UniProtKB - Q13619 (CUL4A_HUMAN)
Cullin-4A
CUL4A
Functioni
Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination of target proteins (PubMed:14578910, PubMed:15811626, PubMed:15548678, PubMed:15448697, PubMed:14739464, PubMed:16678110, PubMed:17041588, PubMed:24209620, PubMed:30166453, PubMed:33854232, PubMed:33854239).
As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme (PubMed:14578910, PubMed:15811626, PubMed:15548678, PubMed:15448697, PubMed:14739464, PubMed:16678110, PubMed:17041588, PubMed:24209620).
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 (PubMed:14578910, PubMed:15811626, PubMed:15548678, PubMed:15448697, PubMed:14739464, PubMed:16678110, PubMed:17041588, PubMed:24209620).
The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition component (PubMed:14578910, PubMed:15811626, PubMed:15548678, PubMed:15448697, PubMed:14739464, PubMed:16678110, PubMed:17041588, PubMed:24209620).
DCX(DET1-COP1) directs ubiquitination of JUN (PubMed:14739464).
DCX(DDB2) directs ubiquitination of XPC (PubMed:15811626).
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 (PubMed:16678110, PubMed:17041588, PubMed:24209620).
DCX(DTL) plays a role in PCNA-dependent polyubiquitination of CDT1 and MDM2-dependent ubiquitination of p53/TP53 in response to radiation-induced DNA damage and during DNA replication (PubMed:14578910, PubMed:15548678, PubMed:15448697).
DCX(DTL) directs autoubiquitination of DTL (PubMed:23478445).
In association with DDB1 and SKP2 probably is involved in ubiquitination of CDKN1B/p27kip (PubMed:16537899).
Is involved in ubiquitination of HOXA9 (PubMed:14609952).
The DDB1-CUL4A-DTL E3 ligase complex regulates the circadian clock function by mediating the ubiquitination and degradation of CRY1 (PubMed:26431207).
A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation (PubMed:29779948).
The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (PubMed:33854232, PubMed:33854239).
The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes (PubMed:30166453).
With CUL4B, contributes to ribosome biogenesis (PubMed:26711351).
17 Publications: protein ubiquitination Pathwayi
This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.10 PublicationsView all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.
GO - Molecular functioni
- protein-macromolecule adaptor activity Source: GO_Central
- ubiquitin protein ligase binding Source: GO_Central
GO - Biological processi
- cellular response to DNA damage stimulus Source: GO_Central
- cellular response to UV Source: ComplexPortal
- DNA repair Source: UniProtKB-KW
- G1/S transition of mitotic cell cycle Source: ProtInc
- hemopoiesis Source: Ensembl
- intrinsic apoptotic signaling pathway Source: ProtInc
- in utero embryonic development Source: Ensembl
- negative regulation of granulocyte differentiation Source: Ensembl
- positive regulation of cell population proliferation Source: Ensembl
- positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
- proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
- protein ubiquitination Source: UniProtKB
- regulation of DNA damage checkpoint Source: Ensembl
- regulation of nucleotide-excision repair Source: Ensembl
- regulation of protein metabolic process Source: Ensembl
- rhythmic process Source: UniProtKB-KW
- ribosome biogenesis Source: UniProtKB
- SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: GO_Central
- somatic stem cell population maintenance Source: Ensembl
Keywordsi
Biological process | Biological rhythms, DNA damage, DNA repair, Host-virus interaction, Ubl conjugation pathway |
Enzyme and pathway databases
PathwayCommonsi | Q13619 |
Reactomei | R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex R-HSA-5696394, DNA Damage Recognition in GG-NER R-HSA-5696395, Formation of Incision Complex in GG-NER R-HSA-5696400, Dual Incision in GG-NER R-HSA-6781823, Formation of TC-NER Pre-Incision Complex R-HSA-6781827, Transcription-Coupled Nucleotide Excision Repair (TC-NER) R-HSA-6782135, Dual incision in TC-NER R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-8951664, Neddylation |
SignaLinki | Q13619 |
SIGNORi | Q13619 |
UniPathwayi | UPA00143 |
Names & Taxonomyi
Protein namesi | Recommended name: Cullin-4ACuratedShort name: CUL-4A1 Publication |
Gene namesi | |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:2554, CUL4A |
MIMi | 603137, gene |
neXtProti | NX_Q13619 |
VEuPathDBi | HostDB:ENSG00000139842 |
Subcellular locationi
Nucleus
- nucleoplasm Source: Reactome
- nucleus Source: ComplexPortal
Other locations
- Cul4-RING E3 ubiquitin ligase complex Source: UniProtKB
- Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
- cullin-RING ubiquitin ligase complex Source: GO_Central
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 86 – 90 | LYQAV → AAAAA: Largely reduces interaction with DDB1; abolishes interaction with DDB2. 2 Publications | 5 | |
Mutagenesisi | 139 – 142 | WQDH → AADA: Largely reduces interaction with DDB1; abolishes interaction with DDB2. 2 Publications | 4 |
Organism-specific databases
DisGeNETi | 8451 |
OpenTargetsi | ENSG00000139842 |
PharmGKBi | PA27050 |
Miscellaneous databases
Pharosi | Q13619, Tchem |
Chemistry databases
ChEMBLi | CHEMBL4523598 |
Genetic variation databases
BioMutai | CUL4A |
DMDMi | 108936013 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000119795 | 1 – 759 | Cullin-4AAdd BLAST | 759 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Cross-linki | 8 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources | ||
Modified residuei | 10 | PhosphoserineCombined sources | 1 | |
Cross-linki | 33 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||
Cross-linki | 705 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)By similarity |
Post-translational modificationi
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q13619 |
jPOSTi | Q13619 |
MassIVEi | Q13619 |
MaxQBi | Q13619 |
PaxDbi | Q13619 |
PeptideAtlasi | Q13619 |
PRIDEi | Q13619 |
ProteomicsDBi | 59609 [Q13619-1] 59610 [Q13619-2] |
PTM databases
GlyGeni | Q13619, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q13619 |
MetOSitei | Q13619 |
PhosphoSitePlusi | Q13619 |
Expressioni
Gene expression databases
Bgeei | ENSG00000139842, Expressed in skeletal muscle tissue and 245 other tissues |
ExpressionAtlasi | Q13619, baseline and differential |
Genevisiblei | Q13619, HS |
Organism-specific databases
HPAi | ENSG00000139842, Tissue enhanced (skeletal) |
Interactioni
Subunit structurei
Can self-associate (PubMed:17254749).
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 (PubMed:14578910, PubMed:12732143, PubMed:15548678, PubMed:14739464, PubMed:29779948, PubMed:30166453).
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 (PubMed:12732143).
Component of the DCX(DET1-COP1) complex with the substrate recognition component DET1 and COP1 (PubMed:14739464).
Component of the DCX(DDB2) complex with the substrate recognition component DDB2 (PubMed:15811626, PubMed:16678110).
Component of the DCX(DTL) complex with the putative substrate recognition component DTL (PubMed:14578910, PubMed:15448697, PubMed:15548678).
Component of DCX complexes part of the DesCEND (destruction via C-end degrons) pathway, which contain either TRPC4AP or DCAF12 as substrate-recognition component (PubMed:29779948).
Component of the DCX(AMBRA1) complex with the substrate recognition component AMBRA1 (PubMed:30166453, PubMed:33854232, PubMed:33854239).
Interacts with DDB1, RBX1, RNF7, CDT1, TIP120A/CAND1, SKP2, CDKN1B, MDM2, TP53 and HOXA9 (PubMed:16964240, PubMed:16537899, PubMed:22118460, PubMed:16482215, PubMed:12609982, PubMed:10230407, PubMed:14609952, PubMed:16678110).
Interacts with DDB2; the interactions with DDB2 and CAND1 are mutually exclusive (PubMed:16678110, PubMed:22118460, PubMed:16482215).
Interacts with DCAF1, DTL, DDA1, DCAF6, DCAF4, DCAF16, DCAF17, DET1, WDTC1, DCAF5, DCAF11, WDR24A, COP1, PAFAH1B1, ERCC8, GRWD1, FBXW5, RBBP7, GNB2, WSB1, WSB2, NUP43, PWP1, FBXW8, ATG16L1, KATNB1, RBBP4, RBBP5, LRWD1 and DCAF8 (PubMed:16949367, PubMed:22935713, PubMed:17079684). May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76, WDR5 (PubMed:17041588).
Interacts (when neddylated) with ARIH1; leading to activate the E3 ligase activity of ARIH1 (PubMed:24076655). The DDB1-CUL4A complex interacts with CRY1 (PubMed:26431207).
Interacts (unneddylated form) with DCUN1D1, DCUN1D2, DCUN1D3, DCUN1D4 and DCUN1D5; these interactions promote the cullin neddylation (PubMed:23201271, PubMed:26906416).
27 Publications(Microbial infection) Interacts with Epstein-Barr virus BPLF1.
1 PublicationBinary interactionsi
Q13619
GO - Molecular functioni
- ubiquitin protein ligase binding Source: GO_Central
Protein-protein interaction databases
BioGRIDi | 114029, 773 interactors |
ComplexPortali | CPX-477, CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant |
CORUMi | Q13619 |
DIPi | DIP-31610N |
IntActi | Q13619, 209 interactors |
MINTi | Q13619 |
STRINGi | 9606.ENSP00000364589 |
Miscellaneous databases
RNActi | Q13619, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | Q13619 |
SMRi | Q13619 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q13619 |
Family & Domainsi
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG2167, Eukaryota |
GeneTreei | ENSGT00940000156905 |
HOGENOMi | CLU_004747_7_2_1 |
InParanoidi | Q13619 |
OMAi | DNVVQSC |
OrthoDBi | 1040292at2759 |
PhylomeDBi | Q13619 |
TreeFami | TF101153 |
Family and domain databases
Gene3Di | 1.10.10.10, 1 hit |
IDEALi | IID00514 |
InterProi | View protein in InterPro IPR045093, Cullin IPR016157, Cullin_CS IPR016158, Cullin_homology IPR036317, Cullin_homology_sf IPR001373, Cullin_N IPR019559, Cullin_neddylation_domain IPR016159, Cullin_repeat-like_dom_sf IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
PANTHERi | PTHR11932, PTHR11932, 1 hit |
Pfami | View protein in Pfam PF00888, Cullin, 1 hit PF10557, Cullin_Nedd8, 1 hit |
SMARTi | View protein in SMART SM00182, CULLIN, 1 hit SM00884, Cullin_Nedd8, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit SSF74788, SSF74788, 1 hit SSF75632, SSF75632, 1 hit |
PROSITEi | View protein in PROSITE PS01256, CULLIN_1, 1 hit PS50069, CULLIN_2, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MADEAPRKGS FSALVGRTNG LTKPAALAAA PAKPGGAGGS KKLVIKNFRD
60 70 80 90 100
RPRLPDNYTQ DTWRKLHEAV RAVQSSTSIR YNLEELYQAV ENLCSHKVSP
110 120 130 140 150
MLYKQLRQAC EDHVQAQILP FREDSLDSVL FLKKINTCWQ DHCRQMIMIR
160 170 180 190 200
SIFLFLDRTY VLQNSTLPSI WDMGLELFRT HIISDKMVQS KTIDGILLLI
210 220 230 240 250
ERERSGEAVD RSLLRSLLGM LSDLQVYKDS FELKFLEETN CLYAAEGQRL
260 270 280 290 300
MQEREVPEYL NHVSKRLEEE GDRVITYLDH STQKPLIACV EKQLLGEHLT
310 320 330 340 350
AILQKGLDHL LDENRVPDLA QMYQLFSRVR GGQQALLQHW SEYIKTFGTA
360 370 380 390 400
IVINPEKDKD MVQDLLDFKD KVDHVIEVCF QKNERFVNLM KESFETFINK
410 420 430 440 450
RPNKPAELIA KHVDSKLRAG NKEATDEELE RTLDKIMILF RFIHGKDVFE
460 470 480 490 500
AFYKKDLAKR LLVGKSASVD AEKSMLSKLK HECGAAFTSK LEGMFKDMEL
510 520 530 540 550
SKDIMVHFKQ HMQNQSDSGP IDLTVNILTM GYWPTYTPME VHLTPEMIKL
560 570 580 590 600
QEVFKAFYLG KHSGRKLQWQ TTLGHAVLKA EFKEGKKEFQ VSLFQTLVLL
610 620 630 640 650
MFNEGDGFSF EEIKMATGIE DSELRRTLQS LACGKARVLI KSPKGKEVED
660 670 680 690 700
GDKFIFNGEF KHKLFRIKIN QIQMKETVEE QVSTTERVFQ DRQYQIDAAI
710 720 730 740 750
VRIMKMRKTL GHNLLVSELY NQLKFPVKPG DLKKRIESLI DRDYMERDKD
NPNQYHYVA
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketA0A0A0MR50 | A0A0A0MR50_HUMAN | Cullin-4A | CUL4A | 667 | Annotation score: | ||
A0A087WWN2 | A0A087WWN2_HUMAN | Cullin-4A | CUL4A | 174 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 281 | S → T in BAD93235 (PubMed:15811626).Curated | 1 | |
Sequence conflicti | 339 – 346 | HWSEYIKT → NSARARAA in AAC50547 (PubMed:8681378).Curated | 8 | |
Sequence conflicti | 496 | K → R in BAD93235 (PubMed:15811626).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_020341 | 644 | K → R. Corresponds to variant dbSNP:rs2302757Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_018577 | 1 – 100 | Missing in isoform 2. 1 PublicationAdd BLAST | 100 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF077188 mRNA Translation: AAD45191.1 AY365124 mRNA Translation: AAR13072.1 AB178950 mRNA Translation: BAD93235.1 AL136221 Genomic DNA No translation available. BC008308 mRNA Translation: AAH08308.2 AB012193 mRNA Translation: BAA33146.1 U58090 mRNA Translation: AAC50547.1 |
CCDSi | CCDS41908.1 [Q13619-1] CCDS9533.1 [Q13619-2] |
RefSeqi | NP_001008895.1, NM_001008895.2 [Q13619-1] NP_001265442.1, NM_001278513.1 [Q13619-2] NP_003580.1, NM_003589.2 [Q13619-2] XP_011535825.1, XM_011537523.2 [Q13619-2] |
Genome annotation databases
Ensembli | ENST00000375440.9; ENSP00000364589.4; ENSG00000139842.15 ENST00000375441.7; ENSP00000364590.3; ENSG00000139842.15 [Q13619-2] ENST00000451881.5; ENSP00000389118.1; ENSG00000139842.15 [Q13619-2] ENST00000617546.4; ENSP00000481782.1; ENSG00000139842.15 [Q13619-2] |
GeneIDi | 8451 |
KEGGi | hsa:8451 |
MANE-Selecti | ENST00000375440.9; ENSP00000364589.4; NM_001008895.4; NP_001008895.1 |
UCSCi | uc021rmu.2, human [Q13619-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AF077188 mRNA Translation: AAD45191.1 AY365124 mRNA Translation: AAR13072.1 AB178950 mRNA Translation: BAD93235.1 AL136221 Genomic DNA No translation available. BC008308 mRNA Translation: AAH08308.2 AB012193 mRNA Translation: BAA33146.1 U58090 mRNA Translation: AAC50547.1 |
CCDSi | CCDS41908.1 [Q13619-1] CCDS9533.1 [Q13619-2] |
RefSeqi | NP_001008895.1, NM_001008895.2 [Q13619-1] NP_001265442.1, NM_001278513.1 [Q13619-2] NP_003580.1, NM_003589.2 [Q13619-2] XP_011535825.1, XM_011537523.2 [Q13619-2] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
2HYE | X-ray | 3.10 | C | 1-759 | [»] | |
4A0K | X-ray | 5.93 | A | 38-759 | [»] | |
7OKQ | electron microscopy | 8.40 | C/G/K/O | 35-759 | [»] | |
7OPC | electron microscopy | 3.00 | e | 1-759 | [»] | |
7OPD | electron microscopy | 3.00 | e | 1-759 | [»] | |
AlphaFoldDBi | Q13619 | |||||
SMRi | Q13619 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 114029, 773 interactors |
ComplexPortali | CPX-477, CRL4-DDB2 E3 ubiquitin ligase complex, CUL4A variant |
CORUMi | Q13619 |
DIPi | DIP-31610N |
IntActi | Q13619, 209 interactors |
MINTi | Q13619 |
STRINGi | 9606.ENSP00000364589 |
Chemistry databases
ChEMBLi | CHEMBL4523598 |
PTM databases
GlyGeni | Q13619, 1 site, 1 O-linked glycan (1 site) |
iPTMneti | Q13619 |
MetOSitei | Q13619 |
PhosphoSitePlusi | Q13619 |
Genetic variation databases
BioMutai | CUL4A |
DMDMi | 108936013 |
Proteomic databases
EPDi | Q13619 |
jPOSTi | Q13619 |
MassIVEi | Q13619 |
MaxQBi | Q13619 |
PaxDbi | Q13619 |
PeptideAtlasi | Q13619 |
PRIDEi | Q13619 |
ProteomicsDBi | 59609 [Q13619-1] 59610 [Q13619-2] |
Protocols and materials databases
Antibodypediai | 11756, 398 antibodies from 38 providers |
DNASUi | 8451 |
Genome annotation databases
Ensembli | ENST00000375440.9; ENSP00000364589.4; ENSG00000139842.15 ENST00000375441.7; ENSP00000364590.3; ENSG00000139842.15 [Q13619-2] ENST00000451881.5; ENSP00000389118.1; ENSG00000139842.15 [Q13619-2] ENST00000617546.4; ENSP00000481782.1; ENSG00000139842.15 [Q13619-2] |
GeneIDi | 8451 |
KEGGi | hsa:8451 |
MANE-Selecti | ENST00000375440.9; ENSP00000364589.4; NM_001008895.4; NP_001008895.1 |
UCSCi | uc021rmu.2, human [Q13619-1] |
Organism-specific databases
CTDi | 8451 |
DisGeNETi | 8451 |
GeneCardsi | CUL4A |
HGNCi | HGNC:2554, CUL4A |
HPAi | ENSG00000139842, Tissue enhanced (skeletal) |
MIMi | 603137, gene |
neXtProti | NX_Q13619 |
OpenTargetsi | ENSG00000139842 |
PharmGKBi | PA27050 |
VEuPathDBi | HostDB:ENSG00000139842 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG2167, Eukaryota |
GeneTreei | ENSGT00940000156905 |
HOGENOMi | CLU_004747_7_2_1 |
InParanoidi | Q13619 |
OMAi | DNVVQSC |
OrthoDBi | 1040292at2759 |
PhylomeDBi | Q13619 |
TreeFami | TF101153 |
Enzyme and pathway databases
UniPathwayi | UPA00143 |
PathwayCommonsi | Q13619 |
Reactomei | R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex R-HSA-5696394, DNA Damage Recognition in GG-NER R-HSA-5696395, Formation of Incision Complex in GG-NER R-HSA-5696400, Dual Incision in GG-NER R-HSA-6781823, Formation of TC-NER Pre-Incision Complex R-HSA-6781827, Transcription-Coupled Nucleotide Excision Repair (TC-NER) R-HSA-6782135, Dual incision in TC-NER R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER R-HSA-8951664, Neddylation |
SignaLinki | Q13619 |
SIGNORi | Q13619 |
Miscellaneous databases
BioGRID-ORCSi | 8451, 17 hits in 1123 CRISPR screens |
ChiTaRSi | CUL4A, human |
EvolutionaryTracei | Q13619 |
GeneWikii | CUL4A |
GenomeRNAii | 8451 |
Pharosi | Q13619, Tchem |
PROi | PR:Q13619 |
RNActi | Q13619, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000139842, Expressed in skeletal muscle tissue and 245 other tissues |
ExpressionAtlasi | Q13619, baseline and differential |
Genevisiblei | Q13619, HS |
Family and domain databases
Gene3Di | 1.10.10.10, 1 hit |
IDEALi | IID00514 |
InterProi | View protein in InterPro IPR045093, Cullin IPR016157, Cullin_CS IPR016158, Cullin_homology IPR036317, Cullin_homology_sf IPR001373, Cullin_N IPR019559, Cullin_neddylation_domain IPR016159, Cullin_repeat-like_dom_sf IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
PANTHERi | PTHR11932, PTHR11932, 1 hit |
Pfami | View protein in Pfam PF00888, Cullin, 1 hit PF10557, Cullin_Nedd8, 1 hit |
SMARTi | View protein in SMART SM00182, CULLIN, 1 hit SM00884, Cullin_Nedd8, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit SSF74788, SSF74788, 1 hit SSF75632, SSF75632, 1 hit |
PROSITEi | View protein in PROSITE PS01256, CULLIN_1, 1 hit PS50069, CULLIN_2, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | CUL4A_HUMAN | |
Accessioni | Q13619Primary (citable) accession number: Q13619 Secondary accession number(s): A2A2W2 Q9UP17 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | May 30, 2006 | |
Last modified: | May 25, 2022 | |
This is version 198 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- Human chromosome 13
Human chromosome 13: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families