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P24557 (THAS_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Thromboxane-A synthase

Short name=TXA synthase
Short name=TXS
EC=5.3.99.5
Alternative name(s):
Cytochrome P450 5A1
Gene names
Name:TBXAS1
Synonyms:CYP5, CYP5A1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

(5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-9-alpha,11-alpha-epoxy-15-hydroxythromboxa-5,13-dienoate.

Cofactor

Heme group.

Subunit structure

Monomer.

Subcellular location

Endoplasmic reticulum membrane; Multi-pass membrane protein Ref.13.

Tissue specificity

Platelets, lung, kidney, spleen, macrophages and lung fibroblasts.

Involvement in disease

Ghosal hematodiaphyseal dysplasia (GHDD) [MIM:231095]: Rare autosomal recessive disorder characterized by increased bone density with predominant diaphyseal involvement and aregenerative corticosteroid-sensitive anemia. Aregenerative anemia is characterized by bone marrow failure, so that functional marrow cells are regenerated slowly or not at all.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.20

Thromboxane synthetase deficiency has been detected in some patients with a bleeding disorder due to platelet dysfunction. Ref.14

Sequence similarities

Belongs to the cytochrome P450 family.

Caution

It is uncertain whether Met-1 is the initiator. An alternative upstream Met is found in primates, but not in other mammals.

Sequence caution

The sequence AAA60617.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAA60618.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAC01761.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence AAC01761.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99269.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99270.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99271.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99272.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99273.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99274.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99275.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99276.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99277.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99278.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAF99279.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence AAH41157.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence BAG58828.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

The sequence EAW83934.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processFatty acid biosynthesis
Fatty acid metabolism
Lipid biosynthesis
Lipid metabolism
Prostaglandin biosynthesis
Prostaglandin metabolism
   Cellular componentEndoplasmic reticulum
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransmembrane
Transmembrane helix
   LigandHeme
Iron
Metal-binding
   Molecular functionIsomerase
Monooxygenase
Oxidoreductase
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processarachidonic acid metabolic process

Traceable author statement. Source: Reactome

cyclooxygenase pathway

Traceable author statement. Source: Reactome

icosanoid metabolic process

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentendoplasmic reticulum membrane

Traceable author statement. Source: Reactome

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionheme binding

Inferred from electronic annotation. Source: InterPro

iron ion binding

Inferred from electronic annotation. Source: InterPro

monooxygenase activity

Inferred from electronic annotation. Source: UniProtKB-KW

oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen

Inferred from electronic annotation. Source: InterPro

thromboxane-A synthase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P24557-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P24557-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P24557-3)

The sequence of this isoform differs from the canonical sequence as follows:
     150-150: E → ELGLLIMQERIKGHMGGQQAPQRIPPTRLSKPSGIYVNLHYATLPFC
Isoform 4 (identifier: P24557-4)

The sequence of this isoform differs from the canonical sequence as follows:
     456-459: FTAE → YRCS
     460-533: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 533533Thromboxane-A synthase
PRO_0000052256

Regions

Topological domain1 – 1010Cytoplasmic Potential
Transmembrane11 – 3121Helical; Potential
Topological domain32 – 7544Lumenal Potential
Transmembrane76 – 9621Helical; Potential
Topological domain97 – 223127Cytoplasmic Potential
Transmembrane224 – 24421Helical; Potential
Topological domain245 – 33591Lumenal Potential
Transmembrane336 – 35621Helical; Potential
Topological domain357 – 533177Cytoplasmic Potential

Sites

Metal binding4791Iron (heme axial ligand) By similarity

Natural variations

Alternative sequence1 – 6767Missing in isoform 2.
VSP_047217
Alternative sequence1501E → ELGLLIMQERIKGHMGGQQA PQRIPPTRLSKPSGIYVNLH YATLPFC in isoform 3.
VSP_054121
Alternative sequence456 – 4594FTAE → YRCS in isoform 4.
VSP_054122
Alternative sequence460 – 53374Missing in isoform 4.
VSP_054123
Natural variant601R → H in allele CYP5A1*2. Ref.5 Ref.15
Corresponds to variant rs6138 [ dbSNP | Ensembl ].
VAR_014157
Natural variant701L → P.
Corresponds to variant rs13306050 [ dbSNP | Ensembl ].
VAR_058465
Natural variant701L → V.
Corresponds to variant rs4529 [ dbSNP | Ensembl ].
VAR_058466
Natural variant821L → P in GHDD. Ref.20
VAR_044386
Natural variant851R → W in a breast cancer sample; somatic mutation. Ref.19
VAR_036294
Natural variant1241V → I. Ref.18
VAR_018378
Natural variant1601D → E in allele CYP5A1*3. Ref.5 Ref.17
Corresponds to variant rs5768 [ dbSNP | Ensembl ].
VAR_010919
Natural variant1621L → I. Ref.15
Corresponds to variant rs6137 [ dbSNP | Ensembl ].
VAR_014158
Natural variant2451N → S in allele CYP5A1*4. Ref.5
VAR_010920
Natural variant2571K → E.
Corresponds to variant rs5769 [ dbSNP | Ensembl ].
VAR_014647
Natural variant2601R → G.
Corresponds to variant rs5770 [ dbSNP | Ensembl ].
VAR_014648
Natural variant3161Q → K.
Corresponds to variant rs5771 [ dbSNP | Ensembl ].
VAR_014649
Natural variant3311I → T. Ref.15
Corresponds to variant rs6140 [ dbSNP | Ensembl ].
VAR_014159
Natural variant3561L → V in allele CYP5A1*5. Ref.5 Ref.15 Ref.17
Corresponds to variant rs4529 [ dbSNP | Ensembl ].
VAR_010921
Natural variant3571L → V.
Corresponds to variant rs4529 [ dbSNP | Ensembl ].
VAR_044387
Natural variant3871E → K.
Corresponds to variant rs3735354 [ dbSNP | Ensembl ].
VAR_055565
Natural variant3881E → K. Ref.18
Corresponds to variant rs3735354 [ dbSNP | Ensembl ].
VAR_018379
Natural variant3891G → V.
Corresponds to variant rs5760 [ dbSNP | Ensembl ].
VAR_016158
Natural variant4121R → Q in GHDD. Ref.20
VAR_044388
Natural variant4161Q → E in allele CYP5A1*6. Ref.5 Ref.15 Ref.17
Corresponds to variant rs4528 [ dbSNP | Ensembl ].
VAR_010922
Natural variant4241R → C. Ref.17
Corresponds to variant rs5762 [ dbSNP | Ensembl ].
VAR_014160
Natural variant4291A → T. Ref.15 Ref.17
Corresponds to variant rs4526 [ dbSNP | Ensembl ].
VAR_014161
Natural variant4491E → K in allele CYP5A1*7. Ref.5 Ref.18
VAR_010923
Natural variant4501T → N in allele CYP5A1*8. Ref.5
Corresponds to variant rs5763 [ dbSNP | Ensembl ].
VAR_010924
Natural variant4651R → Q in allele CYP5A1*9. Ref.5
VAR_010925
Natural variant4811G → W in GHDD. Ref.20
VAR_044389
Natural variant4871L → P in GHDD. Ref.20
VAR_044390
Natural variant5011R → Q. Ref.18
VAR_018380
Natural variant5111P → L.
Corresponds to variant rs13306050 [ dbSNP | Ensembl ].
VAR_055566
Natural variant5121L → P.
Corresponds to variant rs13306050 [ dbSNP | Ensembl ].
VAR_044391

Experimental info

Sequence conflict1021E → Q in AAA36742. Ref.10
Sequence conflict1481L → V in AAC01761. Ref.4
Sequence conflict1941A → P in AAA60617. Ref.2
Sequence conflict1941A → P in AAA60618. Ref.2
Sequence conflict1941A → P in AAC01761. Ref.4
Sequence conflict1941A → P in AAF99269. Ref.5
Sequence conflict1941A → P in AAF99270. Ref.5
Sequence conflict1941A → P in AAF99271. Ref.5
Sequence conflict1941A → P in AAF99272. Ref.5
Sequence conflict1941A → P in AAF99273. Ref.5
Sequence conflict1941A → P in AAF99274. Ref.5
Sequence conflict1941A → P in AAF99275. Ref.5
Sequence conflict1941A → P in AAF99276. Ref.5
Sequence conflict1941A → P in AAF99277. Ref.5
Sequence conflict1941A → P in AAF99278. Ref.5
Sequence conflict1941A → P in AAF99279. Ref.5
Sequence conflict1941A → P in AAA36742. Ref.10
Sequence conflict3851S → G no nucleotide entry Ref.1
Sequence conflict4831R → H in BAA07011. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 28, 2009. Version 3.
Checksum: E95E7B7EA77E6DDC

FASTA53360,518
        10         20         30         40         50         60 
MEALGFLKLE VNGPMVTVAL SVALLALLKW YSTSAFSRLE KLGLRHPKPS PFIGNLTFFR 

        70         80         90        100        110        120 
QGFWESQMEL RKLYGPLCGY YLGRRMFIVI SEPDMIKQVL VENFSNFTNR MASGLEFKSV 

       130        140        150        160        170        180 
ADSVLFLRDK RWEEVRGALM SAFSPEKLNE MVPLISQACD LLLAHLKRYA ESGDAFDIQR 

       190        200        210        220        230        240 
CYCNYTTDVV ASVAFGTPVD SWQAPEDPFV KHCKRFFEFC IPRPILVLLL SFPSIMVPLA 

       250        260        270        280        290        300 
RILPNKNRDE LNGFFNKLIR NVIALRDQQA AEERRRDFLQ MVLDARHSAS PMGVQDFDIV 

       310        320        330        340        350        360 
RDVFSSTGCK PNPSRQHQPS PMARPLTVDE IVGQAFIFLI AGYEIITNTL SFATYLLATN 

       370        380        390        400        410        420 
PDCQEKLLRE VDVFKEKHMA PEFCSLEEGL PYLDMVIAET LRMYPPAFRF TREAAQDCEV 

       430        440        450        460        470        480 
LGQRIPAGAV LEMAVGALHH DPEHWPSPET FNPERFTAEA RQQHRPFTYL PFGAGPRSCL 

       490        500        510        520        530 
GVRLGLLEVK LTLLHVLHKF RFQACPETQV PLQLESKSAL GPKNGVYIKI VSR 

« Hide

Isoform 2 [UniParc].

Checksum: E214331AAC1B7797
Show »

FASTA46652,995
Isoform 3 [UniParc].

Checksum: B3FF6087E8892CCF
Show »

FASTA57965,632
Isoform 4 [UniParc].

Checksum: 7AE5A27B6467D359
Show »

FASTA45952,287

References

« Hide 'large scale' references
[1]"Molecular cloning of human platelet thromboxane A synthase."
Yokoyama C., Miyata A., Ihara H., Ullrich V., Tanabe T.
Biochem. Biophys. Res. Commun. 178:1479-1484(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Platelet.
[2]"Primary structure of human thromboxane synthase determined from the cDNA sequence."
Ohashi K., Ruan K.H., Kulmacz R.J., Wu K.K., Wang L.-H.
J. Biol. Chem. 267:789-793(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4).
Tissue: Lung.
[3]"Characterization of the human gene (TBXAS1) encoding thromboxane synthase."
Miyata A., Yokoyama C., Ihara H., Bandoh S., Takeda O., Takahashi E., Tanabe T.
Eur. J. Biochem. 224:273-279(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Peripheral blood.
[4]"Human thromboxane A2 synthase."
Shen R.-F.
Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Identification of genetic variants in the human thromboxane synthase gene (CYP5A1)."
Chevalier D., Lo-Guidice J.-M., Sergent E., Allorge D., Debuysere H., Ferrari N., Libersa C., Lhermitte M., Broly F.
Mutat. Res. 432:61-67(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS HIS-60; GLU-160; SER-245; VAL-356; GLU-416; LYS-449; ASN-450 AND GLN-465.
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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 T.-O., 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Tissue: Thalamus.
[7]"The DNA sequence of human chromosome 7."
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. expand/collapse author list , Nash W.E., 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 C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., 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 W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Lung.
[10]"Isolation of partial complementary DNA encoding human thromboxane synthase."
Wang L.-H., Oshashi K., Wu K.K.
Biochem. Biophys. Res. Commun. 177:286-291(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 16-244 (ISOFORM 1/2).
Tissue: Lung.
[11]"Immunoaffinity purification of human thromboxane synthase."
Nuesing R., Schneider-Voss S., Ullrich V.
Arch. Biochem. Biophys. 280:325-330(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE OF 1-26; 96-110 AND 237-280.
[12]Nuesing R.
Thesis (1990), University of Konstanz, Germany
Cited for: PARTIAL PROTEIN SEQUENCE.
[13]"Amino-terminal topology of thromboxane synthase in the endoplasmic reticulum."
Ruan K.H., Wang L.-H., Wu K.K., Kulmacz R.J.
J. Biol. Chem. 268:19483-19490(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MEMBRANE TOPOLOGY.
[14]"Severe bleeding associated with defective thromboxane synthetase."
Mestel F., Oetliker O., Beck E., Felix R., Imbach P., Wagner H.P.
Lancet 1:157-157(1980) [PubMed] [Europe PMC] [Abstract]
Cited for: DISEASE.
[15]"Characterization of single-nucleotide polymorphisms in coding regions of human genes."
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 22:231-238(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HIS-60; ILE-162; THR-331; VAL-356; GLU-416 AND THR-429.
[16]Erratum
Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.
Nat. Genet. 23:373-373(1999)
[17]"Patterns of single-nucleotide polymorphisms in candidate genes for blood-pressure homeostasis."
Halushka M.K., Fan J.-B., Bentley K., Hsie L., Shen N., Weder A., Cooper R., Lipshutz R., Chakravarti A.
Nat. Genet. 22:239-247(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GLU-160; VAL-356; GLU-416; CYS-424 AND THR-429.
[18]"Catalog of 680 variations among eight cytochrome p450 (CYP) genes, nine esterase genes, and two other genes in the Japanese population."
Saito S., Iida A., Sekine A., Kawauchi S., Higuchi S., Ogawa C., Nakamura Y.
J. Hum. Genet. 48:249-270(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ILE-124; LYS-388; LYS-449 AND GLN-501.
[19]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] TRP-85.
[20]"Thromboxane synthase mutations in an increased bone density disorder (Ghosal syndrome)."
Genevieve D., Proulle V., Isidor B., Bellais S., Serre V., Djouadi F., Picard C., Vignon-Savoye C., Bader-Meunier B., Blanche S., de Vernejoul M.-C., Legeai-Mallet L., Fischer A.-M., Le Merrer M., Dreyfus M., Gaussem P., Munnich A., Cormier-Daire V.
Nat. Genet. 40:284-286(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS GHDD PRO-82; GLN-412; TRP-481 AND PRO-487.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M80646 mRNA. Translation: AAA60617.1. Different initiation.
M80647 mRNA. Translation: AAA60618.1. Different initiation.
D34625 Genomic DNA. Translation: BAA07011.1.
L36085 expand/collapse EMBL AC list , L36075, L36076, L36077, L36078, L36079, L36080, L36081, L36082, L36083, L36084 Genomic DNA. Translation: AAC01761.1. Different initiation.
AF233615 Genomic DNA. Translation: AAF99269.1. Different initiation.
AF233616 Genomic DNA. Translation: AAF99270.1. Different initiation.
AF233617 Genomic DNA. Translation: AAF99271.1. Different initiation.
AF233618 Genomic DNA. Translation: AAF99272.1. Different initiation.
AF233619 Genomic DNA. Translation: AAF99273.1. Different initiation.
AF233620 Genomic DNA. Translation: AAF99274.1. Different initiation.
AF233621 Genomic DNA. Translation: AAF99275.1. Different initiation.
AF233622 Genomic DNA. Translation: AAF99276.1. Different initiation.
AF233623 Genomic DNA. Translation: AAF99277.1. Different initiation.
AF233624 Genomic DNA. Translation: AAF99278.1. Different initiation.
AF233625 Genomic DNA. Translation: AAF99279.1. Different initiation.
AK296069 mRNA. Translation: BAG58828.1. Different initiation.
AC004914 Genomic DNA. No translation available.
AC004961 Genomic DNA. No translation available.
AC006021 Genomic DNA. No translation available.
CH471070 Genomic DNA. Translation: EAW83934.1. Different initiation.
BC014117 mRNA. Translation: AAH14117.1.
BC041157 mRNA. Translation: AAH41157.1. Different initiation.
M74055 mRNA. Translation: AAA36742.1.
CCDSCCDS55175.1. [P24557-2]
PIRA41766.
S48161.
RefSeqNP_001052.2. NM_001061.4.
NP_001124438.1. NM_001130966.2.
NP_001159725.1. NM_001166253.1.
NP_001159726.1. NM_001166254.1. [P24557-2]
NP_112246.2. NM_030984.3.
UniGeneHs.520757.

3D structure databases

ProteinModelPortalP24557.
SMRP24557. Positions 39-533.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid112778. 1 interaction.
IntActP24557. 1 interaction.
MINTMINT-4823512.

Chemistry

BindingDBP24557.
ChEMBLCHEMBL1835.

PTM databases

PhosphoSiteP24557.

Proteomic databases

MaxQBP24557.
PaxDbP24557.
PRIDEP24557.

Protocols and materials databases

DNASU6916.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000263552; ENSP00000263552; ENSG00000059377.
ENST00000336425; ENSP00000338087; ENSG00000059377.
ENST00000414508; ENSP00000392702; ENSG00000059377.
ENST00000416849; ENSP00000389414; ENSG00000059377.
ENST00000425687; ENSP00000388736; ENSG00000059377.
ENST00000436047; ENSP00000392361; ENSG00000059377.
ENST00000448866; ENSP00000402536; ENSG00000059377.
GeneID6916.
KEGGhsa:6916.
UCSCuc010lne.3. human. [P24557-1]

Organism-specific databases

CTD6916.
GeneCardsGC07P139476.
HGNCHGNC:11609. TBXAS1.
HPAHPA031257.
HPA031258.
HPA031259.
MIM231095. phenotype.
274180. gene.
neXtProtNX_P24557.
Orphanet1802. Ghosal hematodiaphyseal dysplasia.
PharmGKBPA349.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOVERGENHBG108567.
InParanoidP24557.
KOK01832.
OMACIPRPIL.
PhylomeDBP24557.

Enzyme and pathway databases

BioCycMetaCyc:HS00728-MONOMER.
ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressP24557.
BgeeP24557.
GenevestigatorP24557.

Family and domain databases

Gene3D1.10.630.10. 2 hits.
InterProIPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]
PfamPF00067. p450. 2 hits.
[Graphical view]
PRINTSPR00463. EP450I.
PR00385. P450.
SUPFAMSSF48264. SSF48264. 2 hits.
PROSITEPS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiThromboxane-A_synthase.
GenomeRNAi6916.
NextBio27051.
PROP24557.
SOURCESearch...

Entry information

Entry nameTHAS_HUMAN
AccessionPrimary (citable) accession number: P24557
Secondary accession number(s): B4DJG6 expand/collapse secondary AC list , E7EMU9, E7EP08, E7ESB5, O14987, Q16843, Q16844, Q8IUN1, Q96CN2, Q9GZW4, Q9HD77, Q9HD78, Q9HD79, Q9HD80, Q9HD81, Q9HD82, Q9HD83, Q9HD84
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: July 28, 2009
Last modified: July 9, 2014
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM