Reviewed, UniProtKB/Swiss-Prot P05093 (CP17A_HUMAN)

Names and origin

Protein names

Recommended name:
    Steroid 17-alpha-hydroxylase/17,20 lyase
    EC=1.14.99.9
Alternative name(s):
    Cytochrome P450 17A1
    CYPXVII
    P450-C17
      Short name=P450c17
    Steroid 17-alpha-monooxygenase

Gene names

Name:	CYP17A1
Synonyms:	CYP17, S17AH

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	508 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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 steroid + AH2 + O2 = a 17-alpha-hydroxysteroid + A + H2O.
Cofactor	Heme group.
Enzyme regulation	Regulated predominantly by intracellular cAMP levels.
Pathway	Lipid metabolism; steroid biosynthesis.
Subcellular location	Membrane Potential. Membrane; Single-pass membrane protein.
Post-translational modification	Phosphorylation is necessary for 17,20-lyase, but not for 17-alpha-hydroxylase activity.
Involvement in disease	Defects in CYP17A1 are the cause of adrenal hyperplasia type 5 (AH5) [MIM:202110]. AH5 is 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). Ref.10 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
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	Monooxygenase Oxidoreductase
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	C21-steroid hormone biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW sex differentiation Traceable author statement. Source: ProtInc
Cellular component	endoplasmic reticulum membrane Ref.9 Inferred from Experiment. Source: Reactome
Molecular function	electron carrier activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro oxygen binding Ref.10 Traceable author statement. Source: ProtInc steroid 17-alpha-monooxygenase activity Ref.9 Inferred from Experiment. Source: Reactome
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: dbSNP rs762563.

VAR_011755

Natural variant

35

1

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

VAR_022745

Natural variant

53

1

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

VAR_001270

Natural variant

64

1

Y → S in AH5. Ref.14

VAR_001271

Natural variant

93

1

F → C in AH5. Ref.22

VAR_013147

Natural variant

96

1

R → W in AH5; 25% of both 17alpha-hydroxylase and 17,20-lyase activities. Ref.18 Ref.20 Ref.24

VAR_022746

Natural variant

106

1

S → P in AH5. Ref.11

VAR_001272

Natural variant

112

1

I → II in AH5. Ref.14

VAR_001273

Natural variant

114

1

F → V in AH5. Ref.23

VAR_022747

Natural variant

116

1

D → V in AH5. Ref.23

VAR_022748

Natural variant

177

1

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

VAR_022749

Natural variant

329

1

Y → D in AH5. Ref.24

VAR_022750

Natural variant

330

1

Missing in AH5; complete loss of both 17alpha-hydroxylase and 17,20-lyase activities. Ref.14 Ref.20

VAR_022751

Natural variant

342

1

P → T in AH5. Ref.13

VAR_001274

Natural variant

347

1

R → C in AH5. Ref.19 Ref.21 Ref.23

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.21 Ref.23

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.21

VAR_001276

Natural variant

362

1

R → C in AH5. Ref.24

VAR_022753

Natural variant

373

1

H → L in AH5. Ref.15

VAR_001277

Natural variant

406

1

W → R in AH5. Ref.24

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.20 Ref.21

VAR_022755

Natural variant

428

1

P → L in AH5. Ref.24

VAR_022756

Natural variant

440

1

R → H in AH5. Ref.14 Ref.17

VAR_001278

Natural variant

487 – 489

3

Missing in AH5. Ref.16

VAR_001279

Natural variant

496

1

R → C in AH5. Ref.12 Ref.20

VAR_001280

Natural variant

496

1

R → H in AH5; 30% 17alpha-hydroxylase activity and 29% 17,20-lyase activity. Ref.12 Ref.20

VAR_022757

Secondary structure

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508

Helix Strand Turn

Details...

Helix

49 – 51

3

Helix

52 – 55

4

Turn

56 – 59

4

Beta strand

62 – 68

7

Beta strand

71 – 76

6

Helix

79 – 82

4

Helix

83 – 85

3

Turn

89 – 91

3

Helix

99 – 107

9

Helix

111 – 113

3

Helix

119 – 129

11

Turn

130 – 132

3

Helix

135 – 138

4

Beta strand

139 – 142

4

Helix

144 – 150

7

Turn

151 – 153

3

Helix

154 – 159

6

Beta strand

160 – 163

4

Helix

170 – 183

14

Turn

189 – 191

3

Helix

193 – 204

12

Helix

206 – 208

3

Turn

209 – 212

4

Helix

227 – 240

14

Helix

243 – 251

9

Turn

260 – 262

3

Helix

263 – 268

6

Turn

269 – 271

3

Beta strand

278 – 281

4

Helix

289 – 301

13

Helix

303 – 318

16

Helix

322 – 328

7

Turn

329 – 331

3

Helix

332 – 335

4

Beta strand

338 – 340

3

Helix

345 – 348

4

Helix

352 – 363

12

Beta strand

366 – 368

3

Beta strand

373 – 377

5

Turn

381 – 383

3

Beta strand

391 – 394

4

Helix

396 – 399

4

Helix

403 – 406

4

Beta strand

407 – 411

5

Helix

414 – 416

3

Beta strand

418 – 422

5

Beta strand

424 – 426

3

Beta strand

434 – 437

4

Helix

445 – 462

18

Beta strand

481 – 483

3

Sequences

	Sequence		Length	Mass (Da)
	P05093-1 [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: 3025870] [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: 3500022] [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: 3274893] [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: 1964490] [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: 2843762] [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: 15164054] [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: 15489334] [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: 10406467] [Abstract] Cited for: 3D-STRUCTURE MODELING OF 48-501.
[10]	"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: 2808364] [Abstract] Cited for: VARIANT AH5 PHE-53 DEL.
[11]	"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: 1714904] [Abstract] Cited for: VARIANT AH5 PRO-106.
[12]	"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: 1515452] [Abstract] Cited for: VARIANT AH5 CYS-496.
[13]	"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: 1740503] [Abstract] Cited for: VARIANT AH5 THR-342.
[14]	"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: 8396144] [Abstract] Cited for: VARIANTS AH5 SER-64 AND ILE-112 INS.
[15]	"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: 8245018] [Abstract] Cited for: VARIANT AH5 LEU-373.
[16]	"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: 8345056] [Abstract] Cited for: VARIANT AH5 487-ASP--PHE-489 DEL.
[17]	"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: 8027220] [Abstract] Cited for: VARIANT AH5 HIS-440.
[18]	"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: 8550762] [Abstract] Cited for: VARIANT AH5 TRP-96.
[19]	"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.
[20]	"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: 10720067] [Abstract] Cited for: VARIANTS AH5 LEU-35; PHE-53 DEL; TRP-96; ASP-177; GLU-330 DEL; CYS-417 AND HIS-496, PHOSPHORYLATION.
[21]	"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: 11549685] [Abstract] Cited for: VARIANTS AH5 HIS-347; GLN-358 AND CYS-417.
[22]	"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: 11836339] [Abstract] Cited for: VARIANT AH5 CYS-93.
[23]	"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: 12466376] [Abstract] Cited for: VARIANTS AH5 VAL-114; VAL-116; CYS-347 AND HIS-347.
[24]	"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: 14671162] [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

EMBLGenBankDDBJ

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.

UniGene

Hs.438016

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2C17	model	-	A	48-501	[»]

ModBase

Search...

PTM databases

PhosphoSite

P05093.

Genome annotation databases

Ensembl

ENSG00000148795. Homo sapiens. [Contig view]

GeneID

1586.

KEGG

hsa:1586.

Organism-specific databases

GeneCards

GC10M104580.

H-InvDB

HIX0009168.

HGNC

HGNC:2593. CYP17A1.

MIM

202110. phenotype.
609300. gene.

Orphanet

418. Congenital adrenal hyperplasia.

PharmGKB

PA27090.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P05093.

HOVERGEN

P05093.

OMA

P05093. LATHNGQ.

Enzyme and pathway databases

BRENDA

1.14.99.9. 247.

Reactome

REACT_13433. Biological oxidations.
REACT_602. Lipid and lipoprotein metabolism.

Gene expression databases

ArrayExpress

P05093.

Bgee

P05093.

CleanEx

HS_CYP17A1.

GermOnline

ENSG00000148795. Homo sapiens.

Family and domain databases

InterPro

IPR001128. Cyt_P450.
IPR017973. Cyt_P450_C.
IPR017972. Cyt_P450_CS.
IPR002401. Cyt_P450_E_grp-I.
[Graphical view]

Gene3D

G3DSA:1.10.630.10. Cyt_P450. 1 hit.

PANTHER

PTHR19383. Cyt_P450. 1 hit.

Pfam

PF00067. p450. 1 hit.
[Graphical view]

PRINTS

PR00463. EP450I.
PR00385. P450.

PROSITE

PS00086. CYTOCHROME_P450. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00157. NADH.
DB00396. Progesterone.

NextBio

6519.

SOURCE

Search...

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:	June 16, 2009
This is version 114 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)