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Protein Page:
CYP17A1 (rat)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
CYP17A1 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. Defects in CYP17A1 are the cause of adrenal hyperplasia type 5 (AH5). 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). Belongs to the cytochrome P450 family. Note: This description may include information from UniProtKB.
Protein type: EC 1.14.99.9; Oxidoreductase; Lipid Metabolism - C21-steroid hormone
Cellular Component: cell projection; membrane; intracellular membrane-bound organelle; cell soma; mitochondrion; endoplasmic reticulum; axon
Molecular Function: 17-alpha-hydroxyprogesterone aldolase activity; steroid 17-alpha-monooxygenase activity; iron ion binding; heme binding
Biological Process: steroid metabolic process; response to cAMP; dibenzo-p-dioxin metabolic process; response to toxin; androgen biosynthetic process; progesterone metabolic process; response to insecticide; response to organic cyclic substance; response to organic substance; organic acid metabolic process; Leydig cell differentiation; biphenyl metabolic process; response to methylmercury; hormone biosynthetic process; response to nutrient levels; response to drug; response to retinoic acid; adrenal gland development; male gonad development; hippocampus development; phthalate metabolic process; response to herbicide; ovulation; response to acetate; response to steroid hormone stimulus; response to cytokine stimulus; response to ionizing radiation; glucocorticoid biosynthetic process; steroid biosynthetic process; phenol metabolic process
Reference #:  P11715 (UniProtKB)
Alt. Names/Synonyms: CP17A; Cyp17; Cyp17a1; CYPXVII; Cytochrome P450 17A1; cytochrome P450, family 17, subfamily a, polypeptide 1; cytochrome P450, subfamily 17; Cytochrome P450, subfamily XVII; Cytochrome P450-C17; Cytochrome P450c17; P450-C17; P450c17; Steroid 17-alpha-hydroxylase/17,20 lyase
Gene Symbols: Cyp17a1
Molecular weight: 57,250 Da
Basal Isoelectric point: 6.93  Predict pI for various phosphorylation states
Select Structure to View Below

CYP17A1

Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       rat

 
0 1 Y60 FFKLQEKYGPIYSLR
0 2 T70 IYSLRLGTTTTVIIG
0 1 T72 SLRLGTTTTVIIGHY
0 1 K232 NKGLEVIKGYAKVRN
0 1 A235 LEVIKGYAKVRNEVL
0 1 K248 VLTGIFEKCREKFDS
0 1 K252 IFEKCREKFDSQSIS
2 0 S257 REKFDSQSISSLTDI
0 2 Q328 PEVKKKIQKEIDQYV
0 2 K329 EVKKKIQKEIDQYVG
0 1 M499 ITVRQAWMDAQAEVS
  human

 
Y60-p FFKLQKKyGPIYSVR
T70-p IYSVRMGtKtTVIVG
T72-p SVRMGtKtTVIVGHH
K233 NKTLEKLKSHVKIRN
V236 LEKLKSHVKIRNDLL
N249 LLNKILENYKEKFRS
K253 ILENYKEKFRSDsIT
S258-p KEKFRSDsITNMLDT
Y329-p PQVKKKLyEEIDQNV
E330 QVKKKLyEEIDQNVG
R500 IKVRQAWREAQAEGS
  mouse

 
Y60 FFKLQEKYGPIYSLR
T70 IYSLRLGTTTAVIVG
T72 SLRLGTTTAVIVGHY
K232-ub NKNLEMIkEHtKIRE
T235-p LEMIkEHtKIREKTL
K248-ub TLVEMFEkCKEkFNS
K252-ub MFEkCKEkFNSESLS
S257 KEkFNSESLSSLTDI
Q328 PEVKRKIQkEIDQYV
K329-ub EVKRKIQkEIDQYVG
K499-ub ITVRQAWkDAQVEVS
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