P23219 (PGH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Prostaglandin G/H synthase 1
EC=1.14.99.1

Alternative name(s):
Cyclooxygenase-1
Short name=COX-1
Prostaglandin H2 synthase 1
Short name=PGH synthase 1
Short name=PGHS-1
Short name=PHS 1
Prostaglandin-endoperoxide synthase 1

Gene names

Name:	PTGS1
Synonyms:	COX1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	May play an important role in regulating or promoting cell proliferation in some normal and neoplastically transformed cells.
Catalytic activity	Arachidonate + AH2 + 2 O2 = prostaglandin H2 + A + H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit By similarity.
Pathway	Lipid metabolism; prostaglandin biosynthesis.
Subunit structure	Homodimer.
Subcellular location	Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Miscellaneous	This enzyme acts both as a dioxygenase and as a peroxidase. This enzyme is the target of nonsteroidal anti-inflammatory drugs such as aspirin.
Sequence similarities	Belongs to the prostaglandin G/H synthase family. Contains 1 EGF-like domain.
Sequence caution	The sequence CAI14716.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
Biological process	Fatty acid biosynthesis Lipid synthesis Prostaglandin biosynthesis
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Alternative splicing Polymorphism
Domain	EGF-like domain Signal
Ligand	Heme Iron Metal-binding
Molecular function	Dioxygenase Oxidoreductase Peroxidase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cyclooxygenase pathway Inferred from direct assay. Source: BHF-UCL regulation of blood pressure Inferred from sequence or structural similarity. Source: UniProtKB response to oxidative stress Inferred from electronic annotation. Source: InterPro xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA endoplasmic reticulum membrane Traceable author statement. Source: Reactome microsome Inferred from sequence or structural similarity. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA
Molecular function	heme binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen Inferred from electronic annotation. Source: UniProtKB-KW peroxidase activity Inferred from electronic annotation. Source: UniProtKB-KW prostaglandin-endoperoxide synthase activity Inferred from direct assay. Source: BHF-UCL
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: P23219-1)

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 Short (identifier: P23219-2)

The sequence of this isoform differs from the canonical sequence as follows:
     396-432: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 23	23
	Chain	24 – 599	576	Prostaglandin G/H synthase 1		PRO_0000023868
Regions
	Domain	31 – 69	39	EGF-like
Sites
	Active site	206	1	Proton acceptor By similarity
	Active site	384	1	For cyclooxygenase activity By similarity
	Metal binding	387	1	Iron (heme axial ligand) By similarity
	Site	529	1	Aspirin-acetylated serine
Amino acid modifications
	Glycosylation	67	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	143	1	N-linked (GlcNAc...) Potential
	Disulfide bond	35 ↔ 46		By similarity
	Disulfide bond	36 ↔ 158		By similarity
	Disulfide bond	40 ↔ 56		By similarity
	Disulfide bond	58 ↔ 68		By similarity
	Disulfide bond	568 ↔ 574		By similarity
Natural variations
	Alternative sequence	396 – 432	37	Missing in isoform Short.		VSP_004673
	Natural variant	8	1	W → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10 Corresponds to variant rs1236913 [ dbSNP | Ensembl ].		VAR_013451
	Natural variant	17	1	P → L. Ref.5 Ref.7 Corresponds to variant rs3842787 [ dbSNP | Ensembl ].		VAR_013452
	Natural variant	53	1	R → H. Ref.7 Corresponds to variant rs3842789 [ dbSNP | Ensembl ].		VAR_019161
	Natural variant	149	1	R → L. Ref.7 Corresponds to variant rs10306140 [ dbSNP | Ensembl ].		VAR_019162
	Natural variant	185	1	K → T. Corresponds to variant rs3842792 [ dbSNP | Ensembl ].		VAR_056663
	Natural variant	237	1	L → M. Ref.7 Ref.11 Corresponds to variant rs5789 [ dbSNP | Ensembl ].		VAR_019163
	Natural variant	341	1	K → R. Corresponds to variant rs3842799 [ dbSNP | Ensembl ].		VAR_056664
	Natural variant	359	1	K → R. Corresponds to variant rs5791 [ dbSNP | Ensembl ].		VAR_013453
	Natural variant	443	1	I → V. Corresponds to variant rs5792 [ dbSNP | Ensembl ].		VAR_013454
	Natural variant	481	1	V → I. Ref.11 Corresponds to variant rs5794 [ dbSNP | Ensembl ].		VAR_028017
Experimental info
	Mutagenesis	529	1	S → N: Abolishes cyclooxygenase activity. Ref.2
	Sequence conflict	12	1	F → L in AAA36439. Ref.1
	Sequence conflict	113	1	R → L in AAA36439. Ref.1
	Sequence conflict	378	1	M → T in AAA36439. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified January 11, 2011. Version 2. Checksum: 1F4F734BCD00346D	FASTA	599	68,686
	10 20 30 40 50 60 MSRSLLLWFL LFLLLLPPLP VLLADPGAPT PVNPCCYYPC QHQGICVRFG LDRYQCDCTR 70 80 90 100 110 120 TGYSGPNCTI PGLWTWLRNS LRPSPSFTHF LLTHGRWFWE FVNATFIREM LMRLVLTVRS 130 140 150 160 170 180 NLIPSPPTYN SAHDYISWES FSNVSYYTRI LPSVPKDCPT PMGTKGKKQL PDAQLLARRF 190 200 210 220 230 240 LLRRKFIPDP QGTNLMFAFF AQHFTHQFFK TSGKMGPGFT KALGHGVDLG HIYGDNLERQ 250 260 270 280 290 300 YQLRLFKDGK LKYQVLDGEM YPPSVEEAPV LMHYPRGIPP QSQMAVGQEV FGLLPGLMLY 310 320 330 340 350 360 ATLWLREHNR VCDLLKAEHP TWGDEQLFQT TRLILIGETI KIVIEEYVQQ LSGYFLQLKF 370 380 390 400 410 420 DPELLFGVQF QYRNRIAMEF NHLYHWHPLM PDSFKVGSQE YSYEQFLFNT SMLVDYGVEA 430 440 450 460 470 480 LVDAFSRQIA GRIGGGRNMD HHILHVAVDV IRESREMRLQ PFNEYRKRFG MKPYTSFQEL 490 500 510 520 530 540 VGEKEMAAEL EELYGDIDAL EFYPGLLLEK CHPNSIFGES MIEIGAPFSL KGLLGNPICS 550 560 570 580 590 PEYWKPSTFG GEVGFNIVKT ATLKKLVCLN TKTCPYVSFR VPDASQDDGP AVERPSTEL
	Isoform Short [UniParc]. Checksum: 7AB78D6FD94F5FF1	FASTA	562	64,513
	10 20 30 40 50 60 MSRSLLLWFL LFLLLLPPLP VLLADPGAPT PVNPCCYYPC QHQGICVRFG LDRYQCDCTR 70 80 90 100 110 120 TGYSGPNCTI PGLWTWLRNS LRPSPSFTHF LLTHGRWFWE FVNATFIREM LMRLVLTVRS 130 140 150 160 170 180 NLIPSPPTYN SAHDYISWES FSNVSYYTRI LPSVPKDCPT PMGTKGKKQL PDAQLLARRF 190 200 210 220 230 240 LLRRKFIPDP QGTNLMFAFF AQHFTHQFFK TSGKMGPGFT KALGHGVDLG HIYGDNLERQ 250 260 270 280 290 300 YQLRLFKDGK LKYQVLDGEM YPPSVEEAPV LMHYPRGIPP QSQMAVGQEV FGLLPGLMLY 310 320 330 340 350 360 ATLWLREHNR VCDLLKAEHP TWGDEQLFQT TRLILIGETI KIVIEEYVQQ LSGYFLQLKF 370 380 390 400 410 420 DPELLFGVQF QYRNRIAMEF NHLYHWHPLM PDSFKIGGGR NMDHHILHVA VDVIRESREM 430 440 450 460 470 480 RLQPFNEYRK RFGMKPYTSF QELVGEKEMA AELEELYGDI DALEFYPGLL LEKCHPNSIF 490 500 510 520 530 540 GESMIEIGAP FSLKGLLGNP ICSPEYWKPS TFGGEVGFNI VKTATLKKLV CLNTKTCPYV 550 560 SFRVPDASQD DGPAVERPST EL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of human gene encoding prostaglandin endoperoxide synthase and primary structure of the enzyme." Yokoyama C., Tanabe T. Biochem. Biophys. Res. Commun. 165:888-894(1989) [PubMed: 2512924] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-8.
[2]	"Human platelet/erythroleukemia cell prostaglandin G/H synthase: cDNA cloning, expression, and gene chromosomal assignment." Funk C.D., Funk L.B., Kennedy M.E., Pong A.S., Fitzgerald G.A. FASEB J. 5:2304-2312(1991) [PubMed: 1907252] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS OF SER-529, VARIANT ARG-8.
[3]	"Immunoaffinity purification and cDNA cloning of human platelet prostaglandin endoperoxide synthase (cyclooxygenase)." Takahashi Y., Ueda N., Yoshimoto T., Yamamoto S., Yokoyama C., Miyata A., Tanabe T., Fuse I., Hattori A., Shibata A. Biochem. Biophys. Res. Commun. 182:433-438(1992) [PubMed: 1734857] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-8. Tissue: Platelet.
[4]	"Alternative splicing of human prostaglandin G/H synthase mRNA and evidence of differential regulation of the resulting transcripts by transforming growth factor beta 1, interleukin 1 beta, and tumor necrosis factor alpha." Diaz A., Reginato A.M., Jimenez S.A. J. Biol. Chem. 267:10816-10822(1992) [PubMed: 1587858] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-8. Tissue: Lung fibroblast.
[5]	"Characterization of the human prostaglandin H synthase 1 gene (PTGS1): exclusion by genetic linkage analysis as a second modifier gene in familial thrombosis." Scott B.T., Hasstedt S.J., Bovill E.G., Callas P.W., Valliere J.E., Wang L.-H., Wu K.K., Long G.L. Blood Coagul. Fibrinolysis 13:519-531(2002) [PubMed: 12192304] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-8 AND LEU-17.
[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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT ARG-8. Tissue: Hippocampus.
[7]	SeattleSNPs variation discovery resource Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-8; LEU-17; HIS-53; LEU-149 AND MET-237.
[8]	"DNA sequence and analysis of human chromosome 9." Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I. Nature 429:369-374(2004) [PubMed: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	Mural R.J., Istrail S., Sutton G.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. , 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], VARIANT ARG-8.
[10]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG), VARIANT ARG-8. Tissue: Brain.
[11]	"Arachidonate lipoxygenase (ALOX) and cyclooxygenase (COX) polymorphisms and colon cancer risk." Goodman J.E., Bowman E.D., Chanock S.J., Alberg A.J., Harris C.C. Carcinogenesis 25:2467-2472(2004) [PubMed: 15308583] [Abstract] Cited for: VARIANTS MET-237 AND ILE-481.
+	Additional computationally mapped references.

Web resources

SeattleSNPs

Cross-references

Sequence databases
EMBL GenBank DDBJ	M31822 , M31812, M31813, M31814, M31815, M31816, M31817, M31818, M31819, M31820, M31821 Genomic DNA. Translation: AAA36439.1. M59979 mRNA. Translation: AAA03630.1. S78220 mRNA. Translation: AAB21215.1. S36219 mRNA. Translation: AAB22216.1. S36271 mRNA. Translation: AAB22217.1. AF440204 Genomic DNA. Translation: AAL33601.1. AK290022 mRNA. Translation: BAF82711.1. AY449688 Genomic DNA. Translation: AAR08907.1. AL162424, AL359636 Genomic DNA. Translation: CAI14714.1. AL162424, AL359636 Genomic DNA. Translation: CAI14715.1. AL162424 Genomic DNA. Translation: CAI14716.1. Sequence problems. AL359636, AL162424 Genomic DNA. Translation: CAM45740.1. AL359636, AL162424 Genomic DNA. Translation: CAM45741.1. CH471090 Genomic DNA. Translation: EAW87530.1. BC029840 mRNA. Translation: AAH29840.1.
IPI	IPI00298267. IPI00298268.
PIR	JH0259.
RefSeq	NP_000953.2. NM_000962.2. NP_542158.1. NM_080591.1.
UniGene	Hs.201978.
3D structure databases
ProteinModelPortal	P23219.
SMR	P23219. Positions 31-583.
ModBase	Search...
Protein-protein interaction databases
STRING	P23219.
Protein family/group databases
PeroxiBase	3320. HsPGHS01.
Polymorphism databases
DMDM	129899.
Proteomic databases
PRIDE	P23219.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000362012; ENSP00000354612; ENSG00000095303.
GeneID	5742.
KEGG	hsa:5742.
Organism-specific databases
CTD	5742.
GeneCards	GC09P125133.
H-InvDB	HIX0008355.
HGNC	HGNC:9604. PTGS1.
HPA	CAB020315. HPA002834.
MIM	176805. gene.
neXtProt	NX_P23219.
PharmGKB	PA24346.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG14984.
HOVERGEN	HBG000366.
InParanoid	P23219.
OMA	DNLERQY.
OrthoDB	EOG402WRZ.
PhylomeDB	P23219.
Enzyme and pathway databases
BRENDA	1.14.99.1. 2681.
Reactome	REACT_111217. Metabolism. REACT_22258. Metabolism of lipids and lipoproteins.
Gene expression databases
ArrayExpress	P23219.
Bgee	P23219.
CleanEx	HS_PTGS1.
Genevestigator	P23219.
GermOnline	ENSG00000095303. Homo sapiens.
Family and domain databases
InterPro	IPR006210. EGF-like. IPR000742. EGF_3. IPR010255. Haem_peroxidase. IPR002007. Haem_peroxidase_animal. IPR019791. Haem_peroxidase_animal_subgr. [Graphical view]
Gene3D	G3DSA:1.10.640.10. Haem_peroxidase_animal. 1 hit.
KO	K00509.
Pfam	PF03098. An_peroxidase. 2 hits. [Graphical view]
PRINTS	PR00457. ANPEROXIDASE.
SMART	SM00181. EGF. 1 hit. [Graphical view]
SUPFAM	SSF48113. Peroxidase_super. 1 hit.
PROSITE	PS00022. EGF_1. False negative. PS01186. EGF_2. False negative. PS50026. EGF_3. 1 hit. PS50292. PEROXIDASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
DrugBank	DB00316. Acetaminophen. DB00945. Aspirin. DB01014. Balsalazide. DB00963. Bromfenac. DB01188. Ciclopirox. DB00586. Diclofenac. DB00861. Diflunisal. DB04817. Dipyrone. DB00749. Etodolac. DB00573. Fenoprofen. DB00712. Flurbiprofen. DB00154. gamma-Homolinolenic acid. DB01050. Ibuprofen. DB00159. Icosapent. DB00328. Indomethacin. DB01009. Ketoprofen. DB00465. Ketorolac. DB01283. Lumiracoxib. DB00939. Meclofenamic acid. DB00784. Mefenamic acid. DB00244. Mesalazine. DB00350. Minoxidil. DB00461. Nabumetone. DB00788. Naproxen. DB03783. Phenacetin. DB00554. Piroxicam. DB00533. Rofecoxib. DB00936. Salicyclic acid. DB01399. Salsalate. DB00605. Sulindac. DB00870. Suprofen. DB00469. Tenoxicam. DB00500. Tolmetin.
NextBio	22352.
SOURCE	Search...

Entry information

Entry name

PGH1_HUMAN

Accession

Primary (citable) accession number: P23219
Secondary accession number(s): A8K1V7 , Q15122, Q5T7T6, Q5T7T7, Q5T7T8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 11, 2011
Last modified:	January 25, 2012
This is version 140 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.