|
Enzyme 1
[top]
|
| Enzyme 1 ID |
5385 |
| Enzyme 1 Name |
Squalene monooxygenase |
| Enzyme 1 Synonyms |
- Squalene epoxidase
- SE
|
| Enzyme 1 Gene Name |
SQLE |
| Enzyme 1 Protein Sequence |
>Squalene monooxygenase
MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSG
SQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGTAACTSTSS
QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGL
GDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAE
PNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKV
SVSSHFVGFLMKNAPQFKANHAELILANPSPVLIYQISSSETRVLVDIRGEMPRNLREYM
VEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG
MTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKTSHSFVVNILAQALYELFSAT
DDSLHQLRKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAVYFCFKSEPW
ITKPRALLSSGAVLYKACSVIFPLIYSEMKYMVH
|
| Enzyme 1 Number of Residues |
574 |
| Enzyme 1 Molecular Weight |
63922.5 |
| Enzyme 1 Theoretical pI |
8.87 |
| Enzyme 1 GO Classification |
| Function |
- FAD or FADH2 binding
- adenyl nucleotide binding
- binding
- catalytic activity
- monooxygenase activity
- nucleoside binding
- oxidoreductase activity
- purine nucleoside binding
- squalene monooxygenase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 1 General Function |
Involved in oxidoreductase activity |
| Enzyme 1 Specific Function |
Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway |
| Enzyme 1 Pathways |
|
| Enzyme 1 Reactions |
- squalene + AH2 + O2 = (S)-squalene-2,3-epoxide + A + H2O [RN:R02873]
|
| Enzyme 1 Pfam Domain Function |
|
| Enzyme 1 Signals |
|
| Enzyme 1 Transmembrane Regions |
- 20-40
61-81
123-143
546-566
|
| Enzyme 1 Essentiality |
Not Available |
| Enzyme 1 GenBank ID Protein |
62865635  |
| Enzyme 1 UniProtKB/Swiss-Prot ID |
Q14534  |
| Enzyme 1 UniProtKB/Swiss-Prot Entry Name |
ERG1_HUMAN  |
| Enzyme 1 PDB ID |
Not Available |
| Enzyme 1 Cellular Location |
Not Available |
| Enzyme 1 Gene Sequence |
>1725 bp
ATGTGGACTTTTCTGGGCATTGCCACTTTCACCTATTTTTATAAGAAGTTCGGGGACTTC
ATCACTTTGGCCAACAGGGAGGTCCTGTTGTGCGTGCTGGTGTTCCTCTCGCTGGGCCTG
GTGCTCTCCTACCGCTGTCGCCACCGAAACGGGGGTCTCCTCGGGCGCCAGCAGAGCGGC
TCCCAGTTCGCCCTCTTCTCGGATATTCTCTCAGGCCTGCCTTTCATTGGCTTCTTCTGG
GCCAAATCCCCCCCTGAATCAGAAAATAAGGAGCAGCTCGAGGCCAGGAGGCGCAGAAAA
GGAACCAATATTTCAGAAACAAGCTTAATAGGAACAGCTGCCTGTACATCAACATCTTCT
CAGAATGACCCAGAAGTTATCATCGTGGGAGCTGGCGTGCTTGGCTCTGCTTTGGCAGCT
GTGCTTTCCAGAGATGGAAGAAAGGTGACAGTCATTGAGAGAGACTTAAAAGAGCCTGAC
AGAATAGTTGGAGAATTCCTGCAGCCGGGTGGTTATCATGTTCTCAAAGACCTTGGTCTT
GGAGATACAGTGGAAGGTCTTGATGCCCAGGTTGTAAATGGTTACATGATTCATGATCAG
GAAAGCAAATCAGAGGTTCAGATTCCTTACCCTCTGTCAGAAAACAATCAAGTGCAGAGT
GGAAGAGCTTTCCATCACGGAAGATTCATCATGAGTCTCCGGAAAGCAGCTATGGCAGAG
CCCAATGCAAAGTTTATTGAAGGTGTTGTGTTACAGTTATTAGAGGAAGATGATGTTGTG
ATGGGAGTTCAGTACAAGGATAAAGAGACTGGAGATATCAAGGAACTCCATGCTCCACTG
ACTGTTGTTGCAGATGGGCTTTTCTCCAAGTTCAGGAAAAGCCTGGTCTCCAATAAAGTT
TCTGTATCATCTCATTTTGTTGGCTTTCTTATGAAGAATGCACCACAGTTTAAAGCAAAT
CATGCTGAACTTATTTTAGCTAACCCGAGTCCAGTTCTCATCTACCAGATTTCATCCAGT
GAAACTCGAGTACTTGTTGACATTAGAGGAGAAATGCCAAGGAATTTAAGAGAATACATG
GTTGAAAAAATTTACCCACAAATACCTGATCACCTGAAAGAACCATTCTTAGAAGCCACT
GACAATTCTCATCTGAGGTCCATGCCAGCAAGCTTCCTTCCTCCTTCATCAGTGAAGAAA
CGAGGTGTTCTTCTTTTGGGAGACGCATATAATATGAGGCATCCACTTACTGGTGGAGGA
ATGACTGTTGCTTTTAAAGATATAAAACTATGGAGAAAACTGCTAAAGGGTATCCCTGAC
CTTTATGATGATGCAGCTATTTTCGAGGCCAAAAAATCATTTTACTGGGCAAGAAAAACA
TCTCATTCCTTTGTCGTGAATATCCTTGCTCAGGCTCTTTATGAATTATTTTCTGCCACA
GATGATTCCCTGCATCAACTAAGAAAAGCCTGTTTTCTTTATTTCAAACTTGGTGGCGAA
TGTGTTGCGGGTCCTGTTGGGCTGCTTTCTGTATTGTCTCCTAACCCTCTAGTTTTAATT
GGACACTTCTTTGCTGTTGCAATCTATGCCGTGTATTTTTGCTTTAAGTCAGAACCTTGG
ATTACAAAACCTCGAGCCCTTCTCAGTAGTGGTGCTGTATTGTACAAAGCGTGTTCTGTA
ATATTTCCTCTAATTTACTCAGAAATGAAGTATATGGTTCATTAA
|
| Enzyme 1 GenBank Gene ID |
NM_003129.3  |
| Enzyme 1 GeneCard ID |
SQLE  |
| Enzyme 1 GenAtlas ID |
SQLE  |
| Enzyme 1 HGNC ID |
HGNC:11279  |
| Enzyme 1 Chromosome Location |
8 |
| Enzyme 1 Locus |
8q24.1 |
| Enzyme 1 SNPs |
SNPJam Report  |
| Enzyme 1 General References |
- Nagai M, Sakakibara J, Wakui K, Fukushima Y, Igarashi S, Tsuji S, Arakawa M, Ono T: Localization of the squalene epoxidase gene (SQLE) to human chromosome region 8q24.1. Genomics. 1997 Aug 15;44(1):141-3. [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
]
- Nusbaum C, Mikkelsen TS, Zody MC, Asakawa S, Taudien S, Garber M, Kodira CD, Schueler MG, Shimizu A, Whittaker CA, Chang JL, Cuomo CA, Dewar K, FitzGerald MG, Yang X, Allen NR, Anderson S, Asakawa T, Blechschmidt K, Bloom T, Borowsky ML, Butler J, Cook A, Corum B, DeArellano K, DeCaprio D, Dooley KT, Dorris L 3rd, Engels R, Glockner G, Hafez N, Hagopian DS, Hall JL, Ishikawa SK, Jaffe DB, Kamat A, Kudoh J, Lehmann R, Lokitsang T, Macdonald P, Major JE, Matthews CD, Mauceli E, Menzel U, Mihalev AH, Minoshima S, Murayama Y, Naylor JW, Nicol R, Nguyen C, O'Leary SB, O'Neill K, Parker SC, Polley A, Raymond CK, Reichwald K, Rodriguez J, Sasaki T, Schilhabel M, Siddiqui R, Smith CL, Sneddon TP, Talamas JA, Tenzin P, Topham K, Venkataraman V, Wen G, Yamazaki S, Young SK, Zeng Q, Zimmer AR, Rosenthal A, Birren BW, Platzer M, Shimizu N, Lander ES: DNA sequence and analysis of human chromosome 8. Nature. 2006 Jan 19;439(7074):331-5. [PubMed
]
- Nakamura Y, Sakakibara J, Izumi T, Shibata A, Ono T: Transcriptional regulation of squalene epoxidase by sterols and inhibitors in HeLa cells. J Biol Chem. 1996 Apr 5;271(14):8053-6. [PubMed
]
|
| Enzyme 1 Metabolite References |
Not Available |
|
Enzyme 2
[top]
|
| Enzyme 2 ID |
5492 |
| Enzyme 2 Name |
Squalene synthase |
| Enzyme 2 Synonyms |
- SQS
- SS
- FPP:FPP farnesyltransferase
- Farnesyl-diphosphate farnesyltransferase
|
| Enzyme 2 Gene Name |
FDFT1 |
| Enzyme 2 Protein Sequence |
>Squalene synthase
MEFVKCLGHPEEFYNLVRFRIGGKRKVMPKMDQDSLSSSLKTCYKYLNQTSRSFAAVIQA
LDGEMRNAVCIFYLVLRALDTLEDDMTISVEKKVPLLHNFHSFLYQPDWRFMESKEKDRQ
VLEDFPTISLEFRNLAEKYQTVIADICRRMGIGMAEFLDKHVTSEQEWDKYCHYVAGLVG
IGLSRLFSASEFEDPLVGEDTERANSMGLFLQKTNIIRDYLEDQQGGREFWPQEVWSRYV
KKLGDFAKPENIDLAVQCLNELITNALHHIPDVITYLSRLRNQSVFNFCAIPQVMAIATL
AACYNNQQVFKGAVKIRKGQAVTLMMDATNMPAVKAIIYQYMEEIYHRIPDSDPSSSKTR
QIISTIRTQNLPNCQLISRSHYSPIYLSFVMLLAALSWQYLTTLSQVTEDYVQTGEH
|
| Enzyme 2 Number of Residues |
417 |
| Enzyme 2 Molecular Weight |
48114.9 |
| Enzyme 2 Theoretical pI |
6.51 |
| Enzyme 2 GO Classification |
| Function |
- catalytic activity
- farnesyl-diphosphate farnesyltransferase activity
- farnesyltranstransferase activity
- prenyltransferase activity
- transferase activity
- transferase activity, transferring alkyl or aryl (other than methyl) groups
|
| Process |
- biosynthetic process
- lipid biosynthetic process
- lipid metabolic process
- metabolic process
- primary metabolic process
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 2 General Function |
Involved in transferase activity |
| Enzyme 2 Specific Function |
2 farnesyl diphosphate = diphosphate + presqualene diphosphate |
| Enzyme 2 Pathways |
|
| Enzyme 2 Reactions |
- (1) (1a) 2 farnesyl diphosphate = diphosphate + presqualene diphosphate [RN:R00702]
- (2) (1b) presqualene diphosphate + NAD(P)H + H+ = squalene + diphosphate + NAD(P)+ [RN:R02872]
|
| Enzyme 2 Pfam Domain Function |
|
| Enzyme 2 Signals |
|
| Enzyme 2 Transmembrane Regions |
|
| Enzyme 2 Essentiality |
Not Available |
| Enzyme 2 GenBank ID Protein |
Not Available |
| Enzyme 2 UniProtKB/Swiss-Prot ID |
P37268  |
| Enzyme 2 UniProtKB/Swiss-Prot Entry Name |
FDFT_HUMAN  |
| Enzyme 2 PDB ID |
1EZF  |
| Enzyme 2 PDB File |
Show |
| Enzyme 2 3D Structure |
|
| Enzyme 2 Cellular Location |
Not Available |
| Enzyme 2 Gene Sequence |
>1254 bp
ATGGAGTTCGTGAAATGCCTTGGCCACCCCGAAGAGTTCTACAACCTGGTGCGCTTCCGG
ATCGGGGGCAAGCGGAAGGTGATGCCCAAGATGGACCAGGACTCGCTCAGCAGCAGCCTG
AAAACTTGCTACAAGTATCTCAATCAGACCAGTCGCAGTTTCGCAGCTGTTATCCAGGCG
CTGGATGGGGAAATGCGCAACGCAGTGTGCATATTTTATCTGGTTCTCCGAGCTCTGGAC
ACACTGGAAGATGACATGACCATCAGTGTGGAAAAGAAGGTCCCGCTGTTACACAACTTT
CACTCTTTCCTTTACCAACCAGACTGGCGGTTCATGGAGAGCAAGGAGAAGGATCGCCAG
GTGCTGGAGGACTTCCCAACGATCTCCCTTGAGTTTAGAAATCTGGCTGAGAAATACCAA
ACAGTGATTGCCGACATTTGCCGGAGAATGGGCATTGGGATGGCAGAGTTTTTGGATAAG
CATGTGACCTCTGAACAGGAGTGGGACAAGTACTGCCACTATGTTGCTGGGCTGGTCGGA
ATTGGCCTTTCCCGTCTTTTCTCAGCCTCAGAGTTTGAAGACCCCTTAGTTGGTGAAGAT
ACAGAACGTGCCAACTCTATGGGCCTGTTTCTGCAGAAAACAAACATCATCCGTGACTAT
CTGGAAGACCAGCAAGGAGGAAGAGAGTTCTGGCCTCAAGAGGTTTGGAGCAGGTATGTT
AAGAAGTTAGGGGATTTTGCTAAGCCGGAGAATATTGACTTGGCCGTGCAGTGCCTGAAT
GAACTTATAACCAATGCACTGCACCACATCCCAGATGTCATCACCTACCTTTCGAGACTC
AGAAACCAGAGTGTGTTTAACTTCTGCGCTATTCCACAGGTGATGGCCATTGCCACTTTG
GCTGCCTGTTATAATAACCAGCAGGTGTTCAAAGGGGCAGTGAAGATTCGGAAAGGGCAA
GCAGTGACCCTGATGATGGATGCCACCAATATGCCAGCTGTCAAAGCCATCATATATCAG
TATATGGAAGAGATTTATCATAGAATCCCCGACTCAGACCCATCTTCTAGCAAAACAAGG
CAGATCATCTCCACCATCCGGACGCAGAATCTTCCCAACTGTCAGCTGATTTCCCGAAGC
CACTACTCCCCCATCTACCTGTCGTTTGTCATGCTTTTGGCTGCCCTGAGCTGGCAGTAC
CTGACCACTCTCTCCCAGGTAACAGAAGACTATGTTCAGACTGGAGAACACTGA
|
| Enzyme 2 GenBank Gene ID |
L06070  |
| Enzyme 2 GeneCard ID |
FDFT1  |
| Enzyme 2 GenAtlas ID |
FDFT1  |
| Enzyme 2 HGNC ID |
HGNC:3629  |
| Enzyme 2 Chromosome Location |
8 |
| Enzyme 2 Locus |
8p23.1-p22 |
| Enzyme 2 SNPs |
SNPJam Report  |
| Enzyme 2 General References |
- Robinson GW, Tsay YH, Kienzle BK, Smith-Monroy CA, Bishop RW: Conservation between human and fungal squalene synthetases: similarities in structure, function, and regulation. Mol Cell Biol. 1993 May;13(5):2706-17. [PubMed
]
- Jiang G, McKenzie TL, Conrad DG, Shechter I: Transcriptional regulation by lovastatin and 25-hydroxycholesterol in HepG2 cells and molecular cloning and expression of the cDNA for the human hepatic squalene synthase. J Biol Chem. 1993 Jun 15;268(17):12818-24. [PubMed
]
- Summers C, Karst F, Charles AD: Cloning, expression and characterisation of the cDNA encoding human hepatic squalene synthase, and its relationship to phytoene synthase. Gene. 1993 Dec 22;136(1-2Che):185-92. [PubMed
]
- Soltis DA, McMahon G, Caplan SL, Dudas DA, Chamberlin HA, Vattay A, Dottavio D, Rucker ML, Engstrom RG, Cornell-Kennon SA, et al.: Expression, purification, and characterization of the human squalene synthase: use of yeast and baculoviral systems. Arch Biochem Biophys. 1995 Feb 1;316(2):713-23. [PubMed
]
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed
]
- Pandit J, Danley DE, Schulte GK, Mazzalupo S, Pauly TA, Hayward CM, Hamanaka ES, Thompson JF, Harwood HJ Jr: Crystal structure of human squalene synthase. A key enzyme in cholesterol biosynthesis. J Biol Chem. 2000 Sep 29;275(39):30610-7. [PubMed
]
- Do R, Pare G, Montpetit A, Hudson TJ, Gaudet D, Engert JC: K45R variant of squalene synthase increases total cholesterol levels in two study samples from a French Canadian population. Hum Mutat. 2008 May;29(5):689-94. [PubMed
]
|
| Enzyme 2 Metabolite References |
Not Available |
|
Enzyme 3
[top]
|
| Enzyme 3 ID |
7051 |
| Enzyme 3 Name |
Serine palmitoyltransferase 1 |
| Enzyme 3 Synonyms |
- Long chain base biosynthesis protein 1
- LCB 1
- Serine-palmitoyl-CoA transferase 1
- SPT 1
- SPT1
|
| Enzyme 3 Gene Name |
SPTLC1 |
| Enzyme 3 Protein Sequence |
>Serine palmitoyltransferase 1
MATATEQWVLVEMVQALYEAPAYHLILEGILILWIIRLLFSKTYKLQERSDLTVKEKEEL
IEEWQPEPLVPPVPKDHPALNYNIVSGPPSHKTVVNGKECINFASFNFLGLLDNPRVKAA
ALASLKKYGVGTCGPRGFYGTFDVHLDLEDRLAKFMKTEEAIIYSYGFATIASAIPAYSK
RGDIVFVDRAACFAIQKGLQASRSDIKLFKHNDMADLERLLKEQEIEDQKNPRKARVTRR
FIVVEGLYMNTGTICPLPELVKLKYKYKARIFLEESLSFGVLGEHGRGVTEHYGINIDDI
DLISANMENALASIGGFCCGRSFVIDHQRLSGQGYCFSASLPPLLAAAAIEALNIMEENP
GIFAVLKEKCGQIHKALQGISGLKVVGESLSPAFHLQLEESTGSREQDVRLLQEIVDQCM
NRSIALTQARYLEKEEKCLPPPSIRVVVTVEQTEEELERAASTIKEVAQAVLL
|
| Enzyme 3 Number of Residues |
473 |
| Enzyme 3 Molecular Weight |
52743.4 |
| Enzyme 3 Theoretical pI |
5.87 |
| Enzyme 3 GO Classification |
| Function |
- binding
- catalytic activity
- cofactor binding
- pyridoxal phosphate binding
- transferase activity
- transferase activity, transferring nitrogenous groups
|
| Process |
- biosynthetic process
- metabolic process
|
| Component |
| — |
|
| Enzyme 3 General Function |
Involved in transferase activity, transferring nitrogenous groups |
| Enzyme 3 Specific Function |
Serine palmitoyltransferase (SPT). The heterodimer formed with LCB2 (SPTLC2 or SPTLC3) constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2- SSSPTA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SSSPTA isozyme uses both C14-CoA and C16- CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SSSPTB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SSSPTB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference |
| Enzyme 3 Pathways |
Not Available |
| Enzyme 3 Reactions |
- palmitoyl-CoA + L-serine = CoA + 3-dehydro-D-sphinganine + CO2 [RN:R01281]
|
| Enzyme 3 Pfam Domain Function |
|
| Enzyme 3 Signals |
|
| Enzyme 3 Transmembrane Regions |
|
| Enzyme 3 Essentiality |
Not Available |
| Enzyme 3 GenBank ID Protein |
2564247  |
| Enzyme 3 UniProtKB/Swiss-Prot ID |
O15269  |
| Enzyme 3 UniProtKB/Swiss-Prot Entry Name |
SPTC1_HUMAN  |
| Enzyme 3 PDB ID |
Not Available |
| Enzyme 3 Cellular Location |
Not Available |
| Enzyme 3 Gene Sequence |
>1422 bp
ATGGCGACCGCCACGGAGCAGTGGGTTCTGGTGGAGATGGTACAGGCGCTTTACGAGGCT
CCTGCTTACCATCTTATTTTGGAAGGGATTCTGATCCTCTGGATAATCAGACTTCTTTTC
TCTAAGACTTACAAATTACAAGAACGATCTGATCTTACAGTCAAGGAAAAAGAAGAACTG
ATTGAAGAGTGGCAACCAGAACCTCTTGTTCCTCCTGTCCCAAAAGACCATCCTGCTCTC
AACTACAACATCGTTTCAGGCCCTCCAAGCCACAAAACTGTGGTGAATGGAAAAGAATGT
ATAAACTTCGCCTCATTTAATTTTCTTGGATTGTTGGATAACCCTAGGGTTAAGGCAGCA
GCTTTAGCATCTCTAAAGAAGTATGGCGTGGGGACTTGTGGACCCAGAGGATTTTATGGC
ACATTTGATGTTCATTTGGATTTGGAAGACCGCCTGGCAAAATTTATGAAGACAGAAGAA
GCCATTATATACTCATATGGATTTGCCACCATAGCCAGTGCTATTCCTGCTTACTCTAAA
AGAGGGGACATTGTTTTTGTAGATAGAGCTGCCTGCTTTGCTATTCAGAAAGGATTACAG
GCATCCCGTAGTGACATTAAGTTATTTAAGCATAATGACATGGCTGACCTCGAGCGACTA
CTAAAAGAACAAGAGATCGAAGATCAAAAGAATCCTCGCAAGGCTCGTGTAACTCGGCGT
TTCATTGTAGTAGAAGGATTGTATATGAATACTGGAACTATTTGTCCTCTTCCAGAATTG
GTTAAGTTAAAATACAAATACAAAGCAAGAATCTTCCTGGAGGAAAGCCTTTCATTTGGA
GTCCTAGGAGAGCATGGCCGAGGAGTCACTGAACACTATGGAATCAATATTGATGATATT
GATCTTATCAGTGCCAACATGGAGAATGCACTTGCTTCTATTGGAGGTTTCTGCTGTGGC
AGGTCTTTTGTAATTGACCATCAGCGACTTTCCGGCCAGGGATACTGCTTTTCAGCTTCG
TTACCTCCCCTGTTAGCTGCTGCAGCAATTGAGGCCCTCAACATCATGGAAGAGAATCCA
GGTATTTTTGCAGTGTTGAAGGAAAAGTGCGGACAAATTCATAAAGCTTTACAAGGCATT
TCTGGATTAAAAGTGGTGGGGGAGTCCCTTTCTCCAGCCTTTCACCTACAACTGGAAGAG
AGCACTGGGTCTCGCGAGCAAGATGTCAGACTGCTTCAGGAAATTGTAGATCAATGCATG
AACAGAAGTATTGCATTAACTCAGGCGCGCTACTTGGAGAAAGAAGAGAAGTGTCTCCCT
CCTCCCAGCATTCGGGTTGTGGTCACGGTGGAACAAACAGAGGAAGAACTGGAGAGAGCT
GCGTCCACCATCAAGGAGGTAGCCCAGGCCGTCCTGCTCTAG
|
| Enzyme 3 GenBank Gene ID |
Y08685  |
| Enzyme 3 GeneCard ID |
SPTLC1  |
| Enzyme 3 GenAtlas ID |
SPTLC1  |
| Enzyme 3 HGNC ID |
HGNC:11277  |
| Enzyme 3 Chromosome Location |
9 |
| Enzyme 3 Locus |
9q22.2 |
| Enzyme 3 SNPs |
SNPJam Report  |
| Enzyme 3 General References |
- Weiss B, Stoffel W: Human and murine serine-palmitoyl-CoA transferase--cloning, expression and characterization of the key enzyme in sphingolipid synthesis. Eur J Biochem. 1997 Oct 1;249(1):239-47. [PubMed
]
- Dawkins JL, Hulme DJ, Brahmbhatt SB, Auer-Grumbach M, Nicholson GA: Mutations in SPTLC1, encoding serine palmitoyltransferase, long chain base subunit-1, cause hereditary sensory neuropathy type I. Nat Genet. 2001 Mar;27(3):309-12. [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
]
- Hornemann T, Richard S, Rutti MF, Wei Y, von Eckardstein A: Cloning and initial characterization of a new subunit for mammalian serine-palmitoyltransferase. J Biol Chem. 2006 Dec 8;281(49):37275-81. Epub 2006 Oct 4. [PubMed
]
- Han G, Gupta SD, Gable K, Niranjanakumari S, Moitra P, Eichler F, Brown RH Jr, Harmon JM, Dunn TM: Identification of small subunits of mammalian serine palmitoyltransferase that confer distinct acyl-CoA substrate specificities. Proc Natl Acad Sci U S A. 2009 May 19;106(20):8186-91. Epub 2009 May 5. [PubMed
]
- Breslow DK, Collins SR, Bodenmiller B, Aebersold R, Simons K, Shevchenko A, Ejsing CS, Weissman JS: Orm family proteins mediate sphingolipid homeostasis. Nature. 2010 Feb 25;463(7284):1048-53. [PubMed
]
- Verhoeven K, Coen K, De Vriendt E, Jacobs A, Van Gerwen V, Smouts I, Pou-Serradell A, Martin JJ, Timmerman V, De Jonghe P: SPTLC1 mutation in twin sisters with hereditary sensory neuropathy type I. Neurology. 2004 Mar 23;62(6):1001-2. [PubMed
]
- Meggouh F, Bienfait HM, Weterman MA, de Visser M, Baas F: Charcot-Marie-Tooth disease due to a de novo mutation of the RAB7 gene. Neurology. 2006 Oct 24;67(8):1476-8. [PubMed
]
- Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD, Mandelker D, Leary RJ, Ptak J, Silliman N, Szabo S, Buckhaults P, Farrell C, Meeh P, Markowitz SD, Willis J, Dawson D, Willson JK, Gazdar AF, Hartigan J, Wu L, Liu C, Parmigiani G, Park BH, Bachman KE, Papadopoulos N, Vogelstein B, Kinzler KW, Velculescu VE: The consensus coding sequences of human breast and colorectal cancers. Science. 2006 Oct 13;314(5797):268-74. Epub 2006 Sep 7. [PubMed
]
|
| Enzyme 3 Metabolite References |
Not Available |
|
Enzyme 4
[top]
|
| Enzyme 4 ID |
13008 |
| Enzyme 4 Name |
Putative uncharacterized protein DKFZp686B0215 |
| Enzyme 4 Synonyms |
Not Available |
| Enzyme 4 Gene Name |
DKFZp686B0215 |
| Enzyme 4 Protein Sequence |
>Putative uncharacterized protein DKFZp686B0215
MWTFLGIATFTYFYKKFGDFITLANREVLLCVLVFLSLGLVLSYRCRHRNGGLLGRQQSG
SQFALFSDILSGLPFIGFFWAKSPPESENKEQLEARRRRKGTNISETSLIGTAACTSTSS
QNDPEVIIVGAGVLGSALAAVLSRDGRKVTVIERDLKEPDRIVGEFLQPGGYHVLKDLGL
GDTVEGLDAQVVNGYMIHDQESKSEVQIPYPLSENNQVQSGRAFHHGRFIMSLRKAAMAE
PNAKFIEGVVLQLLEEDDVVMGVQYKDKETGDIKELHAPLTVVADGLFSKFRKSLVSNKV
SVSSHFVGFLMKNAPQFKANHAELILANPGPVLIYQISSSETRVLVDIRGEMPRNLREYM
VEKIYPQIPDHLKEPFLEATDNSHLRSMPASFLPPSSVKKRGVLLLGDAYNMRHPLTGGG
MTVAFKDIKLWRKLLKGIPDLYDDAAIFEAKKSFYWARKTSHSFVVNILAQALYELFSAT
DDSLHQLGKACFLYFKLGGECVAGPVGLLSVLSPNPLVLIGHFFAVAIYAVYFCFKSEPW
ITKPRALLSSGAVLYKACSVIFPLIYSEMKYMVH
|
| Enzyme 4 Number of Residues |
574 |
| Enzyme 4 Molecular Weight |
63793.4 |
| Enzyme 4 Theoretical pI |
8.73 |
| Enzyme 4 GO Classification |
| Function |
- FAD or FADH2 binding
- adenyl nucleotide binding
- binding
- catalytic activity
- monooxygenase activity
- nucleoside binding
- oxidoreductase activity
- purine nucleoside binding
- squalene monooxygenase activity
|
| Process |
- metabolic process
- oxidation reduction
|
| Component |
- cell part
- integral to membrane
- intrinsic to membrane
- membrane part
|
|
| Enzyme 4 General Function |
Involved in oxidoreductase activity |
| Enzyme 4 Specific Function |
Not Available |
| Enzyme 4 Pathways |
Not Available |
| Enzyme 4 Reactions |
Not Available |
| Enzyme 4 Pfam Domain Function |
|
| Enzyme 4 Signals |
|
| Enzyme 4 Transmembrane Regions |
|
| Enzyme 4 Essentiality |
Not Available |
| Enzyme 4 GenBank ID Protein |
57997512  |
| Enzyme 4 UniProtKB/Swiss-Prot ID |
Q5HYI4  |
| Enzyme 4 UniProtKB/Swiss-Prot Entry Name |
Q5HYI4_HUMAN  |
| Enzyme 4 PDB ID |
Not Available |
| Enzyme 4 Cellular Location |
Not Available |
| Enzyme 4 Gene Sequence |
>1725 bp
ATGTGGACTTTTCTGGGCATTGCCACTTTCACCTATTTTTATAAGAAGTTCGGGGACTTC
ATCACTTTGGCCAACAGGGAGGTCCTGTTGTGCGTGCTGGTGTTCCTCTCGCTGGGCCTG
GTGCTCTCCTACCGCTGTCGCCACCGAAACGGGGGTCTCCTCGGGCGCCAGCAGAGCGGC
TCCCAGTTCGCCCTCTTCTCGGATATTCTCTCAGGCCTGCCTTTCATTGGCTTCTTCTGG
GCCAAATCCCCCCCTGAATCAGAAAATAAGGAGCAGCTCGAGGCCAGGAGGCGCAGAAAA
GGAACCAATATTTCAGAAACAAGCTTAATAGGAACAGCTGCCTGTACATCAACATCTTCT
CAGAATGACCCAGAAGTTATCATCGTGGGAGCTGGCGTGCTTGGCTCTGCTTTGGCAGCT
GTGCTTTCCAGAGATGGAAGAAAGGTGACAGTCATTGAGAGAGACTTAAAAGAGCCTGAC
AGAATAGTTGGAGAATTCCTGCAGCCGGGTGGTTATCATGTTCTCAAAGACCTTGGTCTT
GGAGATACAGTGGAAGGTCTTGATGCCCAGGTTGTAAATGGTTACATGATTCATGATCAG
GAAAGCAAATCAGAGGTTCAGATTCCTTACCCTCTGTCAGAAAACAATCAAGTGCAGAGT
GGAAGAGCTTTCCATCACGGAAGATTCATCATGAGTCTCCGGAAAGCAGCTATGGCAGAG
CCCAATGCAAAGTTTATTGAAGGTGTTGTGTTACAGTTATTAGAGGAAGATGATGTTGTG
ATGGGAGTTCAGTACAAGGATAAAGAGACTGGAGATATCAAGGAACTCCATGCTCCACTG
ACTGTTGTTGCAGATGGGCTTTTCTCCAAGTTCAGGAAAAGCCTGGTCTCCAATAAAGTT
TCTGTATCATCTCATTTTGTTGGCTTTCTTATGAAGAATGCACCACAGTTTAAAGCAAAT
CATGCTGAACTTATTTTAGCTAACCCGGGTCCAGTTCTCATCTACCAGATTTCATCCAGT
GAAACTCGAGTACTTGTTGACATTAGAGGAGAAATGCCAAGGAATTTAAGAGAATACATG
GTTGAAAAAATTTACCCACAAATACCTGATCACCTGAAAGAACCATTCTTAGAAGCCACT
GACAATTCTCATCTGAGGTCCATGCCAGCAAGCTTCCTTCCTCCTTCATCAGTGAAGAAA
CGAGGTGTTCTTCTTTTGGGAGACGCATATAATATGAGGCATCCACTTACTGGTGGAGGA
ATGACTGTTGCTTTTAAAGATATAAAACTATGGAGAAAACTGCTAAAGGGTATCCCTGAC
CTTTATGATGATGCAGCTATTTTCGAGGCCAAAAAATCATTTTACTGGGCAAGAAAAACA
TCTCATTCCTTTGTCGTGAATATCCTTGCTCAGGCTCTTTATGAATTATTTTCTGCCACA
GATGATTCCCTGCATCAACTAGGAAAAGCCTGTTTTCTTTATTTCAAACTTGGTGGCGAA
TGTGTTGCGGGTCCTGTTGGGCTGCTTTCTGTATTGTCTCCTAACCCTCTAGTTTTAATT
GGACACTTCTTTGCTGTTGCAATCTATGCCGTGTATTTTTGCTTTAAGTCAGAACCTTGG
ATTACAAAACCTCGAGCCCTTCTCAGTAGTGGTGCTGTATTGTACAAAGCGTGTTCTGTA
ATATTTCCTCTAATTTACTCAGAAATGAAGTATATGGTTCATTAA
|
| Enzyme 4 GenBank Gene ID |
BX647605  |
| Enzyme 4 GeneCard ID |
DKFZp686B0215  |
| Enzyme 4 GenAtlas ID |
DKFZp686B0215  |
| Enzyme 4 HGNC ID |
HGNC:11279  |
| Enzyme 4 Chromosome Location |
Not Available |
| Enzyme 4 Locus |
Not Available |
| Enzyme 4 SNPs |
SNPJam Report  |
| Enzyme 4 General References |
Not Available |
| Enzyme 4 Metabolite References |
Not Available |
|
Enzyme 5
[top]
|
| Enzyme 5 ID |
17073 |
| Enzyme 5 Name |
SEC14-like protein 3 |
| Enzyme 5 Synonyms |
- Tocopherol-associated protein 2
|
| Enzyme 5 Gene Name |
SEC14L3 |
| Enzyme 5 Protein Sequence |
>SEC14-like protein 3
MSGRVGDLSPKQAETLAKFRENVQDVLPALPNPDDYFLLRWLRARNFDLQKSEALLRKYM
EFRKTMDIDHILDWQPPEVIQKYMPGGLCGYDRDGCPVWYDIIGPLDPKGLLFSVTKQDL
LKTKMRDCERILHECDLQTERLGKKIETIVMIFDCEGLGLKHFWKPLVEVYQEFFGLLEE
NYPETLKFMLIVKATKLFPVGYNLMKPFLSEDTRRKIIVLGNNWKEGLLKLISPEELPAQ
FGGTLTDPDGNPKCLTKINYGGEIPKSMYVRDQVKTQYEHSVQINRGSSHQVEYEILFPG
CVLRWQFSSDGADIGFGVFLKTKMGERQRAGEMTDVLPSQRYNAHMVPEDGNLTCSEAGV
YVLRFDNTYSFVHAKKVSFTVEVLLPDEGMQKYDKELTPV
|
| Enzyme 5 Number of Residues |
400 |
| Enzyme 5 Molecular Weight |
46047.8 |
| Enzyme 5 Theoretical pI |
5.97 |
| Enzyme 5 GO Classification |
| Function |
|
| Process |
- establishment of localization
- transport
|
| Component |
|
|
| Enzyme 5 General Function |
Involved in transporter activity |
| Enzyme 5 Specific Function |
Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids |
| Enzyme 5 Pathways |
Not Available |
| Enzyme 5 Reactions |
Not Available |
| Enzyme 5 Pfam Domain Function |
|
| Enzyme 5 Signals |
|
| Enzyme 5 Transmembrane Regions |
|
| Enzyme 5 Essentiality |
Not Available |
| Enzyme 5 GenBank ID Protein |
Not Available |
| Enzyme 5 UniProtKB/Swiss-Prot ID |
Q9UDX4  |
| Enzyme 5 UniProtKB/Swiss-Prot Entry Name |
S14L3_HUMAN  |
| Enzyme 5 PDB ID |
Not Available |
| Enzyme 5 Cellular Location |
Not Available |
| Enzyme 5 Gene Sequence |
>1203 bp
ATGAGCGGCCGAGTTGGAGACCTGAGCCCCAAACAGGCAGAGACCCTGGCCAAGTTCCGA
GAAAACGTCCAGGATGTGCTTCCTGCCCTGCCCAACCCTGATGATTATTTCCTTCTACGC
TGGCTCCGAGCTCGGAATTTTGACTTGCAGAAGTCGGAGGCTTTGCTCCGCAAGTACATG
GAGTTCCGGAAGACCATGGATATTGACCATATCCTTGATTGGCAGCCCCCAGAGGTGATC
CAGAAGTACATGCCTGGGGGCCTGTGTGGCTATGACCGTGATGGCTGCCCCGTGTGGTAT
GACATCATTGGGCCACTTGATCCCAAGGGGTTGCTCTTCTCAGTCACCAAGCAGGACCTG
CTCAAGACCAAGATGAGGGACTGTGAGCGCATCCTGCATGAGTGTGACCTGCAGACAGAG
AGGCTAGGGAAGAAGATTGAGACCATCGTGATGATATTTGACTGTGAGGGCCTGGGACTG
AAACACTTCTGGAAACCTCTGGTAGAAGTGTACCAGGAGTTCTTTGGCCTCCTTGAAGAG
AATTACCCAGAGACCCTGAAGTTCATGCTCATCGTGAAAGCTACCAAACTGTTCCCTGTG
GGCTACAACCTCATGAAGCCATTCCTGAGTGAGGACACTCGCAGGAAAATTATTGTGTTG
GGAAATAACTGGAAGGAAGGTTTGCTGAAACTCATCAGTCCTGAGGAACTGCCTGCCCAG
TTTGGGGGCACCCTGACTGACCCAGATGGGAACCCCAAATGTTTAACCAAGATTAACTAT
GGCGGGGAGATCCCCAAGTCCATGTACGTGCGGGACCAGGTGAAGACTCAGTACGAGCAC
TCGGTGCAGATCAACCGCGGCTCATCACACCAAGTGGAATACGAGATCCTATTTCCAGGC
TGCGTTCTCAGGTGGCAGTTCTCATCTGATGGTGCGGACATCGGCTTCGGAGTTTTCCTG
AAGACCAAGATGGGGGAGCGACAGCGGGCAGGGGAGATGACAGATGTTCTACCCAGCCAG
CGCTATAACGCCCACATGGTGCCCGAGGATGGGAACCTCACCTGCTCAGAGGCCGGCGTC
TATGTCCTACGCTTCGACAACACCTATAGCTTTGTCCACGCCAAGAAGGTCAGCTTCACA
GTGGAGGTCCTGCTCCCTGACGAGGGCATGCAGAAATATGATAAGGAGCTCACCCCTGTC
TAG
|
| Enzyme 5 GenBank Gene ID |
AY158086  |
| Enzyme 5 GeneCard ID |
SEC14L3  |
| Enzyme 5 GenAtlas ID |
SEC14L3  |
| Enzyme 5 HGNC ID |
HGNC:18655  |
| Enzyme 5 Chromosome Location |
2 |
| Enzyme 5 Locus |
22q12.2 |
| Enzyme 5 SNPs |
SNPJam Report  |
| Enzyme 5 General References |
- Kempna P, Zingg JM, Ricciarelli R, Hierl M, Saxena S, Azzi A: Cloning of novel human SEC14p-like proteins: ligand binding and functional properties. Free Radic Biol Med. 2003 Jun 1;34(11):1458-72. [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 5 Metabolite References |
Not Available |
|
Enzyme 6
[top]
|
| Enzyme 6 ID |
17074 |
| Enzyme 6 Name |
SEC14-like protein 4 |
| Enzyme 6 Synonyms |
- Tocopherol-associated protein 3
|
| Enzyme 6 Gene Name |
SEC14L4 |
| Enzyme 6 Protein Sequence |
>SEC14-like protein 4
MSSRVGDLSPQQQEALARFRENLQDLLPILPNADDYFLLRWLRARNFDLQKSEDMLRRHM
EFRKQQDLDNIVTWQPPEVIQLYDSGGLCGYDYEGCPVYFNIIGSLDPKGLLLSASKQDM
IRKRIKVCELLLHECELQTQKLGRKIEMALMVFDMEGLSLKHLWKPAVEVYQQFFSILEA
NYPETLKNLIVIRAPKLFPVAFNLVKSFMSEETRRKIVILGDNWKQELTKFISPDQLPVE
FGGTMTDPDGNPKCLTKINYGGEVPKSYYLCEQVRLQYEHTRSVGRGSSLQVENEILFPG
CVLRWQFASDGGDIGFGVFLKTKMGEQQSAREMTEVLPSQRYNAHMVPEDGSLTCLQAGV
YVLRFDNTYSRMHAKKLSYTVEVLLPDKASEETLQSLKAMRPSPTQ
|
| Enzyme 6 Number of Residues |
406 |
| Enzyme 6 Molecular Weight |
46643.4 |
| Enzyme 6 Theoretical pI |
6.52 |
| Enzyme 6 GO Classification |
| Function |
|
| Process |
- establishment of localization
- transport
|
| Component |
|
|
| Enzyme 6 General Function |
Involved in transporter activity |
| Enzyme 6 Specific Function |
Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids |
| Enzyme 6 Pathways |
Not Available |
| Enzyme 6 Reactions |
Not Available |
| Enzyme 6 Pfam Domain Function |
|
| Enzyme 6 Signals |
|
| Enzyme 6 Transmembrane Regions |
|
| Enzyme 6 Essentiality |
Not Available |
| Enzyme 6 GenBank ID Protein |
Not Available |
| Enzyme 6 UniProtKB/Swiss-Prot ID |
Q9UDX3  |
| Enzyme 6 UniProtKB/Swiss-Prot Entry Name |
S14L4_HUMAN  |
| Enzyme 6 PDB ID |
Not Available |
| Enzyme 6 Cellular Location |
Not Available |
| Enzyme 6 Gene Sequence |
>1221 bp
ATGAGCAGCCGAGTCGGGGACCTGAGCCCCCAGCAGCAGGAAGCGCTGGCCAGGTTCCGG
GAGAACCTCCAGGACCTGCTGCCCATACTGCCCAATGCTGATGACTACTTCCTCCTGCGC
TGGCTGCGAGCTCGAAACTTTGACCTGCAGAAATCCGAAGACATGCTCCGAAGGCACATG
GAGTTCCGGAAGCAACAAGACCTGGACAACATTGTCACATGGCAGCCCCCTGAGGTCATC
CAGCTGTATGACTCGGGTGGTCTTTGTGGCTACGACTACGAAGGCTGCCCTGTGTACTTC
AACATCATTGGGTCCCTCGACCCCAAGGGTCTCCTGCTGTCAGCCTCCAAGCAGGATATG
ATCCGGAAGCGCATCAAAGTCTGTGAGCTGCTGTTGCATGAGTGTGAGCTGCAAACTCAG
AAGCTGGGCAGGAAGATCGAGATGGCGCTGATGGTGTTTGACATGGAGGGGCTGAGCCTG
AAACACCTGTGGAAGCCAGCTGTGGAGGTCTACCAGCAGTTTTTTAGCATCCTGGAAGCA
AATTATCCTGAGACCCTGAAGAATTTAATTGTTATTCGAGCCCCAAAACTGTTCCCCGTG
GCCTTCAACTTGGTCAAGTCGTTCATGAGTGAGGAGACACGCAGGAAGATTGTGATTCTG
GGAGACAACTGGAAGCAGGAGCTGACAAAATTCATCAGCCCCGACCAGCTGCCTGTGGAG
TTTGGGGGGACCATGACTGACCCCGATGGCAACCCCAAGTGCCTGACCAAGATCAACTAT
GGGGGTGAGGTGCCCAAGAGCTACTACCTGTGCGAGCAGGTGAGGCTGCAGTATGAGCAC
ACGAGGTCCGTGGGCCGCGGCTCCTCCCTGCAGGTGGAGAACGAGATCCTGTTCCCGGGC
TGTGTGCTCAGGTGGCAGTTTGCTTCAGATGGTGGGGACATCGGCTTTGGGGTTTTCCTG
AAGACCAAGATGGGGGAGCAGCAGAGTGCTAGGGAGATGACGGAGGTGCTGCCCAGCCAG
CGCTACAATGCCCACATGGTGCCTGAGGATGGGAGCCTCACCTGCCTCCAGGCTGGCGTC
TATGTCCTGCGCTTCGACAACACCTACAGCCGGATGCATGCCAAGAAGCTCAGCTACACT
GTGGAGGTGCTGCTTCCCGACAAGGCCTCTGAGGAGACGCTGCAGAGTCTCAAGGCGATG
AGACCCTCCCCAACACAGTGA
|
| Enzyme 6 GenBank Gene ID |
AY158085  |
| Enzyme 6 GeneCard ID |
SEC14L4  |
| Enzyme 6 GenAtlas ID |
SEC14L4  |
| Enzyme 6 HGNC ID |
HGNC:20627  |
| Enzyme 6 Chromosome Location |
2 |
| Enzyme 6 Locus |
22q12.2 |
| Enzyme 6 SNPs |
SNPJam Report  |
| Enzyme 6 General References |
- Kempna P, Zingg JM, Ricciarelli R, Hierl M, Saxena S, Azzi A: Cloning of novel human SEC14p-like proteins: ligand binding and functional properties. Free Radic Biol Med. 2003 Jun 1;34(11):1458-72. [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
]
|
| Enzyme 6 Metabolite References |
Not Available |