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Q13619 (CUL4A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cullin-4A

Short name=CUL-4A
Gene names
Name:CUL4A
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length759 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.11 Ref.13 Ref.14 Ref.18 Ref.20 Ref.29 Ref.30

Pathway

Protein modification; protein ubiquitination.

Subunit structure

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. Ref.2 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.25 Ref.28

Post-translational modification

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.

Sequence similarities

Belongs to the cullin family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13619-1)

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.
Isoform 2 (identifier: Q13619-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 759759Cullin-4A
PRO_0000119795

Amino acid modifications

Modified residue101Phosphoserine Ref.24 Ref.26
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link705Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in NEDD8) By similarity

Natural variations

Alternative sequence1 – 100100Missing in isoform 2.
VSP_018577
Natural variant6441K → R.
Corresponds to variant rs2302757 [ dbSNP | Ensembl ].
VAR_020341

Experimental info

Mutagenesis86 – 905LYQAV → AAAAA: Largely reduces interaction with DDB1; abolishes interaction with DDB2. Ref.16 Ref.17
Mutagenesis139 – 1424WQDH → AADA: Largely reduces interaction with DDB1; abolishes interaction with DDB2. Ref.16 Ref.17
Sequence conflict2811S → T in BAD93235. Ref.3
Sequence conflict339 – 3468HWSEYIKT → NSARARAA in AAC50547. Ref.7
Sequence conflict4961K → R in BAD93235. Ref.3

Secondary structure

............................................................................................................ 759
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 30, 2006. Version 3.
Checksum: 3C4C6A1BBD94D51B

FASTA75987,680
        10         20         30         40         50         60 
MADEAPRKGS FSALVGRTNG LTKPAALAAA PAKPGGAGGS KKLVIKNFRD RPRLPDNYTQ 

        70         80         90        100        110        120 
DTWRKLHEAV RAVQSSTSIR YNLEELYQAV ENLCSHKVSP MLYKQLRQAC EDHVQAQILP 

       130        140        150        160        170        180 
FREDSLDSVL FLKKINTCWQ DHCRQMIMIR SIFLFLDRTY VLQNSTLPSI WDMGLELFRT 

       190        200        210        220        230        240 
HIISDKMVQS KTIDGILLLI ERERSGEAVD RSLLRSLLGM LSDLQVYKDS FELKFLEETN 

       250        260        270        280        290        300 
CLYAAEGQRL MQEREVPEYL NHVSKRLEEE GDRVITYLDH STQKPLIACV EKQLLGEHLT 

       310        320        330        340        350        360 
AILQKGLDHL LDENRVPDLA QMYQLFSRVR GGQQALLQHW SEYIKTFGTA IVINPEKDKD 

       370        380        390        400        410        420 
MVQDLLDFKD KVDHVIEVCF QKNERFVNLM KESFETFINK RPNKPAELIA KHVDSKLRAG 

       430        440        450        460        470        480 
NKEATDEELE RTLDKIMILF RFIHGKDVFE AFYKKDLAKR LLVGKSASVD AEKSMLSKLK 

       490        500        510        520        530        540 
HECGAAFTSK LEGMFKDMEL SKDIMVHFKQ HMQNQSDSGP IDLTVNILTM GYWPTYTPME 

       550        560        570        580        590        600 
VHLTPEMIKL QEVFKAFYLG KHSGRKLQWQ TTLGHAVLKA EFKEGKKEFQ VSLFQTLVLL 

       610        620        630        640        650        660 
MFNEGDGFSF EEIKMATGIE DSELRRTLQS LACGKARVLI KSPKGKEVED GDKFIFNGEF 

       670        680        690        700        710        720 
KHKLFRIKIN QIQMKETVEE QVSTTERVFQ DRQYQIDAAI VRIMKMRKTL GHNLLVSELY 

       730        740        750 
NQLKFPVKPG DLKKRIESLI DRDYMERDKD NPNQYHYVA 

« Hide

Isoform 2 [UniParc].

Checksum: 56D4D196BB1074CB
Show »

FASTA65976,821

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"A new NEDD8-ligating system for cullin-4A."
Osaka F., Kawasaki H., Aida N., Saeki M., Chiba T., Kawashima S., Tanaka K., Kato S.
Genes Dev. 12:2263-2268(1998) [PubMed] [Europe PMC] [Abstract]
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]"Two E3 ubiquitin ligases, SCF-Skp2 and DDB1-Cul4, target human Cdt1 for proteolysis."
Nishitani H., Sugimoto N., Roukos V., Nakanishi Y., Saijo M., Obuse C., Tsurimoto T., Nakayama K.I., Nakayama K., Fujita M., Lygerou Z., Nishimoto T.
EMBO J. 25:1126-1136(2006) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001008895.1. NM_001008895.2.
NP_001265442.1. NM_001278513.1.
NP_003580.1. NM_003589.2.
UniGeneHs.339735.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HYEX-ray3.10C1-759[»]
4A0KX-ray5.93A35-759[»]
ProteinModelPortalQ13619.
SMRQ13619. Positions 41-759.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114029. 273 interactions.
DIPDIP-31610N.
IntActQ13619. 35 interactions.
MINTMINT-4532640.
STRING9606.ENSP00000364589.

PTM databases

PhosphoSiteQ13619.

Polymorphism databases

DMDM108936013.

Proteomic databases

PaxDbQ13619.
PRIDEQ13619.

Protocols and materials databases

DNASU8451.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326335; ENSP00000322132; ENSG00000139842. [Q13619-2]
ENST00000375440; ENSP00000364589; ENSG00000139842. [Q13619-1]
ENST00000375441; ENSP00000364590; ENSG00000139842. [Q13619-2]
ENST00000451881; ENSP00000389118; ENSG00000139842. [Q13619-2]
GeneID8451.
KEGGhsa:8451.
UCSCuc010agu.3. human. [Q13619-1]

Organism-specific databases

CTD8451.
GeneCardsGC13P113863.
HGNCHGNC:2554. CUL4A.
MIM603137. gene.
neXtProtNX_Q13619.
PharmGKBPA27050.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5647.
HOVERGENHBG003619.
InParanoidQ13619.
KOK10609.
OMAHVVEVCF.
OrthoDBEOG75TMB5.
PhylomeDBQ13619.
TreeFamTF101153.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressQ13619.
BgeeQ13619.
CleanExHS_CUL4A.
GenevestigatorQ13619.

Family and domain databases

Gene3D1.10.10.10. 2 hits.
InterProIPR016157. Cullin_CS.
IPR016158. Cullin_homology.
IPR001373. Cullin_N.
IPR019559. Cullin_neddylation_domain.
IPR016159. Cullin_repeat-like_dom.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00888. Cullin. 1 hit.
PF10557. Cullin_Nedd8. 1 hit.
[Graphical view]
SMARTSM00182. CULLIN. 1 hit.
SM00884. Cullin_Nedd8. 1 hit.
[Graphical view]
SUPFAMSSF74788. SSF74788. 1 hit.
SSF75632. SSF75632. 1 hit.
PROSITEPS01256. CULLIN_1. 1 hit.
PS50069. CULLIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ13619.
GeneWikiCUL4A.
GenomeRNAi8451.
NextBio31624.
PROQ13619.
SOURCESearch...

Entry information

Entry nameCUL4A_HUMAN
AccessionPrimary (citable) accession number: Q13619
Secondary accession number(s): A2A2W2 expand/collapse secondary AC list , O75834, Q589T6, Q5TC62, Q6UP08, Q9UP17
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 30, 2006
Last modified: April 16, 2014
This is version 131 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM