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Protein Page:
POR (human)
rdtyret
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitylation
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylation
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
Chromosomal Location of Human Ortholog: 7q11.2
Cellular Component: endoplasmic reticulum membrane; integral to membrane; intracellular membrane-bound organelle; membrane; mitochondrion
Molecular Function: [methionine synthase] reductase activity; cytochrome-b5 reductase activity; electron carrier activity; enzyme binding; FAD binding; FMN binding; hydrolase activity; iron ion binding; iron-cytochrome-c reductase activity; NADP binding; NADPH-hemoprotein reductase activity; nitric oxide dioxygenase activity; protein binding
Biological Process: carnitine metabolic process; fatty acid oxidation; flavonoid metabolic process; internal peptidyl-lysine acetylation; negative regulation of caspase activity; negative regulation of lipase activity; nitrate catabolic process; nitric oxide catabolic process; positive regulation of cholesterol biosynthetic process; positive regulation of chondrocyte differentiation; positive regulation of monooxygenase activity; positive regulation of smoothened signaling pathway; response to drug; response to nutrient
Disease: Antley-bixler Syndrome With Genital Anomalies And Disordered Steroidogenesis; Antley-bixler Syndrome Without Genital Anomalies Or Disordered Steroidogenesis; Disordered Steroidogenesis Due To Cytochrome P450 Oxidoreductase Deficiency
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.


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Modification Sites and Domains  
Click here to view other types of protein modifications

Modification Sites in Parent Protein, Orthologs, and Isoforms  
 

Show Multiple Sequence Alignment


 LTP 

LTP: 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.


 HTP 

HTP: 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 2 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 2 R584 EELAQFHRDGALTQL
0 1 R584 EELAQFHRDGALTQL
0 1 Y604‑p REQSHKVyVQHLLKQ
0 16 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
Y604 REQAHKVYVQHLLkR
K610‑ac VYVQHLLkRDKEHLW
K610‑ub VYVQHLLkRDKEHLW
K664‑ac TQAVDYVkKLMTKGR
  rat

 
K56 EEIPEFSKIQTTAPP
T59 PEFSKIQTTAPPVKE
P62 SKIQTTAPPVKESSF
P63 KIQTTAPPVKESSFV
K65 QTTAPPVKESSFVEK
K72 KESSFVEKMKKTGRN
Y105 LSKDAHRYGMRGMSA
S111 RYGMRGMSADPEEYD
K176 AVFGLGNKTYEHFNA
K186 EHFNAMGKYVDQRLE
K186 EHFNAMGKYVDQRLE
Y245 EESSIRQYELVVHED
K257 HEDMDVAKVYTGEMG
Y259 DMDVAKVYTGEMGRL
K273 LKSYENQKPPFDAKN
K279 QKPPFDAKNPFLAAV
T296 NRKLNQGTERHLMHL
K311 ELDISDSKIRYESGD
K358 LDEESNKKHPFPCPT
Y373 TYRTALTYYLDITNP
Y374 YRTALTYYLDITNPP
Y387 PPRTNVLYELAQYAS
K404 SEQEHLHKMASSSGE
Y416 SGEGKELYLSWVVEA
K487 AKSGRVNKGVATSWL
K523 SQFRLPFKSTTPVIM
K555 AWLREQGKEVGETLL
Y564 VGETLLYYGCRRSDE
Y573 CRRSDEDYLYREELA
Y575 RSDEDYLYREELARF
K584‑ac EELARFHkDGALTQL
K584 EELARFHKDGALTQL
Y604 REQAHKVYVQHLLkR
K610‑ac VYVQHLLkRDREHLW
K610 VYVQHLLKRDREHLW
K664 TQAVDYVKKLMTKGR
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