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Protein Page:
CYP3A4 (human)
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
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; Xenobiotic Metabolism - drug metabolism - cytochrome P450; Xenobiotic Metabolism - drug metabolism - other enzymes; Oxidoreductase; EC 1.14.14.1; Xenobiotic Metabolism - metabolism by cytochrome P450; Lipid Metabolism - linoleic acid; Membrane protein, integral; Cell surface
Chromosomal Location of Human Ortholog: 7q21.1
Cellular Component: cytoplasm; endoplasmic reticulum membrane; intracellular membrane-bound organelle
Molecular Function: enzyme binding; iron ion binding; monooxygenase activity; oxidoreductase activity; oxygen binding; steroid binding; steroid hydroxylase activity; testosterone 6-beta-hydroxylase activity; vitamin D3 25-hydroxylase activity
Biological Process: alkaloid catabolic process; androgen metabolic process; drug catabolic process; drug metabolic process; exogenous drug catabolic process; heterocycle metabolic process; lipid metabolic process; monoterpenoid metabolic process; steroid catabolic process; steroid metabolic process; vitamin D metabolic process; xenobiotic 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.
Download PyMol Script
Download ChimeraX Script


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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



 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 1 K35 HSHGLFKKLGIPGPT
0 1 M59 SYHKGFCMFDMECHK
0 1 K70‑ac ECHKKYGkVWGFYDG
1 0 T92‑p TDPDMIKtVLVKECY
0 2 K96 MIKtVLVKECYsVFt
1 0 S100‑p VLVKECYsVFtNRRP
1 0 T103‑p KECYsVFtNRRPFGP
1 0 K115‑ub FGPVGFMksAIsIAE
1 1 S116‑ub GPVGFMksAIsIAED
1 0 S119‑p GFMksAIsIAEDEEW
0 1 K127‑ac IAEDEEWkRLRsLLs
1 0 K127‑ub IAEDEEWkRLRsLLs
1 0 S131‑p EEWkRLRsLLsPtFT
1 5 S134‑p kRLRsLLsPtFTsGK
1 2 T136‑p LRsLLsPtFTsGKLK
1 2 S139‑p LLsPtFTsGKLKEMV
0 2 K141 sPtFTsGKLKEMVPI
0 2 K143 tFTsGKLKEMVPIIA
1 0 K168‑ub RREAETGkPVTLkDV
1 0 K173‑ub TGkPVTLkDVFGAYS
0 2 R250 REVTNFLRKSVKRMK
0 2 R250 REVTNFLRKSVKRMK
2 0 S259‑p SVKRMKEsRLEDtQK
3 1 T264‑p KEsRLEDtQKHRVDF
1 0 K282‑ub MIDSQNSkEtESHKA
2 0 T284‑p DSQNSkEtESHKALS
0 2 K379 RLERVCKKDVEINGM
1 0 S398‑p GVVVMIPsYALHRDP
0 1 T409‑p HRDPKYWtEPEkFLP
0 1 K413‑ac KYWtEPEkFLPERFs
3 1 S420‑p kFLPERFsKKNKDNI
0 1 K421 FLPERFsKKNKDNID
0 1 K424 ERFsKKNKDNIDPYI
1 0 K466‑ub VLQNFSFkPCKETQI
0 1 K476 KETQIPLKLsLGGLL
3 1 S478‑p TQIPLKLsLGGLLQP
0 1 K487 GGLLQPEKPVVLkVE
1 2 K487‑ub GGLLQPEkPVVLkVE
0 1 K492 PEkPVVLKVESRDGT
1 1 K492‑ub PEkPVVLkVESRDGT
  mouse

 
K35‑ub RTHGLFKkQGIPGPK
K59‑ub NYYKGLWkFDMECYE
K70 ECYEKYGKTWGLFDG
N92 TDPEMIKNVLVkECF
K96‑ub MIKNVLVkECFSVFT
S100 VLVkECFSVFTNRRE
T103 kECFSVFTNRREFGP
S115 FGPVGIMSkAISISK
K116‑ub GPVGIMSkAISISKD
S119 GIMSkAISISKDEEW
K127 ISKDEEWKRYRALLs
K127 ISKDEEWKRYRALLs
A131 EEWKRYRALLsPtFT
S134‑p KRYRALLsPtFTsGk
T136‑p YRALLsPtFTsGkLk
S139‑p LLsPtFTsGkLkEMF
K141‑ub sPtFTsGkLkEMFPV
K143‑ub tFTsGkLkEMFPVIE
K168 MQEAEKGKPVTMKDV
K173 KGKPVTMKDVLGAYS
K250‑ac KDSIEFFkKFVNRMK
K250‑ub KDSIEFFkKFVNRMK
S259 FVNRMKESRLDSKQK
K264 KESRLDSKQKHRVDF
K283 MNAHNNSKDKDSHKA
K285 AHNNSKDKDSHKALS
K380‑ub RLERFCKkDVELNGV
S399 GSTVMIPSYALHHDP
P410 HHDPQHWPEPEEFQP
E414 QHWPEPEEFQPERFS
S421 EFQPERFSkENkGSI
K422‑ub FQPERFSkENkGSID
K425‑ub ERFSkENkGSIDPYL
Q467 VMQNFSFQPCQETQI
K477‑ub QETQIPLkLSRQGLL
S479 TQIPLkLSRQGLLQP
K488 QGLLQPEKPIVLkVV
K488‑ub QGLLQPEkPIVLkVV
K493 PEkPIVLKVVPRDVV
K493‑ub PEkPIVLkVVPRDVV
  rat

 
K35 HRHGIFKKQGIPGPK
R59 NYYKGLGRFDMECYK
K70 ECYKKYGKIWGLFDG
N92 MDTEMIKNVLVKECF
K96 MIKNVLVKECFSVFT
S100 VLVKECFSVFTNRRD
T103 KECFSVFTNRRDFGP
G115 FGPVGIMGKAVSVAK
K116 GPVGIMGKAVSVAKD
S119 GIMGKAVSVAKDEEW
K127 VAKDEEWKRYRALLS
K127 VAKDEEWKRYRALLS
A131 EEWKRYRALLSPTFT
S134 KRYRALLSPTFTSGR
T136 YRALLSPTFTSGRLK
S139 LLSPTFTSGRLKEMF
R141 SPTFTSGRLKEMFPI
K143 TFTSGRLKEMFPIIE
K168 KQEAETGKPVTMKKV
K173 TGKPVTMKKVFGAYS
Q250 KDSIAFFQKFVHRIK
Q250 KDSIAFFQKFVHRIK
T259 FVHRIKETRLDSKHK
K264 KETRLDSKHKHRVDF
K283 LNAHNNSKDEVSHKA
E285 AHNNSKDEVSHKALS
K380 RLERVCKKDIELDGL
T399 GSVVTIPTYALHHDP
P410 HHDPQHWPKPEEFHP
E414 QHWPKPEEFHPERFS
S421 EFHPERFSKENKGSI
K422 FHPERFSKENKGSID
K425 ERFSKENKGSIDPYV
Q467 VLQNFSFQPCKETQI
K477 KETQIPLKLSRQAIL
S479 TQIPLKLSRQAILEP
K488‑ac QAILEPEkPIVLkVL
K488 QAILEPEKPIVLkVL
K493‑ac PEkPIVLkVLPRDAV
K493 PEkPIVLKVLPRDAV
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