Homo sapiens Protein: CUL4A | |||||||||||||||||||||||
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Summary | |||||||||||||||||||||||
InnateDB Protein | IDBP-52960.7 | ||||||||||||||||||||||
Last Modified | 2014-10-13 [Report errors or provide feedback] | ||||||||||||||||||||||
Gene Symbol | CUL4A | ||||||||||||||||||||||
Protein Name | cullin 4A | ||||||||||||||||||||||
Synonyms | |||||||||||||||||||||||
Species | Homo sapiens | ||||||||||||||||||||||
Ensembl Protein | ENSP00000322132 | ||||||||||||||||||||||
InnateDB Gene | IDBG-52956 (CUL4A) | ||||||||||||||||||||||
Protein Structure | |||||||||||||||||||||||
UniProt Annotation | |||||||||||||||||||||||
Function | Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination 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. DCX(DDB2) ubiquitinates histones H3-H4 and is required for efficient histone deposition during replication-coupled (H3.1) and replication-independent (H3.3) nucleosome assembly, probably by facilitating the transfer of H3 from ASF1A/ASF1B to other chaperones involved in histone deposition. 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 CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. DCX(DTL) directs autoubiquitination of DTL. {ECO:0000269PubMed:14578910, ECO:0000269PubMed:14609952, ECO:0000269PubMed:15448697, ECO:0000269PubMed:15548678, ECO:0000269PubMed:16537899, ECO:0000269PubMed:16678110, ECO:0000269PubMed:23478445, ECO:0000269PubMed:24209620}. | ||||||||||||||||||||||
Subcellular Localization | |||||||||||||||||||||||
Disease Associations | |||||||||||||||||||||||
Tissue Specificity | |||||||||||||||||||||||
Comments | |||||||||||||||||||||||
Interactions | |||||||||||||||||||||||
Number of Interactions |
This gene and/or its encoded proteins are associated with 327 experimentally validated interaction(s) in this database.
They are also associated with 9 interaction(s) predicted by orthology.
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Gene Ontology | |||||||||||||||||||||||
Molecular Function |
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Biological Process |
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Cellular Component |
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Protein Structure and Domains | |||||||||||||||||||||||
PDB ID | |||||||||||||||||||||||
InterPro |
IPR001373
Cullin, N-terminal IPR016158 Cullin homology IPR016159 Cullin repeat-like-containing domain IPR019559 Cullin protein, neddylation domain |
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PFAM |
PF00888
PF10557 |
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PRINTS | |||||||||||||||||||||||
PIRSF | |||||||||||||||||||||||
SMART |
SM00182
SM00884 |
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TIGRFAMs | |||||||||||||||||||||||
Post-translational Modifications | |||||||||||||||||||||||
Modification | |||||||||||||||||||||||
Cross-References | |||||||||||||||||||||||
SwissProt | Q13619 | ||||||||||||||||||||||
PhosphoSite | PhosphoSite-Q13619 | ||||||||||||||||||||||
TrEMBL | B4DKT2 | ||||||||||||||||||||||
UniProt Splice Variant | |||||||||||||||||||||||
Entrez Gene | 8451 | ||||||||||||||||||||||
UniGene | Hs.609784 | ||||||||||||||||||||||
RefSeq | NP_001265443 | ||||||||||||||||||||||
HUGO | HGNC:2554 | ||||||||||||||||||||||
OMIM | 603137 | ||||||||||||||||||||||
CCDS | CCDS73604 | ||||||||||||||||||||||
HPRD | 07218 | ||||||||||||||||||||||
IMGT | |||||||||||||||||||||||
EMBL | AB012193 AB178950 AF077188 AK296700 AL136221 AY365124 BC008308 U58090 | ||||||||||||||||||||||
GenPept | AAC50547 AAD45191 AAH08308 AAR13072 BAA33146 BAD93235 BAG59294 CAI13795 CAM18410 | ||||||||||||||||||||||