P05093 (CP17A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	508 AA.
Sequence status	Complete.
Protein existence	Evidence 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.
Catalytic activity	A C(21)-steroid + (reduced NADPH--hemoprotein reductase) + O2 = a 17-alpha-hydroxy-C(21)-steroid + (oxidized NADPH--hemoprotein reductase) + H2O. 17-alpha-hydroxyprogesterone = androst-4-ene-3,17-dione + acetaldehyde.
Cofactor	Heme group.
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.19 Ref.21 Ref.22 Ref.23 Ref.24 Ref.25
Sequence similarities	Belongs to the cytochrome P450 family.

Ontologies

Keywords
Biological process	Steroidogenesis
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Disease	Congenital adrenal hyperplasia Disease mutation
Ligand	Heme Iron Metal-binding
Molecular function	Lyase Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Leydig cell differentiation Inferred from electronic annotation. Source: Compara adrenal gland development Inferred from electronic annotation. Source: Compara androgen biosynthetic process Traceable author statement. Source: Reactome biphenyl metabolic process Inferred from electronic annotation. Source: Compara cellular response to antibiotic Inferred from electronic annotation. Source: Compara cellular response to gonadotropin stimulus Inferred from electronic annotation. Source: Compara cellular response to lipopolysaccharide Inferred from electronic annotation. Source: Compara dibenzo-p-dioxin metabolic process Inferred from electronic annotation. Source: Compara glucocorticoid biosynthetic process Traceable author statement. Source: Reactome hippocampus development Inferred from electronic annotation. Source: Compara ovulation Inferred from electronic annotation. Source: Compara phenol-containing compound metabolic process Inferred from electronic annotation. Source: Compara phthalate metabolic process Inferred from electronic annotation. Source: Compara positive regulation of steroid hormone biosynthetic process Inferred from electronic annotation. Source: Compara response to acetate Inferred from electronic annotation. Source: Compara response to cAMP Inferred from electronic annotation. Source: Compara response to cytokine stimulus Inferred from electronic annotation. Source: Compara response to drug Inferred from electronic annotation. Source: Compara response to fungicide Inferred from electronic annotation. Source: Compara response to herbicide Inferred from electronic annotation. Source: Compara response to insecticide Inferred from electronic annotation. Source: Compara response to ionizing radiation Inferred from electronic annotation. Source: Compara response to methylmercury Inferred from electronic annotation. Source: Compara response to nutrient levels Inferred from electronic annotation. Source: Compara response to retinoic acid Inferred from electronic annotation. Source: Compara response to steroid hormone stimulus Inferred from electronic annotation. Source: Compara sex differentiation Traceable author statement PubMed 9326943. Source: ProtInc small molecule metabolic process Traceable author statement. Source: Reactome xenobiotic metabolic process Traceable author statement. Source: Reactome
Cellular_component	axon Inferred from electronic annotation. Source: Compara endoplasmic reticulum membrane Traceable author statement. Source: Reactome mitochondrion Inferred from electronic annotation. Source: Compara neuronal cell body Inferred from electronic annotation. Source: Compara
Molecular_function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: InterPro oxygen binding Traceable author statement Ref.11. Source: ProtInc steroid 17-alpha-monooxygenase activity Traceable author statement PubMed 1347802. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 508

508

Steroid 17-alpha-hydroxylase/17,20 lyase

PRO_0000051931

Sites

Metal binding

442

1

Iron (heme axial ligand)

Natural variations

Natural variant

22

1

C → W.
Corresponds to variant rs762563 [ dbSNP | Ensembl ].

VAR_011755

Natural variant

35

1

P → L in AH5; 38% 17alpha-hydroxylase activity and 33% 17,20-lyase activity. Ref.21

VAR_022745

Natural variant

53

1

Missing in AH5; 10% 17alpha-hydroxylase activity and 13% 17,20-lyase activity. Ref.11 Ref.21

VAR_001270

Natural variant

64

1

Y → S in AH5. Ref.15

VAR_001271

Natural variant

93

1

F → C in AH5. Ref.23

VAR_013147

Natural variant

96

1

R → W in AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities. Ref.19 Ref.21 Ref.25

VAR_022746

Natural variant

106

1

S → P in AH5. Ref.12

VAR_001272

Natural variant

112

1

I → II in AH5. Ref.15

VAR_001273

Natural variant

114

1

F → V in AH5. Ref.24

VAR_022747

Natural variant

116

1

D → V in AH5. Ref.24

VAR_022748

Natural variant

177

1

N → D in AH5; 10% 17alpha-hydroxylase and 17,20-lyase activities. Ref.21

VAR_022749

Natural variant

329

1

Y → D in AH5. Ref.25

VAR_022750

Natural variant

330

1

Missing in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities. Ref.21

VAR_022751

Natural variant

342

1

P → T in AH5. Ref.14

VAR_001274

Natural variant

347

1

R → C in AH5. Ref.24

VAR_022752

Natural variant

347

1

R → H in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. Ref.19 Ref.22 Ref.24

VAR_001275

Natural variant

358

1

R → Q in AH5; selectively ablates 17,20-lyase activity, while preserving most 17alpha-hydroxylase activity. Ref.19 Ref.22

VAR_001276

Natural variant

362

1

R → C in AH5. Ref.25

VAR_022753

Natural variant

373

1

H → L in AH5. Ref.16

VAR_001277

Natural variant

406

1

W → R in AH5. Ref.25

VAR_022754

Natural variant

417

1

F → 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 variant

428

1

P → L in AH5. Ref.25

VAR_022756

Natural variant

440

1

R → H in AH5. Ref.18

VAR_001278

Natural variant

487 – 489

3

Missing in AH5.

VAR_001279

Natural variant

496

1

R → C in AH5. Ref.13

VAR_001280

Natural variant

496

1

R → H in AH5; 30% 17alpha-hydroxylase activity and 29% 17,20-lyase activity. Ref.21

VAR_022757

Secondary structure

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508

Helix Strand Turn

Details...

Beta strand

36 – 42

7

Helix

49 – 55

7

Helix

57 – 60

4

Beta strand

62 – 68

7

Beta strand

71 – 76

6

Helix

79 – 86

8

Turn

87 – 93

7

Helix

100 – 105

6

Turn

106 – 109

4

Beta strand

111 – 115

5

Helix

119 – 131

13

Turn

132 – 135

4

Beta strand

136 – 138

3

Helix

142 – 159

18

Turn

160 – 162

3

Beta strand

163 – 165

3

Helix

168 – 184

17

Helix

194 – 209

16

Beta strand

211 – 214

4

Helix

220 – 222

3

Helix

228 – 250

23

Turn

251 – 253

3

Helix

262 – 271

10

Helix

285 – 287

3

Helix

289 – 320

32

Helix

322 – 335

14

Beta strand

338 – 340

3

Helix

344 – 348

5

Helix

351 – 363

13

Beta strand

376 – 381

6

Beta strand

384 – 386

3

Beta strand

391 – 394

4

Helix

396 – 401

6

Turn

403 – 405

3

Beta strand

406 – 408

3

Helix

414 – 417

4

Beta strand

422 – 425

4

Helix

438 – 440

3

Helix

445 – 462

18

Beta strand

463 – 466

4

Beta strand

479 – 485

7

Beta strand

491 – 495

5

Helix

497 – 501

5

Sequences

	Sequence		Length	Mass (Da)
	P05093 [UniParc]. Last modified August 13, 1987. Version 1. Checksum: E5454E9E18F96B0E	FASTA	508	57,371
	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

References

	« Hide 'large scale' referencesShow '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. , 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 , 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.

IPI

IPI00006665.

PIR

A26366. A40921.

RefSeq

NP_000093.1. NM_000102.3.

UniGene

Hs.438016.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C17	model	-	A	48-501	[»]
3RUK	X-ray	2.60	A/B/C/D	24-508	[»]
3SWZ	X-ray	2.40	A/B/C/D	24-508	[»]

ProteinModelPortal

P05093.

ModBase

Search...

Protein-protein interaction databases

IntAct

P05093. 6 interactions.

STRING

9606.ENSP00000358903.

PTM databases

PhosphoSite

P05093.

Polymorphism databases

DMDM

117283.

Proteomic databases

PaxDb

P05093.

PRIDE

P05093.

Protocols and materials databases

DNASU

1586.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000369887; ENSP00000358903; ENSG00000148795.

GeneID

1586.

KEGG

hsa:1586.

UCSC

uc001kwg.3. human.

Organism-specific databases

CTD

1586.

GeneCards

GC10M104580.

HGNC

HGNC:2593. CYP17A1.

HPA

HPA048533.

MIM

202110. phenotype.
609300. gene.

neXtProt

NX_P05093.

Orphanet

90796. 46,XY disorder of sex development due to isolated 17, 20 lyase deficiency.
90793. Congenital adrenal hyperplasia due to 17-alpha-hydroxylase deficiency.

PharmGKB

PA27090.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2124.

HOGENOM

HOG000036991.

HOVERGEN

HBG106944.

InParanoid

P05093.

KO

K00512.

OMA

NVISLIC.

OrthoDB

EOG4W9J45.

PhylomeDB

P05093.

Enzyme and pathway databases

BioCyc

MetaCyc:HS07560-MONOMER.

Reactome

REACT_111217. Metabolism.
REACT_15493. Steroid hormones.

SABIO-RK

P05093.

UniPathway

UPA00062.

Gene expression databases

ArrayExpress

P05093.

Bgee

P05093.

CleanEx

HS_CYP17A1.

Genevestigator

P05093.

GermOnline

ENSG00000148795. Homo sapiens.

Family and domain databases

Gene3D

1.10.630.10. 1 hit.

InterPro

IPR001128. Cyt_P450.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR00385. P450.

SUPFAM

SSF48264. Cytochrome_P450. 1 hit.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P05093.

ChEMBL

CHEMBL3522.

ChiTaRS

CYP17A1. human.

DrugBank

DB00157. NADH.
DB00396. Progesterone.

GenomeRNAi

1586.

NextBio

6519.

SOURCE

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Entry information

Entry name

CP17A_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 153 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.