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:
CYP3A4 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
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: Membrane protein, integral; Lipid Metabolism - linoleic acid; Cofactor and Vitamin Metabolism - retinol; EC 1.14.13.-; EC 1.14.13.32; Xenobiotic Metabolism - drug metabolism - cytochrome P450; Xenobiotic Metabolism - metabolism by cytochrome P450; EC 1.14.13.97; EC 1.14.14.1; EC 1.14.13.67; Xenobiotic Metabolism - drug metabolism - other enzymes; Oxidoreductase; Cell surface
Cellular Component: endoplasmic reticulum membrane; intracellular membrane-bound organelle; cytoplasm; integral to membrane
Molecular Function: enzyme binding; quinine 3-monooxygenase activity; iron ion binding; taurochenodeoxycholate 6alpha-hydroxylase activity; albendazole monooxygenase activity; heme binding; 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; steroid hydroxylase activity; oxidoreductase activity; oxygen binding; monooxygenase activity; steroid binding; testosterone 6-beta-hydroxylase activity; vitamin D3 25-hydroxylase activity
Biological Process: steroid metabolic process; drug catabolic process; xenobiotic metabolic process; androgen metabolic process; exogenous drug catabolic process; monoterpenoid metabolic process; alkaloid catabolic process; heterocycle metabolic process; lipid 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.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho3D  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


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

 
1 0 T92-p TDPDMIKtVLVKECY
0 2 K96 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 3 S134-p kRLRsLLsPtFTsGK
1 1 T136-p LRsLLsPtFTsGKLK
1 1 S139-p LLsPtFTsGKLKEMV
0 2 K141 sPtFTsGKLKEMVPI
0 2 K143 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 RLERVCKKDVEINGM
1 0 S398-p GVVVMIPsYALHRDP
0 1 K413-a KYWTEPEkFLPERFs
2 1 S420-p kFLPERFsKKNKDNI
1 0 K466-u VLQNFSFkPCKETQI
2 1 S478-p TQIPLKLsLGGLLQP
1 2 K487-u GGLLQPEkPVVLkVE
1 1 K492-u PEkPVVLkVESRDGT
  mouse

 
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-p YRALLsPtFTsGkLk
S139-p LLsPtFTsGkLkEMF
K141-u sPtFTsGkLkEMFPV
K143-u tFTsGkLkEMFPVIE
K168 MQEAEKGKPVTMKDV
K173 KGKPVTMKDVLGAYS
K250-a KDSIEFFkKFVNRMK
K250-u KDSIEFFkKFVNRMK
S259 FVNRMKESRLDSKQK
K264 KESRLDSKQKHRVDF
K283 MNAHNNSKDKDSHKA
K285 AHNNSKDKDSHKALS
K380-u RLERFCKkDVELNGV
S399 GSTVMIPSYALHHDP
E414 QHWPEPEEFQPERFS
S421 EFQPERFSKENKGSI
Q467 VMQNFSFQPCQETQI
S479 TQIPLKLSRQGLLQP
K488-u QGLLQPEkPIVLkVV
K493-u PEkPIVLkVVPRDVV
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.