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Q13619

- CUL4A_HUMAN

UniProt

Q13619 - CUL4A_HUMAN

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Protein

Cullin-4A

Gene

CUL4A

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.8 Publications

Pathwayi

GO - Biological processi

  1. cell cycle arrest Source: ProtInc
  2. DNA repair Source: UniProtKB-KW
  3. G1/S transition of mitotic cell cycle Source: ProtInc
  4. hemopoiesis Source: Ensembl
  5. intrinsic apoptotic signaling pathway Source: ProtInc
  6. negative regulation of cell proliferation Source: ProtInc
  7. negative regulation of granulocyte differentiation Source: Ensembl
  8. positive regulation of cell proliferation Source: Ensembl
  9. positive regulation of G1/S transition of mitotic cell cycle Source: Ensembl
  10. proteasome-mediated ubiquitin-dependent protein catabolic process Source: Ensembl
  11. protein ubiquitination Source: UniProtKB-UniPathway
  12. regulation of DNA damage checkpoint Source: Ensembl
  13. regulation of nucleotide-excision repair Source: Ensembl
  14. regulation of protein metabolic process Source: Ensembl
  15. somatic stem cell maintenance Source: Ensembl
  16. viral process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA repair, Host-virus interaction, Ubl conjugation pathway

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Cullin-4A
Short name:
CUL-4A
Gene namesi
Name:CUL4A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:2554. CUL4A.

Subcellular locationi

GO - Cellular componenti

  1. Cul4A-RING E3 ubiquitin ligase complex Source: UniProtKB
  2. Cul4-RING E3 ubiquitin ligase complex Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi86 – 905LYQAV → AAAAA: Largely reduces interaction with DDB1; abolishes interaction with DDB2. 2 Publications
Mutagenesisi139 – 1424WQDH → AADA: Largely reduces interaction with DDB1; abolishes interaction with DDB2. 2 Publications

Organism-specific databases

PharmGKBiPA27050.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759Cullin-4APRO_0000119795Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine2 Publications
Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki705 – 705Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8)By similarity

Post-translational modificationi

Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex By similarity. Deneddylated by Epstein-Barr virus BPLF1 leading to a S-phase-like environment that is required for efficient replication of the viral genome.By similarity2 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ13619.
PaxDbiQ13619.
PRIDEiQ13619.

PTM databases

PhosphoSiteiQ13619.

Expressioni

Gene expression databases

BgeeiQ13619.
CleanExiHS_CUL4A.
ExpressionAtlasiQ13619. baseline and differential.
GenevestigatoriQ13619.

Interactioni

Subunit structurei

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, CDKN1B, 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, LRWD1 and DCAF8. May interact with WDR26, WDR51B, SNRNP40, WDR61, WDR76, WDR5. Can self-associate. Interacts with Epstein-Barr virus BPLF1.18 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CAND1Q86VP63EBI-456106,EBI-456077
DDB1Q165314EBI-456106,EBI-350322
DDB2Q924662EBI-456106,EBI-1176171
RBBP5Q152913EBI-456106,EBI-592823

Protein-protein interaction databases

BioGridi114029. 284 interactions.
DIPiDIP-31610N.
IntActiQ13619. 37 interactions.
MINTiMINT-4532640.
STRINGi9606.ENSP00000364589.

Structurei

Secondary structure

1
759
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni58 – 614
Helixi62 – 7110
Helixi83 – 9311
Turni96 – 983
Helixi99 – 12123
Helixi130 – 15223
Helixi154 – 1574
Turni158 – 1625
Beta strandi165 – 1673
Helixi170 – 18011
Turni181 – 1833
Beta strandi184 – 1863
Helixi189 – 1913
Helixi193 – 2019
Turni202 – 2065
Helixi211 – 22313
Turni227 – 2315
Helixi232 – 25322
Helixi256 – 26914
Helixi271 – 2744
Turni275 – 2773
Turni280 – 2823
Helixi283 – 29412
Turni295 – 2973
Helixi300 – 3045
Helixi307 – 3115
Turni312 – 3143
Helixi316 – 32813
Helixi332 – 35221
Helixi355 – 3573
Turni358 – 3603
Helixi361 – 37717
Turni378 – 3825
Helixi384 – 39815
Helixi404 – 41714
Helixi421 – 4233
Helixi429 – 44012
Helixi446 – 46217
Helixi469 – 48012
Turni481 – 4833
Turni485 – 4884
Helixi489 – 51325
Beta strandi522 – 5298
Turni530 – 5323
Helixi545 – 55915
Beta strandi564 – 5663
Helixi571 – 5733
Beta strandi575 – 5795
Beta strandi588 – 5925
Helixi593 – 6019
Helixi610 – 6167
Helixi621 – 6299
Turni630 – 6367
Beta strandi638 – 6414
Beta strandi645 – 6473
Beta strandi653 – 6564
Beta strandi665 – 6684
Helixi670 – 6745
Helixi678 – 70629
Beta strandi707 – 7115
Helixi713 – 72210
Beta strandi723 – 7253
Helixi729 – 74113
Beta strandi754 – 7563

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HYEX-ray3.10C1-759[»]
4A0KX-ray5.93A38-759[»]
ProteinModelPortaliQ13619.
SMRiQ13619. Positions 41-759.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13619.

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00760000119212.
HOVERGENiHBG003619.
InParanoidiQ13619.
KOiK10609.
OMAiHVVEVCF.
OrthoDBiEOG75TMB5.
PhylomeDBiQ13619.
TreeFamiTF101153.

Family and domain databases

Gene3Di1.10.10.10. 2 hits.
InterProiIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTiSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMiSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEiPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q13619-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        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
Length:759
Mass (Da):87,680
Last modified:May 30, 2006 - v3
Checksum:i3C4C6A1BBD94D51B
GO
Isoform 2 (identifier: Q13619-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-100: Missing.

Show »
Length:659
Mass (Da):76,821
Checksum:i56D4D196BB1074CB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti281 – 2811S → T in BAD93235. (PubMed:15811626)Curated
Sequence conflicti339 – 3468HWSEYIKT → NSARARAA in AAC50547. (PubMed:8681378)Curated
Sequence conflicti496 – 4961K → R in BAD93235. (PubMed:15811626)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti644 – 6441K → R.
Corresponds to variant rs2302757 [ dbSNP | Ensembl ].
VAR_020341

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 100100Missing in isoform 2. 1 PublicationVSP_018577Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077188 mRNA. Translation: AAD45191.1.
AY365124 mRNA. Translation: AAR13072.1.
AB178950 mRNA. Translation: BAD93235.1.
AL136221 Genomic DNA. Translation: CAM18410.1.
AL136221 Genomic DNA. Translation: CAI13795.1.
BC008308 mRNA. Translation: AAH08308.2.
AB012193 mRNA. Translation: BAA33146.1.
U58090 mRNA. Translation: AAC50547.1.
CCDSiCCDS41908.1. [Q13619-1]
CCDS9533.1. [Q13619-2]
RefSeqiNP_001008895.1. NM_001008895.2. [Q13619-1]
NP_001265442.1. NM_001278513.1. [Q13619-2]
NP_003580.1. NM_003589.2. [Q13619-2]
UniGeneiHs.339735.

Genome annotation databases

EnsembliENST00000375440; ENSP00000364589; ENSG00000139842. [Q13619-1]
ENST00000375441; ENSP00000364590; ENSG00000139842. [Q13619-2]
ENST00000451881; ENSP00000389118; ENSG00000139842. [Q13619-2]
ENST00000617546; ENSP00000481782; ENSG00000139842. [Q13619-2]
GeneIDi8451.
KEGGihsa:8451.
UCSCiuc010agu.3. human. [Q13619-1]

Polymorphism databases

DMDMi108936013.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077188 mRNA. Translation: AAD45191.1 .
AY365124 mRNA. Translation: AAR13072.1 .
AB178950 mRNA. Translation: BAD93235.1 .
AL136221 Genomic DNA. Translation: CAM18410.1 .
AL136221 Genomic DNA. Translation: CAI13795.1 .
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 ]
UniGenei Hs.339735.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HYE X-ray 3.10 C 1-759 [» ]
4A0K X-ray 5.93 A 38-759 [» ]
ProteinModelPortali Q13619.
SMRi Q13619. Positions 41-759.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114029. 284 interactions.
DIPi DIP-31610N.
IntActi Q13619. 37 interactions.
MINTi MINT-4532640.
STRINGi 9606.ENSP00000364589.

PTM databases

PhosphoSitei Q13619.

Polymorphism databases

DMDMi 108936013.

Proteomic databases

MaxQBi Q13619.
PaxDbi Q13619.
PRIDEi Q13619.

Protocols and materials databases

DNASUi 8451.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000375440 ; ENSP00000364589 ; ENSG00000139842 . [Q13619-1 ]
ENST00000375441 ; ENSP00000364590 ; ENSG00000139842 . [Q13619-2 ]
ENST00000451881 ; ENSP00000389118 ; ENSG00000139842 . [Q13619-2 ]
ENST00000617546 ; ENSP00000481782 ; ENSG00000139842 . [Q13619-2 ]
GeneIDi 8451.
KEGGi hsa:8451.
UCSCi uc010agu.3. human. [Q13619-1 ]

Organism-specific databases

CTDi 8451.
GeneCardsi GC13P113863.
HGNCi HGNC:2554. CUL4A.
MIMi 603137. gene.
neXtProti NX_Q13619.
PharmGKBi PA27050.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5647.
GeneTreei ENSGT00760000119212.
HOVERGENi HBG003619.
InParanoidi Q13619.
KOi K10609.
OMAi HVVEVCF.
OrthoDBi EOG75TMB5.
PhylomeDBi Q13619.
TreeFami TF101153.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

EvolutionaryTracei Q13619.
GeneWikii CUL4A.
GenomeRNAii 8451.
NextBioi 31624.
PROi Q13619.
SOURCEi Search...

Gene expression databases

Bgeei Q13619.
CleanExi HS_CUL4A.
ExpressionAtlasi Q13619. baseline and differential.
Genevestigatori Q13619.

Family and domain databases

Gene3Di 1.10.10.10. 2 hits.
InterProi IPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view ]
SMARTi SM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view ]
SUPFAMi SSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEi PS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human homologue for the Caenorhabditis elegans cul-4 gene is amplified and overexpressed in primary breast cancers."
    Chen L.-C., Manjeshwar S., Lu Y., Moore D., Ljung B.M., Kuo W.L., Dairkee S.H., Wernick M., Collins C., Smith H.S.
    Cancer Res. 58:3677-3683(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint."
    Higa L.A., Mihaylov I.S., Banks D.P., Zheng J., Zhang H.
    Nat. Cell Biol. 5:1008-1015(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH CDT1.
  3. "DDB2, the xeroderma pigmentosum group E gene product, is directly ubiquitylated by Cullin 4A-based ubiquitin ligase complex."
    Matsuda N., Azuma K., Saijo M., Iemura S., Hioki Y., Natsume T., Chiba T., Tanaka K., Tanaka K.
    DNA Repair 4:537-545(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lung.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 236-759 (ISOFORMS 1/2), NEDDYLATION.
  7. "cul-1 is required for cell cycle exit in C. elegans and identifies a novel gene family."
    Kipreos E.T., Lander L.E., Wing J.P., He W.W., Hedgecock E.M.
    Cell 85:829-839(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 339-759 (ISOFORMS 1/2).
  8. "Covalent modification of all members of human cullin family proteins by NEDD8."
    Hori T., Osaka F., Chiba T., Miyamoto C., Okabayashi K., Shimbara N., Kato S., Tanaka K.
    Oncogene 18:6829-6834(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NEDDYLATION.
  9. "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity."
    Ohta T., Michel J.J., Schottelius A.J., Xiong Y.
    Mol. Cell 3:535-541(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RBX1 AND RNF7.
  10. "The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage."
    Groisman R., Polanowska J., Kuraoka I., Sawada J., Saijo M., Drapkin R., Kisselev A.F., Tanaka K., Nakatani Y.
    Cell 113:357-367(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE CSA COMPLEX WITH RBX1; DDB1 AND ERCC8, INTERACTION OF THE CSA COMPLEX WITH RNA POLYMERASE II AND THE COP9 SIGNALOSOME.
  11. "CUL-4A stimulates ubiquitylation and degradation of the HOXA9 homeodomain protein."
    Zhang Y., Morrone G., Zhang J., Chen X., Lu X., Ma L., Moore M., Zhou P.
    EMBO J. 22:6057-6067(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HOXA9, FUNCTION IN UBIQUITINATION OF HOXA9.
  12. "TIP120A associates with cullins and modulates ubiquitin ligase activity."
    Min K.-W., Hwang J.-W., Lee J.-S., Park Y., Tamura T.-A., Yoon J.-B.
    J. Biol. Chem. 278:15905-15910(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIP120A.
  13. "Cul4A physically associates with MDM2 and participates in the proteolysis of p53."
    Nag A., Bagchi S., Raychaudhuri P.
    Cancer Res. 64:8152-8155(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MDM2 AND TP53, FUNCTION IN UBIQUITINATION OF TP53.
  14. "Targeted ubiquitination of CDT1 by the DDB1-CUL4A-ROC1 ligase in response to DNA damage."
    Hu J., McCall C.M., Ohta T., Xiong Y.
    Nat. Cell Biol. 6:1003-1009(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDB1, FUNCTION IN CTD1 UBIQUITINATION.
  15. "Human De-etiolated-1 regulates c-Jun by assembling a CUL4A ubiquitin ligase."
    Wertz I.E., O'Rourke K.M., Zhang Z., Dornan D., Arnott D., Deshaies R.J., Dixit V.M.
    Science 303:1371-1374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE DCX(DET1-COP1) COMPLEX WITH DDB1; RBX1; COP1 AND DET1.
  16. Cited for: INTERACTION WITH DDB1; DDB2 AND CAND1, MUTAGENESIS OF 86-LEU--VAL-90 AND 139-TRP--HIS-142.
  17. "DDB1 functions as a linker to recruit receptor WD40 proteins to CUL4-ROC1 ubiquitin ligases."
    He Y.J., McCall C.M., Hu J., Zeng Y., Xiong Y.
    Genes Dev. 20:2949-2954(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VPRBP; DDB2; ERCC8; DCAF11; GRWD1; RFWD2; FBXW5; RBBP7; GNB2; WSB1; WSB2; NUP43; PWP1; FBXW8; ATG16L1; KATNB1 AND RBBP4, MUTAGENESIS OF 86-LEU--VAL-90 AND 139-TRP--HIS-142.
  18. "Histone H3 and H4 ubiquitylation by the CUL4-DDB-ROC1 ubiquitin ligase facilitates cellular response to DNA damage."
    Wang H., Zhai L., Xu J., Joo H.-Y., Jackson S., Erdjument-Bromage H., Tempst P., Xiong Y., Zhang Y.
    Mol. Cell 22:383-394(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN COMPLEX WITH DDB1; DDB2 AND RBX1, IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION.
  19. "A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2, which is required for S phase destruction of the replication factor Cdt1."
    Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.
    Mol. Cell 23:709-721(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH VPRBP; DTL; DDA1; DCAF6; DCAF4; DCAF16; DCAF17; DDB2; DET1; WDTC1; DCAF5; DCAF11; WDR24A; RFWD2; PAFAH1B1 AND DCAF8.
  20. "Cul4A and DDB1 associate with Skp2 to target p27Kip1 for proteolysis involving the COP9 signalosome."
    Bondar T., Kalinina A., Khair L., Kopanja D., Nag A., Bagchi S., Raychaudhuri P.
    Mol. Cell. Biol. 26:2531-2539(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SKP2 AND CDKN1B, FUNCTION IN UBIQUITINATION OF CDKN1B.
  21. "CUL4-DDB1 ubiquitin ligase interacts with multiple WD40-repeat proteins and regulates histone methylation."
    Higa L.A., Wu M., Ye T., Kobayashi R., Sun H., Zhang H.
    Nat. Cell Biol. 8:1277-1283(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDB2; WDR26; RBBP5; RFWD2; WDR51B; SNRNP40; WDR61; WDR76 AND WDR5.
  22. "Characterization of cullin-based E3 ubiquitin ligases in intact mammalian cells -- evidence for cullin dimerization."
    Chew E.H., Poobalasingam T., Hawkey C.J., Hagen T.
    Cell. Signal. 19:1071-1080(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION.
  23. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "A deneddylase encoded by Epstein-Barr virus promotes viral DNA replication by regulating the activity of cullin-RING ligases."
    Gastaldello S., Hildebrand S., Faridani O., Callegari S., Palmkvist M., Di Guglielmo C., Masucci M.G.
    Nat. Cell Biol. 12:351-361(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH EPSTEIN-BARR VIRUS BPLF1, DENEDDYLATION BY EPSTEIN-BARR VIRUS BPLF1.
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Orc2 protects ORCA from ubiquitin-mediated degradation."
    Shen Z., Prasanth S.G.
    Cell Cycle 11:3578-3589(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRWD1.
  29. "A Cul4 E3 ubiquitin ligase regulates histone hand-off during nucleosome assembly."
    Han J., Zhang H., Zhang H., Wang Z., Zhou H., Zhang Z.
    Cell 155:817-829(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF H3.
  30. "CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration."
    Abbas T., Mueller A.C., Shibata E., Keaton M., Rossi M., Dutta A.
    Mol. Cell 49:1147-1158(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN UBIQUITINATION OF DTL.
  31. "Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery."
    Angers S., Li T., Yi X., MacCoss M.J., Moon R.T., Zheng N.
    Nature 443:590-593(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) IN COMPLEX WITH DDB1; RBX1 AND SV5-V.
  32. "The molecular basis of CRL4DDB2/CSA ubiquitin ligase architecture, targeting, and activation."
    Fischer E.S., Scrima A., Bohm K., Matsumoto S., Lingaraju G.M., Faty M., Yasuda T., Cavadini S., Wakasugi M., Hanaoka F., Iwai S., Gut H., Sugasawa K., Thoma N.H.
    Cell 147:1024-1039(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (5.93 ANGSTROMS) OF 38-759 IN COMPLEX WITH DDB1; RBX1 AND DDB2.

Entry informationi

Entry nameiCUL4A_HUMAN
AccessioniPrimary (citable) accession number: Q13619
Secondary accession number(s): A2A2W2
, O75834, Q589T6, Q5TC62, Q6UP08, Q9UP17
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2006
Last modified: October 29, 2014
This is version 137 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3