|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5292 |
| Enzyme 1 Name |
Group 10 secretory phospholipase A2 |
| Enzyme 1 Synonyms |
- Group X secretory phospholipase A2
- GX sPLA2
- sPLA2-X
- Phosphatidylcholine 2-acylhydrolase 10
|
| Enzyme 1 Gene Name |
PLA2G10 |
| Enzyme 1 Protein Sequence |
>Group 10 secretory phospholipase A2
MGPLPVCLPIMLLLLLPSLLLLLLLPGPGSGEASRILRVHRRGILELAGTVGCVGPRTPI
AYMKYGCFCGLGGHGQPRDAIDWCCHGHDCCYTRAEEAGCSPKTERYSWQCVNQSVLCGP
AENKCQELLCKCDQEIANCLAQTEYNLKYLFYPQFLCEPDSPKCD
|
| Enzyme 1 Number of Residues |
165 |
| Enzyme 1 Molecular Weight |
18153.0 |
| Enzyme 1 Theoretical pI |
6.46 |
| 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. Has a powerful potency for releasing arachidonic acid from cell membrane phospholipids. Prefers phosphatidylethanolamine and phosphatidylcholine liposomes to those of phosphatidylserine |
| 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 |
Not Available |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
O15496  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
PA2GX_HUMAN  |
| Enzyme 1 PDB ID |
1LE7  |
| Enzyme 1 PDB File |
Show |
| Enzyme 1 3D Structure |
|
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>498 bp
ATGGGGCCGCTACCTGTGTGCCTGCCAATCATGCTGCTCCTGCTACTGCCGTCGCTGCTG
CTGCTGCTGCTTCTACCTGGCCCCGGGTCCGGCGAGGCCTCCAGGATATTACGTGTGCAC
CGGCGTGGGATCCTGGAACTGGCAGGAACTGTGGGTTGTGTTGGTCCCCGAACCCCCATC
GCCTATATGAAATATGGTTGCTTTTGTGGCTTGGGAGGCCATGGCCAGCCCCGCGATGCC
ATTGACTGGTGCTGCCATGGCCACGACTGTTGTTACACTCGAGCTGAGGAGGCCGGCTGC
AGCCCCAAGACAGAGCGCTACTCCTGGCAGTGCGTCAATCAGAGCGTCCTGTGCGGACCG
GCAGAGAACAAATGCCAAGAACTGTTGTGCAAGTGTGACCAGGAGATTGCTAACTGCTTA
GCCCAAACTGAGTACAACTTAAAGTACCTCTTCTACCCCCAGTTCCTATGTGAGCCGGAC
TCGCCCAAGTGTGACTGA
|
| Enzyme 1 GenBank Gene ID |
U95301  |
| Enzyme 1 GeneCard ID |
PLA2G10  |
| Enzyme 1 GenAtlas ID |
PLA2G10  |
| Enzyme 1 HGNC ID |
HGNC:9029  |
| Enzyme 1 Chromosome Location |
1 |
| Enzyme 1 Locus |
16p13.1-p12 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 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 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5457 |
| Enzyme 2 Name |
Diacylglycerol kinase gamma |
| Enzyme 2 Synonyms |
- DAG kinase gamma
- Diglyceride kinase gamma
- DGK-gamma
|
| Enzyme 2 Gene Name |
DGKG |
| Enzyme 2 Protein Sequence |
>Diacylglycerol kinase gamma
MGEERWVSLTPEEFDQLQKYSEYSSKKIKDALTEFNEGGSLKQYDPHEPISYDVFKLFMR
AYLEVDLPQPLSTHLFLAFSQKPRHETSDHPTEGASNSEANSADTNIQNADNATKADEAC
APDTESNMAEKQAPAEDQVAATPLEPPVPRSSSSESPVVYLKDVVCYLSLLETGRPQDKL
EFMFRLYDSDENGLLDQAEMDCIVNQMLHIAQYLEWDPTELRPILKEMLQGMDYDRDGFV
SLQEWVHGGMTTIPLLVLLGMDDSGSKGDGRHAWTMKHFKKPTYCNFCHIMLMGVRKQGL
CCTYCKYTVHERCVSKNIPGCVKTYSKAKRSGEVMQHAWVEGNSSVKCDRCHKSIKCYQS
VTARHCVWCRMTFHRKCELSTLCDGGELRDHILLPTSICPITRDRPGEKSDGCVSAKGEL
VMQYKIIPTPGTHPLLVLVNPKSGGRQGERILRKFHYLLNPKQVFNLDNGGPTPGLNFFR
DTPDFRVLACGGDGTVGWILDCIDKANFAKHPPVAVLPLGTGNDLARCLRWGGGYEGGSL
TKILKDIEQSPLVMLDRWHLEVIPREEVENGDQVPYSIMNNYFSIGVDASIAHRFHVMRE
KHPEKFNSRMKNKLWYFEFGTSETFAATCKKLHDHIELECDGVGVDLSNIFLEGIAILNI
PSMYGGTNLWGENKKNRAVIRESRKGVTDPKELKFCVQDLSDQLLEVVGLEGAMEMGQIY
TGLKSAGRRLAQCASVTIRTNKLLPMQVDGEPWMQPCCTIKITHKNQAPMMMGPPQKSSF
FSLRRKSRSKD
|
| Enzyme 2 Number of Residues |
791 |
| Enzyme 2 Molecular Weight |
89095.3 |
| Enzyme 2 Theoretical pI |
6.80 |
| Enzyme 2 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- diacylglycerol kinase activity
- ion binding
- kinase activity
- metal ion binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 2 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 2 Specific Function |
Reverses the normal flow of glycerolipid biosynthesis by phosphorylating diacylglycerol back to phosphatidic acid |
| Enzyme 2 Pathways |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 2 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
124256476  |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P49619  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
DGKG_HUMAN  |
| Enzyme 2 PDB ID |
Not Available |
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>2376 bp
ATGGGTGAAGAACGGTGGGTCTCCCTCACTCCAGAAGAATTTGACCAACTCCAGAAATAT
TCAGAATATTCCTCCAAGAAGATAAAAGATGCCTTGACTGAATTTAATGAGGGTGGGAGC
CTCAAACAATATGACCCACATGAGCCGATTAGCTATGATGTCTTCAAGCTGTTCATGAGG
GCGTACCTGGAGGTGGACCTTCCCCAGCCACTGAGCACTCACCTCTTCCTGGCCTTCAGC
CAGAAGCCCAGACACGAGACCTCTGACCACCCGACGGAGGGAGCCAGCAACAGTGAGGCC
AACAGCGCAGATACTAATATACAGAATGCAGATAATGCCACCAAAGCAGACGAGGCCTGT
GCCCCTGATACTGAATCAAATATGGCTGAGAAGCAAGCACCAGCTGAAGACCAAGTGGCT
GCGACCCCCCTGGAACCCCCCGTCCCTCGGTCTTCAAGCTCGGAATCCCCAGTGGTATAC
CTGAAGGATGTTGTGTGCTACCTGTCCCTGCTGGAGACGGGGAGGCCTCAGGATAAGCTG
GAGTTCATGTTTCGCCTCTATGATTCAGATGAGAACGGTCTCCTGGACCAAGCGGAGATG
GATTGCATTGTCAACCAAATGCTGCATATTGCCCAGTACCTGGAGTGGGATCCCACAGAG
CTGAGGCCTATATTGAAGGAGATGCTGCAAGGGATGGACTACGACCGGGACGGCTTTGTG
TCTCTACAGGAATGGGTCCATGGAGGGATGACCACCATCCCATTGCTGGTCCTCCTGGGG
ATGGATGACTCTGGCTCCAAGGGGGATGGGCGGCACGCCTGGACCATGAAGCACTTCAAG
AAACCAACCTACTGCAACTTCTGCCATATCATGCTCATGGGCGTCCGCAAGCAAGGCCTG
TGCTGCACTTACTGTAAATACACTGTCCACGAACGCTGTGTGTCCAGAAACATTCCTGGT
TGTGTCAAAACGTACTCAAAAGCCAAAAGGAGTGGTGAGGTGATGCAGCACGCATGGGTG
GAAGGGAACTCCTCCGTCAAGTGTGACCGGTGCCACAAAAGTATCAAGTGCTACCAGAGT
GTCACCGCGCGGCACTGCGTGTGGTGCCGGATGACGTTTCACCGCAAATGTGAATTATCA
ACGTTGTGTGACGGTGGGGAACTCAGAGACCACATCTTACTGCCCACCTCCATATGCCCC
ATCACCCGGGACAGGCCAGGTGAGAAGTCTGATGGCTGCGTGTCCGCCAAGGGCGAACTT
GTCATGCAGTATAAGATCATCCCCACCCCGGGTACCCACCCCCTGCTGGTCTTGGTGAAC
CCCAAGAGTGGAGGGAGACAAGGAGAAAGAATTCTTCGGAAATTCCACTATCTGCTCAAC
CCCAAACAAGTTTTCAACCTGGACAATGGGGGGCCTACTCCAGGGTTGAACTTTTTCCGT
GATACTCCAGACTTCCGTGTTTTGGCCTGTGGTGGAGATGGGACAGTTGGCTGGATTTTG
GATTGCATTGATAAGGCCAACTTTGCAAAGCATCCACCAGTGGCTGTCCTGCCTCTTGGA
ACAGGAAATGACCTTGCCCGTTGTCTCCGCTGGGGAGGAGGTTATGAAGGGGGCAGCTTG
ACAAAAATCCTGAAAGACATTGAGCAGAGCCCCTTGGTGATGCTGGACCGCTGGCATCTG
GAAGTCATCCCCAGAGAGGAAGTGGAAAACGGGGACCAGGTCCCATACAGCATCATGAAC
AACTATTTCTCCATTGGTGTGGACGCTTCCATTGCACACAGATTCCATGTGATGAGAGAG
AAACATCCTGAAAAATTCAACAGCAGGATGAAGAACAAGCTGTGGTACTTTGAATTTGGC
ACCTCGGAGACTTTTGCAGCGACCTGCAAGAAACTCCACGACCACATTGAGTTGGAGTGT
GATGGGGTTGGGGTGGACCTGAGCAACATCTTCCTGGAAGGCATTGCCATTCTCAACATT
CCCAGCATGTACGGAGGCACCAATCTCTGGGGAGAAAACAAGAAGAACCGGGCTGTGATC
CGGGAAAGCAGGAAGGGTGTCACTGACCCCAAAGAACTGAAATTCTGCGTTCAAGACCTC
AGTGACCAGCTCCTTGAAGTGGTGGGGCTAGAAGGAGCCATGGAGATGGGGCAGATCTAC
ACCGGCCTGAAGAGTGCAGGCAGGAGGCTGGCCCAGTGCGCCTCTGTCACCATCAGGACA
AACAAGCTGCTGCCAATGCAAGTGGATGGAGAACCCTGGATGCAGCCATGTTGCACGATT
AAAATTACTCACAAGAACCAAGCGCCCATGATGATGGGGCCTCCCCAGAAGAGCAGCTTC
TTCTCGTTGAGAAGGAAGAGCCGTTCAAAAGACTAA
|
| Enzyme 2 GenBank Gene ID |
NM_001346.2  |
| Enzyme 2 GeneCard ID |
DGKG  |
| Enzyme 2 GenAtlas ID |
DGKG  |
| Enzyme 2 HGNC ID |
HGNC:2853  |
| Enzyme 2 Chromosome Location |
3 |
| Enzyme 2 Locus |
3q27.2-q27.3 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Kai M, Sakane F, Imai S, Wada I, Kanoh H: Molecular cloning of a diacylglycerol kinase isozyme predominantly expressed in human retina with a truncated and inactive enzyme expression in most other human cells. J Biol Chem. 1994 Jul 15;269(28):18492-8. [PubMed
]
- Stohr H, Klein J, Gehrig A, Koehler MR, Jurklies B, Kellner U, Leo-Kottler B, Schmid M, Weber BH: Mapping and genomic characterization of the gene encoding diacylglycerol kinase gamma (DAGK3): assessment of its role in dominant optic atrophy (OPA1). Hum Genet. 1999 Jan;104(1):99-105. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA: The DNA sequence, annotation and analysis of human chromosome 3. Nature. 2006 Apr 27;440(7088):1194-8. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
5465 |
| Enzyme 3 Name |
Diacylglycerol kinase alpha |
| Enzyme 3 Synonyms |
- DAG kinase alpha
- 80 kDa diacylglycerol kinase
- Diglyceride kinase alpha
- DGK-alpha
|
| Enzyme 3 Gene Name |
DGKA |
| Enzyme 3 Protein Sequence |
>Diacylglycerol kinase alpha
MAKERGLISPSDFAQLQKYMEYSTKKVSDVLKLFEDGEMAKYVQGDAIGYEGFQQFLKIY
LEVDNVPRHLSLALFQSFETGHCLNETNVTKDVVCLNDVSCYFSLLEGGRPEDKLEFTFK
LYDTDRNGILDSSEVDKIILQMMRVAEYLDWDVSELRPILQEMMKEIDYDGSGSVSQAEW
VRAGATTVPLLVLLGLEMTLKDDGQHMWRPKRFPRPVYCNLCESSIGLGKQGLSCNLCKY
TVHDQCAMKALPCEVSTYAKSRKDIGVQSHVWVRGGCESGRCDRCQKKIRIYHSLTGLHC
VWCHLEIHDDCLQAVGHECDCGLLRDHILPPSSIYPSVLASGPDRKNSKTSQKTMDDLNL
STSEALRIDPVPNTHPLLVFVNPKSGGKQGQRVLWKFQYILNPRQVFNLLKDGPEIGLRL
FKDVPDSRILVCGGDGTVGWILETIDKANLPVLPPVAVLPLGTGNDLARCLRWGGGYEGQ
NLAKILKDLEMSKVVHMDRWSVEVIPQQTEEKSDPVPFQIINNYFSIGVDASIAHRFHIM
REKYPEKFNSRMKNKLWYFEFATSESIFSTCKKLEESLTVEICGKPLDLSNLSLEGIAVL
NIPSMHGGSNLWGDTRRPHGDIYGINQALGATAKVITDPDILKTCVPDLSDKRLEVVGLE
GAIEMGQIYTKLKNAGRRLAKCSEITFHTTKTLPMQIDGEPWMQTPCTIKITHKNQMPML
MGPPPRSTNFFGFLS
|
| Enzyme 3 Number of Residues |
735 |
| Enzyme 3 Molecular Weight |
82629.5 |
| Enzyme 3 Theoretical pI |
6.71 |
| Enzyme 3 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- diacylglycerol kinase activity
- ion binding
- kinase activity
- metal ion binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 3 Specific Function |
Upon cell stimulation converts the second messenger diacylglycerol into phosphatidate, initiating the resynthesis of phosphatidylinositols and attenuating protein kinase C activity |
| Enzyme 3 Pathways |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 3 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
30823  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
P23743  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
DGKA_HUMAN  |
| Enzyme 3 PDB ID |
1TUZ  |
| Enzyme 3 PDB File |
Show |
| Enzyme 3 3D Structure |
|
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>2208 bp
ATGGCCAAGGAGAGGGGCCTAATAAGCCCCAGTGATTTTGCCCAGCTGCAAAAATACATG
GAATACTCCACCAAAAAGGTCAGTGATGTCCTAAAGCTCTTCGAGGATGGCGAGATGGCT
AAATATGTCCAAGGAGATGCCATTGGGTACGAGGGATTCCAGCAATTCCTGAAAATCTAT
CTCGAAGTGGATAATGTTCCCAGACACCTAAGCCTGGCACTGTTTCAATCCTTTGAGACT
GGTCACTGCTTAAATGAGACAAATGTGACAAAAGATGTGGTGTGTCTCAATGATGTTTCC
TGCTACTTTTCCCTTCTGGAGGGTGGTCGGCCAGAAGACAAGTTAGAATTCACCTTCAAG
CTGTACGACACGGACAGAAATGGGATCCTGGACAGCTCAGAAGTGGACAAAATTATCCTA
CAGATGATGCGAGTGGCTGAATACCTGGATTGGGATGTGTCTGAGCTGAGGCCGATTCTT
CAGGAGATGATGAAAGAGATTGACTATGATGGCAGTGGCTCTGTCTCTCAAGCTGAGTGG
GTCCGGGCTGGGGCCACCACCGTGCCACTGCTAGTGCTGCTGGGTCTGGAGATGACTCTG
AAGGACGACGGACAGCACATGTGGAGGCCCAAGAGGTTCCCCAGACCAGTCTACTGCAAT
CTGTGCGAGTCAAGCATTGGTCTTGGCAAACAGGGACTGAGCTGTAACCTCTGTAAGTAC
ACTGTTCACGACCAGTGTGCCATGAAAGCCCTGCCTTGTGAAGTCAGCACCTATGCCAAG
TCTCGGAAGGACATTGGTGTCCAATCACATGTGTGGGTGCGAGGAGGCTGTGAGTCCGGG
CGCTGCGACCGCTGTCAGAAAAAGATCCGGATCTACCACAGTCTGACCGGGCTGCATTGT
GTATGGTGCCACCTAGAGATCCACGATGACTGCCTGCAAGCGGTGGGCCATGAGTGTGAC
TGTGGGCTGCTCCGGGATCACATCCTGCCTCCATCTTCCATCTATCCCAGTGTCCTGGCC
TCTGGACCGGATCGTAAAAATAGCAAAACAAGCCAGAAGACCATGGATGATTTAAATTTG
AGCACCTCTGAGGCTCTGCGGATTGACCCTGTTCCTAACACCCACCCACTTCTCGTCTTT
GTCAATCCTAAGAGTGGCGGGAAGCAGGGGCAGAGGGTGCTCTGGAAGTTCCAGTATATA
TTAAACCCTCGACAGGTGTTCAACCTCCTAAAGGATGGTCCTGAGATAGGGCTCCGATTA
TTCAAGGATGTTCCTGATAGCCGGATTTTGGTGTGTGGTGGAGACGGCACAGTAGGCTGG
ATTCTAGAGACCATTGACAAAGCTAACTTGCCAGTTTTGCCTCCTGTTGCTGTGTTGCCC
CTGGGTACTGGAAATGATCTGGCTCGATGCCTAAGATGGGGAGGAGGTTATGAAGGACAG
AATCTGGCAAAGATCCTCAAGGATTTAGAGATGAGTAAAGTGGTACATATGGATCGATGG
TCTGTGGAGGTGATACCTCAACAAACTGAAGAAAAAAGTGACCCAGTCCCCTTTCAAATC
ATCAATAACTACTTCTCTATTGGCGTGGATGCCTCTATTGCTCATCGATTCCACATCATG
CGAGAGAAATATCCGGAGAAGTTCAACAGCAGAATGAAGAACAAGCTATGGTACTTCGAA
TTTGCCACATCTGAATCCATCTTCTCAACATGCAAAAAGCTGGAGGAGTCTTTGACAGTT
GAGATCTGTGGGAAACCGCTGGATCTGAGCAACCTGTCCCTAGAAGGCATCGCAGTGCTA
AACATCCCTAGCATGCATGGTGGCTCCAACCTCTGGGGTGATACCAGGAGACCCCATGGG
GATATCTATGGGATCAACCAGGCCTTAGGTGCTACAGCTAAAGTCATCACCGACCCTGAT
ATCCTGAAAACCTGTGTACCAGACCTAAGTGACAAGAGACTGGAAGTGGTTGGGCTGGAG
GGTGCAATTGAGATGGGCCAAATCTATACCAAGCTCAAGAATGCTGGACGTCGGCTGGCC
AAGTGCTCTGAGATCACCTTCCACACCACAAAAACCCTTCCCATGCAAATTGACGTAGAA
CCCTGGATGCAGACGCCCTGTACAATCAAGATCACCCACAAGAACCAGATGCCCATGCTC
ATGGGCCCACCCCCCCGCTCCACCAATTTCTTTGGCTTCTTGAGCTAA
|
| Enzyme 3 GenBank Gene ID |
X62535  |
| Enzyme 3 GeneCard ID |
DGKA  |
| Enzyme 3 GenAtlas ID |
DGKA  |
| Enzyme 3 HGNC ID |
HGNC:2849  |
| Enzyme 3 Chromosome Location |
1 |
| Enzyme 3 Locus |
12q13.3 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Schaap D, de Widt J, van der Wal J, Vandekerckhove J, van Damme J, Gussow D, Ploegh HL, van Blitterswijk WJ, van der Bend RL: Purification, cDNA-cloning and expression of human diacylglycerol kinase. FEBS Lett. 1990 Nov 26;275(1-2):151-8. [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
]
- Hart TC, Champagne C, Zhou J, Van Dyke TE: Assignment of the gene for diacylglycerol kinase (DAGK) to human chromosome 12. Mamm Genome. 1994 Feb;5(2):123-4. [PubMed
]
- Hart TC, Zhou J, Champagne C, Van Dyke TE, Rao PN, Pettenati MJ: Assignment of the human diacylglycerol kinase gene (DAGK) to 12q13.3 using fluorescence in situ hybridization analysis. Genomics. 1994 Jul 1;22(1):246-7. [PubMed
]
- Rikova K, Guo A, Zeng Q, Possemato A, Yu J, Haack H, Nardone J, Lee K, Reeves C, Li Y, Hu Y, Tan Z, Stokes M, Sullivan L, Mitchell J, Wetzel R, Macneill J, Ren JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
5466 |
| Enzyme 4 Name |
Diacylglycerol kinase delta |
| Enzyme 4 Synonyms |
- DAG kinase delta
- 130 kDa diacylglycerol kinase
- Diglyceride kinase delta
- DGK-delta
|
| Enzyme 4 Gene Name |
DGKD |
| Enzyme 4 Protein Sequence |
>Diacylglycerol kinase delta
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTIIKEGML
TKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITP
CRKLILCADNRKEMEDWIAALKTVQNREHFEPTQYSMDHFSGMHNWYACSHARPTYCNVC
REALSGVTSHGLSCEVCKFKAHKRCAVRATNNCKWTTLASIGKDIIEDADGIAMPHQWLE
GNLPVSAKCTVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLLTKCPLGLCKVSVIPPTA
LNSIDSDGFWKASCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPH
LGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGS
ACDDDTQLPQILEKLERASTKMLDRWSVMAYEAKLPRQASSSTVTEDFSEDSEVQQILFY
EDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSEESEVMAKKCS
VLKEKLDSLLKTLDDESQASSSLPNPPPTIAEEAEDGDGSGSICGSTGDRLVASACPARP
QIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQEGFVLGLSESEEKMDHRVC
PPLSHSESFGVPKGRSQRKVSKSPCEKLISKGSLSLGSSASLPPQPGSRDGLPALNTKIL
YPNVRAGMSGSLPGGSVISRLLINADPFNSEPETLEYYTEKCVMNNYFGIGLDAKISLDF
NNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYKNLEQKVLLECDGRPIPLPSLQGIAV
LNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIRLQHHRIAQCR
TVKISILGDEGVPVQVDGEAWVQPPGYIRIVHKNRAQTLTRDRAFESTLKSWEDKQKCEL
PRPPSCSLHPEMLSEEEATQMDQFGQAAGVLIHSIREIAQSHRDMEQELAHAVNASSKSM
DRVYGKPRTTEGLNCSFVLEMVNNFRALRSETELLLSGKMALQLDPPQKEQLGSALAEMD
RQLRRLADTPWLCQSAEPGDEESVMLDLAKRSRSGKFRLVTKFKKEKNNKNKEAHSSLGA
PVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILC
GIKELSRSAPAVEA
|
| Enzyme 4 Number of Residues |
1214 |
| Enzyme 4 Molecular Weight |
134524.2 |
| Enzyme 4 Theoretical pI |
7.58 |
| Enzyme 4 GO Classification |
| Function |
- catalytic activity
- diacylglycerol kinase activity
- kinase activity
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 4 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 4 Specific Function |
Isoform 2 may be involved in cell growth and tumorigenesis. Involved in clathrin-dependent endocytosis |
| Enzyme 4 Pathways |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 4 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
22773821  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q16760  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
DGKD_HUMAN  |
| Enzyme 4 PDB ID |
1R79  |
| Enzyme 4 PDB File |
Show |
| Enzyme 4 3D Structure |
|
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>3645 bp
ATGGCGGCGGCGGCGGGCGCCCCTCCGCCGGGTCCCCCGCAACCGCCTCCGCCGCCGCCG
CCCGAGGAGTCGTCCGACAGCGAGCCCGAGGCGGAGCCCGGCTCCCCACAGAAGCTCATC
CGCAAGGTGTCCACGTCGGGTCAGATCCGACAGAAGACCATCATCAAAGAGGGGATGCTG
ACCAAACAGAACAATTCATTCCAGCGATCAAAAAGGAGATACTTTAAGCTTCGAGGGCGA
ACGCTTTACTATGCCAAAACGGCAAAGTCAATCATATTTGATGAGGTGGATCTGACAGAT
GCCAGCGTAGCTGAATCCAGTACCAAAAACGTCAACAACAGTTTTACGGTCATAACTCCA
TGCAGGAAGCTCATCTTGTGTGCTGATAACAGAAAAGAAATGGAAGATTGGATTGCAGCA
TTAAAGACTGTGCAGAACAGGGAGCACTTTGAGCCCACCCAGTACAGCATGGACCACTTC
TCAGGGATGCACAATTGGTACGCCTGTTCCCACGCGAGGCCGACCTACTGCAATGTGTGC
CGTGAGGCTCTGTCTGGGGTCACGTCGCACGGGCTGTCCTGCGAGGTGTGCAAATTTAAG
GCCCACAAGCGCTGTGCTGTGCGTGCAACCAATAACTGCAAGTGGACCACACTGGCCTCG
ATCGGGAAGGACATCATTGAAGATGCAGATGGGATTGCAATGCCCCACCAGTGGTTGGAA
GGAAACCTACCTGTGAGCGCCAAGTGCACTGTGTGCGACAAGACCTGTGGCAGTGTGCTG
CGCCTGCAGGACTGGCGCTGCCTCTGGTGCAAGGCCATGGTTCACACATCGTGTAAAGAA
TCCTTGCTGACCAAGTGCCCACTTGGCCTGTGCAAAGTGTCAGTCATCCCACCCACGGCT
CTCAACAGCATCGACTCCGATGGGTTCTGGAAGGCCAGCTGTCCTCCTTCTTGCACAAGC
CCACTGTTGGTCTTCGTCAATTCAAAAAGTGGGGACAACCAGGGTGTGAAGTTCCTCAGA
AGATTCAAACAGCTACTAAACCCCGCCCAGGTCTTCGACCTCATGAACGGAGGCCCACAC
CTCGGCTTACGGTTATTCCAGAAGTTTGACACATTCCGGATTCTGGTTTGTGGCGGGGAT
GGAAGTGTTGGCTGGGTCCTCTCCGAAATCGACAGCCTCAACCTTCATAAACAGTGTCAG
CTGGGAGTGCTGCCGCTCGGCACAGGGAACGACTTGGCCCGAGTACTGGGCTGGGGCTCA
GCCTGCGATGACGACACCCAGCTCCCCCAGATCTTGGAGAAGTTGGAGAGAGCCAGCACC
AAGATGCTGGACAGGTGGAGCGTCATGGCATACGAGGCCAAGCTCCCCCGGCAGGCCTCC
TCCTCTACCGTCACCGAAGACTTCAGCGAGGATTCCGAGGTACAGCAGATTCTCTTCTAT
GAAGACTCGGTTGCAGCCCACCTTTCTAAAATCCTCACCTCGGACCAGCACTCGGTGGTC
ATCTCCTCGGCCAAAGTGCTCTGTGAGACGGTGAAGGACTTCGTGGCACGGGTGGGGAAG
GCCTATGAGAAGACGACCGAGAGCTCGGAGGAGTCAGAGGTCATGGCCAAGAAGTGCTCT
GTCCTGAAAGAGAAGCTGGATTCCCTTCTCAAGACCTTGGACGATGAGTCCCAGGCCTCG
TCCTCTCTGCCCAACCCGCCCCCCACCATTGCCGAGGAGGCTGAAGATGGAGATGGGTCG
GGCAGCATCTGCGGTTCCACCGGAGACCGCTTGGTGGCATCAGCTTGCCCGGCCCGGCCG
CAGATATTCCGGCCTCGAGAACAGCTCATGCTGAGAGCCAACAGCCTGAAGAAAGCAATT
CGTCAGATCATAGAACACACAGAAAAAGCTGTCGATGAGCAGAATGCCCAGACCCAGGAG
CAGGAGGGCTTCGTCCTGGGCCTCTCTGAGTCAGAGGAGAAGATGGACCACAGAGTGTGC
CCACCACTGTCCCACAGCGAGAGCTTCGGGGTCCCCAAGGGGAGGAGCCAGCGCAAAGTG
TCGAAATCTCCGTGTGAAAAGCTGATCAGCAAAGGGAGTCTGTCCCTAGGCAGTTCTGCT
TCCCTTCCGCCCCAGCCGGGAAGCCGGGACGGCCTGCCTGCGCTCAACACCAAGATCCTG
TACCCAAATGTCCGGGCTGGAATGTCTGGTTCCTTACCCGGTGGCTCAGTCATCAGTCGC
CTGTTAATTAATGCTGATCCCTTCAACTCTGAACCAGAAACCCTAGAGTATTACACGGAG
AAATGTGTCATGAACAACTATTTTGGCATTGGCCTGGATGCGAAGATATCCCTGGACTTT
AACAACAAGCGCGATGAGCACCCAGAGAAGTGCAGGAGCCGAACCAAGAACATGATGTGG
TATGGAGTTCTTGGAACCAAAGAGTTGCTGCACAGAACCTACAAGAACCTGGAGCAAAAG
GTCTTGCTGGAGTGTGACGGGCGACCCATCCCACTCCCCAGTCTTCAGGGAATTGCTGTC
CTTAACATTCCCAGCTATGCCGGAGGAACCAACTTCTGGGGGGGTACCAAGGAAGATGAT
ACTTTCGCAGCTCCATCATTCGATGACAAGATTCTGGAGGTGGTCGCCGTGTTCGGCAGC
ATGCAGATGGCCGTCTCTCGAGTCATCAGGCTACAGCATCATCGGATCGCCCAGTGTCGC
ACGGTGAAGATCTCCATCCTTGGGGATGAGGGCGTGCCTGTGCAGGTGGACGGAGAGGCC
TGGGTCCAGCCGCCAGGGTACATTCGGATTGTCCACAAGAACCGGGCACAGACACTGACC
AGAGACAGGGCATTTGAGAGCACCCTGAAGTCCTGGGAAGACAAGCAGAAGTGCGAGGTG
CCCCGCCCTCCATCCTGTTCCCTGCACCCGGAGATGCTGTCCGAGGAGGAGGCCACCCAG
ATGGACCAGTTTGGGCAGGCAGCAGGGGTCCTCATTCACAGTATCCGAGAAATAGCTCAG
TCTCACCGGGACATGGAGCAGGAACTGGCCCACGCCGTCAATGCCAGCTCCAAGTCCATG
GACCGTGTGTATGGCAAGCCCAGAACCACAGAGGGGCTCAACTGCAGCTTCGTCCTGGAA
ATGGTGAATAACTTCAGAGCTCTGCGCAGTGAGACGGAGCTGCTGCTGTCTGGGAAGATG
GCCCTGCAGCTGGATCCGCCTCAGAAGGAGCAGCTGGGGAGTGCTCTTGCCGAGATGGAC
CGACAGCTCAGGAGGCTGGCAGACACCCCGTGGCTCTGCCAGTCCGCAGAGCCCGGCGAC
GAAGAGAGTGTGATGCTGGATCTTGCCAAGCGCAGTCGCAGTGGTAAATTCCGCCTCGTG
ACCAAGTTTAAAAAGGAGAAAAACAACAAGAACAAAGAAGCTCACAGTAGCCTGGGAGCC
CCGGTTCACCTCTGGGGGACAGAGGAGGTTGCTGCCTGGCTGGAGCACCTCAGTCTCTGT
GAGTATAAGGACATCTTCACACGGCACGACATCCGGGGCTCTGAGCTCCTGCACCTGGAG
CGGAGGGACCTCAAGGACCTGGGCGTGACCAAGGTGGGCCACATGAAGAGGATCCTGTGT
GGCATCAAGGAGCTGAGCCGCAGCGCCCCCGCCGTCGAGGCCTAG
|
| Enzyme 4 GenBank Gene ID |
AB078966  |
| Enzyme 4 GeneCard ID |
DGKD  |
| Enzyme 4 GenAtlas ID |
DGKD  |
| Enzyme 4 HGNC ID |
HGNC:2851  |
| Enzyme 4 Chromosome Location |
2 |
| Enzyme 4 Locus |
2q37.1 |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
- Sakane F, Imai S, Yamada K, Murakami T, Tsushima S, Kanoh H: Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions. J Biol Chem. 2002 Nov 8;277(45):43519-26. Epub 2002 Aug 27. [PubMed
]
- Nagase T, Seki N, Tanaka A, Ishikawa K, Nomura N: Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. DNA Res. 1995 Aug 31;2(4):167-74, 199-210. [PubMed
]
- Sakane F, Imai S, Kai M, Wada I, Kanoh H: Molecular cloning of a novel diacylglycerol kinase isozyme with a pleckstrin homology domain and a C-terminal tail similar to those of the EPH family of protein-tyrosine kinases. J Biol Chem. 1996 Apr 5;271(14):8394-401. [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
]
- Imai S, Sakane F, Kanoh H: Phorbol ester-regulated oligomerization of diacylglycerol kinase delta linked to its phosphorylation and translocation. J Biol Chem. 2002 Sep 20;277(38):35323-32. Epub 2002 Jun 25. [PubMed
]
- Kawasaki T, Kobayashi T, Ueyama T, Shirai Y, Saito N: Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha. Biochem J. 2008 Jan 15;409(2):471-9. [PubMed
]
|
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
5470 |
| Enzyme 5 Name |
Diacylglycerol kinase beta |
| Enzyme 5 Synonyms |
- DAG kinase beta
- 90 kDa diacylglycerol kinase
- Diglyceride kinase beta
- DGK-beta
|
| Enzyme 5 Gene Name |
DGKB |
| Enzyme 5 Protein Sequence |
>Diacylglycerol kinase beta
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDF
EGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPMVKSKPALLSGGLRMNKGAITPPR
TTSPANTCSPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIISQ
MMHVAEYLEWDVTELNPILHEMMEEIDYDHDGTVSLEEWIQGGMTTIPLLVLLGLENNVK
DDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCVARAPPSCIKTYVK
SKRNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQITLHNKCASHLKPECDC
GPLKDHILPPTTICPVVLQTLPTSGVSVPEERQSTVKKEKSGSQQPNKVIDKNKMQRANS
VTVDGQGLQVTPVPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGL
NFFRDVPDFRVLACGGDGTVGWVLDCIEKANVGKHPPVAILPLGTGNDLARCLRWGGGYE
GENLMKILKDIENSTEIMLDRWKFEVIPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFH
IMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLEGIA
ILNIPSMHGGSNLWGESKKRRSHRRIEKKGSDKRTTVTDAKELKFASQDLSDQLLEVVGL
EGAMEMGQIYTGLKSAGRRLAQCSCVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPM
LMGPPPKTGLFCSLVKRTRNRSKE
|
| Enzyme 5 Number of Residues |
804 |
| Enzyme 5 Molecular Weight |
90594.7 |
| Enzyme 5 Theoretical pI |
7.90 |
| Enzyme 5 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- diacylglycerol kinase activity
- ion binding
- kinase activity
- metal ion binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- G-protein coupled receptor protein signaling pathway
- activation of protein kinase C activity by G-protein coupled receptor protein signaling pathway
- cell surface receptor linked signaling pathway
- intracellular signaling pathway
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 5 General Function |
Involved in diacylglycerol kinase activity |
| Enzyme 5 Specific Function |
Exhibits high phosphorylation activity for long-chain diacylglycerols |
| Enzyme 5 Pathways |
- Glycerolipid Metabolism (map00561
)
- Phospholipid Synthesis (map00564
)
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 5 Reactions |
- ATP + 1,2-diacyl-sn-glycerol = ADP + 1,2-diacyl-sn-glycerol 3-phosphate [RN:R02240]
|
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
22027632  |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9Y6T7  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
DGKB_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>2415 bp
ATGACAAACCAGGAAAAATGGGCCCACCTCAGCCCTTCGGAATTTTCCCAACTTCAGAAA
TATGCTGAGTATTCTACAAAGAAATTAAAGGATGTTCTTGAAGAATTCCATGGTAATGGT
GTGCTTGCAAAGTATAATCCTGAAGGGAAACAAGACATTCTTAACCAAACAATAGATTTT
GAAGGTTTCAAACTATTCATGAAGACATTCCTGGAAGCCGAGCTTCCTGATGATTTCACT
GCACACCTTTTCATGTCATTTAGCAACAAGTTTCCTCATTCTAGTCCAATGGTAAAAAGT
AAGCCTGCTCTCCTATCAGGCGGTCTGAGAATGAATAAAGGTGCCATCACCCCTCCCCGG
ACTACTTCTCCTGCAAATACGTGTTCCCCAGAAGTAATCCATCTGAAGGACATTGTCTGT
TACCTGTCTCTGCTTGAAAGAGGAAGACCTGAGGATAAGCTTGAGTTTATGTTTCGCCTT
TATGACACGGATGGGAATGGCTTCCTGGACAGCTCGGAGCTAGAAAATATCATCAGTCAG
ATGATGCATGTTGCAGAATACCTTGAGTGGGATGTCACTGAACTTAATCCAATCCTCCAT
GAAATGATGGAAGAAATTGACTATGATCATGATGGAACCGTGTCTCTGGAGGAATGGATT
CAAGGAGGAATGACAACGATTCCACTTCTTGTGCTCCTGGGCTTAGAAAATAACGTGAAG
GATGATGGACAGCACGTGTGGCGACTGAAGCACTTTAACAAACCTGCCTATTGCAACCTT
TGCCTGAACATGCTGATTGGCGTGGGGAAGCAGGGCCTCTGCTGTTCCTTCTGCAAGTAC
ACAGTCCATGAGCGCTGTGTGGCTCGAGCACCTCCCTCTTGCATCAAGACCTATGTGAAG
TCCAAAAGGAACACTGATGTCATGCACCATTACTGGGTTGAAGGTAACTGCCCAACCAAG
TGTGATAAGTGCCACAAAACTGTTAAATGTTACCAGGGCCTGACAGGACTGCATTGTGTT
TGGTGTCAGATCACACTGCATAATAAATGTGCTTCTCATCTAAAACCTGAATGTGACTGT
GGACCTTTGAAGGACCATATTTTACCACCCACAACAATCTGTCCAGTGGTACTGCAGACT
CTGCCCACTTCAGGAGTTTCAGTTCCTGAGGAAAGACAATCAACAGTGAAAAAGGAAAAG
AGTGGTTCCCAGCAGCCAAACAAAGTGATTGACAAGAATAAAATGCAAAGAGCCAACTCT
GTTACTGTAGATGGACAAGGCCTGCAGGTCACTCCTGTGCCTGGTACTCACCCACTTTTA
GTTTTTGTGAACCCCAAAAGTGGTGGAAAACAAGGAGAACGAATTTACAGAAAATTCCAG
TATCTATTAAATCCTCGTCAGGTTTACAGTCTTTCTGGAAATGGACCAATGCCAGGGTTA
AACTTTTTCCGTGATGTTCCTGACTTCAGAGTGTTAGCCTGTGGTGGAGATGGAACCGTG
GGCTGGGTTTTGGATTGCATAGAAAAGGCCAATGTAGGCAAGCATCCTCCAGTTGCGATT
CTGCCTCTTGGGACTGGCAATGATCTAGCAAGATGCCTGCGATGGGGAGGAGGTTACGAA
GGTGAGAATCTGATGAAAATTCTAAAAGACATTGAAAACAGCACAGAAATCATGTTGGAC
AGGTGGAAGTTTGAAGTCATACCTAATGACAAAGATGAGAAAGGAGACCCAGTGCCTTAC
AGTATCATCAATAATTACTTTTCCATTGGCGTGGATGCCTCCATTGCACACAGATTCCAC
ATCATGAGAGAAAAACACCCAGAGAAATTCAACAGTAGAATGAAGAACAAATTTTGGTAT
TTTGAGTTTGGCACATCTGAAACTTTCTCAGCCACCTGCAAGAAGCTACATGAATCTGTA
GAAATAGAATGTGATGGAGTACAGATAGATTTAATAAACATCTCTCTGGAAGGAATTGCT
ATTTTGAATATACCAAGCATGCATGGAGGATCCAATCTTTGGGGAGAGTCTAAGAAAAGA
CGAAGCCATCGACGAATAGAGAAAAAAGGGTCTGACAAAAGGACCACCGTCACAGATGCC
AAAGAGTTGAAGTTTGCAAGTCAAGATCTCAGTGACCAGCTGCTGGAGGTGGTCGGCTTG
GAAGGAGCCATGGAGATGGGGCAAATATACACAGGCCTGAAAAGTGCTGGCCGGCGGCTG
GCTCAGTGCTCCTGCGTGGTCATCAGGACGAGCAAGTCTCTGCCAATGCAAATTGATGGG
GAGCCATGGATGCAGACCCCATGCACAATAAAAATTACACACAAGAACCAAGCCCCAATG
CTGATGGGCCCGCCTCCAAAAACCGGTTTATTCTGCTCCCTCGTCAAAAGGACAAGAAAC
CGAAGCAAGGAATAA
|
| Enzyme 5 GenBank Gene ID |
NM_004080.2  |
| Enzyme 5 GeneCard ID |
DGKB  |
| Enzyme 5 GenAtlas ID |
DGKB  |
| Enzyme 5 HGNC ID |
HGNC:2850  |
| Enzyme 5 Chromosome Location |
7 |
| Enzyme 5 Locus |
7p21.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- Scherer SW, Cheung J, MacDonald JR, Osborne LR, Nakabayashi K, Herbrick JA, Carson AR, Parker-Katiraee L, Skaug J, Khaja R, Zhang J, Hudek AK, Li M, Haddad M, Duggan GE, Fernandez BA, Kanematsu E, Gentles S, Christopoulos CC, Choufani S, Kwasnicka D, Zheng XH, Lai Z, Nusskern D, Zhang Q, Gu Z, Lu F, Zeesman S, Nowaczyk MJ, Teshima I, Chitayat D, Shuman C, Weksberg R, Zackai EH, Grebe TA, Cox SR, Kirkpatrick SJ, Rahman N, Friedman JM, Heng HH, Pelicci PG, Lo-Coco F, Belloni E, Shaffer LG, Pober B, Morton CC, Gusella JF, Bruns GA, Korf BR, Quade BJ, Ligon AH, Ferguson H, Higgins AW, Leach NT, Herrick SR, Lemyre E, Farra CG, Kim HG, Summers AM, Gripp KW, Roberts W, Szatmari P, Winsor EJ, Grzeschik KH, Teebi A, Minassian BA, Kere J, Armengol L, Pujana MA, Estivill X, Wilson MD, Koop BF, Tosi S, Moore GE, Boright AP, Zlotorynski E, Kerem B, Kroisel PM, Petek E, Oscier DG, Mould SJ, Dohner H, Dohner K, Rommens JM, Vincent JB, Venter JC, Li PW, Mural RJ, Adams MD, Tsui LC: Human chromosome 7: DNA sequence and biology. Science. 2003 May 2;300(5620):767-72. Epub 2003 Apr 10. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
|
| Enzyme 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
6476 |
| Enzyme 6 Name |
Protein kinase C alpha type |
| Enzyme 6 Synonyms |
- PKC-A
- PKC-alpha
|
| Enzyme 6 Gene Name |
PRKCA |
| Enzyme 6 Protein Sequence |
>Protein kinase C alpha type
MADVFPGNDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGF
GKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGS
LLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVADEKLHVTVRDA
KNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRL
SVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNME
LRQKFEKAKLGPAGNKVISPSEDRKQPSNNLDRVKLTDFNFLMVLGKGSFGKVMLADRKG
TEELYAIKILKKDVVIQDDDVECTMVEKRVLALLDKPPFLTQLHSCFQTVDRLYFVMEYV
NGGDLMYHIQQVGKFKEPQAVFYAAEISIGLFFLHKRGIIYRDLKLDNVMLDSEGHIKIA
DFGMCKEHMMDGVTTRTFCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEMLAGQPPFDG
EDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRLGCGPEGERDVREHAFFRRI
DWEKLENREIQPPFKPKVCGKGAENFDKFFTRGQPVLTPPDQLVIANIDQSDFEGFSYVN
PQFVHPILQSAV
|
| Enzyme 6 Number of Residues |
672 |
| Enzyme 6 Molecular Weight |
76763.5 |
| Enzyme 6 Theoretical pI |
7.05 |
| Enzyme 6 GO Classification |
| Function |
- ATP binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- ion binding
- kinase activity
- metal ion binding
- nucleoside binding
- protein kinase C activity
- protein kinase activity
- protein serine/threonine kinase activity
- purine nucleoside binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
- transition metal ion binding
- zinc ion binding
|
| Process |
- cellular metabolic process
- intracellular signaling pathway
- metabolic process
- phosphate metabolic process
- phosphorus metabolic process
- phosphorylation
- protein amino acid phosphorylation
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 6 General Function |
Involved in protein serine/threonine kinase activity |
| Enzyme 6 Specific Function |
PKC is activated by diacylglycerol which in turn phosphorylates a range of cellular proteins. PKC also serves as the receptor for phorbol esters, a class of tumor promoters |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
- ATP + a protein = ADP + a phosphoprotein [RN:R00162]
|
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
35483  |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
P17252  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
KPCA_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>2019 bp
ATGGCTGACGTTTTCCCGGGCAACGACTCCACGGCGTCTCAGGACGTGGCCAACCGCTTC
GCCCGCAAAGGGGCGCTGAGGCAGAAGAACGTGCACGAGGTGAAGGACCACAAATTCATC
GCGCGCTTCTTCAAGCAGCCCACCTTCTGCAGCCACTGCACCGACTTCATCTGGGGGTTT
GGGAAACAAGGCTTCCAGTGCCAAGTTTGCTGTTTTGTGGTCCACAAGAGGTGCCATGAA
TTTGTTACTTTTTCTTGTCCGGGTGCGGATAAGGGACCCGACACTGATGACCCCAGGAGC
AAGCACAAGTTCAAAATCCACACTTACGGAAGCCCCACCTTCTGCGATCACTGTGGGTCA
CTGCTCTATGGACTTATCCATCAAGGGATGAAATGTGACACCTGCGATATGAACGTTCAC
AAGCAATGCGTCATCAATGTCCCCAGCCTCTGCGGAATGGATCACACTGAGAAGAGGGGG
CGGATTTACCTAAAGGCTGAGGTTGCTGATGAAAAGCTCCATGTCACAGTACGAGATGCA
AAAAATCTAATCCCTATGGATCCAAACGGGCTTTCAGATCCTTATGTGAAGCTGAAACTT
ATTCCTGATCCCAAGAATGAAAGCAAGCAAAAAACCAAAACCATCCGCTCCACACTAAAT
CCGCAGTGGAATGAGTCCTTTACATTCAAATTGAAACCTTCAGACAAAGACCGACGACTG
TCTGTAGAAATCTGGGACTGGGATCGAACAACAAGGAATGACTTCATGGGATCCCTTTCC
TTTGGAGTTTCGGAGCTGATGAAGATGCCGGCCAGTGGATGGTACAAGTTGCTTAACCAA
GAAGAAGGTGAGTACTACAACGTACCCATTCCGGAAGGGGACGAGGAAGGAAACATGGAA
CTCAGGCAGAAATTCGAGAAAGCCAAACTTGGCCCTGCTGGCAACAAAGTCATCAGTCCC
TCTGAAGACAGGAAACAACCTTCCAACAACCTTGACCGAGTGAAACTCACGGACTTCAAT
TTCCTCATGGTGTTGGGAAAGGGGAGTTTTGGAAAGGTGATGCTTGCCGACAGGAAGGGC
ACAGAAGAACTGTATGCAATCAAAATCCTGAAGAAGGATGTGGTGATTCAGGATGATGAC
GTGGAGTGCACCATGGTAGAAAAGCGAGTCTTGGCCCTGCTTGACAAACCCCCGTTCTTG
ACGCAGCTGCACTCCTGCTTCCAGACAGTGGATCGGCTGTACTTCGTCATGGAATATGTC
AACGGTGGGGACCTCATGTACCACATTCAGCAAGTAGGAAAATTTAAGGAACCACAAGCA
GTATTCTATGCGGCAGAGATTTCCATCGGATTGTTCTTTCTTCATAAAAGAGGAATCATT
TATAGGGATCTGAAGTTAGATAACGTCATGTTGGATTCAGAAGGACATATCAAAATTGCT
GACTTTGGGATGTGCAAGGAACACATGATGGATGGAGTCACGACCAGGACCTTCTGTGGG
ACTCCAGATTATATCGCCCCAGAGATAATCGCTTATCAGCCGTATGGAAAATCTGTGGAC
TGGTGGGCCTATGGCGTCCTGTTGTATGAAATGCTTGCCGGGCAGCCTCCATTTGATGGT
GAAGATGAAGACGAGCTATTTCAGTCTATCATGGAGCACAACGTTTCCTATCCAAAATCC
TTGTCCAAGGAGGCTGTTTCTATCTGCAAAGGACTGATGACCAAACACCCAGCCAAGCGG
CTGGGCTGTGGGCCTGAGGGGGAGAGGGACGTGAGAGAGCATGCCTTCTTCCGGAGGATC
GACTGGGAAAAACTGGAGAACAGGGAGATCCAGCCACCATTCAAGCCCAAAGTGTGTGGC
AAAGGAGCAGAGAACTTTGACAAGTTCTTCACACGAGGACAGCCCGTCTTAACACCACCT
GATCAGCTGGTTATTGCTAACATAGACCAGTCTGATTTTGAAGGGTTCTCGTATGTCAAC
CCCCAGTTTGTGCACCCCATCTTACAGAGTGCAGTATGA
|
| Enzyme 6 GenBank Gene ID |
X52479  |
| Enzyme 6 GeneCard ID |
PRKCA  |
| Enzyme 6 GenAtlas ID |
PRKCA  |
| Enzyme 6 HGNC ID |
HGNC:9393  |
| Enzyme 6 Chromosome Location |
1 |
| Enzyme 6 Locus |
17q22-q23.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Finkenzeller G, Marme D, Hug H: Sequence of human protein kinase C alpha. Nucleic Acids Res. 1990 Apr 25;18(8):2183. [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
]
- McSwine-Kennick RL, McKeegan EM, Johnson MD, Morin MJ: Phorbol diester-induced alterations in the expression of protein kinase C isozymes and their mRNAs. Analysis in wild-type and phorbol diester-resistant HL-60 cell clones. J Biol Chem. 1991 Aug 15;266(23):15135-43. [PubMed
]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed
]
- Zemlickova E, Dubois T, Kerai P, Clokie S, Cronshaw AD, Wakefield RI, Johannes FJ, Aitken A: Centaurin-alpha(1) associates with and is phosphorylated by isoforms of protein kinase C. Biochem Biophys Res Commun. 2003 Aug 1;307(3):459-65. [PubMed
]
- Dev KK, Nakanishi S, Henley JM: The PDZ domain of PICK1 differentially accepts protein kinase C-alpha and GluR2 as interacting ligands. J Biol Chem. 2004 Oct 1;279(40):41393-7. Epub 2004 Jul 9. [PubMed
]
- Makagiansar IT, Williams S, Dahlin-Huppe K, Fukushi J, Mustelin T, Stallcup WB: Phosphorylation of NG2 proteoglycan by protein kinase C-alpha regulates polarized membrane distribution and cell motility. J Biol Chem. 2004 Dec 31;279(53):55262-70. Epub 2004 Oct 25. [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
]
- Chen D, Gould C, Garza R, Gao T, Hampton RY, Newton AC: Amplitude control of protein kinase C by RINCK, a novel E3 ubiquitin ligase. J Biol Chem. 2007 Nov 16;282(46):33776-87. Epub 2007 Sep 24. [PubMed
]
- Wissing J, Jansch L, Nimtz M, Dieterich G, Hornberger R, Keri G, Wehland J, Daub H: Proteomics analysis of protein kinases by target class-selective prefractionation and tandem mass spectrometry. Mol Cell Proteomics. 2007 Mar;6(3):537-47. Epub 2006 Dec 27. [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
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Greenman C, Stephens P, Smith R, Dalgliesh GL, Hunter C, Bignell G, Davies H, Teague J, Butler A, Stevens C, Edkins S, O'Meara S, Vastrik I, Schmidt EE, Avis T, Barthorpe S, Bhamra G, Buck G, Choudhury B, Clements J, Cole J, Dicks E, Forbes S, Gray K, Halliday K, Harrison R, Hills K, Hinton J, Jenkinson A, Jones D, Menzies A, Mironenko T, Perry J, Raine K, Richardson D, Shepherd R, Small A, Tofts C, Varian J, Webb T, West S, Widaa S, Yates A, Cahill DP, Louis DN, Goldstraw P, Nicholson AG, Brasseur F, Looijenga L, Weber BL, Chiew YE, DeFazio A, Greaves MF, Green AR, Campbell P, Birney E, Easton DF, Chenevix-Trench G, Tan MH, Khoo SK, Teh BT, Yuen ST, Leung SY, Wooster R, Futreal PA, Stratton MR: Patterns of somatic mutation in human cancer genomes. Nature. 2007 Mar 8;446(7132):153-8. [PubMed
]
|
| Enzyme 6 Metabolite References |
Not Available |
|
Enzyme 7
[top]
|
| Enzyme 7 ID |
6655 |
| Enzyme 7 Name |
Probable phospholipid-transporting ATPase IA |
| Enzyme 7 Synonyms |
- ATPase class I type 8A member 1
- Chromaffin granule ATPase II
|
| Enzyme 7 Gene Name |
ATP8A1 |
| Enzyme 7 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 7 Number of Residues |
1164 |
| Enzyme 7 Molecular Weight |
131368.2 |
| Enzyme 7 Theoretical pI |
6.83 |
| Enzyme 7 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 7 General Function |
Involved in ATP binding |
| Enzyme 7 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 7 Pathways |
Not Available |
| Enzyme 7 Reactions |
- ATP + H2O + phospholipidin = ADP + phosphate + phospholipidout [RN:R00086]
|
| Enzyme 7 Pfam Domain Function |
|
| Enzyme 7 Signals |
|
| Enzyme 7 Transmembrane Regions |
- 66-86
93-115
298-319
345-366
858-878
891-910
941-962
977-999
1006-1026
1045-1070
|
| Enzyme 7 Essentiality |
Not Available |
| Enzyme 7 GenBank ID Protein |
Not Available |
| Enzyme 7 UniProtKB/Swiss-Prot ID |
Q9Y2Q0  |
| Enzyme 7 UniProtKB/Swiss-Prot Entry Name |
AT8A1_HUMAN  |
| Enzyme 7 PDB ID |
Not Available |
| Enzyme 7 Cellular Location |
Not Available |
| Enzyme 7 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 7 GenBank Gene ID |
AF067820  |
| Enzyme 7 GeneCard ID |
ATP8A1  |
| Enzyme 7 GenAtlas ID |
ATP8A1  |
| Enzyme 7 HGNC ID |
HGNC:13531  |
| Enzyme 7 Chromosome Location |
4 |
| Enzyme 7 Locus |
4p13 |
| Enzyme 7 SNPs |
SNPJam Report  |
| Enzyme 7 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 7 Metabolite References |
Not Available |
|
Enzyme 8
[top]
|
| Enzyme 8 ID |
7395 |
| Enzyme 8 Name |
Phospholipid scramblase 1 |
| Enzyme 8 Synonyms |
- PL scramblase 1
- Ca(2+)-dependent phospholipid scramblase 1
- Erythrocyte phospholipid scramblase
- MmTRA1b
|
| Enzyme 8 Gene Name |
PLSCR1 |
| Enzyme 8 Protein Sequence |
>Phospholipid scramblase 1
MDKQNSQMNASHPETNLPVGYPPQYPPTAFQGPPGYSGYPGPQVSYPPPPAGHSGPGPAG
FPVPNQPVYNQPVYNQPVGAAGVPWMPAPQPPLNCPPGLEYLSQIDQILIHQQIELLEVL
TGFETNNKYEIKNSFGQRVYFAAEDTDCCTRNCCGPSRPFTLRIIDNMGQEVITLERPLR
CSSCCCPCCLQEIEIQAPPGVPIGYVIQTWHPCLPKFTIQNEKREDVLKISGPCVVCSCC
GDVDFEIKSLDEQCVVGKISKHWTGILREAFTDADNFGIQFPLDLDVKMKAVMIGACFLI
DFMFFESTGSQEQKSGVW
|
| Enzyme 8 Number of Residues |
318 |
| Enzyme 8 Molecular Weight |
35048.8 |
| Enzyme 8 Theoretical pI |
4.57 |
| Enzyme 8 GO Classification |
Not Available |
| Enzyme 8 General Function |
Involved in calcium ion binding |
| Enzyme 8 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 8 Pathways |
Not Available |
| Enzyme 8 Reactions |
Not Available |
| Enzyme 8 Pfam Domain Function |
|
| Enzyme 8 Signals |
|
| Enzyme 8 Transmembrane Regions |
|
| Enzyme 8 Essentiality |
Not Available |
| Enzyme 8 GenBank ID Protein |
3510297  |
| Enzyme 8 UniProtKB/Swiss-Prot ID |
O15162  |
| Enzyme 8 UniProtKB/Swiss-Prot Entry Name |
PLS1_HUMAN  |
| Enzyme 8 PDB ID |
Not Available |
| Enzyme 8 Cellular Location |
Not Available |
| Enzyme 8 Gene Sequence |
>957 bp
ATGGACAAACAAAACTCACAGATGAATGCTTCTCACCCGGAAACAAACTTGCCAGTTGGG
TATCCTCCTCAGTATCCACCGACAGCATTCCAAGGACCTCCAGGATATAGTGGCTACCCT
GGGCCCCAGGTCAGCTACCCACCCCCACCAGCCGGCCATTCAGGTCCTGGCCCAGCTGGC
TTTCCTGTCCCAAATCAGCCAGTGTATAATCAGCCAGTATATAATCAGCCAGTTGGAGCT
GCAGGGGTACCATGGATGCCAGCGCCACAGCCTCCATTAAACTGTCCACCTGGATTAGAA
TATTTAAGTCAGATAGATCAGATACTGATTCATCAGCAAATTGAACTTCTGGAAGTTTTA
ACAGGTTTTGAAACTAATAACAAATATGAAATTAAGAACAGCTTTGGACAGAGGGTTTAC
TTTGCAGCGGAAGATACTGATTGCTGTACCCGAAATTGCTGTGGGCCATCTAGACCTTTT
ACCTTGAGGATTATTGATAATATGGGTCAAGAAGTCATAACTCTGGAGAGACCACTAAGA
TGTAGCAGCTGTTGTTGTCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGT
GTACCAATAGGTTATGTTATTCAGACTTGGCACCCATGTCTACCAAAGTTTACAATTCAA
AATGAGAAAAGAGAGGATGTACTAAAAATAAGTGGTCCATGTGTTGTGTGCAGCTGTTGT
GGAGATGTTGATTTTGAGATTAAATCTCTTGATGAACAGTGTGTGGTTGGCAAAATTTCC
AAGCACTGGACTGGAATTTTGAGAGAGGCATTTACAGACGCTGATAACTTTGGAATCCAG
TTCCCTTTAGACCTTGATGTTAAAATGAAAGCTGTAATGATTGGTGCCTGTTTCCTCATT
GACTTCATGTTTTTTGAAAGCACTGGCAGCCAGGAACAAAAATCAGGAGTGTGGTAG
|
| Enzyme 8 GenBank Gene ID |
AB006746  |
| Enzyme 8 GeneCard ID |
PLSCR1  |
| Enzyme 8 GenAtlas ID |
PLSCR1  |
| Enzyme 8 HGNC ID |
HGNC:9092  |
| Enzyme 8 Chromosome Location |
3 |
| Enzyme 8 Locus |
3q23 |
| Enzyme 8 SNPs |
SNPJam Report  |
| Enzyme 8 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 8 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 9
[top]
|
| Enzyme 9 ID |
7675 |
| Enzyme 9 Name |
Phosphatidylserine synthase 1 |
| Enzyme 9 Synonyms |
- PSS-1
- PtdSer synthase 1
- Serine-exchange enzyme I
|
| Enzyme 9 Gene Name |
PTDSS1 |
| Enzyme 9 Protein Sequence |
>Phosphatidylserine synthase 1
MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTR
DDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLF
LNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKA
LLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFL
EMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLT
ELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVI
GFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECE
DGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK
|
| Enzyme 9 Number of Residues |
473 |
| Enzyme 9 Molecular Weight |
55527.2 |
| Enzyme 9 Theoretical pI |
8.52 |
| Enzyme 9 GO Classification |
| Function |
| — |
| Process |
- glycerophospholipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylserine biosynthetic process
- phosphatidylserine metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 9 General Function |
Involved in phosphatidylserine biosynthetic process |
| Enzyme 9 Specific Function |
Catalyzes a base-exchange reaction in which the polar head group of phosphatidylcholine is replaced by L-serine |
| Enzyme 9 Pathways |
Not Available |
| Enzyme 9 Reactions |
Not Available |
| Enzyme 9 Pfam Domain Function |
|
| Enzyme 9 Signals |
|
| Enzyme 9 Transmembrane Regions |
- 36-56
73-93
103-123
161-181
187-207
217-237
287-307
310-330
356-376
384-404
|
| Enzyme 9 Essentiality |
Not Available |
| Enzyme 9 GenBank ID Protein |
Not Available |
| Enzyme 9 UniProtKB/Swiss-Prot ID |
P48651  |
| Enzyme 9 UniProtKB/Swiss-Prot Entry Name |
PTSS1_HUMAN  |
| Enzyme 9 PDB ID |
Not Available |
| Enzyme 9 Cellular Location |
Not Available |
| Enzyme 9 Gene Sequence |
>1422 bp
ATGGCGTCCTGCGTGGGGAGCCGGACCCTAAGCAAGGATGATGTGAACTACAAAATGCAT
TTCCGGATGATCAACGAGCAGCAAGTGGAGGACATCACCATTGACTTCTTCTACCGGCCG
CATACCATCACCCTGCTCAGCTTCACCATCGTCAGCCTCATGTACTTCGCCTTTACCAGG
GATGACTCTGTTCCAGAAGACAACATCTGGAGAGGCATCCTCTCTGTTATTTTCTTCTTT
CTTATCATCAGTGTGTTAGCTTTCCCCAATGGTCCGTTCACTCGACCTCATCCAGCCTTA
TGGCGAATGGTTTTTGGACTCAGTGTGCTCTACTTCCTGTTCCTGGTATTCCTACTCTTC
CTGAATTTCGAGCAGGTTAAATCTCTAATGTATTGGCTAGATCCAAATCTTCGATACGCC
ACAAGGGAAGCAGATGTCATGGAGTATGCTGTGAACTGCCATGTGATCACCTGGGAGAGG
ATTATCAGCCACTTTGATATTTTTGCATTTGGACATTTCTGGGGCTGGGCCATGAAGGCC
TTGCTGATCCGTAGTTACGGTCTCTGCTGGACAATCAGTATTACCTGGGAGCTGACTGAG
CTCTTCTTCATGCATCTCCTCCCCAATTTTGCCGAGTGCTGGTGGGATCAAGTCATTCTG
GACATCCTGTTGTGCAATGGCGGTGGCATTTGGCTGGGCATGGTCGTTTGCCGGTTTTTA
GAGATGAGGACTTACCACTGGGCAAGCTTCAAGGACATTCATACCACCACCGGGAAGATC
AAGAGAGCTGTTCTGCAGTTCACTCCTGCTAGCTGGACCTATGTTCGATGGTTTGACCCC
AAATCTTCTTTTCAGAGAGTAGCTGGAGTGTACCTTTTCATGATCATCTGGCAGCTGACT
GAGTTGAATACCTTCTTCTTGAAGCATATCTTTGTGTTCCAAGCCAGTCATCCATTAAGT
TGGGGTAGAATTCTCTTTATTGGTGGCATCACAGCTCCCACAGTGAGACAGTACTACGCT
TACCTCACCGACACACAGTGCAAGCGCGTAGGAACACAATGCTGGGTGTTTGGGGTCATT
GGTTTCCTGGAGGCCATTGTTTGCATAAAATTTGGACAAGATCTCTTCTCTAAGACCCAA
ATACTCTATGTTGTGCTTTGGCTTCTTTGCGTGGCTTTCACCACTTTCCTCTGTCTGTAC
GGCATGATTTGGTATGCAGAACACTATGGTCACCGAGAAAAGACCTACTCGGAGTGTGAA
GATGGCACCTACAGTCCAGAGATCTCCTGGCATCACAGGAAAGGGACAAAAGGTTCTGAA
GACAGCCCACCCAAGCATGCAGGCAACAACGAAAGCCATTCTTCCAGGAGAAGGAATCGG
CATTCCAAGTCAAAAGTCACCAATGGCGTTGGAAAGAAATGA
|
| Enzyme 9 GenBank Gene ID |
D14694  |
| Enzyme 9 GeneCard ID |
PTDSS1  |
| Enzyme 9 GenAtlas ID |
PTDSS1  |
| Enzyme 9 HGNC ID |
HGNC:9587  |
| Enzyme 9 Chromosome Location |
8 |
| Enzyme 9 Locus |
8q22 |
| Enzyme 9 SNPs |
SNPJam Report  |
| Enzyme 9 General References |
- Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S: Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. DNA Res. 1994;1(1):27-35. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 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 |
7722 |
| Enzyme 10 Name |
Scavenger receptor class B member 1 |
| Enzyme 10 Synonyms |
- SRB1
- CD36 and LIMPII analogous 1
- CLA-1
- CD36 antigen-like 1
- Collagen type I receptor, thrombospondin receptor-like 1
- SR-BI
- CD36 antigen
|
| Enzyme 10 Gene Name |
SCARB1 |
| Enzyme 10 Protein Sequence |
>Scavenger receptor class B member 1
MGCSAKARWAAGALGVAGLLCAVLGAVMIVMVPSLIKQQVLKNVRIDPSSLSFNMWKEIP
IPFYLSVYFFDVMNPSEILKGEKPQVRERGPYVYREFRHKSNITFNNNDTVSFLEYRTFQ
FQPSKSHGSESDYIVMPNILVLGAAVMMENKPMTLKLIMTLAFTTLGERAFMNRTVGEIM
WGYKDPLVNLINKYFPGMFPFKDKFGLFAELNNSDSGLFTVFTGVQNISRIHLVDKWNGL
SKVDFWHSDQCNMINGTSGQMWPPFMTPESSLEFYSPEACRSMKLMYKESGVFEGIPTYR
FVAPKTLFANGSIYPPNEGFCPCLESGIQNVSTCRFSAPLFLSHPHFLNADPVLAEAVTG
LHPNQEAHSLFLDIHPVTGIPMNCSVKLQLSLYMKSVAGIGQTGKIEPVVLPLLWFAESG
AMEGETLHTFYTQLVLMPKVMHYAQYVLLALGCVLLLVPVICQIRSQVGAGQRAARADSH
SLACWGKGASDRTLWPTAAWSPPPAAVLRLCRSGSGHCWGLRSTLASFACRVATTLPVLE
GLGPSLGGGTGS
|
| Enzyme 10 Number of Residues |
552 |
| Enzyme 10 Molecular Weight |
60877.4 |
| Enzyme 10 Theoretical pI |
8.31 |
| Enzyme 10 GO Classification |
| Function |
| — |
| Process |
- cell adhesion
- cellular process
|
| Component |
|
|
| Enzyme 10 General Function |
Involved in cell adhesion |
| Enzyme 10 Specific Function |
Receptor for different ligands such as phospholipids, cholesterol ester, lipoproteins, phosphatidylserine and apoptotic cells. Probable receptor for HDL, located in particular region of the plasma membrane, called caveolae. Facilitates the flux of free and esterified cholesterol between the cell surface and extracellular donors and acceptors, such as HDL and to a lesser extent, apoB-containing lipoproteins and modified lipoproteins. Probably involved in the phagocytosis of apoptotic cells, via its phosphatidylserine binding activity. Receptor for hepatitis C virus glycoprotein E2. Binding between SCARB1 and E2 was found to be independent of the genotype of the viral isolate. Plays an important role in the uptake of HDL cholesteryl ester |
| Enzyme 10 Pathways |
Not Available |
| Enzyme 10 Reactions |
Not Available |
| Enzyme 10 Pfam Domain Function |
|
| Enzyme 10 Signals |
|
| Enzyme 10 Transmembrane Regions |
|
| Enzyme 10 Essentiality |
Not Available |
| Enzyme 10 GenBank ID Protein |
132566684  |
| Enzyme 10 UniProtKB/Swiss-Prot ID |
Q8WTV0  |
| Enzyme 10 UniProtKB/Swiss-Prot Entry Name |
SCRB1_HUMAN  |
| Enzyme 10 PDB ID |
Not Available |
| Enzyme 10 Cellular Location |
Not Available |
| Enzyme 10 Gene Sequence |
>1530 bp
ATGGGCTGCTCCGCCAAAGCGCGCTGGGCTGCCGGGGCGCTGGGCGTCGCGGGGCTACTG
TGCGCTGTGCTGGGCGCTGTCATGATCGTGATGGTGCCGTCGCTCATCAAGCAGCAGGTC
CTTAAGAACGTGCGCATCGACCCCAGTAGCCTGTCCTTCAACATGTGGAAGGAGATCCCT
ATCCCCTTCTATCTCTCCGTCTACTTCTTTGACGTCATGAACCCCAGCGAGATCCTGAAG
GGCGAGAAGCCGCAGGTGCGGGAGCGCGGGCCCTACGTGTACAGGGAGTTCAGGCACAAA
AGCAACATCACCTTCAACAACAACGACACCGTGTCCTTCCTCGAGTACCGCACCTTCCAG
TTCCAGCCCTCCAAGTCCCACGGCTCGGAGAGCGACTACATCGTCATGCCCAACATCCTG
GTCTTGGGTGCGGCGGTGATGATGGAGAATAAGCCCATGACCCTGAAGCTCATCATGACC
TTGGCATTCACCACCCTCGGCGAACGTGCCTTCATGAACCGCACTGTGGGTGAGATCATG
TGGGGCTACAAGGACCCCCTTGTGAATCTCATCAACAAGTACTTTCCAGGCATGTTCCCC
TTCAAGGACAAGTTCGGATTATTTGCTGAGCTCAACAACTCCGACTCTGGGCTCTTCACG
GTGTTCACGGGGGTCCAGAACATCAGCAGGATCCACCTCGTGGACAAGTGGAACGGGCTG
AGCAAGGTTGACTTCTGGCATTCCGATCAGTGCAACATGATCAATGGAACTTCTGGGCAA
ATGTGGCCGCCCTTCATGACTCCTGAGTCCTCGCTGGAGTTCTACAGCCCGGAGGCCTGC
CGATCCATGAAGCTAATGTACAAGGAGTCAGGGGTGTTTGAAGGCATCCCCACCTATCGC
TTCGTGGCTCCCAAAACCCTGTTTGCCAACGGGTCCATCTACCCACCCAACGAAGGCTTC
TGCCCGTGCCTGGAGTCTGGAATTCAGAACGTCAGCACCTGCAGGTTCAGTGCCCCCTTG
TTTCTCTCCCATCCTCACTTCCTCAACGCTGACCCGGTTCTGGCAGAAGCGGTGACTGGC
CTGCACCCTAACCAGGAGGCACACTCCTTGTTCCTGGACATCCACCCGGTCACGGGAATC
CCCATGAACTGCTCTGTGAAACTGCAGCTGAGCCTCTACATGAAATCTGTCGCAGGCATT
GGACAAACTGGGAAGATTGAGCCTGTGGTCCTGCCGCTGCTCTGGTTTGCAGAGAGCGGG
GCCATGGAGGGGGAGACTCTTCACACATTCTACACTCAGCTGGTGTTGATGCCCAAGGTG
ATGCACTATGCCCAGTACGTCCTCCTGGCGCTGGGCTGCGTCCTGCTGCTGGTCCCTGTC
ATCTGCCAAATCCGGAGCCAAGAGAAATGCTATTTATTTTGGAGTAGTAGTAAAAAGGGC
TCAAAGGATAAGGAGGCCATTCAGGCCTATTCTGAATCCCTGATGACATCAGCTCCCAAG
GGCTCTGTGCTGCAGGAAGCAAAACTGTAG
|
| Enzyme 10 GenBank Gene ID |
Not Available |
| Enzyme 10 GeneCard ID |
SCARB1  |
| Enzyme 10 GenAtlas ID |
SCARB1  |
| Enzyme 10 HGNC ID |
HGNC:1664  |
| Enzyme 10 Chromosome Location |
1 |
| Enzyme 10 Locus |
12q24.31 |
| Enzyme 10 SNPs |
SNPJam Report  |
| Enzyme 10 General References |
- Calvo D, Vega MA: Identification, primary structure, and distribution of CLA-1, a novel member of the CD36/LIMPII gene family. J Biol Chem. 1993 Sep 5;268(25):18929-35. [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
]
- Scarselli E, Ansuini H, Cerino R, Roccasecca RM, Acali S, Filocamo G, Traboni C, Nicosia A, Cortese R, Vitelli A: The human scavenger receptor class B type I is a novel candidate receptor for the hepatitis C virus. EMBO J. 2002 Oct 1;21(19):5017-25. [PubMed
]
- Kawasaki Y, Nakagawa A, Nagaosa K, Shiratsuchi A, Nakanishi Y: Phosphatidylserine binding of class B scavenger receptor type I, a phagocytosis receptor of testicular sertoli cells. J Biol Chem. 2002 Jul 26;277(30):27559-66. Epub 2002 May 16. [PubMed
]
- Bartosch B, Vitelli A, Granier C, Goujon C, Dubuisson J, Pascale S, Scarselli E, Cortese R, Nicosia A, Cosset FL: Cell entry of hepatitis C virus requires a set of co-receptors that include the CD81 tetraspanin and the SR-B1 scavenger receptor. J Biol Chem. 2003 Oct 24;278(43):41624-30. Epub 2003 Aug 11. [PubMed
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
- Tai ES, Adiconis X, Ordovas JM, Carmena-Ramon R, Real J, Corella D, Ascaso J, Carmena R: Polymorphisms at the SRBI locus are associated with lipoprotein levels in subjects with heterozygous familial hypercholesterolemia. Clin Genet. 2003 Jan;63(1):53-8. [PubMed
]
- Morabia A, Cayanis E, Costanza MC, Ross BM, Flaherty MS, Alvin GB, Das K, Gilliam TC: Association of extreme blood lipid profile phenotypic variation with 11 reverse cholesterol transport genes and 10 non-genetic cardiovascular disease risk factors. Hum Mol Genet. 2003 Nov 1;12(21):2733-43. Epub 2003 Sep 9. [PubMed
]
|
| Enzyme 10 Metabolite References |
Not Available |
|
Enzyme 11
[top]
|
| Enzyme 11 ID |
7731 |
| Enzyme 11 Name |
C-X-C motif chemokine 16 |
| Enzyme 11 Synonyms |
- Scavenger receptor for phosphatidylserine and oxidized low density lipoprotein
- SR-PSOX
- Small-inducible cytokine B16
- Transmembrane chemokine CXCL16
|
| Enzyme 11 Gene Name |
CXCL16 |
| Enzyme 11 Protein Sequence |
>C-X-C motif chemokine 16
MGRDLRPGSRVLLLLLLLLLVYLTQPGNGNEGSVTGSCYCGKRISSDSPPSVQFMNRLRK
HLRAYHRCLYYTRFQLLSWSVCGGNKDPWVQELMSCLDLKECGHAYSGIVAHQKHLLPTS
PPISQASEGASSDIHTPAQMLLSTLQSTQRPTLPVGSLSSDKELTRPNETTIHTAGHSLA
AGPEAGENQKQPEKNAGPTARTSATVPVLCLLAIIFILTAALSYVLCKRRRGQSPQSSPD
LPVHYIPVAPDSNT
|
| Enzyme 11 Number of Residues |
254 |
| Enzyme 11 Molecular Weight |
27578.3 |
| Enzyme 11 Theoretical pI |
8.91 |
| Enzyme 11 GO Classification |
Not Available |
| Enzyme 11 General Function |
Involved in chemokine activity |
| Enzyme 11 Specific Function |
Acts as a scavenger receptor on macrophages, which specifically binds to OxLDL (oxidized low density lipoprotein), suggesting that it may be involved in pathophysiology such as atherogenesis. Induces a strong chemotactic response. Induces calcium mobilization. Binds to CXCR6/Bonzo |
| Enzyme 11 Pathways |
Not Available |
| Enzyme 11 Reactions |
Not Available |
| Enzyme 11 Pfam Domain Function |
Not Available |
| Enzyme 11 Signals |
|
| Enzyme 11 Transmembrane Regions |
|
| Enzyme 11 Essentiality |
Not Available |
| Enzyme 11 GenBank ID Protein |
11139544  |
| Enzyme 11 UniProtKB/Swiss-Prot ID |
Q9H2A7  |
| Enzyme 11 UniProtKB/Swiss-Prot Entry Name |
CXL16_HUMAN  |
| Enzyme 11 PDB ID |
Not Available |
| Enzyme 11 Cellular Location |
Not Available |
| Enzyme 11 Gene Sequence |
>765 bp
ATGGGACGGGACTTGCGGCCCGGGTCCCGCGTGCTCCTGCTCCTGCTTCTGCTCCTGCTG
GTGTACCTGACTCAGCCAGGCAATGGCAACGAGGGCAGCGTCACTGGAAGTTGTTATTGT
GGTAAAAGAATTTCTTCCGACTCCCCGCCATCGGTTCAGTTCATGAATCGTCTCCGGAAA
CACCTGAGAGCTTACCATCGGTGTCTATACTACACGAGGTTCCAGCTCCTTTCCTGGAGC
GTGTGTGGGGGCAACAAGGACCCATGGGTTCAGGAATTGATGAGCTGTCTTGATCTCAAA
GAATGTGGACATGCTTACTCGGGGATTGTGGCCCACCAGAAGCATTTACTTCCTACCAGC
CCCCCAATTTCTCAGGCCTCAGAGGGGGCATCTTCAGATATCCACACCCCTGCCCAGATG
CTCCTGTCCACCTTGCAGTCCACTCAGCGCCCCACCCTCCCAGTAGGATCACTGTCCTCG
GACAAAGAGCTCACTCGTCCCAATGAAACCACCATTCACACTGCGGGCCACAGTCTGGCA
GCTGGGCCTGAGGCTGGGGAGAACCAGAAGCAGCCGGAAAAAAATGCTGGTCCCACAGCC
AGGACATCAGCCACAGTGCCGGTCCTGTGCCTCCTGGCCATCATCTTCATCCTCACCGCA
GCCCTTTCCTATGTGCTGTGCAAGAGGAGGAGGGGGCAGTCACCGCAGTCCTCTCCAGAT
CTGCCGGTTCATTATATACCTGTGGCACCTGACTCTAATACCTGA
|
| Enzyme 11 GenBank Gene ID |
AF275260  |
| Enzyme 11 GeneCard ID |
CXCL16  |
| Enzyme 11 GenAtlas ID |
Not Available |
| Enzyme 11 HGNC ID |
Not Available |
| Enzyme 11 Chromosome Location |
1 |
| Enzyme 11 Locus |
17p13 |
| Enzyme 11 SNPs |
SNPJam Report  |
| Enzyme 11 General References |
- Matloubian M, David A, Engel S, Ryan JE, Cyster JG: A transmembrane CXC chemokine is a ligand for HIV-coreceptor Bonzo. Nat Immunol. 2000 Oct;1(4):298-304. [PubMed
]
- Wilbanks A, Zondlo SC, Murphy K, Mak S, Soler D, Langdon P, Andrew DP, Wu L, Briskin M: Expression cloning of the STRL33/BONZO/TYMSTRligand reveals elements of CC, CXC, and CX3C chemokines. J Immunol. 2001 Apr 15;166(8):5145-54. [PubMed
]
- Shimaoka T, Kume N, Minami M, Hayashida K, Kataoka H, Kita T, Yonehara S: Molecular cloning of a novel scavenger receptor for oxidized low density lipoprotein, SR-PSOX, on macrophages. J Biol Chem. 2000 Dec 29;275(52):40663-6. [PubMed
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 11 Metabolite References |
- 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 |
7740 |
| Enzyme 12 Name |
Phosphatidylserine decarboxylase proenzyme |
| Enzyme 12 Synonyms |
- Phosphatidylserine decarboxylase alpha chain
- Phosphatidylserine decarboxylase beta chain
|
| Enzyme 12 Gene Name |
PISD |
| Enzyme 12 Protein Sequence |
>Phosphatidylserine decarboxylase proenzyme
MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPART
MFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLS
RAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPV
CGLHSISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKN
QLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCH
NERVVLTGDWKHGFFSLTAVGATNVGSIRIYFDRDLHTNSPRHSKGSYNDFSFVTHTNRE
GVPMRKGEHLGEFNLGSTIVLIFEAPKDFNFQLKTGQKIRFGEALGSL
|
| Enzyme 12 Number of Residues |
408 |
| Enzyme 12 Molecular Weight |
46572.2 |
| Enzyme 12 Theoretical pI |
9.80 |
| Enzyme 12 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 12 General Function |
Involved in phosphatidylserine decarboxylase activity |
| Enzyme 12 Specific Function |
Phosphatidyl-L-serine = phosphatidylethanolamine + CO(2) |
| Enzyme 12 Pathways |
- Phospholipid Synthesis (map00564
)
- Glycine, Serine and Threonine Metabolism (map00260
)
|
| Enzyme 12 Reactions |
- phosphatidyl-L-serine = phosphatidylethanolamine + CO2 [RN:R02055]
|
| Enzyme 12 Pfam Domain Function |
|
| Enzyme 12 Signals |
|
| Enzyme 12 Transmembrane Regions |
|
| Enzyme 12 Essentiality |
Not Available |
| Enzyme 12 GenBank ID Protein |
13489112  |
| Enzyme 12 UniProtKB/Swiss-Prot ID |
Q9UG56  |
| Enzyme 12 UniProtKB/Swiss-Prot Entry Name |
PISD_HUMAN  |
| Enzyme 12 PDB ID |
Not Available |
| Enzyme 12 Cellular Location |
Not Available |
| Enzyme 12 Gene Sequence |
>1128 bp
ATGATGTGTCAGTCAGAGGCGCGGCAAGGACCAGAGCTCCGCGCGGCGAAATGGTTGCAC
TTCCCCCAGCTGGCCCTGAGGCGGAGGCTGGGGCAGCTGAGCTGCATGTCCAGACCCGCT
CTGAAACTGCGCTCCTGGCCCTTGACCGTCCTCTACTACCTCCTGCCCTTCGGCGCCCTC
AGACCGCTCAGCCGGGTGGGATGGAGGCCCGTAAGCAGGGTGGCTTTGTACAAGTCAGTG
CCAACGCGCTTGCTGTCACGGGCCTGGGGTCGCCTCAATCAGGTGGAGCTGCCACACTGG
CTGCGCAGGCCCGTCTACAGCCTGTACATCTGGACGTTTGGGGTGAACATGAAAGAGGCC
GCTGTGGAGGACCTGCATCACTACCGCAACCTCAGCGAGTTCTTCCGGCGCAAGCTGAAG
CCGCAGGCCCGGCCTGTCTGTGGCCTGCACAGCGTGATTAGCCCATCGGATGGAAGGATC
CTCAACTTTGGGCAGGTGAAGAACTGTGAGGTGGAGCAGGTAAAGGGGGTCACCTACTCC
CTGGAGTCGTTCCTGGGCCCGCGTATGTGCACAGAGGACCTGCCCTTCCCACCAGCCGCG
TCGTGTGACTCCTTCAAGAACCAGCTGGTCACCCGGGAAGGGAATGAGCTCTATCACTGT
GTCATCTACCTGGCCCCTGGGGACTACCACTGCTTCCACTCCCCCACCGACTGGACTGTG
TCCCACCGGCGCCACTTCCCAGGCTCCCTGATGTCAGTGAACCCTGGCATGGCTCGCTGG
ATCAAAGAGCTCTTCTGCCATAACGAGCGGGTGGTCCTGACGGGGGACTGGAAACATGGC
TTCTTCTCACTGACAGCTGTGGGGGCCACCAACGTGGGCTCCATTCGCATCTACTTTGAC
CGGGACCTGCACACAAACAGCCCAAGGCACAGCAAGGGCTCCTACAATGACTTCAGCTTC
GTGACGCACACCAATAGAGAGGGCGTCCCCATGCGTAAGGGCGAGCACCTGGGCGAGTTC
AACCTGGGCTCCACCATCGTGCTCATCTTCGAGGCCCCCAAGGACTTCAATTTCCAGCTG
AAAACAGGACAGAAAATCCGCTTTGGGGAAGCCCTGGGCTCGCTCTAG
|
| Enzyme 12 GenBank Gene ID |
NM_014338  |
| Enzyme 12 GeneCard ID |
PISD  |
| Enzyme 12 GenAtlas ID |
PISD  |
| Enzyme 12 HGNC ID |
HGNC:8999  |
| Enzyme 12 Chromosome Location |
2 |
| Enzyme 12 Locus |
22q12.2 |
| Enzyme 12 SNPs |
SNPJam Report  |
| Enzyme 12 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 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 |
8142 |
| Enzyme 13 Name |
Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6 |
| Enzyme 13 Synonyms |
- Histone arginine demethylase JMJD6
- JmjC domain-containing protein 6
- Jumonji domain-containing protein 6
- Lysyl-hydroxylase JMJD6
- Peptide-lysine 5-dioxygenase JMJD6
- Phosphatidylserine receptor
- Protein PTDSR
|
| Enzyme 13 Gene Name |
JMJD6 |
| Enzyme 13 Protein Sequence |
>Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFV
ERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEY
MESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPP
RSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIY
PRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHK
TVRGRPKLSRKWYRILKQEHPELAVLADSVDLQESTGIASDSSSDSSSSSSSSSSDSDSE
CESGSEGDGTVHRRKKRRTCSMVGNGDTTSQDDCVSKERSSSR
|
| Enzyme 13 Number of Residues |
403 |
| Enzyme 13 Molecular Weight |
46461.6 |
| Enzyme 13 Theoretical pI |
8.98 |
| Enzyme 13 GO Classification |
Not Available |
| Enzyme 13 General Function |
Involved in histone demethylase activity (H3-R2 specific) |
| Enzyme 13 Specific Function |
Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase. Arginine demethylase which demethylates histone H3 at 'Arg-2' (H3R2me) and histone H4 at 'Arg-3' (H4R3me), thereby playing a central role in histone code. Also acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Acts as a regulator of RNA splicing by mediating 5- hydroxylation of U2AF2/U2AF65, affecting the pre-mRNA splicing activity of U2AF2/U2AF65. Required for differentiation of multiple organs during embryogenesis. Probably acts as a key regulator of hematopoietic differentiation. Seems to be necessary for the regulation of macrophage cytokine responses |
| Enzyme 13 Pathways |
Not Available |
| Enzyme 13 Reactions |
Not Available |
| Enzyme 13 Pfam Domain Function |
|
| Enzyme 13 Signals |
|
| Enzyme 13 Transmembrane Regions |
|
| Enzyme 13 Essentiality |
Not Available |
| Enzyme 13 GenBank ID Protein |
125988389  |
| Enzyme 13 UniProtKB/Swiss-Prot ID |
Q6NYC1  |
| Enzyme 13 UniProtKB/Swiss-Prot Entry Name |
JMJD6_HUMAN  |
| Enzyme 13 PDB ID |
Not Available |
| Enzyme 13 Cellular Location |
Not Available |
| Enzyme 13 Gene Sequence |
>1212 bp
ATGAACCACAAGAGCAAGAAGCGCATCCGCGAGGCCAAGCGGAGTGCGCGGCCGGAGCTC
AAGGACTCGCTGGATTGGACCCGGCACAACTACTACGAGAGCTTCTCGCTGAGCCCGGCG
GCCGTGGCGGATAACGTGGAAAGGGCAGATGCTTTACAGCTGTCTGTGGAAGAATTTGTG
GAGCGGTATGAAAGACCTTACAAGCCCGTGGTTTTGTTGAATGCGCAAGAGGGCTGGTCT
GCGCAGGAGAAATGGACTCTGGAGCGCCTAAAAAGGAAATATCGGAACCAGAAGTTCAAG
TGTGGTGAGGATAACGATGGCTACTCAGTGAAGATGAAGATGAAATACTACATCGAGTAC
ATGGAGAGCACTCGAGATGATAGTCCCCTTTACATCTTTGACAGCAGCTATGGTGAACAC
CCTAAAAGAAGGAAACTTTTGGAAGACTACAAGGTGCCAAAGTTTTTCACTGATGACCTT
TTCCAGTATGCTGGGGAGAAGCGCAGGCCCCCTTACAGGTGGTTTGTGATGGGGCCACCA
CGCTCCGGAACTGGGATTCACATCGACCCTCTGGGAACCAGTGCCTGGAATGCCTTAGTT
CAGGGCCACAAGCGCTGGTGCCTGTTTCCTACCAGCACTCCCAGGGAACTCATCAAAGTG
ACCCGAGACGAAGGAGGGAACCAGCAAGACGAAGCTATTACCTGGTTTAATGTTATTTAT
CCCCGGACACAGCTTCCAACCTGGCCACCTGAATTCAAACCCCTGGAAATCTTACAAAAA
CCAGGAGAGACTGTCTTTGTACCAGGAGGCTGGTGGCATGTTGTCCTCAATCTCGACACT
ACTATCGCCATCACCCAAAATTTTGCCAGCAGCACCAACTTCCCTGTGGTATGGCACAAG
ACGGTAAGAGGGAGACCAAAGTTATCAAGGAAATGGTATAGGATTTTGAAGCAAGAGCAC
CCCGAGTTGGCAGTCCTCGCAGACTCGGTTGACCTTCAGGAGTCCACAGGGATAGCTTCC
GACAGCTCCAGCGACTCTTCCAGCTCCTCCAGCTCCAGTTCGTCAGACTCCGACTCAGAG
TGCGAGTCTGGATCCGAGGGCGATGGGACAGTGCACCGCAGGAAGAAGAGGAGGACGTGC
AGCATGGTGGGAAACGGGGACACCACCTCCCAGGACGACTGTGTCAGCAAAGAGCGCAGC
TCCTCCAGGTGA
|
| Enzyme 13 GenBank Gene ID |
NM_015167.2  |
| Enzyme 13 GeneCard ID |
JMJD6  |
| Enzyme 13 GenAtlas ID |
JMJD6  |
| Enzyme 13 HGNC ID |
HGNC:19355  |
| Enzyme 13 Chromosome Location |
1 |
| Enzyme 13 Locus |
17q25 |
| Enzyme 13 SNPs |
SNPJam Report  |
| Enzyme 13 General References |
- 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
]
- 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
]
- Cui P, Qin B, Liu N, Pan G, Pei D: Nuclear localization of the phosphatidylserine receptor protein via multiple nuclear localization signals. Exp Cell Res. 2004 Feb 1;293(1):154-63. [PubMed
]
- Cao WM, Murao K, Imachi H, Hiramine C, Abe H, Yu X, Dobashi H, Wong NC, Takahara J, Ishida T: Phosphatidylserine receptor cooperates with high-density lipoprotein receptor in recognition of apoptotic cells by thymic nurse cells. J Mol Endocrinol. 2004 Apr;32(2):497-505. [PubMed
]
- Koninger J, Balaz P, Wagner M, Shi X, Cima I, Zimmermann A, di Sebastiano P, Buchler MW, Friess H: Phosphatidylserine receptor in chronic pancreatitis: evidence for a macrophage independent role. Ann Surg. 2005 Jan;241(1):144-51. [PubMed
]
- Chang B, Chen Y, Zhao Y, Bruick RK: JMJD6 is a histone arginine demethylase. Science. 2007 Oct 19;318(5849):444-7. [PubMed
]
- Webby CJ, Wolf A, Gromak N, Dreger M, Kramer H, Kessler B, Nielsen ML, Schmitz C, Butler DS, Yates JR 3rd, Delahunty CM, Hahn P, Lengeling A, Mann M, Proudfoot NJ, Schofield CJ, Bottger A: Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing. Science. 2009 Jul 3;325(5936):90-3. [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 |
8475 |
| Enzyme 14 Name |
Phosphatidylserine synthase 2 |
| Enzyme 14 Synonyms |
- PSS-2
- PtdSer synthase 2
- Serine-exchange enzyme II
|
| Enzyme 14 Gene Name |
PTDSS2 |
| Enzyme 14 Protein Sequence |
>Phosphatidylserine synthase 2
MRRGERRDAGGPRPESPVPAGRASLEEPPDGPSAGQATGPGEGRRSTESEVYDDGTNTFF
WRAHTLTVLFILTCTLGYVTLLEETPQDTAYNTKRGIVASILVFLCFGVTQAKDGPFSRP
HPAYWRFWLCVSVVYELFLIFILFQTVQDGRQFLKYVDPKLGVPLPERDYGGNCLIYDPD
NETDPFHNIWDKLDGFVPAHFLGWYLKTLMIRDWWMCMIISVMFEFLEYSLEHQLPNFSE
CWWDHWIMDVLVCNGLGIYCGMKTLEWLSLKTYKWQGLWNIPTYKGKMKRIAFQFTPYSW
VRFEWKPASSLRRWLAVCGIILVFLLAELNTFYLKFVLWMPPEHYLVLLRLVFFVNVGGV
AMREIYDFMDDPKPHKKLGPQAWLVAAITATELLIVVKYDPHTLTLSLPFYISQCWTLGS
VLALTWTVWRFFLRDITLRYKETRWQKWQNKDDQGSTVGNGDQHPLGLDEDLLGPGVAEG
EGAPTPN
|
| Enzyme 14 Number of Residues |
487 |
| Enzyme 14 Molecular Weight |
56252.5 |
| Enzyme 14 Theoretical pI |
6.19 |
| Enzyme 14 GO Classification |
| Function |
| — |
| Process |
- glycerophospholipid metabolic process
- metabolic process
- organophosphate metabolic process
- phosphatidylserine biosynthetic process
- phosphatidylserine metabolic process
- phospholipid metabolic process
|
| Component |
| — |
|
| Enzyme 14 General Function |
Involved in phosphatidylserine biosynthetic process |
| Enzyme 14 Specific Function |
Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine is replaced by L-serine |
| Enzyme 14 Pathways |
Not Available |
| Enzyme 14 Reactions |
Not Available |
| Enzyme 14 Pfam Domain Function |
|
| Enzyme 14 Signals |
|
| Enzyme 14 Transmembrane Regions |
- 63-83
97-117
127-147
242-262
314-334
336-356
377-397
404-424
|
| Enzyme 14 Essentiality |
Not Available |
| Enzyme 14 GenBank ID Protein |
21740008  |
| Enzyme 14 UniProtKB/Swiss-Prot ID |
Q9BVG9  |
| Enzyme 14 UniProtKB/Swiss-Prot Entry Name |
PTSS2_HUMAN  |
| Enzyme 14 PDB ID |
Not Available |
| Enzyme 14 Cellular Location |
Not Available |
| Enzyme 14 Gene Sequence |
>1464 bp
ATGCGGAGGGGCGAGCGCAGGGACGCCGGAGGTCCGCGGCCCGAGTCCCCGGTGCCCGCG
GGCAGGGCCTCGCTGGAGGAGCCGCCTGACGGGCCGTCTGCCGGCCAAGCCACCGGGCCG
GGCGAGGGCCGCCGCAGCACCGAGTCCGAGGTCTACGACGACGGCACCAACACCTTCTTC
TGGCGAGCCCACACCTTAACCGTGCTCTTCATCCTCACCTGTACGCTTGGCTATGTGACG
CTGCTGGAGGAAACACCTCAGGACACGGCCTACAACACCAAGAGAGGTATTGTGGCCAGT
ATTTTGGTTTTCTTATGTTTTGGAGTCACACAAGCTAAAGACGGGCCATTTTCCAGACCT
CATCCAGCTTACTGGAGGTTTTGGCTCTGCGTGAGTGTGGTCTACGAGCTGTTTCTCATC
TTTATACTCTTCCAGACTGTCCAGGACGGCCGGCAGTTTCTAAAGTATGTTGACCCCAAG
CTGGGAGTCCCACTGCCAGAGAGAGACTACGGGGGAAACTGCCTCATCTACGACCCAGAC
AATGAGACTGACCCCTTTCACAACATCTGGGACAAGTTGGATGGCTTTGTTCCCGCGCAC
TTTCTTGGCTGGTACCTGAAGACCCTGATGATCCGAGACTGGTGGATGTGCATGATCATC
AGCGTGATGTTCGAGTTCCTGGAGTACAGCCTGGAGCACCAGCTGCCCAACTTCAGCGAG
TGCTGGTGGGATCACTGGATCATGGACGTGCTCGTCTGCAACGGGCTGGGCATCTACTGC
GGCATGAAGACCCTTGAGTGGCTGTCCCTGAAGACGTACAAGTGGCAGGGCCTCTGGAAC
ATTCCGACCTACAAGGGCAAGATGAAGAGGATCGCCTTCCAGTTCACGCCGTACAGCTGG
GTTCGCTTCGAGTGGAAGCCGGCCTCCAGCCTGCGTCGCTGGCTGGCCGTGTGCGGCATC
ATCCTGGTGTTCCTGTTGGCAGAACTGAACACGTTCTACCTGAAGTTTGTGCTGTGGATG
CCCCCGGAGCACTACCTGGTCCTCCTGCGGCTCGTCTTCTTCGTGAACGTGGGTGGCGTG
GCCATGCGTGAGATCTACGACTTCATGGATGACCCGAAGCCCCACAAGAAGCTGGGCCCG
CAGGCCTGGCTGGTGGCGGCCATCACGGCCACGGAGCTGCTCATCGTGGTGAAGTACGAC
CCCCACACGCTCACCCTGTCCCTGCCCTTCTACATCTCCCAGTGCTGGACCCTCGGCTCC
GTCCTGGCGCTCACCTGGACCGTCTGGCGCTTCTTCCTGCGGGACATCACATTGAGGTAC
AAGGAGACCCGGTGGCAGAAGTGGCAGAACAAGGATGACCAGGGCAGCACCGTCGGCAAC
GGGGACCAGCACCCACTGGGGCTGGACGAAGACCTGCTGGGGCCTGGGGTGGCCGAGGGC
GAGGGAGCACCAACTCCAAACTGA
|
| Enzyme 14 GenBank Gene ID |
AL834357  |
| Enzyme 14 GeneCard ID |
PTDSS2  |
| Enzyme 14 GenAtlas ID |
PTDSS2  |
| Enzyme 14 HGNC ID |
HGNC:15463  |
| Enzyme 14 Chromosome Location |
1 |
| Enzyme 14 Locus |
11p15.5 |
| Enzyme 14 SNPs |
SNPJam Report  |
| Enzyme 14 General References |
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- 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
]
- 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
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- 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
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- 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
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
|
| Enzyme 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 |
8626 |
| Enzyme 15 Name |
2-acylglycerol O-acyltransferase 2 |
| Enzyme 15 Synonyms |
- Acyl-CoA:monoacylglycerol acyltransferase 2
- MGAT2
- hMGAT2
- Diacylglycerol O-acyltransferase candidate 5
- hDC5
- Diacylglycerol acyltransferase 2-like protein 5
- Monoacylglycerol O-acyltransferase 2
|
| Enzyme 15 Gene Name |
MOGAT2 |
| Enzyme 15 Protein Sequence |
>2-acylglycerol O-acyltransferase 2
MVEFAPLFMPWERRLQTLAVLQFVFSFLALAEICTVGFIALLFTRFWLLTVLYAAWWYLD
RDKPRQGGRHIQAIRCWTIWKYMKDYFPISLVKTAELDPSRNYIAGFHPHGVLAVGAFAN
LCTESTGFSSIFPGIRPHLMMLTLWFRAPFFRDYIMSAGLVTSEKESAAHILNRKGGGNL
LGIIVGGAQEALDARPGSFTLLLRNRKGFVRLALTHGAPLVPIFSFGENDLFDQIPNSSG
SWLRYIQNRLQKIMGISLPLFHGRGVFQYSFGLIPYRRPITTVVGKPIEVQKTLHPSEEE
VNQLHQRYIKELCNLFEAHKLKFNIPADQHLEFC
|
| Enzyme 15 Number of Residues |
334 |
| Enzyme 15 Molecular Weight |
38195.3 |
| Enzyme 15 Theoretical pI |
9.77 |
| Enzyme 15 GO Classification |
| Function |
- catalytic activity
- transferase activity
- transferase activity, transferring acyl groups
- transferase activity, transferring acyl groups other than amino-acyl groups
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 15 General Function |
Involved in transferase activity, transferring acyl groups other than amino-acyl groups |
| Enzyme 15 Specific Function |
Catalyzes the formation of diacylglycerol from 2- monoacylglycerol and fatty acyl-CoA. Has a preference toward monoacylglycerols containing unsaturated fatty acids in an order of C18:3 > C18:2 > C18:1 > C18:0. Plays a central role in absorption of dietary fat in the small intestine by catalyzing the resynthesis of triacylglycerol in enterocytes. May play a role in diet-induced obesity |
| Enzyme 15 Pathways |
|
| Enzyme 15 Reactions |
- acyl-CoA + 2-acylglycerol = CoA + diacylglycerol [RN:R01368]
|
| Enzyme 15 Pfam Domain Function |
|
| Enzyme 15 Signals |
|
| Enzyme 15 Transmembrane Regions |
|
| Enzyme 15 Essentiality |
Not Available |
| Enzyme 15 GenBank ID Protein |
37537527  |
| Enzyme 15 UniProtKB/Swiss-Prot ID |
Q3SYC2  |
| Enzyme 15 UniProtKB/Swiss-Prot Entry Name |
MOGT2_HUMAN  |
| Enzyme 15 PDB ID |
Not Available |
| Enzyme 15 Cellular Location |
Not Available |
| Enzyme 15 Gene Sequence |
>1005 bp
ATGGTAGAGTTCGCGCCCTTGTTTATGCCGTGGGAGCGCAGGCTGCAGACACTTGCTGTC
CTACAGTTTGTCTTCTCCTTCTTGGCACTGGCCGAGATCTGCACTGTGGGCTTCATAGCC
CTCCTGTTTACAAGATTCTGGCTCCTCACTGTCCTGTATGCGGCCTGGTGGTATCTGGAC
CGAGACAAGCCACGGCAGGGGGGCCGGCACATCCAGGCCATCAGGTGCTGGACTATATGG
AAGTACATGAAGGACTATTTCCCCATCTCGCTGGTCAAGACTGCTGAGCTGGACCCCTCT
CGGAACTACATTGCGGGCTTCCACCCCCATGGAGTCCTGGCAGTCGGAGCCTTTGCCAAC
CTGTGCACTGAGAGCACAGGCTTCTCTTCGATCTTCCCCGGTATCCGCCCCCATCTGATG
ATGCTGACCTTGTGGTTCCGGGCCCCCTTCTTCAGAGATTACATCATGTCTGCAGGGTTG
GTCACATCAGAAAAGGAGAGTGCTGCTCACATTCTGAACAGGAAGGGTGGCGGAAACTTG
CTGGGCATCATTGTAGGGGGTGCCCAGGAGGCCCTGGATGCCAGGCCTGGATCCTTCACG
CTGTTACTGCGGAACCGAAAGGGCTTCGTCAGGCTCGCCCTGACACACGGGGCACCCCTG
GTGCCAATCTTCTCCTTCGGGGAGAATGACCTATTTGACCAGATTCCCAACTCTTCTGGC
TCCTGGTTACGCTATATCCAGAATCGGTTGCAGAAGATCATGGGCATCTCCCTCCCACTC
TTTCATGGCCGTGGTGTCTTCCAGTACAGCTTTGGTTTAATACCCTACCGCCGGCCCATC
ACCACTGTGGTGGGGAAGCCCATCGAGGTACAGAAGACGCTGCATCCCTCGGAGGAGGAG
GTGAACCAGCTGCACCAGCGTTATATCAAAGAGCTGTGCAACCTCTTCGAGGCCCACAAA
CTTAAGTTCAACATCCCTGCTGACCAGCACTTGGAGTTCTGCTGA
|
| Enzyme 15 GenBank Gene ID |
NM_025098.2  |
| Enzyme 15 GeneCard ID |
MOGAT2  |
| Enzyme 15 GenAtlas ID |
MOGAT2  |
| Enzyme 15 HGNC ID |
HGNC:23248  |
| Enzyme 15 Chromosome Location |
1 |
| Enzyme 15 Locus |
11q13.5 |
| Enzyme 15 SNPs |
SNPJam Report  |
| Enzyme 15 General References |
- Yen CL, Farese RV Jr: MGAT2, a monoacylglycerol acyltransferase expressed in the small intestine. J Biol Chem. 2003 May 16;278(20):18532-7. Epub 2003 Mar 5. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Lockwood JF, Cao J, Burn P, Shi Y: Human intestinal monoacylglycerol acyltransferase: differential features in tissue expression and activity. Am J Physiol Endocrinol Metab. 2003 Nov;285(5):E927-37. Epub 2003 Jun 24. [PubMed
]
|
| Enzyme 15 Metabolite References |
Not Available |
|
Enzyme 16
[top]
|
| Enzyme 16 ID |
8662 |
| Enzyme 16 Name |
Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha |
| Enzyme 16 Synonyms |
- PI3K-C2-alpha
- PtdIns-3-kinase C2 subunit alpha
- Phosphoinositide 3-kinase-C2-alpha
|
| Enzyme 16 Gene Name |
PIK3C2A |
| Enzyme 16 Protein Sequence |
>Phosphatidylinositol-4-phosphate 3-kinase C2 domain-containing subunit alpha
MAQISSNSGFKECPSSHPEPTRAKDVDKEEALQMEAEALAKLQKDRQVTDNQRGFELSSS
TRKKAQVYNKQDYDLMVFPESDSQKRALDIDVEKLTQAELEKLLLDDSFETKKTPVLPVT
PILSPSFSAQLYFRPTIQRGQWPPGLPGPSTYALPSIYPSTYSKQAAFQNGFNPRMPTFP
STEPIYLSLPGQSPYFSYPLTPATPFHPQGSLPIYRPVVSTDMAKLFDKIASTSEFLKNG
KARTDLEITDSKVSNLQVSPKSEDISKFDWLDLDPLSKPKVDNVEVLDHEEEKNVSSLLA
KDPWDAVLLEERSTANCHLERKVNGKSLSVATVTRSQSLNIRTTQLAKAQGHISQKDPNG
TSSLPTGSSLLQEVEVQNEEMAAFCRSITKLKTKFPYTNHRTNPGYLLSPVTAQRNICGE
NASVKVSIDIEGFQLPVTFTCDVSSTVEIIIMQALCWVHDDLNQVDVGSYVLKVCGQEEV
LQNNHCLGSHEHIQNCRKWDTEIRLQLLTFSAMCQNLARTAEDDETPVDLNKHLYQIEKP
CKEAMTRHPVEELLDSYHNQVELALQIENQHRAVDQVIKAVRKICSALDGVETLAITESV
KKLKRAVNLPRSKTADVTSLFGGEDTSRSSTRGSLNPENPVQVSINQLTAAIYDLLRLHA
NSGRSPTDCAQSSKSVKEAWTTTEQLQFTIFAAHGISSNWVSNYEKYYLICSLSHNGKDL
FKPIQSKKVGTYKNFFYLIKWDELIIFPIQISQLPLESVLHLTLFGILNQSSGSSPDSNK
QRKGPEALGKVSLPLFDFKRFLTCGTKLLYLWTSSHTNSVPGTVTKKGYVMERIVLQVDF
PSPAFDIIYTTPQVDRSIIQQHNLETLENDIKGKLLDILHKDSSLGLSKEDKAFLWEKRY
YCFKHPNCLPKILASAPNWKWVNLAKTYSLLHQWPALYPLIALELLDSKFADQEVRSLAV
TWIEAISDDELTDLLPQFVQALKYEIYLNSSLVQFLLSRALGNIQIAHNLYWLLKDALHD
VQFSTRYEHVLGALLSVGGKRLREELLKQTKLVQLLGGVAEKVRQASGSARQVVLQRSME
RVQSFFQKNKCRLPLKPSLVAKELNIKSCSFFSSNAVPLKVTMVNADPMGEEINVMFKVG
EDLRQDMLALQMIKIMDKIWLKEGLDLRMVIFKCLSTGRDRGMVELVPASDTLRKIQVEY
GVTGSFKDKPLAEWLRKYNPSEEEYEKASENFIYSCAGCCVATYVLGICDRHNDNIMLRS
TGHMFHIDFGKFLGHAQMFGSFKRDRAPFVLTSDMAYVINGGEKPTIRFQLFVDLCCQAY
NLIRKQTNLFLNLLSLMIPSGLPELTSIQDLKYVRDALQPQTTDAEATIFFTRLIESSLG
SIATKFNFFIHNLAQLRFSGLPSNDEPILSFSPKTYSFRQDGRIKEVSVFTYHKKYNPDK
HYIYVVRILREGQIEPSFVFRTFDEFQELHNKLSIIFPLWKLPGFPNRMVLGRTHIKDVA
AKRKIELNSYLQSLMNASTDVAECDLVCTFFHPLLRDEKAEGIARSADAGSFSPTPGQIG
GAVKLSISYRNGTLFIMVMHIKDLVTEDGADPNPYVKTYLLPDNHKTSKRKTKISRKTRN
PTFNEMLVYSGYSKETLRQRELQLSVLSAESLRENFFLGGVTLPLKDFNLSKETVKWYQL
TAATYL
|
| Enzyme 16 Number of Residues |
1686 |
| Enzyme 16 Molecular Weight |
190677.8 |
| Enzyme 16 Theoretical pI |
8.10 |
| Enzyme 16 GO Classification |
| Function |
- 1-phosphatidylinositol-3-kinase activity
- binding
- catalytic activity
- inositol or phosphatidylinositol kinase activity
- kinase activity
- lipid binding
- lipid kinase activity
- phosphoinositide 3-kinase activity
- phosphoinositide binding
- phospholipid binding
- phosphotransferase activity, alcohol group as acceptor
- protein binding
- transferase activity
- transferase activity, transferring phosphorus-containing groups
|
| Process |
- biological regulation
- cell communication
- cellular process
- glycerophospholipid metabolic process
- intracellular signal transduction
- metabolic process
- organophosphate metabolic process
- phosphoinositide metabolic process
- phosphoinositide phosphorylation
- phosphoinositide-mediated signaling
- phospholipid metabolic process
- regulation of biological process
- regulation of cellular process
- second-messenger-mediated signaling
- signal transduction
|
| Component |
- macromolecular complex
- phosphoinositide 3-kinase complex
- protein complex
|
|
| Enzyme 16 General Function |
Involved in binding |
| Enzyme 16 Specific Function |
Phosphorylates PtdIns, PtdIns4P and PtdIns(4,5)P2. May play a role in clathrin-coated endocytic vesicle formation and EGF signaling cascade. May be involved in mitosis and UV-induced damage response. May be a downstream effector in insulin signaling cascade |
| Enzyme 16 Pathways |
- Phosphatidylinositol signaling system (map04070
)
|
| Enzyme 16 Reactions |
- ATP + 1-phosphatidyl-1D-myo-inositol 4-phosphate = ADP + 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate [RN:R05795]
|
| Enzyme 16 Pfam Domain Function |
|
| Enzyme 16 Signals |
|
| Enzyme 16 Transmembrane Regions |
|
| Enzyme 16 Essentiality |
Not Available |
| Enzyme 16 GenBank ID Protein |
109731357  |
| Enzyme 16 UniProtKB/Swiss-Prot ID |
O00443  |
| Enzyme 16 UniProtKB/Swiss-Prot Entry Name |
P3C2A_HUMAN  |
| Enzyme 16 PDB ID |
Not Available |
| Enzyme 16 Cellular Location |
Not Available |
| Enzyme 16 Gene Sequence |
>5061 bp
ATGGCTCAGATATCTAGCAACAGCGGATTTAAAGAATGTCCATCTTCACATCCGGAACCA
ACAAGAGCAAAAGATGTGGACAAAGAAGAAGCATTACAGATGGAAGCAGAGGCTTTAGCA
AAACTGCAAAAGGATAGACAAGTGACTGACAATCAGAGAGGCTTTGAGTTGTCAAGCAGC
ACCAGAAAAAAAGCACAGGTTTATAACAAGCAGGATTATGATCTCATGGTGTTTCCTGAA
TCAGATTCCCAAAAAAGAGCATTAGATATTGATGTAGAAAAGCTCACCCAAGCTGAACTT
GAGAAACTATTGCTGGATGACAGTTTCGAGACTAAAAAAACACCTGTATTACCAGTTACT
CCTATTCTGAGCCCTTCCTTTTCAGCACAGCTCTATTTTAGACCTACTATTCAGAGAGGA
CAGTGGCCACCTGGATTACCTGGGCCTTCCACTTATGCTTTACCTTCTATTTATCCTTCT
ACTTACAGTAAACAGGCTGCATTCCAAAATGGCTTCAATCCAAGAATGCCCACTTTTCCA
TCTACAGAACCTATATATTTAAGTCTTCCGGGACAATCTCCATATTTCTCATATCCTTTG
ACACCTGCCACACCCTTTCATCCACAAGGAAGCTTACCTATCTATCGTCCAGTAGTCAGT
ACTGACATGGCAAAACTATTTGACAAAATAGCTAGTACATCAGAATTTTTAAAAAATGGG
AAAGCAAGGACTGATTTGGAGATAACAGATTCAAAAGTCAGCAATCTACAGGTATCTCCA
AAGTCTGAGGATATCAGTAAATTTGACTGGTTAGACTTGGATCCTCTAAGTAAGCCTAAG
GTGGATAATGTGGAGGTATTAGACCATGAGGAAGAGAAAAATGTTTCAAGTTTGCTAGCA
AAGGATCCTTGGGATGCTGTTCTTCTTGAAGAGAGATCGACAGCAAATTGTCATCTTGAA
AGAAAGGTGAATGGAAAATCCCTTTCTGTGGCAACTGTTACAAGAAGCCAGTCTTTAAAT
ATTCGAACAACTCAGCTTGCAAAAGCCCAGGGCCATATATCTCAGAAAGACCCAAATGGG
ACCAGTAGTTTGCCAACTGGAAGTTCTCTTCTTCAAGAAGTTGAAGTACAGAATGAGGAG
ATGGCAGCTTTTTGTCGATCCATTACAAAATTGAAGACCAAATTTCCATATACCAATCAC
CGCACAAACCCAGGCTATTTGTTAAGTCCAGTCACAGCGCAAAGAAACATATGCGGAGAA
AATGCTAGTGTGAAGGTCTCCATTGACATTGAAGGATTTCAGCTACCAGTTACTTTTACG
TGTGATGTGAGTTCTACTGTAGAAATCATTATAATGCAAGCCCTTTGCTGGGTACATGAT
GACTTGAATCAAGTAGATGTTGGCAGCTATGTTCTAAAAGTTTGTGGTCAAGAGGAAGTG
CTGCAGAATAATCATTGCCTTGGAAGTCATGAGCATATTCAAAACTGTCGAAAATGGGAC
ACAGAAATTAGACTACAACTCTTGACCTTCAGTGCAATGTGTCAAAATCTGGCCCGAACA
GCAGAAGATGATGAAACACCCGTGGATTTAAACAAACACCTGTATCAAATAGAAAAACCT
TGCAAAGAAGCCATGACGAGACACCCTGTTGAAGAACTCTTAGATTCTTATCACAACCAA
GTAGAACTGGCTCTTCAAATTGAAAACCAACACCGAGCAGTAGATCAAGTAATTAAAGCT
GTAAGAAAAATCTGTAGTGCTTTAGATGGTGTCGAGACTCTTGCCATTACAGAATCAGTA
AAGAAGCTAAAGAGAGCAGTTAATCTTCCAAGGAGTAAAACTGCTGATGTGACTTCTTTG
TTTGGAGGAGAAGACACTAGCAGGAGTTCAACTAGGGGCTCACTTAATCCTGAAAATCCT
GTTCAAGTAAGCATAAACCAATTAACTGCAGCAATTTATGATCTTCTCAGACTCCATGCA
AATTCTGGTAGGAGTCCTACAGACTGTGCCCAAAGTAGCAAGAGTGTCAAGGAAGCATGG
ACTACAACAGAGCAGCTCCAGTTTACTATTTTTGCTGCTCATGGAATTTCAAGTAATTGG
GTATCAAATTATGAAAAATACTACTTGATATGTTCACTGTCTCACAATGGAAAGGATCTT
TTTAAACCTATTCAATCAAAGAAGGTTGGCACTTACAAGAATTTCTTCTATCTTATTAAA
TGGGATGAACTAATCATTTTTCCTATCCAGATATCACAATTGCCATTAGAATCAGTTCTT
CACCTTACTCTTTTTGGAATTTTAAATCAGAGCAGTGGAAGTTCCCCTGATTCTAATAAG
CAGAGAAAGGGACCAGAAGCTTTGGGCAAAGTTTCTTTACCTCTTTTTGACTTTAAACGG
TTTTTAACATGTGGAACTAAACTTCTATATCTTTGGACTTCATCACATACAAATTCTGTT
CCTGGAACAGTTACCAAAAAAGGATATGTCATGGAAAGAATAGTGCTACAGGTTGATTTT
CCTTCTCCTGCATTTGATATTATTTATACAACTCCTCAAGTTGACAGAAGCATTATACAG
CAACATAACTTAGAAACACTAGAGAATGATATAAAAGGGAAACTTCTTGATATTCTTCAT
AAAGACTCATCACTTGGACTTTCTAAAGAAGATAAAGCTTTTTTATGGGAGAAACGTTAT
TATTGCTTCAAACACCCAAATTGTCTTCCTAAAATATTAGCAAGCGCCCCAAACTGGAAA
TGGGTTAATCTTGCCAAAACTTACTCATTGCTTCACCAGTGGCCTGCATTGTACCCACTA
ATTGCATTGGAACTTCTTGATTCAAAATTTGCTGATCAGGAAGTAAGATCCCTAGCTGTG
ACCTGGATTGAGGCCATTAGTGATGATGAGCTAACAGATCTTCTTCCACAGTTTGTACAA
GCTTTGAAATATGAAATTTACTTGAATAGTTCATTAGTGCAATTCCTTTTGTCCAGGGCA
TTGGGAAATATCCAGATAGCACACAATTTATATTGGCTTCTCAAAGATGCCCTGCATGAT
GTACAGTTTAGTACCCGATACGAACATGTTTTGGGTGCTCTCCTGTCAGTAGGAGGAAAA
CGACTTAGAGAAGAACTTCTAAAACAGACGAAACTTGTACAGCTTTTAGGAGGAGTAGCA
GAAAAAGTAAGGCAGGCTAGTGGATCAGCCAGACAGGTTGTTCTCCAAAGAAGTATGGAA
CGAGTACAGTCCTTTTTTCAGAAAAATAAATGCCGTCTCCCTCTCAAGCCAAGTCTAGTG
GCAAAAGAATTAAATATTAAGTCGTGTTCCTTCTTCAGTTCTAATGCTGTCCCCCTAAAA
GTCACAATGGTGAATGCTGACCCTATGGGAGAAGAAATTAATGTCATGTTTAAGGTTGGT
GAAGATCTTCGGCAAGATATGTTAGCTTTACAGATGATAAAGATTATGGATAAGATCTGG
CTTAAAGAAGGACTAGATCTGAGGATGGTAATTTTCAAATGTCTCTCAACTGGCAGAGAT
CGAGGCATGGTGGAGCTGGTTCCTGCTTCCGATACCCTCAGGAAAATCCAAGTGGAATAT
GGTGTGACAGGATCCTTTAAAGATAAACCACTTGCAGAGTGGCTAAGGAAATACAATCCC
TCTGAAGAAGAATATGAAAAGGCTTCAGAGAACTTTATCTATTCCTGTGCTGGATGCTGT
GTAGCCACCTATGTTTTAGGCATCTGTGATCGACACAATGACAATATAATGCTTCGAAGC
ACGGGACACATGTTTCACATTGACTTTGGAAAGTTTTTGGGACATGCACAGATGTTTGGC
AGCTTCAAAAGGGATCGGGCTCCTTTTGTGCTGACCTCTGATATGGCATATGTCATTAAT
GGGGGTGAAAAGCCCACCATTCGTTTTCAGTTGTTTGTGGACCTCTGCTGTCAGGCCTAC
AACTTGATAAGAAAGCAGACAAACCTTTTTCTTAACCTCCTTTCACTGATGATTCCTTCA
GGGTTACCAGAACTTACAAGTATTCAAGATTTGAAATACGTTAGAGATGCACTTCAACCC
CAAACTACAGACGCAGAAGCTACAATTTTCTTTACTAGGCTTATTGAATCAAGTTTGGGA
AGCATTGCCACAAAGTTTAACTTCTTCATTCACAACCTTGCTCAGCTTCGTTTTTCTGGT
CTTCCTTCTAATGATGAGCCCATCCTTTCATTTTCACCTAAAACATACTCCTTTAGACAA
GATGGTCGAATCAAGGAAGTCTCTGTTTTTACATATCATAAGAAATACAACCCAGATAAA
CATTATATTTATGTAGTCCGAATTTTGAGGGAAGGACAGATTGAACCATCATTTGTCTTC
CGAACATTTGACGAATTTCAGGAACTTCACAATAAGCTCAGTATTATTTTTCCACTTTGG
AAGTTACCAGGCTTTCCTAATAGGATGGTTCTAGGAAGAACACACATAAAAGATGTAGCA
GCCAAAAGGAAAATTGAGTTAAACAGTTACTTACAGAGTTTGATGAATGCTTCAACGGAT
GTAGCAGAGTGTGATCTTGTTTGTACTTTCTTCCACCCTTTACTTCGTGATGAGAAAGCT
GAAGGGATAGCTAGGTCTGCAGATGCAGGTTCCTTCAGTCCTACTCCAGGCCAAATAGGA
GGAGCTGTGAAATTATCCATCTCTTACCGAAATGGTACTCTTTTCATCATGGTGATGCAT
ATCAAAGATCTTGTTACTGAAGATGGAGCTGACCCAAATCCATATGTCAAAACATACCTA
CTTCCAGATAACCACAAAACATCCAAACGTAAAACCAAAATTTCACGAAAAACGAGGAAT
CCGACATTCAATGAAATGCTTGTATACAGTGGATATAGCAAAGAAACCCTAAGACAGCGA
GAACTTCAACTAAGTGTACTCAGTGCAGAATCTCTGCGGGAGAATTTTTTCTTGGGTGGA
GTAACCCTGCCTTTGAAAGATTTCAACTTGAGCAAAGAGACGGTTAAATGGTATCAGCTG
ACTGCGGCAACATACTTGTAA
|
| Enzyme 16 GenBank Gene ID |
BC113658  |
| Enzyme 16 GeneCard ID |
PIK3C2A  |
| Enzyme 16 GenAtlas ID |
PIK3C2A  |
| Enzyme 16 HGNC ID |
HGNC:8971  |
| Enzyme 16 Chromosome Location |
1 |
| Enzyme 16 Locus |
11p15.5-p14 |
| Enzyme 16 SNPs |
SNPJam Report  |
| Enzyme 16 General References |
- Domin J, Pages F, Volinia S, Rittenhouse SE, Zvelebil MJ, Stein RC, Waterfield MD: Cloning of a human phosphoinositide 3-kinase with a C2 domain that displays reduced sensitivity to the inhibitor wortmannin. Biochem J. 1997 Aug 15;326 ( Pt 1):139-47. [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
]
- Domin J, Gaidarov I, Smith ME, Keen JH, Waterfield MD: The class II phosphoinositide 3-kinase PI3K-C2alpha is concentrated in the trans-Golgi network and present in clathrin-coated vesicles. J Biol Chem. 2000 Apr 21;275(16):11943-50. [PubMed
]
- Arcaro A, Zvelebil MJ, Wallasch C, Ullrich A, Waterfield MD, Domin J: Class II phosphoinositide 3-kinases are downstream targets of activated polypeptide growth factor receptors. Mol Cell Biol. 2000 Jun;20(11):3817-30. [PubMed
]
- Didichenko SA, Thelen M: Phosphatidylinositol 3-kinase c2alpha contains a nuclear localization sequence and associates with nuclear speckles. J Biol Chem. 2001 Dec 21;276(51):48135-42. Epub 2001 Oct 17. [PubMed
]
- Gaidarov I, Smith ME, Domin J, Keen JH: The class II phosphoinositide 3-kinase C2alpha is activated by clathrin and regulates clathrin-mediated membrane trafficking. Mol Cell. 2001 Feb;7(2):443-9. [PubMed
]
- El Sheikh SS, Domin J, Tomtitchong P, Abel P, Stamp G, Lalani EN: Topographical expression of class IA and class II phosphoinositide 3-kinase enzymes in normal human tissues is consistent with a role in differentiation. BMC Clin Pathol. 2003 Oct 16;3(1):4. [PubMed
]
- Didichenko SA, Fragoso CM, Thelen M: Mitotic and stress-induced phosphorylation of HsPI3K-C2alpha targets the protein for degradation. J Biol Chem. 2003 Jul 11;278(28):26055-64. Epub 2003 Apr 28. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Oppermann FS, Gnad F, Olsen JV, Hornberger R, Greff Z, Keri G, Mann M, Daub H: Large-scale proteomics analysis of the human kinome. Mol Cell Proteomics. 2009 Jul;8(7):1751-64. Epub 2009 Apr 15. [PubMed
]
- 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
]
- Stahelin RV, Karathanassis D, Bruzik KS, Waterfield MD, Bravo J, Williams RL, Cho W: Structural and membrane binding analysis of the Phox homology domain of phosphoinositide 3-kinase-C2alpha. J Biol Chem. 2006 Dec 22;281(51):39396-406. Epub 2006 Oct 12. [PubMed
]
|
| Enzyme 16 Metabolite References |
Not Available |
|
Enzyme 17
[top]
|
| Enzyme 17 ID |
8839 |
| Enzyme 17 Name |
Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2 |
| Enzyme 17 Synonyms |
- Inositol polyphosphate phosphatase-like protein 1
- INPPL-1
- Protein 51C
- SH2 domain-containing inositol-5'-phosphatase 2
- SH2 domain-containing inositol phosphatase 2
- SHIP-2
|
| Enzyme 17 Gene Name |
INPPL1 |
| Enzyme 17 Protein Sequence |
>Phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase 2
MASACGAPGPGGALGSQAPSWYHRDLSRAAAEELLARAGRDGSFLVRDSESVAGAFALCV
LYQKHVHTYRILPDGEDFLAVQTSQGVPVRRFQTLGELIGLYAQPNQGLVCALLLPVEGE
REPDPPDDRDASDGEDEKPPLPPRSGSTSISAPTGPSSPLPAPETPTAPAAESAPNGLST
VSHDYLKGSYGLDLEAVRGGASHLPHLTRTLATSCRRLHSEVDKVLSGLEILSKVFDQQS
SPMVTRLLQQQNLPQTGEQELESLVLKLSVLKDFLSGIQKKALKALQDMSSTAPPAPQPS
TRKAKTIPVQAFEVKLDVTLGDLTKIGKSQKFTLSVDVEGGRLVLLRRQRDSQEDWTTFT
HDRIRQLIKSQRVQNKLGVVFEKEKDRTQRKDFIFVSARKREAFCQLLQLMKNKHSKQDE
PDMISVFIGTWNMGSVPPPKNVTSWFTSKGLGKTLDEVTVTIPHDIYVFGTQENSVGDRE
WLDLLRGGLKELTDLDYRPIAMQSLWNIKVAVLVKPEHENRISHVSTSSVKTGIANTLGN
KGAVGVSFMFNGTSFGFVNCHLTSGNEKTARRNQNYLDILRLLSLGDRQLNAFDISLRFT
HLFWFGDLNYRLDMDIQEILNYISRKEFEPLLRVDQLNLEREKHKVFLRFSEEEISFPPT
YRYERGSRDTYAWHKQKPTGVRTNVPSWCDRILWKSYPETHIICNSYGCTDDIVTSDHSP
VFGTFEVGVTSQFISKKGLSKTSDQAYIEFESIEAIVKTASRTKFFIEFYSTCLEEYKKS
FENDAQSSDNINFLKVQWSSRQLPTLKPILADIEYLQDQHLLLTVKSMDGYESYGECVVA
LKSMIGSTAQQFLTFLSHRGEETGNIRGSMKVRVPTERLGTRERLYEWISIDKDEAGAKS
KAPSVSRGSQEPRSGSRKPAFTEASCPLSRLFEEPEKPPPTGRPPAPPRAAPREEPLTPR
LKPEGAPEPEGVAAPPPKNSFNNPAYYVLEGVPHQLLPPEPPSPARAPVPSATKNKVAIT
VPAPQLGHHRHPRVGEGSSSDEESGGTLPPPDFPPPPLPDSAIFLPPSLDPLPGPVVRGR
GGAEARGPPPPKAHPRPPLPPGPSPASTFLGEVASGDDRSCSVLQMAKTLSEVDYAPAGP
ARSALLPGPLELQPPRGLPSDYGRPLSFPPPRIRESIQEDLAEEAPCLQGGRASGLGEAG
MSAWLRAIGLERYEEGLVHNGWDDLEFLSDITEEDLEEAGVQDPAHKRLLLDTLQLSK
|
| Enzyme 17 Number of Residues |
1258 |
| Enzyme 17 Molecular Weight |
138597.5 |
| Enzyme 17 Theoretical pI |
6.49 |
| Enzyme 17 GO Classification |
| Function |
- binding
- catalytic activity
- hydrolase activity
- hydrolase activity, acting on ester bonds
- inositol or phosphatidylinositol phosphatase activity
- phosphatase activity
- phosphoric ester hydrolase activity
- protein binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 17 General Function |
Involved in inositol or phosphatidylinositol phosphatase activity |
| Enzyme 17 Specific Function |
Phosphatidylinositol (PtdIns) phosphatase that specifically hydrolyzes the 5-phosphate of phosphatidylinositol- 3,4,5-trisphosphate (PtdIns(3,4,5)P3) to produce PtdIns(3,4)P2, thereby negatively regulating the PI3K (phosphoinositide 3-kinase) pathways. Plays a central role in regulation of PI3K-dependent insulin signaling, although the precise molecular mechanisms and signaling pathways remain unclear. While overexpression reduces both insulin-stimulated MAP kinase and Akt activation, its absence does not affect insulin signaling or GLUT4 trafficking. Confers resistance to dietary obesity. May act by regulating AKT2, but not AKT1, phosphorylation at the plasma membrane. Part of a signaling pathway that regulates actin cytoskeleton remodeling. Required for the maintenance and dynamic remodeling of actin structures as well as in endocytosis, having a major impact on ligand-induced EGFR internalization and degradation. Participates in regulation of cortical and submembraneous actin by hydrolyzing PtdIns(3,4,5)P3 thereby regulating membrane ruffling. Regulates cell adhesion and cell spreading. Required for HGF-mediated lamellipodium formation, cell scattering and spreading. Acts as a negative regulator of EPHA2 receptor endocytosis by inhibiting via PI3K-dependent Rac1 activation. Acts as a regulator of neuritogenesis by regulating PtdIns(3,4,5)P3 level and is required to form an initial protrusive pattern, and later, maintain proper neurite outgrowth. Acts as a negative regulator of the FC-gamma-RIIA receptor (FCGR2A). Mediates signaling from the FC-gamma-RIIB receptor (FCGR2B), playing a central role in terminating signal transduction from activating immune/hematopoietic cell receptor systems. Involved in EGF signaling pathway. Upon stimulation by EGF, it is recruited by EGFR and dephosphorylates PtdIns(3,4,5)P3. Plays a negative role in regulating the PI3K-PKB pathway, possibly by inhibiting PKB activity. Down-regulates Fc-gamma-R-mediated phagocytosis in macrophages independently of INPP5D/SHIP1. In macrophages, down-regulates NF-kappa-B-dependent gene transcription by regulating macrophage colony-stimulating factor (M-CSF)-induced signaling. May also hydrolyze PtdIns(1,3,4,5)P4, and could thus affect the levels of the higher inositol polyphosphates like InsP6 |
| Enzyme 17 Pathways |
Not Available |
| Enzyme 17 Reactions |
Not Available |
| Enzyme 17 Pfam Domain Function |
|
| Enzyme 17 Signals |
|
| Enzyme 17 Transmembrane Regions |
|
| Enzyme 17 Essentiality |
Not Available |
| Enzyme 17 GenBank ID Protein |
222136583  |
| Enzyme 17 UniProtKB/Swiss-Prot ID |
O15357  |
| Enzyme 17 UniProtKB/Swiss-Prot Entry Name |
SHIP2_HUMAN  |
| Enzyme 17 PDB ID |
Not Available |
| Enzyme 17 Cellular Location |
Not Available |
| Enzyme 17 Gene Sequence |
>3777 bp
ATGGCCTCGGCCTGCGGGGCGCCGGGCCCGGGGGGCGCCCTGGGCAGCCAGGCCCCCTCC
TGGTACCACCGCGACCTGAGCCGGGCGGCCGCGGAGGAGCTGCTGGCCCGGGCGGGCCGC
GATGGCAGCTTCCTGGTCCGAGACAGCGAGAGCGTGGCGGGGGCCTTCGCGCTCTGCGTC
CTGTATCAGAAGCATGTGCACACGTATCGCATTCTGCCTGATGGAGAAGATTTCTTGGCT
GTGCAGACCTCGCAGGGTGTGCCTGTGCGCCGCTTCCAGACCCTGGGTGAGCTCATCGGC
CTGTACGCCCAGCCCAACCAGGGCCTTGTGTGCGCCCTGCTTCTTCCTGTAGAGGGTGAG
CGAGAGCCGGACCCACCGGATGACCGGGATGCCTCAGATGGGGAGGATGAGAAGCCCCCG
CTGCCCCCGCGCTCTGGCTCCACCAGCATTTCTGCCCCCACTGGGCCCAGCAGTCCCCTG
CCAGCTCCTGAGACTCCCACAGCTCCAGCTGCTGAGAGTGCTCCCAATGGGCTGAGCACC
GTCTCGCACGACTACCTGAAAGGCAGCTATGGGCTGGACCTGGAAGCTGTGAGGGGTGGA
GCCAGCCACCTGCCCCACCTCACCCGTACCCTCGCTACCTCATGCCGGAGGCTGCACAGT
GAGGTGGACAAGGTCCTGTCAGGCCTGGAGATCCTGTCCAAGGTGTTTGACCAGCAGAGC
TCGCCCATGGTGACCCGCCTTTTGCAGCAGCAGAACCTGCCACAGACAGGGGAGCAGGAA
CTAGAGAGCCTGGTGCTGAAGCTGTCAGTGCTAAAGGACTTCCTGTCAGGCATCCAGAAG
AAGGCCCTGAAGGCCCTACAGGACATGAGCTCCACAGCACCCCCAGCTCCGCAGCCATCC
ACACGTAAGGCCAAGACCATCCCCGTGCAGGCCTTTGAGGTGAAGCTAGATGTGACCCTG
GGTGACCTGACCAAGATTGGGAAGTCACAGAAGTTCACGCTGAGCGTGGATGTGGAGGGT
GGGCGGCTGGTGCTGCTGCGGAGACAGCGGGACTCCCAGGAGGACTGGACCACCTTCACG
CACGACCGCATCCGCCAGCTCATTAAGTCCCAGCGTGTCCAGAACAAGCTGGGTGTTGTG
TTTGAGAAGGAGAAGGACCGGACTCAGCGCAAGGACTTCATCTTTGTCAGTGCCCGGAAG
CGGGAGGCCTTCTGCCAGCTGTTGCAGCTCATGAAGAACAAGCACTCCAAGCAGGACGAG
CCCGACATGATCTCAGTCTTCATAGGCACCTGGAACATGGGAAGTGTACCACCTCCAAAA
AACGTGACATCCTGGTTCACATCGAAGGGTCTGGGGAAGACCCTGGACGAGGTCACAGTG
ACCATACCCCATGACATCTATGTCTTTGGGACCCAGGAGAACTCAGTGGGCGACCGCGAG
TGGCTGGACCTACTGCGCGGGGGCCTCAAGGAGCTTACGGATCTGGATTACCGCCCGATT
GCCATGCAATCACTGTGGAATATCAAGGTGGCAGTGCTGGTCAAGCCAGAGCACGAGAAC
CGTATCAGCCATGTCAGTACGTCCAGTGTGAAGACTGGCATCGCCAACACCCTGGGGAAC
AAGGGGGCTGTGGGCGTCTCCTTCATGTTTAATGGCACCTCATTTGGCTTTGTGAATTGT
CACCTCACCTCGGGAAATGAGAAGACGGCTCGGAGGAACCAAAACTACTTGGACATCCTG
CGGCTGCTCTCGCTGGGCGACCGGCAGCTCAATGCCTTTGACATCTCTCTGCGTTTCACA
CACCTCTTCTGGTTTGGGGACCTCAACTACCGCCTGGACATGGATATCCAGGAGATCCTG
AACTACATCAGCAGGAAAGAGTTTGAGCCCCTCCTCAGGGTGGACCAGCTCAACCTGGAG
CGGGAGAAGCACAAGGTCTTCCTTCGATTCAGTGAGGAGGAGATCTCCTTCCCACCCACC
TACCGCTATGAGCGGGGTTCCCGGGACACATATGCCTGGCACAAGCAGAAGCCAACTGGG
GTCCGGACCAATGTGCCCTCATGGTGTGACCGGATTCTGTGGAAATCCTACCCTGAAACT
CACATCATCTGCAATTCTTATGGTTGCACTGATGACATCGTCACCAGCGACCATTCCCCC
GTGTTTGGGACATTTGAGGTTGGAGTTACCTCCCAGTTCATCTCCAAGAAAGGGCTCTCA
AAGACTTCAGACCAGGCCTACATTGAGTTTGAGAGCATCGAGGCCATTGTGAAGACAGCC
AGCCGCACCAAGTTCTTCATCGAGTTCTACTCTACCTGCCTGGAGGAATACAAGAAGAGC
TTTGAGAATGATGCCCAGAGCAGTGACAACATCAACTTCCTCAAAGTGCAGTGGTCTTCA
CGCCAGCTGCCCACGCTCAAACCAATTCTGGCTGATATCGAGTACCTGCAGGACCAGCAC
CTCCTGCTCACAGTCAAGTCCATGGATGGCTATGAATCCTATGGGGAGTGTGTGGTTGCA
CTCAAATCCATGATCGGCAGCACGGCCCAACAGTTCCTGACCTTCCTATCCCACCGTGGC
GAGGAGACAGGCAATATCAGAGGCTCCATGAAGGTGCGGGTGCCCACGGAGCGCCTGGGC
ACCCGTGAGCGGCTCTACGAGTGGATCAGCATTGATAAGGATGAGGCAGGAGCAAAGAGC
AAAGCCCCCTCTGTGTCCCGAGGGAGCCAGGAGCCCAGGTCAGGGAGCCGCAAGCCAGCC
TTCACAGAGGCCTCCTGCCCGCTCTCCAGGTTATTTGAAGAACCAGAGAAACCGCCACCA
ACGGGGAGGCCCCCAGCCCCACCCCGAGCAGCTCCCCGGGAGGAGCCCTTGACCCCCAGG
TTGAAGCCAGAGGGAGCTCCTGAACCAGAAGGGGTGGCGGCCCCCCCACCCAAGAACAGC
TTCAATAACCCTGCCTACTACGTCCTTGAAGGGGTCCCGCACCAGCTGCTGCCCCCGGAG
CCACCCTCGCCTGCCAGGGCCCCTGTCCCATCTGCCACCAAGAACAAAGTGGCCATTACA
GTGCCTGCTCCACAGCTTGGGCACCACCGGCACCCTCGTGTGGGAGAGGGGAGTTCTTCA
GATGAGGAGTCTGGAGGCACACTGCCCCCTCCAGACTTTCCACCTCCACCACTGCCGGAC
TCAGCCATCTTCCTGCCCCCCAGCCTGGATCCTTTACCAGGGCCAGTGGTCCGGGGCCGT
GGTGGGGCTGAGGCCCGTGGCCCACCACCTCCCAAGGCCCATCCAAGGCCTCCACTGCCC
CCAGGCCCCTCACCAGCCAGCACTTTCCTGGGGGAAGTGGCCAGTGGGGATGACCGGTCC
TGCTCGGTGCTGCAGATGGCCAAGACGCTGAGCGAGGTGGACTATGCCCCTGCTGGGCCT
GCACGCTCAGCGCTCCTCCCAGGCCCCCTGGAGCTGCAGCCCCCCCGGGGACTGCCCTCG
GACTATGGCCGGCCCCTCAGCTTCCCTCCACCCCGCATCCGGGAGAGCATCCAGGAAGAC
CTGGCAGAGGAGGCTCCGTGCCTGCAGGGCGGGCGGGCCAGCGGGCTGGGCGAGGCAGGC
ATGAGTGCCTGGCTGCGGGCCATCGGCTTGGAGCGCTATGAGGAGGGCCTGGTGCATAAT
GGCTGGGACGACCTGGAGTTTCTCAGTGACATCACCGAGGAGGACTTGGAGGAGGCTGGG
GTGCAGGACCCGGCTCACAAGCGCCTCCTTCTGGACACCCTGCAGCTCAGCAAGTGA
|
| Enzyme 17 GenBank Gene ID |
NM_001567.3  |
| Enzyme 17 GeneCard ID |
INPPL1  |
| Enzyme 17 GenAtlas ID |
INPPL1  |
| Enzyme 17 HGNC ID |
HGNC:6080  |
| Enzyme 17 Chromosome Location |
1 |
| Enzyme 17 Locus |
11q23 |
| Enzyme 17 SNPs |
SNPJam Report  |
| Enzyme 17 General References |
- Hejna JA, Saito H, Merkens LS, Tittle TV, Jakobs PM, Whitney MA, Grompe M, Friedberg AS, Moses RE: Cloning and characterization of a human cDNA (INPPL1) sharing homology with inositol polyphosphate phosphatases. Genomics. 1995 Sep 1;29(1):285-7. [PubMed
]
- Pesesse X, Deleu S, De Smedt F, Drayer L, Erneux C: Identification of a second SH2-domain-containing protein closely related to the phosphatidylinositol polyphosphate 5-phosphatase SHIP. Biochem Biophys Res Commun. 1997 Oct 29;239(3):697-700. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Habib T, Hejna JA, Moses RE, Decker SJ: Growth factors and insulin stimulate tyrosine phosphorylation of the 51C/SHIP2 protein. J Biol Chem. 1998 Jul 17;273(29):18605-9. [PubMed
]
- Wisniewski D, Strife A, Swendeman S, Erdjument-Bromage H, Geromanos S, Kavanaugh WM, Tempst P, Clarkson B: A novel SH2-containing phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase (SHIP2) is constitutively tyrosine phosphorylated and associated with src homologous and collagen gene (SHC) in chronic myelogenous leukemia progenitor cells. Blood. 1999 Apr 15;93(8):2707-20. [PubMed
]
- Bruhns P, Vely F, Malbec O, Fridman WH, Vivier E, Daeron M: Molecular basis of the recruitment of the SH2 domain-containing inositol 5-phosphatases SHIP1 and SHIP2 by fcgamma RIIB. J Biol Chem. 2000 Dec 1;275(48):37357-64. [PubMed
]
- Pesesse X, Dewaste V, De Smedt F, Laffargue M, Giuriato S, Moreau C, Payrastre B, Erneux C: The Src homology 2 domain containing inositol 5-phosphatase SHIP2 is recruited to the epidermal growth factor (EGF) receptor and dephosphorylates phosphatidylinositol 3,4,5-trisphosphate in EGF-stimulated COS-7 cells. J Biol Chem. 2001 Jul 27;276(30):28348-55. Epub 2001 May 10. [PubMed
]
- Dyson JM, O'Malley CJ, Becanovic J, Munday AD, Berndt MC, Coghill ID, Nandurkar HH, Ooms LM, Mitchell CA: The SH2-containing inositol polyphosphate 5-phosphatase, SHIP-2, binds filamin and regulates submembraneous actin. J Cell Biol. 2001 Dec 10;155(6):1065-79. Epub 2001 Dec 10. [PubMed
]
- Prasad N, Topping RS, Decker SJ: SH2-containing inositol 5'-phosphatase SHIP2 associates with the p130(Cas) adapter protein and regulates cellular adhesion and spreading. Mol Cell Biol. 2001 Feb;21(4):1416-28. [PubMed
]
- Steen H, Kuster B, Fernandez M, Pandey A, Mann M: Tyrosine phosphorylation mapping of the epidermal growth factor receptor signaling pathway. J Biol Chem. 2002 Jan 11;277(2):1031-9. Epub 2001 Oct 30. [PubMed
]
- Prasad N, Topping RS, Decker SJ: Src family tyrosine kinases regulate adhesion-dependent tyrosine phosphorylation of 5'-inositol phosphatase SHIP2 during cell attachment and spreading on collagen I. J Cell Sci. 2002 Oct 1;115(Pt 19):3807-15. [PubMed
]
- Vandenbroere I, Paternotte N, Dumont JE, Erneux C, Pirson I: The c-Cbl-associated protein and c-Cbl are two new partners of the SH2-containing inositol polyphosphate 5-phosphatase SHIP2. Biochem Biophys Res Commun. 2003 Jan 10;300(2):494-500. [PubMed
]
- Dyson JM, Munday AD, Kong AM, Huysmans RD, Matzaris M, Layton MJ, Nandurkar HH, Berndt MC, Mitchell CA: SHIP-2 forms a tetrameric complex with filamin, actin, and GPIb-IX-V: localization of SHIP-2 to the activated platelet actin cytoskeleton. Blood. 2003 Aug 1;102(3):940-8. Epub 2003 Apr 3. [PubMed
]
- Pengal RA, Ganesan LP, Fang H, Marsh CB, Anderson CL, Tridandapani S: SHIP-2 inositol phosphatase is inducibly expressed in human monocytes and serves to regulate Fcgamma receptor-mediated signaling. J Biol Chem. 2003 Jun 20;278(25):22657-63. Epub 2003 Apr 10. [PubMed
]
- Salomon AR, Ficarro SB, Brill LM, Brinker A, Phung QT, Ericson C, Sauer K, Brock A, Horn DM, Schultz PG, Peters EC: Profiling of tyrosine phosphorylation pathways in human cells using mass spectrometry. Proc Natl Acad Sci U S A. 2003 Jan 21;100(2):443-8. Epub 2003 Jan 9. [PubMed
]
- Vandeput F, Backers K, Villeret V, Pesesse X, Erneux C: The influence of anionic lipids on SHIP2 phosphatidylinositol 3,4,5-trisphosphate 5-phosphatase activity. Cell Signal. 2006 Dec;18(12):2193-9. Epub 2006 May 23. [PubMed
]
- Paternotte N, Zhang J, Vandenbroere I, Backers K, Blero D, Kioka N, Vanderwinden JM, Pirson I, Erneux C: SHIP2 interaction with the cytoskeletal protein Vinexin. FEBS J. 2005 Dec;272(23):6052-66. [PubMed
]
- Prasad NK, Decker SJ: SH2-containing 5'-inositol phosphatase, SHIP2, regulates cytoskeleton organization and ligand-dependent down-regulation of the epidermal growth factor receptor. J Biol Chem. 2005 Apr 1;280(13):13129-36. Epub 2005 Jan 24. [PubMed
]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed
]
- Zhang Y, Wolf-Yadlin A, Ross PL, Pappin DJ, Rush J, Lauffenburger DA, White FM: Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules. Mol Cell Proteomics. 2005 Sep;4(9):1240-50. Epub 2005 Jun 11. [PubMed
]
- Koch A, Mancini A, El Bounkari O, Tamura T: The SH2-domian-containing inositol 5-phosphatase (SHIP)-2 binds to c-Met directly via tyrosine residue 1356 and involves hepatocyte growth factor (HGF)-induced lamellipodium formation, cell scattering and cell spreading. Oncogene. 2005 May 12;24(21):3436-47. [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
]
- 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
]
- Raaijmakers JH, Deneubourg L, Rehmann H, de Koning J, Zhang Z, Krugmann S, Erneux C, Bos JL: The PI3K effector Arap3 interacts with the PI(3,4,5)P3 phosphatase SHIP2 in a SAM domain-dependent manner. Cell Signal. 2007 Jun;19(6):1249-57. Epub 2007 Jan 20. [PubMed
]
- Zhuang G, Hunter S, Hwang Y, Chen J: Regulation of EphA2 receptor endocytosis by SHIP2 lipid phosphatase via phosphatidylinositol 3-Kinase-dependent Rac1 activation. J Biol Chem. 2007 Jan 26;282(4):2683-94. Epub 2006 Nov 29. [PubMed
]
- Artemenko Y, Gagnon A, Ibrahim S, Sorisky A: Regulation of PDGF-stimulated SHIP2 tyrosine phosphorylation and association with Shc in 3T3-L1 preadipocytes. J Cell Physiol. 2007 Jun;211(3):598-607. [PubMed
]
- Marion E, Kaisaki PJ, Pouillon V, Gueydan C, Levy JC, Bodson A, Krzentowski G, Daubresse JC, Mockel J, Behrends J, Servais G, Szpirer C, Kruys V, Gauguier D, Schurmans S: The gene INPPL1, encoding the lipid phosphatase SHIP2, is a candidate for type 2 diabetes in rat and man. Diabetes. 2002 Jul;51(7):2012-7. [PubMed
]
- Kaisaki PJ, Delepine M, Woon PY, Sebag-Montefiore L, Wilder SP, Menzel S, Vionnet N, Marion E, Riveline JP, Charpentier G, Schurmans S, Levy JC, Lathrop M, Farrall M, Gauguier D: Polymorphisms in type II SH2 domain-containing inositol 5-phosphatase (INPPL1, SHIP2) are associated with physiological abnormalities of the metabolic syndrome. Diabetes. 2004 Jul;53(7):1900-4. [PubMed
]
- Kagawa S, Sasaoka T, Yaguchi S, Ishihara H, Tsuneki H, Murakami S, Fukui K, Wada T, Kobayashi S, Kimura I, Kobayashi M: Impact of SRC homology 2-containing inositol 5'-phosphatase 2 gene polymorphisms detected in a Japanese population on insulin signaling. J Clin Endocrinol Metab. 2005 May;90(5):2911-9. Epub 2005 Feb 1. [PubMed
]
- Marcano AC, Burke B, Gungadoo J, Wallace C, Kaisaki PJ, Woon PY, Farrall M, Clayton D, Brown M, Dominiczak A, Connell JM, Webster J, Lathrop M, Caulfield M, Samani N, Gauguier D, Munroe PB: Genetic association analysis of inositol polyphosphate phosphatase-like 1 (INPPL1, SHIP2) variants with essential hypertension. J Med Genet. 2007 Sep;44(9):603-5. Epub 2007 Jun 8. [PubMed
]
- Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- 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
]
|
| Enzyme 17 Metabolite References |
Not Available |
|
Enzyme 18
[top]
|
| Enzyme 18 ID |
10050 |
| Enzyme 18 Name |
1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3 |
| Enzyme 18 Synonyms |
- Phosphoinositide phospholipase C-delta-3
- Phospholipase C-delta-3
- PLC-delta-3
|
| Enzyme 18 Gene Name |
PLCD3 |
| Enzyme 18 Protein Sequence |
>1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase delta-3
MLCGRWRRCRRPPEEPPVAAQVAAQVAAPVALPSPPTPSDGGTKRPGLRALKKMGLTEDE
DVRAMLRGSRLRKIRSRTWHKERLYRLQEDGLSVWFQRRIPRAPSQHIFFVQHIEAVREG
HQSEGLRRFGGAFAPARCLTIAFKGRRKNLDLAAPTAEEAQRWVRGLTKLRARLDAMSQR
ERLDHWIHSYLHRADSNQDSKMSFKEIKSLLRMVNVDMNDMYAYLLFKECDHSNNDRLEG
AEIEEFLRRLLKRPELEEIFHQYSGEDRVLSAPELLEFLEDQGEEGATLARAQQLIQTYE
LNETAKQHELMTLDGFMMYLLSPEGAALDNTHTCVFQDMNQPLAHYFISSSHNTYLTDSQ
IGGPSSTEAYVRAFAQGCRCVELDCWEGPGGEPVIYHGHTLTSKILFRDVVQAVRDHAFT
LSPYPVILSLENHCGLEQQAAMARHLCTILGDMLVTQALDSPNPEELPSPEQLKGRVLVK
GKKLPAARSEDGRALSDREEEEEDDEEEEEEVEAAAQRRLAKQISPELSALAVYCHATRL
RTLHPAPNAPQPCQVSSLSERKAKKLIREAGNSFVRHNARQLTRVYPLGLRMNSANYSPQ
EMWNSGCQLVALNFQTPGYEMDLNAGRFLVNGQCGYVLKPACLRQPDSTFDPEYPGPPRT
TLSIQVLTAQQLPKLNAEKPHSIVDPLVRIEIHGVPADCARQETDYVLNNGFNPRWGQTL
QFQLRAPELALVRFVVEDYDATSPNDFVGQFTLPLSSLKQGYRHIHLLSKDGASLSPATL
FIQIRIQRS
|
| Enzyme 18 Number of Residues |
789 |
| Enzyme 18 Molecular Weight |
89257.5 |
| Enzyme 18 Theoretical pI |
6.97 |
| Enzyme 18 GO Classification |
| Function |
- binding
- calcium ion binding
- catalytic activity
- cation binding
- hydrolase activity
- hydrolase activity, acting on ester bonds
- ion binding
- lipase activity
- metal ion binding
- phosphoinositide phospholipase C activity
- phospholipase C activity
- phospholipase activity
- phosphoric diester hydrolase activity
- phosphoric ester hydrolase activity
|
| Process |
- biological regulation
- intracellular signaling pathway
- lipid metabolic process
- metabolic process
- primary metabolic process
- regulation of biological process
- regulation of cellular process
- signal transduction
- signaling
- signaling pathway
|
| Component |
| — |
|
| Enzyme 18 General Function |
Involved in calcium ion binding |
| Enzyme 18 Specific Function |
Hydrolyzes the phosphatidylinositol 4,5-bisphosphate (PIP2) to generate 2 second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG mediates the activation of protein kinase C (PKC), while IP3 releases Ca(2+) from intracellular stores. Essential for trophoblast and placental development. May participate in cytokinesis by hydrolyzing PIP2 at the cleavage furrow |
| Enzyme 18 Pathways |
|
| Enzyme 18 Reactions |
- 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate + H2O = 1D-myo-inositol 1,4,5-trisphosphate + diacylglycerol
|
| Enzyme 18 Pfam Domain Function |
|
| Enzyme 18 Signals |
|
| Enzyme 18 Transmembrane Regions |
|
| Enzyme 18 Essentiality |
Not Available |
| Enzyme 18 GenBank ID Protein |
Not Available |
| Enzyme 18 UniProtKB/Swiss-Prot ID |
Q8N3E9  |
| Enzyme 18 UniProtKB/Swiss-Prot Entry Name |
PLCD3_HUMAN  |
| Enzyme 18 PDB ID |
Not Available |
| Enzyme 18 Cellular Location |
Not Available |
| Enzyme 18 Gene Sequence |
>2370 bp
ATGCTGTGCGGCCGCTGGAGGCGTTGCCGCCGCCCGCCCGAGGAGCCCCCGGTGGCCGCC
CAGGTCGCAGCCCAAGTCGCGGCGCCGGTCGCTCTCCCGTCCCCGCCGACTCCCTCCGAT
GGCGGCACCAAGAGGCCCGGGCTGCGGGCGCTGAAGAAGATGGGCCTGACGGAGGACGAG
GACGTGCGCGCCATGCTGCGGGGCTCCCGGCTCCGCAAGATCCGCTCGCGCACGTGGCAC
AAGGAGCGGCTGTACCGGCTGCAGGAGGACGGCCTGAGCGTGTGGTTCCAGCGGCGCATC
CCGCGTGCGCCATCGCAGCACATCTTCTTCGTGCAGCACATCGAGGCGGTCCGCGAGGGC
CACCAGTCCGAGGGCCTGCGGCGCTTCGGGGGTGCCTTCGCGCCAGCGCGCTGCCTCACC
ATCGCCTTCAAGGGCCGCCGCAAGAACCTGGACCTGGCGGCGCCCACGGCTGAGGAAGCG
CAGCGCTGGGTGCGCGGTCTGACCAAGCTCCGCGCGCGCCTGGACGCCATGAGCCAGCGC
GAGCGGCTAGACCACTGGATCCACTCCTATCTGCACCGGGCTGACTCCAACCAGGACAGC
AAGATGAGCTTCAAGGAGATCAAGAGCCTGCTGAGAATGGTCAACGTGGACATGAACGAC
ATGTACGCCTACCTCCTCTTCAAGGAGTGTGACCACTCCAACAACGACCGTCTAGAGGGG
GCTGAGATCGAGGAGTTCCTGCGGCGGCTGCTGAAGCGGCCGGAGCTGGAGGAGATCTTC
CATCAGTACTCGGGCGAGGACCGCGTGCTGAGTGCCCCTGAGCTGCTGGAGTTCCTGGAG
GACCAGGGCGAGGAGGGCGCCACACTGGCCCGCGCCCAGCAGCTCATTCAGACCTATGAG
CTCAACGAGACAGCCAAGCAGCATGAGCTGATGACACTGGATGGCTTCATGATGTACCTG
TTGTCGCCGGAGGGGGCTGCCTTGGACAACACCCACACGTGTGTGTTCCAGGACATGAAC
CAGCCCCTTGCCCACTACTTCATCTCTTCCTCCCACAACACCTATCTGACTGACTCCCAG
ATCGGGGGGCCCAGCAGCACCGAGGCCTATGTTAGGGCCTTTGCCCAGGGATGCCGCTGC
GTGGAGCTGGACTGCTGGGAGGGGCCAGGAGGGGAGCCCGTCATCTATCATGGCCATACC
CTCACCTCCAAGATTCTCTTCCGGGACGTGGTCCAAGCCGTGCGCGACCATGCCTTCACG
CTGTCCCCTTACCCTGTCATCCTATCCCTGGAGAACCACTGCGGGCTGGAGCAGCAGGCT
GCCATGGCCCGCCACCTCTGCACCATCCTGGGGGACATGCTGGTGACACAGGCGCTGGAC
TCCCCAAATCCCGAGGAGCTGCCATCCCCAGAGCAGCTGAAGGGCCGGGTCCTGGTGAAG
GGAAAGAAGTTGCCCGCTGCTCGGAGCGAGGATGGCCGGGCTCTGTCGGATCGGGAGGAG
GAGGAGGAGGATGACGAGGAGGAAGAAGAGGAGGTGGAGGCTGCAGCGCAGAGGCGGCTG
GCCAAGCAGATCTCCCCGGAGCTGTCGGCCCTGGCTGTGTACTGCCACGCCACCCGCCTG
CGGACCCTGCACCCTGCCCCCAACGCCCCACAACCCTGCCAGGTCAGCTCCCTCAGCGAG
CGCAAAGCCAAGAAACTCATTCGGGAGGCAGGGAACAGCTTTGTCAGGCACAATGCCCGC
CAGCTGACCCGCGTGTACCCGCTGGGGCTGCGGATGAACTCAGCCAACTACAGTCCCCAG
GAGATGTGGAACTCGGGCTGTCAGCTGGTGGCCTTGAACTTCCAGACGCCAGGCTACGAG
ATGGACCTCAATGCCGGGCGCTTCCTAGTCAATGGGCAGTGTGGCTACGTCCTAAAACCT
GCCTGCCTGCGGCAACCTGACTCGACCTTTGACCCCGAGTACCCAGGACCTCCCAGAACC
ACTCTCAGCATCCAGGTGCTGACTGCACAGCAGCTGCCCAAGCTGAATGCCGAGAAGCCA
CACTCCATTGTGGACCCCCTGGTGCGCATTGAGATCCATGGGGTGCCCGCAGACTGTGCC
CGGCAGGAGACTGACTACGTGCTCAACAATGGCTTCAACCCCCGCTGGGGGCAGACCCTG
CAGTTCCAGCTGCGGGCTCCGGAGCTGGCACTGGTCCGGTTTGTGGTGGAAGATTATGAC
GCCACCTCCCCCAATGACTTTGTGGGCCAGTTTACACTGCCTCTTAGCAGCCTAAAGCAA
GGGTACCGCCACATACACCTGCTTTCCAAGGACGGGGCCTCACTGTCACCAGCCACGCTC
TTCATCCAAATCCGCATCCAGCGCTCCTGA
|
| Enzyme 18 GenBank Gene ID |
AK074240  |
| Enzyme 18 GeneCard ID |
PLCD3  |
| Enzyme 18 GenAtlas ID |
PLCD3  |
| Enzyme 18 HGNC ID |
HGNC:9061  |
| Enzyme 18 Chromosome Location |
1 |
| Enzyme 18 Locus |
17q21.31 |
| Enzyme 18 SNPs |
SNPJam Report  |
| Enzyme 18 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXII. The complete sequences of 50 new cDNA clones which code for large proteins. DNA Res. 2001 Dec 31;8(6):319-27. [PubMed
]
- Pawelczyk T, Matecki A: Expression, purification and kinetic properties of human recombinant phospholipase C delta 3. Acta Biochim Pol. 1997;44(2):221-9. [PubMed
]
- Ghosh S, Pawelczyk T, Lowenstein JM: Phospholipase C isoforms delta 1 and delta 3 from human fibroblasts. High-yield expression in Escherichia coli, simple purification, and properties. Protein Expr Purif. 1997 Mar;9(2):262-78. [PubMed
]
- Pawelczyk T, Matecki A: Localization of phospholipase C delta3 in the cell and regulation of its activity by phospholipids and calcium. Eur J Biochem. 1998 Oct 1;257(1):169-77. [PubMed
]
- Kim H, Suh PG, Ryu SH, Park SH: Assignment of the human PLC delta3 gene (PLCD3) to human chromosome band 17q21 by fluorescence in situ hybridization. Cytogenet Cell Genet. 1999;87(3-4):209-10. [PubMed
]
- Pawelczyk T, Matecki A: Phospholipase C-delta3 binds with high specificity to phosphatidylinositol 4,5-bisphosphate and phosphatidic acid in bilayer membranes. Eur J Biochem. 1999 Jun;262(2):291-8. [PubMed
]
- Lin FG, Cheng HF, Lee IF, Kao HJ, Loh SH, Lee WH: Downregulation of phospholipase C delta3 by cAMP and calcium. Biochem Biophys Res Commun. 2001 Aug 17;286(2):274-80. [PubMed
]
- Ananthanarayanan B, Das S, Rhee SG, Murray D, Cho W: Membrane targeting of C2 domains of phospholipase C-delta isoforms. J Biol Chem. 2002 Feb 1;277(5):3568-75. Epub 2001 Nov 12. [PubMed
]
- Landreville S, Coulombe S, Carrier P, Gelb MH, Guerin SL, Salesse C: Expression of phospholipases A2 and C in human corneal epithelial cells. Invest Ophthalmol Vis Sci. 2004 Nov;45(11):3997-4003. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Naito Y, Okada M, Yagisawa H: Phospholipase C isoforms are localized at the cleavage furrow during cytokinesis. J Biochem. 2006 Dec;140(6):785-91. Epub 2006 Oct 14. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
|
| Enzyme 18 Metabolite References |
Not Available |
|
Enzyme 19
[top]
|
| Enzyme 19 ID |
12250 |
| Enzyme 19 Name |
Sphingomyelin phosphodiesterase 3 |
| Enzyme 19 Synonyms |
- Neutral sphingomyelinase 2
- nSMase-2
- nSMase2
- Neutral sphingomyelinase II
|
| Enzyme 19 Gene Name |
SMPD3 |
| Enzyme 19 Protein Sequence |
>Sphingomyelin phosphodiesterase 3
MVLYTTPFPNSCLSALHCVSWALIFPCYWLVDRLAASFIPTTYEKRQRADDPCCLQLLCT
ALFTPIYLALLVASLPFAFLGFLFWSPLQSARRPYIYSRLEDKGLAGGAALLSEWKGTGP
GKSFCFATANVCLLPDSLARVNNLFNTQARAKEIGQRIRNGAARPQIKIYIDSPTNTSIS
AASFSSLVSPQGGDGVARAVPGSIKRTASVEYKGDGGRHPGDEAANGPASGDPVDSSSPE
DACIVRIGGEEGGRPPEADDPVPGGQARNGAGGGPRGQTPNHNQQDGDSGSLGSPSASRE
SLVKGRAGPDTSASGEPGANSKLLYKASVVKKAAARRRRHPDEAFDHEVSAFFPANLDFL
CLQEVFDKRAATKLKEQLHGYFEYILYDVGVYGCQGCCSFKCLNSGLLFASRYPIMDVAY
HCYPNKCNDDALASKGALFLKVQVGSTPQDQRIVGYIACTHLHAPQEDSAIRCGQLDLLQ
DWLADFRKSTSSSSAANPEELVAFDVVCGDFNFDNCSSDDKLEQQHSLFTHYRDPCRLGP
GEEKPWAIGTLLDTNGLYDEDVCTPDNLQKVLESEEGRREYLAFPTSKSSGQKGRKELLK
GNGRRIDYMLHAEEGLCPDWKAEVEEFSFITQLSGLTDHLPVAMRLMVSSGEEEA
|
| Enzyme 19 Number of Residues |
655 |
| Enzyme 19 Molecular Weight |
71080.1 |
| Enzyme 19 Theoretical pI |
5.53 |
| Enzyme 19 GO Classification |
Not Available |
| Enzyme 19 General Function |
Involved in metal ion binding |
| Enzyme 19 Specific Function |
Catalyzes the hydrolysis of sphingomyelin to form ceramide and phosphocholine. Ceramide mediates numerous cellular functions, such as apoptosis and growth arrest, and is capable of regulating these 2 cellular events independently. Also hydrolyzes sphingosylphosphocholine. Regulates the cell cycle by acting as a growth suppressor in confluent cells. Probably acts as a regulator of postnatal development and participates in bone and dentin mineralization |
| Enzyme 19 Pathways |
|
| Enzyme 19 Reactions |
- sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
|
| Enzyme 19 Pfam Domain Function |
|
| Enzyme 19 Signals |
|
| Enzyme 19 Transmembrane Regions |
|
| Enzyme 19 Essentiality |
Not Available |
| Enzyme 19 GenBank ID Protein |
8247250  |
| Enzyme 19 UniProtKB/Swiss-Prot ID |
Q9NY59  |
| Enzyme 19 UniProtKB/Swiss-Prot Entry Name |
NSMA2_HUMAN  |
| Enzyme 19 PDB ID |
Not Available |
| Enzyme 19 Cellular Location |
Not Available |
| Enzyme 19 Gene Sequence |
>1968 bp
ATGGTTTTGTACACGACCCCCTTTCCTAACAGCTGTCTGTCCGCCCTGCACTGTGTGTCC
TGGGCCCTTATCTTTCCATGCTACTGGCTGGTGGACCGGCTCGCTGCCTCCTTCATACCC
ACCACCTACGAGAAGCGCCAGCGGGCAGACGACCCGTGCTGCCTGCAGCTGCTCTGCACT
GCCCTCTTCACGCCCATCTACCTGGCCCTCCTGGTGGCCTCGCTGCCCTTTGCGTTTCTC
GGCTTTCTCTTCTGGTCCCCACTGCAGTCGGCCCGCCGGCCCTACATCTATTCACGGCTG
GAAGACAAGGGCCTGGCCGGTGGGGCAGCCCTGCTCAGTGAATGGAAGGGCACGGGGCCT
GGCAAAAGCTTCTGCTTTGCCACTGCCAACGTCTGCCTCCTGCCCGACTCACTCGCCAGG
GTCAACAACCTTTTTAACACCCAAGCGCGGGCCAAGGAGATCGGGCAGAGAATCCGCAAT
GGGGCCGCCCGGCCCCAGATCAAAATTTACATCGACTCCCCCACCAATACCTCCATCAGC
GCCGCTAGCTTCAGCAGCCTGGTGTCACCACAGGGCGGCGATGGGGTGGCCCGGGCCGTC
CCCGGGAGCATTAAGAGGACAGCCTCTGTGGAGTACAAGGGTGACGGTGGGCGGCACCCC
GGTGACGAGGCTGCCAACGGCCCAGCCTCTGGGGACCCTGTCGACAGCAGCAGCCCGGAG
GATGCCTGCATCGTGCGCATCGGTGGCGAGGAGGGCGGCCGGCCACCTGAAGCTGACGAC
CCTGTGCCTGGGGGCCAGGCCAGGAACGGAGCTGGCGGGGGCCCAAGGGGCCAGACGCCC
AACCATAATCAGCAGGACGGGGATTCAGGGAGCCTGGGCAGCCCCTCGGCCTCCCGGGAG
TCCCTGGTGAAGGGGCGAGCTGGGCCAGACACCAGTGCCAGCGGGGAGCCAGGTGCCAAC
AGCAAGCTCCTGTACAAGGCCTCGGTGGTGAAGAAGGCGGCTGCACGCAGGAGGCGGCAC
CCCGACGAGGCCTTCGACCATGAGGTCTCCGCCTTCTTCCCCGCCAACCTGGACTTCCTG
TGCCTGCAGGAGGTGTTTGACAAGCGAGCAGCCACCAAATTGAAAGAGCAGCTGCACGGC
TACTTCGAGTACATCCTGTACGACGTCGGGGTCTACGGCTGCCAGGGCTGCTGCAGCTTC
AAGTGTCTCAACAGCGGCCTCCTCTTTGCCAGCCGCTACCCCATCATGGACGTGGCCTAT
CACTGTTACCCCAACAAGTGTAACGACGATGCCCTGGCCTCTAAGGGAGCTCTGTTTCTC
AAGGTGCAGGTGGGAAGCACACCTCAGGACCAAAGAATCGTCGGGTACATCGCCTGCACA
CACCTGCATGCCCCACAAGAGGACAGCGCCATCCGGTGTGGGCAGCTGGACCTGCTTCAG
GACTGGCTGGCTGATTTCCGAAAATCTACCTCCTCGTCCAGCGCAGCCAACCCCGAGGAG
CTGGTGGCATTTGACGTCGTCTGTGGAGATTTCAACTTTGATAACTGCTCCTCTGACGAC
AAGCTGGAGCAGCAACACTCCCTGTTCACCCACTACAGGGACCCCTGCCGCCTGGGGCCT
GGTGAGGAGAAGCCGTGGGCCATCGGTACTCTGCTGGACACGAACGGCCTGTACGATGAG
GATGTGTGCACCCCCGACAACCTGCAGAAGGTCCTGGAGAGTGAGGAGGGCCGCAGGGAG
TACCTGGCGTTTCCCACCAGCAAGAGCTCGGGCCAGAAGGGGCGGAAGGAGCTGCTGAAG
GGCAACGGCCGGCGCATCGACTACATGCTGCATGCAGAGGAGGGGCTGTGCCCAGACTGG
AAGGCCGAGGTGGAAGAATTCAGTTTTATCACCCAGCTGTCCGGCCTGACGGACCACCTG
CCAGTAGCCATGCGACTGATGGTGTCTTCGGGGGAGGAGGAGGCATAG
|
| Enzyme 19 GenBank Gene ID |
AJ250460  |
| Enzyme 19 GeneCard ID |
SMPD3  |
| Enzyme 19 GenAtlas ID |
SMPD3  |
| Enzyme 19 HGNC ID |
HGNC:14240  |
| Enzyme 19 Chromosome Location |
1 |
| Enzyme 19 Locus |
16q22.1 |
| Enzyme 19 SNPs |
SNPJam Report  |
| Enzyme 19 General References |
- Hofmann K, Tomiuk S, Wolff G, Stoffel W: Cloning and characterization of the mammalian brain-specific, Mg2+-dependent neutral sphingomyelinase. Proc Natl Acad Sci U S A. 2000 May 23;97(11):5895-900. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Miura Y, Gotoh E, Nara F, Nishijima M, Hanada K: Hydrolysis of sphingosylphosphocholine by neutral sphingomyelinases. FEBS Lett. 2004 Jan 16;557(1-3):288-92. [PubMed
]
- Marchesini N, Osta W, Bielawski J, Luberto C, Obeid LM, Hannun YA: Role for mammalian neutral sphingomyelinase 2 in confluence-induced growth arrest of MCF7 cells. J Biol Chem. 2004 Jun 11;279(24):25101-11. Epub 2004 Mar 29. [PubMed
]
|
| Enzyme 19 Metabolite References |
Not Available |
|
Enzyme 20
[top]
|
| Enzyme 20 ID |
12915 |
| Enzyme 20 Name |
Phospholipid scramblase 2 |
| Enzyme 20 Synonyms |
- PL scramblase 2
- Ca(2+)-dependent phospholipid scramblase 2
|
| Enzyme 20 Gene Name |
PLSCR2 |
| Enzyme 20 Protein Sequence |
>Phospholipid scramblase 2
MPAPPPPLNCPPGLEYLSQIDMILIHQQIELLEVLFSFESSNMYEIKNSFGQRIYFAAED
TNFCIRNCCGRSRPFTLRITDNVGREVITLERPLRCNCCCCPCCLQEIEIQAPPGVPVGY
VTQTWHPCLTKFTIKNQKREDVLKISGPCIVCSCIAGVDFEITSLDEQIVVGRISKHWSG
FLREAFTDADNFGIQFPRDLDVKMKAVMIGACFLIDYMFFERTR
|
| Enzyme 20 Number of Residues |
224 |
| Enzyme 20 Molecular Weight |
25522.5 |
| Enzyme 20 Theoretical pI |
5.34 |
| Enzyme 20 GO Classification |
Not Available |
| Enzyme 20 General Function |
Involved in calcium ion binding |
| Enzyme 20 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 20 Pathways |
Not Available |
| Enzyme 20 Reactions |
Not Available |
| Enzyme 20 Pfam Domain Function |
|
| Enzyme 20 Signals |
|
| Enzyme 20 Transmembrane Regions |
|
| Enzyme 20 Essentiality |
Not Available |
| Enzyme 20 GenBank ID Protein |
9651165  |
| Enzyme 20 UniProtKB/Swiss-Prot ID |
Q9NRY7  |
| Enzyme 20 UniProtKB/Swiss-Prot Entry Name |
PLS2_HUMAN  |
| Enzyme 20 PDB ID |
Not Available |
| Enzyme 20 Cellular Location |
Not Available |
| Enzyme 20 Gene Sequence |
>675 bp
ATGCCAGCACCACCACCACCATTAAACTGTCCGCCAGGATTGGAATACTTAAGTCAGATA
GATATGATACTAATTCATCAGCAAATTGAACTTCTGGAAGTTCTATTCAGTTTTGAAAGT
AGTAACATGTATGAAATCAAGAACAGCTTTGGGCAGAGGATTTATTTTGCAGCAGAAGAT
ACTAATTTCTGTATCCGAAATTGCTGTGGGCGGTCTAGACCTTTTACCTTGAGGATTACT
GATAATGTGGGTCGAGAAGTCATAACTCTGGAAAGACCACTAAGATGTAACTGTTGTTGT
TGCCCCTGCTGCCTTCAGGAGATAGAAATCCAAGCTCCTCCTGGTGTACCAGTAGGTTAT
GTTACTCAGACCTGGCACCCATGTCTAACAAAGTTTACAATTAAAAATCAGAAAAGAGAG
GATGTACTAAAAATTAGTGGTCCATGTATCGTGTGCAGCTGTATTGCGGGTGTTGATTTT
GAGATTACATCTCTTGATGAACAAATTGTGGTTGGCAGGATTTCTAAGCACTGGTCTGGG
TTTTTAAGAGAGGCATTTACTGATGCTGACAACTTTGGAATCCAATTCCCTAGAGACCTT
GATGTTAAAATGAAAGCCGTGATGATTGGTGCCTGTTTCCTCATTGACTACATGTTTTTT
GAAAGAACTAGGTAA
|
| Enzyme 20 GenBank Gene ID |
AF159441  |
| Enzyme 20 GeneCard ID |
PLSCR2  |
| Enzyme 20 GenAtlas ID |
PLSCR2  |
| Enzyme 20 HGNC ID |
HGNC:16494  |
| Enzyme 20 Chromosome Location |
3 |
| Enzyme 20 Locus |
3q24 |
| Enzyme 20 SNPs |
SNPJam Report  |
| Enzyme 20 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 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 |
12916 |
| Enzyme 21 Name |
Phospholipid scramblase 3 |
| Enzyme 21 Synonyms |
- PL scramblase 3
- Ca(2+)-dependent phospholipid scramblase 3
|
| Enzyme 21 Gene Name |
PLSCR3 |
| Enzyme 21 Protein Sequence |
>Phospholipid scramblase 3
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVAL
GSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAA
EESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTI
GHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQW
GGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAVTS
|
| Enzyme 21 Number of Residues |
295 |
| Enzyme 21 Molecular Weight |
31648.1 |
| Enzyme 21 Theoretical pI |
6.63 |
| Enzyme 21 GO Classification |
Not Available |
| Enzyme 21 General Function |
Involved in calcium ion binding |
| Enzyme 21 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 21 Pathways |
Not Available |
| Enzyme 21 Reactions |
Not Available |
| Enzyme 21 Pfam Domain Function |
|
| Enzyme 21 Signals |
|
| Enzyme 21 Transmembrane Regions |
|
| Enzyme 21 Essentiality |
Not Available |
| Enzyme 21 GenBank ID Protein |
31543417  |
| Enzyme 21 UniProtKB/Swiss-Prot ID |
Q9NRY6  |
| Enzyme 21 UniProtKB/Swiss-Prot Entry Name |
PLS3_HUMAN  |
| Enzyme 21 PDB ID |
Not Available |
| Enzyme 21 Cellular Location |
Not Available |
| Enzyme 21 Gene Sequence |
>888 bp
ATGGCAGGCTACTTGCCCCCCAAAGGCTACGCCCCTTCGCCCCCACCTCCCTACCCTGTC
ACCCCTGGGTACCCGGAGCCGGCGCTACATCCTGGGCCCGGGCAGGCGCCAGTGCCCGCC
CAGGTACCTGCCCCAGCTCCCGGCTTCGCCCTCTTCCCCTCGCCTGGCCCCGTGGCCTTG
GGGTCTGCTGCCCCCTTCTTGCCACTGCCAGGGGTGCCTTCTGGCCTCGAATTCCTGGTG
CAGATTGATCAGATTTTGATTCACCAGAAGGCTGAGCGAGTGGAAACGTTCCTAGGCTGG
GAGACCTGTAATCGGTATGAACTGCGCTCTGGGGCCGGGCAGCCCCTGGGTCAGGCGGCC
GAGGAGAGCAACTGCTGCGCCCGTCTGTGCTGTGGCGCCCGCCGGCCGCTGCGTGTCCGC
CTGGCCGACCCCGGGGACCGTGAGGTGCTGCGTTTGCTCCGCCCGCTGCACTGTGGCTGC
AGCTGCTGCCCCTGTGGCCTCCAGGAGATGGAAGTACAGGCTCCACCAGGCACCACCATT
GGCCACGTGCTACAGACCTGGCATCCCTTCCTCCCCAAGTTCTCCATCCAGGATGCCGAT
CGCCAGACAGTCTTGCGAGTGGTGGGGCCCTGCTGGACCTGTGGCTGTGGCACAGACACC
AACTTTGAGGTGAAGACTCGGGATGAATCCCGCAGTGTGGGCCGCATCAGCAAGCAGTGG
GGGGGCCTGGTCCGAGAAGCCCTCACAGATGCAGATGACTTTGGCCTACAGTTCCCGCTG
GACCTGGATGTGAGGGTGAAGGCTGTGCTGCTGGGAGCCACATTCCTCATTGACTACATG
TTCTTTGAGAAGCGAGGAGGCGCTGGGCCCTCTGCCGTCACCAGTTAG
|
| Enzyme 21 GenBank Gene ID |
NM_020360.2  |
| Enzyme 21 GeneCard ID |
PLSCR3  |
| Enzyme 21 GenAtlas ID |
PLSCR3  |
| Enzyme 21 HGNC ID |
HGNC:16495  |
| Enzyme 21 Chromosome Location |
1 |
| Enzyme 21 Locus |
17p13.1 |
| Enzyme 21 SNPs |
SNPJam Report  |
| Enzyme 21 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 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 |
12917 |
| Enzyme 22 Name |
Phospholipid scramblase 4 |
| Enzyme 22 Synonyms |
- PL scramblase 4
- Ca(2+)-dependent phospholipid scramblase 4
- Cell growth-inhibiting gene 43 protein
- TRA1
|
| Enzyme 22 Gene Name |
PLSCR4 |
| Enzyme 22 Protein Sequence |
>Phospholipid scramblase 4
MSGVVPTAPEQPAGEMENQTKPPDPRPDAPPEYNSHFLPGPPGTAVPPPTGYPGGLPMGY
YSPQQPSTFPLYQPVGGIHPVRYQPGKYPMPNQSVPITWMPGPTPMANCPPGLEYLVQLD
NIHVLQHFEPLEMMTCFETNNRYDIKNNSDQMVYIVTEDTDDFTRNAYRTLRPFVLRVTD
CMGREIMTMQRPFRCTCCCFCCPSARQELEVQCPPGVTIGFVAEHWNLCRAVYSIQNEKK
ENVMRVRGPCSTYGCGSDSVFEVKSLDGISNIGSIIRKWNGLLSAMADADHFDIHFPLDL
DVKMKAMIFGACFLIDFMYFERSPPQRSR
|
| Enzyme 22 Number of Residues |
329 |
| Enzyme 22 Molecular Weight |
37005.2 |
| Enzyme 22 Theoretical pI |
5.62 |
| Enzyme 22 GO Classification |
Not Available |
| Enzyme 22 General Function |
Involved in calcium ion binding |
| Enzyme 22 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 22 Pathways |
Not Available |
| Enzyme 22 Reactions |
Not Available |
| Enzyme 22 Pfam Domain Function |
|
| Enzyme 22 Signals |
|
| Enzyme 22 Transmembrane Regions |
|
| Enzyme 22 Essentiality |
Not Available |
| Enzyme 22 GenBank ID Protein |
9622872  |
| Enzyme 22 UniProtKB/Swiss-Prot ID |
Q9NRQ2  |
| Enzyme 22 UniProtKB/Swiss-Prot Entry Name |
PLS4_HUMAN  |
| Enzyme 22 PDB ID |
Not Available |
| Enzyme 22 Cellular Location |
Not Available |
| Enzyme 22 Gene Sequence |
>990 bp
ATGTCAGGTGTGGTACCCACAGCCCCTGAACAGCCTGCAGGTGAAATGGAAAATCAAACA
AAACCACCAGATCCAAGGCCTGATGCTCCTCCTGAATACAGTTCTCATTTTTTACCAGGA
CCCCCTGGAACAGCTGTCCCTCCACCTACTGGCTACCCAGGAGGCTTGCCTATGGGATAC
TACAGTCCACAGCAACCCAGTACCTTCCCTTTGTACCAGCCAGTTGGTGGTATCCATCCT
GTCCGGTATCAGCCTGGCAAATATCCTATGCCAAATCAGTCTGTTCCAATAACATGGATG
CCAGGGCCAACTCCTATGGCAAACTGCCCTCCTGGTCTGGAATACTTAGTTCAGTTGGAC
AACATACATGTTCTTCAGCATTTTGAGCCTCTGGAAATGATGACATGTTTTGAAACTAAT
AATAGATATGATATTAAAAACAACTCAGACCAGATGGTTTACGTTGTAACCGAAGACACA
GATGACTTTACCAGGAATGCCTATCGGACACTAAGGCCCTTCGTCCTCCGGGTCACTGAT
TGTATGGGCCGAGAAATCATGACAATGCAGAGACCCTTCAGATGCACCTGCTGTTGCTTC
TGTTGCCCCTCTGCCAGACAAGAGCTGGAGGTGCAGTGTCCTCCTGGTGTCACCATTGGC
TTTGTTGCGGAACATTGGAACCTGTGCAGGGCGGTGTACAGCATCCAAAATGAGAAGAAA
GAAAATGTGATGAGAGTTCGTGGGCCATGCTCAACCTATGGCTGTGGTTCAGATTCTGTT
TTTGAGGTCAAATCCCTTGATGGCATATCCAACATCGGCAGTATTATCCGGAAGTGGAAT
GGTTTGTTATCAGCAATGGCAGATGCTGACCATTTTGACATTCACTTCCCACTAGACCTG
GATGTGAAGATGAAAGCCATGATTTTTGGAGCTTGCTTCCTCATTGACTTCATGTATTTT
GAAAGATCTCCACCACAACGTTCAAGATAG
|
| Enzyme 22 GenBank Gene ID |
AF199023  |
| Enzyme 22 GeneCard ID |
PLSCR4  |
| Enzyme 22 GenAtlas ID |
PLSCR4  |
| Enzyme 22 HGNC ID |
HGNC:16497  |
| Enzyme 22 Chromosome Location |
3 |
| Enzyme 22 Locus |
3q24 |
| Enzyme 22 SNPs |
SNPJam Report  |
| Enzyme 22 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 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 |
12918 |
| Enzyme 23 Name |
Phospholipid scramblase family member 5 |
| Enzyme 23 Synonyms |
Not Available |
| Enzyme 23 Gene Name |
PLSCR5 |
| Enzyme 23 Protein Sequence |
>Phospholipid scramblase family member 5
MASKDAQNQRRGLPGFLPGAPDPDQSLPASSNPGNQAWQLSLPLPSSFLPTVSLPPGLEY
LSQLDLIIIHQQVELLGMILGTETSNKYEIKNSLGQRIYFAVEESICFNRTFCSTLRSCT
LRITDNSGREVITVNRPLRCNSCWCPCYLQELEIQAPPGTIVGYVTQKWDPFLPKFTIQN
ANKEDILKIVGPCVTCGCFGDVDFEVKTINEKLTIGKISKYWSGFVNDVFTNADNFGIHV
PADLDVTVKAAMIGACFLFDFMFFEHSLAGL
|
| Enzyme 23 Number of Residues |
271 |
| Enzyme 23 Molecular Weight |
30026.2 |
| Enzyme 23 Theoretical pI |
4.90 |
| Enzyme 23 GO Classification |
Not Available |
| Enzyme 23 General Function |
Not Available |
| Enzyme 23 Specific Function |
Not Available |
| Enzyme 23 Pathways |
Not Available |
| Enzyme 23 Reactions |
Not Available |
| Enzyme 23 Pfam Domain Function |
|
| Enzyme 23 Signals |
|
| Enzyme 23 Transmembrane Regions |
|
| Enzyme 23 Essentiality |
Not Available |
| Enzyme 23 GenBank ID Protein |
146229354  |
| Enzyme 23 UniProtKB/Swiss-Prot ID |
A0PG75  |
| Enzyme 23 UniProtKB/Swiss-Prot Entry Name |
PLS5_HUMAN  |
| Enzyme 23 PDB ID |
Not Available |
| Enzyme 23 Cellular Location |
Not Available |
| Enzyme 23 Gene Sequence |
>816 bp
ATGGCCTCTAAAGATGCCCAGAACCAAAGAAGAGGTCTGCCTGGTTTTCTTCCTGGAGCT
CCAGACCCAGACCAAAGCCTTCCTGCCTCTTCCAATCCAGGGAACCAAGCATGGCAGCTG
AGTCTCCCTCTGCCAAGCAGTTTCCTGCCAACAGTCAGTCTCCCTCCTGGTCTAGAATAT
TTAAGCCAGTTAGACCTGATAATTATACACCAGCAGGTGGAGCTGCTTGGAATGATACTT
GGTACTGAGACCTCCAACAAATATGAGATTAAAAACAGCTTGGGACAAAGAATTTACTTT
GCAGTGGAGGAAAGCATCTGCTTCAATCGTACTTTCTGTTCCACTCTGCGATCTTGCACC
CTGAGGATCACAGATAACTCAGGTCGAGAGGTCATTACAGTGAACAGGCCCTTGAGATGT
AACAGCTGCTGGTGCCCTTGCTACCTACAAGAGTTAGAAATCCAAGCCCCTCCTGGTACT
ATAGTTGGTTACGTTACGCAGAAGTGGGACCCCTTTCTGCCTAAATTCACAATCCAAAAT
GCAAACAAAGAAGATATTTTGAAAATTGTTGGTCCTTGTGTGACATGTGGCTGTTTTGGC
GATGTGGATTTTGAGGTGAAAACCATTAATGAAAAGCTTACAATTGGGAAGATTTCAAAG
TACTGGTCAGGATTTGTAAATGATGTCTTCACAAATGCTGACAATTTCGGAATTCATGTT
CCTGCAGATCTAGATGTAACAGTCAAAGCAGCAATGATCGGTGCCTGTTTTCTCTTTGAT
TTTATGTTCTTTGAACATTCACTGGCTGGATTATAA
|
| Enzyme 23 GenBank Gene ID |
NM_001085420.1  |
| Enzyme 23 GeneCard ID |
PLSCR5  |
| Enzyme 23 GenAtlas ID |
PLSCR5  |
| Enzyme 23 HGNC ID |
HGNC:19952  |
| Enzyme 23 Chromosome Location |
3 |
| Enzyme 23 Locus |
3q24 |
| Enzyme 23 SNPs |
SNPJam Report  |
| Enzyme 23 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 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 |
12929 |
| Enzyme 24 Name |
Phospholipase A1 member A |
| Enzyme 24 Synonyms |
- Phosphatidylserine-specific phospholipase A1
- PS-PLA1
|
| Enzyme 24 Gene Name |
PLA1A |
| Enzyme 24 Protein Sequence |
>Phospholipase A1 member A
MPPGPWESCFWVGGLILWLSVGSSGDAPPTPQPKCADFQSANLFEGTDLKVQFLLFVPSN
PSCGQLVEGSSDLQNSGFNATLGTKLIIHGFRVLGTKPSWIDTFIRTLLRATNANVIAVD
WIYGSTGVYFSAVKNVIKLSLEISLFLNKLLVLGVSESSIHIIGVSLGAHVGGMVGQLFG
GQLGQITGLDPAGPEYTRASVEERLDAGDALFVEAIHTDTDNLGIRIPVGHVDYFVNGGQ
DQPGCPTFFYAGYSYLICDHMRAVHLYISALENSCPLMAFPCASYKAFLAGRCLDCFNPF
LLSCPRIGLVEQGGVKIEPLPKEVKVYLLTTSSAPYCMHHSLVEFHLKELRNKDTNIEVT
FLSSNITSSSKITIPKQQRYGKGIIAHATPQCQINQVKFKFQSSNRVWKKDRTTIIGKFC
TALLPVNDREKMVCLPEPVNLQASVTVSCDLKIACV
|
| Enzyme 24 Number of Residues |
456 |
| Enzyme 24 Molecular Weight |
49715.0 |
| Enzyme 24 Theoretical pI |
7.40 |
| Enzyme 24 GO Classification |
| Function |
|
| Process |
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
| — |
|
| Enzyme 24 General Function |
Involved in catalytic activity |
| Enzyme 24 Specific Function |
Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1- acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid (PA) or phosphatidylinositol (PI). Isoform 2 hydrolyzes lyso-PS but not PS. Hydrolysis of lyso-PS in peritoneal mast cells activated by receptors for IgE leads to stimulate histamine production |
| Enzyme 24 Pathways |
Not Available |
| Enzyme 24 Reactions |
Not Available |
| Enzyme 24 Pfam Domain Function |
|
| Enzyme 24 Signals |
|
| Enzyme 24 Transmembrane Regions |
|
| Enzyme 24 Essentiality |
Not Available |
| Enzyme 24 GenBank ID Protein |
4090960  |
| Enzyme 24 UniProtKB/Swiss-Prot ID |
Q53H76  |
| Enzyme 24 UniProtKB/Swiss-Prot Entry Name |
PLA1A_HUMAN  |
| Enzyme 24 PDB ID |
Not Available |
| Enzyme 24 Cellular Location |
Not Available |
| Enzyme 24 Gene Sequence |
>1371 bp
ATGCCCCCAGGTCCCTGGGAGAGCTGCTTCTGGGTGGGGGGCCTCATTTTGTGGCTCAGC
GTTGGAAGTTCAGGGGATGCACCTCCTACCCCACAGCCAAAGTGCGCTGACTTCCAGAGC
GCCAACCTTTTTGAAGGCACCGATCTCAAAGTCCAGTTTCTCCTCTTTGTCCCTTCGAAT
CCTAGCTGTGGGCAGCTAGTAGAAGGAAGCAGTGACCTCCAAAACTCTGGGTTCAATGCC
ACTCTGGGAACCAAACTAATTATCCATGGATTCAGGGTTTTAGGAACAAAGCCTTCCTGG
ATTGACACATTTATTAGAACCCTTCTGCGTGCAACGAATGCTAATGTGATTGCCGTGGAC
TGGATTTATGGGTCTACAGGAGTCTACTTCTCAGCTGTGAAAAATGTGATTAAGTTGAGC
CTCGAGATCTCCCTTTTCCTCAATAAACTCCTGGTGCTGGGTGTGTCGGAATCCTCAATC
CACATCATTGGTGTTAGCCTGGGGGCCCACGTTGGGGGCATGGTGGGACAGCTCTTCGGA
GGCCAGCTGGGACAGATCACAGGCCTGGACCCCGCTGGACCTGAGTACACCAGGGCCAGT
GTGGAAGAGCGCTTGGATGCTGGAGATGCCCTCTTCGTGGAAGCCATCCACACAGACACC
GACAATTTGGGTATTCGGATTCCCGTTGGACATGTGGACTACTTCGTCAACGGAGGCCAA
GACCAACCTGGCTGCCCCACCTTCTTTTACGCAGGTTATAGTTATCTGATCTGTGATCAC
ATGAGGGCTGTGCACCTCTACATCAGCGCCCTGGAGAATTCCTGTCCACTGATGGCCTTT
CCCTGTGCCAGCTACAAGGCCTTCCTTGCTGGACGCTGTCTGGATTGCTTTAACCCTTTT
CTGCTTTCCTGCCCAAGGATAGGACTGGTGGAACAAGGTGGTGTCAAGATAGAGCCGCTC
CCCAAGGAAGTGAAAGTCTACCTCCTGACTACTTCCAGTGCTCCGTACTGCATGCATCAC
AGCCTCGTGGAGTTTCACTTGAAGGAACTGAGAAACAAGGACACCAACATCGAGGTTACC
TTCCTTAGCAGTAACATCACCTCTTCATCTAAGATCACCATACCTAAGCAGCAACGCTAT
GGGAAAGGAATCATAGCCCATGCCACCCCACAATGCCAGATAAACCAAGTGAAATTCAAG
TTTCAGTCTTCCAACCGAGTTTGGAAAAAAGACCGGACTACCATTATTGGGAAGTTCTGC
ACTGCCCTTTTGCCTGTCAATGACAGAGAAAAGATGGTCTGCTTACCTGAACCAGTGAAC
TTACAAGCAAGTGTGACTGTTTCCTGTGACCTGAAGATAGCCTGTGTGTAG
|
| Enzyme 24 GenBank Gene ID |
AF035268  |
| Enzyme 24 GeneCard ID |
PLA1A  |
| Enzyme 24 GenAtlas ID |
PLA1A  |
| Enzyme 24 HGNC ID |
HGNC:17661  |
| Enzyme 24 Chromosome Location |
3 |
| Enzyme 24 Locus |
3q13.13-q13.2 |
| Enzyme 24 SNPs |
SNPJam Report  |
| Enzyme 24 General References |
- van Groningen JJ, Egmond MR, Bloemers HP, Swart GW: nmd, a novel gene differentially expressed in human melanoma cell lines, encodes a new atypical member of the enzyme family of lipases. FEBS Lett. 1997 Mar 3;404(1):82-6. [PubMed
]
- Nagai Y, Aoki J, Sato T, Amano K, Matsuda Y, Arai H, Inoue K: An alternative splicing form of phosphatidylserine-specific phospholipase A1 that exhibits lysophosphatidylserine-specific lysophospholipase activity in humans. J Biol Chem. 1999 Apr 16;274(16):11053-9. [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
]
- 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, Wen XY, Stewart AK, Hegele RA: Polymorphisms in the gene encoding phosphatidylserine-specific phospholipase A1 ( PSPLA1). J Hum Genet. 2002;47(11):611-3. [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 |
12930 |
| Enzyme 25 Name |
Serum deprivation-response protein |
| Enzyme 25 Synonyms |
- Cavin-2
- PS-p68
- Phosphatidylserine-binding protein
|
| Enzyme 25 Gene Name |
SDPR |
| Enzyme 25 Protein Sequence |
>Serum deprivation-response protein
MGEDAAQAEKFQHPGSDMRQEKPSSPSPMPSSTPSPSLNLGNTEEAIRDNSQVNAVTVLT
LLDKLVNMLDAVQENQHKMEQRQISLEGSVKGIQNDLTKLSKYQASTSNTVSKLLEKSRK
VSAHTRAVKERMDRQCAQVKRLENNHAQLLRRNHFKVLIFQEENEIPASVFVKQPVSGAV
EGKEELPDENKSLEETLHTVDLSSDDDLPHDEEALEDSAEEKVEESRAEKIKRSSLKKVD
SLKKAFSRQNIEKKMNKLGTKIVSVERREKIKKSLTSNHQKISSGKSSPFKVSPLTFGRK
KVREGESHAENETKSEDLPSSEQMPNDQEEESFAEGHSEASLASALVEGEIAEEAAEKAT
SRGSNSGMDSNIDLTIVEDEEEESVALEQAQKVRYEGSYALTSEEAERSDGDPVQPAVLQ
VHQTS
|
| Enzyme 25 Number of Residues |
425 |
| Enzyme 25 Molecular Weight |
47172.8 |
| Enzyme 25 Theoretical pI |
4.88 |
| Enzyme 25 GO Classification |
Not Available |
| Enzyme 25 General Function |
Involved in phosphatidylserine binding |
| Enzyme 25 Specific Function |
May play a role in targeting PRKCA to caveolae |
| Enzyme 25 Pathways |
Not Available |
| Enzyme 25 Reactions |
Not Available |
| Enzyme 25 Pfam Domain Function |
Not Available |
| Enzyme 25 Signals |
|
| Enzyme 25 Transmembrane Regions |
|
| Enzyme 25 Essentiality |
Not Available |
| Enzyme 25 GenBank ID Protein |
4336416  |
| Enzyme 25 UniProtKB/Swiss-Prot ID |
O95810  |
| Enzyme 25 UniProtKB/Swiss-Prot Entry Name |
SDPR_HUMAN  |
| Enzyme 25 PDB ID |
Not Available |
| Enzyme 25 Cellular Location |
Not Available |
| Enzyme 25 Gene Sequence |
>1278 bp
ATGGGAGAGGACGCTGCACAGGCCGAAAAGTTCCAGCACCCTGGGTCTGACATGCGGCAG
GAAAAGCCCTCGAGCCCCAGCCCGATGCCTTCCTCCACACCAAGCCCCAGCCTGAACCTA
GGGAACACAGAGGAGGCCATCCGGGACAACTCACAGGTGAACGCAGTCACGGTGCTCACG
CTCCTGGACAAGCTGGTGAACATGCTAGACGCTGTGCAGGAGAACCAGCACAAGATGGAG
CAGCGACAGATCAGTTTGGAGGGCTCCGTGAAGGGCATCCAGAATGACCTCACCAAGCTC
TCCAAGTACCAGGCCTCCACCAGCAACACGGTGAGCAAGCTGCTGGAGAAGTCCCGCAAG
GTCAGCGCCCACACGCGCGCGGTCAAAGAGCGCATGGATAGGCAGTGCGCACAGGTGAAG
CGGCTGGAGAACAACCACGCCCAGCTCCTCCGACGCAACCATTTCAAAGTGCTCATCTTC
CAGGAGGAAAATGAGATCCCTGCCAGCGTGTTTGTGAAACAGCCCGTTTCCGGTGCCGTG
GAAGGGAAGGAGGAGCTTCCGGATGAAAACAAATCCCTGGAGGAAACCCTGCACACCGTG
GACCTCTCCTCAGATGATGATTTGCCCCACGATGAGGAGGCCCTGGAAGACAGTGCCGAG
GAAAAGGTGGAAGAAAGTAGGGCAGAGAAAATAAAAAGATCCAGCCTGAAGAAAGTGGAT
AGCCTCAAGAAAGCATTTTCTCGCCAGAACATCGAGAAAAAGATGAACAAGCTGGGGACA
AAGATCGTATCTGTAGAGAGGAGAGAGAAGATTAAGAAATCTCTCACGTCAAATCACCAG
AAAATATCCTCAGGAAAAAGCTCCCCCTTCAAGGTTTCTCCCCTCACTTTCGGGCGGAAG
AAAGTCCGAGAGGGAGAAAGCCATGCAGAAAATGAGACCAAGTCAGAAGACCTGCCTAGC
AGTGAGCAGATGCCAAATGACCAGGAAGAGGAGTCCTTTGCAGAGGGTCATTCCGAAGCG
TCCCTCGCCAGCGCTCTGGTGGAAGGGGAAATTGCAGAGGAGGCTGCTGAGAAGGCGACC
TCCAGGGGGAGTAACTCGGGGATGGACAGCAACATCGACTTGACTATTGTGGAAGATGAA
GAGGAGGAGTCAGTGGCCCTGGAACAGGCACAGAAGGTACGCTATGAGGGTAGCTACGCG
CTAACATCCGAGGAGGCGGAGCGCTCCGATGGGGACCCCGTGCAGCCCGCCGTGCTCCAG
GTGCACCAGACCTCCTGA
|
| Enzyme 25 GenBank Gene ID |
AF085481  |
| Enzyme 25 GeneCard ID |
SDPR  |
| Enzyme 25 GenAtlas ID |
SDPR  |
| Enzyme 25 HGNC ID |
HGNC:10690  |
| Enzyme 25 Chromosome Location |
2 |
| Enzyme 25 Locus |
2q32-q33 |
| Enzyme 25 SNPs |
SNPJam Report  |
| Enzyme 25 General References |
- Gustincich S, Vatta P, Goruppi S, Wolf M, Saccone S, Della Valle G, Baggiolini M, Schneider C: The human serum deprivation response gene (SDPR) maps to 2q32-q33 and codes for a phosphatidylserine-binding protein. Genomics. 1999 Apr 1;57(1):120-9. [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
]
- Burgener R, Wolf M, Ganz T, Baggiolini M: Purification and characterization of a major phosphatidylserine-binding phosphoprotein from human platelets. Biochem J. 1990 Aug 1;269(3):729-34. [PubMed
]
- Wolf-Yadlin A, Hautaniemi S, Lauffenburger DA, White FM: Multiple reaction monitoring for robust quantitative proteomic analysis of cellular signaling networks. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5860-5. Epub 2007 Mar 26. [PubMed
]
- Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed
]
- Ogata T, Ueyama T, Isodono K, Tagawa M, Takehara N, Kawashima T, Harada K, Takahashi T, Shioi T, Matsubara H, Oh H: MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK pathway, induces cardiac dysfunction and conduction disturbance. Mol Cell Biol. 2008 May;28(10):3424-36. Epub 2008 Mar 10. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- 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
]
|
| 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 |
13172 |
| Enzyme 26 Name |
Transcriptional regulator ATRX |
| Enzyme 26 Synonyms |
- ATP-dependent helicase ATRX
- X-linked helicase II
- X-linked nuclear protein
- XNP
- Znf-HX
|
| Enzyme 26 Gene Name |
ATRX |
| Enzyme 26 Protein Sequence |
>Transcriptional regulator ATRX
MTAEPMSESKLNTLVQKLHDFLAHSSEESEETSSPPRLAMNQNTDKISGSGSNSDMMENS
KEEGTSSSEKSKSSGSSRSKRKPSIVTKYVESDDEKPLDDETVNEDASNENSENDITMQS
LPKGTVIVQPEPVLNEDKDDFKGPEFRSRSKMKTENLKKRGEDGLHGIVSCTACGQQVNH
FQKDSIYRHPSLQVLICKNCFKYYMSDDISRDSDGMDEQCRWCAEGGNLICCDFCHNAFC
KKCILRNLGRKELSTIMDENNQWYCYICHPEPLLDLVTACNSVFENLEQLLQQNKKKIKV
DSEKSNKVYEHTSRFSPKKTSSNCNGEEKKLDDSCSGSVTYSYSALIVPKEMIKKAKKLI
ETTANMNSSYVKFLKQATDNSEISSATKLRQLKAFKSVLADIKKAHLALEEDLNSEFRAM
DAVNKEKNTKEHKVIDAKFETKARKGEKPCALEKKDISKSEAKLSRKQVDSEHMHQNVPT
EEQRTNKSTGGEHKKSDRKEEPQYEPANTSEDLDMDIVSVPSSVPEDIFENLETAMEVQS
SVDHQGDGSSGTEQEVESSSVKLNISSKDNRGGIKSKTTAKVTKELYVKLTPVSLPNSPI
KGADCQEVPQDKDGYKSCGLNPKLEKCGLGQENSDNEHLVENEVSLLLEESDLRRSPRVK
TTPLRRPTETNPVTSNSDEECNETVKEKQKLSVPVRKKDKRNSSDSAIDNPKPNKLPKSK
QSETVDQNSDSDEMLAILKGVSRMSHSSSSDTDINEIHTNHKTLYDLKTQAGKDDKGKRK
RKSSTSGSDFDTKKGKSAKSSIISKKKRQTQSESSNYDSELEKEIKSMSKIGAARTTKKR
IPNTKDFDSSEDEKHSKKGMDNQGHKNLKTSQEGSSDDAERKQERETFSSAEGTVDKDTT
IMELRDRLPKKQQASASTDGVDKLSGKEQSFTSLEVRKVAETKEKSKHLKTKTCKKVQDG
LSDIAEKFLKKDQSDETSEDDKKQSKKGTEEKKKPSDFKKKVIKMEQQYESSSDGTEKLP
EREEICHFPKGIKQIKNGTTDGEKKSKKIRDKTSKKKDELSDYAEKSTGKGDSCDSSEDK
KSKNGAYGREKKRCKLLGKSSRKRQDCSSSDTEKYSMKEDGCNSSDKRLKRIELRERRNL
SSKRNTKEIQSGSSSSDAEESSEDNKKKKQRTSSKKKAVIVKEKKRNSLRTSTKRKQADI
TSSSSSDIEDDDQNSIGEGSSDEQKIKPVTENLVLSSHTGFCQSSGDEALSKSVPVTVDD
DDDDNDPENRIAKKMLLEEIKANLSSDEDGSSDDEPEEGKKRTGKQNEENPGDEEAKNQV
NSESDSDSEESKKPRYRHRLLRHKLTVSDGESGEEKKTKPKEHKEVKGRNRRKVSSEDSE
DSDFQESGVSEEVSESEDEQRPRTRSAKKAELEENQRSYKQKKKRRRIKVQEDSSSENKS
NSEEEEEEKEEEEEEEEEEEEEEEDENDDSKSPGKGRKKIRKILKDDKLRTETQNALKEE
EERRKRIAEREREREKLREVIEIEDASPTKCPITTKLVLDEDEETKEPLVQVHRNMVIKL
KPHQVDGVQFMWDCCCESVKKTKKSPGSGCILAHCMGLGKTLQVVSFLHTVLLCDKLDFS
TALVVCPLNTALNWMNEFEKWQEGLKDDEKLEVSELATVKRPQERSYMLQRWQEDGGVMI
IGYEMYRNLAQGRNVKSRKLKEIFNKALVDPGPDFVVCDEGHILKNEASAVSKAMNSIRS
RRRIILTGTPLQNNLIEYHCMVNFIKENLLGSIKEFRNRFINPIQNGQCADSTMVDVRVM
KKRAHILYEMLAGCVQRKDYTALTKFLPPKHEYVLAVRMTSIQCKLYQYYLDHLTGVGNN
SEGGRGKAGAKLFQDFQMLSRIWTHPWCLQLDYISKENKGYFDEDSMDEFIASDSDETSM
SLSSDDYTKKKKKGKKGKKDSSSSGSGSDNDVEVIKVWNSRSRGGGEGNVDETGNNPSVS
LKLEESKATSSSNPSSPAPDWYKDFVTDADAEVLEHSGKMVLLFEILRMAEEIGDKVLVF
SQSLISLDLIEDFLELASREKTEDKDKPLIYKGEGKWLRNIDYYRLDGSTTAQSRKKWAE
EFNDETNVRGRLFIISTKAGSLGINLVAANRVIIFDASWNPSYDIQSIFRVYRFGQTKPV
YVYRFLAQGTMEDKIYDRQVTKQSLSFRVVDQQQVERHFTMNELTELYTFEPDLLDDPNS
EKKKKRDTPMLPKDTILAELLQIHKEHIVGYHEHDSLLDHKEEEELTEEERKAAWAEYEA
EKKGLTMRFNIPTGTNLPPVSFNSQTPYIPFNLGALSAMSNQQLEDLINQGREKVVEATN
SVTAVRIQPLEDIISAVWKENMNLSEAQVQALALSRQASQELDVKRREAIYNDVLTKQQM
LISCVQRILMNRRLQQQYNQQQQQQMTYQQATLGHLMMPKPPNLIMNPSNYQQIDMRGMY
QPVAGGMQPPPLQRAPPPMRSKNPGPSQGKSM
|
| Enzyme 26 Number of Residues |
2492 |
| Enzyme 26 Molecular Weight |
282521.6 |
| Enzyme 26 Theoretical pI |
6.57 |
| Enzyme 26 GO Classification |
| Function |
- ATP binding
- DNA binding
- adenyl nucleotide binding
- adenyl ribonucleotide binding
- binding
- catalytic activity
- cation binding
- helicase activity
- hydrolase activity
- hydrolase activity, acting on acid anhydrides
- hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
- ion binding
- metal ion binding
- nucleic acid binding
- nucleoside binding
- nucleoside-triphosphatase activity
- protein binding
- purine nucleoside binding
- pyrophosphatase activity
- transition metal ion binding
- zinc ion binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 26 General Function |
Involved in nucleic acid binding |
| Enzyme 26 Specific Function |
Could be a global transcriptional regulator. Modifies gene expression by affecting chromatin. May be involved in brain development and facial morphogenesis |
| Enzyme 26 Pathways |
Not Available |
| Enzyme 26 Reactions |
- ATP + H2O = ADP + phosphate
|
| Enzyme 26 Pfam Domain Function |
|
| Enzyme 26 Signals |
|
| Enzyme 26 Transmembrane Regions |
|
| Enzyme 26 Essentiality |
Not Available |
| Enzyme 26 GenBank ID Protein |
6960326  |
| Enzyme 26 UniProtKB/Swiss-Prot ID |
P46100  |
| Enzyme 26 UniProtKB/Swiss-Prot Entry Name |
ATRX_HUMAN  |
| Enzyme 26 PDB ID |
Not Available |
| Enzyme 26 Cellular Location |
Not Available |
| Enzyme 26 Gene Sequence |
>7479 bp
ATGACCGCTGAGCCCATGAGTGAAAGCAAGTTGAATACATTGGTGCAGAAGCTTCATGAC
TTCCTTGCACACTCATCAGAAGAATCTGAAGAAACAAGTTCTCCTCCACGACTTGCAATG
AATCAAAACACAGATAAAATCAGTGGTTCTGGAAGTAACTCTGATATGATGGAAAACAGC
AAGGAAGAGGGAACTAGCTCTTCAGAAAAATCCAAGTCTTCAGGATCGTCACGATCAAAG
AGGAAACCTTCAATTGTAACAAAGTATGTAGAATCAGATGATGAAAAACCTTTGGATGAT
GAAACTGTAAATGAAGATGCGTCTAATGAAAATTCAGAAAATGATATTACTATGCAGAGC
TTGCCAAAAGGTACAGTGATTGTACAGCCAGAGCCAGTGCTGAATGAAGACAAAGATGAT
TTTAAAGGGCCTGAATTTAGAAGCAGAAGTAAAATGAAAACTGAAAATCTCAAAAAACGC
GGAGAAGATGGGCTTCATGGGATTGTGAGCTGCACTGCTTGTGGACAACAGGTCAATCAT
TTTCAAAAAGATTCCATTTATAGACACCCTTCATTGCAAGTTCTTATTTGTAAGAATTGC
TTTAAGTATTACATGAGTGATGATATTAGCCGTGACTCAGATGGAATGGATGAACAATGT
AGGTGGTGTGCGGAAGGTGGAAACTTGATTTGTTGTGACTTTTGCCATAATGCTTTCTGC
AAGAAATGCATTCTACGCAACCTTGGTCGAAAGGAGTTGTCCACAATAATGGATGAAAAC
AACCAATGGTATTGCTACATTTGTCACCCAGAGCCTTTGTTGGACTTGGTCACTGCATGT
AACAGCGTATTTGAGAATTTAGAACAGTTGTTGCAGCAAAATAAGAAGAAGATAAAAGTT
GACAGTGAAAAGAGTAATAAAGTATATGAACATACATCCAGATTTTCTCCAAAGAAGACT
AGTTCAAATTGTAATGGAGAAGAAAAGAAATTAGATGATTCCTGTTCTGGCTCTGTAACC
TACTCTTATTCCGCACTAATTGTGCCCAAAGAGATGATTAAGAAGGCAAAAAAACTGATT
GAGACCACAGCCAACATGAACTCCAGTTATGTTAAATTTTTAAAGCAGGCAACAGATAAT
TCAGAAATCAGTTCTGCTACAAAATTACGTCAGCTTAAGGCTTTTAAGTCTGTGTTGGCT
GATATTAAGAAGGCTCATCTTGCATTGGAAGAAGACTTAAATTCCGAGTTTCGAGCGATG
GATGCTGTAAACAAAGAGAAAAATACCAAAGAGCATAAAGTCATAGATGCTAAGTTTGAA
ACAAAAGCACGAAAAGGAGAAAAACCTTGTGCTTTGGAAAAGAAGGATATTTCAAAGTCA
GAAGCTAAACTTTCAAGAAAACAGGTAGATAGTGAGCACATGCATCAGAATGTTCCAACA
GAGGAACAAAGAACAAATAAAAGTACCGGTGGTGAACATAAGAAATCTGATAGAAAAGAA
GAACCTCAATATGAACCTGCCAACACTTCTGAAGATTTAGACATGGATATTGTGTCTGTT
CCTTCCTCAGTTCCAGAAGACATTTTTGAGAATCTTGAGACTGCTATGGAAGTTCAGAGT
TCAGTTGATCATCAAGGGGATGGCAGCAGTGGAACTGAACAAGAAGTGGAGAGTTCATCT
GTAAAATTAAATATTTCTTCAAAAGACAACAGAGGAGGTATTAAATCAAAAACTACAGCT
AAAGTAACAAAAGAATTATATGTTAAACTCACTCCTGTTTCCCTTTCTAATTCCCCAATT
AAAGGTGCTGATTGTCAGGAAGTTCCACAAGATAAAGATGGCTATAAAAGTTGTGGTCTG
AACCCCAAGTTAGAGAAATGTGGACTTGGACAGGAAAACAGTGATAATGAGCATTTGGTT
GAAAATGAAGTTTCATTACTTTTAGAGGAATCTGATCTTCGAAGATCCCCACGTGTAAAG
ACTACACCCTTGAGGCGACCGACAGAAACTAACCCTGTAACATCTAATTCAGATGAAGAA
TGTAATGAAACAGTTAAGGAGAAACAAAAACTATCAGTTCCAGTGAGAAAAAAGGATAAG
CGTAATTCTTCTGACAGTGCTATAGATAATCCTAAGCCTAATAAATTGCCAAAATCTAAG
CAATCAGAGACTGTGGATCAAAATTCAGATTCTGATGAAATGCTAGCAATCCTCAAAGAG
GTGAGCAGGATGAGTCACAGTTCTTCTTCAGATACTGATATTAATGAAATTCATACAAAC
CATAAGACTTTGTATGATTTAAAGACTCAGGCGGGGAAAGATGATAAAGGAAAAAGGAAA
CGAAAAAGTTCTACATCTGGCTCAGATTTTGATACTAAAAAGGGCAAATCAGCTAAGAGC
TCTATAATTTCTAAAAAGAAACGACAAACCCAGTCTGAGTCTTCTAATTATGACTCAGAA
TTAGAAAAAGAGATAAAGAGCATGAGTAAAATTGGTGCTGCCAGAACCACCAAAAAAAGA
ATTCCAAATACAAAAGATTTTGACTCTTCTGAAGATGAGAAACACAGCAAAAAAGGAATG
GATAATCAAGGGCACAAAAATTTGAAGACCTCACAAGAAGGATCATCTGATGATGCTGAA
AGAAAACAAGAGAGAGAGACTTTCTCTTCAGCAGAAGGCACAGTTGATAAAGACACGACC
ATCATGGAATTAAGAGATCGACTTCCTAAGAAGCAGCAAGCAAGTGCTTCCACTGATGGT
GTCGATAAGCTTTCTGGGAAAGAGCAGAGTTTTACTTCTTTGGAAGTTAGAAAAGTTGCT
GAAACTAAAGAAAAGAGCAAGCATCTCAAAACCAAAACATGTAAAAAAGTACAGGATGGC
TTATCTGATATTGCAGAGAAATTCCTAAAGAAAGACCAGAGCGATGAAACTTCTGAAGAT
GATAAAAAGCAGAGCAAAAAGGGAACTGAAGAAAAAAAGAAACCTTCAGACTTTAAGAAA
AAAGTAATTAAAATGGAACAACAGTATGAATCTTCATCTGATGGCACTGAAAAGTTACCT
GAGCGAGAAGAAATTTGTCATTTTCCTAAGGGCATAAAACAAATTAAGAATGGAACAACT
GATGGAGAAAAGAAAAGTAAAAAAATAAGAGATAAAACTTCTAAAAAGAAGGATGAATTA
TCTGATTATGCTGAGAAGTCAACAGGGAAAGGAGATAGTTGTGACTCTTCAGAGGATAAA
AAGAGTAAGAATGGAGCATATGGTAGAGAGAAGAAAAGGTGCAAGTTGCTTGGAAAGAGT
TCAAGGAAGAGACAAGATTGTTCATCATCTGATACTGAGAAATATTCCATGAAAGAAGAT
GGTTGTAACTCTTCTGATAAGAGACTGAAAAGAATAGAATTGAGGGAAAGAAGAAATTTA
AGTTCAAAGAGAAATACTAAGGAAATACAAAGTGGCTCATCATCATCTGATGCTGAGGAA
AGTTCTGAAGATAATAAAAAGAAGAAGCAAAGAACTTCATCTAAAAAGAAGGCAGTCATT
GTCAAGGAGAAAAAGAGAAACTCCCTAAGAACAAGCACTAAAAGGAAGCAAGCTGACATT
ACATCCTCATCTTCTTCTGATATAGAAGATGATGATCAGAATTCTATAGGTGAGGGAAGC
AGCGATGAACAGAAAATTAAGCCTGTGACTGAAAATTTAGTGCTGTCTTCACATACTGGA
TTTTGCCAATCTTCAGGAGATGAAGCCTTATCTAAATCAGTGCCTGTCACAGTGGATGAT
GATGATGACGACAATGATCCTGAGAATAGAATTGCCAAGAAGATGCTTTTAGAAGAAATT
AAAGCCAATCTTTCCTCTGATGAGGATGGATCTTCAGATGATGAGCCAGAAGAAGGGAAA
AAAAGAACTGGAAAACAAAATGAAGAAAACCCAGGAGATGAGGAAGCAAAAAATCAAGTC
AATTCTGAATCAGATTCAGATTCTGAAGAATCTAAGAAGCCAAGATACAGACATAGGCTT
TTGCGGCACAAATTGACTGTGAGTGACGGAGAATCTGGAGAAGAAAAAAAGACAAAGCCT
AAAGAGCATAAAGAAGTCAAAGGCAGAAACAGAAGAAAGGTGAGCAGTGAAGATTCAGAA
GATTCTGATTTTCAGGAATCAGGAGTTAGTGAAGAAGTTAGTGAATCCGAAGATGAACAG
CGGCCCAGAACAAGGTCTGCAAAGAAAGCAGAGTTGGAAGAAAATCAGCGGAGCTATAAA
CAGAAAAAGAAAAGGCGACGTATTAAGGTTCAAGAAGATTCATCCAGTGAAAACAAGAGT
AATTCTGAGGAAGAAGAGGAGGAAAAAGAAGAGGAGGAGGAAGAGGAGGAGGAGGAGGAA
GAGGAGGAGGAAGATGAAAATGATGATTCCAAGTCTCCTGGAAAAGGCAGAAAGAAAATT
CGGAAGATTCTTAAAGATGATAAACTGAGAACAGAAACACAAAATGCTCTTAAGGAAGAG
GAAGAGAGACGAAAACGTATTGCTGAGAGGGAGCGTGAGCGAGAAAAATTGAGAGAGGTG
ATAGAAATTGAAGATGCTTCACCCACCAAGTGTCCAATAACAACCAAGTTGGTTTTAGAT
GAAGATGAAGAAACCAAAGAACCTTTAGTGCAGGTTCATAGAAATATGGTTATCAAATTG
AAACCCCATCAAGTAGATGGTGTTCAGTTTATGTGGGATTGCTGCTGTGAGTCTGTGAAA
AAAACAAAGAAATCTCCAGGTTCAGGATGCATTCTTGCCCACTGTATGGGCCTTGGTAAG
ACTTTACAGGTGGTAAGTTTTCTTCATACAGTTCTTTTGTGTGACAAACTGGATTTCAGC
ACGGCGTTAGTGGTTTGTCCTCTTAATACTGCTTTGAATTGGATGAATGAATTTGAGAAG
TGGCAAGAGGGATTAAAAGATGATGAGAAGCTTGAGGTTTCTGAATTAGCAACTGTGAAA
CGTCCTCAGGAGAGAAGCTACATGCTGCAGAGGTGGCAAGAAGATGGTGGTGTTATGATC
ATAGGCTATGAGATGTATAGAAATCTTGCTCAAGGAAGGAATGTGAAGAGTCGGAAACTT
AAAGAAATATTTAACAAAGCTTTGGTTGATCCAGGCCCTGATTTTGTTGTTTGTGATGAA
GGCCATATTCTAAAAAATGAAGCATCTGCTGTTTCTAAAGCTATGAATTCTATACGATCA
AGGAGGAGGATTATTTTAACAGGAACACCACTTCAAAATAACCTAATTGAGTATCATTGT
ATGGTTAATTTTATCAAGGAAAATTTACTTGGATCCATTAAGGAGTTCAGGAATAGATTT
ATAAATCCAATTCAAAATGGTCAGTGTGCAGATTCTACCATGGTAGATGTCAGAGTGATG
AAAAAACGTGCTCACATTCTCTATGAGATGTTAGCTGGATGTGTTCAGAGGAAAGATTAT
ACAGCATTAACAAAATTCTTGCCTCCAAAACACGAATATGTGTTAGCTGTGAGAATGACT
TCTATTCAGTGCAAGCTCTATCAGTACTACTTAGATCACTTAACAGGTGTGGGCAATAAT
AGTGAAGGTGGAAGAGGAAAGGCAGGTGCAAAGCTTTTCCAAGATTTTCAGATGTTAAGT
AGAATATGGACTCATCCTTGGTGTTTGCAGCTAGACTACATTAGCAAAGAAAATAAGGGT
TATTTTGATGAAGACAGTATGGATGAATTTATAGCCTCAGATTCTGATGAAACCTCCATG
AGTTTAAGCTCCGATGATTATACAAAAAAGAAGAAAAAAGGGAAAAAGGGGAAAAAAGAT
AGTAGCTCAAGTGGAAGTGGCAGTGACAATGATGTTGAAGTGATTAAGGTCTGGAATTCA
AGATCTCGGGGAGGTGGTGAAGGAAATGTGGATGAAACAGGAAACAATCCTTCTGTTTCT
TTAAAACTGGAAGAAAGTAAAGCTACTTCTTCTTCTAATCCAAGCAGCCCAGCTCCAGAC
TGGTACAAAGATTTTGTTACAGATGCTGATGCTGAGGTTTTAGAGCATTCTGGGAAAATG
GTACTTCTCTTTGAAATTCTTCGAATGGCAGAGGAAATTGGGGATAAAGTCCTTGTTTTC
AGCCAGTCCCTCATATCTCTGGACTTGATTGAAGATTTTCTTGAATTAGCTAGTAGGGAG
AAGACAGAAGATAAAGATAAACCCCTTATTTATAAAGGTGAGGGGAAGTGGCTTCGAAAC
ATTGACTATTACCGTTTAGATGGTTCCACTACTGCACAGTCAAGGAAGAAGTGGGCTGAA
GAATTTAATGATGAAACTAATGTGAGAGGACGATTATTTATCATTTCTACTAAAGCAGGA
TCTCTAGGAATTAATCTGGTAGCTGCTAATCGAGTAATTATATTCGACGCTTCTTGGAAT
CCATCTTATGACATCCAGAGTATATTCAGAGTTTATCGCTTTGGACAAACTAAGCCTGTT
TATGTATATAGGTTCTTAGCTCAGGGAACCATGGAAGATAAGATTTATGATCGGCAAGTA
ACTAAGCAGTCACTGTCTTTTCGAGTTGTTGATCAGCAGCAGGTGGAGCGTCATTTTACT
ATGAATGAGCTTACTGAACTTTATACTTTTGAGCCAGACTTATTAGATGACCCTAATTCA
GAAAAGAAGAAGAAGAGGGATACTCCCATGCTGCCAAAGGATACCATACTTGCAGAGCTC
CTTCAGATACATAAAGAACACATTGTAGGATACCATGAACATGATTCTCTTTTGGACCAC
AAAGAAGAAGAAGAGTTGACTGAAGAAGAAAGAAAAGCAGCTTGGGCTGAGTATGAAGCA
GAGAAGAAGGGACTGACCATGCGTTTCAACATACCAACTGGGACCAATTTACCCCCTGTC
AGTTTCAACTCTCAAACTCCTTATATTCCTTTCAATTTGGGAGCCCTGTCAGCAATGAGT
AATCAACAGCTGGAGGACCTCATTAATCAAGGAAGAGAAAAAGTTGTAGAAGCAACAAAC
AGTGTGACAGCAGTGAGGATTCAACCTCTTGAGGATATAATTTCAGCTGTATGGAAGGAG
AACATGAATCTCTCAGAGGCCCAAGTACAGGCGTTAGCATTAAGTAGACAAGCCAGCCAG
GAGCTTGATGTTAAACGAAGAGAAGCAATCTACAATGATGTATTGACAAAACAACAGATG
TTAATCAGCTGTGTTCAGCGAATACTTATGAACAGAAGGCTCCAGCAGCAGTACAATCAG
CAGCAACAGCAACAAATGACTTATCAACAAGCAACACTGGGTCACCTCATGATGCCAAAG
CCCCCAAATTTGATCATGAATCCTTCTAACTACCAGCAGATTGATATGAGAGGAATGTAT
CAGCCAGTGGCTGGTGGTATGCAGCCACCACCATTACAGCGTGCACCACCCCCAATGAGA
AGCAAAAATCCAGGACCTTCCCAAGGGAAATCAATGTGA
|
| Enzyme 26 GenBank Gene ID |
U72937  |
| Enzyme 26 GeneCard ID |
ATRX  |
| Enzyme 26 GenAtlas ID |
ATRX  |
| Enzyme 26 HGNC ID |
HGNC:886  |
| Enzyme 26 Chromosome Location |
Not Available |
| Enzyme 26 Locus |
Not Available |
| Enzyme 26 SNPs |
SNPJam Report  |
| Enzyme 26 General References |
- Picketts DJ, Higgs DR, Bachoo S, Blake DJ, Quarrell OW, Gibbons RJ: ATRX encodes a novel member of the SNF2 family of proteins: mutations point to a common mechanism underlying the ATR-X syndrome. Hum Mol Genet. 1996 Dec;5(12):1899-907. [PubMed
]
- Villard L, Lossi AM, Cardoso C, Proud V, Chiaroni P, Colleaux L, Schwartz C, Fontes M: Determination of the genomic structure of the XNP/ATRX gene encoding a potential zinc finger helicase. Genomics. 1997 Jul 15;43(2):149-55. [PubMed
]
- Kitano T, Schwarz C, Nickel B, Paabo S: Gene diversity patterns at 10 X-chromosomal loci in humans and chimpanzees. Mol Biol Evol. 2003 Aug;20(8):1281-9. Epub 2003 May 30. [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
]
- Stayton CL, Dabovic B, Gulisano M, Gecz J, Broccoli V, Giovanazzi S, Bossolasco M, Monaco L, Rastan S, Boncinelli E, et al.: Cloning and characterization of a new human Xq13 gene, encoding a putative helicase. Hum Mol Genet. 1994 Nov;3(11):1957-64. [PubMed
]
- Gecz J, Pollard H, Consalez G, Villard L, Stayton C, Millasseau P, Khrestchatisky M, Fontes M: Cloning and expression of the murine homologue of a putative human X-linked nuclear protein gene closely linked to PGK1 in Xq13.3. Hum Mol Genet. 1994 Jan;3(1):39-44. [PubMed
]
- Gibbons RJ, Picketts DJ, Villard L, Higgs DR: Mutations in a putative global transcriptional regulator cause X-linked mental retardation with alpha-thalassemia (ATR-X syndrome). Cell. 1995 Mar 24;80(6):837-45. [PubMed
]
- Cardoso C, Timsit S, Villard L, Khrestchatisky M, Fontes M, Colleaux L: Specific interaction between the XNP/ATR-X gene product and the SET domain of the human EZH2 protein. Hum Mol Genet. 1998 Apr;7(4):679-84. [PubMed
]
- McDowell TL, Gibbons RJ, Sutherland H, O'Rourke DM, Bickmore WA, Pombo A, Turley H, Gatter K, Picketts DJ, Buckle VJ, Chapman L, Rhodes D, Higgs DR: Localization of a putative transcriptional regulator (ATRX) at pericentromeric heterochromatin and the short arms of acrocentric chromosomes. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13983-8. [PubMed
]
- Villard L, Fontes M, Ades LC, Gecz J: Identification of a mutation in the XNP/ATR-X gene in a family reported as Smith-Fineman-Myers syndrome. Am J Med Genet. 2000 Mar 6;91(1):83-5. [PubMed
]
- Gibbons RJ, Pellagatti A, Garrick D, Wood WG, Malik N, Ayyub H, Langford C, Boultwood J, Wainscoat JS, Higgs DR: Identification of acquired somatic mutations in the gene encoding chromatin-remodeling factor ATRX in the alpha-thalassemia myelodysplasia syndrome (ATMDS). Nat Genet. 2003 Aug;34(4):446-9. [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
]
- Lechner MS, Schultz DC, Negorev D, Maul GG, Rauscher FJ 3rd: The mammalian heterochromatin protein 1 binds diverse nuclear proteins through a common motif that targets the chromoshadow domain. Biochem Biophys Res Commun. 2005 Jun 17;331(4):929-37. [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
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed
]
- 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
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
- Argentaro A, Yang JC, Chapman L, Kowalczyk MS, Gibbons RJ, Higgs DR, Neuhaus D, Rhodes D: Structural consequences of disease-causing mutations in the ATRX-DNMT3-DNMT3L (ADD) domain of the chromatin-associated protein ATRX. Proc Natl Acad Sci U S A. 2007 Jul 17;104(29):11939-44. Epub 2007 Jul 3. [PubMed
]
- Villard L, Lacombe D, Fontes M: A point mutation in the XNP gene, associated with an ATR-X phenotype without alpha-thalassemia. Eur J Hum Genet. 1996;4(6):316-20. [PubMed
]
- Villard L, Gecz J, Mattei JF, Fontes M, Saugier-Veber P, Munnich A, Lyonnet S: XNP mutation in a large family with Juberg-Marsidi syndrome. Nat Genet. 1996 Apr;12(4):359-60. [PubMed
]
- Gibbons RJ, Bachoo S, Picketts DJ, Aftimos S, Asenbauer B, Bergoffen J, Berry SA, Dahl N, Fryer A, Keppler K, Kurosawa K, Levin ML, Masuno M, Neri G, Pierpont ME, Slaney SF, Higgs DR: Mutations in transcriptional regulator ATRX establish the functional significance of a PHD-like domain. Nat Genet. 1997 Oct;17(2):146-8. [PubMed
]
- Fichera M, Romano C, Castiglia L, Failla P, Ruberto C, Amata S, Greco D, Cardoso C, Fontes M, Ragusa A: New mutations in XNP/ATR-X gene: a further contribution to genotype/phenotype relationship in ATR/X syndrome. Mutations in brief no. 176. Online. Hum Mutat. 1998;12(3):214. [PubMed
]
- Lossi AM, Millan JM, Villard L, Orellana C, Cardoso C, Prieto F, Fontes M, Martinez F: Mutation of the XNP/ATR-X gene in a family with severe mental retardation, spastic paraplegia and skewed pattern of X inactivation: demonstration that the mutation is involved in the inactivation bias. Am J Hum Genet. 1999 Aug;65(2):558-62. [PubMed
]
- Abidi F, Schwartz CE, Carpenter NJ, Villard L, Fontes M, Curtis M: Carpenter-Waziri syndrome results from a mutation in XNP. Am J Med Genet. 1999 Jul 30;85(3):249-51. [PubMed
]
- Villard L, Bonino MC, Abidi F, Ragusa A, Belougne J, Lossi AM, Seaver L, Bonnefont JP, Romano C, Fichera M, Lacombe D, Hanauer A, Philip N, Schwartz C, Fontes M: Evaluation of a mutation screening strategy for sporadic cases of ATR-X syndrome. J Med Genet. 1999 Mar;36(3):183-6. [PubMed
]
- Wada T, Kubota T, Fukushima Y, Saitoh S: Molecular genetic study of japanese patients with X-linked alpha-thalassemia/mental retardation syndrome (ATR-X). Am J Med Genet. 2000 Sep 18;94(3):242-8. [PubMed
]
- Stevenson RE, Abidi F, Schwartz CE, Lubs HA, Holmes LB: Holmes-Gang syndrome is allelic with XLMR-hypotonic face syndrome. Am J Med Genet. 2000 Oct 23;94(5):383-5. [PubMed
]
- Yntema HG, Poppelaars FA, Derksen E, Oudakker AR, van Roosmalen T, Jacobs A, Obbema H, Brunner HG, Hamel BC, van Bokhoven H: Expanding phenotype of XNP mutations: mild to moderate mental retardation. Am J Med Genet. 2002 Jul 1;110(3):243-7. [PubMed
]
- Leahy RT, Philip RK, Gibbons RJ, Fisher C, Suri M, Reardon W: Asplenia in ATR-X syndrome: a second report. Am J Med Genet A. 2005 Nov 15;139(1):37-9. [PubMed
]
- Wieland I, Sabathil J, Ostendorf A, Rittinger O, Ropke A, Winnepenninckx B, Kooy F, Holinski-Feder E, Wieacker P: A missense mutation in the coiled-coil motif of the HP1-interacting domain of ATR-X in a family with X-linked mental retardation. Neurogenetics. 2005 Feb;6(1):45-7. [PubMed
]
- Badens C, Martini N, Courrier S, DesPortes V, Touraine R, Levy N, Edery P: ATRX syndrome in a girl with a heterozygous mutation in the ATRX Zn finger domain and a totally skewed X-inactivation pattern. Am J Med Genet A. 2006 Oct 15;140(20):2212-5. [PubMed
]
|
| Enzyme 26 Metabolite References |
Not Available |
|
Enzyme 27
[top]
|
| Enzyme 27 ID |
13329 |
| Enzyme 27 Name |
Copine-1 |
| Enzyme 27 Synonyms |
- Copine I
|
| Enzyme 27 Gene Name |
CPNE1 |
| Enzyme 27 Protein Sequence |
>Copine-1
MAHCVTLVQLSISCDHLIDKDIGSKSDPLCVLLQDVGGGSWAELGRTERVRNCSSPEFSK
TLQLEYRFETVQKLRFGIYDIDNKTPELRDDDFLGGAECSLGQIVSSQVLTLPLMLKPGK
PAGRGTITVSAQELKDNRVVTMEVEARNLDKKDFLGKSDPFLEFFRQGDGKWHLVYRSEV
IKNNLNPTWKRFSVPVQHFCGGNPSTPIQVQCSDYDSDGSHDLIGTFHTSLAQLQAVPAE
FECIHPEKQQKKKSYKNSGTIRVKICRVETEYSFLDYVMGGCQINFTVGVDFTGSNGDPS
SPDSLHYLSPTGVNEYLMALWSVGSVVQDYDSDKLFPAFGFGAQVPPDWQVSHEFALNFN
PSNPYCAGIQGIVDAYRQALPQVRLYGPTNFAPIINHVARFAAQAAHQGTASQYFMLLLL
TDGAVTDVEATREAVVRASNLPMSVIIVGVGGADFEAMEQLDADGGPLHTRSGQAAARDI
VQFVPYRRFQNAPREALAQTVLAEVPTQLVSYFRAQGWAPLKPLPPSAKDPAQAPQA
|
| Enzyme 27 Number of Residues |
537 |
| Enzyme 27 Molecular Weight |
59058.3 |
| Enzyme 27 Theoretical pI |
5.62 |
| Enzyme 27 GO Classification |
Not Available |
| Enzyme 27 General Function |
Involved in calcium-dependent phospholipid binding |
| Enzyme 27 Specific Function |
May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties |
| 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 |
23397696  |
| Enzyme 27 UniProtKB/Swiss-Prot ID |
Q99829  |
| Enzyme 27 UniProtKB/Swiss-Prot Entry Name |
CPNE1_HUMAN  |
| Enzyme 27 PDB ID |
Not Available |
| Enzyme 27 Cellular Location |
Not Available |
| Enzyme 27 Gene Sequence |
>1614 bp
ATGGCCCACTGCGTGACCTTGGTTCAGCTGTCCATTTCCTGTGACCATCTCATTGACAAG
GACATCGGCTCCAAGTCTGACCCACTCTGCGTCCTTTTACAGGATGTGGGAGGGGGCAGC
TGGGCTGAGCTTGGCCGGACTGAACGGGTGCGGAACTGCTCAAGCCCTGAGTTCTCCAAG
ACTCTACAGCTTGAGTACCGCTTTGAGACAGTCCAGAAGCTACGCTTTGGAATCTATGAC
ATAGACAACAAGACGCCAGAGCTGAGGGATGATGACTTCCTAGGGGGTGCTGAGTGTTCC
CTAGGACAGATTGTGTCCAGCCAGGTACTGACTCTCCCCTTGATGCTGAAGCCTGGAAAA
CCTGCTGGGCGGGGGACCATCACGGTCTCAGCTCAGGAATTAAAGGACAATCGTGTAGTA
ACCATGGAGGTAGAGGCCAGAAACCTAGATAAGAAGGACTTCCTGGGAAAATCAGATCCA
TTTCTGGAGTTCTTCCGCCAGGGTGATGGGAAATGGCACCTGGTGTACAGATCTGAGGTC
ATCAAGAACAACCTGAACCCTACATGGAAGCGTTTCTCAGTCCCCGTTCAGCATTTCTGT
GGTGGGAACCCCAGCACACCCATCCAGGTGCAATGCTCCGATTATGACAGTGACGGGTCA
CATGATCTCATCGGTACCTTCCACACCAGCTTGGCCCAGCTGCAGGCAGTCCCGGCTGAG
TTTGAATGCATCCACCCTGAGAAGCAGCAGAAAAAGAAAAGCTACAAGAACTCTGGAACT
ATCCGTGTCAAGATTTGTCGGGTAGAAACAGAGTACTCCTTTCTGGACTATGTGATGGGA
GGCTGTCAGATCAACTTCACTGTGGGCGTGGACTTCACTGGCTCCAATGGAGACCCCTCC
TCACCTGACTCCCTACACTACCTGAGTCCAACAGGGGTCAATGAGTACCTGATGGCACTG
TGGAGTGTGGGCAGCGTGGTTCAGGACTATGACTCAGACAAGCTGTTCCCTGCATTTGGA
TTTGGGGCCCAGGTTCCCCCTGACTGGCAGGTCTCGCATGAATTTGCCTTGAATTTCAAC
CCCAGTAACCCCTACTGTGCAGGCATCCAGGGCATTGTGGATGCCTACCGCCAAGCCCTG
CCCCAAGTTCGCCTCTATGGCCCTACCAACTTTGCACCCATCATCAACCATGTGGCCAGG
TTTGCAGCCCAGGCTGCACATCAGGGGACTGCCTCGCAATACTTCATGCTGTTGCTGCTG
ACTGATGGTGCTGTGACGGATGTGGAAGCCACACGTGAGGCTGTGGTGCGTGCCTCGAAC
CTGCCCATGTCAGTGATCATTGTGGGTGTGGGTGGTGCTGACTTTGAGGCCATGGAGCAG
CTGGACGCTGATGGTGGACCCCTGCATACACGTTCTGGGCAGGCTGCTGCCCGCGACATT
GTGCAGTTTGTACCCTACCGCCGGTTCCAGAATGCCCCTCGGGAGGCATTGGCACAGACC
GTGCTCGCAGAAGTGCCCACACAACTGGTCTCATACTTCAGGGCCCAGGGTTGGGCCCCG
CTCAAGCCACTTCCACCCTCAGCCAAGGATCCTGCACAGGCCCCCCAGGCCTAG
|
| Enzyme 27 GenBank Gene ID |
NM_152925.2  |
| Enzyme 27 GeneCard ID |
CPNE1  |
| Enzyme 27 GenAtlas ID |
CPNE1  |
| Enzyme 27 HGNC ID |
HGNC:2314  |
| Enzyme 27 Chromosome Location |
2 |
| Enzyme 27 Locus |
20q11.22 |
| Enzyme 27 SNPs |
SNPJam Report  |
| Enzyme 27 General References |
- Creutz CE, Tomsig JL, Snyder SL, Gautier MC, Skouri F, Beisson J, Cohen J: The copines, a novel class of C2 domain-containing, calcium-dependent, phospholipid-binding proteins conserved from Paramecium to humans. J Biol Chem. 1998 Jan 16;273(3):1393-402. [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
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 27 Metabolite References |
Not Available |
|
Enzyme 28
[top]
|
| Enzyme 28 ID |
13333 |
| Enzyme 28 Name |
Copine-6 |
| Enzyme 28 Synonyms |
- Copine VI
- Neuronal-copine
- N-copine
|
| Enzyme 28 Gene Name |
CPNE6 |
| Enzyme 28 Protein Sequence |
>Copine-6
MSDPEMGWVPEPPTMTLGASRVELRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERT
EVLRSCSSPVFSRVLALEYFFEEKQPLQFHVFDAEDGATSPRNDTFLGSTECTLGQIVSQ
TKVTKPLLLKNGKTAGKSTITIVAEEVSGTNDYVQLTFRAYKLDNKDLFSKSDPFMEIYK
TNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGKHDFIG
EFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKNYKSSGTVVLAQCTVEKVHTFLDYIM
GGCQISFTVAIDFTASNGDPRSSQSLHCLSPRQPNHYLQALRAVGGICQDYDSDKRFPAF
GFGARIPPNFEVSHDFAINFDPENPECEEISGVIASYRRCLPQIQLYGPTNVAPIINRVA
EPAQREQSTGQATKYSVLLVLTDGVVSDMAETRTAIVRASRLPMSIIIVGVGNADFSDMR
LLDGDDGPLRCPRGVPAARDIVQFVPFRDFKDAAPSALAKCVLAEVPRQVVEYYASQGIS
PGAPRPCTLATTPSPSP
|
| Enzyme 28 Number of Residues |
557 |
| Enzyme 28 Molecular Weight |
61990.6 |
| Enzyme 28 Theoretical pI |
5.17 |
| Enzyme 28 GO Classification |
Not Available |
| Enzyme 28 General Function |
Involved in calcium ion binding |
| Enzyme 28 Specific Function |
May function in membrane trafficking. Exhibits calcium- dependent phospholipid binding properties. May have a role in synaptic plasticity |
| Enzyme 28 Pathways |
Not Available |
| 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 |
Not Available |
| Enzyme 28 UniProtKB/Swiss-Prot ID |
O95741  |
| Enzyme 28 UniProtKB/Swiss-Prot Entry Name |
CPNE6_HUMAN  |
| Enzyme 28 PDB ID |
Not Available |
| Enzyme 28 Cellular Location |
Not Available |
| Enzyme 28 Gene Sequence |
>1674 bp
ATGTCGGACCCTGAGATGGGATGGGTGCCTGAGCCCCCAACCATGACGCTGGGGGCCTCT
CGGGTGGAGCTGCGGGTGTCCTGCCATGGCCTCCTGGACCGGGACACACTCACCAAACCC
CACCCCTGCGTGCTGCTCAAGCTCTACTCTGATGAGCAGTGGGTGGAGGTAGAGCGCACA
GAGGTGCTTCGCTCCTGTTCCAGCCCTGTCTTCTCCCGGGTGCTGGCCCTTGAGTATTTT
TTTGAGGAGAAGCAGCCCCTGCAGTTCCACGTGTTCGATGCCGAGGACGGAGCCACCAGC
CCCCGAAATGATACCTTCCTCGGCTCTACGGAGTGCACCTTGGGCCAGATTGTGTCACAA
ACCAAGGTCACTAAGCCATTATTGCTGAAGAATGGGAAGACTGCGGGCAAGTCCACCATC
ACGATCGTGGCCGAGGAGGTATCAGGCACAAACGACTATGTGCAACTCACCTTCAGAGCC
TACAAGCTGGACAACAAGGATCTGTTCAGCAAGTCTGACCCTTTCATGGAAATCTATAAG
ACCAACGAGGACCAAAGTGATCAGCTGGTCTGGAGAACTGAGGTGGTGAAGAACAACCTG
AACCCCAGCTGGGAGCCGTTCCGCCTGTCCCTGCATTCCCTATGCAGCTGTGATGTTCAC
CGACCTCTCAAGTTCCTGGTGTATGACTATGACTCCAGTGGGAAGCATGACTTCATCGGC
GAGTTCACCAGCACTTTCCAGGAGATGCAGGAAGGGACGGCAAACCCTGGGCAGGAGATG
CAGTGGGACTGTATCAACCCCAAGTATCGGGACAAGAAGAAGAATTACAAGAGCTCAGGG
ACGGTAGTGCTGGCCCAGTGCACGGTGGAGAAGGTGCACACCTTCCTGGATTACATCATG
GGTGGCTGCCAGATCAGCTTCACGGTGGCCATTGACTTCACTGCCTCCAATGGGGACCCG
AGGAGCAGCCAGTCCCTGCACTGCCTCAGTCCCCGACAGCCCAACCACTACCTGCAGGCC
CTGCGTGCAGTGGGAGGCATCTGCCAGGACTATGACAGTGATAAGCGGTTCCCAGCTTTT
GGCTTTGGGGCTCGAATCCCCCCCAACTTCGAGGTGTCCCATGACTTTGCTATCAACTTT
GACCCGGAAAATCCTGAATGTGAAGAGATCTCAGGGGTCATCGCCTCCTACCGTCGTTGC
CTGCCCCAGATCCAGCTCTACGGCCCCACCAATGTGGCCCCCATCATCAACCGTGTGGCT
GAGCCGGCCCAGCGGGAGCAGAGCACCGGCCAAGCCACGAAGTACTCGGTGCTGCTGGTG
CTAACTGACGGTGTGGTGAGCGACATGGCTGAGACTCGCACTGCTATCGTGCGTGCCTCC
CGCCTGCCCATGTCCATCATCATCGTAGGCGTGGGCAATGCTGACTTCTCTGACATGCGG
CTGCTGGATGGCGACGACGGCCCCTTGCGCTGCCCCCGAGGGGTGCCTGCAGCCCGAGAC
ATTGTCCAGTTCGTGCCCTTCCGAGACTTCAAGGATGCTGCCCCCTCTGCACTCGCCAAG
TGTGTCCTGGCTGAGGTGCCACGGCAGGTGGTGGAGTACTACGCCAGCCAGGGCATCAGC
CCTGGGGCTCCCAGGCCCTGCACACTGGCTACGACTCCCAGCCCTAGCCCGTGA
|
| Enzyme 28 GenBank Gene ID |
AB009288  |
| Enzyme 28 GeneCard ID |
CPNE6  |
| Enzyme 28 GenAtlas ID |
CPNE6  |
| Enzyme 28 HGNC ID |
HGNC:2319  |
| Enzyme 28 Chromosome Location |
1 |
| Enzyme 28 Locus |
14q11.2 |
| Enzyme 28 SNPs |
SNPJam Report  |
| Enzyme 28 General References |
- Nakayama T, Yaoi T, Yasui M, Kuwajima G: N-copine: a novel two C2-domain-containing protein with neuronal activity-regulated expression. FEBS Lett. 1998 May 22;428(1-2):80-4. [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
]
|
| Enzyme 28 Metabolite References |
Not Available |
|
Enzyme 29
[top]
|
| Enzyme 29 ID |
14040 |
| Enzyme 29 Name |
Cdc42-interacting protein 4 |
| Enzyme 29 Synonyms |
- Protein Felic
- Salt tolerant protein
- hSTP
- Thyroid receptor-interacting protein 10
- TR-interacting protein 10
- TRIP-10
|
| Enzyme 29 Gene Name |
TRIP10 |
| Enzyme 29 Protein Sequence |
>Cdc42-interacting protein 4
MDWGTELWDQFEVLERHTQWGLDLLDRYVKFVKERTEVEQAYAKQLRSLVKKYLPKRPAK
DDPESKFSQQQSFVQILQEVNDFAGQRELVAENLSVRVCLELTKYSQEMKQERKMHFQEG
RRAQQQLENGFKQLENSKRKFERDCREAEKAAQTAERLDQDINATKADVEKAKQQAHLRS
HMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELE
VVPIIAKCLEGMKVAANAVDPKNDSHVLIELHKSGFARPGDVEFEDFSQPMNRAPSDSSL
GTPSDGRPELRGPGRSRTKRWPFGKKNKPRPPPLSPLGGPVPSALPNGPPSPRSGRDPLA
ILSEISKSVKPRLASFRSLRGSRGTVVTEDFSHLPPEQQRKRLQQQLEERSRELQKEVDQ
REALKKMKDVYEKTPQMGDPASLEPQIAETLSNIERLKLEVQKYEAWLAEAESRVLSNRG
DSLSRHARPPDPPASAPPDSSSNSASQDTKESSEEPPSEESQDTPIYTEFDEDFEEEPTS
PIGHCVAIYHFEGSSEGTISMAEGEDLSLMEEDKGDGWTRVRRKEGGEGYVPTSYLRVTL
N
|
| Enzyme 29 Number of Residues |
601 |
| Enzyme 29 Molecular Weight |
68351.7 |
| Enzyme 29 Theoretical pI |
5.45 |
| Enzyme 29 GO Classification |
Not Available |
| Enzyme 29 General Function |
Involved in identical protein binding |
| Enzyme 29 Specific Function |
Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling. Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N- WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL |
| Enzyme 29 Pathways |
Not Available |
| Enzyme 29 Reactions |
Not Available |
| Enzyme 29 Pfam Domain Function |
|
| Enzyme 29 Signals |
|
| Enzyme 29 Transmembrane Regions |
|
| Enzyme 29 Essentiality |
Not Available |
| Enzyme 29 GenBank ID Protein |
21311785  |
| Enzyme 29 UniProtKB/Swiss-Prot ID |
Q15642  |
| Enzyme 29 UniProtKB/Swiss-Prot Entry Name |
CIP4_HUMAN  |
| Enzyme 29 PDB ID |
Not Available |
| Enzyme 29 Cellular Location |
Not Available |
| Enzyme 29 Gene Sequence |
>1806 bp
ATGGATTGGGGCACTGAGCTGTGGGATCAGTTCGAGGTGCTCGAGCGCCACACGCAGTGG
GGGCTGGACCTGTTGGACAGATATGTAAAGTTCGTGAAAGAACGCACCGAAGTGGAACAG
GCTTACGCCAAACAACTGCGGAGCCTGGTGAAAAAATATCTGCCCAAGAGACCTGCCAAG
GATGATCCTGAGTCCAAATTCAGCCAGCAACAGTCCTTCGTACAGATTCTCCAGGAGGTG
AATGACTTTGCAGGCCAGCGGGAGCTGGTGGCTGAGAACCTCAGTGTCCGTGTATGTCTT
GAGCTGACCAAGTACTCACAAGAGATGAAACAGGAGAGGAAGATGCACTTCCAAGAAGGG
CGGCGGGCCCAGCAGCAGCTGGAAAATGGCTTTAAACAGCTGGAGAATAGTAAGCGTAAA
TTTGAGCGGGACTGCCGGGAGGCAGAGAAGGCAGCCCAGACTGCTGAACGGCTAGACCAG
GATATCAACGCCACCAAGGCTGATGTGGAGAAGGCCAAGCAGCAAGCCCACCTTCGGAGT
CACATGGCCGAAGAAAGCAAAAACGAATATGCGGCTCAACTGCAGCGCTTCAACCGAGAC
CAAGCCCACTTCTATTTTTCACAGATGCCCCAGATATTCGATAAGCTCCAAGACATGGAT
GAACGCAGGGCCACCCGCCTGGGTGCCGGGTATGGGCTCCTGTCGGAGGCCGAGCTGGAG
GTGGTGCCCATAATAGCCAAGTGCTTGGAGGGCATGAAGGTGGCTGCAAATGCTGTGGAT
CCCAAGAACGACTCCCACGTCCTTATAGAGCTGCACAAGTCAGGTTTTGCCCGCCCGGGC
GACGTGGAATTCGAGGACTTCAGCCAGCCCATGAACCGTGCACCCTCCGACAGCAGTCTG
GGCACCCCCTCGGATGGACGGCCTGAACTCCGAGGCCCGGGTCGCAGCCGCACCAAGCGC
TGGCCTTTTGGCAAGAAGAACAAGCCTCGCCCCCCACCCCTCTCCCCCCTGGGGGGCCCC
GTACCCTCGGCATTGCCTAACGGACCCCCGTCCCCCCGCTCCGGCCGTGACCCCTTGGCC
ATACTGAGCGAGATCAGTAAGTCGGTCAAACCGAGGCTAGCATCCTTCCGCAGCCTTCGA
GGCAGCCGTGGGACAGTGGTGACCGAGGATTTTAGCCACTTGCCCCCAGAGCAGCAGCGA
AAACGGCTTCAACAGCAGTTGGAAGAACGCAGTCGTGAACTTCAGAAGGAGGTTGACCAG
AGGGAAGCCCTAAAGAAAATGAAGGATGTCTATGAGAAGACACCTCAGATGGGGGACCCC
GCCAGCTTGGAGCCCCAGATCGCTGAAACCCTGAGCAACATTGAACGGCTGAAATTGGAA
GTGCAGAAGTATGAGGCGTGGCTGGCAGAAGCTGAAAGTCGAGTCCTTAGCAACCGGGGA
GACAGCCTGAGCCGGCACGCCCGGCCTCCCGACCCCCCCGCTAGCGCCCCGCCAGACAGC
AGCAGCAACAGCGCATCACAGGACACCAAGGAGAGCTCTGAAGAGCCTCCCTCAGAAGAG
AGCCAGGACACCCCCATTTACACGGAGTTTGATGAGGATTTCGAGGAGGAACCCACATCC
CCCATAGGTCACTGTGTGGCCATCTACCACTTTGAAGGGTCCAGCGAGGGCACTATCTCT
ATGGCCGAGGGTGAAGACCTCAGTCTTATGGAAGAAGACAAAGGGGACGGCTGGACCCGG
GTCAGGCGGAAAGAGGGAGGCGAGGGCTACGTGCCCACCTCCTACCTCCGAGTCACGCTC
AATTGA
|
| Enzyme 29 GenBank Gene ID |
AF502289  |
| Enzyme 29 GeneCard ID |
TRIP10  |
| Enzyme 29 GenAtlas ID |
TRIP10  |
| Enzyme 29 HGNC ID |
HGNC:12304  |
| Enzyme 29 Chromosome Location |
1 |
| Enzyme 29 Locus |
19p13.3 |
| Enzyme 29 SNPs |
SNPJam Report  |
| Enzyme 29 General References |
- Aspenstrom P: A Cdc42 target protein with homology to the non-kinase domain of FER has a potential role in regulating the actin cytoskeleton. Curr Biol. 1997 Jul 1;7(7):479-87. [PubMed
]
- Wang L, Rudert WA, Grishin A, Dombrosky-Ferlan P, Sullivan K, Deng X, Whitcomb D, Corey S: Identification and genetic analysis of human and mouse activated Cdc42 interacting protein-4 isoforms. Biochem Biophys Res Commun. 2002 May 24;293(5):1426-30. [PubMed
]
- Tsuji E, Tsuji Y, Fujiwara T, Ogata S, Tsukamoto K, Saku K: Splicing variant of Cdc42 interacting protein-4 disrupts beta-catenin-mediated cell-cell adhesion: expression and function in renal cell carcinoma. Biochem Biophys Res Commun. 2006 Jan 27;339(4):1083-8. Epub 2005 Dec 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
]
- 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
]
- Lee JW, Choi HS, Gyuris J, Brent R, Moore DD: Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol. 1995 Feb;9(2):243-54. [PubMed
]
- Tsuji E, Tsuji Y: Molecular cloning and chromosomal localization of human salt-tolerant protein. Genetica. 2000;108(3):259-62. [PubMed
]
- Tian L, Nelson DL, Stewart DM: Cdc42-interacting protein 4 mediates binding of the Wiskott-Aldrich syndrome protein to microtubules. J Biol Chem. 2000 Mar 17;275(11):7854-61. [PubMed
]
- Linder S, Hufner K, Wintergerst U, Aepfelbacher M: Microtubule-dependent formation of podosomal adhesion structures in primary human macrophages. J Cell Sci. 2000 Dec;113 Pt 23:4165-76. [PubMed
]
- Yuan R, Fan S, Achary M, Stewart DM, Goldberg ID, Rosen EM: Altered gene expression pattern in cultured human breast cancer cells treated with hepatocyte growth factor/scatter factor in the setting of DNA damage. Cancer Res. 2001 Nov 1;61(21):8022-31. [PubMed
]
- Richnau N, Aspenstrom P: Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1. J Biol Chem. 2001 Sep 14;276(37):35060-70. Epub 2001 Jun 28. [PubMed
]
- Dombrosky-Ferlan P, Grishin A, Botelho RJ, Sampson M, Wang L, Rudert WA, Grinstein S, Corey SJ: Felic (CIP4b), a novel binding partner with the Src kinase Lyn and Cdc42, localizes to the phagocytic cup. Blood. 2003 Apr 1;101(7):2804-9. Epub 2002 Nov 27. [PubMed
]
- Holbert S, Dedeoglu A, Humbert S, Saudou F, Ferrante RJ, Neri C: Cdc42-interacting protein 4 binds to huntingtin: neuropathologic and biological evidence for a role in Huntington's disease. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2712-7. Epub 2003 Feb 25. [PubMed
]
- Larocca MC, Shanks RA, Tian L, Nelson DL, Stewart DM, Goldenring JR: AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus. Mol Biol Cell. 2004 Jun;15(6):2771-81. Epub 2004 Mar 26. [PubMed
]
- Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, De Camilli P: Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell. 2005 Dec;9(6):791-804. [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
]
- Qian J, Chen W, Lettau M, Podda G, Zornig M, Kabelitz D, Janssen O: Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL. Cell Signal. 2006 Aug;18(8):1327-37. Epub 2005 Nov 28. [PubMed
]
- Aspenstrom P, Richnau N, Johansson AS: The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics. Exp Cell Res. 2006 Jul 15;312(12):2180-94. Epub 2006 Apr 21. [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
]
- 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 29 Metabolite References |
Not Available |
|
Enzyme 30
[top]
|
| Enzyme 30 ID |
14100 |
| Enzyme 30 Name |
Formin-binding protein 1-like |
| Enzyme 30 Synonyms |
- Transducer of Cdc42-dependent actin assembly protein 1
- Toca-1
|
| Enzyme 30 Gene Name |
FNBP1L |
| Enzyme 30 Protein Sequence |
>Formin-binding protein 1-like
MSWGTELWDQFDSLDKHTQWGIDFLERYAKFVKERIEIEQNYAKQLRNLVKKYCPKRSSK
DEEPRFTSCVAFFNILNELNDYAGQREVVAEEMAHRVYGELMRYAHDLKTERKMHLQEGR
KAQQYLDMCWKQMDNSKKKFERECREAEKAQQSYERLDNDTNATKADVEKAKQQLNLRTH
MADENKNEYAAQLQNFNGEQHKHFYVVIPQIYKQLQEMDERRTIKLSECYRGFADSERKV
IPIISKCLEGMILAAKSVDERRDSQMVVDSFKSGFEPPGDFPFEDYSQHIYRTISDGTIS
ASKQESGKMDAKTTVGKAKGKLWLFGKKPKPQSPPLTPTSLFTSSTPNGSQFLTFSIEPV
HYCMNEIKTGKPRIPSFRSLKRGVSLIMGPALEDFSHLPPEQRRKKLQQRIDELNRELQK
ESDQKDALNKMKDVYEKNPQMGDPGSLQPKLAETMNNIDRLRMEIHKNEAWLSEVEGKTG
GRGDRRHSSDINHLVTQGRESPEGSYTDDANQEVRGPPQQHGHHNEFDDEFEDDDPLPAI
GHCKAIYPFDGHNEGTLAMKEGEVLYIIEEDKGDGWTRARRQNGEEGYVPTSYIDVTLEK
NSKGS
|
| Enzyme 30 Number of Residues |
605 |
| Enzyme 30 Molecular Weight |
69977.0 |
| Enzyme 30 Theoretical pI |
6.52 |
| Enzyme 30 GO Classification |
Not Available |
| Enzyme 30 General Function |
Involved in lipid binding |
| Enzyme 30 Specific Function |
Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. May bind to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promote membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by activating the WASL/N-WASP-WASPIP/WIP complex, the predominant form of WASL/N-WASP in cells. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles |
| Enzyme 30 Pathways |
Not Available |
| Enzyme 30 Reactions |
Not Available |
| Enzyme 30 Pfam Domain Function |
|
| Enzyme 30 Signals |
|
| Enzyme 30 Transmembrane Regions |
|
| Enzyme 30 Essentiality |
Not Available |
| Enzyme 30 GenBank ID Protein |
256600192  |
| Enzyme 30 UniProtKB/Swiss-Prot ID |
Q5T0N5  |
| Enzyme 30 UniProtKB/Swiss-Prot Entry Name |
FBP1L_HUMAN  |
| Enzyme 30 PDB ID |
Not Available |
| Enzyme 30 Cellular Location |
Not Available |
| Enzyme 30 Gene Sequence |
>1818 bp
ATGAGCTGGGGCACGGAGCTGTGGGATCAGTTCGACAGCTTAGACAAGCATACACAATGG
GGAATTGACTTCTTGGAAAGATATGCCAAATTTGTTAAAGAGAGGATAGAAATTGAACAG
AACTATGCGAAACAATTGAGAAATCTGGTTAAGAAGTACTGCCCCAAACGTTCATCCAAA
GATGAAGAGCCACGGTTTACCTCGTGTGTAGCCTTTTTTAATATCCTTAATGAGTTAAAT
GACTATGCAGGACAGCGAGAAGTTGTAGCAGAAGAAATGGCGCACAGAGTGTATGGTGAA
TTAATGAGATATGCTCATGATCTGAAAACTGAAAGAAAAATGCATCTGCAAGAAGGACGA
AAAGCTCAACAATATCTTGACATGTGCTGGAAACAGATGGATAATAGTAAAAAGAAGTTT
GAAAGAGAATGTAGAGAGGCAGAAAAGGCACAACAGAGTTATGAAAGATTGGATAATGAT
ACTAATGCAACCAAGGCAGATGTTGAAAAGGCCAAACAGCAGTTGAATCTGCGTACGCAT
ATGGCCGATGAAAATAAAAATGAATATGCTGCACAATTACAAAACTTTAATGGAGAACAA
CATAAACATTTTTATGTAGTGATTCCTCAGATTTACAAGCAACTACAAGAAATGGACGAA
CGAAGGACTATTAAACTCAGTGAGTGTTACAGAGGATTTGCTGACTCAGAACGCAAAGTT
ATTCCCATCATTTCAAAATGTTTGGAAGGAATGATTCTTGCAGCAAAATCAGTTGATGAA
AGAAGAGACTCTCAAATGGTGGTAGACTCCTTCAAATCTGGTTTTGAACCTCCAGGAGAC
TTTCCATTTGAAGATTACAGTCAACATATATATAGAACCATTTCTGATGGGACTATCAGT
GCATCCAAACAGGAGAGTGGGAAGATGGATGCCAAAACCACAGTAGGAAAGGCCAAGGGC
AAATTGTGGCTCTTTGGAAAGAAGCCAAAGCCACAGTCCCCACCCTTAACCCCTACTAGT
TTATTCACATCCAGTACTCCTAATGGGTCCCAGTTTCTCACATTCTCCATTGAGCCCGTG
CATTATTGTATGAATGAAATAAAAACAGGGAAGCCCAGAATTCCTTCTTTCAGAAGCCTC
AAAAGAGGGTGGTCGGTGAAGATGGGCCCAGCACTAGAAGATTTCAGTCATCTGCCACCA
GAACAGAGACGTAAAAAACTACAGCAGCGCATTGATGAACTTAACAGAGAACTACAGAAA
GAATCAGACCAAAAAGATGCACTCAACAAAATGAAAGATGTATATGAGAAGAATCCACAA
ATGGGGGATCCAGGGAGTTTGCAGCCTAAATTAGCAGAGACCATGAATAACATTGACCGC
CTACGAATGGAAATCCATAAGAATGAGGCTTGGCTCTCTGAAGTCGAAGGCAAAACAGGT
GGGAGAGGAGACAGAAGACATAGCAGTGACATAAATCATCTTGTAACACAGGGACGAGAA
AGTCCTGAGGGAAGTTACACTGATGATGCAAACCAGGAAGTCCGTGGGCCACCCCAGCAG
CATGGTCACCACAATGAGTTTGATGATGAATTTGAGGATGATGATCCCTTGCCTGCTATT
GGACACTGCAAAGCTATCTACCCTTTTGATGGACATAATGAAGGTACTCTAGCAATGAAA
GAAGGTGAAGTTCTCTACATTATAGAGGAGGACAAAGGTGACGGATGGACAAGAGCTCGG
AGACAGAACGGTGAAGAAGGCTACGTTCCCACGTCATACATAGATGTAACTCTAGAGAAA
AACAGTAAAGGTTCCTGA
|
| Enzyme 30 GenBank Gene ID |
NM_001164473.2  |
| Enzyme 30 GeneCard ID |
FNBP1L  |
| Enzyme 30 GenAtlas ID |
FNBP1L  |
| Enzyme 30 HGNC ID |
HGNC:20851  |
| Enzyme 30 Chromosome Location |
1 |
| Enzyme 30 Locus |
1p22.1 |
| Enzyme 30 SNPs |
SNPJam Report  |
| Enzyme 30 General References |
- Ho HY, Rohatgi R, Lebensohn AM, Le Ma, Li J, Gygi SP, Kirschner MW: Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell. 2004 Jul 23;118(2):203-16. [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
]
- 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
]
- Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, De Camilli P: Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell. 2005 Dec;9(6):791-804. [PubMed
]
- Aspenstrom P, Richnau N, Johansson AS: The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics. Exp Cell Res. 2006 Jul 15;312(12):2180-94. Epub 2006 Apr 21. [PubMed
]
- Tsujita K, Suetsugu S, Sasaki N, Furutani M, Oikawa T, Takenawa T: Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J Cell Biol. 2006 Jan 16;172(2):269-79. [PubMed
]
- Kovacs EM, Makar RS, Gertler FB: Tuba stimulates intracellular N-WASP-dependent actin assembly. J Cell Sci. 2006 Jul 1;119(Pt 13):2715-26. Epub 2006 Jun 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
]
- 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 30 Metabolite References |
Not Available |
|
Enzyme 31
[top]
|
| Enzyme 31 ID |
14108 |
| Enzyme 31 Name |
Formin-binding protein 1 |
| Enzyme 31 Synonyms |
- Formin-binding protein 17
- hFBP17
|
| Enzyme 31 Gene Name |
FNBP1 |
| Enzyme 31 Protein Sequence |
>Formin-binding protein 1
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSK
EEEEYKYTSCKAFISNLNEMNDYAGQHEVISENMASQIIVDLARYVQELKQERKSNFHDG
RKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQIRH
QMAEDSKADYSSILQKFNHEQHEYYHTHIPNIFQKIQEMEERRIVRMGESMKTYAEVDRQ
VIPIIGKCLDGIVKAAESIDQKNDSQLVIEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSL
SNSRGEGKPDLKFGGKSKGKLWPFIKKNKLMSLLTSPHQPPPPPPASASPSAVPNGPQSP
KQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGATPEDFSNLPPEQRRKKLQQKVDE
LNKEIQKEMDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVSQNIEKLRVETQKFEAWLA
EVEGRLPARSEQARRQSGLYDSQNPPTVNNCAQDRESPDGSYTEEQSQESEMKVLATDFD
DEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLYVIEEDKGDGWTRIRRNEDEEGY
VPTSYVEVCLDKNAKDS
|
| Enzyme 31 Number of Residues |
617 |
| Enzyme 31 Molecular Weight |
71306.3 |
| Enzyme 31 Theoretical pI |
5.44 |
| Enzyme 31 GO Classification |
Not Available |
| Enzyme 31 General Function |
Involved in identical protein binding |
| Enzyme 31 Specific Function |
May act as a link between RND2 signaling and regulation of the actin cytoskeleton. Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL |
| Enzyme 31 Pathways |
Not Available |
| Enzyme 31 Reactions |
Not Available |
| Enzyme 31 Pfam Domain Function |
|
| Enzyme 31 Signals |
|
| Enzyme 31 Transmembrane Regions |
|
| Enzyme 31 Essentiality |
Not Available |
| Enzyme 31 GenBank ID Protein |
38524622  |
| Enzyme 31 UniProtKB/Swiss-Prot ID |
Q96RU3  |
| Enzyme 31 UniProtKB/Swiss-Prot Entry Name |
FNBP1_HUMAN  |
| Enzyme 31 PDB ID |
Not Available |
| Enzyme 31 Cellular Location |
Not Available |
| Enzyme 31 Gene Sequence |
>1854 bp
ATGAGCTGGGGCACCGAGCTCTGGGATCAGTTTGACAACTTAGAAAAACACACACAGTGG
GGAATTGATATTCTTGAGAAATATATCAAGTTTGTGAAAGAAAGGACAGAGATTGAACTC
AGCTATGCAAAGCAACTCAGGAATCTTTCAAAGAAGTACCAACCTAAAAAGAACTCGAAG
GAGGAAGAAGAATACAAGTATACGTCATGTAAAGCTTTCATTTCCAACCTGAACGAAATG
AATGATTACGCAGGGCAGCATGAAGTTATCTCCGAGAACATGGCATCACAGATCATTGTG
GACTTGGCACGCTATGTTCAGGAACTGAAACAGGAGAGGAAATCAAACTTTCACGATGGC
CGTAAAGCACAGCAGCACATCGAGACTTGCTGGAAGCAGCTTGAATCTAGTAAAAGGCGA
TTTGAACGCGATTGCAAAGAGGCGGACAGGGCGCAGCAGTACTTTGAGAAAATGGACGCT
GACATCAATGTCACAAAAGCGGATGTTGAAAAGGCCCGACAACAAGCTCAAATACGTCAC
CAAATGGCAGAGGACAGCAAAGCAGATTACTCATCCATTCTCCAGAAATTCAACCATGAG
CAGCATGAATATTACCATACTCACATCCCCAACATCTTCCAGAAAATACAAGAGATGGAG
GAAAGGAGGATTGTGAGAATGGGAGAGTCCATGAAGACATATGCAGAGGTTGATCGGCAG
GTGATCCCAATCATTGGGAAGTGCCTGGATGGAATAGTAAAAGCAGCCGAATCAATTGAT
CAGAAAAATGATTCACAGCTGGTAATAGAAGCTTATAAATCAGGGTTTGAGCCTCCTGGA
GACATTGAATTTGAGGATTACACTCAGCCAATGAAGCGCACTGTGTCAGATAACAGCCTT
TCAAATTCCAGAGGAGAAGGCAAACCAGACCTCAAATTTGGTGGCAAATCCAAAGGAAAG
TTATGGCCGTTCATCAAAAAAAATAAGCTTATGTCCCTTTTAACATCCCCCCATCAGCCT
CCCCCTCCCCCTCCTGCCTCTGCCTCACCCTCTGCTGTTCCCAACGGCCCCCAGTCTCCC
AAGCAGCAAAAGGAACCCCTCTCCCATCGCTTCAACGAGTTCATGACCTCCAAACCCAAA
ATCCACTGCTTCAGGAGCCTAAAGCGTGGGCTTTCTCTCAAGCTGGGTGCAACACCGGAG
GATTTCAGCAACCTCCCACCTGAACAAAGAAGGAAAAAGCTGCAGCAGAAAGTCGATGAG
TTAAATAAAGAAATTCAGAAGGAGATGGATCAAAGAGATGCCATAACAAAAATGAAAGAT
GTCTACCTAAAGAATCCTCAGATGGGAGACCCAGCCAGTTTGGATCACAAATTAGCAGAA
GTCAGCCAAAATATAGAGAAACTGCGAGTAGAGACCCAGAAATTTGAGGCCTGGCTGGCT
GAGGTTGAAGGCCGGCTCCCAGCACGCAGCGAGCAGGCGCGCCGGCAGAGCGGACTGTAC
GACAGCCAGAACCCACCCACAGTCAACAACTGCGCCCAGGACCGTGAGAGCCCAGATGGC
AGTTACACAGAGGAGCAGAGTCAGGAGAGTGAGATGAAGGTGCTGGCCACGGATTTTGAC
GACGAGTTTGATGATGAGGAGCCCCTCCCTGCCATAGGGACGTGCAAAGCTCTCTACACA
TTTGAAGGTCAGAATGAAGGAACGATTTCCGTAGTTGAAGGAGAAACATTGTATGTCATA
GAGGAAGACAAAGGCGATGGCTGGACCCGCATTCGGAGAAATGAAGATGAAGAGGGTTAT
GTCCCCACTTCATATGTCGAAGTCTGTTTGGACAAAAATGCCAAAGATTCCTAG
|
| Enzyme 31 GenBank Gene ID |
NM_015033.2  |
| Enzyme 31 GeneCard ID |
FNBP1  |
| Enzyme 31 GenAtlas ID |
FNBP1  |
| Enzyme 31 HGNC ID |
HGNC:17069  |
| Enzyme 31 Chromosome Location |
9 |
| Enzyme 31 Locus |
9q34 |
| Enzyme 31 SNPs |
SNPJam Report  |
| Enzyme 31 General References |
- Fuchs U, Rehkamp G, Haas OA, Slany R, Konig M, Bojesen S, Bohle RM, Damm-Welk C, Ludwig WD, Harbott J, Borkhardt A: The human formin-binding protein 17 (FBP17) interacts with sorting nexin, SNX2, and is an MLL-fusion partner in acute myelogeneous leukemia. Proc Natl Acad Sci U S A. 2001 Jul 17;98(15):8756-61. Epub 2001 Jul 3. [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
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Humphray SJ, Oliver K, Hunt AR, Plumb RW, Loveland JE, Howe KL, Andrews TD, Searle S, Hunt SE, Scott CE, Jones MC, Ainscough R, Almeida JP, Ambrose KD, Ashwell RI, Babbage AK, Babbage S, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beasley H, Beasley O, Bird CP, Bray-Allen S, Brown AJ, Brown JY, Burford D, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Chen Y, Clarke G, Clark SY, Clee CM, Clegg S, Collier RE, Corby N, Crosier M, Cummings AT, Davies J, Dhami P, Dunn M, Dutta I, Dyer LW, Earthrowl ME, Faulkner L, Fleming CJ, Frankish A, Frankland JA, French L, Fricker DG, Garner P, Garnett J, Ghori J, Gilbert JG, Glison C, Grafham DV, Gribble S, Griffiths C, Griffiths-Jones S, Grocock R, Guy J, Hall RE, Hammond S, Harley JL, Harrison ES, Hart EA, Heath PD, Henderson CD, Hopkins BL, Howard PJ, Howden PJ, Huckle E, Johnson C, Johnson D, Joy AA, Kay M, Keenan S, Kershaw JK, Kimberley AM, King A, Knights A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd C, Lloyd DM, Lovell J, Martin S, Mashreghi-Mohammadi M, Matthews L, McLaren S, McLay KE, McMurray A, Milne S, Nickerson T, Nisbett J, Nordsiek G, Pearce AV, Peck AI, Porter KM, Pandian R, Pelan S, Phillimore B, Povey S, Ramsey Y, Rand V, Scharfe M, Sehra HK, Shownkeen R, Sims SK, Skuce CD, Smith M, Steward CA, Swarbreck D, Sycamore N, Tester J, Thorpe A, Tracey A, Tromans A, Thomas DW, Wall M, Wallis JM, West AP, Whitehead SL, Willey DL, Williams SA, Wilming L, Wray PW, Young L, Ashurst JL, Coulson A, Blocker H, Durbin R, Sulston JE, Hubbard T, Jackson MJ, Bentley DR, Beck S, Rogers J, Dunham I: DNA sequence and analysis of human chromosome 9. Nature. 2004 May 27;429(6990):369-74. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Richnau N, Aspenstrom P: Rich, a rho GTPase-activating protein domain-containing protein involved in signaling by Cdc42 and Rac1. J Biol Chem. 2001 Sep 14;276(37):35060-70. Epub 2001 Jun 28. [PubMed
]
- Ghadimi MP, Sanzenbacher R, Thiede B, Wenzel J, Jing Q, Plomann M, Borkhardt A, Kabelitz D, Janssen O: Identification of interaction partners of the cytosolic polyproline region of CD95 ligand (CD178). FEBS Lett. 2002 May 22;519(1-3):50-8. [PubMed
]
- Fuchs U, Rehkamp GF, Slany R, Follo M, Borkhardt A: The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance. FEBS Lett. 2003 Nov 6;554(1-2):10-6. [PubMed
]
- Brill LM, Salomon AR, Ficarro SB, Mukherji M, Stettler-Gill M, Peters EC: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. Anal Chem. 2004 May 15;76(10):2763-72. [PubMed
]
- Kamioka Y, Fukuhara S, Sawa H, Nagashima K, Masuda M, Matsuda M, Mochizuki N: A novel dynamin-associating molecule, formin-binding protein 17, induces tubular membrane invaginations and participates in endocytosis. J Biol Chem. 2004 Sep 17;279(38):40091-9. Epub 2004 Jul 12. [PubMed
]
- Larocca MC, Shanks RA, Tian L, Nelson DL, Stewart DM, Goldenring JR: AKAP350 interaction with cdc42 interacting protein 4 at the Golgi apparatus. Mol Biol Cell. 2004 Jun;15(6):2771-81. Epub 2004 Mar 26. [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
]
- Itoh T, Erdmann KS, Roux A, Habermann B, Werner H, De Camilli P: Dynamin and the actin cytoskeleton cooperatively regulate plasma membrane invagination by BAR and F-BAR proteins. Dev Cell. 2005 Dec;9(6):791-804. [PubMed
]
- Rush J, Moritz A, Lee KA, Guo A, Goss VL, Spek EJ, Zhang H, Zha XM, Polakiewicz RD, Comb MJ: Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat Biotechnol. 2005 Jan;23(1):94-101. Epub 2004 Dec 12. [PubMed
]
- Qian J, Chen W, Lettau M, Podda G, Zornig M, Kabelitz D, Janssen O: Regulation of FasL expression: a SH3 domain containing protein family involved in the lysosomal association of FasL. Cell Signal. 2006 Aug;18(8):1327-37. Epub 2005 Nov 28. [PubMed
]
- Aspenstrom P, Richnau N, Johansson AS: The diaphanous-related formin DAAM1 collaborates with the Rho GTPases RhoA and Cdc42, CIP4 and Src in regulating cell morphogenesis and actin dynamics. Exp Cell Res. 2006 Jul 15;312(12):2180-94. Epub 2006 Apr 21. [PubMed
]
- Tsujita K, Suetsugu S, Sasaki N, Furutani M, Oikawa T, Takenawa T: Coordination between the actin cytoskeleton and membrane deformation by a novel membrane tubulation domain of PCH proteins is involved in endocytosis. J Cell Biol. 2006 Jan 16;172(2):269-79. [PubMed
]
- Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [PubMed
]
- Molina H, Horn DM, Tang N, Mathivanan S, Pandey A: Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry. Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2199-204. Epub 2007 Feb 7. [PubMed
]
- Carrascal M, Ovelleiro D, Casas V, Gay M, Abian J: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment. J Proteome Res. 2008 Dec;7(12):5167-76. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. [PubMed
]
- Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 31 Metabolite References |
Not Available |
|
Enzyme 32
[top]
|
| Enzyme 32 ID |
14494 |
| Enzyme 32 Name |
Sphingomyelin phosphodiesterase 4 |
| Enzyme 32 Synonyms |
- Neutral sphingomyelinase 3
- nSMase-3
- nSMase3
- Neutral sphingomyelinase III
|
| Enzyme 32 Gene Name |
SMPD4 |
| Enzyme 32 Protein Sequence |
>Sphingomyelin phosphodiesterase 4
MAFPHLQQPSFLLASLKADSINKPFAQQCQDLVKVIEDFPAKELHTIFPWLVESIFGSLD
GVLVGWNLRCLQGRVNPVEYSIVMEFLDPGGPMMKLVYKLQAEDYKFDFPVSYLPGPVKA
SIQECILPDSPLYHNKVQFTPTGGLGLNLALNPFEYYIFFFALSLITQKPLPVSLHVRTS
DCAYFILVDRYLSWFLPTEGSVPPPLSSSPGGTSPSPPPRTPAIPFASYGLHHTSLLKRH
ISHQTSVNADPASHEIWRSETLLQVFVEMWLHHYSLEMYQKMQSPHAKLEVLHYRLSVSS
ALYSPAQPSLQALHAYQESFTPTEEHVLVVRLLLKHLHAFANSLKPEQASPSAHSHATSP
LEEFKRAAVPRFVQQKLYLFLQHCFGHWPLDASFRAVLEMWLSYLQPWRYAPDKQAPGSD
SQPRCVSEKWAPFVQENLLMYTKLFVGFLNRALRTDLVSPKHALMVFRVAKVFAQPNLAE
MIQKGEQLFLEPELVIPHRQHRLFTAPTFTGSFLSPWPPAVTDASFKVKSHVYSLEGQDC
KYTPMFGPEARTLVLRLAQLITQAKHTAKSISDQCAESPAGHSFLSWLGFSSMDTNGSYT
ANDLDEMGQDSVRKTDEYLEKALEYLRQIFRLSEAQLRQFTLALGTTQDENGKKQLPDCI
VGEDGLILTPLGRYQIINGLRRFEIEYQGDPELQPIRSYEIASLVRTLFRLSSAINHRFA
GQMAALCSRDDFLGSFCRYHLTEPGLASRHLLSPVGRRQVAGHTRGPRLSLRFLGSYRTL
VSLLLAFFVASLFCVGPLPCTLLLTLGYVLYASAMTLLTERGKLHQP
|
| Enzyme 32 Number of Residues |
827 |
| Enzyme 32 Molecular Weight |
93350.8 |
| Enzyme 32 Theoretical pI |
8.04 |
| Enzyme 32 GO Classification |
Not Available |
| Enzyme 32 General Function |
Involved in metal ion binding |
| Enzyme 32 Specific Function |
Catalyzes the hydrolysis of membrane sphingomyelin to form phosphorylcholine and ceramide |
| Enzyme 32 Pathways |
|
| Enzyme 32 Reactions |
- sphingomyelin + H2O = N-acylsphingosine + choline phosphate [RN:R02541]
|
| Enzyme 32 Pfam Domain Function |
Not Available |
| Enzyme 32 Signals |
|
| Enzyme 32 Transmembrane Regions |
|
| Enzyme 32 Essentiality |
Not Available |
| Enzyme 32 GenBank ID Protein |
102467481  |
| Enzyme 32 UniProtKB/Swiss-Prot ID |
Q9NXE4  |
| Enzyme 32 UniProtKB/Swiss-Prot Entry Name |
NSMA3_HUMAN  |
| Enzyme 32 PDB ID |
Not Available |
| Enzyme 32 Cellular Location |
Not Available |
| Enzyme 32 Gene Sequence |
>2601 bp
ATGACGACTTTCGGCGCCGTGGCGGAATGGCGGCTTCCATCTCTGAGGCGAGCGACGCTA
TGGATCCCACAGTGGTTTGCTAAGAAGGCCATTTTCAACTCTCCACTGGAGGCTGCTATG
GCGTTCCCTCACCTGCAGCAGCCCAGCTTTCTACTGGCTAGCCTGAAAGCTGACTCTATA
AATAAGCCCTTTGCACAGCAGTGCCAAGACTTGGTTAAAGTCATTGAGGACTTTCCAGCA
AAGGAGCTGCACACCATCTTCCCATGGCTGGTAGAAAGCATTTTTGGCAGCCTAGATGGT
GTCCTCGTTGGCTGGAACCTCCGCTGCTTACAGGGGCGCGTGAATCCTGTGGAGTACAGC
ATCGTGATGGAATTTCTCGACCCTGGTGGCCCAATGATGAAGTTGGTTTATAAGCTTCAA
GCTGAAGACTATAAGTTCGACTTTCCTGTCTCCTACTTGCCTGGTCCTGTGAAGGCGTCC
ATCCAGGAGTGCATCCTCCCTGACAGTCCTCTGTACCACAACAAGGTCCAGTTCACCCCT
ACTGGGGGCCTTGGTCTGAACTTGGCCCTGAATCCGTTCGAGTATTACATATTCTTCTTT
GCCTTGAGCCTCATCACTCAGAAGCCACTTCCTGTGTCCCTCCACGTCCGTACTTCAGAC
TGTGCCTATTTCATCCTGGTGGACAGGTACCTGTCATGGTTCCTGCCCACCGAAGGCAGT
GTGCCCCCACCACTCTCCTCCAGCCCAGGGGGGACCAGCCCCTCACCACCTCCCAGGACA
CCAGCCATACCCTTTGCTTCCTATGGCCTCCACCACACTAGCCTCCTAAAGCGACACATC
TCTCATCAGACGTCTGTGAATGCAGACCCCGCCTCCCACGAGATCTGGAGGTCAGAAACT
CTGCTCCAGGTTTTTGTTGAAATGTGGCTTCATCACTATTCCTTGGAGATGTATCAAAAA
ATGCAGTCCCCTCATGCCAAGCTGGAGGTTCTGCACTACCGACTCAGTGTCTCCAGCGCC
CTCTACAGCCCCGCCCAACCCAGCCTCCAGGCCCTCCACGCCTACCAAGAGTCGTTCACG
CCTACTGAGGAGCATGTGTTGGTGGTGCGCCTGCTGCTGAAGCACCTGCACGCCTTTGCC
AACAGCCTGAAGCCAGAGCAGGCCTCACCCTCCGCCCACTCCCACGCCACCAGCCCCCTG
GAGGAGTTCAAACGGGCTGCTGTCCCGAGGTTCGTCCAGCAGAAACTCTACCTCTTCTTG
CAGCATTGCTTTGGCCACTGGCCCCTGGACGCATCGTTCAGAGCTGTCCTGGAGATGTGG
CTGAGCTACCTGCAGCCGTGGCGGTACGCGCCTGACAAGCAGGCTCCGGGCAGCGACTCC
CAGCCCCGGTGTGTGTCGGAGAAATGGGCACCCTTTGTCCAGGAGAACCTGCTGATGTAC
ACCAAGTTGTTTGTGGGCTTTCTGAACCGCGCGCTCCGCACAGACCTGGTCAGCCCCAAG
CACGCGCTCATGGTGTTCCGAGTGGCCAAAGTCTTTGCCCAGCCCAACCTGGCTGAGATG
ATTCAGAAAGGTGAGCAGCTATTCCTGGAGCCAGAGCTGGTCATCCCCCACCGCCAGCAC
CGACTCTTCACGGCCCCCACATTCACTGGGAGCTTCCTGTCACCCTGGCCACCAGCGGTC
ACTGATGCCTCCTTCAAGGTGAAGAGCCACGTCTACAGCCTGGAGGGCCAGGACTGCAAG
TACACCCCGATGTTTGGGCCCGAGGCCCGCACCCTGGTCCTGCGCCTCGCTCAGCTCATC
ACACAGGCCAAACACACAGCCAAGTCCATCTCCGACCAGTGTGCGGAGAGCCCGGCTGGC
CACTCCTTCCTCTCATGGCTGGGCTTTAGCTCCATGGACACCAATGGCTCCTACACAGCC
AACGACCTGGACGAGATGGGGCAAGACAGTGTCCGGAAGACAGATGAATACCTGGAGAAG
GCCCTGGAGTACCTGCGCCAGATATTCCGGCTCAGCGAAGCGCAGCTCAGGCAGTTCACA
CTCGCCTTGGGCACCACCCAGGATGAGAATGGAAAAAAGCAACTCCCCGACTGCATCGTG
GGTGAGGACGGACTCATCCTTACGCCCCTGGGGCGGTACCAGATCATCAATGGGCTGCGA
AGGTTTGAAATTGAGTACCAGGGGGACCCGGAGCTGCAGCCCATCCGGAGCTATGAGATC
GCCAGCTTGGTCCGCACACTCTTTAGGCTGTCGTCTGCCATCAACCACAGATTTGCAGGA
CAGATGGCGGCTCTGTGTTCCCGGGATGACTTCCTCGGCAGCTTCTGTCGCTACCACCTC
ACAGAACCTGGGCTGGCCAGCAGGCACCTGCTGAGCCCTGTGGGGCGGAGGCAGGTGGCC
GGCCACACCCGCGGCCCCAGGCTCAGCCTGCGCTTCCTGGGCAGTTACCGGACGCTGGTC
TCGCTGCTGCTGGCCTTCTTCGTGGCCTCTCTGTTCTGCGTCGGGCCCCTCCCATGCACG
CTGCTGCTCACCCTGGGCTATGTCCTCTACGCCTCTGCCATGACACTGCTGACCGAGCGG
GGGAAGCTGCACCAGCCCTGA
|
| Enzyme 32 GenBank Gene ID |
Not Available |
| Enzyme 32 GeneCard ID |
SMPD4  |
| Enzyme 32 GenAtlas ID |
SMPD4  |
| Enzyme 32 HGNC ID |
HGNC:32949  |
| Enzyme 32 Chromosome Location |
2 |
| Enzyme 32 Locus |
2q21.1 |
| Enzyme 32 SNPs |
SNPJam Report  |
| Enzyme 32 General References |
- Nagase T, Kikuno R, Ishikawa KI, Hirosawa M, Ohara O: Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 2000 Feb 28;7(1):65-73. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Wiemann S, Weil B, Wellenreuther R, Gassenhuber J, Glassl S, Ansorge W, Bocher M, Blocker H, Bauersachs S, Blum H, Lauber J, Dusterhoft A, Beyer A, Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A: Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. Genome Res. 2001 Mar;11(3):422-35. [PubMed
]
- Krut O, Wiegmann K, Kashkar H, Yazdanpanah B, Kronke M: Novel tumor necrosis factor-responsive mammalian neutral sphingomyelinase-3 is a C-tail-anchored protein. J Biol Chem. 2006 May 12;281(19):13784-93. Epub 2006 Mar 3. [PubMed
]
- Yu LR, Zhu Z, Chan KC, Issaq HJ, Dimitrov DS, Veenstra TD: Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra. J Proteome Res. 2007 Nov;6(11):4150-62. Epub 2007 Oct 9. [PubMed
]
- Wang B, Malik R, Nigg EA, Korner R: Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis. Anal Chem. 2008 Dec 15;80(24):9526-33. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
- Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. Epub 2009 Jul 16. [PubMed
]
|
| Enzyme 32 Metabolite References |
Not Available |
|
Enzyme 33
[top]
|
| Enzyme 33 ID |
17005 |
| Enzyme 33 Name |
Serine incorporator 1 |
| Enzyme 33 Synonyms |
- Tumor differentially expressed protein 1-like
- Tumor differentially expressed protein 2
|
| Enzyme 33 Gene Name |
SERINC1 |
| Enzyme 33 Protein Sequence |
>Serine incorporator 1
MGSVLGLCSMASWIPCLCGSAPCLLCRCCPSGNNSTVTRLIYALFLLVGVCVACVMLIPG
MEEQLNKIPGFCENEKGVVPCNILVGYKAVYRLCFGLAMFYLLLSLLMIKVKSSSDPRAA
VHNGFWFFKFAAAIAIIIGAFFIPEGTFTTVWFYVGMAGAFCFILIQLVLLIDFAHSWNE
SWVEKMEEGNSRCWYAALLSATALNYLLSLVAIVLFFVYYTHPASCSENKAFISVNMLLC
VGASVMSILPKIQESQPRSGLLQSSVITVYTMYLTWSAMTNEPETNCNPSLLSIIGYNTT
STVPKEGQSVQWWHAQGIIGLILFLLCVFYSSIRTSNNSQVNKLTLTSDESTLIEDGGAR
SDGSLEDGDDVHRAVDNERDGVTYSYSFFHFMLFLASLYIMMTLTNWYRYEPSREMKSQW
TAVWVKISSSWIGIVLYVWTLVAPLVLTNRDFD
|
| Enzyme 33 Number of Residues |
453 |
| Enzyme 33 Molecular Weight |
50494.4 |
| Enzyme 33 Theoretical pI |
5.65 |
| Enzyme 33 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 33 General Function |
Involved in L-serine transmembrane transporter activity |
| Enzyme 33 Specific Function |
Enhances the incorporation of serine into phosphatidylserine and sphingolipids |
| Enzyme 33 Pathways |
Not Available |
| Enzyme 33 Reactions |
Not Available |
| Enzyme 33 Pfam Domain Function |
|
| Enzyme 33 Signals |
|
| Enzyme 33 Transmembrane Regions |
- 89-109
124-144
152-172
198-218
232-252
260-280
310-330
388-408
427-447
|
| Enzyme 33 Essentiality |
Not Available |
| Enzyme 33 GenBank ID Protein |
24308213  |
| Enzyme 33 UniProtKB/Swiss-Prot ID |
Q9NRX5  |
| Enzyme 33 UniProtKB/Swiss-Prot Entry Name |
SERC1_HUMAN  |
| Enzyme 33 PDB ID |
Not Available |
| Enzyme 33 Cellular Location |
Not Available |
| Enzyme 33 Gene Sequence |
>1362 bp
ATGGGGAGCGTCCTGGGGCTGTGCTCCATGGCGAGCTGGATACCATGTTTGTGTGGAAGT
GCCCCGTGTTTGCTATGCCGATGCTGTCCTAGTGGAAACAACTCCACTGTAACTAGATTG
ATCTATGCACTTTTCTTGCTTGTTGGAGTATGTGTAGCTTGTGTAATGTTGATACCAGGA
ATGGAAGAACAACTGAATAAGATTCCTGGATTTTGTGAGAATGAGAAAGGTGTTGTCCCT
TGTAACATTTTGGTTGGCTATAAAGCTGTATATCGTTTGTGCTTTGGTTTGGCTATGTTC
TATCTTCTTCTCTCTTTACTAATGATCAAAGTGAAGAGTAGCAGTGATCCTAGAGCTGCA
GTGCACAATGGATTTTGGTTCTTTAAATTTGCTGCAGCAATTGCAATTATTATTGGGGCA
TTCTTCATTCCAGAAGGAACTTTTACAACTGTGTGGTTTTATGTAGGCATGGCAGGTGCC
TTTTGTTTCATCCTCATACAACTAGTCTTACTTATTGATTTTGCACATTCATGGAATGAA
TCGTGGGTTGAAAAAATGGAAGAAGGGAACTCGAGATGTTGGTATGCAGCCTTGTTATCA
GCTACAGCTCTGAATTATCTGCTGTCTTTAGTTGCTATCGTCCTGTTCTTTGTCTACTAC
ACTCATCCAGCCAGTTGTTCAGAAAACAAGGCGTTCATCAGTGTCAACATGCTCCTCTGC
GTTGGTGCTTCTGTAATGTCTATACTGCCAAAAATCCAAGAATCACAACCAAGATCTGGT
TTGTTACAGTCTTCAGTAATTACAGTCTACACAATGTATTTGACATGGTCAGCTATGACC
AATGAACCAGAAACAAATTGCAACCCAAGTCTACTAAGCATAATTGGCTACAATACAACA
AGCACTGTCCCAAAGGAAGGGCAGTCAGTCCAGTGGTGGCATGCTCAAGGAATTATAGGA
CTAATTCTCTTTTTGTTGTGTGTATTTTATTCCAGCATCCGTACTTCAAACAATAGTCAG
GTTAATAAACTGACTCTAACAAGTGATGAATCTACATTAATAGAAGATGGTGGAGCTAGA
AGTGATGGATCACTGGAGGATGGGGACGATGTTCACCGAGCTGTAGATAATGAAAGGGAT
GGTGTCACTTACAGTTATTCCTTCTTTCACTTCATGCTTTTCCTGGCTTCACTTTATATC
ATGATGACCCTTACCAACTGGTACAGGTATGAACCCTCTCGTGAGATGAAAAGTCAGTGG
ACAGCTGTCTGGGTGAAAATCTCTTCCAGTTGGATTGGCATCGTGCTGTATGTTTGGACA
CTCGTGGCACCACTTGTTCTTACAAATCGTGATTTTGACTGA
|
| Enzyme 33 GenBank Gene ID |
NM_020755.2  |
| Enzyme 33 GeneCard ID |
SERINC1  |
| Enzyme 33 GenAtlas ID |
SERINC1  |
| Enzyme 33 HGNC ID |
HGNC:13464  |
| Enzyme 33 Chromosome Location |
6 |
| Enzyme 33 Locus |
6q22.31 |
| Enzyme 33 SNPs |
SNPJam Report  |
| Enzyme 33 General References |
- Nagase T, Ishikawa K, Kikuno R, Hirosawa M, Nomura N, Ohara O: Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 1999 Oct 29;6(5):337-45. [PubMed
]
- Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed
]
- 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
]
- Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- Mungall AJ, Palmer SA, Sims SK, Edwards CA, Ashurst JL, Wilming L, Jones MC, Horton R, Hunt SE, Scott CE, Gilbert JG, Clamp ME, Bethel G, Milne S, Ainscough R, Almeida JP, Ambrose KD, Andrews TD, Ashwell RI, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Barker DJ, Barlow KF, Bates K, Beare DM, Beasley H, Beasley O, Bird CP, Blakey S, Bray-Allen S, Brook J, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Carder C, Carter NP, Chapman JC, Clark SY, Clark G, Clee CM, Clegg S, Cobley V, Collier RE, Collins JE, Colman LK, Corby NR, Coville GJ, Culley KM, Dhami P, Davies J, Dunn M, Earthrowl ME, Ellington AE, Evans KA, Faulkner L, Francis MD, Frankish A, Frankland J, French L, Garner P, Garnett J, Ghori MJ, Gilby LM, Gillson CJ, Glithero RJ, Grafham DV, Grant M, Gribble S, Griffiths C, Griffiths M, Hall R, Halls KS, Hammond S, Harley JL, Hart EA, Heath PD, Heathcott R, Holmes SJ, Howden PJ, Howe KL, Howell GR, Huckle E, Humphray SJ, Humphries MD, Hunt AR, Johnson CM, Joy AA, Kay M, Keenan SJ, Kimberley AM, King A, Laird GK, Langford C, Lawlor S, Leongamornlert DA, Leversha M, Lloyd CR, Lloyd DM, Loveland JE, Lovell J, Martin S, Mashreghi-Mohammadi M, Maslen GL, Matthews L, McCann OT, McLaren SJ, McLay K, McMurray A, Moore MJ, Mullikin JC, Niblett D, Nickerson T, Novik KL, Oliver K, Overton-Larty EK, Parker A, Patel R, Pearce AV, Peck AI, Phillimore B, Phillips S, Plumb RW, Porter KM, Ramsey Y, Ranby SA, Rice CM, Ross MT, Searle SM, Sehra HK, Sheridan E, Skuce CD, Smith S, Smith M, Spraggon L, Squares SL, Steward CA, Sycamore N, Tamlyn-Hall G, Tester J, Theaker AJ, Thomas DW, Thorpe A, Tracey A, Tromans A, Tubby B, Wall M, Wallis JM, West AP, White SS, Whitehead SL, Whittaker H, Wild A, Willey DJ, Wilmer TE, Wood JM, Wray PW, Wyatt JC, Young L, Younger RM, Bentley DR, Coulson A, Durbin R, Hubbard T, Sulston JE, Dunham I, Rogers J, Beck S: The DNA sequence and analysis of human chromosome 6. Nature. 2003 Oct 23;425(6960):805-11. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- 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
]
- Chen R, Jiang X, Sun D, Han G, Wang F, Ye M, Wang L, Zou H: Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry. J Proteome Res. 2009 Feb;8(2):651-61. [PubMed
]
|
| Enzyme 33 Metabolite References |
Not Available |
|
Enzyme 34
[top]
|
| Enzyme 34 ID |
17258 |
| Enzyme 34 Name |
Protein kinase C delta-binding protein |
| Enzyme 34 Synonyms |
- Cavin-3
- Serum deprivation response factor-related gene product that binds to C-kinase
- hSRBC
|
| Enzyme 34 Gene Name |
PRKCDBP |
| Enzyme 34 Protein Sequence |
>Protein kinase C delta-binding protein
MRESALEPGPVPEAPAGGPVHAVTVVTLLEKLASMLETLRERQGGLARRQGGLAGSVRRI
QSGLGALSRSHDTTSNTLAQLLAKAERVSSHANAAQERAVRRAAQVQRLEANHGLLVARG
KLHVLLFKEEGEVPASAFQKAPEPLGPADQSELGPEQPEAEVGESSDEEPVESRAQRLRR
TGLQKVQSLRRALSGRKGPAAPPPTPVKPPRLGPGRSAEAQPEAQPALEPTLEPEPPQDT
EEDPGRPGAAEEALLQMESVA
|
| Enzyme 34 Number of Residues |
261 |
| Enzyme 34 Molecular Weight |
27625.8 |
| Enzyme 34 Theoretical pI |
6.07 |
| Enzyme 34 GO Classification |
Not Available |
| Enzyme 34 General Function |
Not Available |
| Enzyme 34 Specific Function |
Seems to have an immune potentiation function |
| Enzyme 34 Pathways |
Not Available |
| Enzyme 34 Reactions |
Not Available |
| Enzyme 34 Pfam Domain Function |
Not Available |
| Enzyme 34 Signals |
|
| Enzyme 34 Transmembrane Regions |
|
| Enzyme 34 Essentiality |
Not Available |
| Enzyme 34 GenBank ID Protein |
47132587  |
| Enzyme 34 UniProtKB/Swiss-Prot ID |
Q969G5  |
| Enzyme 34 UniProtKB/Swiss-Prot Entry Name |
PRDBP_HUMAN  |
| Enzyme 34 PDB ID |
Not Available |
| Enzyme 34 Cellular Location |
Not Available |
| Enzyme 34 Gene Sequence |
>786 bp
ATGAGGGAGAGTGCGTTGGAGCGGGGGCCTGTGCCCGAGGCGCCGGCGGGGGGTCCCGTG
CACGCCGTGACGGTGGTGACCCTGCTGGAGAAGCTGGCCTCCATGCTGGAGACTCTGCGG
GAGCGGCAGGGAGGCCTGGCTCGAAGGCAGGGAGGCCTGGCAGGGTCCGTGCGCCGCATC
CAGAGCGGCCTGGGCGCTCTGAGTCGCAGCCACGACACCACCAGCAACACCTTGGCGCAG
CTGCTGGCCAAGGCGGAGCGCGTGAGCTCGCACGCCAACGCCGCCCAAGAGCGCGCGGTG
CGCCGCGCAGCCCAGGTGCAGCGGCTGGAGGCCAACCACGGGCTGCTGGTGGCGCGCGGG
AAGCTCCACGTTCTGCTCTTCAAGGAGGAGGGTGAAGTCCCAGCCAGCGCTTTCCAGAAG
GCACCAGAGCCCTTGGGCCCGGCGGACCAGTCCGAGCTGGGCCCAGAGCAGCTGGAGGCC
GAAGTTGGAGAGAGCTCGGACGAGGAGCCGGTGGAGTCCAGGGCCCAGCGGCTGCGGCGC
ACCGGATTGCAGAAGGTACAGAGCCTCCGAAGGGCCCTTTCGGGCCGGAAAGGCCCTGCA
GCGCCACCGCCCACCCCGGTCAAGCCGCCTCGCCTTGGGCCTGGCCGGAGCGCTGAAGCC
CAGCCGGAAGCCCAGCCTGCGCTGGAGCCCACGCTGGAGCCAGAGCCTCCGCAGGACACC
GAGGAAGATCCCGGGAGACCTGGGGCTGCCGAAGAAGCTCTGCTCCAAATGGAGAGTGTA
GCCTGA
|
| Enzyme 34 GenBank Gene ID |
NM_145040.2  |
| Enzyme 34 GeneCard ID |
PRKCDBP  |
| Enzyme 34 GenAtlas ID |
PRKCDBP  |
| Enzyme 34 HGNC ID |
HGNC:9400  |
| Enzyme 34 Chromosome Location |
1 |
| Enzyme 34 Locus |
11p15.4 |
| Enzyme 34 SNPs |
SNPJam Report  |
| Enzyme 34 General References |
- Xu XL, Wu LC, Du F, Davis A, Peyton M, Tomizawa Y, Maitra A, Tomlinson G, Gazdar AF, Weissman BE, Bowcock AM, Baer R, Minna JD: Inactivation of human SRBC, located within the 11p15.5-p15.4 tumor suppressor region, in breast and lung cancers. Cancer Res. 2001 Nov 1;61(21):7943-9. [PubMed
]
- Taylor TD, Noguchi H, Totoki Y, Toyoda A, Kuroki Y, Dewar K, Lloyd C, Itoh T, Takeda T, Kim DW, She X, Barlow KF, Bloom T, Bruford E, Chang JL, Cuomo CA, Eichler E, FitzGerald MG, Jaffe DB, LaButti K, Nicol R, Park HS, Seaman C, Sougnez C, Yang X, Zimmer AR, Zody MC, Birren BW, Nusbaum C, Fujiyama A, Hattori M, Rogers J, Lander ES, Sakaki Y: Human chromosome 11 DNA sequence and analysis including novel gene identification. Nature. 2006 Mar 23;440(7083):497-500. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. [PubMed
]
- Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. Epub 2008 Jan 26. [PubMed
]
- Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. [PubMed
]
- Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. Epub 2008 Jul 31. [PubMed
]
|
| Enzyme 34 Metabolite References |
Not Available |
|
Enzyme 35
[top]
|
| Enzyme 35 ID |
17306 |
| Enzyme 35 Name |
Annexin A9 |
| Enzyme 35 Synonyms |
- Annexin XXXI
- Annexin-31
- Annexin-9
- Pemphaxin
|
| Enzyme 35 Gene Name |
ANXA9 |
| Enzyme 35 Protein Sequence |
>Annexin A9
MSVTGGKMAPSLTQEILSHLGLASKTAAWGTLGTLRTFLNFSVDKDAQRLLRAITGQGVD
RSAIVDVLTNRSREQRQLISRNFQERTQQDLMKSLQAALSGNLERIVMALLQPTAQFDAQ
ELRTALKASDSAVDVAIEILATRTPPQLQECLAVYKHNFQVEAVDDITSETSGILQDLLL
ALAKGGRDSYSGIIDYNLAEQDVQALQRAEGPSREETWVPVFTQRNPEHLIRVFDQYQRS
TGQELEEAVQNRFHGDAQVALLGLASVIKNTPLYFADKLHQALQETEPNYQVLIRILISR
CETDLLSIRAEFRKKFGKSLYSSLQDAVKGDCQSALLALCRAEDM
|
| Enzyme 35 Number of Residues |
345 |
| Enzyme 35 Molecular Weight |
38363.2 |
| Enzyme 35 Theoretical pI |
5.48 |
| Enzyme 35 GO Classification |
| Function |
- binding
- calcium ion binding
- calcium-dependent phospholipid binding
- cation binding
- ion binding
- lipid binding
- metal ion binding
- phospholipid binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 35 General Function |
Involved in calcium ion binding |
| Enzyme 35 Specific Function |
Low affinity receptor for acetylcholine known to be targeted by disease-causing pemphigus vulgaris antibodies in keratinocytes |
| 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 |
10436074  |
| Enzyme 35 UniProtKB/Swiss-Prot ID |
O76027  |
| Enzyme 35 UniProtKB/Swiss-Prot Entry Name |
ANXA9_HUMAN  |
| Enzyme 35 PDB ID |
Not Available |
| Enzyme 35 Cellular Location |
Not Available |
| Enzyme 35 Gene Sequence |
>1038 bp
ATGTCTGTGACTGGCGGGAAGATGGCACCGTCCCTCACCCAGGAGATCCTCAGCCACCTG
GGCCTGGCCAGCAAGACTGCAGCGTGGGGGACCCTGGGCACCCTCAGGACCTTCTTGAAC
TTCAGCGTGGACAAGGATGCGCAGAGGCTACTGAGGGCCATTACTGGCCAAGGCGTGGAC
CGCAGTGCCATTGTGGACGTGCTGACCAACCGGAGCAGAGAGCAAAGGCAGCTCATCTCA
CGAAACTTCCAGGAGCGCACCCAACAGGACCTGATGAAGTCTCTACAGGCAGCACTTTCC
GGCAACCTGGAGAGGATTGTGATGGCTCTGCTGCAGCCCACAGCCCAGTTTGACGCCCAG
GAATTGAGGACAGCTCTGAAGGCCTCAGATTCTGCTGTGGACGTGGCCATTGAAATTCTT
GCCACTCGAACCCCACCCCAGCTGCAGGAGTGCTTGGCAGTCTACAAACACAATTTCCAG
GTGGAGGCTGTGGATGGCATCACATCTGAGACCAGTGGCATCTTGCAGGACCTGCTGTTG
GCCCTGGCCAAGGGGGGCCGTGACAGCTACTCTGGAATCATTGACTATAATCTGGCAGAA
CAAGATGTCCAGGCACTGCAGCGGGCAGAAGGACCTAGCAGAGAGGAAACATGGGTCCCA
GTCTTCACCCAGCGAAATCCTGAACACCTCATCCGAGTGTTTGATCAGTACCAGCGGAGC
ACTGGGCAAGAGCTGGAGGAGGCTGTCCAGAACCGTTTCCATGGAGATGCTCAGGTGGCT
CTGCTCGGCCTAGCTTCGGTGATCAAGAACACACCGCTGTACTTTGCTGACAAACTTCAT
CAAGCCCTCCAGGAAACTGAGCCCAATTACCAAGTCCTGATTCGCATCCTTATCTCTCGA
TGTGAGACTGACCTTCTGAGTATCAGAGCTGAGTTCAGGAAGAAATTTGGGAAGTCCCTC
TACTCTTCTCTCCAGGATGCAGTGAAAGGGGATTGCCAGTCAGCCCTCCTGGCCTTGTGC
AGGGCTGAAGACATGTGA
|
| Enzyme 35 GenBank Gene ID |
AF230929  |
| Enzyme 35 GeneCard ID |
ANXA9  |
| Enzyme 35 GenAtlas ID |
ANXA9  |
| Enzyme 35 HGNC ID |
HGNC:547  |
| Enzyme 35 Chromosome Location |
1 |
| Enzyme 35 Locus |
1q21 |
| Enzyme 35 SNPs |
SNPJam Report  |
| Enzyme 35 General References |
- Morgan RO, Fernandez MP: Expression profile and structural divergence of novel human annexin 31. FEBS Lett. 1998 Sep 4;434(3):300-4. [PubMed
]
- Nguyen VT, Ndoye A, Grando SA: Pemphigus vulgaris antibody identifies pemphaxin. A novel keratinocyte annexin-like molecule binding acetylcholine. J Biol Chem. 2000 Sep 22;275(38):29466-76. [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
]
- 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
]
|
| Enzyme 35 Metabolite References |
Not Available |
|
Enzyme 36
[top]
|
| Enzyme 36 ID |
17307 |
| Enzyme 36 Name |
Phosphatidylserine receptor transcript variant 2 |
| Enzyme 36 Synonyms |
Not Available |
| Enzyme 36 Gene Name |
JMJD6 |
| Enzyme 36 Protein Sequence |
>Phosphatidylserine receptor transcript variant 2
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFV
ERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEY
MESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPP
RSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIY
PRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHK
TVRGRPKLSRKWYRTDTARAAAVQATHSHPVPLCPNPDLEGPALGDFEARAPRVGSPRRL
G
|
| Enzyme 36 Number of Residues |
361 |
| Enzyme 36 Molecular Weight |
42002.4 |
| Enzyme 36 Theoretical pI |
9.90 |
| Enzyme 36 GO Classification |
Not Available |
| Enzyme 36 General Function |
Involved in receptor activity |
| Enzyme 36 Specific Function |
Not Available |
| Enzyme 36 Pathways |
Not Available |
| Enzyme 36 Reactions |
Not Available |
| Enzyme 36 Pfam Domain Function |
|
| Enzyme 36 Signals |
|
| Enzyme 36 Transmembrane Regions |
|
| Enzyme 36 Essentiality |
Not Available |
| Enzyme 36 GenBank ID Protein |
156491005  |
| Enzyme 36 UniProtKB/Swiss-Prot ID |
B2WTI4  |
| Enzyme 36 UniProtKB/Swiss-Prot Entry Name |
B2WTI4_HUMAN  |
| Enzyme 36 PDB ID |
Not Available |
| Enzyme 36 Cellular Location |
Not Available |
| Enzyme 36 Gene Sequence |
>1086 bp
ATGAACCACAAGAGCAAGAAGCGCATCCGCGAGGCCAAGCGGAGTGCGCGGCCGGAGCTC
AAGGACTCGCTGGATTGGACCCGGCACAACTACTACGAGAGCTTCTCGCTGAGCCCGGCG
GCCGTGGCGGATAACGTGGAAAGGGCAGATGCTTTACAGCTGTCTGTGGAAGAATTTGTG
GAGCGGTATGAAAGACCTTACAAGCCCGTGGTTTTGTTGAATGCGCAAGAGGGCTGGTCT
GCGCAGGAGAAATGGACTCTGGAGCGCCTAAAAAGGAAATATCGGAACCAGAAGTTCAAG
TGTGGTGAGGATAACGATGGCTACTCAGTGAAGATGAAGATGAAATACTACATCGAGTAC
ATGGAGAGCACTCGAGATGATAGTCCCCTTTACATCTTTGACAGCAGCTATGGTGAACAC
CCTAAAAGAAGGAAACTTTTGGAAGACTACAAGGTGCCAAAGTTTTTCACTGATGACCTT
TTCCAGTATGCTGGGGAGAAGCGCAGGCCCCCTTACAGGTGGTTTGTGATGGGGCCACCA
CGCTCCGGAACTGGGATTCACATCGACCCTCTGGGAACCAGTGCCTGGAATGCCTTAGTT
CAGGGCCACAAGCGCTGGTGCCTGTTTCCTACCAGCACTCCCAGGGAACTCATCAAAGTG
ACCCGAGACGAAGGAGGGAACCAGCAAGACGAAGCTATTACCTGGTTTAATGTTATTTAT
CCCCGGACACAGCTTCCAACCTGGCCACCTGAATTCAAACCCCTGGAAATCTTACAAAAA
CCAGGAGAGACTGTCTTTGTACCAGGAGGCTGGTGGCATGTTGTCCTCAATCTCGACACT
ACTATCGCCATCACCCAAAATTTTGCCAGCAGCACCAACTTCCCTGTGGTATGGCACAAG
ACGGTAAGAGGGAGACCAAAGTTATCAAGGAAATGGTATAGAACAGATACAGCACGGGCA
GCGGCAGTGCAAGCCACCCACAGCCACCCCGTGCCACTGTGTCCCAACCCTGACCTGGAG
GGACCAGCTCTCGGGGATTTTGAAGCAAGAGCACCCCGAGTTGGCAGTCCTCGCAGACTC
GGTTGA
|
| Enzyme 36 GenBank Gene ID |
EF527407  |
| Enzyme 36 GeneCard ID |
JMJD6  |
| Enzyme 36 GenAtlas ID |
JMJD6  |
| Enzyme 36 HGNC ID |
HGNC:19355  |
| Enzyme 36 Chromosome Location |
1 |
| Enzyme 36 Locus |
17q25 |
| Enzyme 36 SNPs |
SNPJam Report  |
| Enzyme 36 General References |
- Hahn P, Bose J, Edler S, Lengeling A: Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins. BMC Genomics. 2008 Jun 18;9:293. [PubMed
]
|
| Enzyme 36 Metabolite References |
Not Available |
|
Enzyme 37
[top]
|
| Enzyme 37 ID |
17308 |
| Enzyme 37 Name |
cDNA FLJ38589 fis, clone HCHON2010074, highly similar to LACTADHERIN |
| Enzyme 37 Synonyms |
Not Available |
| Enzyme 37 Gene Name |
Not Available |
| Enzyme 37 Protein Sequence |
>cDNA FLJ38589 fis, clone HCHON2010074, highly similar to LACTADHERIN
MWPFPEGGNTIPILHTDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKGYAGNHCET
KCVEPLGMENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTSSSNDDNPWI
QVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNK
NAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITA
SSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGAR
NFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFETPILARYVR
ILPVAWHNRIALRLELLGC
|
| Enzyme 37 Number of Residues |
379 |
| Enzyme 37 Molecular Weight |
42459.6 |
| Enzyme 37 Theoretical pI |
7.88 |
| Enzyme 37 GO Classification |
| Function |
| — |
| Process |
- cell adhesion
- cellular process
|
| Component |
| — |
|
| Enzyme 37 General Function |
Involved in cell adhesion |
| Enzyme 37 Specific Function |
Not Available |
| Enzyme 37 Pathways |
Not Available |
| Enzyme 37 Reactions |
Not Available |
| Enzyme 37 Pfam Domain Function |
|
| Enzyme 37 Signals |
|
| Enzyme 37 Transmembrane Regions |
|
| Enzyme 37 Essentiality |
Not Available |
| Enzyme 37 GenBank ID Protein |
193788270  |
| Enzyme 37 UniProtKB/Swiss-Prot ID |
B3KTQ2  |
| Enzyme 37 UniProtKB/Swiss-Prot Entry Name |
B3KTQ2_HUMAN  |
| Enzyme 37 PDB ID |
Not Available |
| Enzyme 37 Cellular Location |
Not Available |
| Enzyme 37 Gene Sequence |
>1140 bp
ATGTGGCCTTTTCCAGAAGGAGGAAACACCATACCTATCTTACACACAGATATCTGTTCC
AAAAACCCCTGCCACAACGGTGGTTTATGCGAGGAGATTTCCCAAGAAGTGCGAGGAGAT
GTCTTCCCCTCGTACACCTGCACGTGCCTTAAGGGCTACGCGGGCAACCACTGTGAGACG
AAATGTGTCGAGCCACTGGGCATGGAGAATGGGAACATTGCCAACTCACAGATCGCCGCC
TCATCTGTGCGTGTGACCTTCTTGGGTTTGCAGCATTGGGTCCCGGAGCTGGCCCGCCTG
AACCGCGCAGGCATGGTCAATGCCTGGACATCCAGCAGCAATGACGATAACCCCTGGATC
CAGGTGAACCTGCTGCGGAGGATGTGGGTAACAGGTGTGGTGACGCAGGGTGCCAGCCGC
TTGGCCAGTCATGAGTACCTGAAGGCCTTCAAGGTGGCCTACAGCCTTAATGGACACGAA
TTCGATTTCATCCATGATGTTAATAAAAAACACAAGGAGTTTGTGGGTAACTGGAACAAA
AACGCGGTGCATGTCAACCTGTTTGAGACCCCTGTGGAGGCTCAGTACGTGAGATTGTAC
CCCACGAGCTGCCACACGGCCTGCACTCTGCGCTTTGAGCTACTGGGCTGTGAGCTGAAC
GGATGCGCCAATCCCCTGGGCCTGAAGAATAACAGCATCCCTGACAAGCAGATCACGGCC
TCCAGCAGCTACAAGACCTGGGGCTTGCATCTCTTCAGCTGGAACCCCTCCTATGCACGG
CTGGACAAGCAGGGCAACTTCAACGCCTGGGTTGCGGGGAGCTACGGTAACGATCAGTGG
CTGCAGGTGGACCTGGGCTCCTCGAAGGAGGTGACAGGCATCATCACCCAGGGGGCCCGT
AACTTTGGCTCTGTCCAGTTTGTGGCATCCTACAAGGTTGCCTACAGTAATGACAGTGCG
AACTGGACTGAGTACCAGGACCCCAGGACTGGCAGCAGTAAGATCTTCCCTGGCAACTGG
GACAACCACTCCCACAAGAAGAACTTGTTTGAGACGCCCATCCTGGCTCGCTATGTGCGC
ATCCTGCCTGTAGCCTGGCACAACCGCATCGCCCTGCGCCTGGAGCTGCTGGGCTGTTAG
|
| Enzyme 37 GenBank Gene ID |
AK095908  |
| Enzyme 37 GeneCard ID |
Not Available |
| Enzyme 37 GenAtlas ID |
Not Available |
| Enzyme 37 HGNC ID |
HGNC:7036  |
| Enzyme 37 Chromosome Location |
Not Available |
| Enzyme 37 Locus |
Not Available |
| Enzyme 37 SNPs |
Not Available |
| Enzyme 37 General References |
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
|
| Enzyme 37 Metabolite References |
Not Available |
|
Enzyme 38
[top]
|
| Enzyme 38 ID |
17309 |
| Enzyme 38 Name |
Putative uncharacterized protein DKFZp686M1886 |
| Enzyme 38 Synonyms |
Not Available |
| Enzyme 38 Gene Name |
DKFZp686M1886 |
| Enzyme 38 Protein Sequence |
>Putative uncharacterized protein DKFZp686M1886
MENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPSSNDDNPWIQVNLLRR
MWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHKEFVGNWNKNAVHVNL
FETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNSIPDKQITASSSYKTW
GLHLFSWNPSYAWLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVTGIITQGARNFGSVQF
VASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHTHKKNLFETPILARYVRILPVAWH
NRIALRLELLGC
|
| Enzyme 38 Number of Residues |
312 |
| Enzyme 38 Molecular Weight |
35233 |
| Enzyme 38 Theoretical pI |
8.89 |
| Enzyme 38 GO Classification |
| Function |
| — |
| Process |
- cell adhesion
- cellular process
|
| Component |
| — |
|
| Enzyme 38 General Function |
Not Available |
| Enzyme 38 Specific Function |
Not Available |
| Enzyme 38 Pathways |
Not Available |
| Enzyme 38 Reactions |
Not Available |
| Enzyme 38 Pfam Domain Function |
|
| Enzyme 38 Signals |
|
| Enzyme 38 Transmembrane Regions |
|
| Enzyme 38 Essentiality |
Not Available |
| Enzyme 38 GenBank ID Protein |
Not Available |
| Enzyme 38 UniProtKB/Swiss-Prot ID |
Q7Z3D2  |
| Enzyme 38 UniProtKB/Swiss-Prot Entry Name |
Q7Z3D2_HUMAN  |
| Enzyme 38 PDB ID |
Not Available |
| Enzyme 38 Cellular Location |
Not Available |
| Enzyme 38 Gene Sequence |
Not Available |
| Enzyme 38 GenBank Gene ID |
BX537974  |
| Enzyme 38 GeneCard ID |
DKFZp686M1886  |
| Enzyme 38 GenAtlas ID |
DKFZp686M1886  |
| Enzyme 38 HGNC ID |
HGNC:7036  |
| Enzyme 38 Chromosome Location |
Not Available |
| Enzyme 38 Locus |
Not Available |
| Enzyme 38 SNPs |
SNPJam Report  |
| Enzyme 38 General References |
Not Available |
| Enzyme 38 Metabolite References |
Not Available |
|
Enzyme 39
[top]
|
| Enzyme 39 ID |
17310 |
| Enzyme 39 Name |
Serine incorporator 5 |
| Enzyme 39 Synonyms |
Not Available |
| Enzyme 39 Gene Name |
SERINC5 |
| Enzyme 39 Protein Sequence |
>Serine incorporator 5
MSAQCCAGQLACCCGSAGCSLCCDCCPRIRQSLSTRFMYALYFILVVVLCCIMMSTTVAH
KMKEHIPFFEDMCKGIKAGDTCEKLVGYSAVYRVCFGMACFFFIFCLLTLKINNSKSCRA
HIHNGFWFFKLLLLGAMCSGAFFIPDQDTFLNAWRYVGAVGGFLFIGIQLLLLVEFAHKW
NKNWTAGTASNKLWYASLALVTLIMYSIATGGLVLMAVFYTQKDSCMENKILLGVNGGLC
LLISLVAISPWVQNRQPHSGLLQSGVISCYVTYLTFSALSSKPAEVVLDEHGKNVTICVP
DFGQDLYRDENLVTILGTSLLIGCILYSCLTSTTRSSSDALQGRYAAPELEIARCCFCFS
PGGEDTEEQQPGKEGPRVIYDEKKGTVYIYSYFHFVFFLASLYVMMTVTNWFNHVRSAFH
LLP
|
| Enzyme 39 Number of Residues |
423 |
| Enzyme 39 Molecular Weight |
47008.7 |
| Enzyme 39 Theoretical pI |
7.65 |
| Enzyme 39 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 39 General Function |
Involved in phosphatidylserine metabolic process |
| Enzyme 39 Specific Function |
Enhances the incorporation of serine into phosphatidylserine and sphingolipids. May play a role in providing serine molecules for the formation of myelin glycosphingolipids in oligodendrocytes |
| Enzyme 39 Pathways |
Not Available |
| Enzyme 39 Reactions |
Not Available |
| Enzyme 39 Pfam Domain Function |
|
| Enzyme 39 Signals |
|
| Enzyme 39 Transmembrane Regions |
- 37-57
90-110
125-145
157-177
199-219
231-251
259-279
312-332
386-406
|
| Enzyme 39 Essentiality |
Not Available |
| Enzyme 39 GenBank ID Protein |
29893239  |
| Enzyme 39 UniProtKB/Swiss-Prot ID |
Q86VE9  |
| Enzyme 39 UniProtKB/Swiss-Prot Entry Name |
SERC5_HUMAN  |
| Enzyme 39 PDB ID |
Not Available |
| Enzyme 39 Cellular Location |
Not Available |
| Enzyme 39 Gene Sequence |
>1272 bp
ATGTCAGCTCAGTGCTGTGCGGGCCAGCTGGCCTGCTGCTGTGGGTCTGCAGGCTGCTCT
CTCTGCTGTGATTGCTGCCCCAGGATTCGGCAGTCCCTCAGCACCCGCTTCATGTACGCC
CTCTACTTCATTCTGGTCGTCGTCCTCTGCTGCATCATGATGTCAACAACCGTGGCTCAC
AAGATGAAAGAGCACATTCCTTTTTTTGAAGATATGTGTAAAGGCATTAAAGCTGGTGAC
ACCTGTGAGAAGCTGGTGGGATATTCTGCCGTGTATAGAGTCTGTTTTGGAATGGCTTGT
TTCTTCTTTATCTTCTGTCTACTGACCTTGAAAATCAACAACAGCAAAAGTTGTAGAGCT
CATATTCACAATGGCTTTTGGTTCTTTAAACTTCTGCTGTTGGGGGCCATGTGCTCAGGA
GCTTTCTTCATTCCAGATCAGGACACCTTTCTGAACGCCTGGCGCTATGTGGGAGCCGTC
GGAGGCTTCCTCTTCATTGGCATCCAGCTCCTCCTGCTCGTGGAGTTTGCACATAAGTGG
AACAAGAACTGGACAGCAGGCACAGCCAGTAACAAGCTGTGGTACGCCTCCCTGGCCCTG
GTGACGCTCATCATGTATTCCATTGCCACTGGAGGCTTGGTTTTGATGGCAGTGTTTTAT
ACACAGAAAGACAGCTGCATGGAAAACAAAATTCTGCTGGGAGTAAATGGAGGCCTGTGC
CTGCTTATATCATTGGTAGCCATCTCACCCTGGGTCCAAAATCGACAGCCACACTCGGGG
CTCTTACAATCAGGGGTCATAAGCTGCTATGTCACCTACCTCACCTTCTCAGCTCTGTCC
AGCAAACCTGCAGAAGTAGTTCTAGATGAACATGGGAAAAATGTTACAATCTGTGTGCCT
GACTTTGGTCAAGACCTGTACAGAGATGAAAACTTGGTGACTATACTGGGGACCAGCCTC
TTAATCGGATGTATCTTGTATTCATGTTTGACATCAACAACAAGATCGAGTTCTGACGCT
CTGCAGGGGCGATACGCAGCTCCTGAATTGGAGATAGCTCGCTGTTGTTTTTGCTTCAGT
CCTGGTGGAGAGGACACTGAAGAGCAGCAGCCGGGGAAGGAGGGACCACGGGTCATTTAT
GACGAGAAGAAAGGCACCGTCTACATCTACTCCTACTTCCACTTCGTGTTCTTCCTAGCT
TCCCTGTATGTGATGATGACCGTCACCAACTGGTTCAACCATGTAAGAAGTGCCTTTCAC
CTCCTGCCATGA
|
| Enzyme 39 GenBank Gene ID |
AF498273  |
| Enzyme 39 GeneCard ID |
SERINC5  |
| Enzyme 39 GenAtlas ID |
SERINC5  |
| Enzyme 39 HGNC ID |
HGNC:18825  |
| Enzyme 39 Chromosome Location |
5 |
| Enzyme 39 Locus |
5q14.1 |
| Enzyme 39 SNPs |
SNPJam Report  |
| Enzyme 39 General References |
- Xu J, Ji C, Wang L, Cao Y, Dai J, Ye X, Zeng L, Dai J, Wu Q, Xie Y, Mao Y: Cloning and expression of a novel human C5orf12 gene*, a member of the TMS_TDE family. Mol Biol Rep. 2003 Mar;30(1):47-52. [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
]
|
| Enzyme 39 Metabolite References |
Not Available |
|
Enzyme 40
[top]
|
| Enzyme 40 ID |
17311 |
| Enzyme 40 Name |
Adseverin |
| Enzyme 40 Synonyms |
- Scinderin
|
| Enzyme 40 Gene Name |
SCIN |
| Enzyme 40 Protein Sequence |
>Adseverin
MARELYHEEFARAGKQAGLQVWRIEKLELVPVPQSAHGDFYVGDAYLVLHTAKTSRGFTY
HLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQNRELQGYESNDFVSYFKGGLKYKAG
GVASGLNHVLTNDLTAKRLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGS
SCNKYERLKANQVATGIRYNERKGRSELIVVEEGSEPSELIKVLGEKPELPDGGDDDDII
ADISNRKMAKLYMVSDASGSMRVTVVAEENPFSMAMLLSEECFILDHGAAKQIFVWKGKD
ANPQERKAAMKTAEEFLQQMNYSKNTQIQVLPEGGETPIFKQFFKDWRDKDQSDGFGKVY
VTEKVAQIKQIPFDASKLHSSPQMAAQHNMVDDGSGKVEIWRVENNGRIQVDQNSYGEFY
GGDCYIILYTYPRGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIRVSQGKEPV
HLLSLFKDKPLIIYKNGTSKKGGQAPAPPTRLFQVRRNLASITRIVEVDVDANSLNSNDV
FVLKLPQNSGYIWVGKGASQEEEKGAEYVASVLKCKTLRIQEGEEPEEFWNSLGGKKDYQ
TSPLLETQAEDHPPRLYGCSNKTGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGK
DANEVEKKESLKSAKMYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSKW
|
| Enzyme 40 Number of Residues |
715 |
| Enzyme 40 Molecular Weight |
80488.3 |
| Enzyme 40 Theoretical pI |
5.41 |
| Enzyme 40 GO Classification |
| Function |
- actin binding
- binding
- cytoskeletal protein binding
- protein binding
|
| Process |
| — |
| Component |
| — |
|
| Enzyme 40 General Function |
Involved in actin binding |
| Enzyme 40 Specific Function |
Ca(2+)-dependent actin filament-severing protein that is presumed to have a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane. In vitro, also has barbed end capping and nucleating activities in the presence of Ca(2+) |
| 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 |
162951877  |
| Enzyme 40 UniProtKB/Swiss-Prot ID |
Q9Y6U3  |
| Enzyme 40 UniProtKB/Swiss-Prot Entry Name |
ADSV_HUMAN  |
| Enzyme 40 PDB ID |
Not Available |
| Enzyme 40 Cellular Location |
Not Available |
| Enzyme 40 Gene Sequence |
>2148 bp
ATGGCGCGGGAGCTATACCACGAAGAGTTCGCCCGGGCGGGCAAGCAGGCGGGGCTGCAG
GTCTGGAGGATTGAGAAGCTGGAGCTGGTGCCCGTGCCCCAGAGCGCTCACGGCGACTTC
TACGTCGGGGATGCCTACCTGGTGCTGCACACGGCCAAGACGAGCCGAGGCTTCACCTAC
CACCTGCACTTCTGGCTCGGAAAGGAGTGTTCCCAGGATGAAAGCACAGCTGCTGCCATC
TTCACTGTTCAGATGGATGACTATTTGGGTGGCAAGCCAGTGCAGAATAGAGAACTTCAA
GGATATGAGTCTAATGACTTTGTTAGCTATTTCAAAGGCGGTCTGAAATACAAGGCTGGA
GGCGTGGCATCTGGATTAAATCATGTTCTTACGAACGACCTGACAGCCAAGAGGCTCCTA
CATGTGAAGGGTCGTAGAGTGGTGAGAGCCACAGAAGTTCCCCTTAGCTGGGACAGTTTC
AACAAGGGTGACTGCTTCATCATTGACCTTGGCACCGAAATTTATCAGTGGTGTGGTTCC
TCGTGCAACAAATATGAACGTCTGAAGGCAAACCAGGTAGCTACTGGCATTCGGTACAAT
GAAAGGAAAGGAAGGTCTGAACTAATTGTCGTGGAAGAAGGAAGTGAACCCTCAGAACTT
ATAAAGGTCTTAGGGGAAAAGCCAGAGCTTCCAGATGGAGGTGATGATGATGACATTATA
GCAGACATAAGTAACAGGAAAATGGCTAAACTATACATGGTTTCAGATGCAAGTGGCTCC
ATGAGAGTGACTGTGGTGGCAGAAGAAAACCCCTTCTCAATGGCAATGCTGCTGTCTGAA
GAATGCTTTATTTTGGACCACGGGGCTGCCAAACAAATTTTCGTATGGAAAGGTAAAGAT
GCTAATCCCCAAGAGAGGAAGGCTGCAATGAAGACAGCTGAAGAATTTCTACAGCAAATG
AATTATTCCAAGAATACCCAAATTCAAGTTCTTCCAGAAGGAGGTGAAACACCAATCTTC
AAACAGTTTTTTAAGGACTGGAGAGATAAAGATCAGAGTGATGGCTTCGGGAAAGTTTAT
GTCACAGAGAAAGTGGCTCAAATAAAACAAATTCCCTTTGATGCCTCAAAATTACACAGT
TCTCCGCAGATGGCAGCCCAGCACAATATGGTGGATGATGGTTCTGGCAAAGTGGAGATT
TGGCGTGTAGAAAACAATGGTAGGATCCAAGTTGACCAAAACTCATATGGTGAATTCTAT
GGTGGTGACTGCTACATCATACTCTACACCTATCCCAGAGGACAGATTATCTACACGTGG
CAAGGAGCAAATGCCACACGAGATGAGCTGACAACATCTGCGTTCCTGACTGTTCAGTTG
GATCGGTCCCTTGGAGGACAGGCTGTGCAGATCCGAGTCTCCCAAGGCAAAGAGCCTGTT
CACCTACTGAGTTTGTTCAAAGACAAACCGCTCATTATTTACAAGAATGGAACATCAAAG
AAAGGAGGTCAGGCACCTGCTCCCCCTACACGCCTCTTTCAAGTCCGGAGAAACCTGGCA
TCTATCACCAGAATTGTGGAGGTTGATGTTGATGCAAATTCACTGAATTCTAACGATGTT
TTTGTCCTGAAACTGCCACAAAATAGTGGCTACATCTGGGTAGGAAAAGGTGCTAGCCAG
GAGGAGGAGAAAGGAGCAGAGTATGTAGCAAGTGTCCTAAAGTGCAAAACCTTAAGGATC
CAAGAAGGCGAGGAGCCAGAGGAGTTCTGGAATTCCCTTGGAGGGAAAAAAGACTACCAG
ACCTCACCACTACTGGAAACCCAGGCTGAAGACCATCCACCTCGGCTTTACGGCTGCTCT
AACAAAACTGGAAGATTTGTTATTGAAGAGATTCCAGGAGAGTTCACCCAGGATGATTTA
GCTGAAGATGATGTCATGTTACTAGATGCTTGGGAACAGATATTTATTTGGATTGGCAAA
GATGCTAATGAAGTTGAGAAAAAAGAATCTCTGAAGTCTGCCAAAATGTACCTTGAGACA
GACCCTTCTGGAAGAGACAAGAGGACACCAATTGTCATCATAAAACAGGGCCATGAGCCA
CCCACATTCACAGGCTGGTTCCTGGGCTGGGATTCCAGCAAGTGGTAA
|
| Enzyme 40 GenBank Gene ID |
NM_001112706.2  |
| Enzyme 40 GeneCard ID |
SCIN  |
| Enzyme 40 GenAtlas ID |
SCIN  |
| Enzyme 40 HGNC ID |
HGNC:21695  |
| Enzyme 40 Chromosome Location |
7 |
| Enzyme 40 Locus |
7p21.3 |
| Enzyme 40 SNPs |
SNPJam Report  |
| Enzyme 40 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
]
- Nagase T, Kikuno R, Ohara O: Prediction of the coding sequences of unidentified human genes. XXI. The complete sequences of 60 new cDNA clones from brain which code for large proteins. DNA Res. 2001 Aug 31;8(4):179-87. [PubMed
]
- Hillier LW, Fulton RS, Fulton LA, Graves TA, Pepin KH, Wagner-McPherson C, Layman D, Maas J, Jaeger S, Walker R, Wylie K, Sekhon M, Becker MC, O'Laughlin MD, Schaller ME, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Cordes M, Du H, Sun H, Edwards J, Bradshaw-Cordum H, Ali J, Andrews S, Isak A, Vanbrunt A, Nguyen C, Du F, Lamar B, Courtney L, Kalicki J, Ozersky P, Bielicki L, Scott K, Holmes A, Harkins R, Harris A, Strong CM, Hou S, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Leonard S, Rohlfing T, Rock SM, Tin-Wollam AM, Abbott A, Minx P, Maupin R, Strowmatt C, Latreille P, Miller N, Johnson D, Murray J, Woessner JP, Wendl MC, Yang SP, Schultz BR, Wallis JW, Spieth J, Bieri TA, Nelson JO, Berkowicz N, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Bedell JA, Mardis ER, Clifton SW, Chissoe SL, Marra MA, Raymond C, Haugen E, Gillett W, Zhou Y, James R, Phelps K, Iadanoto S, Bubb K, Simms E, Levy R, Clendenning J, Kaul R, Kent WJ, Furey TS, Baertsch RA, Brent MR, Keibler E, Flicek P, Bork P, Suyama M, Bailey JA, Portnoy ME, Torrents D, Chinwalla AT, Gish WR, Eddy SR, McPherson JD, Olson MV, Eichler EE, Green ED, Waterston RH, Wilson RK: The DNA sequence of human chromosome 7. Nature. 2003 Jul 10;424(6945):157-64. [PubMed
]
- 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 40 Metabolite References |
Not Available |
|
Enzyme 41
[top]
|
| Enzyme 41 ID |
17312 |
| Enzyme 41 Name |
Serine incorporator 4 |
| Enzyme 41 Synonyms |
Not Available |
| Enzyme 41 Gene Name |
SERINC4 |
| Enzyme 41 Protein Sequence |
>Serine incorporator 4
MVGAKAGPSPGTSLGLAQQHSGGSSVLVKSPFCQVCCCGPAPCASCCHSRWPSLTASTCS
RLFYILLHVGASAICCLLLSRTVVERVWGKTHRIQMPSGLCAHLFGLSDCPVLSGSGAVY
RVCAGTATFHLLQAVLLVHLHSPTSPRAQLHNSFWLLKLLFLLGLCAIAFCIPDEHLFPA
WHYIGICGGFAFILLQLVLITAFAHSWNKNWQTGAAQDCSWFLAVLLATLGFYSMAGVGA
VLLFHYYTHPAGCLLNKMLLSLHLCFCGLISFLSIAPCIRLKQPRSGLLQASVISCYIMY
LTFSALSSRPPERVILQGQNHTLCLPGLSKMEPQTPDISLAMLSASIMYACVLFACNEAS
YLAEVFGPLWIVKVYSYEFQKPSLCFCCPETVEADKGQRGGAARPADQETPPAPPVQVQH
LSYNYSAFHFVFFLASLYVMVTLTNWFSYEGAELEKTFIKGSWATFWVKVASCWACVLLY
LGLLLAPLCWPPTQKPQPLILRRRRHRIISPDNKYPPV
|
| Enzyme 41 Number of Residues |
518 |
| Enzyme 41 Molecular Weight |
56869.4 |
| Enzyme 41 Theoretical pI |
8.39 |
| Enzyme 41 GO Classification |
| Function |
| — |
| Process |
| — |
| Component |
|
|
| Enzyme 41 General Function |
Involved in phospholipid biosynthetic process |
| Enzyme 41 Specific Function |
Incorporates a polar amino acid serine into membranes and facilitates the synthesis of two serine-derived lipids, phosphatidylserine and sphingolipids |
| Enzyme 41 Pathways |
Not Available |
| Enzyme 41 Reactions |
Not Available |
| Enzyme 41 Pfam Domain Function |
|
| Enzyme 41 Signals |
|
| Enzyme 41 Transmembrane Regions |
- 59-79
122-142
153-173
184-204
222-242
259-279
286-306
338-357
427-447
470-490
|
| Enzyme 41 Essentiality |
Not Available |
| Enzyme 41 GenBank ID Protein |
75677608  |
| Enzyme 41 UniProtKB/Swiss-Prot ID |
A6NH21  |
| Enzyme 41 UniProtKB/Swiss-Prot Entry Name |
SERC4_HUMAN  |
| Enzyme 41 PDB ID |
Not Available |
| Enzyme 41 Cellular Location |
Not Available |
| Enzyme 41 Gene Sequence |
Not Available |
| Enzyme 41 GenBank Gene ID |
Not Available |
| Enzyme 41 GeneCard ID |
SERINC4  |
| Enzyme 41 GenAtlas ID |
SERINC4  |
| Enzyme 41 HGNC ID |
HGNC:32237  |
| Enzyme 41 Chromosome Location |
1 |
| Enzyme 41 Locus |
15q15.3 |
| Enzyme 41 SNPs |
SNPJam Report  |
| Enzyme 41 General References |
- Inuzuka M, Hayakawa M, Ingi T: Serinc, an activity-regulated protein family, incorporates serine into membrane lipid synthesis. J Biol Chem. 2005 Oct 21;280(42):35776-83. Epub 2005 Aug 24. [PubMed
]
- Zody MC, Garber M, Sharpe T, Young SK, Rowen L, O'Neill K, Whittaker CA, Kamal M, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Kodira CD, Madan A, Qin S, Yang X, Abbasi N, Abouelleil A, Arachchi HM, Baradarani L, Birditt B, Bloom S, Bloom T, Borowsky ML, Burke J, Butler J, Cook A, DeArellano K, DeCaprio D, Dorris L 3rd, Dors M, Eichler EE, Engels R, Fahey J, Fleetwood P, Friedman C, Gearin G, Hall JL, Hensley G, Johnson E, Jones C, Kamat A, Kaur A, Locke DP, Madan A, Munson G, Jaffe DB, Lui A, Macdonald P, Mauceli E, Naylor JW, Nesbitt R, Nicol R, O'Leary SB, Ratcliffe A, Rounsley S, She X, Sneddon KM, Stewart S, Sougnez C, Stone SM, Topham K, Vincent D, Wang S, Zimmer AR, Birren BW, Hood L, Lander ES, Nusbaum C: Analysis of the DNA sequence and duplication history of human chromosome 15. Nature. 2006 Mar 30;440(7084):671-5. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
|
| Enzyme 41 Metabolite References |
Not Available |
|
Enzyme 42
[top]
|
| Enzyme 42 ID |
17313 |
| Enzyme 42 Name |
Phosphatidylserine receptor transcript variant 1 |
| Enzyme 42 Synonyms |
- SubName: Phosphatidylserine receptor, isoform CRA_d
|
| Enzyme 42 Gene Name |
JMJD6 |
| Enzyme 42 Protein Sequence |
>Phosphatidylserine receptor transcript variant 1
MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFV
ERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEY
MESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPP
RSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIY
PRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHK
TVRGRPKLSRKWYRYSTGSGSASHPQPPRATVSQP
|
| Enzyme 42 Number of Residues |
335 |
| Enzyme 42 Molecular Weight |
39241.2 |
| Enzyme 42 Theoretical pI |
10.00 |
| Enzyme 42 GO Classification |
Not Available |
| Enzyme 42 General Function |
Involved in receptor activity |
| Enzyme 42 Specific Function |
Not Available |
| Enzyme 42 Pathways |
Not Available |
| Enzyme 42 Reactions |
Not Available |
| Enzyme 42 Pfam Domain Function |
|
| Enzyme 42 Signals |
|
| Enzyme 42 Transmembrane Regions |
|
| Enzyme 42 Essentiality |
Not Available |
| Enzyme 42 GenBank ID Protein |
156491003  |
| Enzyme 42 UniProtKB/Swiss-Prot ID |
B2WTI3  |
| Enzyme 42 UniProtKB/Swiss-Prot Entry Name |
B2WTI3_HUMAN  |
| Enzyme 42 PDB ID |
Not Available |
| Enzyme 42 Cellular Location |
Not Available |
| Enzyme 42 Gene Sequence |
>1008 bp
ATGAACCACAAGAGCAAGAAGCGCATCCGCGAGGCCAAGCGGAGTGCGCGGCCGGAGCTC
AAGGACTCGCTGGATTGGACCCGGCACAACTACTACGAGAGCTTCTCGCTGAGCCCGGCG
GCCGTGGCGGATAACGTGGAAAGGGCAGATGCTTTACAGCTGTCTGTGGAAGAATTTGTG
GAGCGGTATGAAAGACCTTACAAGCCCGTGGTTTTGTTGAATGCGCAAGAGGGCTGGTCT
GCGCAGGAGAAATGGACTCTGGAGCGCCTAAAAAGGAAATATCGGAACCAGAAGTTCAAG
TGTGGTGAGGATAACGATGGCTACTCAGTGAAGATGAAGATGAAATACTACATCGAGTAC
ATGGAGAGCACTCGAGATGATAGTCCCCTTTACATCTTTGACAGCAGCTATGGTGAACAC
CCTAAAAGAAGGAAACTTTTGGAAGACTACAAGGTGCCAAAGTTTTTCACTGATGACCTT
TTCCAGTATGCTGGGGAGAAGCGCAGGCCCCCTTACAGGTGGTTTGTGATGGGGCCACCA
CGCTCCGGAACTGGGATTCACATCGACCCTCTGGGAACCAGTGCCTGGAATGCCTTAGTT
CAGGGCCACAAGCGCTGGTGCCTGTTTCCTACCAGCACTCCCAGGGAACTCATCAAAGTG
ACCCGAGACGAAGGAGGGAACCAGCAAGACGAAGCTATTACCTGGTTTAATGTTATTTAT
CCCCGGACACAGCTTCCAACCTGGCCACCTGAATTCAAACCCCTGGAAATCTTACAAAAA
CCAGGAGAGACTGTCTTTGTACCAGGAGGCTGGTGGCATGTTGTCCTCAATCTCGACACT
ACTATCGCCATCACCCAAAATTTTGCCAGCAGCACCAACTTCCCTGTGGTATGGCACAAG
ACGGTAAGAGGGAGACCAAAGTTATCAAGGAAATGGTATAGATACAGCACGGGCAGCGGC
AGTGCAAGCCACCCACAGCCACCCCGTGCCACTGTGTCCCAACCCTGA
|
| Enzyme 42 GenBank Gene ID |
EF527406  |
| Enzyme 42 GeneCard ID |
JMJD6  |
| Enzyme 42 GenAtlas ID |
JMJD6  |
| Enzyme 42 HGNC ID |
HGNC:19355  |
| Enzyme 42 Chromosome Location |
1 |
| Enzyme 42 Locus |
17q25 |
| Enzyme 42 SNPs |
SNPJam Report  |
| Enzyme 42 General References |
- Hahn P, Bose J, Edler S, Lengeling A: Genomic structure and expression of Jmjd6 and evolutionary analysis in the context of related JmjC domain containing proteins. BMC Genomics. 2008 Jun 18;9:293. [PubMed
]
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 42 Metabolite References |
Not Available |
|
Enzyme 43
[top]
|
| Enzyme 43 ID |
17314 |
| Enzyme 43 Name |
cDNA, FLJ94904, Homo sapiens copine VI (neuronal) (CPNE6), mRNA (Copine VI (Neuronal), isoform CRA_c) |
| Enzyme 43 Synonyms |
Not Available |
| Enzyme 43 Gene Name |
CPNE6 |
| Enzyme 43 Protein Sequence |
>cDNA, FLJ94904, Homo sapiens copine VI (neuronal) (CPNE6), mRNA (Copine VI (Neuronal), isoform CRA_c)
MSDPEMGWVPEPPTMTLGASRVELRVSCHGLLDRDTLTKPHPCVLLKLYSDEQWVEVERT
EVLRSCSSPVFSRVLALEYFFEEKQPLQFHVFDAEDGATSPRNDTFLGSTECTLGQIVSQ
TKVTKPLLLKNGKTAGKSTITIVAEEVSGTNDYVQLTFRAYKLDNKDLFSKSDPFMEIYK
TNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGKHDFIG
EFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKNYKSSGTVVLAQCTVEKVHTFLDYIM
GGCQISFTVAIDFTASNGDPRSSQSLHCLSPRQPNHYLQALRAVGGICQDYDSDKRFPAF
GFGARIPPNFEVSHDFAINFDPENPECEEISGVIASYRRCLPQIQLYGPTNVAPIINRVA
EPAQREQSTGQATKYSVLLVLTDGVVSDMAETRTAIVRASRLPMSIIIVGVGNADFSDMR
LLDGDDGPLRCPRGVPAARDIVQFVPFRDFKDAAPSALAKCVLAEVPRQVVEYYASQGIS
PGAPRPCTLATTPSPSP
|
| Enzyme 43 Number of Residues |
557 |
| Enzyme 43 Molecular Weight |
61992 |
| Enzyme 43 Theoretical pI |
5.17 |
| Enzyme 43 GO Classification |
Not Available |
| Enzyme 43 General Function |
Not Available |
| 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 |
Not Available |
| Enzyme 43 UniProtKB/Swiss-Prot ID |
B2RAG6  |
| Enzyme 43 UniProtKB/Swiss-Prot Entry Name |
B2RAG6_HUMAN  |
| Enzyme 43 PDB ID |
Not Available |
| Enzyme 43 Cellular Location |
Not Available |
| Enzyme 43 Gene Sequence |
Not Available |
| Enzyme 43 GenBank Gene ID |
AK314182  |
| Enzyme 43 GeneCard ID |
CPNE6  |
| Enzyme 43 GenAtlas ID |
CPNE6  |
| Enzyme 43 HGNC ID |
HGNC:2319  |
| Enzyme 43 Chromosome Location |
Not Available |
| Enzyme 43 Locus |
Not Available |
| Enzyme 43 SNPs |
SNPJam Report  |
| Enzyme 43 General References |
Not Available |
| Enzyme 43 Metabolite References |
Not Available |
|
Enzyme 44
[top]
|
| Enzyme 44 ID |
17315 |
| Enzyme 44 Name |
cDNA FLJ59612, highly similar to Lactadherin |
| Enzyme 44 Synonyms |
Not Available |
| Enzyme 44 Gene Name |
Not Available |
| Enzyme 44 Protein Sequence |
>cDNA FLJ59612, highly similar to Lactadherin
MPRPRLLAALCGALLRAPSLLVALECVESLGMENGNIANSQIAASSVRVTFLGLQHWVPE
LARLNRAGMVNAWTPSSNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSL
NGHEFDFIHDVNKKHKEFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLG
CELNGCANPLGLKNNSIPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYG
NDQWLQVDLGSSKEVTGIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIF
PGNWDNHSHKKNLFETPILARYVRILPVAWHNRIALRLELLGC
|
| Enzyme 44 Number of Residues |
343 |
| Enzyme 44 Molecular Weight |
38404.4 |
| Enzyme 44 Theoretical pI |
8.99 |
| Enzyme 44 GO Classification |
| Function |
| — |
| Process |
- cell adhesion
- cellular process
|
| Component |
| — |
|
| Enzyme 44 General Function |
Involved in cell adhesion |
| Enzyme 44 Specific Function |
Not Available |
| Enzyme 44 Pathways |
Not Available |
| Enzyme 44 Reactions |
Not Available |
| Enzyme 44 Pfam Domain Function |
|
| Enzyme 44 Signals |
|
| Enzyme 44 Transmembrane Regions |
|
| Enzyme 44 Essentiality |
Not Available |
| Enzyme 44 GenBank ID Protein |
194388048  |
| Enzyme 44 UniProtKB/Swiss-Prot ID |
B4E396  |
| Enzyme 44 UniProtKB/Swiss-Prot Entry Name |
B4E396_HUMAN  |
| Enzyme 44 PDB ID |
Not Available |
| Enzyme 44 Cellular Location |
Not Available |
| Enzyme 44 Gene Sequence |
>1032 bp
ATGCCGCGCCCCCGCCTGCTGGCCGCGCTGTGCGGCGCGCTGCTCCGCGCCCCCAGCCTC
CTCGTCGCCCTGGAATGTGTCGAGTCACTGGGCATGGAGAATGGGAACATTGCCAACTCA
CAGATCGCCGCCTCATCTGTGCGTGTGACCTTCTTGGGTTTGCAGCATTGGGTCCCGGAG
CTGGCCCGCCTGAACCGCGCAGGCATGGTCAATGCCTGGACACCCAGCAGCAATGACGAT
AACCCCTGGATCCAGGTGAACCTGCTGCGGAGGATGTGGGTAACAGGTGTGGTGACGCAG
GGTGCCAGCCGCTTGGCCAGTCATGAGTACCTGAAGGCCTTCAAGGTGGCCTACAGCCTT
AATGGACACGAATTCGATTTCATCCATGATGTTAATAAAAAACACAAGGAGTTTGTGGGT
AACTGGAACAAAAACGCGGTGCATGTCAACCTGTTTGAGACCCCTGTGGAGGCTCAGTAC
GTGAGATTGTACCCCACGAGCTGCCACACGGCCTGCACTCTGCGCTTTGAGCTACTGGGC
TGTGAGCTGAACGGATGCGCCAATCCCCTGGGCCTGAAGAATAACAGCATCCCTGACAAG
CAGATCACGGCCTCCAGCAGCTACAAGACCTGGGGCTTGCATCTCTTCAGCTGGAACCCC
TCCTATGCACGGCTGGACAAGCAGGGCAACTTCAACGCCTGGGTTGCGGGGAGCTACGGT
AACGATCAGTGGCTGCAGGTGGACCTGGGCTCCTCGAAGGAGGTGACAGGCATCATCACC
CAGGGGGCCCGTAACTTTGGCTCTGTCCAGTTTGTGGCATCCTACAAGGTTGCCTACAGT
AATGACAGTGCGAACTGGACTGAGTACCAGGACCCCAGGACTGGCAGCAGTAAGATCTTC
CCTGGCAACTGGGACAACCACTCCCACAAGAAGAACTTGTTTGAGACGCCCATCCTGGCT
CGCTATGTGCGCATCCTGCCTGTAGCCTGGCACAACCGCATCGCCCTGCGCCTGGAGCTG
CTGGGCTGTTAG
|
| Enzyme 44 GenBank Gene ID |
AK304627  |
| Enzyme 44 GeneCard ID |
Not Available |
| Enzyme 44 GenAtlas ID |
Not Available |
| Enzyme 44 HGNC ID |
HGNC:7036  |
| Enzyme 44 Chromosome Location |
Not Available |
| Enzyme 44 Locus |
Not Available |
| Enzyme 44 SNPs |
Not Available |
| Enzyme 44 General References |
Not Available |
| Enzyme 44 Metabolite References |
Not Available |
|
Enzyme 45
[top]
|
| Enzyme 45 ID |
17316 |
| Enzyme 45 Name |
Copine VI (Neuronal), isoform CRA_a |
| Enzyme 45 Synonyms |
- SubName: cDNA FLJ43205 fis, clone FEBRA2009185, highly similar to Copine-6
|
| Enzyme 45 Gene Name |
CPNE6 |
| Enzyme 45 Protein Sequence |
>Copine VI (Neuronal), isoform CRA_a
MEIYKTNEDQSDQLVWRTEVVKNNLNPSWEPFRLSLHSLCSCDVHRPLKFLVYDYDSSGK
HDFIGEFTSTFQEMQEGTANPGQEMQWDCINPKYRDKKKNYKSSGTVVLAQCTVEKVHTF
LDYIMGGCQISFTVAIDFTASNGDPRSSQSLHCLSPRQPNHYLQALRAVGGICQDYDSDK
RFPAFGFGARIPPNFEVSHDFAINFDPENPECEEISGVIASYRRCLPQIQLYGPTNVAPI
INRVAEPAQREQSTGQATKYSVLLVLTDGVVSDMAETRTAIVRASRLPMSIIIVGVGNAD
FSDMRLLDGDDGPLRCPRGVPAARDIVQFVPFRDFKDAAPSALAKCVLAEVPRQVVEYYA
SQGISPGAPRPCTLATTPSPSP
|
| Enzyme 45 Number of Residues |
382 |
| Enzyme 45 Molecular Weight |
42372.5 |
| Enzyme 45 Theoretical pI |
5.44 |
| Enzyme 45 GO Classification |
Not Available |
| Enzyme 45 General Function |
Not Available |
| 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 |
193785010  |
| Enzyme 45 UniProtKB/Swiss-Prot ID |
B3KWK1  |
| Enzyme 45 UniProtKB/Swiss-Prot Entry Name |
B3KWK1_HUMAN  |
| Enzyme 45 PDB ID |
Not Available |
| Enzyme 45 Cellular Location |
Not Available |
| Enzyme 45 Gene Sequence |
>1149 bp
ATGGAAATCTATAAGACCAACGAGGACCAAAGTGATCAGCTGGTCTGGAGAACTGAGGTG
GTGAAGAACAACCTGAACCCCAGCTGGGAGCCGTTCCGCCTGTCCCTGCATTCCCTATGC
AGCTGTGATGTTCACCGACCTCTCAAGTTCCTGGTGTATGACTATGACTCCAGTGGGAAG
CATGACTTCATCGGCGAGTTCACCAGCACTTTCCAGGAGATGCAGGAAGGGACGGCAAAC
CCTGGGCAGGAGATGCAGTGGGACTGTATCAACCCCAAGTATCGGGACAAGAAGAAGAAT
TACAAGAGCTCAGGGACGGTAGTGCTGGCCCAGTGCACGGTGGAGAAGGTGCACACCTTC
CTGGATTACATCATGGGTGGCTGCCAGATCAGCTTCACGGTGGCCATTGACTTCACTGCC
TCCAATGGGGACCCGAGGAGCAGCCAGTCCCTGCACTGCCTCAGTCCCCGACAGCCCAAC
CACTACCTGCAGGCCCTGCGTGCAGTGGGAGGCATCTGCCAGGACTATGACAGTGATAAG
CGGTTCCCAGCTTTTGGCTTTGGGGCTCGAATCCCCCCCAACTTCGAGGTGTCCCATGAC
TTTGCTATCAACTTTGACCCGGAAAATCCTGAATGTGAAGAGATCTCAGGGGTCATCGCC
TCCTACCGTCGTTGCCTGCCCCAGATCCAGCTCTACGGCCCCACCAATGTGGCCCCCATC
ATCAACCGTGTGGCTGAGCCGGCCCAGCGGGAGCAGAGCACCGGCCAAGCCACGAAGTAC
TCGGTGCTGCTGGTGCTCACTGACGGTGTGGTGAGCGACATGGCTGAGACTCGCACTGCT
ATCGTGCGTGCCTCCCGCCTGCCCATGTCCATCATCATCGTAGGCGTGGGCAATGCTGAC
TTCTCTGACATGCGGCTGCTGGATGGCGACGACGGCCCCTTGCGCTGCCCCCGAGGGGTG
CCTGCAGCCCGAGACATTGTCCAGTTCGTGCCCTTCCGAGACTTCAAGGATGCTGCCCCC
TCTGCACTCGCCAAGTGTGTCCTGGCTGAGGTGCCACGGCAGGTGGTGGAGTACTACGCC
AGCCAGGGCATCAGCCCTGGGGCTCCCAGGCCCTGCACACTGGCTACGACTCCCAGCCCT
AGCCCGTGA
|
| Enzyme 45 GenBank Gene ID |
AK125195  |
| Enzyme 45 GeneCard ID |
CPNE6  |
| Enzyme 45 GenAtlas ID |
CPNE6  |
| Enzyme 45 HGNC ID |
HGNC:2319  |
| Enzyme 45 Chromosome Location |
1 |
| Enzyme 45 Locus |
14q11.2 |
| Enzyme 45 SNPs |
SNPJam Report  |
| Enzyme 45 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
]
- Venter JC, Adams MD, Myers EW, Li PW, Mural RJ, Sutton GG, Smith HO, Yandell M, Evans CA, Holt RA, Gocayne JD, Amanatides P, Ballew RM, Huson DH, Wortman JR, Zhang Q, Kodira CD, Zheng XH, Chen L, Skupski M, Subramanian G, Thomas PD, Zhang J, Gabor Miklos GL, Nelson C, Broder S, Clark AG, Nadeau J, McKusick VA, Zinder N, Levine AJ, Roberts RJ, Simon M, Slayman C, Hunkapiller M, Bolanos R, Delcher A, Dew I, Fasulo D, Flanigan M, Florea L, Halpern A, Hannenhalli S, Kravitz S, Levy S, Mobarry C, Reinert K, Remington K, Abu-Threideh J, Beasley E, Biddick K, Bonazzi V, Brandon R, Cargill M, Chandramouliswaran I, Charlab R, Chaturvedi K, Deng Z, Di Francesco V, Dunn P, Eilbeck K, Evangelista C, Gabrielian AE, Gan W, Ge W, Gong F, Gu Z, Guan P, Heiman TJ, Higgins ME, Ji RR, Ke Z, Ketchum KA, Lai Z, Lei Y, Li Z, Li J, Liang Y, Lin X, Lu F, Merkulov GV, Milshina N, Moore HM, Naik AK, Narayan VA, Neelam B, Nusskern D, Rusch DB, Salzberg S, Shao W, Shue B, Sun J, Wang Z, Wang A, Wang X, Wang J, Wei M, Wides R, Xiao C, Yan C, Yao A, Ye J, Zhan M, Zhang W, Zhang H, Zhao Q, Zheng L, Zhong F, Zhong W, Zhu S, Zhao S, Gilbert D, Baumhueter S, Spier G, Carter C, Cravchik A, Woodage T, Ali F, An H, Awe A, Baldwin D, Baden H, Barnstead M, Barrow I, Beeson K, Busam D, Carver A, Center A, Cheng ML, Curry L, Danaher S, Davenport L, Desilets R, Dietz S, Dodson K, Doup L, Ferriera S, Garg N, Gluecksmann A, Hart B, Haynes J, Haynes C, Heiner C, Hladun S, Hostin D, Houck J, Howland T, Ibegwam C, Johnson J, Kalush F, Kline L, Koduru S, Love A, Mann F, May D, McCawley S, McIntosh T, McMullen I, Moy M, Moy L, Murphy B, Nelson K, Pfannkoch C, Pratts E, Puri V, Qureshi H, Reardon M, Rodriguez R, Rogers YH, Romblad D, Ruhfel B, Scott R, Sitter C, Smallwood M, Stewart E, Strong R, Suh E, Thomas R, Tint NN, Tse S, Vech C, Wang G, Wetter J, Williams S, Williams M, Windsor S, Winn-Deen E, Wolfe K, Zaveri J, Zaveri K, Abril JF, Guigo R, Campbell MJ, Sjolander KV, Karlak B, Kejariwal A, Mi H, Lazareva B, Hatton T, Narechania A, Diemer K, Muruganujan A, Guo N, Sato S, Bafna V, Istrail S, Lippert R, Schwartz R, Walenz B, Yooseph S, Allen D, Basu A, Baxendale J, Blick L, Caminha M, Carnes-Stine J, Caulk P, Chiang YH, Coyne M, Dahlke C, Mays A, Dombroski M, Donnelly M, Ely D, Esparham S, Fosler C, Gire H, Glanowski S, Glasser K, Glodek A, Gorokhov M, Graham K, Gropman B, Harris M, Heil J, Henderson S, Hoover J, Jennings D, Jordan C, Jordan J, Kasha J, Kagan L, Kraft C, Levitsky A, Lewis M, Liu X, Lopez J, Ma D, Majoros W, McDaniel J, Murphy S, Newman M, Nguyen T, Nguyen N, Nodell M, Pan S, Peck J, Peterson M, Rowe W, Sanders R, Scott J, Simpson M, Smith T, Sprague A, Stockwell T, Turner R, Venter E, Wang M, Wen M, Wu D, Wu M, Xia A, Zandieh A, Zhu X: The sequence of the human genome. Science. 2001 Feb 16;291(5507):1304-51. [PubMed
]
|
| Enzyme 45 Metabolite References |
Not Available |
|
Enzyme 46
[top]
|
| Enzyme 46 ID |
21034 |
| Enzyme 46 Name |
Lactadherin |
| Enzyme 46 Synonyms |
- Breast epithelial antigen BA46
- HMFG
- MFGM
- Milk fat globule-EGF factor 8
- MFG-E8
- SED1
- Lactadherin short form
- Medin
|
| Enzyme 46 Gene Name |
MFGE8 |
| Enzyme 46 Protein Sequence |
>Lactadherin
MPRPRLLAALCGALLCAPSLLVALDICSKNPCHNGGLCEEISQEVRGDVFPSYTCTCLKG
YAGNHCETKCVEPLGMENGNIANSQIAASSVRVTFLGLQHWVPELARLNRAGMVNAWTPS
SNDDNPWIQVNLLRRMWVTGVVTQGASRLASHEYLKAFKVAYSLNGHEFDFIHDVNKKHK
EFVGNWNKNAVHVNLFETPVEAQYVRLYPTSCHTACTLRFELLGCELNGCANPLGLKNNS
IPDKQITASSSYKTWGLHLFSWNPSYARLDKQGNFNAWVAGSYGNDQWLQVDLGSSKEVT
GIITQGARNFGSVQFVASYKVAYSNDSANWTEYQDPRTGSSKIFPGNWDNHSHKKNLFET
PILARYVRILPVAWHNRIALRLELLGC
|
| Enzyme 46 Number of Residues |
387 |
| Enzyme 46 Molecular Weight |
43122.7 |
| Enzyme 46 Theoretical pI |
8.21 |
| Enzyme 46 GO Classification |
| Function |
| — |
| Process |
- cell adhesion
- cellular process
|
| Component |
| — |
|
| Enzyme 46 General Function |
Involved in cell adhesion |
| Enzyme 46 Specific Function |
Medin is the main constituent of aortic medial amyloid |
| Enzyme 46 Pathways |
Not Available |
| Enzyme 46 Reactions |
Not Available |
| Enzyme 46 Pfam Domain Function |
|
| Enzyme 46 Signals |
|
| Enzyme 46 Transmembrane Regions |
|
| Enzyme 46 Essentiality |
Not Available |
| Enzyme 46 GenBank ID Protein |
62897029  |
| Enzyme 46 UniProtKB/Swiss-Prot ID |
Q08431  |
| Enzyme 46 UniProtKB/Swiss-Prot Entry Name |
MFGM_HUMAN  |
| Enzyme 46 PDB ID |
Not Available |
| Enzyme 46 Cellular Location |
Not Available |
| Enzyme 46 Gene Sequence |
>1164 bp
ATGCCGCGCCCCCGCCTGCTGGCCGCGCTGTGCGGCGCGCTGCTCTGCGCCCCCAGCCTC
CTCGTCGCCCTGGATATCTGTTCCAAAAACCCCTGCCACAACGGTGGTTTATGCGAGGAG
ATTTCCCAAGAAGTGCGAGGAGATGTCTTCCCCTCGTACACCTGCACGTGCCTTAAGGGC
TACGCGGGCAACCACTGTGAGACGAAATGTGTCGAGCCACTGGGCCTGGAGAATGGGAAC
ATTGCCAACTCACAGATCGCCGCCTCGTCTGTGCGTGTGACCTTCTTGGGTTTGCAGCAT
TGGGTCCCGGAGCTGGCCCGCCTGAACCGCGCAGGCATGGTCAATGCCTGGACACCCAGC
AGCAATGACGATAACCCCTGGATCCAGGTGAACCTGCTGCGGAGGATGTGGGTAACAGGT
GTGGTGACGCAGGGTGCCAGCCGCTTGGCCAGTCATGAGTACCTGAAGGCCTTCAAGGTG
GCCTACAGCCTTAATGGACACGAATTCGATTTCATCCATGATGTTAATAAAAAACACAAG
GAGTTTGTGGGTAACTGGAACAAAAACGCGGTGCATGTCAACCTGTTTGAGACCCCTGTG
GAGGCTCAGTACGTGAGATTGTACCCCACGAGCTGCCACACGGCCTGCACTCTGCGCTTT
GAGCTACTGGGCTGTGAGCTGAACGGATGCGCCAATCCCCTGGGCCTGAAGAATAACAGC
ATCCCTGACAAGCAGATCACGGCCTCCAGCAGCTACAAGACCTGGGGCTTGCATCTCTTC
AGCTGGAACCCCTCCTATGCACGGCTGGACAAGCAGGGCAACTTCAACGCCTGGGTTGCG
GGGAGCTACGGTAACGATCAGTGGCTGCAGGTGGACCTGGGCTCCTCGAAGGAGGTGACA
GGCATCATCACCCAGGGGGCCCGTAACTTTGGCTCTGTCCAGTTTGTGGCATCCTACAAG
GTTGCCTACAGTAATGACAGTGCGAACTGGACTGAGTACCAGGACCCCAGGACTGGCAGC
AGTAAGATCTTCCCTGGCAACTGGGACAACCACTCCCACAAGAAGAACTTGTTTGAGACG
CCCATCCTGGCTCGCTATGTGCGCATCCTGCCTGTAGCCTGGCACAACCGCATCGCCCTG
CGCCTGGAGCTGCTGGGCTGTTAG
|
| Enzyme 46 GenBank Gene ID |
AK222735  |
| Enzyme 46 GeneCard ID |
MFGE8  |
| Enzyme 46 GenAtlas ID |
MFGE8  |
| Enzyme 46 HGNC ID |
HGNC:7036  |
| Enzyme 46 Chromosome Location |
1 |
| Enzyme 46 Locus |
15q25 |
| Enzyme 46 SNPs |
SNPJam Report  |
| Enzyme 46 General References |
- Couto JR, Taylor MR, Godwin SG, Ceriani RL, Peterson JA: Cloning and sequence analysis of human breast epithelial antigen BA46 reveals an RGD cell adhesion sequence presented on an epidermal growth factor-like domain. DNA Cell Biol. 1996 Apr;15(4):281-6. [PubMed
]
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed
]
- 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
]
- Larocca D, Peterson JA, Urrea R, Kuniyoshi J, Bistrain AM, Ceriani RL: A Mr 46,000 human milk fat globule protein that is highly expressed in human breast tumors contains factor VIII-like domains. Cancer Res. 1991 Sep 15;51(18):4994-8. [PubMed
]
- Giuffrida MG, Cavaletto M, Giunta C, Conti A, Godovac-Zimmermann J: Isolation and characterization of full and truncated forms of human breast carcinoma protein BA46 from human milk fat globule membranes. J Protein Chem. 1998 Feb;17(2):143-8. [PubMed
]
- Haggqvist B, Naslund J, Sletten K, Westermark GT, Mucchiano G, Tjernberg LO, Nordstedt C, Engstrom U, Westermark P: Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid. Proc Natl Acad Sci U S A. 1999 Jul 20;96(15):8669-74. [PubMed
]
- Taylor MR, Couto JR, Scallan CD, Ceriani RL, Peterson JA: Lactadherin (formerly BA46), a membrane-associated glycoprotein expressed in human milk and breast carcinomas, promotes Arg-Gly-Asp (RGD)-dependent cell adhesion. DNA Cell Biol. 1997 Jul;16(7):861-9. [PubMed
]
- Picariello G, Ferranti P, Mamone G, Roepstorff P, Addeo F: Identification of N-linked glycoproteins in human milk by hydrophilic interaction liquid chromatography and mass spectrometry. Proteomics. 2008 Sep;8(18):3833-47. [PubMed
]
- Raymond A, Ensslin MA, Shur BD: SED1/MFG-E8: a bi-motif protein that orchestrates diverse cellular interactions. J Cell Biochem. 2009 Apr 15;106(6):957-66. [PubMed
]
|
| Enzyme 46 Metabolite References |
Not Available |