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P05093 (CP17A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 164. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Steroid 17-alpha-hydroxylase/17,20 lyase

EC=1.14.99.9
EC=4.1.2.30
Alternative name(s):
17-alpha-hydroxyprogesterone aldolase
CYPXVII
Cytochrome P450 17A1
Cytochrome P450-C17
Short name=Cytochrome P450c17
Steroid 17-alpha-monooxygenase
Gene names
Name:CYP17A1
Synonyms:CYP17, S17AH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length508 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Conversion of pregnenolone and progesterone to their 17-alpha-hydroxylated products and subsequently to dehydroepiandrosterone (DHEA) and androstenedione. Catalyzes both the 17-alpha-hydroxylation and the 17,20-lyase reaction. Involved in sexual development during fetal life and at puberty. Ref.10

Catalytic activity

A C(21)-steroid + (reduced NADPH--hemoprotein reductase) + O2 = a 17-alpha-hydroxy-C(21)-steroid + (oxidized NADPH--hemoprotein reductase) + H2O. Ref.10

17-alpha-hydroxyprogesterone = androst-4-ene-3,17-dione + acetaldehyde. Ref.10

Cofactor

Heme group. Ref.10

Enzyme regulation

Regulated predominantly by intracellular cAMP levels.

Pathway

Lipid metabolism; steroid biosynthesis.

Subcellular location

Membrane Potential.

Post-translational modification

Phosphorylation is necessary for 17,20-lyase, but not for 17-alpha-hydroxylase activity.

Involvement in disease

Adrenal hyperplasia 5 (AH5) [MIM:202110]: A form of congenital adrenal hyperplasia, a common recessive disease due to defective synthesis of cortisol. Congenital adrenal hyperplasia is characterized by androgen excess leading to ambiguous genitalia in affected females, rapid somatic growth during childhood in both sexes with premature closure of the epiphyses and short adult stature. Four clinical types: 'salt wasting' (SW, the most severe type), 'simple virilizing' (SV, less severely affected patients), with normal aldosterone biosynthesis, 'non-classic form' or late-onset (NC or LOAH)and 'cryptic' (asymptomatic).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25

Sequence similarities

Belongs to the cytochrome P450 family.

Ontologies

Keywords
   Biological processSteroidogenesis
   Cellular componentMembrane
   Coding sequence diversityPolymorphism
   DiseaseCongenital adrenal hyperplasia
Disease mutation
   LigandHeme
Iron
Metal-binding
   Molecular functionLyase
Monooxygenase
Oxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processLeydig cell differentiation

Inferred from electronic annotation. Source: Ensembl

adrenal gland development

Inferred from electronic annotation. Source: Ensembl

androgen biosynthetic process

Traceable author statement. Source: Reactome

biphenyl metabolic process

Inferred from electronic annotation. Source: Ensembl

cellular response to antibiotic

Inferred from electronic annotation. Source: Ensembl

cellular response to gonadotropin stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

dibenzo-p-dioxin metabolic process

Inferred from electronic annotation. Source: Ensembl

glucocorticoid biosynthetic process

Traceable author statement. Source: Reactome

hippocampus development

Inferred from electronic annotation. Source: Ensembl

hormone biosynthetic process

Inferred from direct assay Ref.10. Source: UniProtKB

ovulation

Inferred from electronic annotation. Source: Ensembl

phenol-containing compound metabolic process

Inferred from electronic annotation. Source: Ensembl

phthalate metabolic process

Inferred from electronic annotation. Source: Ensembl

positive regulation of steroid hormone biosynthetic process

Inferred from electronic annotation. Source: Ensembl

progesterone metabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

response to acetate

Inferred from electronic annotation. Source: Ensembl

response to cAMP

Inferred from electronic annotation. Source: Ensembl

response to cytokine

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to fungicide

Inferred from electronic annotation. Source: Ensembl

response to herbicide

Inferred from electronic annotation. Source: Ensembl

response to insecticide

Inferred from electronic annotation. Source: Ensembl

response to ionizing radiation

Inferred from electronic annotation. Source: Ensembl

response to methylmercury

Inferred from electronic annotation. Source: Ensembl

response to nutrient levels

Inferred from electronic annotation. Source: Ensembl

response to retinoic acid

Inferred from electronic annotation. Source: Ensembl

response to steroid hormone

Inferred from electronic annotation. Source: Ensembl

sex differentiation

Traceable author statement PubMed 9326943. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

steroid biosynthetic process

Traceable author statement Ref.2. Source: ProtInc

steroid metabolic process

Inferred from direct assay Ref.10. Source: UniProtKB

sterol metabolic process

Traceable author statement. Source: Reactome

xenobiotic metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentaxon

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Non-traceable author statement PubMed 9326943. Source: ProtInc

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_function17-alpha-hydroxyprogesterone aldolase activity

Inferred from electronic annotation. Source: UniProtKB-EC

heme binding

Inferred from direct assay Ref.10. Source: UniProtKB

iron ion binding

Inferred from electronic annotation. Source: InterPro

oxygen binding

Traceable author statement Ref.11. Source: ProtInc

steroid 17-alpha-monooxygenase activity

Inferred from direct assay Ref.10. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 508508Steroid 17-alpha-hydroxylase/17,20 lyase
PRO_0000051931

Sites

Metal binding4421Iron (heme axial ligand)

Natural variations

Natural variant221C → W.
Corresponds to variant rs762563 [ dbSNP | Ensembl ].
VAR_011755
Natural variant351P → L in AH5; 38% 17alpha-hydroxylase activity and 33% 17,20-lyase activity. Ref.21
VAR_022745
Natural variant531Missing in AH5; 10% 17alpha-hydroxylase activity and 13% 17,20-lyase activity. Ref.11 Ref.21
VAR_001270
Natural variant641Y → S in AH5. Ref.15
VAR_001271
Natural variant931F → C in AH5. Ref.23
VAR_013147
Natural variant961R → W in AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities. Ref.19 Ref.21 Ref.25
VAR_022746
Natural variant1061S → P in AH5. Ref.12
VAR_001272
Natural variant1121I → II in AH5. Ref.15
VAR_001273
Natural variant1141F → V in AH5. Ref.24
VAR_022747
Natural variant1161D → V in AH5. Ref.24
VAR_022748
Natural variant1771N → D in AH5; 10% 17alpha-hydroxylase and 17,20-lyase activities. Ref.21
VAR_022749
Natural variant3291Y → D in AH5. Ref.25
Corresponds to variant rs104894144 [ dbSNP | Ensembl ].
VAR_022750
Natural variant3301Missing in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities. Ref.21
VAR_022751
Natural variant3421P → T in AH5. Ref.14
VAR_001274
Natural variant3471R → C in AH5. Ref.24
VAR_022752
Natural variant3471R → H in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. Ref.20 Ref.22 Ref.24
VAR_001275
Natural variant3581R → Q in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. Ref.20 Ref.22
VAR_001276
Natural variant3621R → C in AH5. Ref.25
VAR_022753
Natural variant3731H → L in AH5. Ref.16
VAR_001277
Natural variant4061W → R in AH5. Ref.25
VAR_022754
Natural variant4171F → C in AH5; ablates both 17,20-lyase activity and 17alpha-hydroxylase activity; loss of heme-binding and loss of phosphorylation. Ref.21 Ref.22
VAR_022755
Natural variant4281P → L in AH5. Ref.25
VAR_022756
Natural variant4401R → H in AH5. Ref.18
VAR_001278
Natural variant487 – 4893Missing in AH5.
VAR_001279
Natural variant4961R → C in AH5. Ref.13
VAR_001280
Natural variant4961R → H in AH5; 30% 17alpha-hydroxylase activity and 29% 17,20-lyase activity. Ref.21
VAR_022757

Secondary structure

.............................................................................. 508
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05093 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: E5454E9E18F96B0E

FASTA50857,371
        10         20         30         40         50         60 
MWELVALLLL TLAYLFWPKR RCPGAKYPKS LLSLPLVGSL PFLPRHGHMH NNFFKLQKKY 

        70         80         90        100        110        120 
GPIYSVRMGT KTTVIVGHHQ LAKEVLIKKG KDFSGRPQMA TLDIASNNRK GIAFADSGAH 

       130        140        150        160        170        180 
WQLHRRLAMA TFALFKDGDQ KLEKIICQEI STLCDMLATH NGQSIDISFP VFVAVTNVIS 

       190        200        210        220        230        240 
LICFNTSYKN GDPELNVIQN YNEGIIDNLS KDSLVDLVPW LKIFPNKTLE KLKSHVKIRN 

       250        260        270        280        290        300 
DLLNKILENY KEKFRSDSIT NMLDTLMQAK MNSDNGNAGP DQDSELLSDN HILTTIGDIF 

       310        320        330        340        350        360 
GAGVETTTSV VKWTLAFLLH NPQVKKKLYE EIDQNVGFSR TPTISDRNRL LLLEATIREV 

       370        380        390        400        410        420 
LRLRPVAPML IPHKANVDSS IGEFAVDKGT EVIINLWALH HNEKEWHQPD QFMPERFLNP 

       430        440        450        460        470        480 
AGTQLISPSV SYLPFGAGPR SCIGEILARQ ELFLIMAWLL QRFDLEVPDD GQLPSLEGIP 

       490        500 
KVVFLIDSFK VKIKVRQAWR EAQAEGST 

« Hide

References

« Hide 'large scale' references
[1]"Cytochrome P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): cloning of human adrenal and testis cDNAs indicates the same gene is expressed in both tissues."
Chung B.-C., Picado-Leonard J., Haniu M., Bienkowski M., Hall P.F., Shively J.E., Miller W.L.
Proc. Natl. Acad. Sci. U.S.A. 84:407-411(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and sequence of the human gene for P450c17 (steroid 17 alpha-hydroxylase/17,20 lyase): similarity with the gene for P450c21."
Picado-Leonard J., Miller W.L.
DNA 6:439-448(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Characterization of complementary deoxyribonucleic acid for human adrenocortical 17 alpha-hydroxylase: a probe for analysis of 17 alpha-hydroxylase deficiency."
Bradshaw K.D., Waterman M.R., Couch R.T., Simpson E.R., Zuber M.X.
Mol. Endocrinol. 1:348-354(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]"Tissue-specific, cyclic adenosine 3',5'-monophosphate-induced, and phorbol ester-repressed transcription from the human P450c17 promoter in mouse cells."
Brentano S.T., Picado-Leonard J., Mellon S.H., Moore C.C., Miller W.L.
Mol. Endocrinol. 4:1972-1979(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"Structural characterization of normal and mutant human steroid 17 alpha-hydroxylase genes: molecular basis of one example of combined 17 alpha-hydroxylase/17,20 lyase deficiency."
Kagimoto M., Winter J.S.D., Kagimoto K., Simpson E.R., Waterman M.R.
Mol. Endocrinol. 2:564-570(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[6]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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].
Tissue: Brain.
[9]"Molecular modeling of human P450c17 (17alpha-hydroxylase/17,20-lyase): insights into reaction mechanisms and effects of mutations."
Auchus R.J., Miller W.L.
Mol. Endocrinol. 13:1169-1182(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: 3D-STRUCTURE MODELING OF 48-501.
[10]"Structures of cytochrome P450 17A1 with prostate cancer drugs abiraterone and TOK-001."
DeVore N.M., Scott E.E.
Nature 482:116-119(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 24-508 IN COMPLEXES WITH HEME; ABIRATERONE AND TOK-001, FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
[11]"Deletion of a phenylalanine in the N-terminal region of human cytochrome P-450(17 alpha) results in partial combined 17 alpha-hydroxylase/17,20-lyase deficiency."
Yanase T., Kagimoto M., Suzuki S., Hashiba K., Simpson E.R., Waterman M.R.
J. Biol. Chem. 264:18076-18082(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 PHE-53 DEL.
[12]"Missense mutation serine106-->proline causes 17 alpha-hydroxylase deficiency."
Lin D., Harikrishna J.A., Moore C.C.D., Jones K.L., Miller W.L.
J. Biol. Chem. 266:15992-15998(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 PRO-106.
[13]"Molecular basis of apparent isolated 17,20-lyase deficiency: compound heterozygous mutations in the C-terminal region (Arg(496)-->Cys, Gln(461)-->Stop) actually cause combined 17 alpha-hydroxylase/17,20-lyase deficiency."
Yanase T., Waterman M.R., Zachmann M., Winter J.S.D., Kagimoto M.
Biochim. Biophys. Acta 1139:275-279(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 CYS-496.
[14]"Compound heterozygous mutations (Arg 239-->Stop, Pro 342-->Thr) in the CYP17 (P45017 alpha) gene lead to ambiguous external genitalia in a male patient with partial combined 17 alpha-hydroxylase/17,20-lyase deficiency."
Ahlgren R., Yanase T., Simpson E.R., Winter J.S.D., Waterman M.R.
J. Clin. Endocrinol. Metab. 74:667-672(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 THR-342.
[15]"Expression and purification of functional human 17 alpha-hydroxylase/17,20-lyase (P450c17) in Escherichia coli. Use of this system for study of a novel form of combined 17 alpha-hydroxylase/17,20-lyase deficiency."
Imai T., Globerman H., Gertner J.M., Kagawa N., Waterman M.R.
J. Biol. Chem. 268:19681-19689(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH5 SER-64 AND ILE-112 INS.
[16]"Mutation of histidine 373 to leucine in cytochrome P450c17 causes 17 alpha-hydroxylase deficiency."
Monno S., Ogawa H., Date T., Fujioka M., Miller W.L., Kobayashi M.
J. Biol. Chem. 268:25811-25817(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 LEU-373.
[17]"Deletion of amino acids Asp487-Ser488-Phe489 in human cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency."
Fardella C.E., Zhang L.H., Mahacholklertwattana P., Lin D., Miller W.L.
J. Clin. Endocrinol. Metab. 77:489-493(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 487-ASP--PHE-489 DEL.
[18]"Point mutation of Arg440 to His in cytochrome P450c17 causes severe 17 alpha-hydroxylase deficiency."
Fardella C.E., Hum D.W., Homoki J., Miller W.L.
J. Clin. Endocrinol. Metab. 79:160-164(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 HIS-440.
[19]"Mutation R96W in cytochrome P450c17 gene causes combined 17 alpha-hydroxylase/17-20-lyase deficiency in two French Canadian patients."
Laflamme N., Leblanc J.-F., Mailloux J., Faure N., Labrie F., Simard J.
J. Clin. Endocrinol. Metab. 81:264-268(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 TRP-96.
[20]"The molecular basis of isolated 17,20 lyase deficiency."
Geller D.H., Mendonca B.B., Miller W.L.
Pediatr. Res. 39:89A-89A(1996)
Cited for: VARIANTS AH5 HIS-347 AND GLN-358.
[21]"17alpha-hydroxylase/17,20-lyase deficiency as a model to study enzymatic activity regulation: role of phosphorylation."
Biason-Lauber A., Kempken B., Werder E., Forest M.G., Einaudi S., Ranke M.B., Matsuo N., Brunelli V., Schoenle E.J., Zachmann M.
J. Clin. Endocrinol. Metab. 85:1226-1231(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH5 LEU-35; PHE-53 DEL; TRP-96; ASP-177; GLU-330 DEL; CYS-417 AND HIS-496, PHOSPHORYLATION.
[22]"Pitfalls in characterizing P450c17 mutations associated with isolated 17,20-lyase deficiency."
Gupta M.K., Geller D.H., Auchus R.J.
J. Clin. Endocrinol. Metab. 86:4416-4423(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH5 HIS-347; GLN-358 AND CYS-417.
[23]"Combined 17alpha-hydroxylase/17,20-lyase deficiency caused by Phe93Cys mutation in the CYP17 gene."
Di Cerbo A., Biason-Lauber A., Savino M., Piemontese M.R., Di Giorgio A., Perona M., Savoia A.
J. Clin. Endocrinol. Metab. 87:898-905(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT AH5 CYS-93.
[24]"Differential inhibition of 17alpha-hydroxylase and 17,20-lyase activities by three novel missense CYP17 mutations identified in patients with P450c17 deficiency."
Van Den Akker E.L.T., Koper J.W., Boehmer A.L.M., Themmen A.P.N., Verhoef-Post M., Timmerman M.A., Otten B.J., Drop S.L.S., De Jong F.H.
J. Clin. Endocrinol. Metab. 87:5714-5721(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH5 VAL-114; VAL-116; CYS-347 AND HIS-347.
[25]"P450c17 deficiency in Brazilian patients: biochemical diagnosis through progesterone levels confirmed by CYP17 genotyping."
Martin R.M., Lin C.J., Costa E.M.F., de Oliveira M.L., Carrilho A., Villar H., Longui C.A., Mendonca B.B.
J. Clin. Endocrinol. Metab. 88:5739-5746(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS AH5 TRP-96; ASP-329; CYS-362; ARG-406 AND LEU-428.
+Additional computationally mapped references.

Web resources

SHMPD

The Singapore human mutation and polymorphism database

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14564 mRNA. Translation: AAA52151.1.
M19489 Genomic DNA. Translation: AAA36405.1.
M63871 Genomic DNA. Translation: AAA59984.1.
M31153 expand/collapse EMBL AC list , M31146, M31147, M31148, M31149, M31150, M31151, M31152 Genomic DNA. Translation: AAA52140.1. Sequence problems.
BT020000 mRNA. Translation: AAV38803.1.
AL358790 Genomic DNA. Translation: CAI52498.1.
BC062997 mRNA. Translation: AAH62997.1.
BC063388 mRNA. Translation: AAH63388.1.
PIRA26366. A40921.
RefSeqNP_000093.1. NM_000102.3.
UniGeneHs.438016.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2C17model-A48-501[»]
3RUKX-ray2.60A/B/C/D24-508[»]
3SWZX-ray2.40A/B/C/D24-508[»]
ProteinModelPortalP05093.
SMRP05093. Positions 31-503.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107958. 7 interactions.
IntActP05093. 6 interactions.
STRING9606.ENSP00000358903.

Chemistry

BindingDBP05093.
ChEMBLCHEMBL3522.
DrugBankDB00157. NADH.
DB00396. Progesterone.
GuidetoPHARMACOLOGY1361.

PTM databases

PhosphoSiteP05093.

Polymorphism databases

DMDM117283.

Proteomic databases

PaxDbP05093.
PRIDEP05093.

Protocols and materials databases

DNASU1586.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000369887; ENSP00000358903; ENSG00000148795.
GeneID1586.
KEGGhsa:1586.
UCSCuc001kwg.3. human.

Organism-specific databases

CTD1586.
GeneCardsGC10M104580.
HGNCHGNC:2593. CYP17A1.
HPAHPA048533.
MIM202110. phenotype.
609300. gene.
neXtProtNX_P05093.
Orphanet90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
90793. Congenital adrenal hyperplasia due to 17-alpha-hydroxylase deficiency.
PharmGKBPA27090.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG2124.
HOGENOMHOG000036991.
HOVERGENHBG106944.
InParanoidP05093.
KOK00512.
OMAQELFLIM.
OrthoDBEOG7RBZ85.
PhylomeDBP05093.
TreeFamTF105095.

Enzyme and pathway databases

BioCycMetaCyc:HS07560-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_15493. Steroid hormones.
SABIO-RKP05093.
UniPathwayUPA00062.

Gene expression databases

ArrayExpressP05093.
BgeeP05093.
CleanExHS_CYP17A1.
GenevestigatorP05093.

Family and domain databases

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

ChiTaRSCYP17A1. human.
GeneWikiCYP17A1.
GenomeRNAi1586.
NextBio6519.
PROP05093.
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Entry information

Entry nameCP17A_HUMAN
AccessionPrimary (citable) accession number: P05093
Secondary accession number(s): Q5TZV7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 164 of the entry and version 1 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

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 10

Human chromosome 10: entries, gene names and cross-references to MIM