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Protein Page:
CYP3A4 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
CYP3A4 Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It performs a variety of oxidation reactions (e.g. caffeine 8-oxidation, omeprazole sulphoxidation, midazolam 1'-hydroxylation and midazolam 4- hydroxylation) of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. Acts as a 1,8-cineole 2- exo-monooxygenase. The enzyme also hydroxylates etoposide. Belongs to the cytochrome P450 family. Note: This description may include information from UniProtKB.
Protein type: Cofactor and Vitamin Metabolism - retinol; Cell surface; EC 1.14.14.1; EC 1.14.13.32; EC 1.14.13.97; Membrane protein, integral; EC 1.14.13.67; Xenobiotic Metabolism - metabolism by cytochrome P450; Oxidoreductase; Lipid Metabolism - linoleic acid; Xenobiotic Metabolism - drug metabolism - other enzymes; Xenobiotic Metabolism - drug metabolism - cytochrome P450; EC 1.14.13.-
Cellular Component: endoplasmic reticulum membrane; cell surface; intracellular membrane-bound organelle; cytoplasm; integral to membrane
Molecular Function: quinine 3-monooxygenase activity; albendazole monooxygenase activity; taurochenodeoxycholate 6alpha-hydroxylase activity; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen; oxidoreductase activity; oxygen binding; vitamin D3 25-hydroxylase activity; steroid binding; testosterone 6-beta-hydroxylase activity; enzyme binding; electron carrier activity; iron ion binding; heme binding; steroid hydroxylase activity; monooxygenase activity
Biological Process: steroid metabolic process; drug catabolic process; xenobiotic metabolic process; exogenous drug catabolic process; androgen metabolic process; monoterpenoid metabolic process; alkaloid catabolic process; lipid metabolic process; heterocycle metabolic process; drug metabolic process; steroid catabolic process; vitamin D metabolic process
Reference #:  P08684 (UniProtKB)
Alt. Names/Synonyms: Albendazole monooxygenase; Albendazole sulfoxidase; CP33; CP34; CP3A4; CYP3A; CYP3A3; CYP3A4; CYPIIIA3; CYPIIIA4; Cytochrome P450 3A3; Cytochrome P450 3A4; Cytochrome P450 HLp; Cytochrome P450 NF-25; cytochrome P450, family 3, subfamily A, polypeptide 4; cytochrome P450, subfamily IIIA (niphedipine oxidase), polypeptide 3; cytochrome P450, subfamily IIIA (niphedipine oxidase), polypeptide 4; Cytochrome P450-PCN1; glucocorticoid-inducible P450; HLP; MGC126680; NF-25; Nifedipine oxidase; P450-III, steroid inducible; P450C3; P450PCN1; Quinine 3-monooxygenase; Taurochenodeoxycholate 6-alpha-hydroxylase
Gene Symbols: CYP3A4
Molecular weight: 57,343 Da
Basal Isoelectric point: 8.27  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CYP3A4

Protein Structure Not Found.


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Sites Implicated In
protein degradation: T264‑p, S420‑p, S478‑p
ubiquitination: T264‑p, S420‑p, S478‑p

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 1 K35-u HSHGLFKkLGIPGPT
0 1 M59 SYHKGFCMFDMECHK
0 1 K70-a ECHKKYGkVWGFYDG
1 0 T92-p TDPDMIKtVLVkECY
0 2 K96-u MIKtVLVkECYsVFt
1 0 S100-p VLVkECYsVFtNRRP
1 0 T103-p kECYsVFtNRRPFGP
1 0 K115-u FGPVGFMksAIsIAE
1 1 S116-u GPVGFMksAIsIAED
1 0 S119-p GFMksAIsIAEDEEW
0 1 K127-a IAEDEEWkRLRsLLs
1 0 K127-u IAEDEEWkRLRsLLs
1 0 S131-p EEWkRLRsLLsPtFT
1 1 S134-p kRLRsLLsPtFTsGk
1 1 T136-p LRsLLsPtFTsGkLk
1 0 S139-p LLsPtFTsGkLkEMV
0 2 K141-u sPtFTsGkLkEMVPI
0 2 K143-u tFTsGkLkEMVPIIA
1 0 K168-u RREAETGkPVTLkDV
1 0 K173-u TGkPVTLkDVFGAYS
0 2 R250 REVTNFLRKSVKRMK
0 2 R250 REVTNFLRKSVKRMK
1 0 S259-p SVKRMKEsRLEDtQK
2 1 T264-p KEsRLEDtQKHRVDF
1 0 K282-u MIDSQNSkEtESHKA
1 0 T284-p DSQNSkEtESHKALS
0 2 K379-u RLERVCKkDVEINGM
1 0 S398-p GVVVMIPsYALHRDP
0 1 T409-p HRDPKYWtEPEkFLP
0 1 K413-a KYWtEPEkFLPERFs
2 1 S420-p kFLPERFskKNkDNI
0 1 K421-u FLPERFskKNkDNID
0 1 K424-u ERFskKNkDNIDPYI
1 0 K466-u VLQNFSFkPCKETQI
0 1 K476-u KETQIPLkLsLGGLL
2 1 S478-p TQIPLkLsLGGLLQP
1 2 K487-u GGLLQPEkPVVLkVE
1 1 K492-u PEkPVVLkVESRDGT
  mouse

 
K35-u RTHGLFKkQGIPGPK
K59-u NYYKGLWkFDMECYE
K70 ECYEKYGKTWGLFDG
N92 TDPEMIKNVLVkECF
K96-u MIKNVLVkECFSVFT
S100 VLVkECFSVFTNRRE
T103 kECFSVFTNRREFGP
S115 FGPVGIMSkAISISK
K116-u GPVGIMSkAISISKD
S119 GIMSkAISISKDEEW
K127 ISKDEEWKRYRALLs
K127 ISKDEEWKRYRALLs
A131 EEWKRYRALLsPTFT
S134-p KRYRALLsPTFTSGk
T136 YRALLsPTFTSGkLk
S139 LLsPTFTSGkLkEMF
K141-u sPTFTSGkLkEMFPV
K143-u TFTSGkLkEMFPVIE
K168 MQEAEKGKPVTMKDV
K173 KGKPVTMKDVLGAYS
K250-a KDSIEFFkKFVNRMK
K250-u KDSIEFFkKFVNRMK
S259 FVNRMKESRLDSKQK
K264 KESRLDSKQKHRVDF
- under review  
K285 AHNNSKDKDSHKALS
K380-u RLERFCKkDVELNGV
S399 GSTVMIPSYALHHDP
P410 HHDPQHWPEPEEFQP
E414 QHWPEPEEFQPERFS
S421 EFQPERFSkENkGSI
K422-u FQPERFSkENkGSID
K425-u ERFSkENkGSIDPYL
Q467 VMQNFSFQPCQETQI
K477-u QETQIPLkLSRQGLL
S479 TQIPLkLSRQGLLQP
K488-u QGLLQPEkPIVLkVV
K493-u PEkPIVLkVVPRDVV
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