Metabolite References |
Not Available |
|
Enzyme 67
[top]
|
| Enzyme 67 ID |
17721 |
| Enzyme 67 Name |
Peroxisome proliferative acitvated receptor gamma |
| Enzyme 67 Synonyms |
Not Available |
| Enzyme 67 Gene Name |
PPARG |
| Enzyme 67 Protein Sequence |
>Peroxisome proliferative acitvated receptor gamma
MTMVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDP
VVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASG
FHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNEE
LQKDSY
|
| Enzyme 67 Number of Residues |
186 |
| Enzyme 67 Molecular Weight |
21580.3 |
| Enzyme 67 Theoretical pI |
6.91 |
| Enzyme 67 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- ligand-dependent nuclear receptor activity
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- receptor activity
- sequence-specific DNA binding
- sequence-specific DNA binding transcription factor activity
- signal transducer activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 67 General Function |
Involved in DNA binding |
| Enzyme 67 Specific Function |
Not Available |
| Enzyme 67 Pathways |
Not Available |
| Enzyme 67 Reactions |
Not Available |
| Enzyme 67 Pfam Domain Function |
|
| Enzyme 67 Signals |
|
| Enzyme 67 Transmembrane Regions |
|
| Enzyme 67 Essentiality |
Not Available |
| Enzyme 67 GenBank ID Protein |
86451955  |
| Enzyme 67 UniProtKB/Swiss-Prot ID |
Q0QJH8  |
| Enzyme 67 UniProtKB/Swiss-Prot Entry Name |
Q0QJH8_HUMAN  |
| Enzyme 67 PDB ID |
Not Available |
| Enzyme 67 Cellular Location |
Not Available |
| Enzyme 67 Gene Sequence |
>561 bp
ATGACCATGGTTGACACAGAGATGCCATTCTGGCCCACCAACTTTGGGATCAGCTCCGTG
GATCTCTCCGTAATGGAAGACCACTCCCACTCCTTTGATATCAAGCCCTTCACTACTGTT
GACTTCTCCAGCATTTCTACTCCACATTACGAAGACATTCCATTCACAAGAACAGATCCA
GTGGTTGCAGATTACAAGTATGACCTGAAACTTCAAGAGTACCAAAGTGCAATCAAAGTG
GAGCCTGCATCTCCACCTTATTATTCTGAGAAGACTCAGCTCTACAATAAGCCTCATGAA
GAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGTGTCTGTGGAGATAAAGCTTCTGGA
TTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAGGGTTTCTTCCGGAGAACAATCAGA
TTGAAGCTTATCTATGACAGATGTGATCTTAACTGTCGGATCCACAAAAAAAGTAGAAAT
AAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCAGTGGGGATGTCTCATAATGAGGAA
CTACAAAAGGATAGTTATTAG
|
| Enzyme 67 GenBank Gene ID |
DQ356894  |
| Enzyme 67 GeneCard ID |
PPARG  |
| Enzyme 67 GenAtlas ID |
PPARG  |
| Enzyme 67 HGNC ID |
HGNC:9236  |
| Enzyme 67 Chromosome Location |
3 |
| Enzyme 67 Locus |
3p25 |
| Enzyme 67 SNPs |
SNPJam Report  |
| Enzyme 67 General References |
- Kim HJ, Woo IS, Kang ES, Eun SY, Kim HJ, Lee JH, Chang KC, Kim JH, Seo HG: Identification of a truncated alternative splicing variant of human PPARgamma1 that exhibits dominant negative activity. Biochem Biophys Res Commun. 2006 Sep 1;347(3):698-706. Epub 2006 Jul 5. [PubMed
]
|
| Enzyme 67 Metabolite References |
Not Available |
|
Enzyme 68
[top]
|
| Enzyme 68 ID |
17722 |
| Enzyme 68 Name |
CREB3L2-PPARgamma |
| Enzyme 68 Synonyms |
Not Available |
| Enzyme 68 Gene Name |
Not Available |
| Enzyme 68 Protein Sequence |
>CREB3L2-PPARgamma
MEVLESGEQGVLQWDRKLSELSEPGDGEALMYHTHFSELLDEFSQNVLGQLLNDPFLSEK
SVSMEVEPSPTSPAPLIQAEHSYSLCEEPRAQSPFTHITTSDSFNDEMTMVDTEMPFWPT
NFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQE
YQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKG
FFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKL
LAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSPFVIYDMN
SLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEYAKSIPGFVNLDLND
QVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKPFGDFMEPKFEFAVK
FNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALELQLKLNHPESSQLFA
KLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
|
| Enzyme 68 Number of Residues |
584 |
| Enzyme 68 Molecular Weight |
66632.5 |
| Enzyme 68 Theoretical pI |
5.16 |
| Enzyme 68 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- ligand-dependent nuclear receptor activity
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- receptor activity
- sequence-specific DNA binding
- sequence-specific DNA binding transcription factor activity
- signal transducer activity
- steroid hormone receptor activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 68 General Function |
Involved in DNA binding |
| Enzyme 68 Specific Function |
Not Available |
| Enzyme 68 Pathways |
Not Available |
| Enzyme 68 Reactions |
Not Available |
| Enzyme 68 Pfam Domain Function |
|
| Enzyme 68 Signals |
|
| Enzyme 68 Transmembrane Regions |
|
| Enzyme 68 Essentiality |
Not Available |
| Enzyme 68 GenBank ID Protein |
29169314  |
| Enzyme 68 UniProtKB/Swiss-Prot ID |
Q86WD1  |
| Enzyme 68 UniProtKB/Swiss-Prot Entry Name |
Q86WD1_HUMAN  |
| Enzyme 68 PDB ID |
1I7I  |
| Enzyme 68 PDB File |
Show |
| Enzyme 68 3D Structure |
|
| Enzyme 68 Cellular Location |
Not Available |
| Enzyme 68 Gene Sequence |
>1755 bp
ATGGAGGTGCTGGAGAGCGGGGAGCAGGGCGTGCTGCAGTGGGACCGCAAGCTGAGCGAG
CTGTCAGAGCCCGGGGACGGCGAGGCCCTCATGTACCACACGCACTTCTCAGAACTTCTG
GATGAGTTTTCCCAGAACGTCTTGGGTCAGCTCCTGAATGATCCTTTCCTCTCAGAGAAG
AGTGTGTCAATGGAGGTGGAACCTTCCCCGACGTCCCCGGCGCCTCTCATCCAGGCTGAG
CACAGCTACTCCCTGTGCGAGGAGCCTCGGGCCCAGTCGCCCTTCACCCACATTACCACC
AGTGACAGCTTCAATGACGAAATGACCATGGTTGACACAGAGATGCCATTCTGGCCCACC
AACTTTGGGATCAGCTCCGTGGATCTCTCCGTAATGGAAGACCACTCCCACTCCTTTGAT
ATCAAGCCCTTCACTACTGTTGACTTCTCCAGCATTTCTACTCCACATTACGAAGACATT
CCATTCACAAGAACAGATCCAGTGGTTGCAGATTACAAGTATGACCTGAAACTTCAAGAG
TACCAAAGTGCAATCAAAGTGGAGCCTGCATCTCCACCTTATTATTCTGAGAAGACTCAG
CTCTACAATAAGCCTCATGAAGAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGTGTC
TGTGGAGATAAAGCTTCTGGATTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAGGGT
TTCTTCCGGAGAACAATCAGATTGAAGCTTATCTATGACAGATGTGATCTTAACTGTCGG
ATCCACAAAAAAAGTAGAAATAAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCAGTG
GGGATGTCTCATAATGCCATCAGGTTTGGGCGGATGCCACAGGCCGAGAAGGAGAAGCTG
TTGGCGGAGATCTCCAGTGATATCGACCAGCTGAATCCAGAGTCCGCTGACCTCCGGGCC
CTGGCAAAACATTTGTATGACTCATACATAAAGTCCTTCCCGCTGACCAAAGCAAAGGCG
AGGGCGATCTTGACAGGAAAGACAACAGACAAATCACCATTCGTTATCTATGACATGAAT
TCCTTAATGATGGGAGAAGATAAAATCAAGTTCAAACACATCACCCCCCTGCAGGAGCAG
AGCAAAGAGGTGGCCATCCGCATCTTTCAGGGCTGCCAGTTTCGCTCCGTGGAGGCTGTG
CAGGAGATCACAGAGTATGCCAAAAGCATTCCTGGTTTTGTAAATCTTGACTTGAACGAC
CAAGTAACTCTCCTCAAATATGGAGTCCACGAGATCATTTACACAATGCTGGCCTCCTTG
ATGAATAAAGATGGGGTTCTCATATCCGAGGGCCAAGGCTTCATGACAAGGGAGTTTCTA
AAGAGCCTGCGAAAGCCTTTTGGTGACTTTATGGAGCCCAAGTTTGAGTTTGCTGTGAAG
TTCAATGCACTGGAATTAGATGACAGCGACTTGGCAATATTTATTGCTGTCATTATTCTC
AGTGGAGACCGCCCAGGTTTGCTGAATGTGAAGCCCATTGAAGACATTCAAGACAACCTG
CTACAAGCCCTGGAGCTCCAGCTGAAGCTGAACCACCCTGAGTCCTCACAGCTGTTTGCC
AAGCTGCTCCAGAAAATGACAGACCTCAGACAGATTGTCACGGAACACGTGCAGCTACTG
CAGGTGATCAAGAAGACGGAGACAGACATGAGTCTTCACCCGCTCCTGCAGGAGATCTAC
AAGGACTTGTACTAG
|
| Enzyme 68 GenBank Gene ID |
AY222643  |
| Enzyme 68 GeneCard ID |
Not Available |
| Enzyme 68 GenAtlas ID |
Not Available |
| Enzyme 68 HGNC ID |
HGNC:9236  |
| Enzyme 68 Chromosome Location |
Not Available |
| Enzyme 68 Locus |
Not Available |
| Enzyme 68 SNPs |
Not Available |
| Enzyme 68 General References |
Not Available |
| Enzyme 68 Metabolite References |
Not Available |
|
Enzyme 69
[top]
|
| Enzyme 69 ID |
17723 |
| Enzyme 69 Name |
cDNA FLJ57380, highly similar to Adipophilin |
| Enzyme 69 Synonyms |
Not Available |
| Enzyme 69 Gene Name |
Not Available |
| Enzyme 69 Protein Sequence |
>cDNA FLJ57380, highly similar to Adipophilin
MSSAYLSTKDQYPYLKSVCEMAENGVKTITSVAMTSALPIIQKLEPQIAVANTYACKGLD
RIEERLPILNQPSTQIVANAKGAVTGAKDAVTTTVTGAKDSVASTITGVMDKTKGAVTGS
VEKTKSVVSGSINTVLGSRMMQLVSSGVENALTKSELLVEQYLPLTEEELEKEAKKVEGF
DLVQKPSYYVRLGSLSTKLHSRAYQQALSRVKEAKQKSQQTISQLHSTVHLIEFARKNVY
SANQKIQDAQDKLYLSWVEWKRSIGYDDTDESHCAEHIESRTLAIARNLTQQLQTTCHTL
LSNIQGVPQNIQDQAKHMGVMAGDIYSVFRNAASFKEVSDSLLTSSKGQLQKMKESLDDV
MDYLVNNTPLNWLVGPFYPQLTESQNAQDQGAEMDKSSQETQRSEHKTH
|
| Enzyme 69 Number of Residues |
409 |
| Enzyme 69 Molecular Weight |
45134.7 |
| Enzyme 69 Theoretical pI |
7.01 |
| Enzyme 69 GO Classification |
Not Available |
| Enzyme 69 General Function |
Not Available |
| Enzyme 69 Specific Function |
Not Available |
| Enzyme 69 Pathways |
Not Available |
| Enzyme 69 Reactions |
Not Available |
| Enzyme 69 Pfam Domain Function |
|
| Enzyme 69 Signals |
|
| Enzyme 69 Transmembrane Regions |
|
| Enzyme 69 Essentiality |
Not Available |
| Enzyme 69 GenBank ID Protein |
194382232  |
| Enzyme 69 UniProtKB/Swiss-Prot ID |
B4DJK9  |
| Enzyme 69 UniProtKB/Swiss-Prot Entry Name |
B4DJK9_HUMAN  |
| Enzyme 69 PDB ID |
Not Available |
| Enzyme 69 Cellular Location |
Not Available |
| Enzyme 69 Gene Sequence |
>1230 bp
ATGTCCTCAGCCTATCTCAGTACAAAGGACCAGTATCCCTACCTGAAGTCTGTGTGTGAG
ATGGCAGAGAACGGTGTGAAGACCATCACCTCCGTGGCCATGACCAGTGCTCTGCCCATC
ATCCAGAAGCTAGAGCCGCAAATTGCAGTTGCCAATACCTATGCCTGTAAGGGGCTAGAC
AGGATTGAGGAGAGACTGCCTATTCTGAATCAGCCATCAACTCAGATTGTTGCCAATGCC
AAAGGCGCTGTGACTGGGGCAAAAGATGCTGTGACGACTACTGTGACTGGGGCCAAGGAT
TCTGTGGCCAGCACGATCACAGGGGTGATGGACAAGACCAAAGGGGCAGTGACTGGCAGT
GTGGAGAAGACCAAGTCTGTGGTCAGTGGCAGCATTAACACAGTCTTGGGGAGTCGGATG
ATGCAGCTCGTGAGCAGTGGCGTAGAAAATGCACTCACCAAATCAGAGCTGTTGGTAGAA
CAGTACCTCCCTCTCACTGAGGAAGAACTAGAAAAAGAAGCAAAAAAAGTTGAAGGATTT
GATCTGGTTCAGAAGCCAAGTTATTATGTTAGACTGGGATCCCTGTCTACCAAGCTTCAC
TCCCGTGCCTACCAGCAGGCTCTCAGCAGGGTTAAAGAAGCTAAGCAAAAAAGCCAACAG
ACCATTTCTCAGCTCCATTCTACTGTTCACCTGATTGAATTTGCCAGGAAGAATGTGTAT
AGTGCCAATCAGAAAATTCAGGATGCTCAGGATAAGCTCTACCTCTCATGGGTAGAGTGG
AAAAGGAGCATTGGATATGATGATACTGATGAGTCCCACTGTGCTGAGCACATTGAGTCA
CGTACTCTTGCAATTGCCCGCAACCTGACTCAGCAGCTCCAGACCACGTGCCACACCCTC
CTGTCCAACATCCAAGGTGTACCACAGAACATCCAAGATCAAGCCAAGCACATGGGGGTG
ATGGCAGGCGACATCTACTCAGTGTTCCGCAATGCTGCCTCCTTTAAAGAAGTGTCTGAC
AGCCTCCTCACTTCTAGCAAGGGGCAGCTGCAGAAAATGAAGGAATCTTTAGATGACGTG
ATGGATTATCTTGTTAACAACACGCCCCTCAACTGGCTGGTAGGTCCCTTTTATCCTCAG
CTGACTGAGTCTCAGAATGCTCAGGACCAAGGTGCAGAGATGGACAAGAGCAGCCAGGAG
ACCCAGCGATCTGAGCATAAAACTCATTAA
|
| Enzyme 69 GenBank Gene ID |
AK296125  |
| Enzyme 69 GeneCard ID |
Not Available |
| Enzyme 69 GenAtlas ID |
Not Available |
| Enzyme 69 HGNC ID |
HGNC:248  |
| Enzyme 69 Chromosome Location |
Not Available |
| Enzyme 69 Locus |
Not Available |
| Enzyme 69 SNPs |
Not Available |
| Enzyme 69 General References |
Not Available |
| Enzyme 69 Metabolite References |
Not Available |
|
Enzyme 70
[top]
|
| Enzyme 70 ID |
17724 |
| Enzyme 70 Name |
Adipose differentiation-related protein |
| Enzyme 70 Synonyms |
Not Available |
| Enzyme 70 Gene Name |
ADFP |
| Enzyme 70 Protein Sequence |
>Adipose differentiation-related protein
MASVAVDPQPSVVTRVVNLPLVSSTYDLMSSAYLSTKDQYPYLKSVCEMAENGVKTITSV
AMTSALPIIQKLEPQIAVANTYACKGLDRIEERLPILNQPSTQIVANAKGAVTGAKDAVT
TTVTG
|
| Enzyme 70 Number of Residues |
125 |
| Enzyme 70 Molecular Weight |
13231.1 |
| Enzyme 70 Theoretical pI |
6.54 |
| Enzyme 70 GO Classification |
Not Available |
| Enzyme 70 General Function |
Involved in protein binding |
| Enzyme 70 Specific Function |
Not Available |
| Enzyme 70 Pathways |
Not Available |
| Enzyme 70 Reactions |
Not Available |
| Enzyme 70 Pfam Domain Function |
|
| Enzyme 70 Signals |
|
| Enzyme 70 Transmembrane Regions |
|
| Enzyme 70 Essentiality |
Not Available |
| Enzyme 70 GenBank ID Protein |
55960890  |
| Enzyme 70 UniProtKB/Swiss-Prot ID |
Q5SYF5  |
| Enzyme 70 UniProtKB/Swiss-Prot Entry Name |
Q5SYF5_HUMAN  |
| Enzyme 70 PDB ID |
Not Available |
| Enzyme 70 Cellular Location |
Not Available |
| Enzyme 70 Gene Sequence |
Not Available |
| Enzyme 70 GenBank Gene ID |
AL591206  |
| Enzyme 70 GeneCard ID |
ADFP  |
| Enzyme 70 GenAtlas ID |
Not Available |
| Enzyme 70 HGNC ID |
HGNC:248  |
| Enzyme 70 Chromosome Location |
9 |
| Enzyme 70 Locus |
9p22.1 |
| Enzyme 70 SNPs |
SNPJam Report  |
| Enzyme 70 General References |
Not Available |
| Enzyme 70 Metabolite References |
Not Available |
|
Enzyme 71
[top]
|
| Enzyme 71 ID |
17725 |
| Enzyme 71 Name |
ADFP protein |
| Enzyme 71 Synonyms |
- SubName: Adipose differentiation-related protein
- SubName: Adipose differentiation-related protein, isoform CRA_b
- SubName: cDNA, FLJ93444, highly similar to Homo sapiens adipose differentiation-related protein (ADFP), mRNA
|
| Enzyme 71 Gene Name |
ADFP |
| Enzyme 71 Protein Sequence |
>ADFP protein
MASVAVDPQPSVVTRVVNLPLVSSTYDLMSSAYLSTKDQYPYLKSVCEMAENGVKTITSV
AMTSALPIIQKLEPQIAVANTYACKGLDRIEERLPILNQPSTQIVANAKGAVTGAKDAVT
TTVTGAKDSVASTITGVMDKTKGAVTGSVEKTKSVVSGSINTVLGSRMMQLVSSGVENAL
TKSELLVEQYLPLTEEELEKEAKKVEGFDLVQKPSYYVRLGSLSTKLHSRAYQQALSRVK
EAKQKSQQTISQLHSTVHLIEFARKNVYSANQKIQDAQDKLYLSWVEWKRSIGYDDTDES
HCAEHIESRTLAIARNLTQQLQTTCHTLLSNIQGVPQNIQDQAKHMGVMAGDIYSVFRNA
ASFKEVSDSLLTSSKGQLQKMKESLDDVMDYLVNNTPLNWLVGPFYPQLTESQNAQDQGA
EMDKSSQETQRSEHKTH
|
| Enzyme 71 Number of Residues |
437 |
| Enzyme 71 Molecular Weight |
48075.1 |
| Enzyme 71 Theoretical pI |
6.80 |
| Enzyme 71 GO Classification |
Not Available |
| Enzyme 71 General Function |
Not Available |
| Enzyme 71 Specific Function |
Not Available |
| Enzyme 71 Pathways |
Not Available |
| Enzyme 71 Reactions |
Not Available |
| Enzyme 71 Pfam Domain Function |
|
| Enzyme 71 Signals |
|
| Enzyme 71 Transmembrane Regions |
|
| Enzyme 71 Essentiality |
Not Available |
| Enzyme 71 GenBank ID Protein |
189066570  |
| Enzyme 71 UniProtKB/Swiss-Prot ID |
Q6FHZ7  |
| Enzyme 71 UniProtKB/Swiss-Prot Entry Name |
Q6FHZ7_HUMAN  |
| Enzyme 71 PDB ID |
Not Available |
| Enzyme 71 Cellular Location |
Not Available |
| Enzyme 71 Gene Sequence |
>1314 bp
ATGGCATCCGTTGCAGTTGATCCACAACCGAGTGTGGTGACTCGGGTGGTCAACCTGCCC
TTGGTGAGCTCCACGTATGACCTCATGTCCTCAGCCTATCTCAGTACAAAGGACCAGTAT
CCCTACCTGAAGTCTGTGTGTGAGATGGCAGAGAACGGTGTGAAGACCATCACCTCCGTG
GCCATGACCAGTGCTCTGCCCATCATCCAGAAGCTAGAGCCGCAAATTGCAGTTGCCAAT
ACCTATGCCTGTAAGGGGCTAGACAGGATTGAGGAGAGACTGCCTATTCTGAATCAGCCA
TCAACTCAGATTGTTGCCAATGCCAAAGGCGCTGTGACTGGGGCAAAAGATGCTGTGACG
ACTACTGTGACTGGGGCCAAGGATTCTGTGGCCAGCACGATCACAGGGGTGATGGACAAG
ACCAAAGGGGCAGTGACTGGCAGTGTGGAGAAGACCAAGTCTGTGGTCAGTGGCAGCATT
AACACAGTCTTGGGGAGTCGGATGATGCAGCTCGTGAGCAGTGGCGTAGAAAATGCACTC
ACCAAATCAGAGCTGTTGGTAGAACAGTACCTCCCTCTCACTGAGGAAGAACTAGAAAAA
GAAGCAAAAAAAGTTGAAGGATTTGATCTGGTTCAGAAGCCAAGTTATTATGTTAGACTG
GGATCCCTGTCTACCAAGCTTCACTCCCGTGCCTACCAGCAGGCTCTCAGCAGGGTTAAA
GAAGCTAAGCAAAAAAGCCAACAGACCATTTCTCAGCTCCATTCTACTGTTCACCTGATT
GAATTTGCCAGGAAGAATGTGTATAGTGCCAATCAGAAAATTCAGGATGCTCAGGATAAG
CTCTACCTCTCATGGGTAGAGTGGAAAAGGAGCATTGGATATGATGATACTGATGAGTCC
CACTGTGCTGAGCACATTGAGTCACGTACTCTTGCAATTGCCCGCAACCTGACTCAGCAG
CTCCAGACCACGTGCCACACCCTCCTGTCCAACATCCAAGGTGTACCACAGAACATCCAA
GATCAAGCCAAGCACATGGGGGTGATGGCAGGCGACATCTACTCAGTGTTCCGCAATGCT
GCCTCCTTTAAAGAAGTGTCTGACAGCCTCCTCACTTCTAGCAAGGGGCAGCTGCAGAAA
ATGAAGGAATCTTTAGATGACGTGATGGATTATCTTGTTAACAACACGCCCCTCAACTGG
CTGGTAGGTCCCTTTTATCCTCAGCTGACTGAGTCTCAGAATGCTCAGGACCAAGGTGCA
GAGATGGACAAGAGCAGCCAGGAGACCCAGCGATCTGAGCATAAAACTCATTAA
|
| Enzyme 71 GenBank Gene ID |
AK312983  |
| Enzyme 71 GeneCard ID |
ADFP  |
| Enzyme 71 GenAtlas ID |
ADFP  |
| Enzyme 71 HGNC ID |
HGNC:248  |
| Enzyme 71 Chromosome Location |
Not Available |
| Enzyme 71 Locus |
Not Available |
| Enzyme 71 SNPs |
SNPJam Report  |
| Enzyme 71 General References |
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 71 Metabolite References |
Not Available |
|
Enzyme 72
[top]
|
| Enzyme 72 ID |
17726 |
| Enzyme 72 Name |
Peroxisome proliferator activated-receptor gamma |
| Enzyme 72 Synonyms |
Not Available |
| Enzyme 72 Gene Name |
ppar gamma2 |
| Enzyme 72 Protein Sequence |
>Peroxisome proliferator activated-receptor gamma
MGETLGDSPIDPESDSFTDTLSANISQ
|
| Enzyme 72 Number of Residues |
27 |
| Enzyme 72 Molecular Weight |
2827.9 |
| Enzyme 72 Theoretical pI |
3.12 |
| Enzyme 72 GO Classification |
Not Available |
| Enzyme 72 General Function |
Involved in receptor activity |
| Enzyme 72 Specific Function |
Not Available |
| Enzyme 72 Pathways |
Not Available |
| Enzyme 72 Reactions |
Not Available |
| Enzyme 72 Pfam Domain Function |
Not Available |
| Enzyme 72 Signals |
|
| Enzyme 72 Transmembrane Regions |
|
| Enzyme 72 Essentiality |
Not Available |
| Enzyme 72 GenBank ID Protein |
2605489  |
| Enzyme 72 UniProtKB/Swiss-Prot ID |
Q9UEF6  |
| Enzyme 72 UniProtKB/Swiss-Prot Entry Name |
Q9UEF6_HUMAN  |
| Enzyme 72 PDB ID |
Not Available |
| Enzyme 72 Cellular Location |
Not Available |
| Enzyme 72 Gene Sequence |
>82 bp
ATGGGTGAAACTCTGGGAGATTCTCCTATTGACCCAGAAAGCGATTCCTTCACTGATACA
CTGTCTGCAAACATATCACAAG
|
| Enzyme 72 GenBank Gene ID |
AB005520  |
| Enzyme 72 GeneCard ID |
ppar gamma2  |
| Enzyme 72 GenAtlas ID |
ppar+gamma2  |
| Enzyme 72 HGNC ID |
HGNC:9236  |
| Enzyme 72 Chromosome Location |
Not Available |
| Enzyme 72 Locus |
Not Available |
| Enzyme 72 SNPs |
SNPJam Report  |
| Enzyme 72 General References |
Not Available |
| Enzyme 72 Metabolite References |
Not Available |
|
Enzyme 73
[top]
|
| Enzyme 73 ID |
17727 |
| Enzyme 73 Name |
cDNA FLJ53798, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-) |
| Enzyme 73 Synonyms |
Not Available |
| Enzyme 73 Gene Name |
Not Available |
| Enzyme 73 Protein Sequence |
>cDNA FLJ53798, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-)
MRAPGAGAASVVSLALLWLLGLPWTWSAAAALGVYVGSGGWRFLRIVCKTARRDLFGLSV
LIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLF
RQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI
FGGEMVAAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKGM
DDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNIIG
VGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVRL
AVGSGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPIR
LVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHSV
FSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAVY
GVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKIQ
KTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAFAL
|
| Enzyme 73 Number of Residues |
646 |
| Enzyme 73 Molecular Weight |
71080.5 |
| Enzyme 73 Theoretical pI |
8.63 |
| Enzyme 73 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 73 General Function |
Involved in catalytic activity |
| Enzyme 73 Specific Function |
Not Available |
| Enzyme 73 Pathways |
Not Available |
| Enzyme 73 Reactions |
Not Available |
| Enzyme 73 Pfam Domain Function |
|
| Enzyme 73 Signals |
|
| Enzyme 73 Transmembrane Regions |
|
| Enzyme 73 Essentiality |
Not Available |
| Enzyme 73 GenBank ID Protein |
221041300  |
| Enzyme 73 UniProtKB/Swiss-Prot ID |
B7Z3U1  |
| Enzyme 73 UniProtKB/Swiss-Prot Entry Name |
B7Z3U1_HUMAN  |
| Enzyme 73 PDB ID |
Not Available |
| Enzyme 73 Cellular Location |
Not Available |
| Enzyme 73 Gene Sequence |
>1941 bp
ATGCGGGCTCCGGGTGCGGGCGCGGCCTCGGTGGTCTCGCTGGCGCTGTTGTGGCTGCTG
GGGCTGCCGTGGACCTGGAGCGCGGCAGCGGCGCTCGGCGTGTACGTGGGCAGCGGCGGC
TGGCGCTTCCTGCGCATCGTCTGCAAGACCGCGAGGCGAGACCTCTTCGGTCTCTCTGTG
CTGATCCGCGTGCGCCTGGAGCTGCGGCGGCACCAGCGTGCCGGCCACACCATCCCGCGC
ATCTTTCAGGCGGTAGTGCAGCGACAGCCCGAGCGCCTGGCGCTGGTGGATGCCGGGACC
GGCGAGTGCTGGACCTTTGCGCAGCTGGACGCCTACTCCAATGCGGTAGCCAACCTCTTC
CGCCAGCTGGGCTTCGCGCCGGGCGACGTGGTGGCCATCTTCCTGGAGGGCCGGCCGGAG
TTCGTGGGGCTGTGGCTGGGCCTGGCCAAGGCGGGCATGGAGGCCGCGCTGCTCAACGTG
AACCTGCGGCGCGAGCCCCTGGCCTTCTGCCTGGGCACCTCGGGCGCTAAGGCCCTGATC
TTTGGAGGAGAAATGGTGGCGGCGGTGGCCGAAGTGAGCGGGCATCTGGGGAAAAGTTTG
ATCAAGTTCTGCTCTGGAGACTTGGGGCCCGAGGGCATCTTGCCGGACACCCACCTCCTG
GACCCGCTGCTGAAGGAGGCCTCTACTGCCCCCTTGGCACAGATCCCCAGCAAGGGCATG
GACGATCGTCTCTTCTACATCTACACGTCGGGGACCACCGGGCTGCCCAAGGCTGCCATT
GTCGTGCACAGCAGGTACTACCGCATGGCAGCCTTCGGCCACCACGCCTACCGCATGCAG
GCGGCTGACGTGCTCTATGACTGCCTGCCCCTGTACCACTCGGCAGGAAACATCATCGGC
GTGGGGCAGTGTCTCATCTATGGGCTGACAGTCGTCCTCCGCAAGAAATTCTCGGCCAGC
CGCTTCTGGGACGACTGCATCAAGTACAACTGCACGGTGGTTCAGTACATCGGGGAGATC
TGCCGCTACCTGCTGAAGCAGCCGGTGCGCGAGGCGGAGAGGCGACACCGCGTGCGCCTG
GCGGTGGGGAGCGGGCTGCGTCCTGCCATCTGGGAGGAGTTCACGGAGCGCTTCGGCGTA
CGCCAAATCGGGGAGTTCTACGGCGCCACCGAGTGCAACTGCAGCATTGCCAACATGGAC
GGCAAGGTCGGCTCCTGTGGTTTCAACAGCCGCATCCTGCCCCACGTGTACCCCATCCGG
CTGGTGAAGGTCAATGAGGACACAATGGAGCTGCTGCGGGATGCCCAGGGCCTCTGCATC
CCCTGCCAGGCCGGGGAGCCTGGCCTCCTTGTGGGTCAGATCAACCAACAGGACCCGCTG
CGCCGCTTCGATGGCTATGTCAGCGAGAGCGCCACCAGCAAGAAGATCGCCCACAGCGTC
TTCAGCAAGGGCGACAGCGCCTACCTCTCAGGTGACGTGCTAGTGATGGATGAGCTGGGC
TACATGTACTTCCGGGACCGTAGCGGGGACACCTTCCGCTGGCGAGGGGAGAACGTCTCC
ACCACCGAGGTGGAGGGCGTGCTGAGCCGCCTGCTGGGCCAGACAGACGTGGCCGTCTAT
GGGGTGGCTGTTCCAGGAGTGGAGGGTAAGGCAGGGATGGCGGCCGTCGCAGACCCCCAC
AGCCTGCTGGACCCCAACGCGATATACCAGGAGCTGCAGAAGGTGCTGGCACCCTATGCC
CGGCCCATCTTCCTGCGCCTCCTGCCCCAGGTGGACACCACAGGCACCTTCAAGATCCAG
AAGACGAGGCTGCAGCGAGAGGGCTTTGACCCACGCCAGACCTCAGACCGGCTCTTCTTC
CTGGACCTGAAGCAGGGCCACTACCTGCCCTTAAATGAGGCAGTCTACACTCGCATCTGC
TCGGGCGCCTTCGCCCTCTGA
|
| Enzyme 73 GenBank Gene ID |
AK296355  |
| Enzyme 73 GeneCard ID |
Not Available |
| Enzyme 73 GenAtlas ID |
Not Available |
| Enzyme 73 HGNC ID |
HGNC:10995  |
| Enzyme 73 Chromosome Location |
Not Available |
| Enzyme 73 Locus |
Not Available |
| Enzyme 73 SNPs |
Not Available |
| Enzyme 73 General References |
Not Available |
| Enzyme 73 Metabolite References |
Not Available |
|
Enzyme 74
[top]
|
| Enzyme 74 ID |
17728 |
| Enzyme 74 Name |
Peroxisome proliferative activated receptor gamma isoform 2 variant |
| Enzyme 74 Synonyms |
Not Available |
| Enzyme 74 Gene Name |
Not Available |
| Enzyme 74 Protein Sequence |
>Peroxisome proliferative activated receptor gamma isoform 2 variant
EMTMVDTEMPFWPTNFGISSVDLSVVEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTD
PVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKAS
GFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNA
IRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTG
KTTDKSPFVIYDMNSLMMGEDKIKFKHITPLQEQSKEVAIRIFQGCQFRSVEAVQEITEY
AKSIPGFVNLDLNDQVTLLKYGVHEIIYTMLASLMNKDGVLISEGQGFMTREFLKSLRKP
FGDFMEPKFEFAVKFNALELDDSDLAIFIAVIILSGDRPGLLNVKPIEDIQDNLLQALEL
QLKLNHPESSQLFAKLLQKMTDLRQIVTEHVQLLQVIKKTETDMSLHPLLQEIYKDLY
|
| Enzyme 74 Number of Residues |
478 |
| Enzyme 74 Molecular Weight |
54777.6 |
| Enzyme 74 Theoretical pI |
6.51 |
| Enzyme 74 GO Classification |
| Function |
- DNA binding
- binding
- cation binding
- ion binding
- ligand-dependent nuclear receptor activity
- metal ion binding
- molecular transducer activity
- nucleic acid binding
- receptor activity
- sequence-specific DNA binding
- sequence-specific DNA binding transcription factor activity
- signal transducer activity
- steroid hormone receptor activity
- transition metal ion binding
- zinc ion binding
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 74 General Function |
Involved in DNA binding |
| Enzyme 74 Specific Function |
Not Available |
| Enzyme 74 Pathways |
Not Available |
| Enzyme 74 Reactions |
Not Available |
| Enzyme 74 Pfam Domain Function |
|
| Enzyme 74 Signals |
|
| Enzyme 74 Transmembrane Regions |
|
| Enzyme 74 Essentiality |
Not Available |
| Enzyme 74 GenBank ID Protein |
62898788  |
| Enzyme 74 UniProtKB/Swiss-Prot ID |
Q53EW1  |
| Enzyme 74 UniProtKB/Swiss-Prot Entry Name |
Q53EW1_HUMAN  |
| Enzyme 74 PDB ID |
1I7I  |
| Enzyme 74 PDB File |
Show |
| Enzyme 74 3D Structure |
|
| Enzyme 74 Cellular Location |
Not Available |
| Enzyme 74 Gene Sequence |
>1438 bp
AGAAATGACCATGGTTGACACAGAGATGCCATTCTGGCCCACCAACTTTGGGATCAGCTC
CGTGGATCTCTCCGTAGTGGAAGACCACTCCCACTCCTTTGATATCAAGCCCTTCACTAC
TGTTGACTTCTCCAGCATTTCTACTCCACATTACGAAGACATTCCATTCACAAGAACAGA
TCCAGTGGTTGCAGATTACAAGTATGACCTGAAACTTCAAGAGTACCAAAGTGCAATCAA
AGTGGAGCCTGCATCTCCACCTTATTATTCTGAGAAGACTCAGCTCTACAATAAGCCTCA
TGAAGAGCCTTCCAACTCCCTCATGGCAATTGAATGTCGTGTCTGTGGAGATAAAGCTTC
TGGATTTCACTATGGAGTTCATGCTTGTGAAGGATGCAAGGGTTTCTTCCGGAGAACAAT
CAGATTGAAGCTTATCTATGACAGATGTGATCTTAACTGTCGGATCCACAAAAAAAGTAG
AAATAAATGTCAGTACTGTCGGTTTCAGAAATGCCTTGCAGTGGGGATGTCTCATAATGC
CATCAGGTTTGGGCGGATGCCACAGGCCGAGAAGGAGAAGCTGTTGGCGGAGATCTCCAG
TGATATCGACCAGCTGAATCCAGAGTCCGCTGACCTCCGGGCCCTGGCAAAACATTTGTA
TGACTCATACATAAAGTCCTTCCCGCTGACCAAAGCAAAGGCGAGGGCGATCTTGACAGG
AAAGACAACAGACAAATCACCATTCGTTATCTATGACATGAATTCCTTAATGATGGGAGA
AGATAAAATCAAGTTCAAACACATCACCCCCCTGCAGGAGCAGAGCAAAGAGGTGGCCAT
CCGCATCTTTCAGGGCTGCCAGTTTCGCTCCGTGGAGGCTGTGCAGGAGATCACAGAGTA
TGCCAAAAGCATTCCTGGTTTTGTAAATCTTGACTTGAACGACCAAGTAACTCTCCTCAA
ATATGGAGTCCACGAGATCATTTACACAATGCTGGCCTCCTTGATGAATAAAGATGGGGT
TCTCATATCCGAGGGCCAAGGCTTCATGACAAGGGAGTTTCTAAAGAGCCTGCGAAAGCC
TTTTGGTGACTTTATGGAGCCCAAGTTTGAGTTTGCTGTGAAGTTCAATGCACTGGAATT
AGATGACAGCGACTTGGCAATATTTATTGCTGTCATTATTCTCAGTGGAGACCGCCCAGG
TTTGCTGAATGTGAAGCCCATTGAAGACATTCAAGACAACCTGCTACAAGCCCTGGAGCT
CCAGCTGAAGCTGAACCACCCTGAGTCCTCACAGCTGTTTGCCAAGCTGCTCCAGAAAAT
GACAGACCTCAGACAGATTGTCACGGAACACGTGCAGCTACTGCAGGTGATCAAGAAGAC
GGAGACAGACATGAGTCTTCACCCGCTCCTGCAGGAGATCTACAAGGACTTGTACTAG
|
| Enzyme 74 GenBank Gene ID |
AK223528  |
| Enzyme 74 GeneCard ID |
Not Available |
| Enzyme 74 GenAtlas ID |
Not Available |
| Enzyme 74 HGNC ID |
HGNC:9236  |
| Enzyme 74 Chromosome Location |
Not Available |
| Enzyme 74 Locus |
Not Available |
| Enzyme 74 SNPs |
Not Available |
| Enzyme 74 General References |
- Maruyama K, Sugano S: Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 1994 Jan 28;138(1-2):171-4. [PubMed
]
- Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S: Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. Gene. 1997 Oct 24;200(1-2):149-56. [PubMed
]
|
| Enzyme 74 Metabolite References |
Not Available |
|
Enzyme 75
[top]
|
| Enzyme 75 ID |
17729 |
| Enzyme 75 Name |
cDNA FLJ14598 fis, clone NT2RM4002558, highly similar to Long-chain fatty acid transport protein 4 (EC 6.2.1.-) |
| Enzyme 75 Synonyms |
Not Available |
| Enzyme 75 Gene Name |
Not Available |
| Enzyme 75 Protein Sequence |
>cDNA FLJ14598 fis, clone NT2RM4002558, highly similar to Long-chain fatty acid transport protein 4 (EC 6.2.1.-)
MENRNEFVGLWLGMAKLGVEAALINTNLRRDALLHCLTTSRARALVFGSEMASAICEVHA
SLDPSLSLFCSGSWEPGAVPPSTEHLDPLLKDAPKHLPSCPDKGFTDKLFYIYTSGTTGL
PKAAIVVHSRYYRMAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRK
KFSASRFWDDCIEYNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGPRQSIWTNFS
SRFHIPQVAEFYGATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRVNEDTMELIRGP
DGVCIPCQPGEPGQLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLV
MDELGYLYFRDRTGDTFRWKGENVSTTEVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAA
VASPTGNCDLERFAQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVK
DPLFYLDAQKGRYVPLDQEAYSRIQAGEEKL
|
| Enzyme 75 Number of Residues |
511 |
| Enzyme 75 Molecular Weight |
57194.0 |
| Enzyme 75 Theoretical pI |
6.99 |
| Enzyme 75 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 75 General Function |
Involved in catalytic activity |
| Enzyme 75 Specific Function |
Not Available |
| Enzyme 75 Pathways |
Not Available |
| Enzyme 75 Reactions |
Not Available |
| Enzyme 75 Pfam Domain Function |
|
| Enzyme 75 Signals |
|
| Enzyme 75 Transmembrane Regions |
|
| Enzyme 75 Essentiality |
Not Available |
| Enzyme 75 GenBank ID Protein |
193786550  |
| Enzyme 75 UniProtKB/Swiss-Prot ID |
B3KNH1  |
| Enzyme 75 UniProtKB/Swiss-Prot Entry Name |
B3KNH1_HUMAN  |
| Enzyme 75 PDB ID |
Not Available |
| Enzyme 75 Cellular Location |
Not Available |
| Enzyme 75 Gene Sequence |
>1536 bp
ATGGAGAACCGCAATGAGTTCGTGGGCCTATGGCTGGGCATGGCCAAGCTCGGTGTGGAG
GCAGCCCTCATCAACACCAACCTGCGGCGGGATGCTCTGCTCCACTGCCTCACCACCTCG
CGCGCACGGGCCCTTGTCTTTGGCAGCGAAATGGCCTCAGCCATCTGTGAGGTCCATGCC
AGCCTGGACCCCTCGCTCAGCCTCTTCTGCTCTGGCTCCTGGGAGCCCGGTGCGGTGCCT
CCAAGCACAGAACACCTGGACCCTCTGCTGAAAGATGCTCCCAAGCACCTTCCCAGTTGC
CCTGACAAGGGCTTCACAGATAAACTGTTCTACATCTACACATCCGGCACCACAGGGCTG
CCCAAGGCCGCCATCGTGGTGCACAGCAGGTATTACCGCATGGCTGCCCTGGTGTACTAT
GGATTCCGCATGCGGCCCAACGACATCGTCTATGACTGCCTCCCCCTCTACCACTCAGCA
GGAAACATCGTGGGAATCGGCCAGTGCCTGCTGCATGGCATGACGGTGGTGATTCGGAAG
AAGTTCTCAGCCTCCCGGTTCTGGGACGATTGTATCGAGTACAACTGCACGATTGTGCAG
TACATTGGTGAACTGTGCCGCTACCTCCTGAACCAGCCACCGCGGGAGGCAGAAAACCAG
CACCAGGTTCGCATGGCACTAGGCAATGGCCCCCGGCAGTCCATCTGGACCAACTTTTCC
AGCCGCTTCCACATACCCCAGGTGGCTGAGTTCTATGGGGCCACAGAGTGCAACTGTAGC
CTGGGCAACTTCGACAGCCAGGTGGGGGCCTGTGGTTTCAATAGCCGCATCCTGTCCTTC
GTGTACCCCATCCGGTTGGTACGTGTCAACGAGGACACCATGGAGCTGATCCGGGGGCCC
GACGGCGTCTGCATTCCCTGCCAGCCAGGTGAGCCGGGCCAGCTGGTGGGCCGCATCATC
CAGAAAGACCCCCTGCGCCGCTTCGATGGCTACCTCAACCAGGGCGCCAACAACAAGAAG
ATTGCCAAGGATGTCTTCAAGAAGGGGGACCAGGCCTACCTTACTGGTGATGTGCTGGTG
ATGGACGAGCTGGGCTACCTGTACTTCCGAGACCGCACTGGGGACACGTTCCGCTGGAAA
GGTGAGAACGTGTCCACCACCGAGGTGGAAGGCACACTCAGCCGCCTGCTGGACATGGCT
GACGTGGCCGTGTATGGTGTCGAGGTGCCAGGAACCGAGGGCCGGGCCGGAATGGCTGCT
GTGGCCAGCCCCACTGGCAACTGTGACCTGGAGCGCTTTGCTCAGGTCTTGGAGAAGGAA
CTGCCCCTGTATGCGCGCCCCATCTTCCTGCGCCTCCTGCCTGAGCTGCACAAAACAGGA
ACCTACAAGTTCCAGAAGACAGAGCTACGGAAGGAGGGCTTTGACCCGGCTATTGTGAAA
GACCCGCTGTTCTATCTAGATGCCCAGAAGGGCCGCTACGTCCCGCTGGACCAAGAGGCC
TACAGCCGCATCCAGGCAGGCGAGGAGAAGCTGTGA
|
| Enzyme 75 GenBank Gene ID |
AK027504  |
| Enzyme 75 GeneCard ID |
Not Available |
| Enzyme 75 GenAtlas ID |
Not Available |
| Enzyme 75 HGNC ID |
HGNC:10998  |
| Enzyme 75 Chromosome Location |
Not Available |
| Enzyme 75 Locus |
Not Available |
| Enzyme 75 SNPs |
Not Available |
| Enzyme 75 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 75 Metabolite References |
Not Available |
|
Enzyme 76
[top]
|
| Enzyme 76 ID |
17730 |
| Enzyme 76 Name |
cDNA FLJ61377, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-) |
| Enzyme 76 Synonyms |
Not Available |
| Enzyme 76 Gene Name |
Not Available |
| Enzyme 76 Protein Sequence |
>cDNA FLJ61377, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-)
MTHVLGTTAVAEVSGHLGKSLIKFCSGDLGPEGILPDTHLLDPLLKEASTAPLAQIPSKG
MDDRLFYIYTSGTTGLPKAAIVVHSRYYRMAAFGHHAYRMQAADVLYDCLPLYHSAGNII
GVGQCLIYGLTVVLRKKFSASRFWDDCIKYNCTVVQYIGEICRYLLKQPVREAERRHRVR
LAVGNGLRPAIWEEFTERFGVRQIGEFYGATECNCSIANMDGKVGSCGFNSRILPHVYPI
RLVKVNEDTMELLRDAQGLCIPCQAGEPGLLVGQINQQDPLRRFDGYVSESATSKKIAHS
VFSKGDSAYLSGDVLVMDELGYMYFRDRSGDTFRWRGENVSTTEVEGVLSRLLGQTDVAV
YGVAVPGVEGKAGMAAVADPHSLLDPNAIYQELQKVLAPYARPIFLRLLPQVDTTGTFKI
QKTRLQREGFDPRQTSDRLFFLDLKQGHYLPLNEAVYTRICSGAFAL
|
| Enzyme 76 Number of Residues |
467 |
| Enzyme 76 Molecular Weight |
51780.0 |
| Enzyme 76 Theoretical pI |
7.85 |
| Enzyme 76 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 76 General Function |
Involved in catalytic activity |
| Enzyme 76 Specific Function |
Not Available |
| Enzyme 76 Pathways |
Not Available |
| Enzyme 76 Reactions |
Not Available |
| Enzyme 76 Pfam Domain Function |
|
| Enzyme 76 Signals |
|
| Enzyme 76 Transmembrane Regions |
|
| Enzyme 76 Essentiality |
Not Available |
| Enzyme 76 GenBank ID Protein |
221042942  |
| Enzyme 76 UniProtKB/Swiss-Prot ID |
B7Z662  |
| Enzyme 76 UniProtKB/Swiss-Prot Entry Name |
B7Z662_HUMAN  |
| Enzyme 76 PDB ID |
Not Available |
| Enzyme 76 Cellular Location |
Not Available |
| Enzyme 76 Gene Sequence |
>1404 bp
ATGACCCATGTGTTGGGGACCACAGCGGTGGCCGAAGTGAGCGGGCATCTGGGGAAAAGT
TTGATCAAGTTCTGCTCTGGAGACTTGGGGCCCGAGGGCATCTTGCCGGACACCCACCTC
CTGGACCCGCTGCTGAAGGAGGCCTCTACTGCCCCCTTGGCACAGATCCCCAGCAAGGGC
ATGGACGATCGTCTTTTCTACATCTACACGTCGGGGACCACCGGGCTGCCCAAGGCTGCC
ATTGTCGTGCACAGCAGGTACTACCGCATGGCAGCCTTCGGCCACCACGCCTACCGCATG
CAGGCGGCTGACGTGCTCTATGACTGCCTGCCCCTGTACCACTCGGCAGGAAACATCATC
GGCGTGGGGCAGTGTCTCATCTATGGGCTGACAGTCGTCCTCCGCAAGAAATTCTCGGCC
AGCCGCTTCTGGGACGACTGCATCAAGTACAACTGCACGGTGGTTCAGTACATCGGGGAG
ATCTGCCGCTACCTGCTGAAGCAGCCGGTGCGCGAGGCGGAGAGGCGACACCGCGTGCGC
CTGGCGGTGGGGAACGGGCTGCGTCCTGCCATCTGGGAGGAGTTCACGGAGCGCTTCGGC
GTACGCCAAATCGGGGAGTTCTACGGCGCCACCGAGTGCAACTGCAGCATTGCCAACATG
GACGGCAAGGTCGGCTCCTGTGGTTTCAACAGCCGCATCCTGCCCCACGTGTACCCCATC
CGGCTGGTGAAGGTCAATGAGGACACAATGGAGCTGCTGCGGGATGCCCAGGGCCTCTGC
ATCCCCTGCCAGGCCGGGGAGCCTGGCCTCCTTGTGGGTCAGATCAACCAACAGGACCCG
CTGCGCCGCTTCGATGGCTATGTCAGCGAGAGCGCCACCAGCAAGAAGATCGCCCACAGC
GTCTTCAGCAAGGGCGACAGCGCCTACCTCTCAGGTGACGTGCTAGTGATGGATGAGCTG
GGCTACATGTACTTCCGGGACCGTAGCGGGGACACCTTCCGCTGGCGAGGGGAGAACGTC
TCCACCACCGAGGTGGAGGGCGTGCTGAGCCGCCTGCTGGGCCAGACAGACGTGGCCGTC
TATGGGGTGGCTGTTCCAGGAGTGGAGGGTAAGGCAGGGATGGCGGCCGTCGCAGACCCC
CACAGCCTGCTGGACCCCAACGCGATATACCAGGAGCTGCAGAAGGTGCTGGCACCCTAT
GCCCGGCCCATCTTCCTGCGCCTCCTGCCCCAGGTGGACACCACAGGCACCTTCAAGATC
CAGAAGACGAGGCTGCAGCGAGAGGGCTTTGACCCACGCCAGACCTCAGACCGGCTCTTC
TTCCTGGACCTGAAGCAGGGCCACTACCTGCCCTTAAATGAGGCAGTCTACACTCGCATC
TGCTCGGGCGCCTTCGCCCTCTGA
|
| Enzyme 76 GenBank Gene ID |
AK299852  |
| Enzyme 76 GeneCard ID |
Not Available |
| Enzyme 76 GenAtlas ID |
Not Available |
| Enzyme 76 HGNC ID |
HGNC:10995  |
| Enzyme 76 Chromosome Location |
Not Available |
| Enzyme 76 Locus |
Not Available |
| Enzyme 76 SNPs |
Not Available |
| Enzyme 76 General References |
Not Available |
| Enzyme 76 Metabolite References |
Not Available |
|
Enzyme 77
[top]
|
| Enzyme 77 ID |
17731 |
| Enzyme 77 Name |
CPT1B protein |
| Enzyme 77 Synonyms |
Not Available |
| Enzyme 77 Gene Name |
CPT1B |
| Enzyme 77 Protein Sequence |
>CPT1B protein
MELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEEYIYLRGRSPLMVNSNYYVMDLVL
IKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALGIVPMCSYQMERMFNTTRIPGKDT
DVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDLEMQFQRILDDPSPPQPGEEKLAA
LTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVALDEESYSYDPEDEASLSLYGKAL
LHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPIIGHLWEFVLGTDSFHLGYTETGH
CLGKPNPALAPPTRLQWDIPKQAVIKSSYQVAKALADDVELYCFQFLPFGKGLIKKCRTS
PDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREGRTETVRSCTSESTAFVQAMMEGSHT
KADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCLYLVSKYLGVSSPFLAEVLSEPWRLS
TSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGYGVSYMIAGENTIFFHISSKFSSSET
NAQRFGNHIRKALLDIADLFQVPKAYS
|
| Enzyme 77 Number of Residues |
567 |
| Enzyme 77 Molecular Weight |
64474.2 |
| Enzyme 77 Theoretical pI |
8.20 |
| Enzyme 77 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 77 General Function |
Involved in acyltransferase activity |
| Enzyme 77 Specific Function |
Not Available |
| Enzyme 77 Pathways |
Not Available |
| Enzyme 77 Reactions |
Not Available |
| Enzyme 77 Pfam Domain Function |
|
| Enzyme 77 Signals |
|
| Enzyme 77 Transmembrane Regions |
|
| Enzyme 77 Essentiality |
Not Available |
| Enzyme 77 GenBank ID Protein |
124297731  |
| Enzyme 77 UniProtKB/Swiss-Prot ID |
A2RRE8  |
| Enzyme 77 UniProtKB/Swiss-Prot Entry Name |
A2RRE8_HUMAN  |
| Enzyme 77 PDB ID |
Not Available |
| Enzyme 77 Cellular Location |
Not Available |
| Enzyme 77 Gene Sequence |
>1704 bp
ATGGAGTTGCTGGCCAAAGAATTCCAGGACAAGACTGCCCCCAGGCTGCAGAAATACCTG
GTGCTCAAGTCATGGTGGGCAAGTAACTATGTGAGTGACTGGTGGGAAGAGTACATCTAC
CTTCGAGGCAGGAGCCCTCTCATGGTGAACAGCAACTATTATGTCATGGACCTTGTGCTC
ATCAAGAATACAGACGTGCAGGCAGCCCGCCTGGGAAACATCATCCACGCCATGATCATG
TATCGCCGTAAACTGGACCGTGAAGAAATCAAGCCTGTGATGGCACTGGGCATAGTGCCT
ATGTGCTCCTACCAGATGGAGAGGATGTTCAACACCACTCGGATCCCGGGCAAGGACACA
GATGTGCTACAGCACCTCTCAGACAGCCGGCACGTGGCTGTCTACCACAAGGGACGCTTC
TTCAAGCTGTGGCTCTATGAGGGCGCCCGTCTGCTCAAGCCTCAGGATCTGGAGATGCAG
TTCCAGAGGATCCTGGACGACCCCTCCCCACCTCAGCCTGGGGAGGAGAAGCTGGCAGCC
CTCACTGCAGGAGGAAGGGTGGAGTGGGCGCAGGCACGCCAGGCCTTCTTTAGCTCTGGA
AAGAATAAGGCTGCCTTGGAGGCCATCGAGCGTGCCGCTTTCTTCGTGGCCCTGGATGAG
GAATCCTACTCCTATGACCCCGAAGATGAGGCCAGCCTCAGCCTCTATGGCAAGGCCCTG
CTACATGGCAACTGCTACAACAGGTGGTTTGACAAATCCTTCACTCTCATTTCCTTCAAG
AATGGCCAGTTGGGTCTCAATGCAGAGCATGCGTGGGCAGATGCTCCCATCATTGGGCAC
CTCTGGGAGTTTGTCCTGGGCACAGACAGCTTCCACCTGGGCTACACGGAGACCGGGCAC
TGCCTGGGCAAACCGAACCCTGCGCTCGCACCTCCTACACGGCTGCAGTGGGACATTCCA
AAACAGGCGGTCATCAAGAGTTCCTACCAGGTGGCCAAGGCGTTGGCAGACGACGTGGAG
TTGTACTGCTTCCAGTTCCTGCCCTTTGGCAAAGGCCTCATCAAGAAGTGCCGGACCAGC
CCTGATGCCTTTGTGCAGATCGCGCTGCAGCTGGCTCACTTCCGGGACAGGGGTAAGTTC
TGCCTGACCTATGAGGCCTCAATGACCAGAATGTTCCGGGAGGGACGGACTGAGACTGTG
CGTTCCTGTACCAGCGAGTCCACAGCCTTTGTGCAGGCCATGATGGAGGGGTCCCACACA
AAAGCAGACCTGCGAGATCTCTTCCAGAAGGCTGCTAAGAAGCACCAGAATATGTACCGC
CTGGCCATGACCGGGGCAGGGATCGACAGGCACCTCTTCTGCCTTTACTTGGTCTCCAAG
TACCTAGGAGTCAGCTCTCCTTTCCTTGCTGAGGTGCTCTCGGAACCCTGGCGTCTCTCC
ACCAGCCAGATCCCCCAATCCCAGATCCGCATGTTCGACCCAGAGCAGCACCCCAATCAC
CTGGGCGCTGGAGGTGGCTTTGGCCCTGTAGCAGATGATGGCTATGGAGTTTCCTACATG
ATTGCAGGCGAGAACACGATCTTCTTCCACATCTCCAGCAAGTTCTCAAGCTCAGAGACG
AACGCCCAGCGCTTTGGAAACCACATCCGCAAAGCCCTGCTGGACATTGCTGATCTTTTC
CAAGTTCCCAAGGCCTACAGCTGA
|
| Enzyme 77 GenBank Gene ID |
BC131570  |
| Enzyme 77 GeneCard ID |
CPT1B  |
| Enzyme 77 GenAtlas ID |
CPT1B  |
| Enzyme 77 HGNC ID |
HGNC:2329  |
| Enzyme 77 Chromosome Location |
2 |
| Enzyme 77 Locus |
22q13.33 |
| Enzyme 77 SNPs |
SNPJam Report  |
| Enzyme 77 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 77 Metabolite References |
Not Available |
|
Enzyme 78
[top]
|
| Enzyme 78 ID |
17732 |
| Enzyme 78 Name |
Peroxisome proliferator-activated receptor |
| Enzyme 78 Synonyms |
- SubName: Peroxisome proliferator-activated receptor gamma 1
|
| Enzyme 78 Gene Name |
PPARG |
| Enzyme 78 Protein Sequence |
>Peroxisome proliferator-activated receptor
MVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFS
|
| Enzyme 78 Number of Residues |
41 |
| Enzyme 78 Molecular Weight |
4695.2 |
| Enzyme 78 Theoretical pI |
3.91 |
| Enzyme 78 GO Classification |
| Function |
- DNA binding
- binding
- ligand-dependent nuclear receptor activity
- molecular transducer activity
- nucleic acid binding
- receptor activity
- signal transducer activity
|
| Process |
- biological regulation
- regulation of biological process
- regulation of gene expression
- regulation of macromolecule metabolic process
- regulation of metabolic process
- regulation of transcription
- regulation of transcription, DNA-dependent
|
| Component |
- intracellular membrane-bounded organelle
- membrane-bounded organelle
- nucleus
- organelle
|
|
| Enzyme 78 General Function |
Involved in DNA binding |
| Enzyme 78 Specific Function |
Not Available |
| Enzyme 78 Pathways |
Not Available |
| Enzyme 78 Reactions |
Not Available |
| Enzyme 78 Pfam Domain Function |
Not Available |
| Enzyme 78 Signals |
|
| Enzyme 78 Transmembrane Regions |
|
| Enzyme 78 Essentiality |
Not Available |
| Enzyme 78 GenBank ID Protein |
47678891  |
| Enzyme 78 UniProtKB/Swiss-Prot ID |
Q6L9M1  |
| Enzyme 78 UniProtKB/Swiss-Prot Entry Name |
Q6L9M1_HUMAN  |
| Enzyme 78 PDB ID |
Not Available |
| Enzyme 78 Cellular Location |
Not Available |
| Enzyme 78 Gene Sequence |
>123 bp
ATGGTTGACACAGAGATGCCATTCTGGCCCACCAACTTTGGGATCAGCTCCGTGGATCTC
TCCGTAATGGAAGACCACTCCCACTCCTTTGATATCAAGCCCTTCACTACTGTTGACTTC
TCC
|
| Enzyme 78 GenBank Gene ID |
AB097931  |
| Enzyme 78 GeneCard ID |
PPARG  |
| Enzyme 78 GenAtlas ID |
PPARG  |
| Enzyme 78 HGNC ID |
HGNC:9236  |
| Enzyme 78 Chromosome Location |
3 |
| Enzyme 78 Locus |
3p25 |
| Enzyme 78 SNPs |
SNPJam Report  |
| Enzyme 78 General References |
Not Available |
| Enzyme 78 Metabolite References |
Not Available |
|
Enzyme 79
[top]
|
| Enzyme 79 ID |
17733 |
| Enzyme 79 Name |
CPT1B protein |
| Enzyme 79 Synonyms |
Not Available |
| Enzyme 79 Gene Name |
CPT1B |
| Enzyme 79 Protein Sequence |
>CPT1B protein
MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPT
SWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTG
IFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPR
VSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEE
YIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALG
IVPMCSYQMEGMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDL
EMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVA
LDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPI
IGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKAL
ADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREG
RTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCL
YLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGY
GVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS
|
| Enzyme 79 Number of Residues |
772 |
| Enzyme 79 Molecular Weight |
87701.3 |
| Enzyme 79 Theoretical pI |
8.69 |
| Enzyme 79 GO Classification |
| Function |
- acyltransferase activity
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 79 General Function |
Involved in acyltransferase activity |
| Enzyme 79 Specific Function |
Not Available |
| Enzyme 79 Pathways |
Not Available |
| Enzyme 79 Reactions |
Not Available |
| Enzyme 79 Pfam Domain Function |
|
| Enzyme 79 Signals |
|
| Enzyme 79 Transmembrane Regions |
|
| Enzyme 79 Essentiality |
Not Available |
| Enzyme 79 GenBank ID Protein |
148744459  |
| Enzyme 79 UniProtKB/Swiss-Prot ID |
A5PLL0  |
| Enzyme 79 UniProtKB/Swiss-Prot Entry Name |
A5PLL0_HUMAN  |
| Enzyme 79 PDB ID |
Not Available |
| Enzyme 79 Cellular Location |
Not Available |
| Enzyme 79 Gene Sequence |
>2319 bp
ATGGCGGAAGCTCACCAGGCCGTGGCCTTCCAGTTCACGGTGACCCCAGACGGGGTCGAC
TTCCGGCTCAGTCGGGAGGCCCTGAAACACGTCTACCTGTCTGGGATCAACTCCTGGAAG
AAACGCCTGATCCGCATCAAGAATGGCATCCTCAGGGGCGTGTACCCTGGCAGCCCCACC
AGCTGGCTGGTCGTCATCATGGCAACAGTGGGTTCCTCCTTCTGCAACGTGGACATCTCC
TTGGGGCTGGTCAGTTGCATCCAGAGATGCCTCCCTCAGGGGTGTGGCCCCTACCAGACC
CCGCAGACCCGGGCACTTCTCAGCATGGCCATCTTCTCCACGGGCGTCTGGGTGACGGGC
ATCTTCTTCTTCCGCCAAACCCTGAAGCTGCTTCTCTGCTACCATGGGTGGATGTTTGAG
ATGCATGGCAAGACCAGCAACTTGACCAGGATCTGGGCTATGTGTATCCGCCTTCTATCC
AGCCGGCACCCTATGCTCTACAGCTTCCAGACATCTCTGCCCAAGCTTCCTGTGCCCAGG
GTGTCAGCCACAATTCAGCGGTACCTAGAGTCTGTGCGCCCCTTGTTGGATGATGAGGAA
TATTACCGCATGGAGTTGCTGGCCAAAGAATTCCAGGACAAGACTGCCCCCAGGCTGCAG
AAATACCTGGTGCTCAAGTCATGGTGGGCAAGTAACTATGTGAGTGACTGGTGGGAAGAG
TACATCTACCTTCGAGGCAGGAGCCCTCTCATGGTGAACAGCAACTATTATGTCATGGAC
CTTGTGCTCATCAAGAATACAGACGTGCAGGCAGCCCGCCTGGGAAACATCATCCACGCC
ATGATCATGTATCGCCGTAAACTGGACCGTGAAGAAATCAAGCCTGTGATGGCACTGGGC
ATAGTGCCTATGTGCTCCTACCAGATGGAGGGGATGTTCAACACCACTCGGATCCCGGGC
AAGGACACAGATGTGCTACAGCACCTCTCAGACAGCCGGCACGTGGCTGTCTACCACAAG
GGACGCTTCTTCAAGCTGTGGCTCTATGAGGGCGCCCGTCTGCTCAAGCCTCAGGATCTG
GAGATGCAGTTCCAGAGGATCCTGGACGACCCCTCCCCACCTCAGCCTGGGGAGGAGAAG
CTGGCAGCCCTCACTGCAGGAGGAAGGGTGGAGTGGGCGCAGGCACGCCAGGCCTTCTTT
AGCTCTGGAAAGAATAAGGCTGCCTTGGAGGCCATCGAGCGTGCCGCTTTCTTCGTGGCC
CTGGATGAGGAATCCTACTCCTATGACCCCGAAGATGAGGCCAGCCTCAGCCTCTATGGC
AAGGCCCTGCTACATGGCAACTGCTACAACAGGTGGTTTGACAAATCCTTCACTCTCATT
TCCTTCAAGAATGGCCAGTTGGGTCTCAATGCAGAGCATGCGTGGGCAGATGCTCCCATC
ATTGGGCACCTCTGGGAGTTTGTCCTGGGCACAGACAGCTTCCACCTGGGCTACACGGAG
ACCGGGCACTGCCTGGGCAAACCGAACCCTGCGCTCGCACCTCCTACACGGCTGCAGTGG
GACATTCCAAAACAGTGCCAGGCGGTCATCGAGAGTTCCTACCAGGTGGCCAAGGCGTTG
GCAGACGACGTGGAGTTGTACTGCTTCCAGTTCCTGCCCTTTGGCAAAGGCCTCATCAAG
AAGTGCCGGACCAGCCCTGATGCCTTTGTGCAGATCGCGCTGCAGCTGGCTCACTTCCGG
GACAGGGGTAAGTTCTGCCTGACCTATGAGGCCTCAATGACCAGAATGTTCCGGGAGGGA
CGGACTGAGACTGTGCGTTCCTGTACCAGCGAGTCCACAGCCTTTGTGCAGGCCATGATG
GAGGGGTCCCACACAAAAGCAGACCTGCGAGATCTCTTCCAGAAGGCTGCTAAGAAGCAC
CAGAATATGTACCGCCTGGCCATGACCGGGGCAGGGATCGACAGGCACCTCTTCTGCCTT
TACTTGGTCTCCAAGTACCTAGGAGTCAGCTCTCCTTTCCTTGCTGAGGTGCTCTCGGAA
CCCTGGCGTCTCTCCACCAGCCAGATCCCCCAATCCCAGATCCGCATGTTCGACCCAGAG
CAGCACCCCAATCACCTGGGCGCTGGAGGTGGCTTTGGCCCTGTAGCAGATGATGGCTAT
GGAGTTTCCTACATGATTGCAGGCGAGAACACGATCTTCTTCCACATCTCCAGCAAGTTC
TCAAGCTCAGAGACGAACGCCCAGCGCTTTGGAAACCACATCCGCAAAGCCCTGCTGGAC
ATTGCTGATCTTTTCCAAGTTCCCAAGGCCTACAGCTGA
|
| Enzyme 79 GenBank Gene ID |
BC142954  |
| Enzyme 79 GeneCard ID |
CPT1B  |
| Enzyme 79 GenAtlas ID |
CPT1B  |
| Enzyme 79 HGNC ID |
HGNC:2329  |
| Enzyme 79 Chromosome Location |
2 |
| Enzyme 79 Locus |
22q13.33 |
| Enzyme 79 SNPs |
SNPJam Report  |
| Enzyme 79 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 79 Metabolite References |
Not Available |
|
Enzyme 80
[top]
|
| Enzyme 80 ID |
17734 |
| Enzyme 80 Name |
cDNA FLJ90350 fis, clone NT2RP2003210, highly similar to Long-chain fatty acid transport protein 4 (EC 6.2.1.-) |
| Enzyme 80 Synonyms |
Not Available |
| Enzyme 80 Gene Name |
Not Available |
| Enzyme 80 Protein Sequence |
>cDNA FLJ90350 fis, clone NT2RP2003210, highly similar to Long-chain fatty acid transport protein 4 (EC 6.2.1.-)
MAALVYYGFRMRPNDIVYDCLPLYHSAGNIVGIGQCLLHGMTVVIRKKFSASRFWDDCIK
YNCTIVQYIGELCRYLLNQPPREAENQHQVRMALGNGLRQSIWTNFSSRFHIPQVAEFYG
ATECNCSLGNFDSQVGACGFNSRILSFVYPIRLVRVNEDTMELIRGPDGVCIPCQPGEPG
QLVGRIIQKDPLRRFDGYLNQGANNKKIAKDVFKKGDQAYLTGDVLVMDELGYLYFRDRT
GDTFRWKGENVSTTGVEGTLSRLLDMADVAVYGVEVPGTEGRAGMAAVASPTGNCDLERF
AQVLEKELPLYARPIFLRLLPELHKTGTYKFQKTELRKEGFDPAIVKDPLFYLDAQKGRY
VPLDQEAYSRIQAGEEKL
|
| Enzyme 80 Number of Residues |
378 |
| Enzyme 80 Molecular Weight |
42622.5 |
| Enzyme 80 Theoretical pI |
7.60 |
| Enzyme 80 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 80 General Function |
Involved in catalytic activity |
| Enzyme 80 Specific Function |
Not Available |
| Enzyme 80 Pathways |
Not Available |
| Enzyme 80 Reactions |
Not Available |
| Enzyme 80 Pfam Domain Function |
|
| Enzyme 80 Signals |
|
| Enzyme 80 Transmembrane Regions |
|
| Enzyme 80 Essentiality |
Not Available |
| Enzyme 80 GenBank ID Protein |
193786687  |
| Enzyme 80 UniProtKB/Swiss-Prot ID |
B3KQE8  |
| Enzyme 80 UniProtKB/Swiss-Prot Entry Name |
B3KQE8_HUMAN  |
| Enzyme 80 PDB ID |
Not Available |
| Enzyme 80 Cellular Location |
Not Available |
| Enzyme 80 Gene Sequence |
>1137 bp
ATGGCTGCCCTGGTGTACTATGGATTCCGCATGCGGCCCAACGACATCGTCTATGACTGC
CTCCCCCTCTACCACTCAGCAGGAAACATCGTGGGAATCGGCCAGTGCCTGCTGCATGGC
ATGACGGTGGTGATTCGGAAGAAGTTCTCAGCCTCCCGGTTCTGGGACGATTGTATCAAG
TACAACTGCACGATTGTGCAGTACATTGGTGAACTGTGCCGCTACCTCCTGAACCAGCCA
CCGCGGGAGGCAGAAAACCAGCACCAGGTTCGCATGGCACTAGGCAATGGCCTCCGGCAG
TCCATCTGGACCAACTTTTCCAGCCGCTTCCACATACCCCAGGTGGCTGAGTTCTACGGG
GCCACAGAGTGCAACTGTAGCCTGGGCAACTTCGACAGCCAGGTGGGGGCCTGTGGTTTC
AATAGCCGCATCCTGTCCTTCGTGTACCCCATCCGGTTGGTACGTGTCAACGAGGACACC
ATGGAGCTGATCCGGGGGCCCGACGGCGTCTGCATTCCCTGCCAGCCAGGTGAGCCGGGC
CAGCTGGTGGGCCGCATCATCCAGAAAGACCCCCTGCGCCGCTTCGATGGCTACCTCAAC
CAGGGCGCCAACAACAAGAAGATTGCCAAGGATGTCTTCAAGAAGGGGGACCAGGCCTAC
CTTACTGGTGATGTGCTGGTGATGGACGAGCTGGGCTACCTGTACTTCCGAGACCGCACT
GGGGACACGTTCCGCTGGAAAGGTGAGAACGTGTCCACCACCGGGGTGGAAGGCACACTC
AGCCGCCTGCTGGACATGGCTGACGTGGCCGTGTATGGTGTCGAGGTGCCAGGGACCGAG
GGCCGTGCCGGAATGGCTGCTGTGGCCAGCCCCACTGGCAACTGTGACCTGGAGCGCTTT
GCTCAGGTCTTGGAGAAGGAACTGCCCCTGTATGCGCGCCCCATCTTCCTGCGCCTCCTG
CCTGAGCTGCACAAAACAGGAACCTACAAGTTCCAGAAGACAGAGCTACGGAAGGAGGGC
TTTGACCCGGCTATTGTGAAAGACCCGCTGTTCTATCTAGATGCCCAGAAGGGCCGCTAC
GTCCCGCTGGACCAAGAGGCCTACAGCCGCATCCAGGCAGGCGAGGAGAAGCTGTGA
|
| Enzyme 80 GenBank Gene ID |
AK074831  |
| Enzyme 80 GeneCard ID |
Not Available |
| Enzyme 80 GenAtlas ID |
Not Available |
| Enzyme 80 HGNC ID |
HGNC:10998  |
| Enzyme 80 Chromosome Location |
Not Available |
| Enzyme 80 Locus |
Not Available |
| Enzyme 80 SNPs |
Not Available |
| Enzyme 80 General References |
Not Available |
| Enzyme 80 Metabolite References |
Not Available |
|
Enzyme 81
[top]
|
| Enzyme 81 ID |
17735 |
| Enzyme 81 Name |
cDNA FLJ50069, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-) |
| Enzyme 81 Synonyms |
- SubName: cDNA, FLJ78834, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-)
|
| Enzyme 81 Gene Name |
Not Available |
| Enzyme 81 Protein Sequence |
>cDNA FLJ50069, highly similar to Long-chain fatty acid transport protein 1 (EC 6.2.1.-)
MRAPGAGAASVVSLALLWLLGLPWTWSAAAALGVYVGSGGWRFLRIVCKTARRDLFGLSV
LIRVRLELRRHQRAGHTIPRIFQAVVQRQPERLALVDAGTGECWTFAQLDAYSNAVANLF
RQLGFAPGDVVAIFLEGRPEFVGLWLGLAKAGMEAALLNVNLRREPLAFCLGTSGAKALI
FGGEMVAGEARRGHQVGGDPGLAPGRAGRCCAPGLGRRPPWTWA
|
| Enzyme 81 Number of Residues |
224 |
| Enzyme 81 Molecular Weight |
23992.8 |
| Enzyme 81 Theoretical pI |
11.40 |
| Enzyme 81 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 81 General Function |
Involved in catalytic activity |
| Enzyme 81 Specific Function |
Not Available |
| Enzyme 81 Pathways |
Not Available |
| Enzyme 81 Reactions |
Not Available |
| Enzyme 81 Pfam Domain Function |
|
| Enzyme 81 Signals |
|
| Enzyme 81 Transmembrane Regions |
|
| Enzyme 81 Essentiality |
Not Available |
| Enzyme 81 GenBank ID Protein |
221039896  |
| Enzyme 81 UniProtKB/Swiss-Prot ID |
B7Z225  |
| Enzyme 81 UniProtKB/Swiss-Prot Entry Name |
B7Z225_HUMAN  |
| Enzyme 81 PDB ID |
Not Available |
| Enzyme 81 Cellular Location |
Not Available |
| Enzyme 81 Gene Sequence |
>675 bp
ATGCGGGCTCCGGGTGCGGGCGCGGCCTCGGTGGTCTCGCTGGCGCTGTTGTGGCTGCTG
GGGCTGCCGTGGACCTGGAGCGCGGCAGCGGCGCTCGGCGTGTACGTGGGCAGCGGCGGC
TGGCGCTTCCTGCGCATCGTCTGCAAGACCGCGAGGCGAGACCTCTTCGGTCTCTCTGTG
CTGATCCGCGTGCGCCTGGAGCTGCGGCGGCACCAGCGTGCCGGCCACACCATCCCGCGC
ATCTTTCAGGCGGTAGTGCAGCGACAGCCCGAGCGCCTGGCGCTGGTGGATGCCGGGACC
GGCGAGTGCTGGACCTTTGCGCAGCTGGACGCCTACTCCAATGCGGTAGCCAACCTCTTC
CGCCAGCTGGGCTTCGCGCCGGGCGACGTGGTGGCCATCTTCCTGGAGGGCCGGCCGGAG
TTCGTGGGGCTGTGGCTGGGCCTGGCCAAGGCGGGCATGGAGGCCGCGCTGCTCAACGTG
AACCTGCGGCGCGAGCCCCTGGCCTTCTGCCTGGGCACCTCGGGCGCTAAGGCCCTGATC
TTTGGAGGAGAAATGGTGGCGGGTGAGGCCAGGCGTGGGCATCAGGTGGGCGGGGACCCA
GGACTGGCCCCTGGGCGGGCGGGGAGATGCTGCGCCCCAGGCCTCGGAAGGCGGCCGCCC
TGGACGTGGGCATGA
|
| Enzyme 81 GenBank Gene ID |
AK294238  |
| Enzyme 81 GeneCard ID |
Not Available |
| Enzyme 81 GenAtlas ID |
Not Available |
| Enzyme 81 HGNC ID |
Not Available |
| Enzyme 81 Chromosome Location |
Not Available |
| Enzyme 81 Locus |
Not Available |
| Enzyme 81 SNPs |
Not Available |
| Enzyme 81 General References |
Not Available |
| Enzyme 81 Metabolite References |
Not Available |
|
Enzyme 82
[top]
|
| Enzyme 82 ID |
21032 |
| Enzyme 82 Name |
S-acyl fatty acid synthase thioesterase, medium chain |
| Enzyme 82 Synonyms |
- Oleoyl-ACP hydrolase
- Thioesterase II
- Thioesterase domain-containing protein 1
|
| Enzyme 82 Gene Name |
OLAH |
| Enzyme 82 Protein Sequence |
>S-acyl fatty acid synthase thioesterase, medium chain
MERGDQPKRTRNENIFNCLYKNPEATFKLICFPWMGGGSTHFAKWGQDTHDLLEVHSLRL
PGRESRVEEPLENDISQLVDEVVCALQPVIQDKPFAFFGHSMGSYIAFRTALGLKENNQP
EPLHLFLSSATPVHSKAWHRIPKDDELSEEQISHYLMEFGGTPKHFAEAKEFVKQCSPII
RADLNIVRSCTSNVPSKAVLSCDLTCFVGSEDIAKDMEAWKDVTSGNAKIYQLPGGHFYL
LDPANEKLIKNYIIKCLEVSSISNF
|
| Enzyme 82 Number of Residues |
265 |
| Enzyme 82 Molecular Weight |
29930.8 |
| Enzyme 82 Theoretical pI |
6.17 |
| Enzyme 82 GO Classification |
| Function |
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 82 General Function |
Involved in biosynthetic process |
| Enzyme 82 Specific Function |
In fatty acid biosynthesis chain termination and release of the free fatty acid product is achieved by hydrolysis of the thio ester by a thioesterase I, a component of the fatty acid synthetase complex. The chain length of the released fatty acid is usually C16. However, in the mammary glands of non-ruminant mammals, and in the uropygial gland of certain waterfowl there exists a second thioesterase which releases medium-chain length fatty acids (C8 to C2) |
| Enzyme 82 Pathways |
Not Available |
| Enzyme 82 Reactions |
- an oleoyl-[acyl-carrier protein] + H2O = an [acyl-carrier protein] + oleate [RN:R02814]
|
| Enzyme 82 Pfam Domain Function |
|
| Enzyme 82 Signals |
|
| Enzyme 82 Transmembrane Regions |
|
| Enzyme 82 Essentiality |
Not Available |
| Enzyme 82 GenBank ID Protein |
7023364  |
| Enzyme 82 UniProtKB/Swiss-Prot ID |
Q9NV23  |
| Enzyme 82 UniProtKB/Swiss-Prot Entry Name |
SAST_HUMAN  |
| Enzyme 82 PDB ID |
Not Available |
| Enzyme 82 Cellular Location |
Not Available |
| Enzyme 82 Gene Sequence |
>798 bp
ATGGAGAGAGGAGACCAACCTAAGAGAACCAGGAATGAAAACATTTTCAACTGCTTATAC
AAAAACCCTGAGGCAACTTTTAAGCTGATTTGCTTTCCCTGGATGGGAGGTGGCTCCACT
CATTTTGCCAAATGGGGCCAAGATACTCATGATTTGCTGGAAGTGCACTCCTTAAGGCTT
CCTGGAAGAGAAAGCAGAGTTGAAGAACCTCTTGAAAATGACATCTCCCAGTTAGTTGAT
GAAGTTGTTTGTGCTCTGCAGCCAGTCATCCAGGATAAACCATTTGCATTTTTTGGCCAC
AGTATGGGATCCTACATTGCTTTTAGGACTGCACTAGGTCTAAAAGAAAACAATCAACCA
GAACCATTGCATTTATTTTTGTCAAGTGCAACTCCTGTACATTCAAAGGCCTGGCATCGC
ATTCCCAAAGATGATGAATTGTCAGAAGAACAAATAAGTCATTACCTTATGGAATTTGGA
GGCACCCCCAAGCATTTTGCTGAAGCCAAGGAATTTGTGAAACAATGTAGTCCCATCATA
AGGGCAGATCTGAACATTGTTAGAAGTTGCACCTCTAACGTACCATCTAAGGCTGTTCTT
TCCTGTGACTTGACATGTTTTGTTGGATCTGAAGACATAGCAAAGGACATGGAAGCCTGG
AAAGATGTAACCAGTGGAAATGCTAAAATTTACCAGCTTCCAGGGGGTCACTTTTATCTT
CTGGATCCTGCGAACGAGAAATTAATCAAGAACTACATAATCAAGTGTCTAGAAGTATCA
TCGATATCCAATTTTTAG
|
| Enzyme 82 GenBank Gene ID |
AK001844  |
| Enzyme 82 GeneCard ID |
OLAH  |
| Enzyme 82 GenAtlas ID |
OLAH  |
| Enzyme 82 HGNC ID |
HGNC:25625  |
| Enzyme 82 Chromosome Location |
1 |
| Enzyme 82 Locus |
10p13 |
| Enzyme 82 SNPs |
SNPJam Report  |
| Enzyme 82 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J: The DNA sequence and comparative analysis of human chromosome 10. Nature. 2004 May 27;429(6990):375-81. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 82 Metabolite References |
Not Available |