P31213 (S5A2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-oxo-5-alpha-steroid 4-dehydrogenase 2
EC=1.3.1.22

Alternative name(s):
5 alpha-SR2
SR type 2
Steroid 5-alpha-reductase 2
Short name=S5AR 2
Type II 5-alpha reductase

Gene names

Name:

SRD5A2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	254 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Catalytic activity	A 3-oxo-5-alpha-steroid + NADP+ = a 3-oxo-Delta(4)-steroid + NADPH.
Subcellular location	Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein Potential.
Tissue specificity	Expressed in high levels in the prostate and many other androgen-sensitive tissues.
Polymorphism	Individuals with Thr-49 have an increased risk of prostate cancer. The enzyme with Thr-49 has a higher in vitro V(max) than the Ala-49 enzyme.
Involvement in disease	Pseudovaginal perineoscrotal hypospadias (PPSH) [MIM:264600]: A form of male pseudohermaphroditism in which 46,XY males show ambiguous genitalia at birth, including perineal hypospadias and a blind perineal pouch, and develop masculinization at puberty. The name of the disorder stems from the finding of a blind-ending perineal opening resembling a vagina and a severely hypospadiac penis with the urethra opening onto the perineum. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.22 Ref.23 Ref.24 Ref.25
Sequence similarities	Belongs to the steroid 5-alpha reductase family.
Biophysicochemical properties	pH dependence: Optimally active at acidic pHs.

Ontologies

Keywords
Biological process	Differentiation Sexual differentiation
Cellular component	Endoplasmic reticulum Membrane Microsome
Coding sequence diversity	Polymorphism
Disease	Disease mutation Pseudohermaphroditism
Domain	Transmembrane Transmembrane helix
Ligand	NADP
Molecular function	Oxidoreductase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	androgen biosynthetic process Traceable author statement. Source: Reactome cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW cell-cell signaling Traceable author statement Ref.1. Source: UniProtKB male gonad development Inferred from mutant phenotype Ref.1. Source: UniProtKB small molecule metabolic process Traceable author statement. Source: Reactome
Cellular_component	endoplasmic reticulum membrane Traceable author statement. Source: Reactome integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	3-oxo-5-alpha-steroid 4-dehydrogenase activity Inferred from electronic annotation. Source: InterPro cholestenone 5-alpha-reductase activity Inferred from electronic annotation. Source: EC sterol 5-alpha reductase activity Inferred from direct assay Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 254	254	3-oxo-5-alpha-steroid 4-dehydrogenase 2		PRO_0000213676
Regions
	Transmembrane	8 – 28	21	Helical; Potential
	Transmembrane	72 – 92	21	Helical; Potential
	Transmembrane	146 – 166	21	Helical; Potential
	Transmembrane	206 – 226	21	Helical; Potential
Natural variations
	Natural variant	49	1	A → T. Ref.4 Ref.16 Ref.21 Ref.23 Ref.24 Corresponds to variant rs9282858 [ dbSNP | Ensembl ].		VAR_013104
	Natural variant	55	1	L → Q in PPSH. Ref.12		VAR_013105
	Natural variant	85	1	G → D in PPSH. Ref.17		VAR_013130
	Natural variant	89	1	V → L. Ref.3 Ref.4 Ref.7 Ref.19 Ref.20 Ref.23 Ref.24 Corresponds to variant rs523349 [ dbSNP | Ensembl ].		VAR_013131
	Natural variant	113	1	L → V. Ref.4 Corresponds to variant rs28383048 [ dbSNP | Ensembl ].		VAR_022302
	Natural variant	115	1	G → D in PPSH. Ref.11 Ref.17 Ref.22		VAR_013106
	Natural variant	123	1	G → R in PPSH. Ref.25		VAR_025854
	Natural variant	126	1	Q → R in PPSH. Ref.24		VAR_025855
	Natural variant	145	1	R → W in PPSH. Ref.23		VAR_025851
	Natural variant	157	1	Missing in PPSH. Ref.10		VAR_013107
	Natural variant	158	1	G → R in PPSH. Ref.24		VAR_025856
	Natural variant	181	1	P → L in PPSH. Ref.23		VAR_025852
	Natural variant	183	1	G → S in PPSH. Ref.11 Ref.24		VAR_013108
	Natural variant	196	1	G → S in PPSH. Ref.15 Ref.23 Ref.24		VAR_013109
	Natural variant	197	1	E → D in PPSH. Ref.18		VAR_013110
	Natural variant	200	1	E → K in PPSH. Ref.13		VAR_013132
	Natural variant	203	1	G → S. Corresponds to variant rs9332961 [ dbSNP | Ensembl ].		VAR_059791
	Natural variant	207	1	A → D in PPSH. Ref.24		VAR_025857
	Natural variant	212	1	P → R in PPSH. Ref.17 Ref.18		VAR_013111
	Natural variant	224	1	L → H. Corresponds to variant rs9332963 [ dbSNP | Ensembl ].		VAR_059792
	Natural variant	224	1	L → M. Corresponds to variant rs9332963 [ dbSNP | Ensembl ].		VAR_037585
	Natural variant	227	1	R → Q in micropenis. Ref.20 Corresponds to variant rs9332964 [ dbSNP | Ensembl ].		VAR_037586
	Natural variant	228	1	A → T in PPSH. Ref.14		VAR_013112
	Natural variant	231	1	H → R in PPSH. Ref.15		VAR_013113
	Natural variant	235	1	Y → F in PPSH. Ref.23		VAR_025853
	Natural variant	245	1	S → Y in PPSH. Ref.17		VAR_013133
	Natural variant	246	1	R → Q in PPSH. Ref.17 Ref.23 Corresponds to variant rs9332967 [ dbSNP | Ensembl ].		VAR_013134
	Natural variant	246	1	R → W in PPSH. Ref.9 Ref.11 Ref.22 Ref.24		VAR_005609

Sequences

	Sequence		Length	Mass (Da)
	P31213 [UniParc]. Last modified July 1, 1993. Version 1. Checksum: E65A19C8600DED05	FASTA	254	28,393
	10 20 30 40 50 60 MQVQCQQSPV LAGSATLVAL GALALYVAKP SGYGKHTESL KPAATRLPAR AAWFLQELPS 70 80 90 100 110 120 FAVPAGILAR QPLSLFGPPG TVLLGLFCVH YFHRTFVYSL LNRGRPYPAI LILRGTAFCT 130 140 150 160 170 180 GNGVLQGYYL IYCAEYPDGW YTDIRFSLGV FLFILGMGIN IHSDYILRQL RKPGEISYRI 190 200 210 220 230 240 PQGGLFTYVS GANFLGEIIE WIGYALATWS LPALAFAFFS LCFLGLRAFH HHRFYLKMFE 250 DYPKSRKALI PFIF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Deletion of steroid 5 alpha-reductase 2 gene in male pseudohermaphroditism." Andersson S., Berman D.M., Jenkins E.P., Russell D.W. Nature 354:159-161(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure of human type II 5 alpha-reductase gene." Labrie F., Sugimoto Y., Luu-The V., Simard J., Lachance Y., Bachvarov D., Leblanc G., Durocher F., Paquet N. Endocrinology 131:1571-1573(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	Schupp I. Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT LEU-89. Tissue: Liver tumor.
[4]	NIEHS SNPs program Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-49; LEU-89 AND VAL-113.
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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], VARIANT LEU-89.
[8]	"Transcription of type II 5 alpha-reductase is up-regulated by SRY in human dermal papilla cells." Nakanishi J., Hibino T. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-67. Tissue: Placenta.
[9]	"Molecular genetics of steroid 5 alpha-reductase 2 deficiency." Thigpen A.E., Davis D.L., Milatovich A., Mendonca B.B., Imperato-Mcginley J., Griffin J.E., Francke U., Wilson J.D., Russell D.W. J. Clin. Invest. 90:799-809(1992) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PPSH TRP-246.
[10]	"A new deletion of the 5-alpha-reductase type 2 gene in a Turkish family with 5-alpha-reductase deficiency." Boudon C., Lobaccaro J.-M., Lumbroso S., Ogur G., Ocal G., Belon C., Sultan C. Clin. Endocrinol. (Oxf.) 43:183-188(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PPSH MET-157 DEL.
[11]	"5-alpha-reductase-2 gene mutations in the Dominican Republic." Cai L.-Q., Zhu Y.-S., Katz M.D., Herrera C., Baez J., DeFillo-Ricart M., Shackleton C.H.L., Imperato-McGinley J. J. Clin. Endocrinol. Metab. 81:1730-1735(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PPSH ASP-115; SER-183 AND TRP-246.
[12]	"Clinical, biochemical, and genetic findings in a large pedigree of male and female patients with 5-alpha-reductase 2 deficiency." Hochberg Z., Chayen R., Reiss N., Falik Z., Makler A., Munichor M., Farkas A., Goldfarb H., Ohana N., Hiort O. J. Clin. Endocrinol. Metab. 81:2821-2827(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PPSH GLN-55.
[13]	"Male pseudohermaphroditism resulting from a novel mutation in the human steroid 5 alpha-reductase type 2 gene (SRD5A2)." Anwar R., Gilbey S.G., New J.P., Markham A.F. Mol. Pathol. 50:51-52(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PPSH LYS-200.
[14]	"Homozygous mutation (A228T) in the 5-alpha-reductase type 2 gene in a boy with 5-alpha-reductase deficiency: genotype-phenotype correlations." Nordenskjold A., Magnus O., Aagenaes O., Knudtzon J. Am. J. Med. Genet. 80:269-272(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PPSH THR-228.
[15]	"Molecular characterization of 5-alpha-reductase type 2 deficiency and fertility in a Swedish family." Nordenskjold A., Ivarsson S.-A. J. Clin. Endocrinol. Metab. 83:3236-3238(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PPSH SER-196 AND ARG-231.
[16]	"Association of mis-sense substitution in SRD5A2 gene with prostate cancer in African-American and Hispanic men in Los Angeles, USA." Makridakis N.M., Ross R.K., Pike M.C., Crocitto L.E., Kolonel L.N., Pearce C.L., Henderson B.E., Reichardt J.K.V. Lancet 354:975-978(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-49.
[17]	"Identification of missense mutations in the SRD5A2 gene from patients with steroid 5alpha-reductase 2 deficiency." Vilchis F., Mendez J.P., Canto P., Lieberman E., Chavez B. Clin. Endocrinol. (Oxf.) 52:383-387(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PPSH ASP-85; ASP-115; ARG-212; TYR-245 AND GLN-246.
[18]	"Uniparental disomy in steroid 5-alpha-reductase 2 deficiency." Chavez B., Valdez E., Vilchis F. J. Clin. Endocrinol. Metab. 85:3147-3150(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PPSH ASP-197 AND ARG-212.
[19]	"Steroid 5-alpha reductase type II V89L substitution is not associated with risk of prostate cancer in a multiethnic population study." Pearce C.L., Makridakis N.M., Ross R.K., Pike M.C., Kolonel L.N., Henderson B.E., Reichardt J.K.V. Cancer Epidemiol. Biomarkers Prev. 11:417-418(2002) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LEU-89.
[20]	"Micropenis and the 5alpha-reductase-2 (SRD5A2) gene: mutation and V89L polymorphism analysis in 81 Japanese patients." Sasaki G., Ogata T., Ishii T., Kosaki K., Sato S., Homma K., Takahashi T., Hasegawa T., Matsuo N. J. Clin. Endocrinol. Metab. 88:3431-3436(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MICROPENIS GLN-227, VARIANT LEU-89.
[21]	"Comprehensive evaluation of the association between prostate cancer and genotypes/haplotypes in CYP17A1, CYP3A4, and SRD5A2." Loukola A., Chadha M., Penn S.G., Rank D., Conti D.V., Thompson D., Cicek M., Love B., Bivolarevic V., Yang Q., Jiang Y., Hanzel D.K., Dains K., Paris P.L., Casey G., Witte J.S. Eur. J. Hum. Genet. 12:321-332(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT THR-49, LACK OF ASSOCIATION WITH PROSTATE CANCER.
[22]	"Clinical, biochemical and morphologic diagnostic markers in an infant male pseudohermaphrodite patient with compound heterozygous mutations (G115D/R246W) in SRD5A2 gene." Fernandez-Cancio M., Rodo J., Andaluz P., Martinez de Osaba M.J., Rodriguez-Hierro F., Esteban C., Carrascosa A., Audi L. Horm. Res. 62:259-264(2004) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PPSH ASP-115 AND TRP-246.
[23]	"SRD5A2 gene analysis in an Italian population of under-masculinized 46,XY subjects." Nicoletti A., Baldazzi L., Balsamo A., Barp L., Pirazzoli P., Gennari M., Radetti G., Cacciari E., Cicognani A. Clin. Endocrinol. (Oxf.) 63:375-380(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PPSH TRP-145; LEU-181; SER-196; PHE-235 AND GLN-246, VARIANTS THR-49 AND LEU-89.
[24]	"New mutations, hotspots, and founder effects in Brazilian patients with steroid 5alpha-reductase deficiency type 2." Hackel C., Oliveira L.E., Ferraz L.F., Tonini M.M., Silva D.N., Toralles M.B., Stuchi-Perez E.G., Guerra-Junior G. J. Mol. Med. 83:569-576(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS PPSH ARG-126; ARG-158; SER-183; SER-196; ASP-207 AND TRP-246, VARIANTS THR-49 AND LEU-89.
[25]	"A novel missense mutation of 5-alpha reductase type 2 gene (SRD5A2) leads to severe male pseudohermaphroditism in a Turkish family." Bahceci M., Ersay A.R., Tuzcu A., Hiort O., Richter-Unruh A., Gokalp D. Urology 66:407-410(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT PPSH ARG-123.
+	Additional computationally mapped references.

Web resources

GeneReviews

NIEHS-SNPs

Wikipedia

5-alpha reductase entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	M74047 mRNA. Translation: AAA60586.1. AB047857 Genomic DNA. Translation: BAB40419.1. EF560740 mRNA. Translation: ABQ59050.1. AY884245 Genomic DNA. Translation: AAW56942.1. AK316597 mRNA. Translation: BAG38184.1. CH471053 Genomic DNA. Translation: EAX00478.1. BC112252 mRNA. Translation: AAI12253.1. BC113641 mRNA. Translation: AAI13642.1. L03843 Genomic DNA. No translation available.
IPI	IPI00010651.
PIR	A49169.
RefSeq	NP_000339.2. NM_000348.3.
UniGene	Hs.458345.
3D structure databases
ProteinModelPortal	P31213.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000233139.
PTM databases
PhosphoSite	P31213.
Polymorphism databases
DMDM	401056.
Proteomic databases
PaxDb	P31213.
PRIDE	P31213.
Protocols and materials databases
DNASU	6716.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6716.
KEGG	hsa:6716.
UCSC	uc002rnw.1. human.
Organism-specific databases
CTD	6716.
GeneCards	GC02M031661.
H-InvDB	HIX0030017.
HGNC	HGNC:11285. SRD5A2.
MIM	264600. phenotype. 607306. gene.
neXtProt	NX_P31213.
Orphanet	753. 46,XY disorder of sex development due to 5-alpha-reductase 2 deficiency. 1331. Familial prostate cancer.
PharmGKB	PA36113.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG282706.
HOVERGEN	HBG003402.
InParanoid	P31213.
KO	K12344.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism. REACT_15493. Steroid hormones.
Gene expression databases
CleanEx	HS_SRD5A2.
Genevestigator	P31213.
GermOnline	ENSG00000049319. Homo sapiens.
Family and domain databases
InterPro	IPR016636. 3-oxo-5-alpha-steroid_4-DH. IPR001104. 3-oxo-5_a-steroid_4-DH_C. [Graphical view]
Pfam	PF02544. Steroid_dh. 1 hit. [Graphical view]
PIRSF	PIRSF015596. 5_alpha-SR2. 1 hit.
PROSITE	PS50244. S5A_REDUCTASE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P31213.
ChEMBL	CHEMBL1856.
ChiTaRS	SRD5A2. human.
DrugBank	DB00548. Azelaic Acid. DB01126. Dutasteride.
GenomeRNAi	6716.
NextBio	26196.
SOURCE	Search...

Entry information

Entry name

S5A2_HUMAN

Accession

Primary (citable) accession number: P31213
Secondary accession number(s): B2RE87, Q2M1R4, Q9BYE6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1993
Last sequence update:	July 1, 1993
Last modified:	May 1, 2013
This is version 130 of the entry and version 1 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.