Homo sapiens thromboxane A synthase 1 (platelet) (TBXAS1), transcript variant 2, mRNA.
| RefSeq Version | NM_030984.3, 261278364 |
| Length | 1919 bp |
| Structure | linear |
| Update Date | 11-MAR-2011 |
| Organism | Homo sapiens (human) |
| Definition | Homo sapiens thromboxane A synthase 1 (platelet) (TBXAS1), transcript variant 2, mRNA. |
| Product | thromboxane-A synthase isoform 2 |
| Comment | Summary: This gene encodes a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are monooxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. However, this protein is considered a member of the cytochrome P450 superfamily on the basis of sequence similarity rather than functional similarity. This endoplasmic reticulum membrane protein catalyzes the conversion of prostglandin H2 to thromboxane A2, a potent vasoconstrictor and inducer of platelet aggregation. The enzyme plays a role in several pathophysiological processes including hemostasis, cardiovascular disease, and stroke. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq]. Transcript Variant: This variant (2, also known as TXS-II) lacks an alternate exon in the 3' coding region that encodes the heme binding site, compared to transcript variant 1. The encoded isoform (2, also known as isoform TXS-II) lacks thromboxane A synthase activity, has a distinct C-terminus, and is shorter than isoform 1. CCDS Note: This CCDS representation uses the 5'-most in-frame start codon. It should be noted that this start codon is restricted to primate species (human, chimp, orangutan, rhesus and marmoset), whereas other mammalian species use a much better-conserved downstream start codon, which has a stronger Kozak signal. It is possible that the first start codon is used in human some of the time, while leaky scanning by ribosomes allows the second start codon to be used more of the time. The use of the latter would reduce the protein length by 1 aa. There is no experimental evidence indicating which start codon is preferably used in vivo. |
| RefSeq | NP_112246.2 |
| CDS | 236..1618 | Exon (1) | 1..327 | Exon (2) | 1..327 | Exon (3) | 328..421 | Exon (4) | 422..474 | Exon (5) | 475..571 | Exon (6) | 572..688 | Exon (7) | 689..777 | Exon (8) | 778..926 | Exon (9) | 927..1057 | Exon (10) | 1058..1372 | Exon (11) | 1373..1464 | Exon (12) | 1465..1602 | Exon (13) | 1603..1903 |
| Translation | MMEALGFLKLEVNGPMVTVALSVALLALLKWYSTSAFSRLEKLGLRHPKPSPFIGNLTFF
RQGFWESQMELRKLYGPLCGYYLGRRMFIVISEPDMIKQVLVENFSNFTNRMASGLEFKS
VADSVLFLRDKRWEEVRGALMSAFSPEKLNEMVPLISQACDLLLAHLKRYAESGDAFDIQ
RCYCNYTTDVVASVAFGTPVDSWQAPEDPFVKHCKRFFEFCIPRPILVLLLSFPSIMVPL
ARILPNKNRDELNGFFNKLIRNVIALRDQQAAEERRRDFLQMVLDARHSASPMGVQDFDI
VRDVFSSTGCKPNPSRQHQPSPMARPLTVDEIVGQAFIFLIAGYEIITNTLSFATYLLAT
NPDCQEKLLREVDVFKEKHMAPEFCSLEEGLPYLDMVIAETLRMYPPAFRFTREAAQDCE
VLGQRIPAGAVLEMAVGALHHDPEHWPSPETFNPERYRCS
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| Position | Chain | Variation | Link |
| 288 | + | c, t | dbSNP:61733586 |
| 305 | + | g, t | dbSNP:77579057 |
| 417 | + | a, g | dbSNP:6138 |
| 595 | + | a, c, g | dbSNP:41275018 |
| 608 | + | a, g | dbSNP:8192833 |
| complement(718) | - | t, g | dbSNP:5768 |
| 722 | + | a, c | dbSNP:6137 |
| 820 | + | c, g | dbSNP:1042561 |
| 972 | + | a, g | dbSNP:55856189 |
| 1007 | + | a, g | dbSNP:5769 |
| 1016 | + | a, g | dbSNP:5770 |
| 1118 | + | a, g | dbSNP:13306052 |
| 1184 | + | a, c | dbSNP:5771 |
| 1230 | + | c, t | dbSNP:6140 |
| 1304 | + | c, g | dbSNP:4529 |
| 1372 | + | c, t | dbSNP:13306054 |
| complement(1397) | - | t, c | dbSNP:3735354 |
| 1404 | + | g, t | dbSNP:5760 |
| 1437 | + | c, t | dbSNP:78666490 |
| 1441 | + | a, g | dbSNP:5761 |
| 1464 | + | a, g | dbSNP:13306055 |
| 1484 | + | c, g | dbSNP:4528 |
| 1492 | + | c, t | dbSNP:13306049 |
| 1508 | + | c, t | dbSNP:5762 |
| complement(1517) | - | t, c | dbSNP:2286199 |
| 1523 | + | a, g | dbSNP:4526 |
| 1540 | + | c, t | dbSNP:4527 |
| 1579 | + | c, t | dbSNP:113298427 |
| 1583 | + | a, g | dbSNP:8192868 |
| 1587 | + | a, c | dbSNP:5763 |
| 1601..1602 | + | , largedeletion | dbSNP:71761170 |
| 1607 | + | c, t | dbSNP:13306050 |
| 1798 | + | a, g | dbSNP:56091454 |
| 1799 | + | a, g | dbSNP:5765 |
| 1842 | + | a, g | dbSNP:13306051 |
| Gene Symbol | TBXAS1 |
| Gene Synonym | CYP5; CYP5A1; FLJ52771; GHOSAL; THAS; TS; TXAS; TXS |
| Chromosome | 7 |
| Locus Map | 7q34-q35 |
| All Transcripts | NM_030984 , NM_001061 , NM_001130966 , NM_001166253 , NM_001166254 |
| Title | [Association of the Pro1770Leu polymorphism in CYP5A1 gene with myocardial infarction in Uigur population of Xinjiang] . |
| Author | Wang,B.Z., Ma,Y.T., Fu,Z.Y., Xie,X., Chen,B.D., Zhang,X.L., Liu,F. and Yu,Z.X. |
| Journal | Zhonghua Yi Xue Yi Chuan Xue Za Zhi 27 (5), 535-539 (2010) |
| Title | Thromboxane synthase: structure and function of protein and gene . |
| Author | Wang,L.H. and Kulmacz,R.J. |
| Journal | Prostaglandins Other Lipid Mediat. 68-69, 409-422 (2002) |
| Title | Characterization of the complete genomic structure of human thromboxane synthase gene and functional analysis of its promoter . |
| Author | Tazawa,R., Green,E.D., Ohashi,K., Wu,K.K. and Wang,L.H. |
| Journal | Arch. Biochem. Biophys. 334 (2), 349-356 (1996) |
| Title | Genomic structure and polymorphism of the human thromboxane synthase-encoding gene . |
| Author | Baek,S.J., Lee,K.D. and Shen,R.F. |
| Journal | Gene 173 (2), 251-256 (1996) |
| Title | Alternate splicing of human thromboxane synthase mRNA . |
| Author | Wang,L.H., Tazawa,R., Lang,A.Q. and Wu,K.K. |
| Journal | Arch. Biochem. Biophys. 315 (2), 273-278 (1994) |
| Title | Characterization of the human gene (TBXAS1) encoding thromboxane synthase . |
| Author | Miyata,A., Yokoyama,C., Ihara,H., Bandoh,S., Takeda,O., Takahashi,E. and Tanabe,T. |
| Journal | Eur. J. Biochem. 224 (2), 273-279 (1994) |
| Title | Cloning and characterization of the human thromboxane synthase gene promoter . |
| Author | Lee,K.D., Baek,S.J. and Shen,R.F. |
| Journal | Biochem. Biophys. Res. Commun. 201 (1), 379-387 (1994) |
| Title | Primary structure of human thromboxane synthase determined from the cDNA sequence . |
| Author | Ohashi,K., Ruan,K.H., Kulmacz,R.J., Wu,K.K. and Wang,L.H. |
| Journal | J. Biol. Chem. 267 (2), 789-793 (1992) |
| Title | Thromboxane A2 synthesis in human erythroleukemia cells . |
| Author | Jones,D.A., Fitzpatrick,F.A. and Malcolm,K.C. |
| Journal | Biochem. Biophys. Res. Commun. 180 (1), 8-14 (1991) |
| Title | Molecular cloning of human platelet thromboxane A synthase . |
| Author | Yokoyama,C., Miyata,A., Ihara,H., Ullrich,V. and Tanabe,T. |
| Journal | Biochem. Biophys. Res. Commun. 178 (3), 1479-1484 (1991) |
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