|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5287 |
| Enzyme 1 Name |
Calcium-dependent phospholipase A2 |
| Enzyme 1 Synonyms |
- Group V phospholipase A2
- PLA2-10
- Phosphatidylcholine 2-acylhydrolase 5
|
| Enzyme 1 Gene Name |
PLA2G5 |
| Enzyme 1 Protein Sequence |
>Calcium-dependent phospholipase A2
MKGLLPLAWFLACSVPAVQGGLLDLKSMIEKVTGKNALTNYGFYGCYCGWGGRGTPKDGT
DWCCWAHDHCYGRLEEKGCNIRTQSYKYRFAWGVVTCEPGPFCHVNLCACDRKLVYCLKR
NLRSYNPQYQYFPNILCS
|
| Enzyme 1 Number of Residues |
138 |
| Enzyme 1 Molecular Weight |
15674.1 |
| Enzyme 1 Theoretical pI |
8.48 |
| Enzyme 1 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 1 General Function |
Involved in phospholipase A2 activity |
| Enzyme 1 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 1 Pathways |
|
| Enzyme 1 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
10862735  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
P39877  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PA2G5_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>417 bp
ATGAAAGGCCTCCTCCCACTGGCTTGGTTCCTGGCTTGTAGTGTGCCTGCTGTGCAAGGA
GGCTTGCTGGACCTAAAATCAATGATCGAGAAGGTGACAGGGAAGAACGCCCTGACAAAC
TACGGCTTCTACGGCTGTTACTGCGGCTGGGGCGGCCGAGGAACCCCCAAGGATGGCACC
GATTGGTGCTGTTGGGCGCATGACCACTGCTATGGGCGGCTGGAGGAGAAGGGCTGCAAC
ATTCGCACACAGTCCTACAAATACAGATTCGCGTGGGGCGTGGTCACCTGCGAGCCCGGG
CCCTTCTGCCATGTGAACCTCTGTGCCTGTGACCGGAAGCTCGTCTACTGCCTCAAGAGA
AACCTACGGAGCTACAACCCACAGTACCAATACTTTCCCAACATCCTCTGCTCCTAG
|
| Enzyme 1 GenBank Gene ID |
AL158172  |
| Enzyme 1 GeneCard ID |
PLA2G5  |
| Enzyme 1 GenAtlas ID |
PLA2G5  |
| Enzyme 1 HGNC ID |
HGNC:9038  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
1p36-p34 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5288 |
| Enzyme 2 Name |
Group IIF secretory phospholipase A2 |
| Enzyme 2 Synonyms |
- GIIF sPLA2
- sPLA2-IIF
- Phosphatidylcholine 2-acylhydrolase 2F
|
| Enzyme 2 Gene Name |
PLA2G2F |
| Enzyme 2 Protein Sequence |
>Group IIF secretory phospholipase A2
MKKFFTVAILAGSVLSTAHGSLLNLKAMVEAVTGRSAILSFVGYGCYCGLGGRGQPKDEV
DWCCHAHDCCYQELFDQGCHPYVDHYDHTIENNTEIVCSDLNKTECDKQTCMCDKNMVLC
LMNQTYREEYRGFLNVYCQGPTPNCSIYEPPPEEVTCSHQSPAPPAPP
|
| Enzyme 2 Number of Residues |
168 |
| Enzyme 2 Molecular Weight |
18658.0 |
| Enzyme 2 Theoretical pI |
4.94 |
| 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. Hydrolyzes phosphatidylglycerol versus phosphatidylcholine with a 15-fold preference |
| 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 |
12276060  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
Q9BZM2  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
PA2GF_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>507 bp
ATGAAGAAGTTCTTCACCGTGGCCATCCTTGCTGGCAGCGTTCTGTCCACAGCTCACGGC
AGCCTGCTCAACCTGAAGGCCATGGTGGAGGCCGTCACAGGGAGGAGCGCCATCCTGTCC
TTCGTGGGCTACGGTTGCTACTGTGGGCTGGGGGGCCGTGGCCAGCCCAAGGATGAGGTG
GACTGGTGCTGCCACGCCCACGACTGCTGCTACCAGGAACTCTTTGACCAAGGCTGTCAC
CCCTATGTGGACCACTATGATCACACCATCGAGAACAACACTGAGATAGTCTGCAGTGAC
CTCAACAAGACAGAGTGTGACAAGCAGACATGCATGTGTGACAAGAACATGGTTCTGTGC
CTCATGAACCAGACGTACCGAGAGGAGTACCGTGGCTTCCTCAATGTCTACTGCCAGGGC
CCCACGCCCAACTGCAGCATCTATGAACCGCCCCCTGAGGAGGTCACCTGCAGTCACCAA
TCCCCAGCGCCCCCCGCCCCTCCCTAG
|
| Enzyme 2 GenBank Gene ID |
AF306566  |
| Enzyme 2 GeneCard ID |
PLA2G2F  |
| Enzyme 2 GenAtlas ID |
PLA2G2F  |
| Enzyme 2 HGNC ID |
HGNC:30040  |
| Enzyme 2 Chromosome Location |
1 |
| Enzyme 2 Locus |
1p35 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 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 2 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5289 |
| Enzyme 3 Name |
Cytosolic phospholipase A2 |
| Enzyme 3 Synonyms |
- cPLA2
- Phospholipase A2 group IVA
- Phospholipase A2
- Phosphatidylcholine 2-acylhydrolase
- Lysophospholipase
|
| Enzyme 3 Gene Name |
PLA2G4A |
| Enzyme 3 Protein Sequence |
>Cytosolic phospholipase A2
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGAFGDMLDTPDPYVELFISTTPDSRKRT
RHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFTVSSMKVGEKKEV
PFIFNQVTEMVLEMSLEVCSCPDLRFSMALCDQEKTFRQQRKEHIRESMKKLLGPKNSEG
LHSARDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSH
PDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIG
ETLIHNRMNTTLSSLKEKVNTAQCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYG
TFMAPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQSRGSTMEEE
LENITTKHIVSNDSSDSDDESHEPKGTENEDAGSDYQSDNQASWIHRMIMALVSDSALFN
TREGRAGKVHNFMLGLNLNTSYPLSPLSDFATQDSFDDDELDAAVADPDEFERIYEPLDV
KSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDSSPPFKELLLAEKWAKMN
KLPFPKIDPYVFDREGLKECYVFKPKNPDMEKDCPTIIHFVLANINFRKYKAPGVPRETE
EEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMHFNTLNNIDVIKEAMVESIEYRR
QNPSRCSVSLSNVEARRFFNKEFLSKPKA
|
| Enzyme 3 Number of Residues |
749 |
| Enzyme 3 Molecular Weight |
85210.2 |
| Enzyme 3 Theoretical pI |
5.03 |
| Enzyme 3 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 3 General Function |
Involved in metabolic process |
| Enzyme 3 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 3 Pathways |
|
| Enzyme 3 Reactions |
- 2-lysophosphatidylcholine + H2O = glycerophosphocholine + a carboxylate [RN:R07291]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
Not Available |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P47712  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
PA24A_HUMAN  |
| Enzyme 3 PDB ID |
1CJY  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 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 3 GenBank Gene ID |
M72393  |
| Enzyme 3 GeneCard ID |
PLA2G4A  |
| Enzyme 3 GenAtlas ID |
PLA2G4A  |
| Enzyme 3 HGNC ID |
HGNC:9035  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
1q25 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 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 3 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5290 |
| Enzyme 4 Name |
Phospholipase A2 |
| Enzyme 4 Synonyms |
- Group IB phospholipase A2
- Phosphatidylcholine 2-acylhydrolase 1B
|
| Enzyme 4 Gene Name |
PLA2G1B |
| Enzyme 4 Protein Sequence |
>Phospholipase A2
MKLLVLAVLLTVAAADSGISPRAVWQFRKMIKCVIPGSDPFLEYNNYGCYCGLGGSGTPV
DELDKCCQTHDNCYDQAKKLDSCKFLLDNPYTHTYSYSCSGSAITCSSKNKECEAFICNC
DRNAAICFSKAPYNKAHKNLDTKKYCQS
|
| Enzyme 4 Number of Residues |
148 |
| Enzyme 4 Molecular Weight |
16359.5 |
| Enzyme 4 Theoretical pI |
7.91 |
| Enzyme 4 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in phospholipase A2 activity |
| Enzyme 4 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides |
| Enzyme 4 Pathways |
|
| Enzyme 4 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
Not Available |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
P04054  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
PA21B_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>447 bp
ATGAAACTCCTTGTGCTAGCTGTGCTGCTCACAGTGGCCGCCGCCGACAGCGGCATCAGC
CCTCGGGCCGTGTGGCAGTTCCGCAAAATGATCAAGTGCGTGATCCCGGGGAGTGACCCC
TTCTTGGAATACAACAACTACGGCTGCTACTGTGGCTTGGGGGGCTCAGGCACCCCCGTG
GATGAACTGGACAAGTGCTGCCAGACACATGACAACTGCTATGACCAGGCCAAGAAGCTG
GACAGCTGTAAATTTCTGCTGGACAACCCGTACACCCACACCTATTCATACTCGTGCTCT
GGCTCGGCAATCACCTGTAGCAGCAAAAACAAAGAGTGTGAGGCCTTCATTTGCAACTGC
GACCGCAACGCTGCCATCTGCTTTTCAAAAGCTCCATATAACAAGGCACACAAGAACCTG
GACACCAAGAAGTATTGTCAGAGTTGA
|
| Enzyme 4 GenBank Gene ID |
M21054  |
| Enzyme 4 GeneCard ID |
PLA2G1B  |
| Enzyme 4 GenAtlas ID |
PLA2G1B  |
| Enzyme 4 HGNC ID |
HGNC:9030  |
| Enzyme 4 Chromosome Location |
1 |
| Enzyme 4 Locus |
12q23-q24.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 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 4 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5291 |
| Enzyme 5 Name |
Group XIIB secretory phospholipase A2-like protein |
| Enzyme 5 Synonyms |
- Group XIII secretory phospholipase A2-like protein
- GXIII sPLA2-like
- sPLA2-GXIIB
- GXIIB
|
| Enzyme 5 Gene Name |
PLA2G12B |
| Enzyme 5 Protein Sequence |
>Group XIIB secretory phospholipase A2-like protein
MKLASGFLVLWLSLGGGLAQSDTSPDTEESYSDWGLRHLRGSFESVNSYFDSFLELLGGK
NGVCQYRCRYGKAPMPRPGYKPQEPNGCGSYFLGLKVPESMDLGIPAMTKCCNQLDVCYD
TCGANKYRCDAKFRWCLHSICSDLKRSLGFVSKVEAACDSLVDTVFNTVWTLGCRPFMNS
QRAACICAEEEKEEL
|
| Enzyme 5 Number of Residues |
195 |
| Enzyme 5 Molecular Weight |
21658.5 |
| Enzyme 5 Theoretical pI |
5.81 |
| 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
- primary metabolic process
|
| Component |
|
|
| Enzyme 5 General Function |
Involved in phospholipase A2 activity |
| Enzyme 5 Specific Function |
Not known; does not seem to have catalytic activity |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
15824793  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9BX93  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
PG12B_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>588 bp
ATGAAGCTGGCCAGTGGCTTCTTGGTTTTGTGGCTCAGCCTTGGGGGTGGCCTGGCTCAG
AGCGACACGAGCCCTGACACGGAGGAGTCCTATTCAGACTGGGGCCTTCGGCACCTCCGG
GGAAGCTTTGAATCCGTCAATAGCTACTTCGATTCTTTTCTGGAGCTGCTGGGAGGGAAG
AATGGAGTCTGTCAGTACAGGTGCCGATATGGAAAGGCACCAATGCCCAGACCTGGCTAC
AAGCCCCAAGAGCCCAATGGCTGCGGCTCCTATTTCCTGGGTCTCAAGGTACCAGAAAGT
ATGGACTTGGGCATTCCAGCAATGACAAAGTGCTGCAACCAGCTGGATGTCTGTTATGAC
ACTTGCGGTGCCAACAAATATCGCTGTGATGCAAAATTCCGATGGTGTCTCCACTCGATC
TGCTCTGACCTTAAGCGGAGTCTGGGCTTTGTCTCCAAAGTGGAAGCAGCCTGTGATTCC
CTGGTTGACACTGTGTTCAACACCGTGTGGACCTTGGGCTGCCGCCCCTTTATGAATAGT
CAGCGGGCAGCTTGCATCTGTGCAGAGGAGGAGAAGGAAGAGTTATGA
|
| Enzyme 5 GenBank Gene ID |
AF339053  |
| Enzyme 5 GeneCard ID |
PLA2G12B  |
| Enzyme 5 GenAtlas ID |
PLA2G12B  |
| Enzyme 5 HGNC ID |
HGNC:18555  |
| Enzyme 5 Chromosome Location |
1 |
| Enzyme 5 Locus |
10q22.1 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Rouault M, Bollinger JG, Lazdunski M, Gelb MH, Lambeau G: Novel mammalian group XII secreted phospholipase A2 lacking enzymatic activity. Biochemistry. 2003 Oct 7;42(39):11494-503. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed
]
|
| Enzyme 5 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
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 |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
5294 |
| Enzyme 7 Name |
Group IIE secretory phospholipase A2 |
| Enzyme 7 Synonyms |
- GIIE sPLA2
- sPLA2-IIE
- Phosphatidylcholine 2-acylhydrolase 2E
|
| Enzyme 7 Gene Name |
PLA2G2E |
| Enzyme 7 Protein Sequence |
>Group IIE secretory phospholipase A2
MKSPHVLVFLCLLVALVTGNLVQFGVMIEKMTGKSALQYNDYGCYCGIGGSHWPVDQTDW
CCHAHDCCYGRLEKLGCEPKLEKYLFSVSERGIFCAGRTTCQRLTCECDKRAALCFRRNL
GTYNRKYAHYPNKLCTGPTPPC
|
| Enzyme 7 Number of Residues |
142 |
| Enzyme 7 Molecular Weight |
15988.5 |
| Enzyme 7 Theoretical pI |
8.28 |
| Enzyme 7 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 7 General Function |
Involved in phospholipase A2 activity |
| Enzyme 7 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 7 Pathways |
|
| Enzyme 7 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9NZK7  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
PA2GE_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 Gene Sequence |
>429 bp
ATGAAATCTCCCCACGTGCTGGTGTTCCTTTGCCTCCTGGTGGCTCTGGTCACCGGGAAC
CTGGTTCAGTTTGGGGTGATGATCGAGAAGATGACAGGCAAGTCCGCCCTGCAGTACAAC
GACTATGGCTGTTACTGCGGCATCGGTGGCTCCCACTGGCCGGTGGACCAGACTGACTGG
TGCTGCCACGCCCACGACTGCTGCTACGGGCGTCTGGAGAAGCTGGGCTGTGAGCCCAAA
CTGGAAAAGTATCTTTTCTCTGTCAGCGAACGTGGCATTTTCTGCGCCGGCAGGACCACC
TGCCAGCGGCTGACCTGCGAGTGTGACAAGAGGGCTGCCCTCTGCTTTCGCCGCAACCTG
GGCACCTACAACCGCAAATATGCCCATTATCCCAACAAGCTGTGCACCGGGCCCACCCCG
CCCTGCTGA
|
| Enzyme 7 GenBank Gene ID |
AF189279  |
| Enzyme 7 GeneCard ID |
PLA2G2E  |
| Enzyme 7 GenAtlas ID |
PLA2G2E  |
| Enzyme 7 HGNC ID |
HGNC:13414  |
| Enzyme 7 Chromosome Location |
1 |
| Enzyme 7 Locus |
1p36.13 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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 7 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
5297 |
| Enzyme 8 Name |
85 kDa calcium-independent phospholipase A2 |
| Enzyme 8 Synonyms |
- CaI-PLA2
- iPLA2
- Group VI phospholipase A2
- GVI PLA2
|
| Enzyme 8 Gene Name |
PLA2G6 |
| Enzyme 8 Protein Sequence |
>85 kDa calcium-independent phospholipase A2
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRLVTRKAILTLLRTVGAEYCFPPIHG
VPAEQGSAAPHHPFSLERAQPPPISLNNLELQDLMHISRARKPAFILGSMRDEKRTHDHL
LCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGM
YFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFR
NYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNP
TLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKT
VFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVN
ALWETEVYIYEHREEFQKLIQLLLSP
|
| Enzyme 8 Number of Residues |
806 |
| Enzyme 8 Molecular Weight |
89902.3 |
| Enzyme 8 Theoretical pI |
7.28 |
| Enzyme 8 GO Classification |
| Function |
| — |
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 8 General Function |
Involved in metabolic process |
| Enzyme 8 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 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 |
3142700  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O60733  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PA2G6_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 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 8 GenBank Gene ID |
AF064594  |
| Enzyme 8 GeneCard ID |
PLA2G6  |
| Enzyme 8 GenAtlas ID |
PLA2G6  |
| Enzyme 8 HGNC ID |
HGNC:9039  |
| Enzyme 8 Chromosome Location |
2 |
| Enzyme 8 Locus |
22q13.1 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 Metabolite References |
Not Available |
|
Enzyme 9
[top]
|
| Enzyme 9 ID |
5302 |
| Enzyme 9 Name |
Group IID secretory phospholipase A2 |
| Enzyme 9 Synonyms |
- GIID sPLA2
- sPLA2-IID
- PLA2IID
- Phosphatidylcholine 2-acylhydrolase 2D
- Secretory-type PLA, stroma-associated homolog
|
| Enzyme 9 Gene Name |
PLA2G2D |
| Enzyme 9 Protein Sequence |
>Group IID secretory phospholipase A2
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDAT
DWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLK
RNLDTYQKRLRFYWRPHCRGQTPGC
|
| Enzyme 9 Number of Residues |
145 |
| Enzyme 9 Molecular Weight |
16546.1 |
| Enzyme 9 Theoretical pI |
8.28 |
| Enzyme 9 GO Classification |
| Function |
- binding
- calcium ion binding
- carboxylesterase activity
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- metal ion binding
- phospholipase A2 activity
|
| Process |
- lipid catabolic process
- lipid metabolic process
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in phospholipase A2 activity |
| Enzyme 9 Specific Function |
PA2 catalyzes the calcium-dependent hydrolysis of the 2- acyl groups in 3-sn-phosphoglycerides. L-alpha-1-palmitoyl-2- linoleoyl phosphatidylethanolamine is more efficiently hydrolyzed than the other phospholipids examined |
| 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 |
5771420  |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
Q9UNK4  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PA2GD_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>438 bp
ATGGAACTTGCACTGCTGTGTGGGCTGGTGGTGATGGCTGGTGTGATTCCAATCCAGGGC
GGGATCCTGAACCTGAACAAGATGGTCAAGCAAGTGACTGGGAAAATGCCCATCCTCTCC
TACTGGCCCTACGGCTGTCACTGCGGACTAGGTGGCAGAGGCCAACCCAAAGATGCCACG
GACTGGTGCTGCCAGACCCATGACTGCTGCTATGACCACCTGAAGACCCAGGGGTGCGGC
ATCTACAAGGACTATTACAGATACAACTTTTCCCAGGGGAACATCCACTGCTCTGACAAG
GGAAGCTGGTGTGAGCAGCAGCTGTGTGCCTGTGACAAGGAGGTGGCCTTCTGCCTGAAG
CGCAACCTGGACACCTACCAGAAGCGACTGCGTTTCTACTGGCGGCCCCACTGCCGGGGG
CAGACCCCTGGGTGCTAG
|
| Enzyme 9 GenBank Gene ID |
AF112982  |
| Enzyme 9 GeneCard ID |
PLA2G2D  |
| Enzyme 9 GenAtlas ID |
PLA2G2D  |
| Enzyme 9 HGNC ID |
HGNC:9033  |
| Enzyme 9 Chromosome Location |
1 |
| Enzyme 9 Locus |
1p36.12 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 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 9 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 10
[top]
|
| Enzyme 10 ID |
5309 |
| Enzyme 10 Name |
Phospholipase D2 |
| Enzyme 10 Synonyms |
- PLD 2
- hPLD2
- Choline phosphatase 2
- PLD1C
- Phosphatidylcholine-hydrolyzing phospholipase D2
|
| Enzyme 10 Gene Name |
PLD2 |
| Enzyme 10 Protein Sequence |
>Phospholipase D2
MTATPESLFPTGDELDSSQLQMESDEVDTLKEGEDPADRMHPFLAIYELQSLKVHPLVFA
PGVPVTAQVVGTERYTSGSKVGTCTLYSVRLTHGDFSWTTKKKYRHFQELHRDLLRHKVL
MSLLPLARFAVAYSPARDAGNREMPSLPRAGPEGSTRHAASKQKYLENYLNRLLTMSFYR
NYHAMTEFLEVSQLSFIPDLGRKGLEGMIRKRSGGHRVPGLTCCGRDQVCYRWSKRWLVV
KDSFLLYMCLETGAISFVQLFDPGFEVQVGKRSTEARHGVRIDTSHRSLILKCSSYRQAR
WWAQEITELAQGPGRDFLQLHRHDSYAPPRPGTLARWFVNGAGYFAAVADAILRAQEEIF
ITDWWLSPEVYLKRPAHSDDWRLDIMLKRKAEEGVRVSILLFKEVELALGINSGYSKRAL
MLLHPNIKVMRHPDQVTLWAHHEKLLVVDQVVAFLGGLDLAYGRWDDLHYRLTDLGDSSE
SAASQPPTPRPDSPATPDLSHNQFFWLGKDYSNLITKDWVQLDRPFEDFIDRETTPRMPW
RDVGVVVHGLPARDLARHFIQRWNFTKTTKAKYKTPTYPYLLPKSTSTANQLPFTLPGGQ
CTTVQVLRSVDRWSAGTLENSILNAYLHTIRESQHFLYIENQFFISCSDGRTVLNKVGDE
IVDRILKAHKQGWCYRVYVLLPLLPGFEGDISTGGGNSIQAILHFTYRTLCRGEYSILHR
LKAAMGTAWRDYISICGLRTHGELGGHPVSELIYIHSKVLIADDRTVIIGSANINDRSLL
GKRDSELAVLIEDTETEPSLMNGAEYQAGRFALSLRKHCFGVILGANTRPDLDLRDPICD
DFFQLWQDMAESNANIYEQIFRCLPSNATRSLRTLREYVAVEPLATVSPPLARSELTQVQ
GHLVHFPLKFLEDESLLPPLGSKEGMIPLEVWT
|
| Enzyme 10 Number of Residues |
933 |
| Enzyme 10 Molecular Weight |
105986.1 |
| Enzyme 10 Theoretical pI |
7.68 |
| Enzyme 10 GO Classification |
| Function |
- binding
- catalytic activity
- lipid binding
- phosphoinositide binding
- phospholipid binding
- protein binding
|
| Process |
- cell communication
- cellular process
- metabolic process
|
| Component |
| — |
|
| Enzyme 10 General Function |
Involved in protein binding |
| Enzyme 10 Specific Function |
May have a role in signal-induced cytoskeletal regulation and/or endocytosis |
| Enzyme 10 Pathways |
|
| Enzyme 10 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
2645858  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
O14939  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
PLD2_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>2802 bp
ATGACGGCGACCCCTGAGAGCCTCTTCCCCACTGGGGACGAACTGGACTCCAGCCAGCTC
CAGATGGAGTCCGATGAGGTGGACACCCTGAAGGAGGGAGAGGACCCAGCCGACCGGATG
CACCCGTTTCTGGCCATCTATGAGCTTCAGTCTCTGAAAGTGCACCCCTTGGTGTTCGCA
CCTGGGGTCCCTGTCACAGCCCAGGTGGTGGGCACCGAAAGATATACCAGCGGATCCAAG
GTGGGAACCTGCACTCTGTATTCTGTCCGCTTGACTCACGGCGACTTTTCCTGGACAACC
AAGAAGAAATACCGTCATTTTCAGGAGCTGCATCGGGACCTCCTGAGACACAAAGTCTTG
ATGAGTCTGCTCCCTCTGGCTCGATTTGCCGTTGCCTATTCTCCAGCCCGAGATGCAGGC
AACAGAGAGATGCCCTCTCTACCCCGGGCAGGTCCTGAGGGCTCCACCAGACATGCAGCC
AGCAAACAGAAATACCTGGAGAATTACCTCAACTGTCTCTTGACCATGTCTTTCTATCGC
AACTACCATGCCATGACAGAGTTCCTGGAAGTCAGTCAGCTGTCCTTTATCCCGGACTTG
GGCCGCAAAGGACTGGAGGGGATGATCCGGAAGCGCTCAGGTGGCCACCGTGTTCCTGGC
CTCACCTGCTGTGGCCGAGACCAAGTTTGTTATCGCTGGTCCAAGAGGTGGCTGGTGGTG
AAGGACTCCTTCCTGCTGTACATGTGCCTCGAGACAGGTGCCATCTCATTTGTTCAGCTC
TTTGACCCTGGCTTTGAGGTGCAAGTGGGGAAAAGGAGCACGGAGGCACGGCACGGCGTG
CGGATCGATACCTCCCACAGGTCCTTGATTCTCAAGTGCAGCAGCTACCGGCAGGCACGG
TGGTGGGCCCAAGAGATCACTGAGCTGGCACAGGGCCCAGGCAGAGACTTCCTACAGCTG
CACCGGCATGACAGCTACGCCCCACCCCGGCCTGGGACCTTGGCCCGGTGGTTTGTGAAT
GGGGCAGGTTACTTTGCTGCTGTGGCAGATGCCATCCTTCGAGCTCAAGAGGAGATTTTC
ATCACAGACTGGTGGTTGAGTCCTGAGGTTTACCTGAAGCGTCCGGCCCATTCAGATGAC
TGGAGACTGGACATTATGCTCAAGAGGAAGGCGGAGGAAGGTGTCCGTGTGTCTATTCTG
CTGTTTAAAGAAGTGGAATTGGCCTTGGGCATCAACAGTGGCTATAGCAAGAGGGCGCTG
ATGCTGCTGCACCCCAACATAAAGGTGATGCGTCACCCAGACCAAGTGACGTTGTGGGCC
CATCATGAGAAGCTCCTGGTGGTGGACCAAGTGGTAGCATTCCTGGGGGGACTGGACCTT
GCCTATGGCCGCTGGGATGACCTGCACTACCGACTGACTGACCTTGGAGACTCCTCTGAA
TCAGCTGCCTCCCAGCCTCCCACCCCGCGCCCAGACTCACCAGCCACCCCAGACCTCTCT
CACAACCAATTCTTCTGGCTGGGCAAGGACTACAGCAATCTTATCACCAAGGACTGGGTG
CAGCTGGACCGGCCTTTCGAAGATTTCATTGACAGGGAGACGACCCCTCGGATGCCATGG
CGGGACGTTGGGGTGGTCGTCCATGGCCTACCGGCCCGGGACCTTGCCCGGCACTTCATC
CAGCGCTGGAACTTCACCAAGACCACCAAGGCCAAGTACAAGACTCCCACATACCCCTAC
CTGCTTCCCAAGTCTACCAGCACGGCCAATCAGCTCCCCTTCACACTTCCAGGAGGGCAG
TGCACCACCGTACAGGTCTTGCGATCAGTGGACCGCTGGTCAGCAGGGACTCTGGAGAAC
TCCATCCTCAATGCCTACCTGCACACCATCAGGGAGAGCCAGCACTTCCTCTACATTGAG
AATCAGTTCTTCATTAGCTGCTCAGATGGGCGGACGGTTCTGAACAAGGTGGGCGATGAG
ATTGTGGACAGAATCCTGAAGGCCCACAAACAGGGGTGGTGTTACCGAGTCTACGTGCTT
TTGCCCTTACTCCCTGGCTTCGAGGGTGACATCTCCACGGGCGGTGGCAACTCCATCCAG
GCCATTCTGCACTTTACTTACAGGACCCTGTGTCGTGGGGAGTATTCAATCCTGCATCGC
CTTAAAGCAGCCATGGGGACAGCATGGCGGGACTATATTTCCATCTGCGGGCTTCGTACA
CACGGAGAGCTGGGCGGGCACCCCGTCTCGGAGCTCATCTACATCCACAGCAAGGTGCTC
ATCGCAGATGACCGGACAGTCATCATTGGTTCTGCAAACATCAATGACCGGAGCTTGCTG
GGGAAGCGGGACAGTGAGCTGGCCGTGCTGATCGAGGACACAGAGACGGAACCATCCCTC
ATGAATGGGGCAGAGTATCAGGCGGGCAGGTTTGCCTTGAGTCTGCGGAAGCACTGCTTC
GGTGTGATTCTTGGAGCAAATACCCGGCCAGACTTGGATCTCCGAGACCCCATCTGTGAT
GACTTCTTCCAGTTGTGGCAAGACATGGCTGAGAGCAACGCCAATATCTATGAGCAGATC
TTCCGCTGCCTGCCATCCAATGCCACGCGTTCCCTGCGGACTCTCCGGGAGTACGTGGCC
GTGGAGCCCTTGGCCACGGTCAGTCCCCCCTTGGCTCGGTCTGAGCTCACCCAGGTCCAG
GGCCACCTGGTCCACTTCCCCCTCAAGTTCCTAGAGGATGAGTCTTTGCTGCCCCCGCTG
GGTAGCAAGGAGGGCATGATCCCCCTAGAAGTGTGGACATAG
|
| Enzyme 10 GenBank Gene ID |
AF033850  |
| Enzyme 10 GeneCard ID |
PLD2  |
| Enzyme 10 GenAtlas ID |
PLD2  |
| Enzyme 10 HGNC ID |
HGNC:9068  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
17p13.1 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed
]
- Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Divecha N, Roefs M, Halstead JR, D'Andrea S, Fernandez-Borga M, Oomen L, Saqib KM, Wakelam MJ, D'Santos C: Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity. EMBO J. 2000 Oct 16;19(20):5440-9. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 10 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
5310 |
| Enzyme 11 Name |
Phosphatidylethanolamine N-methyltransferase |
| Enzyme 11 Synonyms |
- PEAMT
- PEMT
- PEMT2
|
| Enzyme 11 Gene Name |
PEMT |
| Enzyme 11 Protein Sequence |
>Phosphatidylethanolamine N-methyltransferase
MTRLLGYVDPLDPSFVAAVITITFNPLYWNVVARWEHKTRKLSRAFGSPYLACYSLSVTI
LLLNFLRSHCFTQAMLSQPRMESLDTPAAYSLGLALLGLGVVLVLSSFFALGFAGTFLGD
YFGILKEARVTVFPFNILDNPMYWGSTANYLGWAIMHASPTGLLLTVLVALTYIVALLYE
EPFTAEIYRQKASGSHKRS
|
| Enzyme 11 Number of Residues |
199 |
| Enzyme 11 Molecular Weight |
22133.6 |
| Enzyme 11 Theoretical pI |
8.96 |
| Enzyme 11 GO Classification |
| Function |
- N-methyltransferase activity
- catalytic activity
- methyltransferase activity
- transferase activity
- transferase activity, transferring one-carbon groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 11 General Function |
Involved in N-methyltransferase activity |
| Enzyme 11 Specific Function |
Catalyzes three sequential methylation of phosphatidylethanolamine (PE) by AdoMet, thus producing phosphatidylcholine (PC) |
| Enzyme 11 Pathways |
- Phospholipid Synthesis (map00564
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 11 Reactions |
- S-adenosyl-L-methionine + phosphatidylethanolamine = S-adenosyl-L-homocysteine + phosphatidyl-N-methylethanolamine [RN:R02056]
|
| Enzyme 11 Pfam Domain Function |
|
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
- 13-33
46-66
94-114
158-178
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
5459516  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9UBM1  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
PEMT_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>600 bp
ATGACCCGGCTGCTGGGCTACGTGGACCCCCTGGATCCCAGCTTTGTGGCTGCCGTCATC
ACCATCACCTTCAATCCGCTCTACTGGAATGTGGTTGCACGATGGGAACACAAGACCCGC
AAGCTGAGCAGGGCCTTCGGATCCCCCTACCTGGCCTGCTACTCTCTAAGCATCACCATC
CTGCTCCTGAACTTCCTGCGCTCGCACTGCTTCACGCAGGCCATGCTGAGCCAGCCCAGG
ATGGAGAGCCTGGACACCCCCGCGGCCTACAGCCTGGGCCTCGCGCTCCTGGGACTGGGC
GTCGTGCTCGTGCTCTCCAGCTTCTTTGCACTGGGGTTCGCTGGAACTTTCCTAGGTGAT
TACTTCGGGATCCTCAAGGAGGCGAGAGTGACCGTGTTCCCCTTCAACATCCTGGACAAC
CCCATGTACTGGGGAAGCACAGCCAACTACCTGGGCTGGGCCATCATGCACGCCAGCCCC
ACGGGCCTGCTCCTGACGGTGCTGGTGGCCCTCACCTACATAATGGCTCTCCTATACGAA
GAGCCCTTCACCGCTGAGATCTACCGGCAGAAAGCCTCCGGGTCCCACAAGAGGAGCTGA
|
| Enzyme 11 GenBank Gene ID |
AB029821  |
| Enzyme 11 GeneCard ID |
PEMT  |
| Enzyme 11 GenAtlas ID |
PEMT  |
| Enzyme 11 HGNC ID |
HGNC:8830  |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
17p11.2 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Walkey CJ, Shields DJ, Vance DE: Identification of three novel cDNAs for human phosphatidylethanolamine N-methyltransferase and localization of the human gene on chromosome 17p11.2. Biochim Biophys Acta. 1999 Jan 4;1436(3):405-12. [PubMed
]
- Shields DJ, Agellon LB, Vance DE: Structure, expression profile and alternative processing of the human phosphatidylethanolamine N-methyltransferase (PEMT) gene. Biochim Biophys Acta. 2001 May 31;1532(1-2):105-14. [PubMed
]
- Hu RM, Han ZG, Song HD, Peng YD, Huang QH, Ren SX, Gu YJ, Huang CH, Li YB, Jiang CL, Fu G, Zhang QH, Gu BW, Dai M, Mao YF, Gao GF, Rong R, Ye M, Zhou J, Xu SH, Gu J, Shi JX, Jin WR, Zhang CK, Wu TM, Huang GY, Chen Z, Chen MD, Chen JL: Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning. Proc Natl Acad Sci U S A. 2000 Aug 15;97(17):9543-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Resseguie M, Song J, Niculescu MD, da Costa KA, Randall TA, Zeisel SH: Phosphatidylethanolamine N-methyltransferase (PEMT) gene expression is induced by estrogen in human and mouse primary hepatocytes. FASEB J. 2007 Aug;21(10):2622-32. Epub 2007 Apr 24. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
|
| Enzyme 11 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 12
[top]
|
| Enzyme 12 ID |
5311 |
| Enzyme 12 Name |
Phospholipase D1 |
| Enzyme 12 Synonyms |
- PLD 1
- hPLD1
- Choline phosphatase 1
- Phosphatidylcholine-hydrolyzing phospholipase D1
|
| Enzyme 12 Gene Name |
PLD1 |
| Enzyme 12 Protein Sequence |
>Phospholipase D1
MSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEGEEVDYDVSPSDPKIQEVYIPFSA
IYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRVPSINLYTIELTHGEFKWQVKRKF
KHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEPREMPSLPRSSENMIREEQFLGRR
KQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDLGPKGIEGMIMKRSGGHRIPGLNC
CGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLLVDKEFKIKVGKKETETKYGIRID
NLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKDHRFGSYAAIQENALAKWYVNAKG
YFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGNRWRLDCILKRKAQQGVRIFIMLY
KEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSSTVYLWAHHEKLVIIDQSVAFVGGI
DLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAMESMESLRLKDKNEPVQNLPIQKS
IDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSISSIDSTSSYFNHYRSHHNLIHGL
KPHFKLFHPSSESEQGLTRPHADTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQL
DKPFADFIDRYSTPRMPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLL
PKSQTTAHELRYQVPGSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIE
NQFFISCADDKVVFNKIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQ
AIMHFNYRTMCRGENSILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLL
IADDNTVIIGSANINDRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCF
RVVLGYLDDPSEDIQDPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFI
NKPVLAKEDPIRAEEELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
|
| Enzyme 12 Number of Residues |
1074 |
| Enzyme 12 Molecular Weight |
124183.1 |
| Enzyme 12 Theoretical pI |
9.07 |
| Enzyme 12 GO Classification |
| Function |
- binding
- catalytic activity
- lipid binding
- phosphoinositide binding
- phospholipid binding
- protein binding
|
| Process |
- cell communication
- cellular process
- metabolic process
|
| Component |
| — |
|
| Enzyme 12 General Function |
Involved in protein binding |
| Enzyme 12 Specific Function |
Implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. May be involved in the regulation of perinuclear intravesicular membrane traffic |
| Enzyme 12 Pathways |
|
| Enzyme 12 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| 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 |
Q13393  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PLD1_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>3225 bp
ATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAATTGCTGCTGAC
ATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGGGAGAGGAGGTA
GACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCCCTTTCTCTGCT
ATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCTCCGGCTGTCCA
ATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGGTACCAAGTATT
AATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTAAGAGGAAATTC
AAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTATCCGCATCCCC
ATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGCCTCGAGAGATG
CCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCCTTGGTAGAAGA
AAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATAGAAACTATCAT
GCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATTTGGGACCAAAG
GGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAGGCTTGAATTGC
TGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAGTGAAAGATTCC
TTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGCTGGTAGACAAA
GAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAATCCGAATTGAT
AATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTCGGTGGTGGGGA
GGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAGATCATCGATTT
GGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTAATGCCAAAGGA
TATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTTTTATCACAGAC
TGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAAATCGTTGGAGG
TTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCATAATGCTCTAC
AAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGACTTTGATGCGT
CTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCACCGTCTATTTG
TGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTGTGGGAGGGATT
GACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACGTGGGCAGTGTG
AAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAATGGAGTCTATG
GAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCATCCAGAAGAGT
ATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGTTCTCCAAATTT
AGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCATCAGCAGCATT
GACAGCACCTCCAGTTATTTTAATCACTATAGAAGTCATCACAATTTAATCCATGGTTTA
AAACCCCACTTCAAACTCTTTCACCCGTCCAGTGAGTCTGAGCAAGGACTCACTAGACCT
CATGCTGATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGGGAGAGCTGCATGGGGAA
ACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCAAAGACTGGGTTCAACTT
GATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCCGGATGCCCTGGCATGAC
ATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCACGTCACTTCATCCAGCGC
TGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTTCTTATCCTTTTCTGCTT
CCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGCCTGGGTCTGTCCATGCT
AACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTATAAAGTACCATGAAGAG
TCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGCACTATATCTATATCGAA
AACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCAACAAGATAGGCGATGCC
ATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAATACCGGGTATATGTCGTG
ATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCGGAGGAAATGCTCTACAG
GCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAAATTCCATCCTTGGACAG
TTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCATTCTGTGGTCTTAGAACA
CATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATGTCCACAGCAAGTTGTTA
ATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAAATGACCGCAGCATGCTG
GGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAGAGACTGTTCCTTCAGTA
ATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGACTTCGGCTACAGTGCTTT
AGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTCAGGATCCAGTGAGTGAC
AAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATGCTACAATTTATGACAAG
GTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTCAGCTGAGAGACTTTATA
AACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGGAGGAACTGAAGAAGATC
CGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAGAAAGCCTACTGCCTTCT
GTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTTAA
|
| Enzyme 12 GenBank Gene ID |
U38545  |
| Enzyme 12 GeneCard ID |
PLD1  |
| Enzyme 12 GenAtlas ID |
PLD1  |
| Enzyme 12 HGNC ID |
HGNC:9067  |
| Enzyme 12 Chromosome Location |
3 |
| Enzyme 12 Locus |
3q26 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 General References |
- Hammond SM, Altshuller YM, Sung TC, Rudge SA, Rose K, Engebrecht J, Morris AJ, Frohman MA: Human ADP-ribosylation factor-activated phosphatidylcholine-specific phospholipase D defines a new and highly conserved gene family. J Biol Chem. 1995 Dec 15;270(50):29640-3. [PubMed
]
- Hammond SM, Jenco JM, Nakashima S, Cadwallader K, Gu Q, Cook S, Nozawa Y, Prestwich GD, Frohman MA, Morris AJ: Characterization of two alternately spliced forms of phospholipase D1. Activation of the purified enzymes by phosphatidylinositol 4,5-bisphosphate, ADP-ribosylation factor, and Rho family monomeric GTP-binding proteins and protein kinase C-alpha. J Biol Chem. 1997 Feb 7;272(6):3860-8. [PubMed
]
- Steed PM, Clark KL, Boyar WC, Lasala DJ: Characterization of human PLD2 and the analysis of PLD isoform splice variants. FASEB J. 1998 Oct;12(13):1309-17. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lopez I, Arnold RS, Lambeth JD: Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2. J Biol Chem. 1998 May 22;273(21):12846-52. [PubMed
]
- Divecha N, Roefs M, Halstead JR, D'Andrea S, Fernandez-Borga M, Oomen L, Saqib KM, Wakelam MJ, D'Santos C: Interaction of the type Ialpha PIPkinase with phospholipase D: a role for the local generation of phosphatidylinositol 4, 5-bisphosphate in the regulation of PLD2 activity. EMBO J. 2000 Oct 16;19(20):5440-9. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
|
| Enzyme 12 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 13
[top]
|
| Enzyme 13 ID |
5783 |
| Enzyme 13 Name |
Group 3 secretory phospholipase A2 |
| Enzyme 13 Synonyms |
- Group III secretory phospholipase A2
- GIII sPLA2
- sPLA2-III
- Phosphatidylcholine 2-acylhydrolase 3
|
| Enzyme 13 Gene Name |
PLA2G3 |
| Enzyme 13 Protein Sequence |
>Group 3 secretory phospholipase A2
MGVQAGLFGMLGFLGVALGGSPALRWYRTSCHLTKAVPGNPLGYLSFLAKDAQGLALIHA
RWDAHRRLQACSWEDEPELTAAYGALCAHETAWGSFIHTPGPELQRALATLQSQWEACRA
LEESPAGARKKRAAGQSGVPGGGHQREKRGWTMPGTLWCGVGDSAGNSSELGVFQGPDLC
CREHDRCPQNISPLQYNYGIRNYRFHTISHCDCDTRFQQCLQNQHDSISDIVGVAFFNVL
EIPCFVLEEQEACVAWYWWGGCRMYGTVPLARLQPRTFYNASWSSRATSPTPSSRSPAPP
KPRQKQHLRKGPPHQKGSKRPSKANTTALQDPMVSPRLDVAPTGLQGPQGGLKPQGARWV
CRSFRRHLDQCEHQIGPREIEFQLLNSAQEPLFHCNCTRRLARFLRLHSPPEVTNMLWEL
LGTTCFKLAPPLDCVEGKNCSRDPRAIRVSARHLRRLQQRRHQLQDKGTDERQPWPSEPL
RGPMSFYNQCLQLTQAARRPDRQQKSWSQ
|
| Enzyme 13 Number of Residues |
509 |
| Enzyme 13 Molecular Weight |
57150.5 |
| Enzyme 13 Theoretical pI |
9.23 |
| Enzyme 13 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 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. 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 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 |
142976884  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q9NZ20  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
PA2G3_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 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 13 GenBank Gene ID |
NM_015715.3  |
| Enzyme 13 GeneCard ID |
PLA2G3  |
| Enzyme 13 GenAtlas ID |
PLA2G3  |
| Enzyme 13 HGNC ID |
HGNC:17934  |
| Enzyme 13 Chromosome Location |
2 |
| Enzyme 13 Locus |
22q12.2 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 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 13 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 14
[top]
|
| Enzyme 14 ID |
6427 |
| Enzyme 14 Name |
Probable phospholipid-transporting ATPase IG |
| Enzyme 14 Synonyms |
- ATPase IQ
- ATPase class VI type 11C
|
| Enzyme 14 Gene Name |
ATP11C |
| Enzyme 14 Protein Sequence |
>Probable phospholipid-transporting ATPase IG
MQMVPSLPPASECAGEEKRVGTRTVFVGNHPVSETEAYIAQRFCDNRIVSSKYTLWNFLP
KNLFEQFRRIANFYFLIIFLVQVTVDTPTSPVTSGLPLFFVITVTAIKQGYEDCLRHRAD
NEVNKSTVYIIENAKRVRKESEKIKVGDVVEVQADETFPCDLILLSSCTTDGTCYVTTAS
LDGESNCKTHYAVRDTIALCTAESIDTLRAAIECEQPQPDLYKFVGRINIYSNSLEAVAR
SLGPENLLLKGATLKNTEKIYGVAVYTGMETKMALNYQGKSQKRSAVEKSINAFLIVYLF
ILLTKAAVCTTLKYVWQSTPYNDEPWYNQKTQKERETLKVLKMFTDFLSFMVLFNFIIPV
SMYVTVEMQKFLGSFFISWDKDFYDEEINEGALVNTSDLNEELGQVDYVFTDKTGTLTEN
SMEFIECCIDGHKYKGVTQEVDGLSQTDGTLTYFDKVDKNREELFLRALCLCHTVEIKTN
DAVDGATESAELTYISSSPDEIALVKGAKRYGFTFLGNRNGYMRVENQRKEIEEYELLHT
LNFDAVRRRMSVIVKTQEGDILLFCKGADSAVFPRVQNHEIELTKVHVERNAMDGYRTLC
VAFKEIAPDDYERINRQLIEAKMALQDREEKMEKVFDDIETNMNLIGATAVEDKLQDQAA
ETIEALHAAGLKVWVLTGDKMETAKSTCYACRLFQTNTELLELTTKTIEESERKEDRLHE
LLIEYRKKLLHEFPKSTRSFKKAWTEHQEYGLIIDGSTLSLILNSSQDSSSNNYKSIFLQ
ICMKCTAVLCCRMAPLQKAQIVRMVKNLKGSPITLSIGDGANDVSMILESHVGIGIKGKE
GRQAARNSDYSVPKFKHLKKLLLAHGHLYYVRIAHLVQYFFYKNLCFILPQFLYQFFCGF
SQQPLYDAAYLTMYNICFTSLPILAYSLLEQHINIDTLTSDPRLYMKISGNAMLQLGPFL
YWTFLAAFEGTVFFFGTYFLFQTASLEENGKVYGNWTFGTIVFTVLVFTVTLKLALDTRF
WTWINHFVIWGSLAFYVFFSFFWGGIIWPFLKQQRMYFVFAQMLSSVSTWLAIILLIFIS
LFPEILLIVLKNVRRRSARRNLSCRRASDSLSARPSVRPLLLRTFSDESNVL
|
| Enzyme 14 Number of Residues |
1132 |
| Enzyme 14 Molecular Weight |
129476.0 |
| Enzyme 14 Theoretical pI |
6.63 |
| Enzyme 14 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 14 General Function |
Involved in ATP binding |
| Enzyme 14 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
- 67-85
87-107
291-311
347-367
880-900
909-929
956-976
996-1016
1027-1047
1070-1090
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
39573513  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q8NB49  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
AT11C_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>3399 bp
ATGCAGATGGTCCCATCTCTCCCTCCAGCCTCTGAGTGTGCTGGAGAAGAGAAACGAGTT
GGCACACGCACAGTGTTTGTTGGCAATCATCCAGTTTCGGAAACAGAAGCTTACATTGCA
CAAAGATTTTGTGATAATAGAATAGTCTCATCTAAGTATACACTTTGGAATTTTCTCCCA
AAGAATCTGTTTGAACAGTTTAGAAGAATTGCAAATTTTTATTTTCTCATAATCTTCCTT
GTACAGGTCACAGTAGACACACCAACTAGCCCAGTTACCAGTGGACTTCCACTTTTCTTT
GTTATAACTGTTACAGCCATCAAGCAGGGATATGAGGATTGGCTGAGACACAGAGCTGAC
AATGAAGTCAACAAAAGCACTGTTTACATTATTGAAAATGCAAAGCGAGTGAGAAAAGAA
AGTGAAAAAATCAAGGTTGGTGATGTAGTAGAAGTACAGGCAGATGAAACCTTTCCCTGT
GATCTTATTCTTCTATCATCTTGCACCACTGATGGAACCTGTTATGTCACTACAGCCAGT
CTTGATGGGGAATCCAATTGCAAGACACATTATGCAGTACGTGATACCATTGCACTGTGT
ACAGCAGAATCCATCGATACCCTCCGAGCAGCAATTGAATGTGAACAGCCTCAACCTGAC
CTCTACAAATTTGTTGGGCGAATCAATATCTACAGTAATAGTCTTGAGGCTGTTGCCAGG
TCTTTGGGACCTGAAAATCTCTTGCTGAAAGGAGCTACGCTAAAAAATACCGAGAAGATA
TATGGAGTTGCTGTTTACACTGGAATGGAAACCAAAATGGCTTTGAACTACCAAGGGAAA
TCTCAGAAACGTTCTGCTGTTGAAAAATCTATTAATGCTTTCCTGATTGTATATTTATTT
ATCTTACTGACCAAAGCTGCAGTATGCACTACTCTAAAGTATGTTTGGCAAAGTACCCCA
TACAATGATGAACCTTGGTATAACCAAAAGACTCAGAAAGAGCGAGAGACCTTGAAGGTT
TTAAAAATGTTCACCGACTTCCTATCATTTATGGTTCTATTCAACTTTATCATTCCTGTC
TCCATGTACGTCACAGTAGAAATGCAGAAATTCTTGGGCTCCTTCTTCATCTCATGGGAT
AAGGACTTTTATGATGAAGAAATTAATGAAGGAGCCCTGGTTAACACATCAGACCTTAAT
GAAGAACTTGGTCAGGTGGATTATGTATTTACAGATAAGACTGGAACACTCACTGAAAAC
AGCATGGAATTCATTGAATGCTGCATAGATGGCCACAAATATAAAGGTGTAACTCAAGAG
GTTGATGGATTATCTCAAACTGATGGAACTTTAACATATTTTGACAAAGTAGATAAGAAT
CGAGAAGAGCTGTTTCTACGTGCCTTGTGTTTATGTCATACTGTAGAAATCAAAACAAAC
GATGCTGTTGATGGAGCTACAGAATCAGCTGAATTAACCTATATCTCCTCTTCACCAGAT
GAAATAGCTTTGGTGAAAGGAGCTAAAAGGTACGGGTTCACATTTTTAGGAAATCGAAAT
GGATATATGAGAGTAGAGAACCAAAGAAAAGAAATAGAAGAATATGAACTTCTTCACACC
TTAAACTTTGATGCTGTCCGGCGACGTATGAGTGTAATTGTGAAGACTCAAGAAGGAGAC
ATACTTCTCTTTTGTAAAGGAGCAGACTCGGCAGTTTTTCCCAGAGTGCAAAATCATGAA
ATTGAGTTAACTAAAGTCCATGTGGAACGTAATGCAATGGATGGGTATCGGACACTCTGT
GTAGCCTTCAAAGAAATTGCTCCAGATGATTATGAAAGAATTAACAGACAGCTCATAGAG
GCAAAAATGGCCTTACAAGACAGAGAAGAAAAAATGGAAAAAGTTTTCGATGATATTGAG
ACAAACATGAATTTAATTGGAGCCACTGCAGTTGAAGACAAGCTACAAGATCAAGCTGCA
GAGACCATTGAAGCTCTGCATGCAGCAGGCCTGAAAGTCTGGGTGCTCACTGGGGACAAG
ATGGAGACAGCTAAATCCACATGCTATGCCTGCCGCCTTTTCCAGACCAACACTGAGCTC
TTAGAACTAACCACAAAAACCATTGAAGAAAGTGAAAGGAAAGAAGATCGATTACATGAA
TTATTGATAGAATATCGCAAGAAATTGCTGCATGAGTTTCCTAAAAGTACTAGAAGCTTT
AAAAAAGCATGGACAGAACATCAGGAATATGGATTAATCATAGATGGCTCCACATTGTCA
CTCATACTAAATTCTAGTCAAGACTCTAGTTCAAACAATTACAAAAGCATTTTCCTACAA
ATATGTATGAAGTGTACTGCAGTGCTCTGCTGTCGGATGGCACCATTACAGAAAGCCCAG
ATTGTCAGAATGGTGAAGAATTTAAAAGGCAGCCCAATAACTCTGTCGATAGGTGATGGT
GCCAATGATGTTAGTATGATCTTGGAATCCCATGTGGGAATAGGTATTAAAGGCAAAGAA
GGTCGCCAAGCAGCTAGGAATAGCGATTATTCTGTTCCAAAGTTTAAACACTTAAAGAAA
CTGCTGTTGGCTCATGGACATCTATATTATGTGAGAATAGCACACCTTGTACAGTACTTC
TTCTATAAGAACCTTTGTTTCATTTTGCCACAGTTTTTGTACCAGTTCTTCTGTGGATTC
TCACAACAGCCACTGTATGATGCTGCTTACCTTACAATGTACAATATCTGCTTCACATCC
TTGCCCATCCTGGCCTATAGTCTACTGGAACAGCACATCAACATTGACACTCTGACCTCA
GATCCCCGATTGTATATGAAAATTTCTGGCAATGCCATGCTACAGTTGGGCCCCTTCTTA
TATTGGACATTTCTGGCTGCCTTTGAAGGGACAGTGTTCTTCTTTGGGACTTACTTTCTT
TTTCAGACTGCATCCCTAGAAGAAAATGGAAAGGTATACGGAAACTGGACTTTTGGAACC
ATTGTTTTTACAGTCTTAGTATTCACTGTAACCCTGAAGCTTGCCTTGGATACCCGATTC
TGGACGTGGATAAATCACTTTGTGATTTGGGGTTCTTTAGCCTTCTATGTATTTTTCTCA
TTCTTCTGGGGAGGAATTATTTGGCCTTTTCTCAAGCAACAGAGAATGTATTTTGTATTT
GCCCAAATGCTGTCTTCTGTATCCACATGGTTGGCTATAATTCTTCTAATATTTATCAGC
CTGTTCCCTGAGATTCTTCTGATAGTATTAAAGAATGTAAGAAGAAGAAGTGCCAGGAGA
AATCTGAGCTGTAGAAGGGCATCTGACTCATTATCCGCCAGACCTTCAGTCAGACCTCTT
CTTTTACGAACATTCTCAGACGAATCTAATGTATTGTAA
|
| Enzyme 14 GenBank Gene ID |
AJ580093  |
| Enzyme 14 GeneCard ID |
ATP11C  |
| Enzyme 14 GenAtlas ID |
ATP11C  |
| Enzyme 14 HGNC ID |
HGNC:13554  |
| Enzyme 14 Chromosome Location |
Not Available |
| Enzyme 14 Locus |
Not Available |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Andrew Nesbit M, Bowl MR, Harding B, Schlessinger D, Whyte MP, Thakker RV: X-linked hypoparathyroidism region on Xq27 is evolutionarily conserved with regions on 3q26 and 13q34 and contains a novel P-type ATPase. Genomics. 2004 Dec;84(6):1060-70. [PubMed
]
- Ross MT, Grafham DV, Coffey AJ, Scherer S, McLay K, Muzny D, Platzer M, Howell GR, Burrows C, Bird CP, Frankish A, Lovell FL, Howe KL, Ashurst JL, Fulton RS, Sudbrak R, Wen G, Jones MC, Hurles ME, Andrews TD, Scott CE, Searle S, Ramser J, Whittaker A, Deadman R, Carter NP, Hunt SE, Chen R, Cree A, Gunaratne P, Havlak P, Hodgson A, Metzker ML, Richards S, Scott G, Steffen D, Sodergren E, Wheeler DA, Worley KC, Ainscough R, Ambrose KD, Ansari-Lari MA, Aradhya S, Ashwell RI, Babbage AK, Bagguley CL, Ballabio A, Banerjee R, Barker GE, Barlow KF, Barrett IP, Bates KN, Beare DM, Beasley H, Beasley O, Beck A, Bethel G, Blechschmidt K, Brady N, Bray-Allen S, Bridgeman AM, Brown AJ, Brown MJ, Bonnin D, Bruford EA, Buhay C, Burch P, Burford D, Burgess J, Burrill W, Burton J, Bye JM, Carder C, Carrel L, Chako J, Chapman JC, Chavez D, Chen E, Chen G, Chen Y, Chen Z, Chinault C, Ciccodicola A, Clark SY, Clarke G, Clee CM, Clegg S, Clerc-Blankenburg K, Clifford K, Cobley V, Cole CG, Conquer JS, Corby N, Connor RE, David R, Davies J, Davis C, Davis J, Delgado O, Deshazo D, Dhami P, Ding Y, Dinh H, Dodsworth S, Draper H, Dugan-Rocha S, Dunham A, Dunn M, Durbin KJ, Dutta I, Eades T, Ellwood M, Emery-Cohen A, Errington H, Evans KL, Faulkner L, Francis F, Frankland J, Fraser AE, Galgoczy P, Gilbert J, Gill R, Glockner G, Gregory SG, Gribble S, Griffiths C, Grocock R, Gu Y, Gwilliam R, Hamilton C, Hart EA, Hawes A, Heath PD, Heitmann K, Hennig S, Hernandez J, Hinzmann B, Ho S, Hoffs M, Howden PJ, Huckle EJ, Hume J, Hunt PJ, Hunt AR, Isherwood J, Jacob L, Johnson D, Jones S, de Jong PJ, Joseph SS, Keenan S, Kelly S, Kershaw JK, Khan Z, Kioschis P, Klages S, Knights AJ, Kosiura A, Kovar-Smith C, Laird GK, Langford C, Lawlor S, Leversha M, Lewis L, Liu W, Lloyd C, Lloyd DM, Loulseged H, Loveland JE, Lovell JD, Lozado R, Lu J, Lyne R, Ma J, Maheshwari M, Matthews LH, McDowall J, McLaren S, McMurray A, Meidl P, Meitinger T, Milne S, Miner G, Mistry SL, Morgan M, Morris S, Muller I, Mullikin JC, Nguyen N, Nordsiek G, Nyakatura G, O'Dell CN, Okwuonu G, Palmer S, Pandian R, Parker D, Parrish J, Pasternak S, Patel D, Pearce AV, Pearson DM, Pelan SE, Perez L, Porter KM, Ramsey Y, Reichwald K, Rhodes S, Ridler KA, Schlessinger D, Schueler MG, Sehra HK, Shaw-Smith C, Shen H, Sheridan EM, Shownkeen R, Skuce CD, Smith ML, Sotheran EC, Steingruber HE, Steward CA, Storey R, Swann RM, Swarbreck D, Tabor PE, Taudien S, Taylor T, Teague B, Thomas K, Thorpe A, Timms K, Tracey A, Trevanion S, Tromans AC, d'Urso M, Verduzco D, Villasana D, Waldron L, Wall M, Wang Q, Warren J, Warry GL, Wei X, West A, Whitehead SL, Whiteley MN, Wilkinson JE, Willey DL, Williams G, Williams L, Williamson A, Williamson H, Wilming L, Woodmansey RL, Wray PW, Yen J, Zhang J, Zhou J, Zoghbi H, Zorilla S, Buck D, Reinhardt R, Poustka A, Rosenthal A, Lehrach H, Meindl A, Minx PJ, Hillier LW, Willard HF, Wilson RK, Waterston RH, Rice CM, Vaudin M, Coulson A, Nelson DL, Weinstock G, Sulston JE, Durbin R, Hubbard T, Gibbs RA, Beck S, Rogers J, Bentley DR: The DNA sequence of the human X chromosome. Nature. 2005 Mar 17;434(7031):325-37. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed
]
- Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y: Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Anal Sci. 2008 Jan;24(1):161-6. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 14 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 15
[top]
|
| Enzyme 15 ID |
6428 |
| Enzyme 15 Name |
Probable phospholipid-transporting ATPase IH |
| Enzyme 15 Synonyms |
- ATPase IS
- ATPase class VI type 11A
|
| Enzyme 15 Gene Name |
ATP11A |
| Enzyme 15 Protein Sequence |
>Probable phospholipid-transporting ATPase IH
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNF
IPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHK
ADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTT
ASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPV
VRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVY
LCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYII
PVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLT
ENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHT
VQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNREN
HIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVER
NAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATA
VEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEE
QSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNY
RELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGI
GVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLY
QFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALL
RWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKL
ALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIV
LLVTISLLPDVLKKVLCRQLWPTATERVQTKSQCLSVEQSTIFMLSQTSSSLSF
|
| Enzyme 15 Number of Residues |
1134 |
| Enzyme 15 Molecular Weight |
129754.6 |
| Enzyme 15 Theoretical pI |
6.58 |
| Enzyme 15 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 15 General Function |
Involved in ATP binding |
| Enzyme 15 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 15 Pathways |
Not Available |
| Enzyme 15 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
- 62-82
89-110
297-318
350-372
882-902
915-934
965-986
1001-1023
1030-1050
1069-1093
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
150421684  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
P98196  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
AT11A_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>3405 bp
ATGGACTGCAGCCTCGTGCGGACGCTCGTGCACAGATACTGTGCAGGAGAAGAGAATTGG
GTGGACAGCAGGACCATCTACGTGGGACACAGGGAGCCACCTCCGGGCGCAGAGGCCTAC
ATCCCACAGAGATACCCAGACAACAGGATCGTCTCGTCCAAGTACACATTTTGGAACTTT
ATACCCAAGAATTTATTTGAACAATTCAGAAGAGTAGCCAACTTTTATTTCCTTATCATA
TTTCTGGTGCAGTTGATTATTGATACACCCACAAGTCCAGTGACAAGCGGACTTCCACTC
TTCTTTGTCATTACTGTGACGGCTATCAAACAGGGTTATGAAGACTGGCTTCGACATAAA
GCAGACAATGCCATGAACCAGTGTCCTGTTCATTTCATTCAGCACGGCAAGCTCGTTCGG
AAACAAAGTCGAAAGCTGCGAGTTGGGGACATTGTCATGGTTAAGGAGGACGAGACCTTT
CCCTGCGACTTGATCTTCCTTTCCAGCAACCGGGGAGATGGGACGTGCCACGTCACCACC
GCCAGCTTGGATGGAGAATCCAGCCATAAAACGCATTACGCGGTCCAGGACACCAAAGGC
TTCCACACAGAGGAGGATATCGGCGGACTTCACGCCACCATCGAGTGTGAGCAGCCCCAG
CCCGACCTCTACAAGTTCGTGGGTCGCATCAACGTTTACAGTGACCTGAATGACCCCGTG
GTGAGGCCCTTAGGATCGGAAAACCTGCTGCTTAGAGGAGCTACACTGAAGAACACTGAG
AAAATCTTTGGTGTGGCTATTTACACGGGAATGGAAACCAAGATGGCATTAAATTATCAA
TCAAAATCTCAGAAGCGATCTGCCGTGGAAAAATCGATGAATGCGTTCCTCATTGTGTAT
CTCTGCATTCTGATCAGCAAAGCCCTGATAAACACTGTGCTGAAATACATGTGGCAGAGT
GAGCCCTTTCGGGATGAGCCGTGGTATAATCAGAAAACGGAGTCGGAAAGGCAGAGGAAT
CTGTTCCTCAAGGCATTCACGGACTTCCTGGCCTTCATGGTCCTCTTTAACTACATCATC
CCTGTGTCCATGTACGTCACGGTCGAGATGCAGAAGTTCCTCGGCTCTTACTTCATCACC
TGGGACGAAGACATGTTTGACGAGGAGACTGGCGAGGGGCCTCTGGTGAACACGTCGGAC
CTCAATGAAGAGCTGGGACAGGTGGAGTACATCTTCACAGACAAGACCGGCACCCTCACG
GAAAACAACATGGAGTTCAAGGAGTGCTGCATCGAAGGCCATGTCTACGTGCCCCACGTC
ATCTGCAACGGGCAGGTCCTCCCAGAGTCGTCAGGAATCGACATGATTGACTCGTCCCCC
AGCGTCAACGGGAGGGAGCGCGAGGAGCTGTTTTTCCGGGCCCTCTGTCTCTGCCACACC
GTCCAGGTGAAAGACGATGACAGCGTAGACGGCCCCAGGAAATCGCCGGACGGGGGGAAA
TCCTGTGTGTACATCTCATCCTCGCCCGACGAGGTGGCGCTGGTCGAAGGTGTCCAGAGA
CTTGGCTTTACCTACCTAAGGCTGAAGGACAATTACATGGAGATATTAAACAGGGAGAAC
CACATCGAAAGGTTTGAATTGCTGGAAATTTTGAGTTTTGACTCAGTCAGAAGGAGAATG
AGTGTAATTGTAAAATCTGCTACAGGAGAAATTTATCTGTTTTGCAAAGGAGCAGATTCT
TCGATATTCCCCCGAGTGATAGAAGGCAAAGTTGACCAGATCCGAGCCAGAGTGGAGCGT
AACGCAGTGGAGGGGCTCCGAACTTTGTGTGTTGCTTATAAAAGGCTGATCCAAGAAGAA
TATGAAGGCATTTGTAAGCTGCTGCAGGCTGCCAAAGTGGCCCTTCAAGATCGAGAGAAA
AAGTTAGCAGAAGCCTATGAGCAAATAGAGAAAGATCTTACTCTGCTTGGTGCTACAGCT
GTTGAGGACCGGCTGCAGGAGAAAGCTGCAGACACCATCGAGGCCCTGCAGAAGGCCGGG
ATCAAAGTCTGGGTTCTCACGGGAGACAAGATGGAGACGGCCGCGGCCACGTGCTACGCC
TGCAAGCTCTTCCGCAGGAACACGCAGCTGCTGGAGCTGACCACCAAGAGGATCGAGGAG
CAGAGCCTGCACGACGTCCTGTTCGAGCTGAGCAAGACGGTCCTGCGCCACAGCGGGAGC
CTGACCAGAGACAACCTGTCCGGACTTTCAGCAGATATGCAGGACTACGGTTTAATTATC
GACGGAGCTGCACTGTCTCTGATAATGAAGCCTCGAGAAGACGGGAGTTCCGGCAACTAC
AGGGAGCTCTTCCTGGAAATCTGCCGGAGCTGCAGCGCGGTGCTCTGCTGCCGCATGGCG
CCCTTGCAGAAGGCTCAGATTGTTAAATTAATCAAATTTTCAAAAGAGCACCCAATCACG
TTAGCAATTGGCGATGGTGCAAATGATGTCAGCATGATTCTGGAAGCGCACGTGGGCATA
GGTGTCATCGGCAAGGAAGGCCGCCAGGCTGCCAGGAACAGCGACTATGCAATCCCAAAG
TTTAAGCATTTGAAGAAGATGCTGCTTGTTCACGGGCATTTTTATTACATTAGGATCTCT
GAGCTCGTGCAGTACTTCTTCTATAAGAACGTCTGCTTCATCTTCCCTCAGTTTTTATAC
CAGTTCTTCTGTGGGTTTTCACAACAGACTTTGTACGACACCGCGTATCTGACCCTCTAC
AACATCAGCTTCACCTCCCTCCCCATCCTCCTGTACAGCCTCATGGAGCAGCATGTTGGC
ATTGACGTGCTCAAGAGAGACCCGACCCTGTACAGGGACGTCGCCAAGAATGCCCTGCTG
CGCTGGCGCGTGTTCATCTACTGGACGCTCCTGGGACTGTTTGACGCACTGGTGTTCTTC
TTTGGTGCTTATTTCGTGTTTGAAAATACAACTGTGACAAGCAACGGGCAGATATTTGGA
AACTGGACGTTTGGAACGCTGGTATTCACCGTGATGGTGTTCACAGTTACACTAAAGCTT
GCATTGGACACACACTACTGGACTTGGATCAACCATTTTGTCATCTGGGGGTCGCTGCTG
TTCTACGTTGTCTTTTCGCTTCTCTGGGGAGGAGTGATCTGGCCGTTCCTCAACTACCAG
AGGATGTACTACGTGTTCATCCAGATGCTGTCCAGCGGGCCCGCCTGGCTGGCCATCGTG
CTGCTGGTGACCATCAGCCTCCTTCCCGACGTCCTCAAGAAAGTCCTGTGCCGGCAGCTG
TGGCCAACAGCAACAGAGAGAGTCCAGACTAAGAGCCAGTGCCTTTCTGTCGAGCAGTCA
ACCATCTTTATGCTTTCTCAGACTTCCAGCAGCCTGAGTTTCTGA
|
| Enzyme 15 GenBank Gene ID |
NM_015205.2  |
| Enzyme 15 GeneCard ID |
ATP11A  |
| Enzyme 15 GenAtlas ID |
ATP11A  |
| Enzyme 15 HGNC ID |
HGNC:13552  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
13q34 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed
]
- Kikuno R, Nagase T, Ishikawa K, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Jun 30;6(3):197-205. [PubMed
]
|
| Enzyme 15 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
6465 |
| Enzyme 16 Name |
Probable phospholipid-transporting ATPase VA |
| Enzyme 16 Synonyms |
- ATPase class V type 10A
- Aminophospholipid translocase VA
|
| Enzyme 16 Gene Name |
ATP10A |
| Enzyme 16 Protein Sequence |
>Probable phospholipid-transporting ATPase VA
MEREPAGTEEPGPPGRRRRREGRTRTVRSNLLPPPGAEDPAAGAAKGERRRRRGCAQHLA
DNRLKTTKYTLLSFLPKNLFEQFHRPANVYFVFIALLNFVPAVNAFQPGLALAPVLFILA
ITAFRDLWEDYSRHRSDHKINHLGCLVFSREEKKYVNRFWKEIHVGDFVRLRCNEIFPAD
ILLLSSSDPDGLCHIETANLDGETNLKRRQVVRGFSELVSEFNPLTFTSVIECEKPNNDL
SRFRGCIIHDNGKKAGLYKENLLLRGCTLRNTDAVVGIVIYAGHETKALLNNSGPRYKRS
KLERQMNCDVLWCVLLLVCMSLFSAVGHGLWIWRYQEKKSLFYVPKSDGSSLSPVTAAVY
SFLTMIIVLQVLIPISLYVSIEIVKACQVYFINQDMQLYDEETDSQLQCRALNITEDLGQ
IQYIFSDKTGTLTENKMVFRRCTVSGVEYSHDANAQRLARYQEADSEEEEVVPRGGSVSQ
RGSIGSHQSVRVVHRTQSTKSHRRTGSRAEAKRASMLSKHTAFSSPMEKDITPDPKLLEK
VSECDKSLAVARHQEHLLAHLSPELSDVFDFFIALTICNTVVVTSPDQPRTKVRVRFELK
SPVKTIEDFLRRFTPSCLTSGCSSIGSLAANKSSHKLGSSFPSTPSSDGMLLRLEERLGQ
PTSAIASNGYSSQADNWASELAQEQESERELRYEAESPDEAALVYAARAYNCVLVERLHD
QVSVELPHLGRLTFELLHTLGFDSVRKRMSVVIRHPLTDEINVYTKGADSVVMDLLQPCS
SVDARGRHQKKIRSKTQNYLNVYAAEGLRTLCIAKRVLSKEEYACWLQSHLEAESSLENS
EELLFQSAIRLETNLHLLGATGIEDRLQDGVPETISKLRQAGLQIWVLTGDKQETAVNIA
YACKLLDHDEEVITLNATSQEACAALLDQCLCYVQSRGLQRAPEKTKGKVSMRFSSLCPP
STSTASGRRPSLVIDGRSLAYALEKNLEDKFLFLAKQCRSVLCCRSTPLQKSMVVKLVRS
KLKAMTLAIGDGANDVSMIQVADVGVGISGQEGMQAVMASDFAVPKFRYLERLLILHGHW
CYSRLANMVLYFFYKNTMFVGLLFWFQFFCGFSASTMIDQWYLIFFNLLFSSLPPLVTGV
LDRDVPANVLLTNPQLYKSGQNMEEYRPRTFWFNMADAAFQSLVCFSIPYLAYYDSNVDL
FTWGTPIVTIALLTFLLHLGIETKTWTWLNWITCGFSVLLFFTVALIYNASCATCYPPSN
PYWTMQALLGDPVFYLTCLMTPVAALLPRLFFRSLQGRVFPTQLQLARQLTRKSPRRCSA
PKETFAQGRLPKDSGTEHSSGRTVKTSVPLSQPSWHTQQPVCSLEASGEPSTVDMSMPVR
EHTLLEGLSAPAPMSSAPGEAVLRSPGGCPEESKVRAASTGRVTPLSSLFSLPTFSLLNW
ISSWSLVSRLGSVLQFSRTEQLADGQAGRGLPVQPHSGRSGLQGPDHRLLIGASSRRSQ
|
| Enzyme 16 Number of Residues |
1499 |
| Enzyme 16 Molecular Weight |
167686.6 |
| Enzyme 16 Theoretical pI |
8.43 |
| Enzyme 16 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 16 General Function |
Involved in ATP binding |
| Enzyme 16 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 16 Pathways |
Not Available |
| Enzyme 16 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
- 87-106
111-128
310-332
363-384
1088-1108
1120-1140
1171-1192
1200-1222
1229-1249
1268-1292
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
14424433  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
O60312  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
AT10A_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>4500 bp
ATGGAGCGGGAGCCGGCGGGGACCGAGGAGCCCGGGCCTCCGGGACGGCGGAGGCGCCGA
GAGGGCAGGACGCGCACGGTGCGCTCCAACCTGCTGCCGCCCCCGGGCGCCGAGGACCCT
GCGGCTGGCGCGGCCAAGGGCGAGCGGCGACGGCGGCGCGGGTGTGCCCAGCACCTGGCC
GACAACCGGCTCAAGACTACCAAGTACACGCTGCTGTCCTTCCTGCCCAAGAACCTGTTC
GAGCAGTTCCACCGCCCGGCCAACGTGTACTTTGTCTTCATCGCGCTGCTCAACTTCGTG
CCGGCGGTGAACGCCTTCCAGCCCGGCCTGGCACTGGCGCCGGTGCTCTTCATCCTGGCC
ATCACGGCCTTCAGGGACCTGTGGGAGGACTACAGCCGCCACCGCTCCGACCACAAGATC
AACCACCTGGGCTGCCTGGTCTTCAGCAGGGAAGAAAAGAAATACGTGAACCGATTCTGG
AAAGAAATCCACGTGGGAGACTTTGTGCGTCTTCGCTGCAACGAAATCTTCCCTGCGGAC
ATTCTGCTGCTCTCCTCCAGTGACCCCGACGGGCTATGCCACATCGAGACCGCCAACCTG
GATGGAGAGACCAACCTGAAGCGGCGGCAGGTGGTCCGCGGCTTCTCGGAGCTTGTCTCC
GAATTCAATCCTTTGACGTTCACCAGCGTGATCGAATGCGAGAAGCCAAACAACGACCTG
AGTAGGTTTCGCGGCTGCATCATACATGACAACGGGAAAAAGGCCGGGCTGTATAAAGAA
AACCTGCTGCTGAGGGGCTGCACCCTTAGGAACACGGACGCAGTCGTCGGCATTGTCATC
TACGCAGGACATGAAACCAAGGCTCTGCTGAACAACAGTGGGCCCCGCTACAAGCGCAGC
AAGCTGGAGAGGCAGATGAACTGCGACGTGCTCTGGTGTGTCCTGCTCCTTGTTTGCATG
TCTCTGTTTTCAGCAGTCGGACATGGACTGTGGATATGGCGGTATCAAGAGAAGAAGTCA
TTATTTTATGTCCCCAAGTCTGATGGAAGCTCCTTATCCCCAGTCACAGCTGCAGTTTAC
TCATTTTTAACAATGATAATAGTTCTGCAGGTTTTGATCCCAATTTCCTTATACGTTTCC
ATTGAAATTGTTAAAGCATGCCAAGTGTACTTCATTAACCAGGACATGCAGTTGTATGAC
GAAGAAACAGACTCGCAGCTGCAGTGCCGAGCTCTGAACATCACGGAAGACTTAGGACAG
ATACAGTACATTTTCTCAGATAAAACTGGCACTTTGACAGAGAATAAGATGGTTTTCCGA
AGATGCACTGTGTCTGGTGTAGAATATTCTCATGATGCAAATGCGCAGCGTCTGGCCAGG
TACCAAGAGGCAGACTCGGAGGAGGAGGAGGTGGTGCCCAGAGGGGGCTCGGTGTCCCAG
CGCGGCAGCATCGGCAGCCACCAGAGTGTCCGGGTGGTGCACAGAACCCAGAGCACCAAG
TCCCACCGGCGCACGGGCAGCCGGGCCGAGGCCAAGAGGGCCAGCATGCTGTCCAAGCAC
ACGGCCTTCAGCAGCCCCATGGAGAAGGATATCACGCCCGACCCAAAGCTGCTGGAGAAG
GTGAGTGAGTGTGACAAGAGCCTAGCCGTGGCGAGGCATCAGGAGCACCTGCTGGCCCAC
CTCTCGCCTGAGCTGTCTGACGTCTTTGATTTCTTCATCGCACTCACCATCTGCAACACA
GTCGTCGTCACGTCCCCGGATCAGCCACGAACAAAGGTGAGGGTGAGGTTTGAGCTGAAG
TCCCCGGTGAAGACGATAGAAGACTTCCTGCGGAGGTTCACACCCAGCTGCCTGACCTCA
GGCTGCAGCAGCATCGGGAGCCTGGCCGCCAACAAGTCCAGCCACAAGTTGGGCTCCAGC
TTCCCGTCCACCCCGTCCAGCGACGGCATGCTTCTCAGGCTGGAGGAGAGGCTGGGCCAG
CCCACCTCGGCCATCGCCAGCAACGGCTACAGCAGCCAGGCGGACAACTGGGCCTCGGAG
CTTGCTCAGGAGCAGGAGTCAGAGCGCGAGCTGCGGTACGAGGCGGAGAGCCCGGATGAG
GCCGCACTGGTGTATGCGGCCAGAGCCTACAACTGCGTGCTTGTGGAGCGGCTGCACGAC
CAAGTGTCAGTGGAGCTGCCCCACCTGGGCAGGCTCACCTTCGAGCTCCTGCACACACTG
GGTTTCGATTCCGTCCGCAAGAGGATGTCAGTGGTGATCCGGCACCCGCTTACCGATGAG
ATCAACGTCTACACCAAGGGGGCCGACTCAGTGGTCATGGATCTCCTGCAGCCCTGCTCT
TCAGTTGACGCCAGAGGGAGGCATCAAAAAAAGATTCGGAGCAAAACTCAGAATTACCTC
AACGTGTATGCGGCGGAAGGCCTGCGCACCTTGTGCATCGCCAAGAGAGTTCTGAGTAAA
GAAGAGTATGCCTGCTGGTTGCAAAGCCACCTAGAAGCCGAATCCTCCCTGGAAAACAGC
GAGGAGCTCCTCTTCCAGTCTGCCATTCGCCTGGAGACCAACCTGCACTTGTTAGGTGCC
ACTGGGATTGAAGACCGCCTGCAGGACGGAGTCCCTGAAACTATTTCTAAATTGCGTCAA
GCGGGCCTGCAGATTTGGGTTCTCACTGGTGACAAACAAGAAACAGCTGTCAACATTGCA
TATGCCTGCAAACTGCTGGACCACGACGAGGAGGTCATCACCCTGAATGCCACCTCCCAG
GAGGCGTGTGCAGCCCTGCTAGACCAGTGCCTATGCTACGTGCAGTCCAGAGGCCTCCAG
AGAGCCCCTGAGAAGACCAAGGGCAAAGTGAGCATGAGGTTCTCCTCTCTCTGCCCACCC
TCCACGTCCACTGCCTCTGGCCGCAGACCCAGCCTCGTGATCGATGGGAGAAGCCTGGCC
TACGCTCTCGAGAAAAACCTGGAGGACAAATTCCTCTTCCTTGCCAAGCAGTGCCGCTCC
GTCCTCTGCTGTCGGTCGACGCCTCTGCAGAAGAGCATGGTGGTGAAGCTGGTGCGGAGC
AAGCTCAAGGCCATGACCCTGGCCATAGGTGATGGAGCCAATGATGTCAGCATGATCCAG
GTGGCAGATGTGGGTGTGGGAATCTCCGGCCAGGAGGGTATGCAGGCAGTGATGGCCAGC
GACTTTGCAGTGCCGAAATTCCGATACCTGGAGAGGCTCTTGATTCTTCACGGGCATTGG
TGCTACTCCCGACTTGCCAACATGGTGCTGTACTTCTTCTACAAAAACACAATGTTCGTG
GGCCTCCTGTTTTGGTTCCAGTTTTTCTGTGGCTTCTCTGCATCTACCATGATTGACCAG
TGGTATCTAATCTTCTTTAATCTGCTCTTCTCGTCACTTCCCCCGCTCGTGACTGGGGTG
CTGGACAGGGATGTGCCAGCCAATGTGCTGCTGACCAACCCGCAGCTCTACAAGAGTGGC
CAGAACATGGAGGAATACCGGCCACGAACGTTCTGGTTTAACATGGCCGACGCCGCCTTC
CAGAGCCTGGTTTGCTTTTCCATTCCTTACCTGGCCTACTATGACTCGAACGTGGACCTG
TTTACCTGGGGGACCCCTATTGTGACAATCGCGCTGCTCACTTTCCTGCTCCACCTGGGC
ATTGAAACCAAAACCTGGACCTGGCTCAACTGGATAACGTGTGGCTTCAGTGTCCTTTTG
TTTTTCACCGTGGCTTTGATTTACAATGCGTCTTGTGCCACGTGCTATCCTCCGTCCAAC
CCTTACTGGACTATGCAAGCCTTACTGGGTGACCCAGTGTTTTACTTGACTTGCCTGATG
ACGCCTGTCGCTGCACTGCTGCCCAGATTGTTTTTCAGATCCCTCCAGGGGAGGGTTTTC
CCCACACAACTTCAGCTGGCACGTCAGTTGACCAGGAAGTCCCCCAGGAGATGCAGTGCT
CCCAAAGAGACCTTTGCTCAGGGACGCCTCCCGAAGGACTCGGGAACCGAGCACTCATCA
GGGAGGACAGTCAAGACCTCTGTGCCCCTGTCCCAGCCTTCTTGGCACACACAGCAGCCG
GTCTGCTCCCTGGAGGCCAGCGGGGAGCCCAGCACAGTGGACATGAGCATGCCAGTGAGG
GAGCACACCCTGCTGGAGGGGCTGAGCGCACCGGCCCCCATGTCCTCTGCGCCAGGGGAG
GCTGTCCTGAGGAGTCCAGGAGGGTGTCCTGAGGAGTCCAAGGTGAGAGCTGCCAGCACC
GGCAGGGTGACCCCCCTGTCTTCCCTCTTCAGCCTGCCTACCTTCAGCTTACTCAACTGG
ATTTCCTCCTGGTCGCTGGTCAGCAGGCTGGGGAGTGTCTTACAGTTCTCCCGGACGGAG
CAGCTTGCAGATGGACAAGCGGGACGTGGACTTCCTGTCCAGCCCCACTCAGGCCGATCA
GGACTTCAAGGGCCAGACCACAGACTACTTATAGGAGCATCTTCAAGGCGGTCACAGTGA
|
| Enzyme 16 GenBank Gene ID |
NM_024490.3  |
| Enzyme 16 GeneCard ID |
ATP10A  |
| Enzyme 16 GenAtlas ID |
ATP10A  |
| Enzyme 16 HGNC ID |
HGNC:13542  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
15q11.2 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Meguro M, Kashiwagi A, Mitsuya K, Nakao M, Kondo I, Saitoh S, Oshimura M: A novel maternally expressed gene, ATP10C, encodes a putative aminophospholipid translocase associated with Angelman syndrome. Nat Genet. 2001 May;28(1):19-20. [PubMed
]
- Herzing LB, Kim SJ, Cook EH Jr, Ledbetter DH: The human aminophospholipid-transporting ATPase gene ATP10C maps adjacent to UBE3A and exhibits similar imprinted expression. Am J Hum Genet. 2001 Jun;68(6):1501-5. Epub 2001 May 11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Nagase T, Ishikawa K, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Feb 28;5(1):31-9. [PubMed
]
|
| Enzyme 16 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
6488 |
| Enzyme 17 Name |
Probable phospholipid-transporting ATPase IC |
| Enzyme 17 Synonyms |
- ATPase class I type 8B member 1
- Familial intrahepatic cholestasis type 1
|
| Enzyme 17 Gene Name |
ATP8B1 |
| Enzyme 17 Protein Sequence |
>Probable phospholipid-transporting ATPase IC
MSTERDSETTFDEDSQPNDEVVPYSDDETEDELDDQGSAVEPEQNRVNREAEENREPFRK
ECTWQVKANDRKYHEQPHFMNTKFLCIKESKYANNAIKTYKYNAFTFIPMNLFEQFKRAA
NLYFLALLILQAVPQISTLAWYTTLVPLLVVLGVTAIKDLVDDVARHKMDKEINNRTCEV
IKDGRFKVAKWKEIQVGDVIRLKKNDFVPADILLLSSSEPNSLCYVETAELDGETNLKFK
MSLEITDQYLQREDTLATFDGFIECEEPNNRLDKFTGTLFWRNTSFPLDADKILLRGCVI
RNTDFCHGLVIFAGADTKIMKNSGKTRFKRTKIDYLMNYMVYTIFVVLILLSAGLAIGHA
YWEAQVGNSSWYLYDGEDDTPSYRGFLIFWGYIIVLNTMVPISLYVSVEVIRLGQSHFIN
WDLQMYYAEKDTPAKARTTTLNEQLGQIHYIFSDKTGTLTQNIMTFKKCCINGQIYGDHR
DASQHNHNKIEQVDFSWNTYADGKLAFYDHYLIEQIQSGKEPEVRQFFFLLAVCHTVMVD
RTDGQLNYQAASPDEGALVNAARNFGFAFLARTQNTITISELGTERTYNVLAILDFNSDR
KRMSIIVRTPEGNIKLYCKGADTVIYERLHRMNPTKQETQDALDIFANETLRTLCLCYKE
IEEKEFTEWNKKFMAASVASTNRDEALDKVYEEIEKDLILLGATAIEDKLQDGVPETISK
LAKADIKIWVLTGDKKETAENIGFACELLTEDTTICYGEDINSLLHARMENQRNRGGVYA
KFAPPVQESFFPPGGNRALIITGSWLNEILLEKKTKRNKILKLKFPRTEEERRMRTQSKR
RLEAKKEQRQKNFVDLACECSAVICCRVTPKQKAMVVDLVKRYKKAITLAIGDGANDVNM
IKTAHIGVGISGQEGMQAVMSSDYSFAQFRYLQRLLLVHGRWSYIRMCKFLRYFFYKNFA
FTLVHFWYSFFNGYSAQTAYEDWFITLYNVLYTSLPVLLMGLLDQDVSDKLSLRFPGLYI
VGQRDLLFNYKRFFVSLLHGVLTSMILFFIPLGAYLQTVGQDGEAPSDYQSFAVTIASAL
VITVNFQIGLDTSYWTFVNAFSIFGSIALYFGIMFDFHSAGIHVLFPSAFQFTGTASNAL
RQPYIWLTIILAVAVCLLPVVAIRFLSMTIWPSESDKIQKHRKRLKAEEQWQRRQQVFRR
GVSTRRSAYAFSHQRGYADLISSGRSIRKKRSPLDAIVADGTAEYRRTGDS
|
| Enzyme 17 Number of Residues |
1251 |
| Enzyme 17 Molecular Weight |
143694.1 |
| Enzyme 17 Theoretical pI |
7.16 |
| Enzyme 17 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 17 General Function |
Involved in ATP binding |
| Enzyme 17 Specific Function |
May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids in the canicular membrane. May have a role in transport of bile acids into the canaliculus, uptake of bile acids from intestinal contents into intestinal mucosa or both |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
- 109-130
137-156
341-362
390-411
950-970
983-1002
1033-1054
1069-1091
1098-1118
1139-1163
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
5031697  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
O43520  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
AT8B1_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>3756 bp
ATGAGTACAGAAAGAGACTCAGAAACGACATTTGACGAGGATTCTCAGCCTAATGACGAA
GTGGTTCCCTACAGTGATGATGAAACAGAAGATGAACTTGATGACCAGGGGTCTGCTGTT
GAACCAGAACAAAACCGAGTCAACAGGGAAGCAGAGGAGAACCGGGAGCCATTCAGAAAA
GAATGTACATGGCAAGTCAAAGCAAACGATCGCAAGTACCACGAACAACCTCACTTTATG
AACACAAAATTCTTGTGTATTAAGGAGAGTAAATATGCGAATAATGCAATTAAAACATAC
AAGTACAACGCATTTACCTTTATACCAATGAATCTGTTTGAGCAGTTTAAGAGAGCAGCC
AATTTATATTTCCTGGCTCTTCTTATCTTACAGGCAGTTCCTCAAATCTCTACCCTGGCT
TGGTACACCACACTAGTGCCCCTGCTTGTGGTGCTGGGCGTCACTGCAATCAAAGACCTG
GTGGACGATGTGGCTCGCCATAAAATGGATAAGGAAATCAACAATAGGACGTGTGAAGTC
ATTAAGGATGGCAGGTTCAAAGTTGCTAAGTGGAAAGAAATTCAAGTTGGAGACGTCATT
CGTCTGAAAAAAAATGATTTTGTTCCAGCTGACATTCTCCTGCTGTCTAGCTCTGAGCCT
AACAGCCTCTGCTATGTGGAAACAGCAGAACTGGATGGAGAAACCAATTTAAAATTTAAG
ATGTCACTTGAAATCACAGACCAGTACCTCCAAAGAGAAGATACATTGGCTACATTTGAT
GGTTTTATTGAATGTGAAGAACCCAATAACAGACTAGATAAGTTTACAGGAACACTATTT
TGGAGAAACACAAGTTTTCCTTTGGATGCTGATAAAATTTTGTTACGTGGCTGTGTAATT
AGGAACACCGATTTCTGCCACGGCTTAGTCATTTTTGCAGGTGCTGACACTAAAATAATG
AAGAATAGTGGGAAAACCAGATTTAAAAGAACTAAAATTGATTACTTGATGAACTACATG
GTTTACACGATCTTTGTTGTTCTTATTCTGCTTTCTGCTGGTCTTGCCATCGGCCATGCT
TATTGGGAAGCACAGGTGGGCAATTCCTCTTGGTACCTCTATGATGGAGAAGACGATACA
CCCTCCTACCGTGGATTCCTCATTTTCTGGGGCTATATCATTGTTCTCAACACCATGGTA
CCCATCTCTCTCTATGTCAGCGTGGAAGTGATTCGTCTTGGACAGAGTCACTTCATCAAC
TGGGACCTGCAAATGTACTATGCTGAGAAGGACACACCCGCAAAAGCTAGAACCACCACA
CTCAATGAACAGCTCGGGCAGATCCATTATATCTTCTCTGATAAGACGGGGACACTCACA
CAAAATATCATGACCTTTAAAAAGTGCTGTATCAACGGGCAGATATATGGGGACCATCGG
GATGCCTCTCAACACAACCACAACAAAATAGAGCAAGTTGATTTTAGCTGGAATACATAT
GCTGATGGGAAGCTTGCATTTTATGACCACTATCTTATTGAGCAAATCCAGTCAGGGAAA
GAGCCAGAAGTACGACAGTTCTTCTTCTTGCTCGCAGTTTGCCACACAGTCATGGTGGAT
AGGACTGATGGTCAGCTCAACTACCAGGCAGCCTCTCCCGATGAAGGTGCCCTGGTAAAC
GCTGCCAGGAACTTTGGCTTTGCCTTCCTCGCCAGGACCCAGAACACCATCACCATCAGT
GAACTGGGCACTGAAAGGACTTACAATGTTCTTGCCATTTTGGACTTCAACAGTGACCGG
AAGCGAATGTCTATCATTGTAAGAACCCCAGAAGGCAATATCAAGCTTTACTGTAAAGGT
GCTGACACTGTTATTTATGAACGGTTACATCGAATGAATCCTACTAAGCAAGAAACACAG
GATGCCCTGGATATCTTTGCAAATGAAACTCTTAGAACCCTATGCCTTTGCTACAAGGAA
ATTGAAGAAAAAGAATTTACAGAATGGAATAAAAAGTTTATGGCTGCCAGTGTGGCCTCC
ACCAACCGGGACGAAGCTCTGGATAAAGTATATGAGGAGATTGAAAAAGACTTAATTCTC
CTGGGAGCTACAGCTATTGAAGACAAGCTACAGGATGGAGTTCCAGAAACCATTTCAAAA
CTTGCAAAAGCTGACATTAAGATCTGGGTGCTTACTGGAGACAAAAAGGAAACTGCTGAA
AATATAGGATTTGCTTGTGAACTTCTGACTGAAGACACCACCATCTGCTATGGGGAGGAT
ATTAATTCTCTTCTTCATGCAAGGATGGAAAACCAGAGGAATAGAGGTGGCGTCTACGCA
AAGTTTGCACCTCCTGTGCAGGAATCTTTTTTTCCACCCGGTGGAAACCGTGCCTTAATC
ATCACTGGTTCTTGGTTGAATGAAATTCTTCTCGAGAAAAAGACCAAGAGAAATAAGATT
CTGAAGCTGAAGTTCCCAAGAACAGAAGAAGAAAGACGGATGCGGACCCAAAGTAAAAGG
AGGCTAGAAGCTAAGAAAGAGCAGCGGCAGAAAAACTTTGTGGACCTGGCCTGCGAGTGC
AGCGCAGTCATCTGCTGCCGCGTCACCCCCAAGCAGAAGGCCATGGTGGTGGACCTGGTG
AAGAGGTACAAGAAAGCCATCACGCTGGCCATCGGAGATGGGGCCAATGACGTGAACATG
ATCAAAACTGCCCACATTGGCGTTGGAATAAGTGGACAAGAAGGAATGCAAGCTGTCATG
TCGAGTGACTATTCCTTTGCTCAGTTCCGATATCTGCAGAGGCTACTGCTGGTGCATGGC
CGATGGTCTTACATAAGGATGTGCAAGTTCCTACGATACTTCTTTTACAAAAACTTTGCC
TTTACTTTGGTTCATTTCTGGTACTCCTTCTTCAATGGCTACTCTGCGCAGACTGCATAC
GAGGATTGGTTCATCACCCTCTACAACGTGCTGTACACCAGCCTGCCCGTGCTCCTCATG
GGGCTGCTCGACCAGGATGTGAGTGACAAACTGAGCCTCCGATTCCCTGGGTTATACATA
GTGGGACAAAGAGACTTACTATTCAACTATAAGAGATTCTTTGTAAGCTTGTTGCATGGG
GTCCTAACATCGATGATCCTCTTCTTCATACCTCTTGGAGCTTATCTGCAAACCGTAGGG
CAGGATGGAGAGGCACCTTCCGACTACCAGTCTTTTGCCGTCACCATTGCCTCTGCTCTT
GTAATAACAGTCAATTTCCAGATTGGCTTGGATACTTCTTATTGGACTTTTGTGAATGCT
TTTTCAATTTTTGGAAGCATTGCACTTTATTTTGGCATCATGTTTGACTTTCATAGTGCT
GGAATACATGTTCTCTTTCCATCTGCATTTCAATTTACAGGCACAGCTTCAAACGCTCTG
AGACAGCCATACATTTGGTTAACTATCATCCTGACTGTTGCTGTGTGCTTACTACCCGTC
GTTGCCATTCGATTCCTGTCAATGACCATCTGGCCATCAGAAAGTGATAAGATCCAGAAG
CATCGCAAGCGGTTGAAGGCGGAGGAGCAGTGGCAGCGACGGCAGCAGGTGTTCCGCCGG
GGCGTGTCAACGCGGCGCTCGGCCTACGCCTTCTCGCACCAGCGGGGCTACGCGGACCTC
ATCTCCTCCGGGCGCAGCATCCGCAAGAAGCGCTCGCCGCTTGATGCCATCGTGGCGGAT
GGCACCGCGGAGTACAGGCGCACCGGGGACAGCTGA
|
| Enzyme 17 GenBank Gene ID |
NM_005603.4  |
| Enzyme 17 GeneCard ID |
ATP8B1  |
| Enzyme 17 GenAtlas ID |
ATP8B1  |
| Enzyme 17 HGNC ID |
HGNC:3706  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
18q21-q22|18q21.31 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Bull LN, van Eijk MJ, Pawlikowska L, DeYoung JA, Juijn JA, Liao M, Klomp LW, Lomri N, Berger R, Scharschmidt BF, Knisely AS, Houwen RH, Freimer NB: A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis. Nat Genet. 1998 Mar;18(3):219-24. [PubMed
]
- Nusbaum C, Zody MC, Borowsky ML, Kamal M, Kodira CD, Taylor TD, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Abouelleil A, Allen NR, Anderson S, Bloom T, Bugalter B, Butler J, Cook A, DeCaprio D, Engels R, Garber M, Gnirke A, Hafez N, Hall JL, Norman CH, Itoh T, Jaffe DB, Kuroki Y, Lehoczky J, Lui A, Macdonald P, Mauceli E, Mikkelsen TS, Naylor JW, Nicol R, Nguyen C, Noguchi H, O'Leary SB, O'Neill K, Piqani B, Smith CL, Talamas JA, Topham K, Totoki Y, Toyoda A, Wain HM, Young SK, Zeng Q, Zimmer AR, Fujiyama A, Hattori M, Birren BW, Sakaki Y, Lander ES: DNA sequence and analysis of human chromosome 18. Nature. 2005 Sep 22;437(7058):551-5. [PubMed
]
- Halleck MS, Pradhan D, Blackman C, Berkes C, Williamson P, Schlegel RA: Multiple members of a third subfamily of P-type ATPases identified by genomic sequences and ESTs. Genome Res. 1998 Apr;8(4):354-61. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Heibeck TH, Ding SJ, Opresko LK, Zhao R, Schepmoes AA, Yang F, Tolmachev AV, Monroe ME, Camp DG 2nd, Smith RD, Wiley HS, Qian WJ: An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells. J Proteome Res. 2009 Aug;8(8):3852-61. [PubMed
]
- Tygstrup N, Steig BA, Juijn JA, Bull LN, Houwen RH: Recurrent familial intrahepatic cholestasis in the Faeroe Islands. Phenotypic heterogeneity but genetic homogeneity. Hepatology. 1999 Feb;29(2):506-8. [PubMed
]
- Klomp LW, Bull LN, Knisely AS, van Der Doelen MA, Juijn JA, Berger R, Forget S, Nielsen IM, Eiberg H, Houwen RH: A missense mutation in FIC1 is associated with greenland familial cholestasis. Hepatology. 2000 Dec;32(6):1337-41. [PubMed
]
- Klomp LW, Vargas JC, van Mil SW, Pawlikowska L, Strautnieks SS, van Eijk MJ, Juijn JA, Pabon-Pena C, Smith LB, DeYoung JA, Byrne JA, Gombert J, van der Brugge G, Berger R, Jankowska I, Pawlowska J, Villa E, Knisely AS, Thompson RJ, Freimer NB, Houwen RH, Bull LN: Characterization of mutations in ATP8B1 associated with hereditary cholestasis. Hepatology. 2004 Jul;40(1):27-38. [PubMed
]
- Painter JN, Savander M, Ropponen A, Nupponen N, Riikonen S, Ylikorkala O, Lehesjoki AE, Aittomaki K: Sequence variation in the ATP8B1 gene and intrahepatic cholestasis of pregnancy. Eur J Hum Genet. 2005 Apr;13(4):435-9. [PubMed
]
- Mullenbach R, Bennett A, Tetlow N, Patel N, Hamilton G, Cheng F, Chambers J, Howard R, Taylor-Robinson SD, Williamson C: ATP8B1 mutations in British cases with intrahepatic cholestasis of pregnancy. Gut. 2005 Jun;54(6):829-34. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 17 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
6516 |
| Enzyme 18 Name |
Probable phospholipid-transporting ATPase IIA |
| Enzyme 18 Synonyms |
- ATPase class II type 9A
|
| Enzyme 18 Gene Name |
ATP9A |
| Enzyme 18 Protein Sequence |
>Probable phospholipid-transporting ATPase IIA
MTDNIPLQPVRQKKRMDSRPRAGCCEWLRCCGGGEARPRTVWLGHPEKRDQRYPRNVINN
QKYNFFTFLPGVLFNQFKYFFNLYFLLLACSQFVPEMRLGALYTYWVPLGFVLAVTVIRE
AVEEIRCYVRDKEVNSQVYSRLTARGTVKVKSSNIQVGDLIIVEKNQRVPADMIFLRTSE
KNGSCFLRTDQLDGETDWKLRLPVACTQRLPTAADLLQIRSYVYAEEPNIDIHNFVGTFT
REDSDPPISESLSIENTLWAGTVVASGTVVGVVLYTGRELRSVMNTSNPRSKIGLFDLEV
NCLTKILFGALVVVSLVMVALQHFAGRWYLQIIRFLLLFSNIIPISLRVNLDMGKIVYSW
VIRRDSKIPGTVVRSSTIPEQLGRISYLLTDKTGTLTQNEMIFKRLHLGTVAYGLDSMDE
VQSHIFSIYTQQSQDPPAQKGPTLTTKVRRTMSSRVHEAVKAIALCHNVTPVYESNGVTD
QAEAEKQYEDSCRVYQASSPDEVALVQWTESVGLTLVGRDQSSMQLRTPGDQILNFTILQ
IFPFTYESKRMGIIVRDESTGEITFYMKGADVVMAGIVQYNDWLEEECGNMAREGLRVLV
VAKKSLAEEQYQDFEARYVQAKLSVHDRSLKVATVIESLEMEMELLCLTGVEDQLQADVR
PTLETLRNAGIKVWMLTGDKLETATCTAKNAHLVTRNQDIHVFRLVTNRGEAHLELNAFR
RKHDCALVISGDSLEVCLKYYEYEFMELACQCPAVVCCRCAPTQKAQIVRLLQERTGKLT
CAVGDGGNDVSMIQESDCGVGVEGKEGKQASLAADFSITQFKHLGRLLMVHGRNSYKRSA
ALSQFVIHRSLCISTMQAVFSSVFYFASVPLYQGFLIIGYSTIYTMFPVFSLVLDKDVKS
EVAMLYPELYKDLLKGRPLSYKTFLIWVLISIYQGSTIMYGALLLFESEFVHIVAISFTS
LILTELLMVALTIQTWHWLMTVAELLSLACYIASLVFLHEFIDVYFIATLSFLWKVSVIT
LVSCLPLYVLKYLRRRFSPPSYSKLTS
|
| Enzyme 18 Number of Residues |
1047 |
| Enzyme 18 Molecular Weight |
118581.5 |
| Enzyme 18 Theoretical pI |
7.81 |
| Enzyme 18 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 18 General Function |
Involved in ATP binding |
| Enzyme 18 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 18 Pathways |
Not Available |
| Enzyme 18 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
- 70-91
97-119
304-325
333-354
842-862
875-893
924-942
950-972
979-999
1007-1030
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
65301139  |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
O75110  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
ATP9A_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>3144 bp
ATGACGGACAACATCCCGCTGCAGCCGGTGCGCCAGAAGAAGCGGATGGACAGCAGGCCC
CGCGCCGGGTGCTGCGAGTGGCTGAGATGCTGCGGTGGAGGGGAGGCCAGGCCCCGCACT
GTCTGGCTGGGGCACCCCGAGAAGAGAGACCAGAGGTATCCTCGGAATGTCATCAACAAT
CAGAAGTACAATTTCTTCACCTTTCTTCCTGGGGTGCTGTTCAACCAGTTCAAATACTTT
TTCAACCTCTATTTCTTACTTCTTGCCTGCTCTCAGTTTGTTCCCGAAATGAGACTTGGT
GCACTCTATACCTACTGGGTTCCCCTGGGCTTCGTGCTGGCCGTCACTGTCATCCGTGAG
GCGGTGGAGGAGATCCGATGCTACGTGCGGGACAAGGAAGTCAACTCCCAGGTCTACAGC
CGGCTCACAGCACGAGGCACAGTGAAGGTGAAGAGTTCTAACATCCAAGTTGGAGACCTT
ATCATCGTTGAAAAGAACCAGCGGGTCCCTGCCGACATGATCTTCCTGAGGACATCAGAA
AAAAACGGGTCATGCTTCTTGCGGACGGATCAGCTGGATGGGGAGACGGACTGGAAGCTG
CGGCTTCCCGTGGCCTGCACGCAGAGGCTCCCCACGGCCGCCGACCTTCTTCAGATTCGA
TCGTATGTGTACGCAGAAGAGCCAAATATTGACATTCACAACTTCGTGGGAACTTTTACC
CGAGAAGACAGCGACCCCCCGATCAGCGAGAGCCTGAGCATAGAGAACACGCTGTGGGCT
GGCACTGTGGTCGCATCAGGTACTGTTGTGGGTGTTGTTCTTTACACTGGCAGAGAACTC
CGGAGTGTCATGAATACCTCAAATCCCCGAAGTAAGATCGGCCTGTTCGACTTGGAAGTG
AACTGCCTCACCAAGATCCTCTTTGGTGCCCTGGTGGTGGTCTCGCTGGTCATGGTTGCC
CTTCAGCACTTTGCAGGCCGTTGGTACCTGCAGATCATCCGCTTCCTCCTCTTGTTTTCC
AACATCATCCCCATTAGTTTGCGCGTGAACCTGGACATGGGCAAGATCGTGTACAGCTGG
GTGATTCGAAGGGACTCGAAAATCCCCGGGACCGTGGTTCGCTCCAGCACGATTCCTGAG
CAGCTGGGCAGGATTTCGTACTTACTCACAGACAAGACAGGCACTCTTACCCAGAACGAG
ATGATTTTCAAACGGCTCCATCTCGGAACAGTAGCCTACGGCCTCGACTCAATGGACGAA
GTACAAAGCCACATTTTCAGCATTTACACCCAGCAATCCCAGGACCCACCGGCTCAGAAG
GGCCCAACGCTCACCACTAAGGTCCGGCGGACCATGAGCAGCCGCGTGCACGAAGCCGTG
AAGGCCATCGCGCTCTGCCACAACGTGACTCCCGTGTATGAGTCCAACGGTGTGACTGAT
CAGGCTGAGGCCGAGAAGCAGTACGAAGACTCCTGCCGCGTATACCAGGCATCCAGCCCC
GATGAGGTGGCCCTGGTACAGTGGACGGAAAGTGTGGGCTTAACCCTGGTGGGCCGAGAC
CAGTCTTCCATGCAGCTGAGGACCCCTGGCGACCAGATCCTGAACTTCACCATCCTACAG
ATCTTCCCTTTCACCTATGAAAGCAAACGTATGGGCATCATCGTGCGGGATGAATCAACT
GGAGAAATTACGTTTTACATGAAGGGAGCAGATGTGGTCATGGCTGGCATTGTGCAGTAC
AATGACTGGTTGGAGGAAGAGTGTGGCAACATGGCCCGAGAAGGGCTGCGGGTGCTCGTG
GTGGCAAAGAAGTCTCTTGCAGAGGAGCAGTATCAGGACTTTGAAGCCCGCTACGTCCAG
GCCAAGCTGAGTGTGCACGACCGCTCCCTCAAAGTGGCCACGGTGATCGAGAGCCTGGAG
ATGGAGATGGAACTGCTGTGCCTGACGGGCGTGGAGGACCAGCTGCAGGCAGATGTGCGG
CCCACGCTGGAGACCCTGAGGAATGCTGGCATCAAGGTTTGGATGCTGACAGGGGACAAG
CTGGAGACAGCTACGTGCACAGCGAAGAATGCACATCTGGTGACCAGAAACCAAGACATC
CACGTTTTTCGGCTGGTGACCAACCGCGGGGAGGCTCACCTCGAGCTGAACGCCTTCCGC
AGGAAGCATGATTGTGCCCTGGTCATCTCGGGAGACTCCCTGGAGGTTTGCCTCAAGTAC
TATGAGTACGAGTTCATGGAGCTGGCCTGCCAGTGCCCGGCCGTAGTCTGCTGCCGATGT
GCCCCCACCCAGAAGGCCCAGATCGTGCGCCTGCTTCAGGAGCGCACGGGCAAGCTCACC
TGTGCAGTAGGGGACGGAGGCAATGACGTCAGCATGATTCAGGAATCTGACTGCGGCGTG
GGAGTGGAAGGAAAGGAAGGAAAACAGGCTTCGTTGGCTGCAGACTTCTCCATCACTCAA
TTTAAGCATCTTGGCCGGTTGCTTATGGTGCATGGCCGGAACAGCTACAAGCGGTCAGCC
GCCCTCAGCCAGTTCGTGATTCACAGGAGCCTCTGTATCAGCACCATGCAGGCTGTCTTT
TCCTCCGTGTTTTACTTTGCCTCCGTCCCTCTCTATCAAGGATTCCTCATCATTGGGTAC
TCCACAATTTACACCATGTTTCCTGTGTTTTCTCTGGTCCTGGACAAAGATGTCAAATCG
GAAGTTGCCATGCTGTATCCTGAGCTCTACAAGGATCTTCTCAAGGGACGGCCGTTGTCC
TACAAGACATTCTTAATATGGGTTTTGATTAGCATCTATCAAGGGAGCACCATCATGTAC
GGGGCGCTGCTGCTGTTTGAGTCGGAGTTCGTGCACATCGTGGCCATCTCCTTCACCTCG
CTGATCCTCACCGAGCTGCTCATGGTGGCGCTGACCATCCAGACCTGGCACTGGCTCATG
ACAGTGGCGGAGCTGCTCAGCCTGGCCTGCTACATCGCCTCCCTGGTGTTCTTACACGAG
TTCATCGATGTGTACTTCATCGCCACCTTGTCATTCTTGTGGAAAGTCTCCGTCATCACT
CTGGTCAGCTGCCTCCCCCTCTATGTCCTCAAGTACCTGCGAAGACGGTTCTCTCCCCCC
AGCTACTCAAAGCTCACATCATAG
|
| Enzyme 18 GenBank Gene ID |
NM_006045.1  |
| Enzyme 18 GeneCard ID |
ATP9A  |
| Enzyme 18 GenAtlas ID |
ATP9A  |
| Enzyme 18 HGNC ID |
HGNC:13540  |
| Enzyme 18 Chromosome Location |
2 |
| Enzyme 18 Locus |
20q13.2 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Ishikawa K, Nagase T, Suyama M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro. DNA Res. 1998 Jun 30;5(3):169-76. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 18 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
6535 |
| Enzyme 19 Name |
Probable phospholipid-transporting ATPase VD |
| Enzyme 19 Synonyms |
- ATPase class V type 10D
|
| Enzyme 19 Gene Name |
ATP10D |
| Enzyme 19 Protein Sequence |
>Probable phospholipid-transporting ATPase VD
MTEALQWARYHWRRLIRGATRDDDSGPYNYSSLLACGRKSSQTPKLSGRHRIVVPHIQPF
KDEYEKFSGAYVNNRIRTTKYTLLNFVPRNLFEQFHRAANLYFLFLVVLNWVPLVEAFQK
EITMLPLVVVLTIIAIKDGLEDYRKYKIDKQINNLITKVYSRKEKKYIDRCWKDVTVGDF
IRLSCNEVIPADMVLLFSTDPDGICHIETSGLDGESNLKQRQVVRGYAEQDSEVDPEKFS
SRIECESPNNDLSRFRGFLEHSNKERVGLSKENLLLRGCTIRNTEAVVGIVVYAGHETKA
MLNNSGPRYKRSKLERRANTDVLWCVMLLVIMCLTGAVGHGIWLSRYEKMHFFNVPEPDG
HIISPLLAGFYMFWTMIILLQVLIPISLYVSIEIVKLGQIYFIQSDVDFYNEKMDSIVQC
RALNIAEDLGQIQYLFSDKTGTLTENKMVFRRCSVAGFDYCHEENARRLESYQEAVSEDE
DFIDTVSGSLSNMAKPRAPSCRTVHNGPLGNKPSNHLAGSSFTLGSGEGASEVPHSRQAA
FSSPIETDVVPDTRLLDKFSQITPRLFMPLDETIQNPPMETLYIIDFFIALAICNTVVVS
APNQPRQKIRHPSLGGLPIKSLEEIKSLFQRWSVRRSSSPSLNSGKEPSSGVPNAFVSRL
PLFSRMKPASPVEEEVSQVCESPQCSSSSACCTETEKQHGDAGLLNGKAESLPGQPLACN
LCYEAESPDEAALVYAARAYQCTLRSRTPEQVMVDFAALGPLTFQLLHILPFDSVRKRMS
VVVRHPLSNQVVVYTKGADSVIMELLSVASPDGASLEKQQMIVREKTQKHLDDYAKQGLR
TLCIAKKVMSDTEYAEWLRNHFLAETSIDNREELLLESAMRLENKLTLLGATGIEDRLQE
GVPESIEALHKAGIKIWMLTGDKQETAVNIAYACKLLEPDDKLFILNTQSKDACGMLMST
ILKELQKKTQALPEQVSLSEDLLQPPVPRDSGLRAGLIITGKTLEFALQESLQKQFLELT
SWCQAVVCCRATPLQKSEVVKLVRSHLQVMTLAIGDGANDVSMIQVADIGIGVSGQEGMQ
AVMASDFAVSQFKHLSKLLLVHGHWCYTRLSNMILYFFYKNVAYVNLLFWYQFFCGFSGT
SMTDYWVLIFFNLLFTSAPPVIYGVLEKDVSAETLMQLPELYRSGQKSEAYLPHTFWITL
LDAFYQSLVCFFVPYFTYQGSDTDIFAFGNPLNTAALFIVLLHLVIESKSLTWIHLLVII
GSILSYFLFAIVFGAMCVTCNPPSNPYWIMQEHMLDPVFYLVCILTTSIALLPRFVYRVL
QGSLFPSPILRAKHFDRLTPEERTKALKKWRGAGKMNQVTSKYANQSAGKSGRRPMPGPS
AVFAMKSASSCAIEQGNLSLCETALDQGYSETKAFEMAGPSKGKES
|
| Enzyme 19 Number of Residues |
1426 |
| Enzyme 19 Molecular Weight |
160272.3 |
| Enzyme 19 Theoretical pI |
7.15 |
| Enzyme 19 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 19 General Function |
Involved in ATP binding |
| Enzyme 19 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 19 Pathways |
Not Available |
| Enzyme 19 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
- 98-118
122-142
322-342
366-386
1114-1134
1146-1166
1196-1216
1225-1245
1253-1273
1293-1313
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
222352161  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9P241  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
AT10D_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>4281 bp
ATGACTGAGGCTCTCCAATGGGCCAGATATCACTGGCGACGGCTGATCAGAGGTGCAACC
AGGGATGATGATTCAGGGCCATACAACTATTCCTCGTTGCTCGCCTGTGGGCGCAAGTCC
TCTCAGACCCCTAAACTGTCAGGAAGGCACCGGATTGTTGTTCCCCACATCCAGCCCTTC
AAGGATGAGTATGAGAAGTTCTCCGGAGCCTATGTGAACAATCGAATACGAACAACAAAG
TACACACTTCTGAATTTTGTGCCAAGAAATTTATTTGAACAATTTCACAGAGCTGCCAAT
TTATATTTCCTGTTCCTAGTTGTCCTGAACTGGGTACCTTTGGTAGAAGCCTTCCAAAAG
GAAATCACCATGTTGCCTCTGGTGGTGGTCCTTACAATTATCGCAATTAAAGATGGCCTG
GAAGATTATCGGAAATACAAAATTGACAAACAGATCAATAATTTAATAACTAAAGTTTAT
AGTAGGAAAGAGAAAAAATACATTGACCGATGCTGGAAAGACGTTACTGTTGGGGACTTT
ATTCGCCTCTCCTGCAACGAGGTCATCCCTGCAGACATGGTACTACTCTTTTCCACTGAT
CCAGATGGAATCTGTCACATTGAGACTTCTGGTCTTGATGGAGAGAGCAATTTAAAACAG
AGGCAGGTGGTTCGGGGATATGCAGAACAGGACTCTGAAGTTGATCCTGAGAAGTTTTCC
AGTAGGATAGAATGTGAAAGCCCAAACAATGACCTCAGCAGATTCCGAGGCTTCCTAGAA
CATTCCAACAAAGAACGCGTGGGTCTCAGTAAAGAAAATTTGTTGCTTAGAGGATGCACC
ATTAGAAACACAGAGGCTGTTGTGGGCATTGTGGTTTATGCAGGCCATGAAACCAAAGCA
ATGCTGAACAACAGTGGGCCACGGTATAAGCGCAGCAAATTAGAAAGAAGAGCAAACACA
GATGTCCTCTGGTGTGTCATGCTTCTGGTCATAATGTGCTTAACTGGCGCAGTAGGTCAT
GGAATCTGGCTGAGCAGGTATGAAAAGATGCATTTTTTCAATGTTCCCGAGCCTGATGGA
CATATCATATCACCACTGTTGGCAGGATTTTATATGTTTTGGACCATGATCATTTTGTTA
CAGGTCTTGATTCCTATTTCTCTCTATGTTTCCATCGAAATTGTGAAGCTTGGACAAATA
TATTTCATTCAAAGTGATGTGGATTTCTACAATGAAAAAATGGATTCTATTGTTCAGTGC
CGAGCCCTGAACATCGCCGAGGATCTGGGACAGATTCAGTACCTCTTTTCCGATAAGACA
GGAACCCTCACTGAGAATAAGATGGTTTTTCGAAGATGTAGTGTGGCAGGATTTGATTAC
TGCCATGAAGAAAATGCCAGGAGGTTGGAGTCCTATCAGGAAGCTGTCTCTGAAGATGAA
GATTTTATAGACACAGTCAGTGGTTCCCTCAGCAATATGGCAAAACCGAGAGCCCCCAGC
TGCAGGACAGTTCATAATGGGCCTTTGGGAAATAAGCCCTCAAATCATCTTGCTGGGAGC
TCTTTTACTCTAGGAAGTGGAGAAGGAGCCAGTGAAGTGCCTCATTCCAGACAGGCTGCT
TTCAGTAGCCCCATTGAAACAGACGTGGTACCAGACACCAGGCTTTTAGACAAATTTAGT
CAGATTACACCTCGGCTCTTTATGCCACTAGATGAGACCATCCAAAATCCACCAATGGAA
ACTTTGTACATTATCGACTTTTTCATTGCATTGGCAATTTGCAACACAGTAGTGGTTTCT
GCTCCTAACCAACCCCGACAAAAGATCAGACACCCTTCACTGGGGGGGTTGCCCATTAAG
TCTTTGGAAGAGATTAAAAGTCTTTTCCAGAGATGGTCTGTCCGAAGATCAAGTTCTCCA
TCGCTTAACAGTGGGAAAGAGCCATCTTCTGGAGTTCCAAACGCCTTTGTGAGCAGACTC
CCTCTCTTTAGTCGAATGAAACCAGCTTCACCTGTGGAGGAAGAGGTCTCCCAGGTGTGT
GAGAGCCCCCAGTGCTCCAGTAGCTCAGCTTGCTGCACAGAAACAGAGAAACAACACGGT
GATGCAGGCCTCCTGAATGGCAAGGCAGAGTCCCTCCCTGGACAGCCATTGGCCTGCAAC
CTGTGTTATGAGGCCGAGAGCCCAGACGAAGCGGCCTTAGTGTATGCCGCCAGGGCTTAC
CAATGCACTTTACGGTCTCGGACACCAGAGCAGGTCATGGTGGACTTTGCTGCTTTGGGA
CCATTAACATTTCAACTCCTACACATCCTGCCCTTTGACTCAGTAAGAAAAAGAATGTCT
GTTGTGGTCCGACACCCTCTTTCCAATCAAGTTGTGGTGTATACGAAAGGCGCTGATTCT
GTGATCATGGAGTTACTGTCGGTGGCTTCCCCAGATGGAGCAAGTCTGGAGAAACAACAG
ATGATAGTAAGGGAGAAAACCCAGAAGCACTTGGATGACTATGCCAAACAAGGCCTTCGT
ACTTTATGTATAGCAAAGAAGGTCATGAGTGACACTGAATATGCAGAGTGGCTGAGGAAT
CATTTTTTAGCTGAAACCAGCATTGACAACAGGGAAGAATTACTACTTGAATCTGCCATG
AGGTTGGAGAACAAACTTACATTACTTGGTGCTACTGGCATTGAAGACCGTCTGCAGGAG
GGAGTCCCTGAATCTATAGAAGCTCTTCACAAAGCGGGCATCAAGATCTGGATGCTGACA
GGGGACAAGCAGGAGACAGCTGTCAACATAGCTTATGCATGCAAACTACTGGAGCCAGAT
GACAAGCTTTTTATCCTCAATACCCAAAGTAAAGATGCCTGTGGGATGCTGATGAGCACA
ATTTTGAAAGAACTTCAGAAGAAAACTCAAGCCCTGCCAGAGCAAGTGTCATTAAGTGAA
GATTTACTTCAGCCTCCTGTCCCCCGGGACTCAGGGTTACGAGCTGGACTCATTATCACT
GGGAAGACCCTGGAGTTTGCCCTGCAAGAAAGTCTGCAAAAGCAGTTCCTGGAACTGACA
TCTTGGTGTCAAGCTGTGGTCTGCTGCCGAGCCACACCGCTGCAGAAAAGTGAAGTGGTG
AAATTGGTCCGCAGCCATCTCCAGGTGATGACCCTTGCTATTGGTGATGGTGCCAATGAT
GTTAGCATGATACAAGTGGCAGACATTGGGATAGGGGTCTCAGGTCAAGAAGGCATGCAG
GCTGTGATGGCCAGTGACTTTGCCGTTTCTCAGTTCAAACATCTCAGCAAGCTCCTTCTT
GTCCATGGACACTGGTGTTATACACGGCTTTCCAACATGATTCTCTATTTTTTCTATAAG
AATGTGGCCTATGTGAACCTCCTTTTCTGGTACCAGTTCTTTTGTGGATTTTCAGGAACA
TCCATGACTGATTACTGGGTTTTGATCTTCTTCAACCTCCTCTTCACATCTGCCCCTCCT
GTCATTTATGGTGTTTTGGAGAAAGATGTGTCTGCAGAGACCCTCATGCAACTGCCTGAA
CTTTACAGAAGTGGTCAGAAATCAGAGGCATACTTACCCCATACCTTCTGGATCACCTTA
TTGGATGCTTTTTATCAAAGCCTGGTCTGCTTCTTTGTGCCTTATTTTACCTACCAGGGC
TCAGATACTGACATCTTTGCATTTGGAAACCCCCTGAACACAGCCGCTCTGTTCATCGTT
CTCCTCCATCTGGTCATTGAAAGCAAGAGTTTGACTTGGATTCACTTGCTGGTCATCATT
GGTAGCATCTTGTCTTATTTTTTATTTGCCATAGTTTTTGGAGCCATGTGTGTAACTTGC
AACCCACCATCCAACCCTTACTGGATTATGCAGGAGCACATGCTGGATCCAGTATTCTAC
TTAGTTTGTATCCTCACGACGTCCATTGCTCTTCTGCCCAGGTTTGTATACAGAGTTCTT
CAGGGATCCCTGTTTCCATCTCCAATTCTGAGAGCTAAGCACTTTGACAGACTAACTCCA
GAGGAGAGGACTAAAGCTCTCAAGAAGTGGAGAGGGGCTGGAAAGATGAATCAAGTGACA
TCAAAGTATGCTAACCAATCAGCTGGCAAGTCAGGAAGAAGACCCATGCCTGGCCCTTCT
GCTGTATTTGCAATGAAGTCAGCAAGTTCCTGTGCTATTGAGCAAGGAAACTTATCTCTG
TGTGAAACTGCTTTAGATCAAGGCTACTCTGAAACTAAGGCCTTTGAGATGGCTGGACCC
TCCAAAGGTAAAGAAAGCTAG
|
| Enzyme 19 GenBank Gene ID |
NM_020453.3  |
| Enzyme 19 GeneCard ID |
ATP10D  |
| Enzyme 19 GenAtlas ID |
ATP10D  |
| Enzyme 19 HGNC ID |
HGNC:13549  |
| Enzyme 19 Chromosome Location |
4 |
| Enzyme 19 Locus |
4p12 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Flamant S, Pescher P, Lemercier B, Clement-Ziza M, Kepes F, Fellous M, Milon G, Marchal G, Besmond C: Characterization of a putative type IV aminophospholipid transporter P-type ATPase. Mamm Genome. 2003 Jan;14(1):21-30. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Nagase T, Kikuno R, Ishikawa K, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Apr 28;7(2):143-50. [PubMed
]
|
| Enzyme 19 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
6543 |
| Enzyme 20 Name |
Probable phospholipid-transporting ATPase IB |
| Enzyme 20 Synonyms |
- ATPase class I type 8A member 2
- ML-1
|
| Enzyme 20 Gene Name |
ATP8A2 |
| Enzyme 20 Protein Sequence |
>Probable phospholipid-transporting ATPase IB
MSRATSVGDQLEAPARTIYLNQPHLNKFRDNQISTAKYSVLTFLPRFLYEQIRRAANAFF
LFIALLQQIPDVSPTGRYTTLVPLIIILTIAGIKEIVEDFKRHKADNAVNKKKTIVLRNG
MWHTIMWKEVAVGDIVKVVNGQYLPADVVLLSSSEPQAMCYVETANLDGETNLKIRQGLS
HTADMQTREVLMKLSGTIECEGPNRHLYDFTGNLNLDGKSLVALGPDQILLRGTQLRNTQ
WVFGIVVYTGHDTKLMQNSTKAPLKRSNVEKVTNVQILVLFGILLVMALVSSAGALYWNR
SHGEKNWYIKKMDTTSDNFGYNLLTFIILYNNLIPISLLVTLEVVKYTQALFINWDTDMY
YIGNDTPAMARTSNLNEELGQVKYLFSDKTGTLTCNIMNFKKCSIAGVTYGHFPELAREP
SSDDFCRMPPPCSDSCDFDDPRLLKNIEDRHPTAPCIQEFLTLLAVCHTVVPEKDGDNII
YQASSPDEAALVKGAKKLGFVFTARTPFSVIIEAMGQEQTFGILNVLEFSSDRKRMSVIV
RTPSGRLRLYCKGADNVIFERLSKDSKYMEETLCHLEYFATEGLRTLCVAYADLSENEYE
EWLKVYQEASTILKDRAQRLEECYEIIEKNLLLLGATAIEDRLQAGVPETIATLLKAEIK
IWVLTGDKQETAINIGYSCRLVSQNMALILLKEDSLDATRAAITQHCTDLGNLLGKENDV
ALIIDGHTLKYALSFEVRRSFLDLALSCKAVICCRVSPLQKSEIVDVVKKRVKAITLAIG
DGANDVGMIQTAHVGVGISGNEGMQATNNSDYAIAQFSYLEKLLLVHGAWSYNRVTKCIL
YCFYKNVVLYIIELWFAFVNGFSGQILFERWCIGLYNVIFTALPPFTLGIFERSCTQESM
LRFPQLYKITQNGEGFNTKVFWGHCINALVHSLILFWFPMKALEHDTVLTSGHATDYLFV
GNIVYTYVVVTVCLKAGLETTAWTKFSHLAVWGSMLTWLVFFGIYSTIWPTIPIAPDMRG
QATMVLSSAHFWLGLFLVPTACLIEDVAWRAAKHTCKKTLLEEVQELETKSRVLGKAVLR
DSNGKRLNERDRLIKRLGRKTPPTLFRGSSLQQGVPHGYAFSQEEHGAVSQEEVIRAYDT
TKKKSRKK
|
| Enzyme 20 Number of Residues |
1148 |
| Enzyme 20 Molecular Weight |
129240.4 |
| Enzyme 20 Theoretical pI |
7.84 |
| Enzyme 20 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 20 General Function |
Involved in ATP binding |
| Enzyme 20 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
- 45-66
72-94
277-298
324-345
838-858
871-890
921-942
957-979
986-1006
1025-1049
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
117168245  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q9NTI2  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
AT8A2_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>3567 bp
ATGCTGAACGGCGCAGGCCTGGACAAAGCTCTTAAGATGTCCCTGCCGCGGAGGTCGAGG
ATCCGCTCGTCCGTGGGACCTGTTCGTTCTTCTTTGGGCTATAAGAAGGCAGAGGATGAG
ATGTCCCGGGCCACGTCTGTTGGAGACCAGCTGGAGGCACCCGCCCGCACCATTTACCTC
AACCAACCGCATCTCAACAAATTCCGCGACAACCAGATCAGTACGGCCAAGTACAGCGTG
TTGACATTTCTACCTCGATTCTTGTATGAGCAGATTAGAAGAGCTGCTAATGCCTTCTTT
CTCTTCATTGCCTTATTACAGCAAATTCCAGATGTATCTCCAACAGGAAGATATACCACC
CTGGTGCCATTGATCATTATTTTAACAATTGCAGGCATCAAAGAGATTGTAGAAGATTTT
AAGCGACACAAGGCAGACAATGCAGTTAACAAAAAGAAAACAATAGTGTTAAGAAATGGT
ATGTGGCATACCATTATGTGGAAAGAGGTGGCAGTGGGAGACATTGTGAAGGTCGTCAAT
GGGCAGTATCTTCCAGCAGATGTGGTCCTGCTGTCATCCAGTGAACCTCAGGCAATGTGT
TATGTTGAAACAGCTAATCTGGATGGGGAGACGAACCTTAAAATACGTCAGGGTTTGAGT
CACACTGCTGACATGCAAACACGTGAAGTTCTGATGAAGTTATCTGGAACTATAGAGTGT
GAAGGGCCCAACCGCCACCTCTATGACTTCACTGGAAACTTGAACTTAGATGGGAAAAGC
CTTGTTGCCCTTGGGCCTGACCAGATCTTATTAAGAGGTACACAGCTTAGAAATACTCAG
TGGGTCTTTGGCATAGTTGTTTATACTGGACACGACACCAAACTCATGCAGAATTCAACC
AAAGCGCCTCTCAAGAGATCAAATGTTGAGAAGGTGACTAACGTGCAGATCCTGGTGTTG
TTTGGCATCCTCTTGGTCATGGCCTTGGTGAGCTCGGCGGGGGCCCTGTACTGGAACAGG
TCTCATGGTGAAAAGAACTGGTACATCAAGAAGATGGACACCACCTCAGATAATTTTGGA
TACAACCTACTGACGTTCATCATCTTATACAACAATCTTATTCCCATCAGTCTGTTGGTG
ACTCTTGAGGTTGTGAAGTATACTCAAGCCCTTTTCATAAACTGGGACACAGATATGTAT
TATATAGGAAATGACACTCCTGCCATGGCCAGGACATCAAACCTTAATGAAGAGCTTGGG
CAGGTGAAATATCTCTTTTCTGACAAGACTGGAACGCTTACATGCAATATCATGAACTTT
AAGAAGTGCAGCATTGCCGGAGTAACCTATGGTCACTTCCCAGAATTGGCAAGAGAGCCG
TCTTCAGATGACTTCTGTCGGATGCCTCCTCCCTGTAGTGATTCCTGTGACTTTGATGAC
CCCAGGCTGTTGAAGAACATTGAGGATCGCCATCCCACAGCCCCTTGCATTCAGGAGTTC
CTCACCCTTCTGGCCGTGTGCCACACGGTTGTTCCTGAGAAGGATGGAGATAACATCATC
TACCAGGCCTCTTCCCCAGATGAAGCTGCTTTGGTGAAAGGAGCTAAAAAGCTGGGCTTT
GTCTTCACAGCCAGAACACCATTCTCAGTCATCATAGAAGCGATGGGACAGGAACAAACA
TTCGGAATCCTTAATGTCCTGGAATTTTCTAGTGACAGAAAAAGAATGTCTGTAATTGTT
CGAACTCCTTCAGGACGACTTCGGCTTTACTGTAAAGGGGCTGATAATGTGATTTTTGAG
AGACTTTCAAAAGACTCAAAATATATGGAGGAAACATTATGCCATCTGGAATACTTTGCC
ACGGAAGGCTTGCGGACTCTCTGTGTGGCTTATGCTGATCTCTCTGAGAATGAGTATGAG
GAGTGGCTGAAAGTCTATCAGGAAGCCAGCACCATATTGAAGGACAGAGCTCAACGGTTG
GAAGAGTGTTACGAGATCATTGAGAAGAATTTGCTGCTACTTGGAGCCACAGCCATAGAA
GATCGCCTTCAAGCAGGAGTTCCAGAAACCATCGCAACACTGTTGAAGGCAGAAATTAAA
ATATGGGTGTTGACAGGAGACAAACAAGAAACTGCGATTAATATAGGGTATTCCTGCCGA
TTGGTATCGCAGAATATGGCCCTTATCCTATTGAAGGAGGACTCTTTGGATGCCACAAGG
GCAGCCATTACTCAGCACTGCACTGACCTTGGGAATTTGCTGGGCAAGGAAAATGACGTG
GCCCTGATCATCGATGGCCACACCCTGAAGTACGCGCTCTCCTTCGAAGTCCGGAGGAGT
TTCCTGGATTTGGCACTCTCGTGCAAAGCGGTCATATGCTGCAGAGTGTCTCCTCTGCAG
AAGTCTGAGATAGTGGATGTGGTGAAGAAGCGGGTGAAGGCCATCACCCTCGCCATCGGA
GACGGCGCCAACGATGTCGGGATGATCCAGACAGCCCACGTGGGTGTGGGAATCAGTGGG
AATGAAGGCATGCAGGCCACCAACAACTCGGATTACGCCATCGCACAGTTTTCCTACTTA
GAGAAGCTTCTGTTGGTTCATGGAGCCTGGAGCTACAACCGGGTGACCAAGTGCATCTTG
TACTGCTTCTATAAGAACGTGGTCCTGTATATTATTGAGCTTTGGTTCGCCTTTGTTAAT
GGATTTTCTGGGCAGATTTTATTTGAACGTTGGTGCATCGGCCTGTACAATGTGATTTTC
ACCGCTTTGCCGCCCTTCACTCTGGGAATCTTTGAGAGGTCTTGCACTCAGGAGAGCATG
CTCAGGTTTCCCCAGCTCTACAAAATCACCCAGAATGGCGAAGGCTTCAACACAAAGGTT
TTCTGGGGTCACTGCATCAACGCCTTGGTCCACTCCCTCATCCTCTTCTGGTTTCCCATG
AAAGCTCTGGAGCATGATACTGTGTTGACAAGTGGTCATGCTACCGACTATTTATTTGTT
GGAAATATTGTTTACACATATGTTGTTGTTACTGTTTGTCTGAAAGCTGGTTTGGAGACC
ACAGCTTGGACTAAATTCAGTCATCTGGCTGTCTGGGGAAGCATGCTGACCTGGCTGGTG
TTTTTTGGCATCTACTCGACCATCTGGCCCACCATTCCCATTGCTCCAGATATGAGAGGA
CAGGCAACTATGGTCCTGAGCTCCGCACACTTCTGGTTGGGATTATTTCTGGTTCCTACT
GCCTGTTTGATTGAAGATGTGGCATGGAGAGCAGCCAAGCACACCTGCAAAAAGACATTG
CTGGAGGAGGTGCAGGAGCTGGAAACCAAGTCTCGAGTCCTGGGAAAAGCGGTGCTGCGG
GATAGCAATGGAAAGAGGCTGAACGAGCGCGACCGCCTGATCAAGAGGCTGGGCCGGAAG
ACGCCCCCGACGCTGTTCCGGGGCAGCTCCCTGCAGCAGGGCGTCCCGCATGGGTATGCT
TTTTCTCAAGAAGAACACGGAGCTGTTAGTCAGGAAGAAGTCATCCGTGCTTATGACACC
ACCAAAAAGAAATCCAGGAAGAAATAA
|
| Enzyme 20 GenBank Gene ID |
NM_016529  |
| Enzyme 20 GeneCard ID |
ATP8A2  |
| Enzyme 20 GenAtlas ID |
ATP8A2  |
| Enzyme 20 HGNC ID |
HGNC:13533  |
| Enzyme 20 Chromosome Location |
1 |
| Enzyme 20 Locus |
13q12 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 General References |
- Dunham A, Matthews LH, Burton J, Ashurst JL, Howe KL, Ashcroft KJ, Beare DM, Burford DC, Hunt SE, Griffiths-Jones S, Jones MC, Keenan SJ, Oliver K, Scott CE, Ainscough R, Almeida JP, Ambrose KD, Andrews DT, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Bannerjee R, Barlow KF, Bates K, Beasley H, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burrill W, Carder C, Carter NP, Chapman JC, Clamp ME, Clark SY, Clarke G, Clee CM, Clegg SC, Cobley V, Collins JE, Corby N, Coville GJ, Deloukas P, Dhami P, Dunham I, Dunn M, Earthrowl ME, Ellington AG, Faulkner L, Frankish AG, Frankland J, French L, Garner P, Garnett J, Gilbert JG, Gilson CJ, Ghori J, Grafham DV, Gribble SM, Griffiths C, Hall RE, Hammond S, Harley JL, Hart EA, Heath PD, Howden PJ, Huckle EJ, Hunt PJ, Hunt AR, Johnson C, Johnson D, Kay M, Kimberley AM, King A, Laird GK, Langford CJ, Lawlor S, Leongamornlert DA, Lloyd DM, Lloyd C, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, McLaren SJ, McMurray A, Milne S, Moore MJ, Nickerson T, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter KM, Rice CM, Searle S, Sehra HK, Shownkeen R, Skuce CD, Smith M, Steward CA, Sycamore N, Tester J, Thomas DW, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Wilming L, Wray PW, Wright MW, Young L, Coulson A, Durbin R, Hubbard T, Sulston JE, Beck S, Bentley DR, Rogers J, Ross MT: The DNA sequence and analysis of human chromosome 13. Nature. 2004 Apr 1;428(6982):522-8. [PubMed
]
- Sun XL, Li D, Fang J, Noyes I, Casto B, Theil K, Shuler C, Milo GE: Changes in levels of normal ML-1 gene transcripts associated with the conversion of human nontumorigenic to tumorigenic phenotypes. Gene Expr. 1999;8(2):129-39. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 20 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 21
[top]
|
| Enzyme 21 ID |
6655 |
| Enzyme 21 Name |
Probable phospholipid-transporting ATPase IA |
| Enzyme 21 Synonyms |
- ATPase class I type 8A member 1
- Chromaffin granule ATPase II
|
| Enzyme 21 Gene Name |
ATP8A1 |
| Enzyme 21 Protein Sequence |
>Probable phospholipid-transporting ATPase IA
MPTMRRTVSEIRSRAEGYEKTDDVSEKTSLADQEEVRTIFINQPQLTKFCNNHVSTAKYN
IITFLPRFLYSQFRRAANSFFLFIALLQQIPDVSPTGRYTTLVPLLFILAVAAIKEIIED
IKRHKADNAVNKKQTQVLRNGAWEIVHWEKVAVGEIVKVTNGEHLPADLISLSSSEPQAM
CYIETSNLDGETNLKIRQGLPATSDIKDVDSLMRISGRIECESPNRHLYDFVGNIRLDGH
GTVPLGADQILLRGAQLRNTQWVHGIVVYTGHDTKLMQNSTSPPLKLSNVERITNVQILI
LFCILIAMSLVCSVGSAIWNRRHSGKDWYLNLNYGGASNFGLNFLTFIILFNNLIPISLL
VTLEVVKFTQAYFINWDLDMHYEPTDTAAMARTSNLNEELGQVKYIFSDKTGTLTCNVMQ
FKKCTIAGVAYGHVPEPEDYGCSPDEWQNSQFGDEKTFSDSSLLENLQNNHPTAPIICEF
LTMMAVCHTAVPEREGDKIIYQAASPDEGALVRAAKQLNFVFTGRTPDSVIIDSLGQEER
YELLNVLEFTSARKRMSVIVRTPSGKLRLYCKGADTVIYDRLAETSKYKEITLKHLEQFA
TEGLRTLCFAVAEISESDFQEWRAVYQRASTSVQNRLLKLEESYELIEKNLQLLGATAIE
DKLQDQVPETIETLMKADIKIWILTGDKQETAINIGHSCKLLKKNMGMIVINEGSLDGTR
ETLSRHCTTLGDALRKENDFALIIDGKTLKYALTFGVRQYFLDLALSCKAVICCRVSPLQ
KSEVVEMVKKQVKVVTLAIGDGANDVSMIQTAHVGVGISGNEGLQAANSSDYSIAQFKYL
KNLLMIHGAWNYNRVSKCILYCFYKNIVLYIIEIWFAFVNGFSGQILFERWCIGLYNVMF
TAMPPLTLGIFERSCRKENMLKYPELYKTSQNALDFNTKVFWVHCLNGLFHSVILFWFPL
KALQYGTAFGNGKTSDYLLLGNFVYTFVVITVCLKAGLETSYWTWFSHIAIWGSIALWVV
FFGIYSSLWPAIPMAPDMSGEAAMLFSSGVFWMGLLFIPVASLLLDVVYKVIKRTAFKTL
VDEVQELEAKSQDPGAVVLGKSLTERAQLLKNVFKKNHVNLYRSESLQQNLLHGYAFSQD
ENGIVSQSEVIRAYDTTKQRPDEW
|
| Enzyme 21 Number of Residues |
1164 |
| Enzyme 21 Molecular Weight |
131368.2 |
| Enzyme 21 Theoretical pI |
6.83 |
| Enzyme 21 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 21 General Function |
Involved in ATP binding |
| Enzyme 21 Specific Function |
May play a role in the transport of aminophospholipids from the outer to the inner leaflet of various membranes and the maintenance of asymmetric distribution of phospholipids, mainly in secretory vesicles |
| Enzyme 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
- 66-86
93-115
298-319
345-366
858-878
891-910
941-962
977-999
1006-1026
1045-1070
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
Not Available |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9Y2Q0  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
AT8A1_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>3492 bp
ATGCCCACCATGCGGAGGACCGTGTCGGAGATCCGCTCGCGCGCCGAAGGTTATGAGAAG
ACAGATGATGTTTCAGAGAAGACCTCACTGGCTGACCAGGAGGAAGTAAGGACTATTTTC
ATCAACCAGCCCCAGCTGACAAAATTCTGCAATAACCATGTCAGCACTGCAAAATACAAC
ATAATCACATTCCTTCCAAGATTTCTCTACTCTCAGTTCAGAAGAGCTGCTAATTCATTT
TTTCTCTTTATTGCACTGCTGCAGCAAATACCTGATGTGTCACCAACAGGTCGTTATACA
ACACTGGTTCCTCTCTTATTTATTTTAGCTGTGGCAGCTATCAAAGAGATAATAGAAGAT
ATTAAACGACATAAAGCTGATAATGCAGTGAACAAGAAACAAACGCAAGTTTTGAGAAAT
GGTGCTTGGGAAATTGTCCACTGGGAAAAGGTGGCAGTAGGGGAGATAGTGAAAGTGACC
AATGGGGAACATCTCCCAGCAGATCTCATCAGTCTGTCCTCAAGTGAGCCCCAAGCCATG
TGCTACATTGAAACATCCAACTTAGATGGTGAAACAAACTTGAAAATTAGACAGGGCTTA
CCAGCAACATCAGATATCAAAGACGTTGACAGTTTGATGAGGATTTCTGGCAGAATTGAG
TGTGAAAGTCCAAACAGACATCTCTACGATTTTGTTGGAAACATAAGGCTTGATGGACAT
GGCACCGTTCCACTGGGAGCAGATCAGATTCTTCTTCGAGGAGCTCAGTTGAGAAATACA
CAGTGGGTTCATGGAATAGTTGTCTACACTGGACATGACACCAAGCTGATGCAGAATTCA
ACAAGTCCACCACTTAAGCTCTCAAATGTGGAACGGATTACAAATGTACAAATTTTGATT
TTATTTTGTATCTTAATTGCCATGTCTCTTGTCTGTTCTGTGGGCTCAGCCATTTGGAAT
CGAAGGCATTCTGGAAAAGACTGGTATCTCAATCTAAACTATGGTGGCGCTAGTAATTTT
GGACTGAATTTCTTGACCTTCATCATCCTTTTCAACAATCTCATTCCTATCAGCTTATTG
GTTACATTAGAAGTTGTGAAATTTACCCAGGCATACTTCATAAATTGGGATCTTGACATG
CACTATGAACCCACAGACACTGCTGCTATGGCTCGAACATCTAATCTGAATGAGGAACTT
GGCCAGGTTAAATACATATTTTCTGACAAAACTGGTACTCTGACATGCAATGTAATGCAG
TTTAAGAAGTGCACCATAGCGGGAGTTGCTTATGGCCATGTCCCTGAACCTGAGGATTAT
GGCTGCTCTCCTGATGAATGGCAGAACTCACAGTTTGGAGATGAAAAAACATTTAGTGAT
TCATCATTGCTGGAAAATCTCCAAAATAATCATCCAACTGCACCTATAATATGTGAATTT
CTTACAATGATGGCAGTCTGTCACACAGCAGTGCCAGAGCGAGAAGGTGACAAGATTATT
TATCAAGCAGCATCTCCAGATGAGGGAGCATTGGTCAGAGCAGCCAAGCAATTGAATTTT
GTTTTCACTGGAAGAACACCCGACTCGGTGATTATAGATTCACTGGGGCAGGAAGAAAGA
TATGAATTGCTCAATGTCTTGGAGTTTACCAGTGCTAGGAAAAGAATGTCAGTGATTGTT
CGCACTCCATCTGGAAAGTTACGACTCTACTGCAAAGGAGCTGACACTGTAATTTATGAT
CGACTGGCAGAGACGTCAAAATACAAAGAAATTACCCTAAAACATTTAGAGCAGTTTGCT
ACAGAAGGGTTAAGAACTTTATGTTTTGCTGTGGCTGAGATTTCAGAGAGCGACTTTCAG
GAGTGGCGAGCAGTCTATCAGCGAGCATCTACATCTGTGCAGAACAGGCTACTCAAACTC
GAAGAGAGTTATGAGTTGATTGAAAAGAATCTTCAGCTACTTGGAGCAACAGCCATTGAG
GATAAATTACAAGATCAAGTGCCTGAAACCATAGAAACGCTAATGAAAGCAGACATCAAA
ATCTGGATCCTTACAGGGGACAAGCAAGAAACTGCCATTAACATCGGACACTCCTGCAAA
CTGTTGAAGAAGAACATGGGAATGATTGTTATAAATGAAGGCTCTCTTGATGGAACAAGG
GAAACTCTCAGTCGTCACTGTACTACCCTTGGTGATGCTCTCCGGAAAGAGAATGATTTT
GCTCTTATAATTGATGGGAAAACCCTCAAATATGCCTTAACCTTTGGAGTACGACAGTAT
TTCCTGGACTTAGCTTTGTCATGCAAAGCTGTCATTTGCTGTCGGGTTTCTCCTCTTCAA
AAATCTGAAGTTGTTGAGATGGTTAAGAAACAAGTCAAAGTCGTAACGCTTGCAATCGGT
GATGGAGCAAATGATGTCAGCATGATACAGACAGCGCACGTTGGTGTTGGTATCAGTGGC
AATGAAGGCCTGCAGGCAGCTAATTCCTCTGACTACTCCATAGCTCAGTTCAAATATTTG
AAGAATTTACTGATGATTCATGGTGCCTGGAACTATAACAGAGTCTCCAAGTGCATCTTA
TACTGCTTCTACAAGAATATAGTGCTCTATATTATCGAGATCTGGTTTGCCTTTGTTAAT
GGCTTTTCTGGACAGATCCTCTTTGAAAGATGGTGTATAGGTCTCTATAACGTGATGTTT
ACAGCAATGCCTCCTTTAACTCTTGGAATATTTGAGAGATCATGCAGAAAAGAGAACATG
TTGAAGTACCCTGAATTATACAAAACATCTCAGAATGCCCTGGACTTCAACACCAAGGTT
TTCTGGGTTCATTGTTTAAATGGCCTCTTCCACTCAGTTATTCTGTTTTGGTTTCCACTA
AAAGCCCTTCAGTATGGTACTGCATTTGGAAATGGGAAAACCTCGGATTATCTGCTACTG
GGAAACTTTGTGTACACTTTTGTGGTGATAACTGTGTGTTTGAAAGCTGGATTGGAGACA
TCATATTGGACATGGTTCAGCCACATAGCGATATGGGGGAGCATCGCACTCTGGGTGGTG
TTTTTTGGAATCTACTCATCTCTGTGGCCTGCCATTCCGATGGCCCCTGATATGTCAGGA
GAGGCAGCCATGTTGTTCAGTTCTGGAGTCTTTTGGATGGGCTTGTTATTCATCCCTGTG
GCATCTCTGCTCCTTGATGTGGTGTACAAGGTTATCAAGAGGACTGCTTTTAAAACATTG
GTCGATGAAGTTCAGGAGCTGGAGGCAAAATCTCAAGACCCAGGAGCAGTTGTACTTGGA
AAAAGCCTGACCGAGAGGGCGCAACTGCTCAAGAACGTCTTTAAGAAGAACCACGTGAAC
TTGTACCGCTCTGAATCCTTGCAACAAAATCTGCTCCATGGGTATGCGTTCTCTCAAGAT
GAAAATGGAATCGTTTCACAGTCTGAAGTGATAAGAGCATATGATACCACGAAACAGAGG
CCCGACGAATGG
|
| Enzyme 21 GenBank Gene ID |
AF067820  |
| Enzyme 21 GeneCard ID |
ATP8A1  |
| Enzyme 21 GenAtlas ID |
ATP8A1  |
| Enzyme 21 HGNC ID |
HGNC:13531  |
| Enzyme 21 Chromosome Location |
4 |
| Enzyme 21 Locus |
4p13 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 General References |
- Mouro I, Halleck MS, Schlegel RA, Mattei MG, Williamson P, Zachowski A, Devaux P, Cartron JP, Colin Y: Cloning, expression, and chromosomal mapping of a human ATPase II gene, member of the third subfamily of P-type ATPases and orthologous to the presumed bovine and murine aminophospholipid translocase. Biochem Biophys Res Commun. 1999 Apr 13;257(2):333-9. [PubMed
]
- Zahedi RP, Lewandrowski U, Wiesner J, Wortelkamp S, Moebius J, Schutz C, Walter U, Gambaryan S, Sickmann A: Phosphoproteome of resting human platelets. J Proteome Res. 2008 Feb;7(2):526-34. Epub 2007 Dec 19. [PubMed
]
|
| Enzyme 21 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 22
[top]
|
| Enzyme 22 ID |
6759 |
| Enzyme 22 Name |
Probable phospholipid-transporting ATPase IM |
| Enzyme 22 Synonyms |
- ATPase class I type 8B member 4
|
| Enzyme 22 Gene Name |
ATP8B4 |
| Enzyme 22 Protein Sequence |
>Probable phospholipid-transporting ATPase IM
MFCSEKKLREVERIVKANDREYNEKFQYADNRIHTSKYNILTFLPINLFEQFQRVANAYF
LCLLILQLIPEISSLTWFTTIVPLVLVITMTAVKDATDDYFRHKSDNQVNNRQSEVLINS
KLQNEKWMNVKVGDIIKLENNQFVAADLLLLSSSEPHGLCYVETAELDGETNLKVRHALS
VTSELGADISRLAGFDGIVVCEVPNNKLDKFMGILSWKDSKHSLNNEKIILRGCILRNTS
WCFGMVIFAGPDTKLMQNSGKTKFKRTSIDRLMNTLVLWIFGFLICLGIILAIGNSIWES
QTGDQFRTFLFWNEGEKSSVFSGFLTFWSYIIILNTVVPISLYVSVEVIRLGHSYFINWD
RKMYYSRKAIPAVARTTTLNEELGQIEYIFSDKTGTLTQNIMTFKRCSINGRIYGEVHDD
LDQKTEITQEKEPVDFSVKSQADREFQFFDHHLMESIKMGDPKVHEFLRLLALCHTVMSE
ENSAGELIYQVQSPDEGALVTAARNFGFIFKSRTPETITIEELGTLVTYQLLAFLDFNNT
RKRMSVIVRNPEGQIKLYSKGADTILFEKLHPSNEVLLSLTSDHLSEFAGEGLRTLAIAY
RDLDDKYFKEWHKMLEDANAATEERDERIAGLYEEIERDLMLLGATAVEDKLQEGVIETV
TSLSLANIKIWVLTGDKQETAINIGYACNMLTDDMNDVFVIAGNNAVEVREELRKAKQNL
FGQNRNFSNGHVVCEKKQQLELDSIVEETITGDYALIINGHSLAHALESDVKNDLLELAC
MCKTVICCRVTPLQKAQVVELVKKYRNAVTLAIGDGANDVSMIKSAHIGVGISGQEGLQA
VLASDYSFAQFRYLQRLLLVHGRWSYFRMCKFLCYFFYKNFAFTLVHFWFGFFCGFSAQT
VYDQWFITLFNIVYTSLPVLAMGIFDQDVSDQNSVDCPQLYKPGQLNLLFNKRKFFICVL
HGIYTSLVLFFIPYGAFYNVAGEDGQHIADYQSFAVTMATSLVIVVSVQIALDTSYWTFI
NHVFIWGSIAIYFSILFTMHSNGIFGIFPNQFPFVGNARHSLTQKCIWLVILLTTVASVM
PVVAFRFLKVDLYPTLSDQIRRWQKAQKKARPPSSRRPRTRRSSSRRSGYAFAHQEGYGE
LITSGKNMRAKNPPPTSGLEKTHYNSTSWIENLCKKTTDTVSSFSQDKTVKL
|
| Enzyme 22 Number of Residues |
1192 |
| Enzyme 22 Molecular Weight |
135867.0 |
| Enzyme 22 Theoretical pI |
6.99 |
| Enzyme 22 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 22 General Function |
Involved in ATP binding |
| Enzyme 22 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
- 45-66
73-92
277-298
328-349
872-892
905-924
955-976
991-1013
1020-1040
1061-1085
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
50083277  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q8TF62  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
AT8B4_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>3579 bp
ATGTTCTGCAGTGAAAAGAAATTGCGTGAAGTGGAACGGATAGTGAAAGCCAATGACCGT
GAATATAATGAAAAGTTCCAGTATGCGGATAATCGTATCCACACATCGAAATATAATATT
CTCACCTTCTTGCCAATTAATTTATTTGAACAGTTCCAAAGAGTGGCAAATGCCTATTTT
CTTTGCCTTCTGATTTTACAGCTAATTCCAGAAATTTCCTCCTTGACCTGGTTTACCACC
ATTGTGCCTTTGGTCCTGGTGATAACTATGACAGCTGTCAAAGATGCCACAGATGACTAT
TTTCGCCACAAGAGTGATAATCAAGTGAATAATCGGCAGTCTGAAGTGCTCATCAACAGC
AAACTGCAGAATGAAAAATGGATGAATGTCAAAGTGGGAGACATCATTAAATTAGAAAAT
AACCAATTTGTTGCTGCTGATTTACTTCTCCTATCAAGTAGTGAGCCACATGGTCTCTGT
TATGTTGAAACTGCTGAGCTTGATGGGGAAACGAACCTAAAAGTCCGCCATGCACTATCA
GTTACTTCAGAACTTGGAGCAGATATCAGCAGACTTGCAGGGTTTGATGGGATTGTTGTC
TGTGAGGTGCCTAACAACAAGTTAGATAAATTCATGGGAATCCTTTCTTGGAAAGACAGC
AAGCATTCCCTCAACAATGAGAAGATAATCCTGAGAGGCTGCATCCTGAGAAATACCAGC
TGGTGTTTTGGAATGGTTATTTTTGCAGGTCCTGACACTAAACTAATGCAGAATAGTGGT
AAGACAAAGTTTAAAAGGACAAGCATTGATAGATTGATGAATACTCTAGTACTATGGATT
TTTGGGTTTCTGATATGCTTGGGAATTATTCTTGCAATAGGAAATTCAATCTGGGAGAGT
CAAACTGGGGACCAATTCAGAACTTTCCTCTTTTGGAATGAAGGAGAGAAGAGCTCTGTG
TTCTCCGGATTCTTAACATTCTGGTCATATATTATTATTCTCAATACAGTTGTACCCATT
TCCTTATATGTGAGTGTGGAAGTAATTCGTCTAGGACACAGTTATTTTATAAACTGGGAC
CGGAAGATGTATTATTCTCGAAAAGCAATACCTGCAGTGGCTCGAACGACCACGCTCAAT
GAGGAACTGGGGCAGATTGAGTACATTTTCTCCGACAAAACGGGTACCCTCACTCAAAAC
ATCATGACCTTTAAAAGATGTTCCATTAATGGGAGAATCTATGGTGAAGTACATGATGAC
CTGGATCAGAAGACAGAAATAACTCAGGAAAAAGAGCCTGTGGATTTCTCAGTCAAATCT
CAAGCGGATAGAGAATTTCAGTTCTTTGACCACCATCTGATGGAATCCATTAAAATGGGT
GATCCCAAAGTTCATGAATTCCTTAGGTTACTTGCTCTCTGCCACACTGTAATGTCAGAA
GAGAATAGCGCAGGAGAGCTGATTTACCAAGTTCAGTCACCTGATGAAGGGGCTCTAGTG
ACTGCCGCTAGAAATTTTGGGTTCATTTTTAAATCCCGGACCCCAGAGACCATAACAATA
GAAGAATTGGGAACACTAGTTACTTATCAATTACTTGCCTTTTTGGATTTCAACAACACC
AGAAAAAGGATGTCTGTCATAGTTCGAAACCCAGAAGGACAGATAAAGCTTTATTCCAAA
GGAGCAGATACTATTCTGTTTGAAAAACTTCATCCTTCCAATGAAGTCCTTTTGTCTTTG
ACGTCAGACCACCTCAGTGAATTTGCAGGGGAAGGCCTTCGGACCTTGGCCATCGCATAC
AGAGACCTGGATGACAAGTACTTTAAAGAGTGGCATAAGATGCTTGAAGATGCGAATGCT
GCCACAGAAGAGAGGGATGAACGAATAGCTGGGCTATATGAAGAAATTGAAAGAGATTTG
ATGCTACTAGGTGCCACTGCTGTAGAAGATAAGTTACAGGAGGGTGTTATTGAAACAGTT
ACAAGTTTATCACTAGCCAATATTAAGATCTGGGTCCTAACAGGAGACAAACAAGAAACT
GCCATCAACATCGGTTATGCCTGCAACATGCTGACTGACGACATGAATGATGTGTTTGTG
ATAGCAGGGAATAATGCTGTGGAAGTGAGAGAAGAACTCAGGAAAGCAAAACAAAATTTG
TTTGGACAAAACAGAAATTTTTCCAATGGCCATGTAGTTTGTGAAAAAAAGCAGCAGCTG
GAGTTGGATTCTATTGTAGAAGAAACCATAACAGGAGATTATGCCTTAATCATAAATGGC
CACAGTTTGGCTCATGCCCTAGAAAGTGATGTCAAGAATGATCTCCTAGAACTTGCTTGC
ATGTGTAAGACTGTAATTTGCTGCAGGGTCACTCCACTCCAGAAAGCCCAAGTGGTAGAG
CTGGTGAAGAAGTACAGAAATGCTGTTACTTTGGCCATTGGTGATGGAGCCAATGATGTC
AGCATGATTAAAAGTGCTCACATTGGTGTTGGCATCAGCGGCCAGGAAGGATTGCAAGCA
GTCTTAGCCAGCGACTATTCATTTGCACAGTTTAGATATCTCCAAAGGCTTCTCCTTGTT
CATGGAAGGTGGTCTTATTTCCGAATGTGCAAATTCTTATGCTATTTCTTCTATAAGAAT
TTTGCATTTACACTTGTGCATTTCTGGTTTGGTTTCTTCTGTGGTTTCTCAGCCCAGACT
GTTTATGACCAGTGGTTCATCACCCTTTTTAACATTGTTTACACATCACTGCCTGTTTTA
GCCATGGGGATTTTTGACCAGGATGTGAGTGACCAGAACAGCGTGGACTGTCCCCAGCTC
TACAAACCAGGACAGCTGAATCTGCTTTTTAACAAGCGTAAATTTTTCATTTGCGTGTTG
CATGGAATCTACACCTCATTAGTCCTTTTCTTCATCCCCTATGGGGCCTTTTACAACGTG
GCTGGAGAAGATGGGCAACATATTGCTGACTACCAGTCCTTTGCAGTTACCATGGCCACA
TCTTTGGTCATTGTGGTCAGTGTGCAGATAGCCTTGGATACCAGTTACTGGACTTTCATT
AATCACGTCTTCATCTGGGGGAGCATTGCCATTTATTTCTCCATTTTATTTACAATGCAC
AGTAATGGCATCTTTGGCATCTTCCCAAACCAGTTTCCATTTGTTGGTAATGCACGACAT
TCCCTGACCCAGAAGTGCATCTGGCTTGTAATTCTCTTAACAACAGTGGCTTCAGTTATG
CCAGTGGTGGCATTCAGATTTTTGAAGGTGGATTTATACCCAACCCTGAGTGATCAGATC
CGCCGGTGGCAGAAGGCTCAAAAGAAGGCAAGGCCTCCAAGTAGCCGAAGGCCTCGGACC
CGCAGGTCAAGCTCAAGAAGGTCTGGATATGCTTTTGCTCACCAAGAAGGCTATGGAGAG
CTTATCACATCTGGAAAAAATATGCGAGCTAAAAATCCACCCCCAACATCAGGGCTGGAA
AAGACACATTATAATAGCACTAGCTGGATTGAAAATTTATGTAAGAAAACCACAGACACC
GTGAGCAGCTTTAGCCAGGATAAAACAGTGAAACTGTGA
|
| Enzyme 22 GenBank Gene ID |
NM_024837.2  |
| Enzyme 22 GeneCard ID |
ATP8B4  |
| Enzyme 22 GenAtlas ID |
ATP8B4  |
| Enzyme 22 HGNC ID |
HGNC:13536  |
| Enzyme 22 Chromosome Location |
1 |
| Enzyme 22 Locus |
15q21.2 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 General References |
- Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 22 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 23
[top]
|
| Enzyme 23 ID |
6781 |
| Enzyme 23 Name |
Probable phospholipid-transporting ATPase IF |
| Enzyme 23 Synonyms |
- ATPase IR
- ATPase class VI type 11B
|
| Enzyme 23 Gene Name |
ATP11B |
| Enzyme 23 Protein Sequence |
>Probable phospholipid-transporting ATPase IF
MWRWIRQQLGFDPPHQSDTRTIYVANRFPQNGLYTPQKFIDNRIISSKYTVWNFVPKNLF
EQFRRVANFYFLIIFLVQLMIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHNSDNEVN
GAPVYVVRSGGLVKTRSKNIRVGDIVRIAKDEIFPADLVLLSSDRLDGSCHVTTASLDGE
TNLKTHVAVPETALLQTVANLDTLVAVIECQQPEADLYRFMGRMIITQQMEEIVRPLGPE
SLLLRGARLKNTKEIFGVAVYTGMETKMALNYKSKSQKRSAVEKSMNTFLIIYLVILISE
AVISTILKYTWQAEEKWDEPWYNQKTEHQRNSSKILRFISDFLAFLVLYNFIIPISLYVT
VEMQKFLGSFFIGWDLDLYHEESDQKAQVNTSDLNEELGQVEYVFTDKTGTLTENEMQFR
ECSINGMKYQEINGRLVPEGPTPDSSEGNLSYLSSLSHLNNLSHLTTSSSFRTSPENETE
LIKEHDLFFKAVSLCHTVQISNVQTDCTGDGPWQSNLAPSQLEYYASSPDEKALVEAAAR
IGIVFIGNSEETMEVKTLGKLERYKLLHILEFDSDRRRMSVIVQAPSGEKLLFAKGAESS
ILPKCIGGEIEKTRIHVDEFALKGLRTLCIAYRKFTSKEYEEIDKRIFEARTALQQREEK
LAAVFQFIEKDLILLGATAVEDRLQDKVRETIEALRMAGIKVWVLTGDKHETAVSVSLSC
GHFHRTMNILELINQKSDSECAEQLRQLARRITEDHVIQHGLVVDGTSLSLALREHEKLF
MEVCRNCSAVLCCRMAPLQKAKVIRLIKISPEKPITLAVGDGANDVSMIQEAHVGIGIMG
KEGRQAARNSDYAIARFKFLSKLLFVHGHFYYIRIATLVQYFFYKNVCFITPQFLYQFYC
LFSQQTLYDSVYLTLYNICFTSLPILIYSLLEQHVDPHVLQNKPTLYRDISKNRLLSIKT
FLYWTILGFSHAFIFFFGSYLLIGKDTSLLGNGQMFGNWTFGTLVFTVMVITVTVKMALE
THFWTWINHLVTWGSIIFYFVFSLFYGGILWPFLGSQNMYFVFIQLLSSGSAWFAIILMV
VTCLFLDIIKKVFDRHLHPTSTEKAQLTETNAGIKCLDSMCCFPEGEAACASVGRMLERV
IGRCSPTHISRSWSASDPFYTNDRSILTLSTMDSSTC
|
| Enzyme 23 Number of Residues |
1177 |
| Enzyme 23 Molecular Weight |
134188.6 |
| Enzyme 23 Theoretical pI |
6.95 |
| Enzyme 23 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 23 General Function |
Involved in ATP binding |
| Enzyme 23 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
- 56-77
83-104
290-311
342-359
877-898
911-930
961-982
998-1020
1026-1047
1066-1090
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
62632750  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
Q9Y2G3  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
AT11B_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>3534 bp
ATGTGGCGCTGGATCCGGCAGCAGCTGGGTTTTGACCCACCACATCAGAGTGACACAAGA
ACCATCTACGTAGCCAACAGGTTTCCTCAGAATGGCCTTTACACACCTCAGAAATTTATA
GATAACAGGATCATTTCATCTAAGTACACTGTGTGGAATTTTGTTCCAAAAAATTTATTT
GAACAGTTCAGAAGAGTGGCAAACTTTTATTTTCTTATTATATTTTTGGTTCAGCTTATG
ATTGATACACCTACCAGTCCAGTTACCAGTGGACTTCCATTATTCTTTGTGATAACAGTA
ACTGCCATAAAGCAGGGATATGAAGATTGGTTACGGCATAACTCAGATAATGAAGTAAAT
GGAGCTCCTGTTTATGTTGTTCGAAGTGGTGGCCTTGTAAAAACTAGATCAAAAAACATT
CGGGTGGGTGATATTGTTCGAATAGCCAAAGATGAAATTTTTCCTGCAGACTTGGTGCTT
CTGTCCTCAGATCGACTGGATGGTTCCTGTCACGTTACAACTGCTAGTTTGGACGGAGAA
ACTAACCTGAAGACACATGTGGCAGTTCCAGAAACAGCATTATTACAAACAGTTGCCAAT
TTGGACACTCTAGTAGCTGTAATAGAATGCCAGCAACCAGAAGCAGACTTATACAGATTC
ATGGGACGAATGATCATAACCCAACAAATGGAAGAAATTGTAAGACCTCTGGGGCCGGAG
AGTCTCCTGCTTCGTGGAGCCAGATTAAAAAACACAAAAGAAATTTTTGGTGTTGCGGTA
TACACTGGAATGGAAACTAAGATGGCATTAAATTACAAGAGCAAATCACAGAAACGATCT
GCAGTAGAAAAGTCAATGAATACATTTTTGATAATTTATCTAGTAATTCTTATATCTGAA
GCTGTCATCAGCACTATCTTGAAGTATACATGGCAAGCTGAAGAAAAATGGGATGAACCT
TGGTATAACCAAAAAACAGAACATCAAAGAAATAGCAGTAAGATTCTGAGATTTATTTCA
GACTTCCTTGCTTTTTTGGTTCTCTACAATTTCATCATTCCAATTTCATTATATGTGACA
GTCGAAATGCAGAAATTTCTTGGATCATTTTTTATTGGCTGGGATCTTGATCTGTATCAT
GAAGAATCAGATCAGAAAGCTCAAGTCAATACTTCCGATCTGAATGAAGAGCTTGGACAG
GTAGAGTACGTGTTTACAGATAAAACTGGTACACTGACAGAAAATGAGATGCAGTTTCGG
GAATGTTCAATTAATGGCATGAAATACCAAGAAATTAATGGTAGACTTGTACCCGAAGGA
CCAACACCAGACTCTTCAGAAGGAAACTTATCTTATCTTAGTAGTTTATCCCATCTTAAC
AACTTATCCCATCTTACAACCAGTTCCTCTTTCAGAACCAGTCCTGAAAATGAAACTGAA
CTAATTAAAGAACATGATCTCTTCTTTAAAGCAGTCAGTCTCTGTCACACTGTACAGATT
AGCAATGTTCAAACTGACTGCACTGGTGATGGTCCCTGGCAATCCAACCTGGCACCATCG
CAGTTGGAGTACTATGCATCTTCACCAGATGAAAAGGCTCTAGTAGAAGCTGCTGCAAGG
ATTGGTATTGTGTTTATTGGCAATTCTGAAGAAACTATGGAGGTTAAAACTCTTGGAAAA
CTGGAACGGTACAAACTGCTTCATATTCTGGAATTTGATTCAGATCGTAGGAGAATGAGT
GTAATTGTTCAGGCACCTTCAGGTGAGAAGTTATTATTTGCTAAAGGAGCTGAGTCATCA
ATTCTCCCTAAATGTATAGGTGGAGAAATAGAAAAAACCAGAATTCATGTAGATGAATTT
GCTTTGAAAGGGCTAAGAACTCTGTGTATAGCATATAGAAAATTTACATCAAAAGAGTAT
GAGGAAATAGATAAACGCATATTTGAAGCCAGGACTGCCTTGCAGCAGCGGGAAGAGAAA
TTGGCAGCTGTTTTCCAGTTCATAGAGAAAGACCTGATATTACTTGGAGCCACAGCAGTA
GAAGACAGACTACAAGATAAAGTTCGAGAAACTATTGAAGCATTGAGAATGGCTGGTATC
AAAGTATGGGTACTTACTGGGGATAAACATGAAACAGCTGTTAGTGTGAGTTTATCATGT
GGCCATTTTCATAGAACCATGAACATCCTTGAACTTATAAACCAGAAATCAGACAGCGAG
TGTGCTGAACAATTGAGGCAGCTTGCCAGAAGAATTACAGAGGATCATGTGATTCAGCAT
GGGCTGGTAGTGGATGGGACCAGCCTATCTCTTGCACTCAGGGAGCATGAAAAACTATTT
ATGGAAGTTTGCAGAAATTGTTCAGCTGTATTATGCTGTCGTATGGCTCCACTGCAGAAA
GCAAAAGTAATAAGACTAATAAAAATATCACCTGAGAAACCTATAACATTGGCTGTTGGT
GATGGTGCTAATGACGTAAGCATGATACAAGAAGCCCATGTTGGCATAGGAATCATGGGT
AAAGAAGGAAGACAGGCTGCAAGAAACAGTGACTATGCAATAGCCAGATTTAAGTTCCTC
TCCAAATTGCTTTTTGTTCATGGTCATTTTTATTATATTAGAATAGCTACCCTTGTACAG
TATTTTTTTTATAAGAATGTGTGCTTTATCACACCCCAGTTTTTATATCAGTTCTACTGT
TTGTTTTCTCAGCAAACATTGTATGACAGCGTGTACCTGACTTTATACAATATTTGTTTT
ACTTCCCTACCTATTCTGATATATAGTCTTTTGGAACAGCATGTAGACCCTCATGTGTTA
CAAAATAAGCCCACCCTTTATCGAGACATTAGTAAAAACCGCCTCTTAAGTATTAAAACA
TTTCTTTATTGGACCATCCTGGGCTTCAGTCATGCCTTTATTTTCTTTTTTGGATCCTAT
TTACTAATAGGGAAAGATACATCTCTGCTTGGAAATGGCCAGATGTTTGGAAACTGGACA
TTTGGCACTTTGGTCTTCACAGTCATGGTTATTACAGTCACAGTAAAGATGGCTCTGGAA
ACTCATTTTTGGACTTGGATCAACCATCTCGTTACCTGGGGATCTATTATATTTTATTTT
GTATTTTCCTTGTTTTATGGAGGGATTCTCTGGCCATTTTTGGGCTCCCAGAATATGTAT
TTTGTGTTTATTCAGCTCCTGTCAAGTGGTTCTGCTTGGTTTGCCATAATCCTCATGGTT
GTTACATGTCTATTTCTTGATATCATAAAGAAGGTCTTTGACCGACACCTCCACCCTACA
AGTACTGAAAAGGCACAGCTTACTGAAACAAATGCAGGTATCAAGTGCTTGGACTCCATG
TGCTGTTTCCCGGAAGGAGAAGCAGCGTGTGCATCTGTTGGAAGAATGCTGGAACGAGTT
ATAGGAAGATGTAGTCCAACCCACATCAGCAGATCATGGAGTGCATCGGATCCTTTCTAT
ACCAACGACAGGAGCATCTTGACTCTCTCCACAATGGACTCATCTACTTGTTAA
|
| Enzyme 23 GenBank Gene ID |
NM_014616.1  |
| Enzyme 23 GeneCard ID |
ATP11B  |
| Enzyme 23 GenAtlas ID |
ATP11B  |
| Enzyme 23 HGNC ID |
HGNC:13553  |
| Enzyme 23 Chromosome Location |
3 |
| Enzyme 23 Locus |
3q27 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 General References |
- Halleck MS, Lawler JF JR, Blackshaw S, Gao L, Nagarajan P, Hacker C, Pyle S, Newman JT, Nakanishi Y, Ando H, Weinstock D, Williamson P, Schlegel RA: Differential expression of putative transbilayer amphipath transporters. Physiol Genomics. 1999 Nov 11;1(3):139-50. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Halleck MS, Schlegel RA, Williamson PL: Reanalysis of ATP11B, a type IV P-type ATPase. J Biol Chem. 2002 Mar 22;277(12):9736-40. Epub 2002 Jan 14. [PubMed
]
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Hirosawa M, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XIII. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Feb 26;6(1):63-70. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
|
| Enzyme 23 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 24
[top]
|
| Enzyme 24 ID |
6785 |
| Enzyme 24 Name |
Probable phospholipid-transporting ATPase IK |
| Enzyme 24 Synonyms |
- ATPase class I type 8B member 3
|
| Enzyme 24 Gene Name |
ATP8B3 |
| Enzyme 24 Protein Sequence |
>Probable phospholipid-transporting ATPase IK
MGTGPAQTPRSTRAGPEPSPAPPGPGDTGDSDVTQEGSGPAGIRGGETVIRAGMGDSPGR
GAPERRHKAQPGRARKYEWRPEGPTSMGSLGQREDLQDEDRNSAFTWKVQANNRAYNGQF
KEKVILCWQRKKYKTNVIRTAKYNFYSFLPLNLYEQFHRVSNLFFLIIIILQSIPDISTL
PWFSLSTPMVCLLFIRATRDLVDDMGRHKSDRAINNRPCQILMGKSFKQKKWQDLCVGDV
VCLRKDNIVPADMLLLASTEPSSLCYVETVDIDGETNLKFRQALMVTHKELATIKKMASF
QGTVTCEAPNSRMHHFVGCLEWNDKKYSLDIGNLLLRGCRIRNTDTCYGLVIYAGFDTKI
MKNCGKIHLKRTKLDLLMNKLVVVIFISVVLVCLVLAFGFGFSVKEFKDHHYYLSGVHGS
SVAAESFFVFWSFLILLSVTIPMSMFILSEFIYLGNSVFIDWDVQMYYKPQDVPAKARST
SLNDHLGQVEYIFSDKTGTLTQNILTFNKCCISGRVYGPDSEATTRPKENPYLWNKFADG
KLLFHNAALLHLVRTNGDEAVREFWRLLAICHTVMVRESPRERPDQLLYQAASPDEGALV
TAARNFGYVFLSRTQDTVTIMELGEERVYQVLAIMDFNSTRKRMSVLVRKPEGAICLYTK
GADTVIFERLHRRGAMEFATEEALAAFAQETLRTLCLAYREVAEDIYEDWQQRHQEASLL
LQNRAQALQQLLGATAIEDRLQDGVPETIKCLKKSNIKIWVLTGDKQETAVNIGFACELL
SENMLILEEKEISRILETYWENSNNLLTRESLSQVKLALVINGDFLDKLLVSLRKEPRAL
AQNVNMDEAWQELGQSRRDFLYARRLSLLCRRFGLPLAAPPAQDSRARRSSEVLQERAFV
DLASKCQAVICCRVTPKQKALIVALVKKYHQVVTLAIGDGANDINMIKTADVGVGLAGQE
GMQAVQNSDFVLGQFCFLQRLLLVHGRWSYVRICKFLRYFFYKSMASMMVQVWFACYNGF
TGQPLYEGWFLALFNLLYSTLPVLYIGLFEQDVSAEQSLEKPELYVVGQKDELFNYWVFV
QAIAHGVTTSLVNFFMTLWISRDTAGPASFSDHQSFAVVVALSCLLSITMEVILIIKYWT
ALCVATILLSLGFYAIMTTTTQSFWLFRVSPTTFPFLYADLSVMSSPSILLVVLLSVSIN
TFPVLALRVIFPALKELRAKEEKVEEGPSEEIFTMEPLPHVHRESRARRSSYAFSHREGY
ANLITQGTILRRGPGVSSDIASESLDPSDEEAASSPKESQ
|
| Enzyme 24 Number of Residues |
1300 |
| Enzyme 24 Molecular Weight |
146750.9 |
| Enzyme 24 Theoretical pI |
7.96 |
| Enzyme 24 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 24 General Function |
Involved in ATP binding |
| Enzyme 24 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
- 150-171
178-197
382-403
431-452
996-1016
1029-1048
1079-1100
1113-1135
1142-1162
1183-1207
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
44888835  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
O60423  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
AT8B3_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>3903 bp
ATGGGCACTGGCCCCGCTCAGACTCCCAGGAGCACCAGAGCTGGCCCTGAGCCAAGCCCT
GCCCCACCAGGACCTGGGGACACGGGTGACTCAGACGTGACTCAGGAAGGCTCAGGTCCT
GCTGGCATCCGCGGAGGTGAGACGGTGATCAGAGCTGGGATGGGAGACTCCCCAGGCAGA
GGGGCACCTGAGAGGAGGCACAAGGCCCAGCCTGGCCGGGCTAGGAAGTATGAATGGAGA
CCAGAAGGCCCCACCAGCATGGGCAGCCTCGGCCAGAGAGAAGATCTCCAAGATGAGGAC
AGGAACTCAGCATTCACCTGGAAGGTCCAGGCCAACAACCGTGCCTACAACGGGCAGTTC
AAGGAGAAGGTGATCCTGTGCTGGCAAAGGAAGAAATACAAGACCAATGTCATCCGCACG
GCCAAGTACAACTTCTACTCGTTCCTGCCGCTGAACCTGTACGAGCAGTTCCACCGCGTG
TCCAACCTGTTCTTCCTCATCATCATCATCCTGCAGAGCATTCCCGACATCTCCACGCTG
CCCTGGTTCTCGCTCAGTACCCCTATGGTCTGCCTCCTCTTCATCCGTGCCACCCGGGAC
CTGGTGGACGACATGGGGAGACACAAGAGTGACAGAGCCATCAACAACAGACCCTGCCAG
ATTCTGATGGGGAAGAGCTTCAAGCAGAAGAAATGGCAGGATCTGTGCGTGGGGGATGTG
GTCTGTCTCCGCAAGGACAACATCGTCCCAGCCGACATGCTCTTGCTGGCCAGCACGGAG
CCCAGCAGCCTGTGCTATGTGGAGACGGTGGACATTGACGGGGAGACCAACTTGAAGTTC
AGACAGGCCCTGATGGTCACCCACAAAGAACTGGCCACTATAAAGAAGATGGCGTCCTTT
CAAGGCACAGTGACGTGTGAGGCGCCTAACAGTCGGATGCACCACTTCGTGGGGTGCCTG
GAATGGAATGACAAGAAATACTCCCTGGACATTGGCAACCTCCTCCTCCGAGGCTGCAGG
ATTCGCAACACAGACACCTGCTATGGACTGGTCATTTATGCTGGTTTTGACACAAAAATT
ATGAAGAACTGTGGCAAGATCCATTTGAAGAGAACCAAGCTGGACCTCCTGATGAACAAG
CTGGTGGTTGTGATCTTCATCTCCGTGGTGCTTGTCTGCCTGGTGTTGGCCTTCGGCTTC
GGTTTCTCAGTCAAAGAATTCAAAGACCACCACTACTACCTCTCGGGGGTGCATGGGAGC
AGCGTGGCCGCAGAGTCCTTCTTCGTCTTCTGGAGCTTCCTCATCCTGCTCAGCGTCACC
ATCCCGATGTCCATGTTCATCCTGTCCGAGTTCATCTACCTGGGGAACAGCGTCTTCATC
GACTGGGACGTGCAGATGTACTACAAGCCGCAGGACGTGCCTGCCAAGGCCCGCAGCACC
AGCCTCAACGACCACCTGGGCCAGGTGGAATACATCTTCTCGGACAAGACGGGCACGCTC
ACGCAGAACATCTTGACCTTCAACAAGTGCTGCATCAGCGGCCGCGTCTATGGGCCGGAT
TCAGAGGCCACGACCCGACCTAAGGAGAACCCCTACCTCTGGAACAAGTTCGCCGACGGG
AAGCTGCTCTTCCACAATGCGGCCCTGCTGCACCTCGTGCGGACCAACGGGGACGAGGCC
GTGCGGGAGTTCTGGCGCCTGCTGGCCATCTGCCACACGGTGATGGTGCGGGAGAGCCCC
CGTGAGCGCCCAGACCAGCTGTTGTACCAGGCGGCCTCCCCCGACGAGGGGGCGCTGGTC
ACCGCAGCCCGGAACTTCGGCTACGTGTTCCTGTCCCGCACCCAGGACACCGTCACGATC
ATGGAGCTGGGGGAGGAACGGGTCTACCAGGTCCTGGCCATAATGGACTTCAACAGCACG
CGCAAACGGATGTCGGTGCTGGTTCGAAAGCCAGAGGGCGCCATCTGCCTGTACACCAAG
GGCGCCGACACGGTCATCTTCGAACGCTTGCACAGGAGGGGGGCAATGGAATTTGCCACA
GAGGAGGCCTTGGCTGCCTTTGCCCAGGAGACCCTGCGGACACTGTGCCTGGCCTACAGG
GAGGTGGCTGAGGACATTTACGAGGACTGGCAGCAGCGCCACCAGGAGGCCAGCCTCCTG
CTGCAGAACCGGGCACAGGCCCTGCAACAGCTGCTGGGAGCCACAGCCATCGAGGACAGA
CTCCAGGACGGTGTCCCTGAAACCATCAAATGTCTCAAGAAGAGCAACATCAAAATATGG
GTGCTCACCGGGGACAAGCAGGAAACGGCTGTGAACATCGGCTTCGCCTGCGAGCTGCTG
TCAGAGAATATGCTCATTCTGGAGGAGAAGGAGATTAGCCGCATCCTGGAGACCTACTGG
GAAAACAGTAACAACCTTCTAACCAGGGAGTCCCTGTCGCAGGTCAAGCTGGCCTTGGTC
ATTAACGGAGACTTCCTGGACAAACTGCTGGTGTCCCTGCGGAAGGAGCCGCGCGCCCTG
GCGCAGAACGTGAACATGGACGAGGCGTGGCAGGAGCTCGGCCAGTCCAGGAGGGATTTC
CTCTACGCCAGGCGCCTGTCCCTGCTGTGCCGGAGGTTCGGGCTCCCGCTGGCTGCACCG
CCAGCCCAGGACTCCAGAGCCCGCCGTAGCTCCGAGGTGCTGCAGGAGCGCGCCTTCGTG
GACCTGGCGTCCAAGTGCCAGGCGGTCATCTGCTGCCGCGTGACGCCCAAGCAGAAGGCC
CTGATCGTGGCCCTGGTCAAGAAGTACCACCAGGTGGTGACCCTGGCCATCGGGGACGGT
GCCAACGACATCAACATGATCAAGACCGCGGACGTGGGCGTGGGGCTGGCGGGCCAGGAG
GGCATGCAGGCAGTTCAGAACAGCGACTTCGTGCTCGGCCAGTTCTGCTTCCTGCAGCGC
CTCCTGCTGGTGCACGGCCGCTGGTCCTACGTGCGGATCTGCAAGTTCCTGCGCTACTTC
TTCTACAAGAGCATGGCCAGCATGATGGTGCAGGTCTGGTTTGCCTGCTACAACGGCTTC
ACCGGCCAGCCCCTGTATGAAGGATGGTTCCTGGCTCTTTTCAACCTCCTGTACAGCACC
CTGCCAGTTCTCTACATTGGGCTCTTTGAGCAGGACGTGAGCGCAGAGCAGAGCCTGGAG
AAGCCGGAGCTGTACGTGGTGGGGCAGAAGGACGAGCTCTTCAACTACTGGGTCTTCGTC
CAAGCCATCGCCCATGGTGTGACCACCTCTCTGGTCAACTTCTTCATGACACTGTGGATC
AGCCGCGACACGGCGGGACCCGCCAGCTTCAGCGACCACCAGTCCTTTGCGGTCGTGGTG
GCCCTGTCTTGCCTGCTGTCCATCACCATGGAGGTCATTCTTATCATCAAGTACTGGACC
GCCCTGTGCGTGGCGACCATCCTCCTCAGCCTTGGTTTCTACGCCATCATGACTACCACC
ACCCAGAGCTTCTGGCTCTTCAGAGTATCCCCCACGACCTTCCCGTTTCTGTATGCCGAC
CTCAGCGTGATGTCCTCTCCCTCCATCCTGCTGGTGGTCCTGCTGAGTGTGTCCATAAAC
ACCTTCCCTGTCCTGGCCCTCCGAGTCATCTTCCCAGCCCTCAAGGAGCTACGTGCCAAG
GAGGAGAAGGTGGAGGAGGGCCCCAGCGAGGAGATTTTCACCATGGAGCCCTTGCCTCAT
GTACACCGGGAGTCTCGTGCCCGCCGTTCCAGCTATGCTTTCTCCCACCGTGAGGGATAT
GCAAACCTCATCACTCAGGGCACAATTCTGCGGAGGGGACCAGGGGTCAGCAGTGACATA
GCATCTGAATCCCTAGACCCATCTGATGAAGAGGCAGCTTCGAGCCCAAAAGAGTCACAG
TGA
|
| Enzyme 24 GenBank Gene ID |
NM_138813.2  |
| Enzyme 24 GeneCard ID |
ATP8B3  |
| Enzyme 24 GenAtlas ID |
ATP8B3  |
| Enzyme 24 HGNC ID |
HGNC:13535  |
| Enzyme 24 Chromosome Location |
1 |
| Enzyme 24 Locus |
19p13.3 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- Grimwood J, Gordon LA, Olsen A, Terry A, Schmutz J, Lamerdin J, Hellsten U, Goodstein D, Couronne O, Tran-Gyamfi M, Aerts A, Altherr M, Ashworth L, Bajorek E, Black S, Branscomb E, Caenepeel S, Carrano A, Caoile C, Chan YM, Christensen M, Cleland CA, Copeland A, Dalin E, Dehal P, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Garcia C, Georgescu AM, Glavina T, Gomez M, Gonzales E, Groza M, Hammon N, Hawkins T, Haydu L, Ho I, Huang W, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Larionov V, Leem SH, Lopez F, Lou Y, Lowry S, Malfatti S, Martinez D, McCready P, Medina C, Morgan J, Nelson K, Nolan M, Ovcharenko I, Pitluck S, Pollard M, Popkie AP, Predki P, Quan G, Ramirez L, Rash S, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, She X, Smith D, Slezak T, Solovyev V, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wagner M, Wheeler J, Wu K, Xie G, Yang J, Dubchak I, Furey TS, DeJong P, Dickson M, Gordon D, Eichler EE, Pennacchio LA, Richardson P, Stubbs L, Rokhsar DS, Myers RM, Rubin EM, Lucas SM: The DNA sequence and biology of human chromosome 19. Nature. 2004 Apr 1;428(6982):529-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 24 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 25
[top]
|
| Enzyme 25 ID |
7395 |
| Enzyme 25 Name |
Phospholipid scramblase 1 |
| Enzyme 25 Synonyms |
- PL scramblase 1
- Ca(2+)-dependent phospholipid scramblase 1
- Erythrocyte phospholipid scramblase
- MmTRA1b
|
| Enzyme 25 Gene Name |
PLSCR1 |
| Enzyme 25 Protein Sequence |
>Phospholipid scramblase 1
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAG
FPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVL
TGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLR
CSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLI
DFMFFESTGSQEQKSGVW
|
| Enzyme 25 Number of Residues |
318 |
| Enzyme 25 Molecular Weight |
35048.8 |
| Enzyme 25 Theoretical pI |
4.57 |
| Enzyme 25 GO Classification |
Not Available |
| Enzyme 25 General Function |
Involved in calcium ion binding |
| Enzyme 25 Specific Function |
May play a role in the antiviral response of interferon (IFN) by amplifying and enhancing the IFN response through increased expression of select subset of potent antiviral genes. May contribute to cytokine-regulated cell proliferation and differentiation |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
|
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
3510297  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
O15162  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
PLS1_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>957 bp
ATGGACAAACAAAACTCACAGATGAATGCTTCTCACCCGGAAACAAACTTGCCAGTTGGG
TATCCTCCTCAGTATCCACCGACAGCATTCCAAGGACCTCCAGGATATAGTGGCTACCCT
GGGCCCCAGGTCAGCTACCCACCCCCACCAGCCGGCCATTCAGGTCCTGGCCCAGCTGGC
TTTCCTGTCCCAAATCAGCCAGTGTATAATCAGCCAGTATATAATCAGCCAGTTGGAGCT
GCAGGGGTACCATGGATGCCAGCGCCACAGCCTCCATTAAACTGTCCACCTGGATTAGAA
TATTTAAGTCAGATAGATCAGATACTGATTCATCAGCAAATTGAACTTCTGGAAGTTTTA
ACAGGTTTTGAAACTAATAACAAATATGAAATTAAGAACAGCTTTGGACAGAGGGTTTAC
TTTGCAGCGGAAGATACTGATTGCTGTACCCGAAATTGCTGTGGGCCATCTAGACCTTTT
ACCTTGAGGATTATTGATAATATGGGTCAAGAAGTCATAACTCTGGAGAGACCACTAAGA
TGTAGCAGCTGTTGTTGTCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGT
GTACCAATAGGTTATGTTATTCAGACTTGGCACCCATGTCTACCAAAGTTTACAATTCAA
AATGAGAAAAGAGAGGATGTACTAAAAATAAGTGGTCCATGTGTTGTGTGCAGCTGTTGT
GGAGATGTTGATTTTGAGATTAAATCTCTTGATGAACAGTGTGTGGTTGGCAAAATTTCC
AAGCACTGGACTGGAATTTTGAGAGAGGCATTTACAGACGCTGATAACTTTGGAATCCAG
TTCCCTTTAGACCTTGATGTTAAAATGAAAGCTGTAATGATTGGTGCCTGTTTCCTCATT
GACTTCATGTTTTTTGAAAGCACTGGCAGCCAGGAACAAAAATCAGGAGTGTGGTAG
|
| Enzyme 25 GenBank Gene ID |
AB006746  |
| Enzyme 25 GeneCard ID |
PLSCR1  |
| Enzyme 25 GenAtlas ID |
PLSCR1  |
| Enzyme 25 HGNC ID |
HGNC:9092  |
| Enzyme 25 Chromosome Location |
3 |
| Enzyme 25 Locus |
3q23 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Zhou Q, Zhao J, Stout JG, Luhm RA, Wiedmer T, Sims PJ: Molecular cloning of human plasma membrane phospholipid scramblase. A protein mediating transbilayer movement of plasma membrane phospholipids. J Biol Chem. 1997 Jul 18;272(29):18240-4. [PubMed
]
- Kasukabe T, Kobayashi H, Kaneko Y, Okabe-Kado J, Honma Y: Identity of human normal counterpart (MmTRA1b) of mouse leukemogenesis-associated gene (MmTRA1a) product as plasma membrane phospholipid scramblase and chromosome mapping of the human MmTRA1b/phospholipid scramblase gene. Biochem Biophys Res Commun. 1998 Aug 19;249(2):449-55. [PubMed
]
- Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Basse F, Stout JG, Sims PJ, Wiedmer T: Isolation of an erythrocyte membrane protein that mediates Ca2+-dependent transbilayer movement of phospholipid. J Biol Chem. 1996 Jul 19;271(29):17205-10. [PubMed
]
- Frasch SC, Henson PM, Kailey JM, Richter DA, Janes MS, Fadok VA, Bratton DL: Regulation of phospholipid scramblase activity during apoptosis and cell activation by protein kinase Cdelta. J Biol Chem. 2000 Jul 28;275(30):23065-73. [PubMed
]
- Sun J, Zhao J, Schwartz MA, Wang JY, Wiedmer T, Sims PJ: c-Abl tyrosine kinase binds and phosphorylates phospholipid scramblase 1. J Biol Chem. 2001 Aug 3;276(31):28984-90. Epub 2001 Jun 4. [PubMed
]
- Zhao J, Zhou Q, Wiedmer T, Sims PJ: Palmitoylation of phospholipid scramblase is required for normal function in promoting Ca2+-activated transbilayer movement of membrane phospholipids. Biochemistry. 1998 May 5;37(18):6361-6. [PubMed
]
- Zhou Q, Sims PJ, Wiedmer T: Identity of a conserved motif in phospholipid scramblase that is required for Ca2+-accelerated transbilayer movement of membrane phospholipids. Biochemistry. 1998 Feb 24;37(8):2356-60. [PubMed
]
- Dong B, Zhou Q, Zhao J, Zhou A, Harty RN, Bose S, Banerjee A, Slee R, Guenther J, Williams BR, Wiedmer T, Sims PJ, Silverman RH: Phospholipid scramblase 1 potentiates the antiviral activity of interferon. J Virol. 2004 Sep;78(17):8983-93. [PubMed
]
|
| Enzyme 25 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 26
[top]
|
| Enzyme 26 ID |
7740 |
| Enzyme 26 Name |
Phosphatidylserine decarboxylase proenzyme |
| Enzyme 26 Synonyms |
- Phosphatidylserine decarboxylase alpha chain
- Phosphatidylserine decarboxylase beta chain
|
| Enzyme 26 Gene Name |
PISD |
| Enzyme 26 Protein Sequence |
>Phosphatidylserine decarboxylase proenzyme
MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPART
MFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLS
RAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPV
CGLHSISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKN
QLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCH
NERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNRE
GVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
|
| Enzyme 26 Number of Residues |
408 |
| Enzyme 26 Molecular Weight |
46572.2 |
| Enzyme 26 Theoretical pI |
9.80 |
| Enzyme 26 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
- phosphatidylserine decarboxylase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in phosphatidylserine decarboxylase activity |
| Enzyme 26 Specific Function |
Phosphatidyl-L-serine = phosphatidylethanolamine + CO(2) |
| Enzyme 26 Pathways |
- Phospholipid Synthesis (map00564
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 26 Reactions |
- phosphatidyl-L-serine = phosphatidylethanolamine + CO2 [RN:R02055]
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
13489112  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
Q9UG56  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
PISD_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>1128 bp
ATGATGTGTCAGTCAGAGGCGCGGCAAGGACCAGAGCTCCGCGCGGCGAAATGGTTGCAC
TTCCCCCAGCTGGCCCTGAGGCGGAGGCTGGGGCAGCTGAGCTGCATGTCCAGACCCGCT
CTGAAACTGCGCTCCTGGCCCTTGACCGTCCTCTACTACCTCCTGCCCTTCGGCGCCCTC
AGACCGCTCAGCCGGGTGGGATGGAGGCCCGTAAGCAGGGTGGCTTTGTACAAGTCAGTG
CCAACGCGCTTGCTGTCACGGGCCTGGGGTCGCCTCAATCAGGTGGAGCTGCCACACTGG
CTGCGCAGGCCCGTCTACAGCCTGTACATCTGGACGTTTGGGGTGAACATGAAAGAGGCC
GCTGTGGAGGACCTGCATCACTACCGCAACCTCAGCGAGTTCTTCCGGCGCAAGCTGAAG
CCGCAGGCCCGGCCTGTCTGTGGCCTGCACAGCGTGATTAGCCCATCGGATGGAAGGATC
CTCAACTTTGGGCAGGTGAAGAACTGTGAGGTGGAGCAGGTAAAGGGGGTCACCTACTCC
CTGGAGTCGTTCCTGGGCCCGCGTATGTGCACAGAGGACCTGCCCTTCCCACCAGCCGCG
TCGTGTGACTCCTTCAAGAACCAGCTGGTCACCCGGGAAGGGAATGAGCTCTATCACTGT
GTCATCTACCTGGCCCCTGGGGACTACCACTGCTTCCACTCCCCCACCGACTGGACTGTG
TCCCACCGGCGCCACTTCCCAGGCTCCCTGATGTCAGTGAACCCTGGCATGGCTCGCTGG
ATCAAAGAGCTCTTCTGCCATAACGAGCGGGTGGTCCTGACGGGGGACTGGAAACATGGC
TTCTTCTCACTGACAGCTGTGGGGGCCACCAACGTGGGCTCCATTCGCATCTACTTTGAC
CGGGACCTGCACACAAACAGCCCAAGGCACAGCAAGGGCTCCTACAATGACTTCAGCTTC
GTGACGCACACCAATAGAGAGGGCGTCCCCATGCGTAAGGGCGAGCACCTGGGCGAGTTC
AACCTGGGCTCCACCATCGTGCTCATCTTCGAGGCCCCCAAGGACTTCAATTTCCAGCTG
AAAACAGGACAGAAAATCCGCTTTGGGGAAGCCCTGGGCTCGCTCTAG
|
| Enzyme 26 GenBank Gene ID |
NM_014338  |
| Enzyme 26 GeneCard ID |
PISD  |
| Enzyme 26 GenAtlas ID |
PISD  |
| Enzyme 26 HGNC ID |
HGNC:8999  |
| Enzyme 26 Chromosome Location |
2 |
| Enzyme 26 Locus |
22q12.2 |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- 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
]
- 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
]
- 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
]
|
| Enzyme 26 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
8048 |
| Enzyme 27 Name |
Phospholipid transfer protein |
| Enzyme 27 Synonyms |
- Lipid transfer protein II
|
| Enzyme 27 Gene Name |
PLTP |
| Enzyme 27 Protein Sequence |
>Phospholipid transfer protein
MALFGALFLALLAGAHAEFPGCKIRVTSKALELVKQEGLRFLEQELETITIPDLRGKEGH
FYYNISEVKVTELQLTSSELDFQPQQELMLQITNASLGLRFRRQLLYWFFYDGGYINASA
EGVSIRTGLELSRDPAGRMKVSNVSCQASVSRMHAAFGGTFKKVYDFLSTFITSGMRFLL
NQQICPVLYHAGTVLLNSLLDTVPVRSSVDELVGIDYSLMKDPVASTSNLDMDFRGAFFP
LTERNWSLPNRAVEPQLQEEERMVYVAFSEFFFDSAMESYFRAGALQLLLVGDKVPHDLD
MLLRATYFGSIVLLSPAVIDSPLKLELRVLAPPRCTIKPSGTTISVTASVTIALVPPDQP
EVQLSSMTMDARLSAKMALRGKALRTQLDLRRFRIYSNHSALESLALIPLQAPLKTMLQI
GVMPMLNERTWRGVQIPLPEGINFVHEVVTNHAGFLTIGADLHFAKGLREVIEKNRPADV
RASTAPTPSTAAV
|
| Enzyme 27 Number of Residues |
493 |
| Enzyme 27 Molecular Weight |
54738.8 |
| Enzyme 27 Theoretical pI |
7.01 |
| Enzyme 27 GO Classification |
| Function |
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 27 General Function |
Involved in lipid binding |
| Enzyme 27 Specific Function |
Converts HDL into larger and smaller particles. May play a key role in extracellular phospholipid transport and modulation of hdl particles |
| Enzyme 27 Pathways |
Not Available |
| Enzyme 27 Reactions |
Not Available |
| Enzyme 27 Pfam Domain Function |
|
| Enzyme 27 Signals |
|
| Enzyme 27 Transmembrane Regions |
|
| Enzyme 27 Essentiality |
Not Available |
| Enzyme 27 GenBank ID Protein |
18143452  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
P55058  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
PLTP_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1482 bp
ATGGCCCTCTTCGGGGCCCTCTTCCTAGCGCTGCTGGCAGGCGCACATGCAGAGTTCCCA
GGCTGCAAGATCCGCGTCACCTCCAAGGCGCTGGAGCTGGTGAAGCAGGAGGGGCTGCGC
TTTCTGGAGCAAGAGCTGGAGACTATCACCATTCCGGACCTGCGGGGCAAAGAAGGCCAC
TTCTACTACAACATCTCTGAGGTGAAGGTCACAGAGCTGCAACTGACATCTTCCGAGCTC
GATTTCCAGCCACAGCAGGAGCTGATGCTTCAAATCACCAATGCCTCCTTGGGGCTGCGC
TTCCGGAGACAGCTGCTCTACTGGTTCTTCTATGATGGGGGCTACATCAACGCCTCAGCT
GAGGGTGTGTCCATCCGCACTGGTCTGGAGCTCTCCCGGGATCCCGCTGGACGGATGAAA
GTGTCCAATGTCTCCTGCCAGGCCTCTGTCTCCAGAATGCACGCGGCCTTCGGGGGAACC
TTCAAGAAGGTGTATGATTTTCTCTCCACGTTCATCACCTCAGGGATGCGCTTCCTCCTC
AACCAGCAGATCTGCCCTGTCCTCTACCACGCAGGGACGGTCCTGCTCAACTCCCTCCTG
GACACCGTGCCTGTGCGCAGTTCTGTGGACGAGCTTGTTGGCATTGACTATTCCCTCATG
AAGGATCCTGTGGCTTCCACCAGCAACCTGGACATGGACTTCCGGGGGGCCTTCTTCCCC
CTGACTGAGAGGAACTGGAGCCTCCCCAACCGGGCAGTGGAGCCCCAGCTGCAGGAGGAA
GAGCGGATGGTGTATGTGGCCTTCTCTGAGTTCTTCTTCGACTCTGCCATGGAGAGCTAC
TTCCGGGCGGGGGCCCTGCAGCTGTTGCTGGTGGGGGACAAGGTGCCCCACGACCTGGAC
ATGCTGCTGAGGGCCACCTACTTTGGGAGCATTGTCCTGCTGAGCCCAGCAGTGATTGAC
TCCCCATTGAAGCTGGAGCTGCGGGTCCTGGCCCCACCGCGCTGCACCATCAAGCCCTCT
GGCACCACCATCTCTGTCACTGCTAGCGTCACCATTGCCCTGGTCCCACCAGACCAGCCT
GAGGTCCAGCTGTCCAGCATGACTATGGACGCCCGTCTCAGCGCCAAGATGGCTCTCCGG
GGGAAGGCCCTGCGCACGCAGCTGGACCTGCGCAGGTTCCGAATCTATTCCAACCATTCT
GCACTGGAGTCGCTGGCTCTGATCCCATTACAGGCCCCTCTGAAGACCATGCTGCAGATT
GGGGTGATGCCCATGCTCAATGAGCGGACCTGGCGTGGGGTGCAGATCCCACTACCTGAG
GGCATCAACTTTGTGCATGAGGTGGTGACGAACCATGCGGGATTCCTCACCATCGGGGCT
GATCTCCACTTTGCCAAAGGGCTGCGAGAGGTGATTGAGAAGAACCGGCCTGCTGATGTC
AGGGCGTCCACTGCCCCCACACCGTCCACAGCAGCTGTCTGA
|
| Enzyme 27 GenBank Gene ID |
AB076694  |
| Enzyme 27 GeneCard ID |
PLTP  |
| Enzyme 27 GenAtlas ID |
PLTP  |
| Enzyme 27 HGNC ID |
HGNC:9093  |
| Enzyme 27 Chromosome Location |
2 |
| Enzyme 27 Locus |
20q13.12 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Day JR, Albers JJ, Lofton-Day CE, Gilbert TL, Ching AF, Grant FJ, O'Hara PJ, Marcovina SM, Adolphson JL: Complete cDNA encoding human phospholipid transfer protein from human endothelial cells. J Biol Chem. 1994 Mar 25;269(12):9388-91. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Deloukas P, Matthews LH, Ashurst J, Burton J, Gilbert JG, Jones M, Stavrides G, Almeida JP, Babbage AK, Bagguley CL, Bailey J, Barlow KF, Bates KN, Beard LM, Beare DM, Beasley OP, Bird CP, Blakey SE, Bridgeman AM, Brown AJ, Buck D, Burrill W, Butler AP, Carder C, Carter NP, Chapman JC, Clamp M, Clark G, Clark LN, Clark SY, Clee CM, Clegg S, Cobley VE, Collier RE, Connor R, Corby NR, Coulson A, Coville GJ, Deadman R, Dhami P, Dunn M, Ellington AG, Frankland JA, Fraser A, French L, Garner P, Grafham DV, Griffiths C, Griffiths MN, Gwilliam R, Hall RE, Hammond S, Harley JL, Heath PD, Ho S, Holden JL, Howden PJ, Huckle E, Hunt AR, Hunt SE, Jekosch K, Johnson CM, Johnson D, Kay MP, Kimberley AM, King A, Knights A, Laird GK, Lawlor S, Lehvaslaiho MH, Leversha M, Lloyd C, Lloyd DM, Lovell JD, Marsh VL, Martin SL, McConnachie LJ, McLay K, McMurray AA, Milne S, Mistry D, Moore MJ, Mullikin JC, Nickerson T, Oliver K, Parker A, Patel R, Pearce TA, Peck AI, Phillimore BJ, Prathalingam SR, Plumb RW, Ramsay H, Rice CM, Ross MT, Scott CE, Sehra HK, Shownkeen R, Sims S, Skuce CD, Smith ML, Soderlund C, Steward CA, Sulston JE, Swann M, Sycamore N, Taylor R, Tee L, Thomas DW, Thorpe A, Tracey A, Tromans AC, Vaudin M, Wall M, Wallis JM, Whitehead SL, Whittaker P, Willey DL, Williams L, Williams SA, Wilming L, Wray PW, Hubbard T, Durbin RM, Bentley DR, Beck S, Rogers J: The DNA sequence and comparative analysis of human chromosome 20. Nature. 2001 Dec 20-27;414(6866):865-71. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Qu SJ, Fan HZ, Kilinc C, Pownall HJ: Role of cysteine residues in human plasma phospholipid transfer protein. J Protein Chem. 1999 Feb;18(2):193-8. [PubMed
]
- Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed
]
|
| Enzyme 27 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
8755 |
| Enzyme 28 Name |
Phospholipase A2, group XIIA, isoform CRA_b |
| Enzyme 28 Synonyms |
- SubName: cDNA PSEC0079 fis, clone NT2RP2004049, highly similar to Group XII secretory phospholipase A2 (EC 3.1.1.4)
- SubName: cDNA, FLJ93563, Homo sapiens phospholipase A2, group XII (PLA2G12), mRNA
|
| Enzyme 28 Gene Name |
PLA2G12A |
| Enzyme 28 Protein Sequence |
>Phospholipase A2, group XIIA, isoform CRA_b
MALLSRPALTLLLLLMAAVVRCQEQAQTTDWRATLKTIRNGVHKIDTYLNAALDLLGGED
GLCQYKCSDGSKPFPRYGYKPSPPNGCGSPLFGVHLNIGIPSLTKCCNQHDRCYETCGKS
KNDCDEEFQYCLSKICRDVQKTLGLTQHVQACETTVELLFDSVIHLGCKPYLDSQRAACR
CHYEEKTDL
|
| Enzyme 28 Number of Residues |
189 |
| Enzyme 28 Molecular Weight |
21067.0 |
| Enzyme 28 Theoretical pI |
7.27 |
| Enzyme 28 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 28 General Function |
Involved in phospholipase A2 activity |
| Enzyme 28 Specific Function |
Not Available |
| Enzyme 28 Pathways |
|
| Enzyme 28 Reactions |
Not Available |
| Enzyme 28 Pfam Domain Function |
|
| Enzyme 28 Signals |
|
| Enzyme 28 Transmembrane Regions |
|
| Enzyme 28 Essentiality |
Not Available |
| Enzyme 28 GenBank ID Protein |
22761446  |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
Q542Y6  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
Q542Y6_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>570 bp
ATGGCCCTGCTCTCGCGCCCCGCGCTCACCCTCCTGCTCCTCCTCATGGCCGCTGTTGTC
AGGTGCCAGGAGCAGGCCCAGACCACCGACTGGAGAGCCACCCTGAAGACCATCCGGAAC
GGCGTTCATAAGATAGACACGTACCTGAACGCCGCCTTGGACCTCCTAGGAGGCGAGGAC
GGTCTCTGCCAGTATAAATGCAGTGACGGATCTAAGCCTTTCCCACGTTATGGTTATAAA
CCCTCCCCACCGAATGGATGTGGCTCTCCACTGTTTGGTGTTCATCTTAACATTGGTATC
CCTTCCCTGACAAAGTGTTGCAACCAACACGACAGGTGCTATGAGACCTGTGGCAAAAGC
AAGAATGACTGTGATGAAGAATTCCAGTATTGCCTCTCCAAGATCTGCCGAGATGTACAG
AAAACACTAGGACTAACTCAGCATGTTCAGGCATGTGAAACAACAGTGGAGCTCTTGTTT
GACAGTGTTATACATTTAGGTTGTAAACCATATCTGGACAGCCAACGAGCCGCATGCAGG
TGTCATTATGAAGAAAAAACTGATCTTTAA
|
| Enzyme 28 GenBank Gene ID |
AK075389  |
| Enzyme 28 GeneCard ID |
PLA2G12A  |
| Enzyme 28 GenAtlas ID |
PLA2G12A  |
| Enzyme 28 HGNC ID |
HGNC:18554  |
| Enzyme 28 Chromosome Location |
4 |
| Enzyme 28 Locus |
4q25 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Otsuki T, Ota T, Nishikawa T, Hayashi K, Suzuki Y, Yamamoto J, Wakamatsu A, Kimura K, Sakamoto K, Hatano N, Kawai Y, Ishii S, Saito K, Kojima S, Sugiyama T, Ono T, Okano K, Yoshikawa Y, Aotsuka S, Sasaki N, Hattori A, Okumura K, Nagai K, Sugano S, Isogai T: Signal sequence and keyword trap in silico for selection of full-length human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA libraries. DNA Res. 2005;12(2):117-26. [PubMed
]
|
| Enzyme 28 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
8937 |
| Enzyme 29 Name |
Choline/ethanolaminephosphotransferase 1 |
| Enzyme 29 Synonyms |
- hCEPT1
|
| Enzyme 29 Gene Name |
CEPT1 |
| Enzyme 29 Protein Sequence |
>Choline/ethanolaminephosphotransferase 1
MSGHRSTRKRCGDSHPESPVGFGHMSTTGCVLNKLFQLPTPPLSRHQLKRLEEHRYQSAG
RSLLEPLMQGYWEWLVRRVPSWIAPNLITIIGLSINICTTILLVFYCPTATEQAPLWAYI
ACACGLFIYQSLDAIDGKQARRTNSSSPLGELFDHGCDSLSTVFVVLGTCIAVQLGTNPD
WMFFCCFAGTFMFYCAHWQTYVSGTLRFGIIDVTEVQIFIIIMHLLAVIGGPPFWQSMIP
VLNIQMKIFPALCTVAGTIFSCTNYFRVIFTGGVGKNGSTIAGTSVLSPFLHIGSVITLA
AMIYKKSAVQLFEKHPCLYILTFGFVSAKITNKLVVAHMTKSEMHLHDTAFIGPALLFLD
QYFNSFIDEYIVLWIALVFSFFDLIRYCVSVCNQIASHLHIHVFRIKVSTAHSNHH
|
| Enzyme 29 Number of Residues |
416 |
| Enzyme 29 Molecular Weight |
46553.1 |
| Enzyme 29 Theoretical pI |
8.25 |
| Enzyme 29 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, for other substituted phosphate groups
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
|
|
| Enzyme 29 General Function |
Involved in phosphotransferase activity, for other substituted phosphate groups |
| Enzyme 29 Specific Function |
Catalyzes both phosphatidylcholine and phosphatidylethanolamine biosynthesis from CDP-choline and CDP- ethanolamine, respectively. Involved in protein-dependent process of phospholipid transport to distribute phosphatidyl choline to the lumenal surface. Has a higher cholinephosphotransferase activity than ethanolaminephosphotransferase activity |
| Enzyme 29 Pathways |
|
| Enzyme 29 Reactions |
- CDP-choline + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylcholine [RN:R01321]
|
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
- 87-107
115-135
186-206
209-229
239-259
283-303
317-337
365-385
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
4584877  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q9Y6K0  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
CEPT1_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1251 bp
ATGAGTGGGCATCGATCAACAAGGAAAAGATGTGGAGATTCTCACCCGGAGTCCCCAGTG
GGCTTCGGGCATATGAGTACTACAGGATGTGTATTAAATAAATTGTTTCAGTTACCAACA
CCACCATTGTCAAGACACCAACTAAAGCGGCTAGAAGAACACAGATATCAAAGTGCTGGA
CGGTCCCTGCTTGAGCCCTTAATGCAAGGGTATTGGGAATGGCTCGTTAGAAGAGTTCCC
TCCTGGATTGCCCCAAATCTCATCACCATCATTGGACTGTCAATAAACATCTGTACAACT
ATTTTATTAGTCTTCTACTGCCCTACAGCTACAGAGCAGGCACCTCTGTGGGCATATATT
GCTTGTGCCTGTGGCCTTTTCATTTACCAGTCTTTGGATGCTATTGATGGGAAACAGGCA
AGAAGAACCAATAGTAGTTCTCCTCTGGGAGAACTTTTTGATCATGGCTGTGATTCACTA
TCAACAGTTTTTGTGGTTCTTGGAACTTGTATTGCAGTGCAGCTGGGGACAAACCCTGAT
TGGATGTTTTTTTGTTGTTTTGCGGGGACATTTATGTTCTATTGTGCGCACTGGCAAACG
TATGTTTCTGGAACATTGCGATTTGGAATAATTGATGTGACTGAAGTGCAAATCTTCATA
ATAATCATGCATTTGCTGGCAGTGATTGGAGGACCACCTTTTTGGCAATCTATGATTCCA
GTGCTGAATATTCAAATGAAAATTTTTCCTGCACTTTGTACTGTAGCAGGGACCATATTT
TCCTGTACAAATTACTTCCGTGTAATCTTCACAGGTGGTGTTGGCAAAAATGGATCAACA
ATAGCAGGAACAAGTGTCCTTTCTCCTTTTCTCCATATTGGATCAGTGATTACATTAGCT
GCAATGATCTACAAGAAATCTGCAGTTCAGCTTTTTGAAAAGCATCCCTGTCTTTATATA
CTGACATTTGGTTTTGTGTCTGCTAAAATCACTAATAAGCTTGTGGTTGCACACATGACG
AAAAGTGAAATGCATTTGCATGACACAGCATTCATAGGTCCGGCACTTTTGTTTCTGGAC
CAGTATTTTAACAGCTTTATTGATGAATATATTGTACTTTGGATTGCCCTGGTTTTCTCT
TTCTTTGATTTGATCCGCTACTGTGTCAGTGTTTGCAATCAGATTGCGTCTCACCTGCAC
ATACATGTCTTCAGAATCAAGGTCTCTACAGCTCATTCTAATCATCATTAA
|
| Enzyme 29 GenBank Gene ID |
AF068302  |
| Enzyme 29 GeneCard ID |
CEPT1  |
| Enzyme 29 GenAtlas ID |
CEPT1  |
| Enzyme 29 HGNC ID |
HGNC:24289  |
| Enzyme 29 Chromosome Location |
1 |
| Enzyme 29 Locus |
1p13.3 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Henneberry AL, McMaster CR: Cloning and expression of a human choline/ethanolaminephosphotransferase: synthesis of phosphatidylcholine and phosphatidylethanolamine. Biochem J. 1999 Apr 15;339 ( Pt 2):291-8. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Henneberry AL, Wistow G, McMaster CR: Cloning, genomic organization, and characterization of a human cholinephosphotransferase. J Biol Chem. 2000 Sep 22;275(38):29808-15. [PubMed
]
- Wright MM, McMaster CR: PC and PE synthesis: mixed micellar analysis of the cholinephosphotransferase and ethanolaminephosphotransferase activities of human choline/ethanolamine phosphotransferase 1 (CEPT1). Lipids. 2002 Jul;37(7):663-72. [PubMed
]
- Henneberry AL, Wright MM, McMaster CR: The major sites of cellular phospholipid synthesis and molecular determinants of Fatty Acid and lipid head group specificity. Mol Biol Cell. 2002 Sep;13(9):3148-61. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
|
| Enzyme 29 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
12911 |
| Enzyme 30 Name |
Phospholipase D3 |
| Enzyme 30 Synonyms |
- PLD 3
- Choline phosphatase 3
- HindIII K4L homolog
- Hu-K4
- Phosphatidylcholine-hydrolyzing phospholipase D3
|
| Enzyme 30 Gene Name |
PLD3 |
| Enzyme 30 Protein Sequence |
>Phospholipase D3
MKPKLMYQELKVPAEEPANELPMNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLW
EYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLDFPNASTGNPSTSQAWLGLLAGAHSSL
DIASFYWTLTNNDTHTQEPSAQQGEEVLRQLQTLAPKGVNVRIAVSKPSGPQPQADLQAL
LQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCL
ARDLTKIFEAYWFLGQAGSSIPSTWPRFYDTRYNQETPMEICLNGTPALAYLASAPPPLC
PSGRTPDLKALLNVVDNARSFIYVAVMNYLPTLEFSHPHRFWPAIDDGLRRATYERGVKV
RLLISCWGHSEPSMRAFLLSLAALRDNHTHSDIQVKLFVVPADEAQARIPYARVNHNKYM
VTERATYIGTSNWSGNYFTETAGTSLLVTQNGRGGLRSQLEAIFLRDWDSPYSHDLDTSA
DSVGNACRLL
|
| Enzyme 30 Number of Residues |
490 |
| Enzyme 30 Molecular Weight |
54704.9 |
| Enzyme 30 Theoretical pI |
6.45 |
| Enzyme 30 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 30 General Function |
Involved in catalytic activity |
| Enzyme 30 Specific Function |
A phosphatidylcholine + H(2)O = choline + a phosphatidate |
| Enzyme 30 Pathways |
|
| Enzyme 30 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
72534684  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q8IV08  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
PLD3_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>1473 bp
ATGAAGCCTAAACTGATGTACCAGGAGCTGAAGGTGCCTGCAGAGGAGCCCGCCAATGAG
CTGCCCATGAATGAGATTGAGGCGTGGAAGGCTGCGGAAAAGAAAGCCCGCTGGGTCCTG
CTGGTCCTCATTCTGGCGGTTGTGGGCTTCGGAGCCCTGATGACTCAGCTGTTTCTATGG
GAATACGGCGACTTGCATCTCTTTGGGCCCAACCAGCGCCCAGCCCCCTGCTATGACCCT
TGCGAAGCAGTGCTGGTGGAAAGCATTCCTGAGGGCCTGGACTTCCCCAATGCCTCCACG
GGGAACCCTTCCACCAGCCAGGCCTGGCTGGGCCTGCTCGCCGGTGCGCACAGCAGCCTG
GACATCGCCTCCTTCTACTGGACCCTCACCAACAATGACACCCACACGCAGGAGCCCTCT
GCCCAGCAGGGTGAGGAGGTCCTCCGGCAGCTGCAGACCCTGGCACCAAAGGGCGTGAAC
GTCCGCATCGCTGTGAGCAAGCCCAGCGGGCCCCAGCCACAGGCGGACCTGCAGGCTCTG
CTGCAGAGCGGTGCCCAGGTCCGCATGGTGGACATGCAGAAGCTGACCCATGGCGTCCTG
CATACCAAGTTCTGGGTGGTGGACCAGACCCACTTCTACCTGGGCAGTGCCAACATGGAC
TGGCGTTCACTGACCCAGGTCAAGGAGCTGGGCGTGGTCATGTACAACTGCAGCTGCCTG
GCTCGAGACCTGACCAAGATCTTTGAGGCCTACTGGTTCCTGGGCCAGGCAGGCAGCTCC
ATCCCATCAACTTGGCCCCGGTTCTATGACACCCGCTACAACCAAGAGACACCAATGGAG
ATCTGCCTCAATGGAACCCCTGCTCTGGCCTACCTGGCGAGTGCGCCCCCACCCCTGTGT
CCAAGTGGCCGCACTCCAGACCTGAAGGCTCTACTCAACGTGGTGGACAATGCCCGGAGT
TTCATCTACGTCGCTGTCATGAACTACCTGCCCACTCTGGAGTTCTCCCACCCTCACAGG
TTCTGGCCTGCCATTGACGATGGGCTGCGGCGGGCCACCTACGAGCGTGGCGTCAAGGTG
CGCCTGCTCATCAGCTGCTGGGGACACTCGGAGCCATCCATGCGGGCCTTCCTGCTCTCT
CTGGCTGCCCTGCGTGACAACCATACCCACTCTGACATCCAGGTGAAACTCTTTGTGGTC
CCCGCGGATGAGGCCCAGGCTCGAATCCCATATGCCCGTGTCAACCACAACAAGTACATG
GTGACTGAACGCGCCACCTACATCGGAACCTCCAACTGGTCTGGCAACTACTTCACGGAG
ACGGCGGGCACCTCGCTGCTGGTGACGCAGAATGGGAGGGGCGGCCTGCGGAGCCAGCTG
GAGGCCATTTTCCTGAGGGACTGGGACTCCCCTTACAGCCATGACCTTGACACCTCAGCT
GACAGCGTGGGCAACGCCTGCCGCCTGCTCTGA
|
| Enzyme 30 GenBank Gene ID |
NM_001031696.2  |
| Enzyme 30 GeneCard ID |
PLD3  |
| Enzyme 30 GenAtlas ID |
PLD3  |
| Enzyme 30 HGNC ID |
HGNC:17158  |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
19q13.2 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Cao JX, Koop BF, Upton C: A human homolog of the vaccinia virus HindIII K4L gene is a member of the phospholipase D superfamily. Virus Res. 1997 Apr;48(1):11-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Munck A, Bohm C, Seibel NM, Hashemol Hosseini Z, Hampe W: Hu-K4 is a ubiquitously expressed type 2 transmembrane protein associated with the endoplasmic reticulum. FEBS J. 2005 Apr;272(7):1718-26. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
|
| Enzyme 30 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
12912 |
| Enzyme 31 Name |
Phospholipase D4 |
| Enzyme 31 Synonyms |
- PLD 4
- Choline phosphatase 4
- Phosphatidylcholine-hydrolyzing phospholipase D4
|
| Enzyme 31 Gene Name |
PLD4 |
| Enzyme 31 Protein Sequence |
>Phospholipase D4
MLKPLWKAAVAPTWPCSMPPRRPWDREAGTLQVLGALAVLWLGSVALICLLWQVPRPPTW
GQVQPKDVPRSWEHGSSPAWEPLEAEARQQRDSCQLVLVESIPQDLPSAAGSPSAQPLGQ
AWLQLLDTAQESVHVASYYWSLTGPDIGVNDSSSQLGEALLQKLQQLLGRNISLAVATSS
PTLARTSTDLQVLAARGAHVRQVPMGRLTRGVLHSKFWVVDGRHIYMGSANMDWRSLTQV
KELGAVIYNCSHLAQDLEKTFQTYWVLGVPKAVLPKTWPQNFSSHFNRFQPFHGLFDGVP
TTAYFSASPPALCPQGRTRDLEALLAVMGSAQEFIYASVMEYFPTTRFSHPPRYWPVLDN
ALRAAAFGKGVRVRLLVGCGLNTDPTMFPYLRSLQALSNPAANVSVDVKVFIVPVGNHSN
IPFSRVNHSKFMVTEKAAYIGTSNWSEDYFSSTAGVGLVVTQSPGAQPAGATVQEQLRQL
FERDWSSRYAVGLDGQAPGQDCVWQG
|
| Enzyme 31 Number of Residues |
506 |
| Enzyme 31 Molecular Weight |
55626.1 |
| Enzyme 31 Theoretical pI |
8.46 |
| Enzyme 31 GO Classification |
| Function |
|
| Process |
|
| Component |
| — |
|
| Enzyme 31 General Function |
Involved in catalytic activity |
| Enzyme 31 Specific Function |
A phosphatidylcholine + H(2)O = choline + a phosphatidate |
| Enzyme 31 Pathways |
|
| Enzyme 31 Reactions |
- a phosphatidylcholine + H2O = choline + a phosphatidate [RN:R01310]
|
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
94681038  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
Q96BZ4  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
PLD4_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1521 bp
ATGCTGAAGCCTCTTTGGAAAGCAGCAGTGGCCCCCACATGGCCATGCTCCATGCCGCCC
CGCCGCCCGTGGGACAGAGAGGCTGGCACGTTGCAGGTCCTGGGAGCGCTGGCTGTGCTG
TGGCTGGGCTCCGTGGCTCTTATCTGCCTCCTGTGGCAAGTGCCCCGTCCTCCCACCTGG
GGCCAGGTGCAGCCCAAGGACGTGCCCAGGTCCTGGGAGCATGGCTCCAGCCCAGCTTGG
GAGCCCCTGGAAGCAGAGGCCAGGCAGCAGAGGGACTCCTGCCAGCTTGTCCTTGTGGAA
AGCATCCCCCAGGACCTGCCATCTGCAGCCGGCAGCCCCTCTGCCCAGCCTCTGGGCCAG
GCCTGGCTGCAGCTGCTGGACACTGCCCAGGAGAGCGTCCACGTGGCTTCATACTACTGG
TCCCTCACAGGGCCTGACATCGGGGTCAACGACTCGTCTTCCCAGCTGGGAGAGGCTCTT
CTGCAGAAGCTGCAGCAGCTGCTGGGCAGGAACATTTCCCTGGCTGTGGCCACCAGCAGC
CCGACACTGGCCAGGACATCCACCGACCTGCAGGTTCTGGCTGCCCGAGGTGCCCATGTA
CGACAGGTGCCCATGGGGCGGCTCACCAGGGGTGTTTTGCACTCCAAATTCTGGGTTGTG
GATGGACGGCACATATACATGGGCAGTGCCAACATGGACTGGCGGTCTCTGACGCAGGTG
AAGGAGCTTGGCGCTGTCATCTATAACTGCAGCCACCTGGCCCAAGACCTGGAGAAGACC
TTCCAGACCTACTGGGTACTGGGGGTGCCCAAGGCTGTCCTCCCCAAAACCTGGCCTCAG
AACTTCTCATCTCACTTCAACCGTTTCCAGCCCTTCCACGGCCTCTTTGATGGGGTGCCC
ACCACTGCCTACTTCTCAGCGTCGCCACCAGCACTCTGTCCCCAGGGCCGCACCCGGGAC
CTGGAGGCGCTGCTGGCGGTGATGGGGAGCGCCCAGGAGTTCATCTATGCCTCCGTGATG
GAGTATTTCCCCACCACGCGCTTCAGCCACCCCCCGAGGTACTGGCCGGTGCTGGACAAC
GCGCTGCGGGCGGCAGCCTTCGGCAAGGGCGTGCGCGTGCGCCTGCTGGTCGGCTGCGGA
CTCAACACGGACCCCACCATGTTCCCCTACCTGCGGTCCCTGCAGGCGCTCAGCAACCCC
GCGGCCAACGTCTCTGTGGACGTGAAAGTCTTCATCGTGCCGGTGGGGAACCATTCCAAC
ATCCCATTCAGCAGGGTGAACCACAGCAAGTTCATGGTCACGGAGAAGGCAGCCTACATA
GGCACCTCCAACTGGTCGGAGGATTACTTCAGCAGCACGGCGGGGGTGGGCTTGGTGGTC
ACCCAGAGCCCTGGCGCGCAGCCCGCGGGGGCCACGGTGCAGGAGCAGCTGCGGCAGCTC
TTTGAGCGGGACTGGAGTTCGCGCTACGCCGTCGGCCTGGACGGACAGGCTCCGGGCCAG
GACTGCGTTTGGCAGGGCTGA
|
| Enzyme 31 GenBank Gene ID |
NM_138790.2  |
| Enzyme 31 GeneCard ID |
PLD4  |
| Enzyme 31 GenAtlas ID |
PLD4  |
| Enzyme 31 HGNC ID |
HGNC:23792  |
| Enzyme 31 Chromosome Location |
1 |
| Enzyme 31 Locus |
14q32.33 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Tao WA, Wollscheid B, O'Brien R, Eng JK, Li XJ, Bodenmiller B, Watts JD, Hood L, Aebersold R: Quantitative phosphoproteome analysis using a dendrimer conjugation chemistry and tandem mass spectrometry. Nat Methods. 2005 Aug;2(8):591-8. [PubMed
]
|
| Enzyme 31 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
12915 |
| Enzyme 32 Name |
Phospholipid scramblase 2 |
| Enzyme 32 Synonyms |
- PL scramblase 2
- Ca(2+)-dependent phospholipid scramblase 2
|
| Enzyme 32 Gene Name |
PLSCR2 |
| Enzyme 32 Protein Sequence |
>Phospholipid scramblase 2
MPAPPPPLNCPPGLEYLSQIDMILIHQQIELLEVLFSFESSNMYEIKNSFGQRIYFAAED
TNFCIRNCCGRSRPFTLRITDNVGREVITLERPLRCNCCCCPCCLQEIEIQAPPGVPVGY
VTQTWHPCLTKFTIKNQKREDVLKISGPCIVCSCIAGVDFEITSLDEQIVVGRISKHWSG
FLREAFTDADNFGIQFPRDLDVKMKAVMIGACFLIDYMFFERTR
|
| Enzyme 32 Number of Residues |
224 |
| Enzyme 32 Molecular Weight |
25522.5 |
| Enzyme 32 Theoretical pI |
5.34 |
| Enzyme 32 GO Classification |
Not Available |
| Enzyme 32 General Function |
Involved in calcium ion binding |
| Enzyme 32 Specific Function |
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system |
| Enzyme 32 Pathways |
Not Available |
| Enzyme 32 Reactions |
Not Available |
| Enzyme 32 Pfam Domain Function |
|
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
9651165  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q9NRY7  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
PLS2_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>675 bp
ATGCCAGCACCACCACCACCATTAAACTGTCCGCCAGGATTGGAATACTTAAGTCAGATA
GATATGATACTAATTCATCAGCAAATTGAACTTCTGGAAGTTCTATTCAGTTTTGAAAGT
AGTAACATGTATGAAATCAAGAACAGCTTTGGGCAGAGGATTTATTTTGCAGCAGAAGAT
ACTAATTTCTGTATCCGAAATTGCTGTGGGCGGTCTAGACCTTTTACCTTGAGGATTACT
GATAATGTGGGTCGAGAAGTCATAACTCTGGAAAGACCACTAAGATGTAACTGTTGTTGT
TGCCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGTGTACCAGTAGGTTAT
GTTACTCAGACCTGGCACCCATGTCTAACAAAGTTTACAATTAAAAATCAGAAAAGAGAG
GATGTACTAAAAATTAGTGGTCCATGTATCGTGTGCAGCTGTATTGCGGGTGTTGATTTT
GAGATTACATCTCTTGATGAACAAATTGTGGTTGGCAGGATTTCTAAGCACTGGTCTGGG
TTTTTAAGAGAGGCATTTACTGATGCTGACAACTTTGGAATCCAATTCCCTAGAGACCTT
GATGTTAAAATGAAAGCCGTGATGATTGGTGCCTGTTTCCTCATTGACTACATGTTTTTT
GAAAGAACTAGGTAA
|
| Enzyme 32 GenBank Gene ID |
AF159441  |
| Enzyme 32 GeneCard ID |
PLSCR2  |
| Enzyme 32 GenAtlas ID |
PLSCR2  |
| Enzyme 32 HGNC ID |
HGNC:16494  |
| Enzyme 32 Chromosome Location |
3 |
| Enzyme 32 Locus |
3q24 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 32 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
12916 |
| Enzyme 33 Name |
Phospholipid scramblase 3 |
| Enzyme 33 Synonyms |
- PL scramblase 3
- Ca(2+)-dependent phospholipid scramblase 3
|
| Enzyme 33 Gene Name |
PLSCR3 |
| Enzyme 33 Protein Sequence |
>Phospholipid scramblase 3
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVAL
GSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAA
EESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTI
GHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQW
GGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAVTS
|
| Enzyme 33 Number of Residues |
295 |
| Enzyme 33 Molecular Weight |
31648.1 |
| Enzyme 33 Theoretical pI |
6.63 |
| Enzyme 33 GO Classification |
Not Available |
| Enzyme 33 General Function |
Involved in calcium ion binding |
| Enzyme 33 Specific Function |
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
31543417  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q9NRY6  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
PLS3_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>888 bp
ATGGCAGGCTACTTGCCCCCCAAAGGCTACGCCCCTTCGCCCCCACCTCCCTACCCTGTC
ACCCCTGGGTACCCGGAGCCGGCGCTACATCCTGGGCCCGGGCAGGCGCCAGTGCCCGCC
CAGGTACCTGCCCCAGCTCCCGGCTTCGCCCTCTTCCCCTCGCCTGGCCCCGTGGCCTTG
GGGTCTGCTGCCCCCTTCTTGCCACTGCCAGGGGTGCCTTCTGGCCTCGAATTCCTGGTG
CAGATTGATCAGATTTTGATTCACCAGAAGGCTGAGCGAGTGGAAACGTTCCTAGGCTGG
GAGACCTGTAATCGGTATGAACTGCGCTCTGGGGCCGGGCAGCCCCTGGGTCAGGCGGCC
GAGGAGAGCAACTGCTGCGCCCGTCTGTGCTGTGGCGCCCGCCGGCCGCTGCGTGTCCGC
CTGGCCGACCCCGGGGACCGTGAGGTGCTGCGTTTGCTCCGCCCGCTGCACTGTGGCTGC
AGCTGCTGCCCCTGTGGCCTCCAGGAGATGGAAGTACAGGCTCCACCAGGCACCACCATT
GGCCACGTGCTACAGACCTGGCATCCCTTCCTCCCCAAGTTCTCCATCCAGGATGCCGAT
CGCCAGACAGTCTTGCGAGTGGTGGGGCCCTGCTGGACCTGTGGCTGTGGCACAGACACC
AACTTTGAGGTGAAGACTCGGGATGAATCCCGCAGTGTGGGCCGCATCAGCAAGCAGTGG
GGGGGCCTGGTCCGAGAAGCCCTCACAGATGCAGATGACTTTGGCCTACAGTTCCCGCTG
GACCTGGATGTGAGGGTGAAGGCTGTGCTGCTGGGAGCCACATTCCTCATTGACTACATG
TTCTTTGAGAAGCGAGGAGGCGCTGGGCCCTCTGCCGTCACCAGTTAG
|
| Enzyme 33 GenBank Gene ID |
NM_020360.2  |
| Enzyme 33 GeneCard ID |
PLSCR3  |
| Enzyme 33 GenAtlas ID |
PLSCR3  |
| Enzyme 33 HGNC ID |
HGNC:16495  |
| Enzyme 33 Chromosome Location |
1 |
| Enzyme 33 Locus |
17p13.1 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Zody MC, Garber M, Adams DJ, Sharpe T, Harrow J, Lupski JR, Nicholson C, Searle SM, Wilming L, Young SK, Abouelleil A, Allen NR, Bi W, Bloom T, Borowsky ML, Bugalter BE, Butler J, Chang JL, Chen CK, Cook A, Corum B, Cuomo CA, de Jong PJ, DeCaprio D, Dewar K, FitzGerald M, Gilbert J, Gibson R, Gnerre S, Goldstein S, Grafham DV, Grocock R, Hafez N, Hagopian DS, Hart E, Norman CH, Humphray S, Jaffe DB, Jones M, Kamal M, Khodiyar VK, LaButti K, Laird G, Lehoczky J, Liu X, Lokyitsang T, Loveland J, Lui A, Macdonald P, Major JE, Matthews L, Mauceli E, McCarroll SA, Mihalev AH, Mudge J, Nguyen C, Nicol R, O'Leary SB, Osoegawa K, Schwartz DC, Shaw-Smith C, Stankiewicz P, Steward C, Swarbreck D, Venkataraman V, Whittaker CA, Yang X, Zimmer AR, Bradley A, Hubbard T, Birren BW, Rogers J, Lander ES, Nusbaum C: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage. Nature. 2006 Apr 20;440(7087):1045-9. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Shibata H, Suzuki H, Kakiuchi T, Inuzuka T, Yoshida H, Mizuno T, Maki M: Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants. J Biol Chem. 2008 Apr 11;283(15):9623-32. Epub 2008 Feb 6. [PubMed
]
|
| Enzyme 33 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
12917 |
| Enzyme 34 Name |
Phospholipid scramblase 4 |
| Enzyme 34 Synonyms |
- PL scramblase 4
- Ca(2+)-dependent phospholipid scramblase 4
- Cell growth-inhibiting gene 43 protein
- TRA1
|
| Enzyme 34 Gene Name |
PLSCR4 |
| Enzyme 34 Protein Sequence |
>Phospholipid scramblase 4
MSGVVPTAPEQPAGEMENQTKPPDPRPDAPPEYNSHFLPGPPGTAVPPPTGYPGGLPMGY
YSPQQPSTFPLYQPVGGIHPVRYQPGKYPMPNQSVPITWMPGPTPMANCPPGLEYLVQLD
NIHVLQHFEPLEMMTCFETNNRYDIKNNSDQMVYIVTEDTDDFTRNAYRTLRPFVLRVTD
CMGREIMTMQRPFRCTCCCFCCPSARQELEVQCPPGVTIGFVAEHWNLCRAVYSIQNEKK
ENVMRVRGPCSTYGCGSDSVFEVKSLDGISNIGSIIRKWNGLLSAMADADHFDIHFPLDL
DVKMKAMIFGACFLIDFMYFERSPPQRSR
|
| Enzyme 34 Number of Residues |
329 |
| Enzyme 34 Molecular Weight |
37005.2 |
| Enzyme 34 Theoretical pI |
5.62 |
| Enzyme 34 GO Classification |
Not Available |
| Enzyme 34 General Function |
Involved in calcium ion binding |
| Enzyme 34 Specific Function |
May mediate accelerated ATP-independent bidirectional transbilayer migration of phospholipids upon binding calcium ions that results in a loss of phospholipid asymmetry in the plasma membrane. May play a central role in the initiation of fibrin clot formation, in the activation of mast cells and in the recognition of apoptotic and injured cells by the reticuloendothelial system |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
|
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
9622872  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q9NRQ2  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
PLS4_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>990 bp
ATGTCAGGTGTGGTACCCACAGCCCCTGAACAGCCTGCAGGTGAAATGGAAAATCAAACA
AAACCACCAGATCCAAGGCCTGATGCTCCTCCTGAATACAGTTCTCATTTTTTACCAGGA
CCCCCTGGAACAGCTGTCCCTCCACCTACTGGCTACCCAGGAGGCTTGCCTATGGGATAC
TACAGTCCACAGCAACCCAGTACCTTCCCTTTGTACCAGCCAGTTGGTGGTATCCATCCT
GTCCGGTATCAGCCTGGCAAATATCCTATGCCAAATCAGTCTGTTCCAATAACATGGATG
CCAGGGCCAACTCCTATGGCAAACTGCCCTCCTGGTCTGGAATACTTAGTTCAGTTGGAC
AACATACATGTTCTTCAGCATTTTGAGCCTCTGGAAATGATGACATGTTTTGAAACTAAT
AATAGATATGATATTAAAAACAACTCAGACCAGATGGTTTACGTTGTAACCGAAGACACA
GATGACTTTACCAGGAATGCCTATCGGACACTAAGGCCCTTCGTCCTCCGGGTCACTGAT
TGTATGGGCCGAGAAATCATGACAATGCAGAGACCCTTCAGATGCACCTGCTGTTGCTTC
TGTTGCCCCTCTGCCAGACAAGAGCTGGAGGTGCAGTGTCCTCCTGGTGTCACCATTGGC
TTTGTTGCGGAACATTGGAACCTGTGCAGGGCGGTGTACAGCATCCAAAATGAGAAGAAA
GAAAATGTGATGAGAGTTCGTGGGCCATGCTCAACCTATGGCTGTGGTTCAGATTCTGTT
TTTGAGGTCAAATCCCTTGATGGCATATCCAACATCGGCAGTATTATCCGGAAGTGGAAT
GGTTTGTTATCAGCAATGGCAGATGCTGACCATTTTGACATTCACTTCCCACTAGACCTG
GATGTGAAGATGAAAGCCATGATTTTTGGAGCTTGCTTCCTCATTGACTTCATGTATTTT
GAAAGATCTCCACCACAACGTTCAAGATAG
|
| Enzyme 34 GenBank Gene ID |
AF199023  |
| Enzyme 34 GeneCard ID |
PLSCR4  |
| Enzyme 34 GenAtlas ID |
PLSCR4  |
| Enzyme 34 HGNC ID |
HGNC:16497  |
| Enzyme 34 Chromosome Location |
3 |
| Enzyme 34 Locus |
3q24 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Wiedmer T, Zhou Q, Kwoh DY, Sims PJ: Identification of three new members of the phospholipid scramblase gene family. Biochim Biophys Acta. 2000 Jul 31;1467(1):244-53. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Shibata H, Suzuki H, Kakiuchi T, Inuzuka T, Yoshida H, Mizuno T, Maki M: Identification of Alix-type and Non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants. J Biol Chem. 2008 Apr 11;283(15):9623-32. Epub 2008 Feb 6. [PubMed
]
|
| Enzyme 34 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
12918 |
| Enzyme 35 Name |
Phospholipid scramblase family member 5 |
| Enzyme 35 Synonyms |
Not Available |
| Enzyme 35 Gene Name |
PLSCR5 |
| Enzyme 35 Protein Sequence |
>Phospholipid scramblase family member 5
MASKDAQNQRRGLPGFLPGAPDPDQSLPASSNPGNQAWQLSLPLPSSFLPTVSLPPGLEY
LSQLDLIIIHQQVELLGMILGTETSNKYEIKNSLGQRIYFAVEESICFNRTFCSTLRSCT
LRITDNSGREVITVNRPLRCNSCWCPCYLQELEIQAPPGTIVGYVTQKWDPFLPKFTIQN
ANKEDILKIVGPCVTCGCFGDVDFEVKTINEKLTIGKISKYWSGFVNDVFTNADNFGIHV
PADLDVTVKAAMIGACFLFDFMFFEHSLAGL
|
| Enzyme 35 Number of Residues |
271 |
| Enzyme 35 Molecular Weight |
30026.2 |
| Enzyme 35 Theoretical pI |
4.90 |
| Enzyme 35 GO Classification |
Not Available |
| Enzyme 35 General Function |
Not Available |
| Enzyme 35 Specific Function |
Not Available |
| Enzyme 35 Pathways |
Not Available |
| Enzyme 35 Reactions |
Not Available |
| Enzyme 35 Pfam Domain Function |
|
| Enzyme 35 Signals |
|
| Enzyme 35 Transmembrane Regions |
|
| Enzyme 35 Essentiality |
Not Available |
| Enzyme 35 GenBank ID Protein |
146229354  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
A0PG75  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
PLS5_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>816 bp
ATGGCCTCTAAAGATGCCCAGAACCAAAGAAGAGGTCTGCCTGGTTTTCTTCCTGGAGCT
CCAGACCCAGACCAAAGCCTTCCTGCCTCTTCCAATCCAGGGAACCAAGCATGGCAGCTG
AGTCTCCCTCTGCCAAGCAGTTTCCTGCCAACAGTCAGTCTCCCTCCTGGTCTAGAATAT
TTAAGCCAGTTAGACCTGATAATTATACACCAGCAGGTGGAGCTGCTTGGAATGATACTT
GGTACTGAGACCTCCAACAAATATGAGATTAAAAACAGCTTGGGACAAAGAATTTACTTT
GCAGTGGAGGAAAGCATCTGCTTCAATCGTACTTTCTGTTCCACTCTGCGATCTTGCACC
CTGAGGATCACAGATAACTCAGGTCGAGAGGTCATTACAGTGAACAGGCCCTTGAGATGT
AACAGCTGCTGGTGCCCTTGCTACCTACAAGAGTTAGAAATCCAAGCCCCTCCTGGTACT
ATAGTTGGTTACGTTACGCAGAAGTGGGACCCCTTTCTGCCTAAATTCACAATCCAAAAT
GCAAACAAAGAAGATATTTTGAAAATTGTTGGTCCTTGTGTGACATGTGGCTGTTTTGGC
GATGTGGATTTTGAGGTGAAAACCATTAATGAAAAGCTTACAATTGGGAAGATTTCAAAG
TACTGGTCAGGATTTGTAAATGATGTCTTCACAAATGCTGACAATTTCGGAATTCATGTT
CCTGCAGATCTAGATGTAACAGTCAAAGCAGCAATGATCGGTGCCTGTTTTCTCTTTGAT
TTTATGTTCTTTGAACATTCACTGGCTGGATTATAA
|
| Enzyme 35 GenBank Gene ID |
NM_001085420.1  |
| Enzyme 35 GeneCard ID |
PLSCR5  |
| Enzyme 35 GenAtlas ID |
PLSCR5  |
| Enzyme 35 HGNC ID |
HGNC:19952  |
| Enzyme 35 Chromosome Location |
3 |
| Enzyme 35 Locus |
3q24 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
|
| Enzyme 35 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
12919 |
| Enzyme 36 Name |
Probable phospholipid-transporting ATPase VB |
| Enzyme 36 Synonyms |
- ATPase class V type 10B
|
| Enzyme 36 Gene Name |
ATP10B |
| Enzyme 36 Protein Sequence |
>Probable phospholipid-transporting ATPase VB
MALSVDSSWHRWQWRVRDGFPHCPSETTPLLSPEKGRQSYNLTQQRVVFPNNSIFHQDWE
EVSRRYPGNRTCTTKYTLFTFLPRNLFEQFHRWANLYFLFLVILNWMPSMEVFHREITML
PLAIVLFVIMIKDGMEDFKRHRFDKAINCSNIRIYERKEQTYVQKCWKDVRVGDFIQMKC
NEIVPADILLLFSSDPNGICHLETASLDGETNLKQRCVVKGFSQQEVQFEPELFHNTIVC
EKPNNHLNKFKGYMEHPDQTRTGFGCESLLLRGCTIRNTEMAVGIVIYAGHETKAMLNNS
GPRYKRSKIERRMNIDIFFCIGILILMCLIGAVGHSIWNGTFEEHPPFDVPDANGSFLPS
ALGGFYMFLTMIILLQVLIPISLYVSIELVKLGQVFFLSNDLDLYDEETDLSIQCRALNI
AEDLGQIQYIFSDKTGTLTENKMVFRRCTIMGSEYSHQENAKRLETPKELDSDGEEWTQY
QCLSFSARWAQDPATMRSQKGAQPLRRSQSARVPIQGHYRQRSMGHRESSQPPVAFSSSI
EKDVTPDKNLLTKVRDAALWLETLSDSRPAKASLSTTSSIADFFLALTICNSVMVSTTTE
PRQRVTIKPSSKALGTSLEKIQQLFQKLKLLSLSQSFSSTAPSDTDLGESLGANVATTDS
DERDDASVCSGGDSTDDGGYRSSMWDQGDILESGSGTSLEEALEAPATDLARPEFCYEAE
SPDEAALVHAAHAYSFTLVSRTPEQVTVRLPQGTCLTFSLLCTLGFDSVRKRMSVVVRHP
LTGEIVVYTKGADSVIMDLLEDPACVPDINMEKKLRKIRARTQKHLDLYARDGLRTLCIA
KKVVSEEDFRRWASFRREAEASLDNRDELLMETAQHLENQLTLLGATGIEDRLQEGVPDT
IATLREAGIQLWVLTGDKQETAVNIAHSCRLLNQTDTVYTINTENQETCESILNCALEEL
KQFRELQKPDRKLFGFRLPSKTPSITSEAVVPEAGLVIDGKTLNAIFQGKLEKKFLELTQ
YCRSVLCCRSTPLQKSMIVKLVRDKLRVMTLSIGDGANDVSMIQAADIGIGISGQEGMQA
VMSSDFAITRFKHLKKLLLVHGHWCYSRLARMVVYYLYKNVCYVNLLFWYQFFCGFSSST
MIDYWQMIFFNLFFTSLPPLVFGVLDKDISAETLLALPELYKSGQNSECYNLSTFWISMV
DAFYQSLICFFIPYLAYKGSDIDVFTFGTPINTISLTTILLHQAMEMKTWTIFHGVVLLG
SFLMYFLVSLLYNATCVICNSPTNPYWVMEGQLSNPTFYLVCFLTPVVALLPRYFFLSLQ
GTCGKSLISKAQKIDKLPPDKRNLEIQSWRSRQRPAPVPEVARPTHHPVSSITGQDFSAS
TPKSSNPPKRKHVEESVLHEQRCGTECMRDDSCSGDSSAQLSSGEHLLGPNRIMAYSRGQ
TDMCRCSKRSSHRRSQSSLTI
|
| Enzyme 36 Number of Residues |
1461 |
| Enzyme 36 Molecular Weight |
165388.9 |
| Enzyme 36 Theoretical pI |
6.87 |
| Enzyme 36 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 36 General Function |
Involved in ATP binding |
| Enzyme 36 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
- 83-104
111-132
317-338
369-390
1112-1132
1145-1164
1195-1216
1224-1246
1253-1273
1292-1316
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
149944474  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
O94823  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
AT10B_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>4386 bp
ATGGCCCTCTCAGTGGACTCATCGTGGCATCGGTGGCAGTGGAGAGTCAGAGATGGCTTC
CCCCATTGTCCATCGGAAACCACACCGCTGCTCTCTCCAGAGAAAGGGAGACAGAGCTAC
AACTTGACACAGCAGCGGGTCGTGTTCCCCAACAACAGCATATTCCATCAAGATTGGGAA
GAGGTCTCCAGGAGATACCCTGGCAACAGAACCTGCACAACCAAATACACCCTCTTCACC
TTCCTGCCCCGGAATCTCTTTGAGCAATTTCATAGATGGGCTAACCTCTATTTCCTGTTC
CTGGTGATTTTGAACTGGATGCCCTCCATGGAAGTCTTCCACAGAGAAATCACCATGTTA
CCATTGGCCATTGTCCTGTTCGTCATCATGATCAAGGATGGCATGGAGGACTTCAAGAGA
CACCGCTTTGATAAAGCAATAAACTGCTCCAACATTCGAATTTATGAAAGAAAAGAGCAG
ACCTATGTGCAGAAGTGCTGGAAGGATGTGCGCGTGGGAGACTTCATCCAAATGAAATGC
AATGAGATTGTCCCAGCAGACATACTCCTCCTTTTTTCCTCTGACCCCAATGGGATATGC
CATCTGGAAACTGCCAGCTTGGATGGAGAGACAAACCTCAAGCAAAGATGTGTCGTGAAG
GGCTTCTCACAGCAGGAGGTACAGTTCGAACCAGAGCTTTTCCACAATACCATCGTGTGT
GAGAAACCCAACAACCACCTCAACAAATTTAAGGGTTATATGGAGCATCCTGACCAGACC
AGGACTGGCTTTGGCTGTGAGAGTCTTCTGCTTCGAGGCTGCACCATCAGAAACACCGAG
ATGGCTGTTGGCATTGTCATCTATGCAGGCCATGAGACGAAAGCCATGCTGAACAACAGT
GGCCCCCGGTACAAACGCAGCAAGATTGAGCGGCGCATGAATATAGACATCTTCTTCTGC
ATTGGGATCCTCATCCTCATGTGCCTTATTGGAGCTGTAGGTCACAGCATCTGGAATGGG
ACCTTTGAAGAACACCCTCCCTTCGATGTGCCAGATGCCAATGGCAGCTTCCTTCCCAGT
GCCCTTGGGGGCTTCTACATGTTCCTCACAATGATCATCCTGCTCCAGGTGCTGATCCCC
ATCTCTTTGTATGTCTCCATTGAGCTGGTGAAGCTCGGGCAAGTGTTCTTCTTGAGCAAT
GACCTTGACCTGTATGATGAAGAGACCGATTTATCCATTCAATGTCGAGCCCTCAACATC
GCAGAGGACTTGGGCCAGATCCAGTACATCTTCTCCGATAAGACGGGGACCCTGACAGAG
AACAAGATGGTGTTCCGACGTTGCACCATCATGGGCAGCGAGTATTCTCACCAAGAAAAT
GCTAAGCGACTGGAGACCCCAAAGGAGCTGGACTCAGATGGTGAAGAGTGGACCCAATAC
CAATGCCTGTCCTTCTCGGCTAGATGGGCCCAGGATCCAGCAACTATGAGAAGCCAAAAA
GGTGCTCAGCCTCTGAGGAGGAGCCAGAGTGCCCGGGTGCCCATCCAGGGCCACTACCGG
CAAAGGTCTATGGGGCACCGTGAAAGCTCACAGCCTCCTGTGGCCTTCAGCAGCTCCATA
GAAAAAGATGTAACTCCAGATAAAAACCTACTGACCAAGGTTCGAGATGCTGCCCTGTGG
TTGGAGACCTTGTCAGACAGCAGACCTGCCAAGGCTTCCCTCTCCACCACCTCCTCCATT
GCTGATTTCTTCCTTGCCTTAACCATCTGCAACTCTGTCATGGTGTCCACAACCACCGAG
CCCAGGCAGAGGGTCACCATCAAACCCTCAAGCAAGGCTCTGGGGACGTCCCTGGAGAAG
ATTCAGCAGCTCTTCCAGAAGTTGAAGCTATTGAGCCTCAGCCAGTCATTCTCATCCACT
GCACCCTCTGACACAGACCTCGGGGAGAGCTTAGGGGCCAACGTGGCCACCACAGACTCG
GATGAGAGAGATGATGCATCTGTGTGCAGTGGAGGTGACTCCACTGATGACGGTGGCTAC
AGGAGCAGCATGTGGGACCAGGGCGACATCCTGGAGTCTGGGTCAGGCACTTCCTTGGAG
GAGGCATTGGAGGCCCCAGCCACAGACCTGGCCAGGCCTGAGTTCTGTTACGAGGCTGAG
AGCCCTGATGAGGCCGCCCTGGTGCACGCTGCCCATGCCTACAGCTTCACACTAGTGTCC
CGGACACCTGAGCAGGTGACTGTGCGCCTGCCCCAGGGCACCTGCCTCACCTTCAGCCTC
CTCTGCACCCTGGGCTTTGACTCTGTCAGGAAGAGAATGTCTGTGGTTGTGAGGCACCCA
CTGACTGGCGAGATTGTTGTCTACACCAAGGGTGCTGACTCGGTCATCATGGACCTGCTG
GAAGACCCAGCCTGCGTACCTGACATTAATATGGAAAAGAAGCTGAGAAAAATCCGAGCC
CGGACCCAAAAGCATCTAGACTTGTATGCAAGAGATGGCCTGCGCACACTATGCATTGCC
AAGAAGGTTGTAAGCGAAGAGGACTTCCGGAGATGGGCCAGTTTCCGGCGTGAGGCTGAG
GCATCCCTCGACAACCGAGATGAGCTTCTCATGGAAACTGCACAGCATCTGGAGAATCAA
CTCACCTTACTTGGAGCCACTGGGATCGAAGACCGGCTGCAGGAAGGAGTTCCAGATACG
ATTGCCACTCTGCGGGAGGCTGGGATCCAGCTCTGGGTCCTGACTGGAGATAAGCAGGAG
ACAGCGGTCAACATTGCCCATTCCTGCAGACTGTTAAATCAGACCGACACTGTTTATACC
ATCAATACAGAGAATCAGGAGACCTGTGAATCCATCCTCAATTGTGCATTGGAAGAGCTA
AAGCAATTTCGTGAACTACAGAAGCCAGACCGCAAGCTCTTTGGATTCCGCTTACCTTCC
AAGACACCATCCATCACCTCAGAAGCTGTGGTTCCAGAAGCTGGATTGGTCATCGATGGG
AAGACATTGAATGCCATCTTCCAGGGAAAGCTAGAGAAGAAGTTTCTGGAATTGACCCAG
TATTGTCGGTCCGTCCTGTGCTGCCGCTCCACGCCACTCCAGAAGAGTATGATAGTCAAG
CTGGTGCGAGACAAGTTGCGCGTCATGACCCTTTCCATAGGTGATGGAGCAAATGATGTA
AGCATGATTCAAGCTGCTGATATTGGAATTGGAATATCTGGACAGGAAGGCATGCAGGCT
GTCATGTCCAGCGACTTTGCCATCACCCGCTTTAAGCATCTCAAGAAGTTGCTGCTCGTG
CATGGCCACTGGTGTTACTCGCGCCTGGCCAGGATGGTGGTGTACTACCTCTACAAGAAC
GTGTGCTACGTCAACCTGCTCTTCTGGTATCAGTTCTTCTGTGGTTTCTCCAGCTCCACC
ATGATTGATTACTGGCAGATGATATTCTTCAATCTCTTCTTTACCTCCTTGCCTCCTCTT
GTCTTTGGAGTCCTTGACAAAGACATCTCTGCAGAAACACTCCTGGCATTGCCTGAGCTA
TACAAGAGTGGCCAGAACTCTGAGTGCTATAACCTGTCGACTTTCTGGATTTCTATGGTG
GATGCATTCTACCAGAGCCTCATCTGTTTCTTTATCCCTTACCTGGCCTATAAGGGCTCT
GATATAGATGTCTTTACCTTTGGGACACCAATCAACACCATCTCCCTCACCACAATCCTT
TTGCACCAGGCAATGGAAATGAAGACATGGACCATTTTCCACGGAGTCGTGCTCCTCGGC
AGCTTCCTGATGTACTTTCTGGTATCCCTCCTGTACAATGCCACCTGCGTCATCTGCAAC
AGCCCCACCAATCCCTATTGGGTGATGGAAGGCCAGCTCTCAAACCCCACTTTCTACCTC
GTCTGCTTTCTCACACCAGTTGTTGCTCTTCTCCCAAGATACTTTTTCCTGTCTCTGCAA
GGAACTTGTGGGAAGTCTCTAATCTCAAAAGCTCAGAAAATTGACAAACTCCCCCCAGAC
AAAAGAAACCTGGAAATCCAGAGTTGGAGAAGCAGACAGAGGCCTGCCCCTGTCCCCGAA
GTGGCTCGACCAACTCACCACCCAGTGTCATCTATCACAGGACAGGACTTCAGTGCCAGC
ACCCCAAAGAGCTCTAACCCTCCCAAGAGGAAGCATGTGGAAGAGTCAGTACTCCACGAA
CAGAGATGTGGCACGGAGTGCATGAGGGATGACTCATGCTCAGGGGACTCCTCAGCTCAA
CTCTCATCCGGGGAGCACCTGCTGGGACCTAACAGGATAATGGCCTACTCAAGAGGACAG
ACTGATATGTGCCGGTGCTCAAAGAGGAGCAGCCATCGCCGATCCCAGAGTTCACTGACC
ATATGA
|
| Enzyme 36 GenBank Gene ID |
NM_025153.2  |
| Enzyme 36 GeneCard ID |
ATP10B  |
| Enzyme 36 GenAtlas ID |
ATP10B  |
| Enzyme 36 HGNC ID |
HGNC:13543  |
| Enzyme 36 Chromosome Location |
5 |
| Enzyme 36 Locus |
5q34 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Nagase T, Ishikawa K, Suyama M, Kikuno R, Miyajima N, Tanaka A, Kotani H, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1998 Oct 30;5(5):277-86. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Schmutz J, Martin J, Terry A, Couronne O, Grimwood J, Lowry S, Gordon LA, Scott D, Xie G, Huang W, Hellsten U, Tran-Gyamfi M, She X, Prabhakar S, Aerts A, Altherr M, Bajorek E, Black S, Branscomb E, Caoile C, Challacombe JF, Chan YM, Denys M, Detter JC, Escobar J, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Israni S, Jett J, Kadner K, Kimball H, Kobayashi A, Lopez F, Lou Y, Martinez D, Medina C, Morgan J, Nandkeshwar R, Noonan JP, Pitluck S, Pollard M, Predki P, Priest J, Ramirez L, Retterer J, Rodriguez A, Rogers S, Salamov A, Salazar A, Thayer N, Tice H, Tsai M, Ustaszewska A, Vo N, Wheeler J, Wu K, Yang J, Dickson M, Cheng JF, Eichler EE, Olsen A, Pennacchio LA, Rokhsar DS, Richardson P, Lucas SM, Myers RM, Rubin EM: The DNA sequence and comparative analysis of human chromosome 5. Nature. 2004 Sep 16;431(7006):268-74. [PubMed
]
|
| Enzyme 36 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
12920 |
| Enzyme 37 Name |
Probable phospholipid-transporting ATPase ID |
| Enzyme 37 Synonyms |
- ATPase class I type 8B member 2
|
| Enzyme 37 Gene Name |
ATP8B2 |
| Enzyme 37 Protein Sequence |
>Probable phospholipid-transporting ATPase ID
MTVPKEMPEKWARAQAPPSWSRKKPSWGTEEERRARANDREYNEKFQYASNCIKTSKYNI
LTFLPVNLFEQFQEVANTYFLFLLILQLIPQISSLSWFTTIVPLVLVLTITAVKDATDDY
FRHKSDNQVNNRQSQVLINGILQQEQWMNVCVGDIIKLENNQFVAADLLLLSSSEPHGLC
YIETAELDGETNMKVRQAIPVTSELGDISKLAKFDGEVICEPPNNKLDKFSGTLYWKENK
FPLSNQNMLLRGCVLRNTEWCFGLVIFAGPDTKLMQNSGRTKFKRTSIDRLMNTLVLWIF
GFLVCMGVILAIGNAIWEHEVGMRFQVYLPWDEAVDSAFFSGFLSFWSYIIILNTVVPIS
LYVSVEVIRLGHSYFINWDKKMFCMKKRTPAEARTTTLNEELGQVEYIFSDKTGTLTQNI
MVFNKCSINGHSYGDVFDVLGHKAELGERPEPVDFSFNPLADKKFLFWDPSLLEAVKIGD
PHTHEFFRLLSLCHTVMSEEKNEGELYYKAQSPDEGALVTAARNFGFVFRSRTPKTITVH
EMGTAITYQLLAILDFNNIRKRMSVIVRNPEGKIRLYCKGADTILLDRLHHSTQELLNTT
MDHLNEYAGEGLRTLVLAYKDLDEEYYEEWAERRLQASLAQDSREDRLASIYEEVENNMM
LLGATAIEDKLQQGVPETIALLTLANIKIWVLTGDKQETAVNIGYSCKMLTDDMTEVFIV
TGHTVLEVREELRKAREKMMDSSRSVGNGFTYQDKLSSSKLTSVLEAVAGEYALVINGHS
LAHALEADMELEFLETACACKAVICCRVTPLQKAQVVELVKKYKKAVTLAIGDGANDVSM
IKTAHIGVGISGQEGIQAVLASDYSFSQFKFLQRLLLVHGRWSYLRMCKFLCYFFYKNFA
FTMVHFWFGFFCGFSAQTVYDQYFITLYNIVYTSLPVLAMGVFDQDVPEQRSMEYPKLYE
PGQLNLLFNKREFFICIAQGIYTSVLMFFIPYGVFADATRDDGTQLADYQSFAVTVATSL
VIVVSVQIGLDTGYWTAINHFFIWGSLAVYFAILFAMHSNGLFDMFPNQFRFVGNAQNTL
AQPTVWLTIVLTTVVCIMPVVAFRFLRLNLKPDLSDTVRYTQLVRKKQKAQHRCMRRVGR
TGSRRSGYAFSHQEGFGELIMSGKNMRLSSLALSSFTTRSSSSWIESLRRKKSDSASSPS
GGADKPLKG
|
| Enzyme 37 Number of Residues |
1209 |
| Enzyme 37 Molecular Weight |
137439.1 |
| Enzyme 37 Theoretical pI |
6.99 |
| Enzyme 37 GO Classification |
| Function |
- ATP binding
- ATPase activity, coupled to transmembrane movement of ions
- ATPase activity, coupled to transmembrane movement of ions, phosphorylative mechanism
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, catalyzing transmembrane movement of substances
- ion binding
- ion transmembrane transporter activity
- lipid transporter activity
- magnesium ion binding
- metal ion binding
- nucleoside binding
- phospholipid transporter activity
- phospholipid-translocating ATPase activity
- purine nucleoside binding
- substrate-specific transmembrane transporter activity
- substrate-specific transporter activity
- transmembrane transporter activity
- transporter activity
|
| Process |
- ATP biosynthetic process
- cellular nitrogen compound metabolic process
- establishment of localization
- lipid transport
- metabolic process
- nitrogen compound metabolic process
- nucleobase, nucleoside and nucleotide metabolic process
- nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
- nucleoside phosphate metabolic process
- nucleotide metabolic process
- phospholipid transport
- purine nucleoside triphosphate biosynthetic process
- purine nucleotide biosynthetic process
- purine nucleotide metabolic process
- purine ribonucleoside triphosphate biosynthetic process
- transport
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane
- membrane part
|
|
| Enzyme 37 General Function |
Involved in ATP binding |
| Enzyme 37 Specific Function |
ATP + H(2)O + phospholipid(In) = ADP + phosphate + phospholipid(Out) |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
- 65-86
93-112
296-317
347-368
890-910
923-942
973-994
1009-1031
1038-1058
1079-1103
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
40316837  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
P98198  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
AT8B2_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>3672 bp
ATGGATACCTTGAGAGCTGTTCCCCTTTTTTCAATATCTGGCCTCTTCTCCTTTCCCTAC
AGGGTCTCCCATGGGATTGCTGGGATCTTGCTGGGTGAGATGGCAGTGTGTGCAAAAAAG
CGCCCCCCAGAAGAAGAAAGGAGGGCGCGGGCTAATGACCGAGAATACAATGAGAAATTC
CAGTATGCGAGTAACTGCATCAAGACCTCCAAGTACAATATTCTCACCTTCCTGCCTGTC
AACCTCTTTGAGCAGTTCCAGGAAGTTGCCAACACTTACTTCCTGTTCCTCCTCATTCTG
CAGTTGATCCCCCAGATCTCTTCCCTGTCCTGGTTCACCACCATTGTGCCTTTGGTTCTT
GTCCTCACCATCACAGCTGTTAAAGATGCCACTGATGACTATTTCCGCCACAAGAGCGAT
AACCAGGTGAATAACCGCCAGTCTCAGGTGCTGATCAATGGAATCCTCCAGCAGGAGCAG
TGGATGAATGTCTGTGTTGGTGATATTATCAAGCTAGAAAATAACCAGTTTGTGGCGGCG
GATCTCCTCCTCCTTTCCAGCAGTGAGCCCCATGGGCTGTGTTACATAGAGACAGCAGAA
CTTGATGGCGAGACCAACATGAAAGTACGTCAGGCGATTCCAGTCACCTCAGAATTGGGA
GACATCAGTAAGCTTGCCAAGTTTGACGGTGAAGTGATCTGTGAACCTCCCAACAACAAA
CTGGACAAATTCAGCGGAACCCTCTACTGGAAGGAAAATAAGTTCCCTCTGAGCAACCAG
AACATGCTGCTGCGGGGCTGTGTGCTGCGAAACACCGAGTGGTGCTTCGGGCTGGTCATC
TTTGCAGGTCCCGACACTAAGCTGATGCAAAACAGCGGCAGAACAAAGTTCAAAAGAACG
AGTATCGATCGCCTAATGAATACCCTGGTGCTCTGGATTTTTGGATTCCTGGTTTGCATG
GGGGTGATCCTGGCCATTGGCAATGCCATCTGGGAGCACGAGGTGGGGATGCGTTTCCAG
GTCTACCTGCCGTGGGATGAGGCAGTGGACAGTGCCTTCTTCTCTGGCTTCCTCTCCTTC
TGGTCCTACATCATCATCCTCAACACCGTTGTGCCCATTTCACTCTATGTCAGTGTGGAG
GTCATCCGTCTGGGCCACAGCTACTTCATCAACTGGGATAAGAAGATGTTCTGCATGAAG
AAGCGGACGCCTGCAGAAGCCCGCACCACCACCCTAAACGAGGAGCTGGGCCAGGTGGAG
TACATCTTCTCCGACAAGACGGGCACCCTCACCCAGAACATCATGGTTTTCAACAAGTGC
TCCATCAATGGCCACAGCTATGGTGATGTGTTTGACGTCCTGGGACACAAAGCTGAATTG
GGAGAGAGGCCTGAACCTGTTGACTTCTCCTTCAATCCTCTGGCTGACAAGAAGTTCTTA
TTTTGGGACCCCAGCCTGCTGGAGGCTGTCAAGATCGGGGACCCCCACACGCATGAGTTC
TTCCGCCTCCTTTCCCTGTGTCATACTGTCATGTCAGAAGAAAAGAACGAAGGAGAGCTG
TACTACAAAGCTCAGTCCCCAGATGAGGGGGCCCTGGTCACCGCAGCCAGGAACTTTGGT
TTTGTTTTCCGCTCTCGCACCCCCAAAACAATCACCGTCCATGAGATGGGCACAGCCATC
ACCTACCAGCTGCTGGCCATCCTGGACTTCAACAACATCCGCAAGCGGATGTCGGTCATA
GTGCGGAATCCAGAGGGGAAGATCCGACTCTACTGCAAAGGGGCTGACACTATCCTACTG
GACAGACTGCACCACTCCACTCAAGAGCTGCTCAACACCACCATGGACCACCTTAATGAG
TACGCAGGGGAAGGGCTGAGGACCCTGGTGCTGGCCTACAAGGATCTGGATGAAGAGTAC
TACGAGGAGTGGGCTGAGCGACGCCTCCAGGCCAGCCTGGCCCAGGACAGCCGGGAGGAC
AGGCTGGCTAGCATCTATGAGGAGGTTGAGAACAACATGATGCTGCTGGGTGCAACGGCC
ATTGAGGACAAACTTCAGCAAGGGGTTCCAGAGACCATTGCCCTCCTGACACTGGCCAAC
ATCAAGATTTGGGTGCTAACCGGAGACAAGCAAGAGACGGCTGTGAACATCGGCTATTCC
TGCAAGATGCTGACGGATGACATGACTGAGGTTTTCATAGTCACTGGCCATACTGTCCTG
GAGGTGCGGGAGGAGCTCAGGAAAGCCCGGGAGAAGATGATGGACTCATCCCGCTCCGTA
GGCAACGGCTTCACCTATCAGGACAAGCTTTCTTCTTCCAAGCTAACTTCTGTCCTGGAG
GCCGTTGCTGGGGAGTACGCCCTGGTCATAAATGGTCACAGCCTGGCCCACGCACTGGAG
GCAGACATGGAGCTGGAGTTTCTGGAGACAGCGTGTGCCTGCAAAGCTGTCATCTGCTGC
CGGGTGACCCCCTTGCAGAAGGCACAGGTGGTAGAACTGGTCAAGAAGTACAAGAAGGCT
GTGACGCTTGCCATTGGAGACGGAGCCAATGATGTCAGCATGATCAAAACGGCTCACATT
GGTGTGGGGATCAGTGGGCAGGAAGGGATCCAGGCTGTCTTGGCCTCCGATTACTCCTTC
TCCCAGTTCAAGTTCCTGCAGCGCCTCCTGCTGGTGCATGGGCGCTGGTCCTACCTGCGA
ATGTGCAAGTTTCTTTGCTATTTCTTCTACAAAAACTTTGCTTTCACCATGGTCCACTTC
TGGTTTGGCTTCTTCTGTGGCTTCTCAGCCCAGACCGTCTATGACCAGTATTTCATCACC
CTGTATAACATCGTGTACACCTCCCTGCCAGTCCTGGCTATGGGGGTCTTTGATCAGGAT
GTCCCCGAGCAGCGGAGCATGGAGTACCCTAAGCTGTATGAGCCGGGCCAGCTGAACCTT
CTCTTCAACAAGCGGGAGTTCTTCATCTGCATCGCCCAGGGCATCTACACCTCCGTGCTC
ATGTTCTTCATTCCCTATGGGGTGTTTGCTGATGCCACCCGGGATGATGGCACTCAGCTG
GCTGACTACCAGTCCTTTGCAGTCACTGTGGCCACATCCTTGGTCATTGTGGTTAGCGTG
CAGATTGGGCTCGACACAGGCTACTGGACGGCCATCAACCACTTCTTCATCTGGGGAAGC
CTTGCTGTTTACTTTGCCATCCTCTTTGCCATGCACAGCAATGGGCTCTTCGACATGTTT
CCCAACCAGTTCCGGTTTGTGGGGAATGCCCAGAACACCTTGGCCCAGCCCACGGTGTGG
CTGACCATTGTGCTCACCACAGTCGTCTGCATCATGCCCGTGGTTGCCTTCCGATTCCTC
AGGCTCAACCTGAAGCCGGATCTCTCCGACACGGTCCGCTACACACAGCTCGTGAGGAAG
AAGCAGAAGGCCCAGCACCGCTGCATGCGGCGGGTTGGCCGCACTGGCTCCCGGCGCTCC
GGCTATGCCTTCTCCCATCAGGAGGGCTTCGGGGAGCTCATCATGTCTGGCAAGAACATG
CGGCTGAGCTCTCTCGCGCTCTCCAGCTTCACCACCCGCTCCAGCTCCAGCTGGATTGAG
AGCCTGCGCAGGAAGAAGAGTGACAGTGCCAGTAGCCCCAGTGGCGGTGCCGACAAGCCC
CTCAAGGGCTGA
|
| Enzyme 37 GenBank Gene ID |
Not Available |
| Enzyme 37 GeneCard ID |
ATP8B2  |
| Enzyme 37 GenAtlas ID |
ATP8B2  |
| Enzyme 37 HGNC ID |
HGNC:13534  |
| Enzyme 37 Chromosome Location |
1 |
| Enzyme 37 Locus |
1q21.3 |
| Enzyme 37 SNPs |
SNPJam Report  |
| Enzyme 37 General References |
- Harris MJ, Arias IM: FIC1, a P-type ATPase linked to cholestatic liver disease, has homologues (ATP8B2 and ATP8B3) expressed throughout the body. Biochim Biophys Acta. 2003 Jul 21;1633(2):127-31. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hirosawa M, Nagase T, Ishikawa K, Kikuno R, Nomura N, Ohara O: Characterization of cDNA clones selected by the GeneMark analysis from size-fractionated cDNA libraries from human brain. DNA Res. 1999 Oct 29;6(5):329-36. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
|
| Enzyme 37 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
12924 |
| Enzyme 38 Name |
Abhydrolase domain-containing protein 4 |
| Enzyme 38 Synonyms |
- Alpha/beta-hydrolase 4
- Lyso-N-acylphosphatidylethanolamine lipase
|
| Enzyme 38 Gene Name |
ABHD4 |
| Enzyme 38 Protein Sequence |
>Abhydrolase domain-containing protein 4
MADDLEQQSQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVT
VSPEQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGA
EDEFVTSIETWRETMGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTN
PSEIRAPPAWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFEDDTISE
YIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGSDTWIDTSTGKK
VKMQRPDSYVRDMEIKGASHHVYADQPHIFNAVVEEICDSVD
|
| Enzyme 38 Number of Residues |
342 |
| Enzyme 38 Molecular Weight |
38794.1 |
| Enzyme 38 Theoretical pI |
7.69 |
| Enzyme 38 GO Classification |
Not Available |
| Enzyme 38 General Function |
Involved in hydrolase activity |
| Enzyme 38 Specific Function |
Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
Not Available |
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
10434528  |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q8TB40  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
ABHD4_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
>1029 bp
ATGGCCGATGATCTGGAGCAGCAGTCTCAAGGCTGGCTGAGTAGCTGGCTGCCCACGTGG
CGCCCCACTTCCATGTCTCAGCTGAAGAATGTGGAAGCCAGGATCCTCCAGTGTCTCCAG
AATAAGTTCCTGGCCAGATATGTATCCCTCCCAAACCAGAATAAGATCTGGACGGTGACT
GTGAGCCCCGAGCAAAACGACCGCACCCCCTTGGTGATGGTGCATGGTTTTGGGGGCGGC
GTGGGTCTCTGGATCCTCAACATGGACTCACTGAGTGCCCGCCGCACACTGCACACCTTC
GATCTGCTTGGCTTCGGGCGAAGCTCAAGGCCAGCATTCCCAAGGGACCCGGAGGGGGCT
GAGGATGAGTTTGTGACATCGATAGAGACATGGCGGGAGACCATGGGGATCCCCAGCATG
ATCCTCCTGGGGCACAGTTTGGGAGGATTCCTGGCCACTTCTTACTCAATCAAGTACCCT
GATAGAGTTAAACACCTCATCCTGGTGGACCCATGGGGCTTTCCCCTCCGACCAACTAAC
CCCAGTGGGATCTGTGCACCCCCAGCCTGGGTCAAAGCCGTGGCATCTGTCCTAGGACGT
TCCAATCCATTGGCTGTTCTTCGAGTAGCTGGGCCCTGGGGGCCTGGTCTGGTGCAGCGA
TTCCGGCCGGACTTCAAACGCAAGTTTGCAGACTTCTTTGAAGATGATACCATATCAGAG
TATATTTACCACTGCAACGCACAGAATCCCAGTGGTGAGACAGCATTCAAAGCCATGATG
GAGTCCTTTGGCTGGGCCCGGCGCCCTATGCTGGAGCGAATTCACTTGATTCGAAAAGAT
GTGCCTATCACTATGATCTACGGGTCCGACACCTGGATAGATACCAGTACGGGAAAAAAG
GTGAAGATGCAGCGGCCGGATTCCTATGTCCGAGACATGGAGATTAAGGGTGCCTCCCAC
CATGTCTATGCTGACCAGCCACACATCTTCAATGCTGTGGTGGAGGAGATCTGCGACTCA
GTTGATTGA
|
| Enzyme 38 GenBank Gene ID |
AK022878  |
| Enzyme 38 GeneCard ID |
ABHD4  |
| Enzyme 38 GenAtlas ID |
ABHD4  |
| Enzyme 38 HGNC ID |
HGNC:20154  |
| Enzyme 38 Chromosome Location |
1 |
| Enzyme 38 Locus |
14q11.2 |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 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 38 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
12925 |
| Enzyme 39 Name |
N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D |
| Enzyme 39 Synonyms |
- N-acyl phosphatidylethanolamine phospholipase D
- NAPE-PLD
- NAPE-hydrolyzing phospholipase D
|
| Enzyme 39 Gene Name |
NAPEPLD |
| Enzyme 39 Protein Sequence |
>N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
MDENESNQSLMTSSQYPKEAVRKRQNSARNSGASDSSRFSRKSFKLDYRLEEDVTKSKKG
KDGRFVNPWPTWKNPSIPNVLRWLIMEKDHSSVPSSKEELDKELPVLKPYFITNPEEAGV
REAGLRVTWLGHATVMVEMDELIFLTDPIFSSRASPSQYMGPKRFRRSPCTISELPPIDA
VLISHNHYDHLDYNSVIALNERFGNELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPG
HDKVTFVFTPSQHWCKRTLMDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGP
FDLAAIPIGAYEPRWFMKYQHVDPEEAVRIHTDVQTKKSMAIHWGTFALANEHYLEPPVK
LNEALERYGLNAEDFFVLKHGESRYLNNDDENF
|
| Enzyme 39 Number of Residues |
393 |
| Enzyme 39 Molecular Weight |
45595.2 |
| Enzyme 39 Theoretical pI |
5.95 |
| Enzyme 39 GO Classification |
Not Available |
| Enzyme 39 General Function |
Involved in metal ion binding |
| Enzyme 39 Specific Function |
Hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce N-acylethanolamines (NAEs) and phosphatidic acid. Responsible for the generation of anandamide (N- arachidonoylethanolamine), the ligand of cannabinoid and vanilloid receptors |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
Not Available |
| Enzyme 39 Pfam Domain Function |
Not Available |
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
38524476  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q6IQ20  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
NAPEP_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1182 bp
ATGGATGAAAATGAAAGCAACCAGTCTCTGATGACAAGCAGCCAATATCCTAAAGAAGCA
GTAAGAAAACGTCAAAATTCAGCACGGAATTCCGGAGCAAGTGATTCTTCTAGGTTTTCT
AGGAAAAGCTTCAAACTGGATTATAGACTAGAAGAAGATGTAACTAAATCCAAGAAAGGA
AAAGATGGGAGATTTGTGAATCCGTGGCCAACATGGAAAAACCCCTCTATTCCAAATGTT
CTCAGATGGCTGATAATGGAGAAAGATCACAGCAGTGTTCCAAGTTCTAAAGAGGAACTA
GACAAAGAACTCCCAGTGCTTAAGCCATATTTTATCACTAACCCTGAAGAAGCTGGAGTG
AGGGAAGCTGGCTTAAGAGTCACATGGCTGGGACATGCCACGGTAATGGTGGAAATGGAT
GAGCTCATATTTCTCACGGATCCCATCTTTAGCTCTCGTGCTTCACCATCGCAGTACATG
GGTCCAAAGCGATTTCGTCGTTCCCCGTGCACAATAAGTGAACTCCCTCCAATAGATGCG
GTCCTTATCAGTCACAACCACTATGACCATCTGGACTACAATTCTGTCATTGCTTTGAAT
GAGCGATTTGGTAATGAGTTGAGATGGTTTGTGCCTTTGGGTCTCCTTGACTGGATGCAA
AAATGTGGCTGTGAGAATGTGATTGAGTTGGACTGGTGGGAGGAGAATTGTGTCCCCGGA
CATGATAAGGTCACTTTTGTCTTTACACCTTCCCAGCACTGGTGTAAAAGGACTCTAATG
GATGACAACAAGGTGCTATGGGGCAGCTGGTCTGTCTTGGGGCCTTGGAATCGATTTTTT
TTCGCAGGAGATACTGGTTATTGCCCTGCTTTTGAAGAGATAGGAAAAAGATTTGGACCT
TTTGACCTTGCAGCTATTCCCATCGGAGCTTATGAACCGAGGTGGTTTATGAAATACCAG
CATGTAGACCCAGAAGAAGCTGTAAGGATTCACACTGATGTCCAAACAAAGAAATCTATG
GCAATTCACTGGGGAACTTTTGCCTTAGCAAATGAGCATTACTTAGAGCCTCCAGTGAAG
CTGAATGAAGCTCTAGAGAGATACGGACTTAACGCTGAAGATTTTTTTGTCTTGAAGCAT
GGAGAATCAAGATACCTAAATAATGATGATGAAAACTTTTAA
|
| Enzyme 39 GenBank Gene ID |
AB112352  |
| Enzyme 39 GeneCard ID |
NAPEPLD  |
| Enzyme 39 GenAtlas ID |
NAPEPLD  |
| Enzyme 39 HGNC ID |
HGNC:21683  |
| Enzyme 39 Chromosome Location |
7 |
| Enzyme 39 Locus |
7q22.1 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Okamoto Y, Morishita J, Tsuboi K, Tonai T, Ueda N: Molecular characterization of a phospholipase D generating anandamide and its congeners. J Biol Chem. 2004 Feb 13;279(7):5298-305. Epub 2003 Nov 21. [PubMed
]
- Curtiss NP, Bonifas JM, Lauchle JO, Balkman JD, Kratz CP, Emerling BM, Green ED, Le Beau MM, Shannon KM: Isolation and analysis of candidate myeloid tumor suppressor genes from a commonly deleted segment of 7q22. Genomics. 2005 May;85(5):600-7. [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
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Wang J, Okamoto Y, Morishita J, Tsuboi K, Miyatake A, Ueda N: Functional analysis of the purified anandamide-generating phospholipase D as a member of the metallo-beta-lactamase family. J Biol Chem. 2006 May 5;281(18):12325-35. Epub 2006 Mar 9. [PubMed
]
|
| Enzyme 39 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
12926 |
| Enzyme 40 Name |
Phosphatidylethanolamine-binding protein 1 |
| Enzyme 40 Synonyms |
- PEBP-1
- HCNPpp
- Neuropolypeptide h3
- Prostatic-binding protein
- Raf kinase inhibitor protein
- RKIP
- Hippocampal cholinergic neurostimulating peptide
- HCNP
|
| Enzyme 40 Gene Name |
PEBP1 |
| Enzyme 40 Protein Sequence |
>Phosphatidylethanolamine-binding protein 1
MPVDLSKWSGPLSLQEVDEQPQHPLHVTYAGAAVDELGKVLTPTQVKNRPTSISWDGLDS
GKLYTLVLTDPDAPSRKDPKYREWHHFLVVNMKGNDISSGTVLSDYVGSGPPKGTGLHRY
VWLVYEQDRPLKCDEPILSNRSGDHRGKFKVASFRKKYELRAPVAGTCYQAEWDDYVPKL
YEQLSGK
|
| Enzyme 40 Number of Residues |
187 |
| Enzyme 40 Molecular Weight |
21056.6 |
| Enzyme 40 Theoretical pI |
7.65 |
| Enzyme 40 GO Classification |
Not Available |
| Enzyme 40 General Function |
Involved in ATP binding |
| Enzyme 40 Specific Function |
HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor |
| Enzyme 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 |
189065145  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
P30086  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
PEBP1_HUMAN  |
| Enzyme 40 PDB ID |
1BEH  |
| Enzyme 40 PDB File |
Show |
| Enzyme 40 3D Structure |
|
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>564 bp
ATGCCGGTGGACCTCAGCAAGTGGTCCGGGCCCTTGAGCCTGCAAGAAGTGGACGAGCAG
CCGCAGCACCCGCTGCATGTCACCTACGCCGGGGCGGCGGTGGACGAGCTGGGCAAAGTG
CTGACGCCCACCCAGGTTAAGAATAGACCCACCAGCATTTCGTGGGATGGTCTTGATTCA
GGGAAGCTCTACACCTTGGTCCTGACAGACCCGGATGCTCCCAGCAGGAAGGATCCCAAA
TACAGAGAATGGCATCATTTCCTGGTGGTCAACATGAAGGGCAATGACATCAGCAGTGGC
ACAGTCCTCTCCGATTATGTGGGCTCGGGGCCTCCCAAGGGCACAGGCCTCCACCGCTAT
GTCTGGCTGGTTTACGAGCAGGACAGGCCGCTAAAGTGTGACGAGCCCATCCTCAGCAAC
CGATCTGGAGACCACCGTGGCAAATTCAAGGTGGCGTCCTTCCGTAAAAAGTATGAGCTC
AGGGCCCCGGTGGCTGGCACGTGTTACCAGGCCGAGTGGGATGACTATGTGCCCAAACTG
TACGAGCAGCTGTCTGGGAAGTAG
|
| Enzyme 40 GenBank Gene ID |
AK311927  |
| Enzyme 40 GeneCard ID |
PEBP1  |
| Enzyme 40 GenAtlas ID |
PEBP1  |
| Enzyme 40 HGNC ID |
HGNC:8630  |
| Enzyme 40 Chromosome Location |
1 |
| Enzyme 40 Locus |
12q24.23 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 General References |
- Hori N, Chae KS, Murakawa K, Matoba R, Fukushima A, Okubo K, Matsubara K: A human cDNA sequence homologue of bovine phosphatidylethanolamine-binding protein. Gene. 1994 Mar 25;140(2):293-4. [PubMed
]
- Tohdoh N, Tojo S, Agui H, Ojika K: Sequence homology of rat and human HCNP precursor proteins, bovine phosphatidylethanolamine-binding protein and rat 23-kDa protein associated with the opioid-binding protein. Brain Res Mol Brain Res. 1995 Jun;30(2):381-4. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Hochstrasser DF, Frutiger S, Paquet N, Bairoch A, Ravier F, Pasquali C, Sanchez JC, Tissot JD, Bjellqvist B, Vargas R, et al.: Human liver protein map: a reference database established by microsequencing and gel comparison. Electrophoresis. 1992 Dec;13(12):992-1001. [PubMed
]
- Seddiqi N, Bollengier F, Alliel PM, Perin JP, Bonnet F, Bucquoy S, Jolles P, Schoentgen F: Amino acid sequence of the Homo sapiens brain 21-23-kDa protein (neuropolypeptide h3), comparison with its counterparts from Rattus norvegicus and Bos taurus species, and expression of its mRNA in different tissues. J Mol Evol. 1994 Dec;39(6):655-60. [PubMed
]
- Ojika K, Mitake S, Tohdoh N, Appel SH, Otsuka Y, Katada E, Matsukawa N: Hippocampal cholinergic neurostimulating peptides (HCNP). Prog Neurobiol. 2000 Jan;60(1):37-83. [PubMed
]
- Yeung K, Seitz T, Li S, Janosch P, McFerran B, Kaiser C, Fee F, Katsanakis KD, Rose DW, Mischak H, Sedivy JM, Kolch W: Suppression of Raf-1 kinase activity and MAP kinase signalling by RKIP. Nature. 1999 Sep 9;401(6749):173-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Banfield MJ, Barker JJ, Perry AC, Brady RL: Function from structure? The crystal structure of human phosphatidylethanolamine-binding protein suggests a role in membrane signal transduction. Structure. 1998 Oct 15;6(10):1245-54. [PubMed
]
|
| Enzyme 40 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
12927 |
| Enzyme 41 Name |
Phosphatidylethanolamine-binding protein 4 |
| Enzyme 41 Synonyms |
- PEBP-4
- hPEBP4
- Protein cousin-of-RKIP 1
|
| Enzyme 41 Gene Name |
PEBP4 |
| Enzyme 41 Protein Sequence |
>Phosphatidylethanolamine-binding protein 4
MGWTMRLVTAALLLGLMMVVTGDEDENSPCAHEALLDEDTLFCQGLEVFYPELGNIGCKV
VPDCNNYRQKITSWMEPIVKFPGAVDGATYILVMVDPDAPSRAEPRQRFWRHWLVTDIKG
ADLKKGKIQGQELSAYQAPSPPAHSGFHRYQFFVYLQEGKVISLLPKENKTRGSWKMDRF
LNRFHLGEPEASTQFMTQNYQDSPTLQAPRERASEPKHKNQAEIAAC
|
| Enzyme 41 Number of Residues |
227 |
| Enzyme 41 Molecular Weight |
25733.2 |
| Enzyme 41 Theoretical pI |
6.51 |
| Enzyme 41 GO Classification |
Not Available |
| Enzyme 41 General Function |
Not Available |
| Enzyme 41 Specific Function |
Seems to promote cellular resistance to TNF-induced apoptosis by inhibiting activation of the Raf-1/MEK/ERK pathway, JNK and phosphatidylethanolamine externalization |
| Enzyme 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 |
14585855  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
Q96S96  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
PEBP4_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
>684 bp
ATGGGTTGGACAATGAGGCTGGTCACAGCAGCACTGTTACTGGGTCTCATGATGGTGGTC
ACTGGAGACGAGGATGAGAACAGCCCGTGTGCCCATGAGGCCCTCTTGGACGAGGACACC
CTCTTTTGCCAGGGCCTTGAAGTTTTCTACCCAGAGTTGGGGAACATTGGCTGCAAGGTT
GTTCCTGATTGTAACAACTACAGACAGAAGATCACCTCCTGGATGGAGCCGATAGTCAAG
TTCCCGGGGGCCGTGGACGGCGCAACCTATATCCTGGTGATGGTGGATCCAGATGCCCCT
AGCAGAGCAGAACCCAGACAGAGATTCTGGAGACATTGGCTGGTAACAGATATCAAGGGC
GCCGACCTGAAGGAAGGGAAGATTCAGGGCCAGGAGTTATCAGCCTACCAGGCTCCCTCC
CCACCGGCACACAGTGGCTTCCATCGCTACCAGTTCTTTGTCTATCTTCAGGAAGGAAAA
GTCATCTCTCTCCTTCCCAAGGAAAACAAAACTCGAGGCTCTTGGAAAATGGACAGATTT
CTGAACCGTTTCCACCTGGGCGAACCTGAAGCAAGCACCCAGTTCATGACCCAGAACTAC
CAGGACTCACCAACCCTCCAGGCTCCCAGAGAAAGGGCCAGCGAGCCCAAGCACAAAAAC
CAGGCGGAGATAGCTGCCTGCTAG
|
| Enzyme 41 GenBank Gene ID |
AY037148  |
| Enzyme 41 GeneCard ID |
PEBP4  |
| Enzyme 41 GenAtlas ID |
PEBP4  |
| Enzyme 41 HGNC ID |
HGNC:28319  |
| Enzyme 41 Chromosome Location |
8 |
| Enzyme 41 Locus |
8p21.3 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Wang X, Li N, Liu B, Sun H, Chen T, Li H, Qiu J, Zhang L, Wan T, Cao X: A novel human phosphatidylethanolamine-binding protein resists tumor necrosis factor alpha-induced apoptosis by inhibiting mitogen-activated protein kinase pathway activation and phosphatidylethanolamine externalization. J Biol Chem. 2004 Oct 29;279(44):45855-64. Epub 2004 Aug 9. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Zhang Z, Henzel WJ: Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci. 2004 Oct;13(10):2819-24. Epub 2004 Aug 31. [PubMed
]
|
| Enzyme 41 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
12928 |
| Enzyme 42 Name |
Ethanolaminephosphotransferase 1 |
| Enzyme 42 Synonyms |
- hEPT1
- Selenoprotein I
- SelI
|
| Enzyme 42 Gene Name |
EPT1 |
| Enzyme 42 Protein Sequence |
>Ethanolaminephosphotransferase 1
MAGYEYVSPEQLAGFDKYKYSAVDTNPLSLYVMHPFWNTIVKVFPTWLAPNLITFSGFLL
VVFNFLLMAYFDPDFYASAPGHKHVPDWVWIVVGILNFVAYTLDGVDGKQARRTNSSTPL
GELFDHGLDSWSCVYFVVTVYSIFGRGSTGVSVFVLYLLLWVVLFSFILSHWEKYNTGIL
FLPWGYDISQVTISFVYIVTAVVGVEAWYEPFLFNFLYRDLFTAMIIGCALCVTLPMSLL
NFFRSYKNNTLKLNSVYEAMVPLFSPCLLFILSTAWILWSPSDILELHPRVFYFMVGTAF
ANSTCQLIVCQMSSTRCPTLNWLLVPLFLVVLVVNLGVASYVESILLYTLTTAFTLAHIH
YGVRVVKQLSSHFQIYPFSLRKPNSDULGMEEKNIGL
|
| Enzyme 42 Number of Residues |
397 |
| Enzyme 42 Molecular Weight |
45228.4 |
| Enzyme 42 Theoretical pI |
6.59 |
| Enzyme 42 GO Classification |
| Function |
- catalytic activity
- phosphotransferase activity, for other substituted phosphate groups
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
|
|
| Enzyme 42 General Function |
Involved in phosphotransferase activity, for other substituted phosphate groups |
| Enzyme 42 Specific Function |
Catalyzes phosphatidylethanolamine biosynthesis from CDP-ethanolamine. It thereby plays a central role in the formation and maintenance of vesicular membranes. Involved in the formation of phosphatidylethanolamine via 'Kennedy' pathway |
| Enzyme 42 Pathways |
|
| Enzyme 42 Reactions |
- CDP-ethanolamine + 1,2-diacyl-sn-glycerol = CMP + a phosphatidylethanolamine [RN:R02057]
|
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
- 47-69
84-103
123-145
150-172
179-201
221-243
256-278
291-310
317-339
344-366
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
52078126  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
Q9C0D9  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
EPT1_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>1194 bp
ATGGCTGGCTACGAATACGTGAGCCCGGAGCAGCTGGCTGGCTTTGATAAGTACAAGTAC
AGTGCTGTGGATACCAATCCACTTTCTCTGTATGTCATGCATCCATTCTGGAACACTATA
GTAAAGGTATTTCCTACTTGGCTGGCGCCCAATCTGATAACTTTTTCTGGCTTTCTGCTG
GTCGTATTCAATTTTCTGCTAATGGCATACTTTGATCCTGACTTTTATGCCTCAGCACCA
GGTCACAAGCACGTGCCTGACTGGGTTTGGATTGTAGTGGGCATCCTCAACTTCGTAGCC
TACACTCTAGATGGTGTGGACGGAAAGCAAGCTCGCAGAACCAATTCTAGCACTCCCTTA
GGGGAGCTTTTTGATCATGGCCTGGATAGTTGGTCATGTGTTTACTTTGTTGTGACTGTT
TATTCCATCTTTGGAAGAGGATCAACTGGTGTCAGTGTTTTTGTTCTTTATCTCCTGCTA
TGGGTAGTTTTGTTTTCTTTCATCCTGTCCCACTGGGAAAAGTATAACACAGGGATTCTT
TTCCTGCCATGGGGATATGACATTAGCCAGGTGACTATTTCTTTTGTCTACATAGTGACT
GCAGTTGTGGGAGTTGAGGCCTGGTATGAACCTTTCCTGTTTAATTTCTTATATAGAGAC
CTATTCACTGCAATGATTATTGGTTGTGCATTATGTGTGACTCTTCCAATGAGTTTATTA
AACTTTTTCAGAAGCTATAAAAATAACACCTTGAAACTCAATTCAGTCTATGAAGCTATG
GTTCCCTTATTTTCTCCATGCTTGCTGTTCATTTTGTCTACAGCGTGGATCCTTTGGTCA
CCTTCAGATATTTTAGAGCTACATCCTAGAGTATTCTACTTTATGGTTGGAACAGCCTTT
GCCAACAGTACATGTCAGCTGATTGTTTGCCAAATGAGTAGTACCCGGTGTCCAACTTTG
AATTGGTTGCTGGTTCCTCTCTTCTTGGTTGTCTTAGTGGTAAACCTAGGAGTAGCCTCT
TACGTTGAGAGCATTCTCCTGTATACATTAACAACTGCTTTTACTCTGGCCCACATCCAT
TATGGAGTACGAGTGGTAAAGCAGCTGAGCAGCCATTTTCAGATTTACCCCTTCTCATTG
AGGAAACCAAACTCAGATTGACTAGGAATGGAAGAAAAGAATATTGGCCTGTAA
|
| Enzyme 42 GenBank Gene ID |
BK001426  |
| Enzyme 42 GeneCard ID |
EPT1  |
| Enzyme 42 GenAtlas ID |
EPT1  |
| Enzyme 42 HGNC ID |
HGNC:29361  |
| Enzyme 42 Chromosome Location |
2 |
| Enzyme 42 Locus |
2p23.3 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Kryukov GV, Castellano S, Novoselov SV, Lobanov AV, Zehtab O, Guigo R, Gladyshev VN: Characterization of mammalian selenoproteomes. Science. 2003 May 30;300(5624):1439-43. [PubMed
]
- Nagase T, Kikuno R, Hattori A, Kondo Y, Okumura K, Ohara O: Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Dec 31;7(6):347-55. [PubMed
]
- Horibata Y, Hirabayashi Y: Identification and characterization of human ethanolaminephosphotransferase1. J Lipid Res. 2007 Mar;48(3):503-8. Epub 2006 Nov 28. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
|
| Enzyme 42 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
13054 |
| Enzyme 43 Name |
Phosphatidylserine decarboxylase |
| Enzyme 43 Synonyms |
- SubName: Phosphatidylserine decarboxylase, isoform CRA_a
|
| Enzyme 43 Gene Name |
PISD |
| Enzyme 43 Protein Sequence |
>Phosphatidylserine decarboxylase
MMCQSEARQGPELRAAKWLHFPQLALRRRLGQLSCMSRPALKLRSWPLTVLYYLLPFGAL
RPLSRVGWRPVSRVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEA
AVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYS
LESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTV
SHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIYFD
RDLHTNSPRHSKGSYNDFSFVTHTNREGVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQL
KTGQKIRFGEALGSL
|
| Enzyme 43 Number of Residues |
375 |
| Enzyme 43 Molecular Weight |
43046.3 |
| Enzyme 43 Theoretical pI |
10.14 |
| Enzyme 43 GO Classification |
| Function |
- carbon-carbon lyase activity
- carboxy-lyase activity
- catalytic activity
- lyase activity
- phosphatidylserine decarboxylase activity
|
| Process |
- metabolic process
- organophosphate metabolic process
- phospholipid biosynthetic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 43 General Function |
Involved in phosphatidylserine decarboxylase activity |
| Enzyme 43 Specific Function |
Not Available |
| 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 |
5921491  |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
B1AKM7  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
B1AKM7_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
>1128 bp
ATGATGTGTCAGTCAGAGGCGCGGCAAGGACCAGAGCTCCGCGCGGCGAAATGGTTGCAC
TTCCCCCAGCTGGCCCTGAGGCGGAGGCTGGGGCAGCTGAGCTGCATGTCCAGACCCGCT
CTGAAACTGCGCTCCTGGCCCTTGACCGTCCTCTACTACCTCCTGCCCTTCGGCGCCCTC
AGACCGCTCAGCCGGGTGGGATGGAGGCCCGTAAGCAGGGTGGCTTTGTACAAGTCAGTG
CCAACGCGCTTGCTGTCACGGGCCTGGGGTCGCCTCAATCAGGTGGAGCTGCCACACTGG
CTGCGCAGGCCCGTCTACAGCCTGTACATCTGGACGTTTGGGGTGAACATGAAAGAGGCC
GCTGTGGAGGACCTGCATCACTACCGCAACCTCAGCGAGTTCTTCCGGCGCAAGCTGAAG
CCGCAGGCCCGGCCTGTCTGTGGCCTGCACAGCGTGATTAGCCCATCGGATGGAAGGATC
CTCAACTTTGGGCAGGTGAAGAACTGTGAGGTGGAGCAGGTAAAGGGGGTCACCTACTCC
CTGGAGTCGTTCCTGGGCCCGCGTATGTGCACAGAGGACCTGCCCTTCCCACCAGCCGCG
TCGTGTGACTCCTTCAAGAACCAGCTGGTCACCCGGGAAGGGAATGAGCTCTATCACTGT
GTCATCTACCTGGCCCCTGGGGACTACCACTGCTTCCACTCCCCCACCGACTGGACTGTG
TCCCACCGGCGCCACTTCCCAGGCTCCCTGATGTCAGTGAACCCTGGCATGGCTCGCTGG
ATCAAAGAGCTCTTCTGCCATAACGAGCGGGTGGTCCTGACGGGGGACTGGAAACATGGC
TTCTTCTCACTGACAGCTGTGGGGGCCACCAACGTGGGCTCCATTCGCATCTACTTTGAC
CGGGACCTGCACACAAACAGCCCAAGGCACAGCAAGGGCTCCTACAATGACTTCAGCTTC
GTGACGCACACCAATAGAGAGGGCGTCCCCATGCGTAAGGGCGAGCACCTGGGCGAGTTC
AACCTGGGCTCCACCATCGTGCTCATCTTCGAGGCCCCCAAGGACTTCAATTTCCAGCTG
AAAACAGGACAGAAAATCCGCTTTGGGGAAGCCCTGGGCTCGCTCTAG
|
| Enzyme 43 GenBank Gene ID |
AL096768  |
| Enzyme 43 GeneCard ID |
PISD  |
| Enzyme 43 GenAtlas ID |
PISD  |
| Enzyme 43 HGNC ID |
HGNC:8999  |
| Enzyme 43 Chromosome Location |
2 |
| Enzyme 43 Locus |
22q12.2 |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
Not Available |
| Enzyme 43 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
14866 |
| Enzyme 44 Name |
Cytosolic phospholipase A2 beta |
| Enzyme 44 Synonyms |
- cPLA2-beta
- Phospholipase A2 group IVB
|
| Enzyme 44 Gene Name |
PLA2G4B |
| Enzyme 44 Protein Sequence |
>Cytosolic phospholipase A2 beta
MAVAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVW
NQSFHFRIHRQLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEG
RLEVEFRLQSLADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGP
QEASVGTGTFRFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMR
VELKKEAGLRELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIM
ATGGGIRAMTSLYGQLAGLKELGLLDCVSYITGASGSTWALANLYEDPEWSQKDLAGPTE
LLKTQVTKNKLGVLAPSQLQRYRQELAERARLGYPSCFTNLWALINEALLHDEPHDHKLS
DQREALSHGQNPLPIYCALNTKGQSLTTFEFGEWCEFSPYEVGFPKYGAFIPSELFGSEF
FMGQLMKRLPESRICFLEGIWSNLYAANLQDSLYWASEPSQFWDRWVRNQANLDKEQVPL
LKIEEPPSTAGRIAEFFTDLLTWRPLAQATHNFLRGLHFHKDYFQHPHFSTWKATTLDGL
PNQLTPSEPHLCLLDVGYLINTSCLPLLQPTRDVDLILSLDYNLHGAFQQLQLLGRFCQE
QGIPFPPISPSPEEQLQPRECHTFSDPTCPGAPAVLHFPLVSDSFREYSAPGVRRTPEEA
AAGEVNLSSSDSPYHYTKVTYSQEDVDKLLHLTHYNVCNNQEQLLEALRQAVQRRRQRRP
H
|
| Enzyme 44 Number of Residues |
781 |
| Enzyme 44 Molecular Weight |
87977.0 |
| Enzyme 44 Theoretical pI |
5.85 |
| Enzyme 44 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 44 General Function |
Involved in metabolic process |
| Enzyme 44 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 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
- phosphatidylcholine + H2O = 1-acylglycerophosphocholine + a carboxylate [RN:R01313]
|
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
194387976  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
P0C869  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
PA24B_HUMAN  |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 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 44 GenBank Gene ID |
AK299419  |
| Enzyme 44 GeneCard ID |
PLA2G4B  |
| Enzyme 44 GenAtlas ID |
PLA2G4B  |
| Enzyme 44 HGNC ID |
HGNC:9036  |
| Enzyme 44 Chromosome Location |
1 |
| Enzyme 44 Locus |
15q11.2-q21.3 |
| Enzyme 44 SNPs |
SNPJam Report  |
| Enzyme 44 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 44 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
15207 |
| Enzyme 45 Name |
Phospholipase D1 variant |
| Enzyme 45 Synonyms |
Not Available |
| Enzyme 45 Gene Name |
Not Available |
| Enzyme 45 Protein Sequence |
>Phospholipase D1 variant
ANAQVLAAPSPCSPFAFTLSKVNMSLKNEPRVNTSALQKIAADMSNIIENLDTRELHFEG
EEVDYDVSPSDPKIQEVYIPFSAIYNTQGFKEPNIQTYLSGCPIKAQVLEVERFTSTTRV
PSINLYTIELTHGEFKWQVKRKFKHFQEFHRELLKYKAFIRIPIPTRRHTFRRQNVREEP
REMPSLPRSSENMIREEQFLGRRKQLEDYLTKILKMPMYRNYHATTEFLDISQLSFIHDL
GPKGIEGMIMKRSGGHRIPGLNCCGQGRACYRWSKRWLIVKDSFLLYMKPDSGAIAFVLL
VDKEFKIKVGKKETETKYGIRIDNLSRTLILKCNSYRHARWWGGAIEEFIQKHGTNFLKD
HRFGSYAAIQENALAKWYVNAKGYFEDVANAMEEANEEIFITDWWLSPEIFLKRPVVEGN
RWRLDCILKRKAQQGVRIFIMLYKEVELALGINSEYTKRTLMRLHPNIKVMRHPDHVSST
VYLWAHHEKLVIIDQSVAFVGGIDLAYGRWDDNEHRLTDVGSVKRVTSGPSLGSLPPAAM
ESMESLRLKDKNEPVQNLPIQKSIDDVDSKLKGIGKPRKFSKFSLYKQLHRHHLHDADSI
SSIDSTSNTGSIRSLQTGVGELHGETRFWHGKDYCNFVFKDWVQLDKPFADFIDRYSTPR
MPWHDIASAVHGKAARDVARHFIQRWNFTKIMKSKYRSLSYPFLLPKSQTTAHELRYQVP
GSVHANVQLLRSAADWSAGIKYHEESIHAAYVHVIENSRHYIYIENQFFISCADDKVVFN
KIGDAIAQRILKAHRENQKYRVYVVIPLLPGFEGDISTGGGNALQAIMHFNYRTMCRGEN
SILGQLKAELGNQWINYISFCGLRTHAELEGNLVTELIYVHSKLLIADDNTVIIGSANIN
DRSMLGKRDSEMAVIVQDTETVPSVMDGKEYQAGRFARGLRLQCFRVVLGYLDDPSEDIQ
DPVSDKFFKEVWVSTAARNATIYDKVFRCLPNDEVHNLIQLRDFINKPVLAKEDPIRAEE
ELKKIRGFLVQFPFYFLSEESLLPSVGTKEAIVPMEVWT
|
| Enzyme 45 Number of Residues |
1059 |
| Enzyme 45 Molecular Weight |
122007.8 |
| Enzyme 45 Theoretical pI |
9.03 |
| Enzyme 45 GO Classification |
| Function |
- binding
- catalytic activity
- lipid binding
- phosphoinositide binding
- phospholipid binding
- protein binding
|
| Process |
- cell communication
- cellular process
- metabolic process
|
| Component |
| — |
|
| Enzyme 45 General Function |
Involved in protein binding |
| Enzyme 45 Specific Function |
Not Available |
| Enzyme 45 Pathways |
Not Available |
| Enzyme 45 Reactions |
Not Available |
| Enzyme 45 Pfam Domain Function |
|
| Enzyme 45 Signals |
|
| Enzyme 45 Transmembrane Regions |
|
| Enzyme 45 Essentiality |
Not Available |
| Enzyme 45 GenBank ID Protein |
62089400  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
Q59EA4  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
Q59EA4_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>3182 bp
CCGCCAACGCGCAGGTGCTAGCGGCCCCTTCGCCCTGCAGCCCCTTTGCTTTTACTCTGT
CCAAAGTTAACATGTCACTGAAAAACGAGCCACGGGTAAATACCTCTGCACTGCAGAAAA
TTGCTGCTGACATGAGTAATATCATAGAAAATCTGGACACGCGGGAACTCCACTTTGAGG
GAGAGGAGGTAGACTACGACGTGTCTCCCAGCGATCCCAAGATACAAGAAGTGTATATCC
CTTTCTCTGCTATTTATAACACTCAAGGATTTAAGGAGCCTAATATACAGACGTATCTCT
CCGGCTGTCCAATAAAAGCACAAGTTCTGGAAGTGGAACGCTTCACATCTACAACAAGGG
TACCAAGTATTAATCTTTACACTATTGAATTAACACATGGGGAATTTAAATGGCAAGTTA
AGAGGAAATTCAAGCATTTTCAAGAATTTCACAGAGAGCTGCTCAAGTACAAAGCCTTTA
TCCGCATCCCCATTCCCACTAGAAGACACACGTTTAGGAGGCAAAACGTCAGAGAGGAGC
CTCGAGAGATGCCCAGTTTGCCCCGTTCATCTGAAAACATGATAAGAGAAGAACAATTCC
TTGGTAGAAGAAAACAACTGGAAGATTACTTGACAAAGATACTAAAAATGCCCATGTATA
GAAACTATCATGCCACAACAGAGTTTCTTGATATAAGCCAGCTGTCTTTCATCCATGATT
TGGGACCAAAGGGCATAGAAGGTATGATAATGAAAAGATCTGGAGGACACAGAATACCAG
GCTTGAATTGCTGTGGTCAGGGAAGAGCCTGCTACAGATGGTCAAAAAGATGGTTAATAG
TGAAAGATTCCTTTTTATTGTATATGAAACCAGACAGCGGTGCCATTGCCTTCGTCCTGC
TGGTAGACAAAGAATTCAAAATTAAGGTGGGGAAGAAGGAGACAGAAACGAAATATGGAA
TCCGAATTGATAATCTTTCAAGGACACTTATTTTAAAATGCAACAGCTATAGACATGCTC
GGTGGTGGGGAGGGGCTATAGAAGAATTCATCCAGAAACATGGCACCAACTTTCTCAAAG
ATCATCGATTTGGGTCATATGCTGCTATCCAAGAGAATGCTTTAGCTAAATGGTATGTTA
ATGCCAAAGGATATTTTGAAGATGTGGCAAATGCAATGGAAGAGGCAAATGAAGAGATTT
TTATCACAGACTGGTGGCTGAGTCCAGAAATCTTCCTGAAACGCCCAGTGGTTGAGGGAA
ATCGTTGGAGGTTGGACTGCATTCTTAAACGAAAAGCACAACAAGGAGTGAGGATCTTCA
TAATGCTCTACAAAGAGGTGGAACTCGCTCTTGGCATCAATAGTGAATACACCAAGAGGA
CTTTGATGCGTCTACATCCCAACATAAAGGTGATGAGACACCCGGATCATGTGTCATCCA
CCGTCTATTTGTGGGCTCACCATGAGAAGCTTGTCATCATTGACCAATCGGTGGCCTTTG
TGGGAGGGATTGACCTGGCCTATGGAAGGTGGGACGACAATGAGCACAGACTCACAGACG
TGGGCAGTGTGAAGCGGGTCACTTCAGGACCGTCTCTGGGTTCCCTCCCACCTGCCGCAA
TGGAGTCTATGGAATCCTTAAGACTCAAAGATAAAAATGAGCCTGTTCAAAACCTACCCA
TCCAGAAGAGTATTGATGATGTGGATTCAAAACTGAAAGGAATAGGAAAGCCAAGAAAGT
TCTCCAAATTTAGTCTCTACAAGCAGCTCCACAGGCACCACCTGCACGACGCAGATAGCA
TCAGCAGCATTGACAGCACCTCCAATACCGGGTCCATCCGTAGTTTACAGACAGGTGTGG
GAGAGCTGCATGGGGAAACCAGATTCTGGCATGGAAAGGACTACTGCAATTTCGTCTTCA
AAGACTGGGTTCAACTTGATAAACCTTTTGCTGATTTCATTGACAGGTACTCCACGCCCC
GGATGCCCTGGCATGACATTGCCTCTGCAGTCCACGGGAAGGCGGCTCGTGATGTGGCAC
GTCACTTCATCCAGCGCTGGAACTTCACAAAAATTATGAAATCAAAATATCGGTCCCTTT
CTTATCCTTTTCTGCTTCCAAAGTCTCAAACAACAGCCCATGAGTTGAGATATCAAGTGC
CTGGGTCTGTCCATGCTAACGTACAGTTGCTCCGCTCTGCTGCTGATTGGTCTGCTGGTA
TAAAGTACCATGAAGAGTCCATCCACGCCGCTTACGTCCATGTGATAGAGAACAGCAGGC
ACTATATCTATATCGAAAACCAGTTTTTCATAAGCTGTGCTGATGACAAAGTTGTGTTCA
ACAAGATAGGCGATGCCATTGCCCAGAGGATCCTGAAAGCTCACAGGGAAAACCAGAAAT
ACCGGGTATATGTCGTGATACCACTTCTGCCAGGGTTCGAAGGAGACATTTCAACCGGCG
GAGGAAATGCTCTACAGGCAATCATGCACTTCAACTACAGAACCATGTGCAGAGGAGAAA
ATTCCATCCTTGGACAGTTAAAAGCAGAGCTTGGTAATCAGTGGATAAATTACATATCAT
TCTGTGGTCTTAGAACACATGCAGAGCTCGAAGGAAACCTAGTAACTGAGCTTATCTATG
TCCACAGCAAGTTGTTAATTGCTGATGATAACACTGTTATTATTGGCTCTGCCAACATAA
ATGACCGCAGCATGCTGGGAAAGCGTGACAGTGAAATGGCTGTCATTGTGCAAGATACAG
AGACTGTTCCTTCAGTAATGGATGGAAAAGAGTACCAAGCTGGCCGGTTTGCCCGAGGAC
TTCGGCTACAGTGCTTTAGGGTTGTCCTTGGCTATCTTGATGACCCAAGTGAGGACATTC
AGGATCCAGTGAGTGACAAATTCTTCAAGGAGGTGTGGGTTTCAACAGCAGCTCGAAATG
CTACAATTTATGACAAGGTTTTCCGGTGCCTTCCCAATGATGAAGTACACAATTTAATTC
AGCTGAGAGACTTTATAAACAAGCCCGTATTAGCTAAGGAAGATCCCATTCGAGCTGAGG
AGGAACTGAAGAAGATCCGTGGATTTTTGGTGCAATTCCCCTTTTATTTCTTGTCTGAAG
AAAGCCTACTGCCTTCTGTTGGGACCAAAGAGGCCATAGTGCCCATGGAGGTTTGGACTT
AA
|
| Enzyme 45 GenBank Gene ID |
AB209907  |
| Enzyme 45 GeneCard ID |
Not Available |
| Enzyme 45 GenAtlas ID |
Not Available |
| Enzyme 45 HGNC ID |
HGNC:9067  |
| Enzyme 45 Chromosome Location |
Not Available |
| Enzyme 45 Locus |
Not Available |
| Enzyme 45 SNPs |
Not Available |
| Enzyme 45 General References |
Not Available |
| Enzyme 45 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
15299 |
| Enzyme 46 Name |
cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a) |
| Enzyme 46 Synonyms |
Not Available |
| Enzyme 46 Gene Name |
PLA2G2A |
| Enzyme 46 Protein Sequence |
>cDNA FLJ75686, highly similar to Homo sapiens phospholipase A2, group IIA (platelets, synovial fluid) (PLA2G2A), mRNA (Phospholipase A2, group IIA (Platelets, synovial fluid), isoform CRA_a)
MKTLLLLAVIMIFGLLQAHGNLVNFHRMIKLTTGKEAALSYGFYGCHCGVGGRGSPKDAT
DRCCVTHDCCYKRLEKRGCGTKFLSYKFSNSGSRITCAKQDSCRSQLCECDKAAATCFAR
NKTTYNKKYQYYSNKHCRGSTPRC
|
| Enzyme 46 Number of Residues |
144 |
| Enzyme 46 Molecular Weight |
16083 |
| Enzyme 46 Theoretical pI |
9.51 |
| Enzyme 46 GO Classification |
Not Available |
| Enzyme 46 General Function |
Not Available |
| Enzyme 46 Specific Function |
Not Available |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
Not Available |
| Enzyme 46 Pfam Domain Function |
Not Available |
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
158256040  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
A8K5I7  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
A8K5I7_HUMAN  |
| Enzyme 46 PDB ID |
1DB4  |
| Enzyme 46 PDB File |
Show |
| Enzyme 46 3D Structure |
|
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>435 bp
ATGAAGACCCTCCTACTGTTGGCAGTGATCATGATCTTTGGCCTACTGCAGGCCCATGGG
AATTTGGTGAATTTCCACAGAATGATCAAGTTGACGACAGGAAAGGAAGCCGCACTCAGT
TATGGCTTCTACGGCTGCCACTGTGGCGTGGGTGGCAGAGGATCCCCCAAGGATGCAACG
GATCGCTGCTGTGTCACTCATGACTGTTGCTACAAACGTCTGGAGAAACGTGGATGTGGC
ACCAAATTTCTGAGCTACAAGTTTAGCAACTCGGGGAGCAGAATCACCTGTGCAAAACAG
GACTCCTGCAGAAGTCAACTGTGTGAGTGTGATAAGGCTGCTGCCACCTGTTTTGCTAGA
AACAAGACGACCTACAATAAAAAGTACCAGTACTATTCCAATAAACACTGCAGAGGGAGC
ACCCCTCGTTGCTGA
|
| Enzyme 46 GenBank Gene ID |
AK291302  |
| Enzyme 46 GeneCard ID |
A8K5I7  |
| Enzyme 46 GenAtlas ID |
Not Available |
| Enzyme 46 HGNC ID |
Not Available |
| Enzyme 46 Chromosome Location |
Not Available |
| Enzyme 46 Locus |
Not Available |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
Not Available |
| Enzyme 46 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
|
|
Enzyme 47
[top]
|
| Enzyme 47 ID |
16561 |
| Enzyme 47 Name |
Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a) |
| Enzyme 47 Synonyms |
Not Available |
| Enzyme 47 Gene Name |
PLA2G6 |
| Enzyme 47 Protein Sequence |
>Phospholipase A2, group VI (Cytosolic, calcium-independent) (Phospholipase A2, group VI (Cytosolic, calcium-independent), isoform CRA_a)
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLV
NPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSW
SVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMD
VTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLL
LCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMA
RMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSK
DNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRQLQDLMHISRARKPAFILGSMRDEK
RTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSM
AYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPA
ELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGG
LLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNP
WELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVS
DTVLVNALWETEVYIYEHREEFQKLIQLLLSP
|
| Enzyme 47 Number of Residues |
752 |
| Enzyme 47 Molecular Weight |
84094 |
| Enzyme 47 Theoretical pI |
7.24 |
| Enzyme 47 GO Classification |
| Function |
| — |
| Process |
- lipid metabolism
- metabolism
- physiological process
- primary metabolism
|
| Component |
| — |
|
| Enzyme 47 General Function |
Not Available |
| Enzyme 47 Specific Function |
Not Available |
| Enzyme 47 Pathways |
Not Available |
| Enzyme 47 Reactions |
Not Available |
| Enzyme 47 Pfam Domain Function |
|
| Enzyme 47 Signals |
|
| Enzyme 47 Transmembrane Regions |
|
| Enzyme 47 Essentiality |
Not Available |
| Enzyme 47 GenBank ID Protein |
Not Available |
| Enzyme 47 UniProtKB/Swiss-Prot ID |
B0QYE8  |
| Enzyme 47 UniProtKB/Swiss-Prot Entry Name |
B0QYE8_HUMAN  |
| Enzyme 47 PDB ID |
Not Available |
| Enzyme 47 Cellular Location |
Not Available |
| Enzyme 47 Gene Sequence |
Not Available |
| Enzyme 47 GenBank Gene ID |
AL022322  |
| Enzyme 47 GeneCard ID |
B0QYE8  |
| Enzyme 47 GenAtlas ID |
Not Available |
| Enzyme 47 HGNC ID |
Not Available |
| Enzyme 47 Chromosome Location |
22 |
| Enzyme 47 Locus |
22q13.1 |
| Enzyme 47 SNPs |
SNPJam Report  |
| Enzyme 47 General References |
Not Available |
| Enzyme 47 Metabolite References |
- Kurz M, Brachvogel V, Matter H, Stengelin S, Thuring H, Kramer W: Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures. Proteins. 2003 Feb 1;50(2):312-28. [PubMed
]
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