Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
POR (human)
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
POR This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Defects in POR are the cause of Antley-Bixler syndrome with genital anomalies and disordered steroidogenesis (ABS1). A disease characterized by the association of Antley-Bixler syndrome with steroidogenesis defects and abnormal genitalia. Antley-Bixler syndrome is characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Defects in POR are the cause of disordered steroidogenesis due to cytochrome P450 oxidoreductase deficiency (DISPORD). A disorder resulting in a rare variant of congenital adrenal hyperplasia, with apparent combined P450C17 and P450C21 deficiency and accumulation of steroid metabolites. Affected girls are born with ambiguous genitalia, but their circulating androgens are low and virilization does not progress. Conversely, affected boys are sometimes born undermasculinized. Boys and girls can present with bone malformations, in some cases resembling the pattern seen in patients with Antley-Bixler syndrome. Note: This description may include information from UniProtKB.
Protein type: Oxidoreductase; EC 1.6.2.4
Cellular Component: endoplasmic reticulum membrane; mitochondrion; intracellular membrane-bound organelle
Molecular Function: protein binding; enzyme binding; FAD binding; electron carrier activity; hydrolase activity; NADPH-hemoprotein reductase activity; FMN binding; cytochrome-b5 reductase activity; nitric oxide dioxygenase activity; iron ion binding; NADP binding; iron-cytochrome-c reductase activity
Biological Process: response to drug; nitric oxide catabolic process; internal peptidyl-lysine acetylation; positive regulation of monooxygenase activity; positive regulation of cholesterol biosynthetic process; negative regulation of caspase activity; negative regulation of lipase activity; nitrate catabolic process; positive regulation of chondrocyte differentiation; flavonoid metabolic process; positive regulation of smoothened signaling pathway; fatty acid oxidation; carnitine metabolic process; response to nutrient; negative regulation of apoptosis
Reference #:  P16435 (UniProtKB)
Alt. Names/Synonyms: CPR; CYPOR; DKFZp686G04235; FLJ26468; NADPH--cytochrome P450 reductase; NADPH-dependent cytochrome P450 reductase; NCPR; P450 (cytochrome) oxidoreductase; P450R; POR
Gene Symbols: POR
Molecular weight: 76,690 Da
Basal Isoelectric point: 5.38  Predict pI for various phosphorylation states
Select Structure to View Below

POR

Protein Structure Not Found.


STRING  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Phospho.ELM  |  NetworKIN  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB


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.


       human

 
0 2 K56-ub EEVPEFTkIQtLTss
0 1 T59-p PEFTkIQtLTssVRE
0 1 S62-p TkIQtLTssVRESSF
0 1 S63-p kIQtLTssVRESSFV
0 1 R65 QtLTssVRESSFVEK
0 1 K72 RESSFVEKMKKTGRN
0 1 Y105 LSKDAHRYGMRGMSA
0 1 S111 RYGMRGMSADPEEYD
0 1 K176 AVFGLGNKTYEHFNA
0 1 K186 EHFNAMGKYVDKRLE
0 1 K186 EHFNAMGKYVDKRLE
0 2 Y245-p EESSIRQyELVVHTD
0 1 K257 HTDIDAAKVyMGEMG
0 2 Y259-p DIDAAKVyMGEMGRL
0 1 K273 LKSYENQKPPFDAKN
0 1 K279 QKPPFDAKNPFLAAV
0 1 T296-p NRKLNQGtERHLMHL
0 1 K311 ELDISDSKIRYESGD
0 1 K358 LDEESNKKHPFPCPT
0 26 Y373-p SYRTALTyyLDITNP
0 26 Y374-p YRTALTyyLDITNPP
0 1 Y387 PPRTNVLYELAQYAS
0 1 K404 SEQELLRKMASSSGE
0 1 Y416-p SGEGKELyLSWVVEA
0 2 K487-ub TKAGRINkGVATNWL
0 3 K523-ub SQFRLPFkATTPVIM
0 1 K555 AWLRQQGKEVGETLL
0 1 Y564-p VGETLLYyGCRRSDE
0 1 Y573-p CRRSDEDyLyREELA
0 2 Y575-p RSDEDyLyREELAQF
0 1 R584 EELAQFHRDGALTQL
0 1 R584 EELAQFHRDGALTQL
0 15 K610 VYVQHLLKQDREHLW
0 1 K610 VYVQHLLKQDREHLW
0 7 K663 AQAVDYIKKLMTKGR
  mouse

 
K56-ub EEIPEFSkIQTTAPP
T59 PEFSkIQTTAPPVkE
P62 SkIQTTAPPVkESSF
P63 kIQTTAPPVkESSFV
K65-ub QTTAPPVkESSFVEk
K72-ac kESSFVEkMKKTGRN
Y105-p LSKDAHRyGMRGMsA
S111-p RyGMRGMsADPEEYD
K176-ub AVFGLGNkTYEHFNA
K186-ac EHFNAMGkYVDQRLE
K186-ub EHFNAMGkYVDQRLE
Y245 EESSIRQYELVVHED
K257-ub HEDMDTAkVYTGEMG
Y259 DMDTAkVYTGEMGRL
K273-ub LKSYENQkPPFDAkN
K279-ub QkPPFDAkNPFLAAV
T296 NRKLNQGTERHLMHL
K311-ub ELDISDSkIRYESGD
K358-ub LDEESNKkHPFPCPT
Y373-p TYRTALTyyLDITNP
Y374-p YRTALTyyLDITNPP
Y387-p PPRTNVLyELAQYAS
K404-ub SEQEHLHkMASSSGE
Y416 SGEGKELYLSWVVEA
K487-ub AKSGRVNkGVATSWL
K523-ub SQFRLPFkPTTPVIM
K555-ub AWLREQGkEVGETLL
Y564 VGETLLYYGCRRSDE
Y573 CRRSDEDYLyREELA
Y575-p RSDEDYLyREELARF
K584-ac EELARFHkDGALTQL
K584-ub EELARFHkDGALTQL
K610-ac VYVQHLLkRDKEHLW
K610-ub VYVQHLLkRDKEHLW
K664-ac TQAVDYVkKLMTKGR
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.