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Protein Page:
CUL4A (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
CUL4A Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. The E3 ubiquitin-protein ligase activity of the complex is dependent on the neddylation of the cullin subunit and is inhibited by the association of the deneddylated cullin subunit with TIP120A/CAND1. The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component. DCX(DET1-COP1) directs ubiquitination of JUN. DCX(DDB2) directs ubiquitination of XPC. In association with RBX1, DDB1 and DDB2 is required for histone H3 and histone H4 ubiquitination in response to ultraviolet and may be important for subsequent DNA repair. DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of TP53 in response to radiation-induced DNA damage and during DNA replication. In association with DDB1 and SKP2 probably is involved in ubiquitination of p27Kip1/p27kip. Is involved in ubiquitination of HOXA9. Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin- protein ligase complexes that seem to consist of DDB1, CUL4A or CUL4B, RBX1 and a variable substrate recognition component which seems to belong to a protein family described as DCAF (Ddb1- and Cul4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Component of the CSA complex (DCX(ERCC8) complex) containing ERCC8, RBX1, DDB1 and CUL4A; the CSA complex interacts with RNA polymerase II; upon UV irradiation it interacts with the COP9 signalosome and preferentially with the hyperphosphorylated form of RNA polymerase II. Component of the DCX(DET1-COP1) complex with the substrate recognition component DET1 and COP1. Component of the DCX(DDB2) complex with the substrate recognition component DDB2. Component of the DCX(DTL) complex with the putative substrate recognition component DTL. Interacts with DDB1, RBX1, RNF7, CTD1, TIP120A/CAND1, SKP2, p27Kip1, MDM2, TP53 and HOXA9. Interacts with DDB2; the interactions with DDB2 and CAND1 are mutually exclusive. Interacts with VPRBP, DTL, DDA1, DCAF6, DCAF4, DCAF16, DCAF17, DET1, WDTC1, DCAF5, DCAF11, WDR24A, RFWD2, PAFAH1B1, ERCC8, GRWD1, FBXW5, RBBP7, GNB2, WSB1, WSB2, NUP43, PWP1, FBXW8, ATG16L1, KATNB1, RBBP4, RBBP5 and DCAF8. May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76, WDR5. Can self- associate. Interacts with Epstein-Barr virus BPLF1. Belongs to the cullin family. 2 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Ubiquitin conjugating system
Chromosomal Location of Human Ortholog: 13q34
Molecular Function: protein binding; ubiquitin protein ligase binding
Biological Process: ubiquitin-dependent protein catabolic process; negative regulation of cell proliferation; viral reproduction; regulation of protein metabolic process; protein ubiquitination; DNA repair; cell cycle arrest; G1/S transition of mitotic cell cycle
Reference #:  Q13619 (UniProtKB)
Alt. Names/Synonyms: CUL-4A; CUL4A; cullin 4A; Cullin-4A
Gene Symbols: CUL4A
Molecular weight: 87,680 Da
Basal Isoelectric point: 8.29  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

CUL4A

Protein Structure Not Found.


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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 34 S10-p DEAPRKGsFSALVGR
0 1 T22-p VGRTNGLtkPAALAA
0 1 K23-ac GRTNGLtkPAALAAA
0 1 K33-ub ALAAAPAkPGGAGGS
0 3 K41-ac PGGAGGSkkLVIKNF
0 1 K42-ac GGAGGSkkLVIKNFR
0 1 S99-p NLCSHKVsPMLYkQL
0 2 K104-ub KVsPMLYkQLRQACE
0 1 Y227-p MLSDLQVyKDSFELK
0 1 K369 VQDLLDFKDKVDHVI
0 1 K371 DLLDFKDKVDHVIEV
0 2 K422-ac SKLRAGNkEATDEEL
0 2 K422-ub SKLRAGNkEATDEEL
0 4 K454-ub DVFEAFYkKDLAKRL
0 3 K465 AKRLLVGKSASVDAE
0 2 K496-ub SKLEGMFkDMELSKD
0 1 K555-ac IKLQEVFkAFYLGKH
0 1 K635 LQSLACGKARVLIKs
0 1 S642-p KARVLIKsPKGKEVE
0 1 R702-m2 QIDAAIVrIMkMRKT
0 1 K705-ne AAIVrIMkMRKTLGH
0 10 K705-ub AAIVrIMkMRKTLGH
0 2 Y744-p ESLIDRDyMERDKDN
  mouse

 
S10-p DEGPRKGsVSALMGR
T22 MGRTNGLTKPAALAG
K23 GRTNGLTKPAALAGG
K33 ALAGGPAKPGGTGGS
R41 PGGTGGSRKLVIKNF
K42 GGTGGSRKLVIKNFR
S99 NLCSHKVSPTLYkQL
K104-ub KVSPTLYkQLRQVCE
Y227 MLSDLQVYKDSFELK
K369-ub VQDLLDFkDkVDHVV
K371-ub DLLDFkDkVDHVVEV
K422-ac SKLRAGNkEATDEEL
K422-ub SKLRAGNkEATDEEL
K454-ub DVFEAFYkKDLAKRL
K465-ub AKRLLVGkSASVDAE
K496-ub SKLEGMFkDMELSKD
K555 VRLQEVFKTFYLGKH
K635-ub LQSLACGkARVLIKS
S642 kARVLIKSPKGKEVE
R702 QIDAAIVRIMkMRKT
K705 AAIVRIMKMRKTLGH
K705-ub AAIVRIMkMRKTLGH
Y744 ESLIDRDYMERDKDS
  rat

 
S10-p DEGPRKGsVSALMGR
T22 MGRTNGLTKPAALAS
K23 GRTNGLTKPAALASG
K33 ALASGPAKPGGTGGS
R41 PGGTGGSRKLVIKNF
K42 GGTGGSRKLVIKNFR
S99 NLCSHKVSPTLYKQL
K104 KVSPTLYKQLRQVCE
Y227 MLSDLQVYKDSFELK
K369 VQDLLDFKDKVDHVV
K371 DLLDFKDKVDHVVEV
K422 SKLRAGNKEATDEEL
K422 SKLRAGNKEATDEEL
K454 DVFEAFYKKDLAKRL
K465 AKRLLVGKSASVDAE
K496 SKLEGMFKDMELSKD
K555 VRLQEVFKTFYLGKH
K635 LQSLACGKARVLIKS
S642 KARVLIKSPKGKEVE
R702 QIDAAIVRIMKMRKT
K705 AAIVRIMKMRKTLGH
K705 AAIVRIMKMRKTLGH
Y744 ESLIDRDYMERDKDS
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