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Q3TCH7

- CUL4A_MOUSE

UniProt

Q3TCH7 - CUL4A_MOUSE

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Protein

Cullin-4A

Gene

Cul4a

Organism
Mus musculus (Mouse)
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 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 CDKN1B/p27kip. Is involved in ubiquitination of HOXA9. DCX(DTL) directs autoubiquitination of DTL (By similarity).By similarity

Pathwayi

GO - Biological processi

  1. DNA repair Source: UniProtKB-KW
  2. hemopoiesis Source: MGI
  3. negative regulation of granulocyte differentiation Source: MGI
  4. positive regulation of cell proliferation Source: MGI
  5. positive regulation of G1/S transition of mitotic cell cycle Source: MGI
  6. positive regulation of protein catabolic process Source: MGI
  7. proteasome-mediated ubiquitin-dependent protein catabolic process Source: MGI
  8. protein ubiquitination Source: UniProtKB-UniPathway
  9. regulation of DNA damage checkpoint Source: MGI
  10. regulation of nucleotide-excision repair Source: MGI
  11. regulation of protein metabolic process Source: MGI
  12. somatic stem cell maintenance Source: MGI
  13. ubiquitin-dependent protein catabolic process Source: MGI
  14. 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 8

Organism-specific databases

MGIiMGI:1914487. 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...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 759759Cullin-4APRO_0000236184Add
BLAST

Amino acid modifications

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

Post-translational modificationi

Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity). Deneddylated by murine cytomegalovirus M48 leading to a S-phase-like environment that is required for efficient replication of the viral genome.By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ3TCH7.
PaxDbiQ3TCH7.
PRIDEiQ3TCH7.

PTM databases

PhosphoSiteiQ3TCH7.

Expressioni

Gene expression databases

BgeeiQ3TCH7.
CleanExiMM_CUL4A.
ExpressionAtlasiQ3TCH7. baseline and differential.
GenevestigatoriQ3TCH7.

Interactioni

Subunit structurei

Component of multiple DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes that seem to be formed 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 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 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(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 murine cytomegalovirus M48.1 Publication

Protein-protein interaction databases

BioGridi221235. 13 interactions.
IntActiQ3TCH7. 5 interactions.
MINTiMINT-4122171.

Structurei

3D structure databases

ProteinModelPortaliQ3TCH7.
SMRiQ3TCH7. Positions 41-759.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cullin family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5647.
GeneTreeiENSGT00760000119212.
HOGENOMiHOG000176712.
HOVERGENiHBG003619.
InParanoidiQ3TCH7.
KOiK10609.
OMAiHVVEVCF.
OrthoDBiEOG75TMB5.
PhylomeDBiQ3TCH7.
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]

Sequencei

Sequence statusi: Complete.

Q3TCH7-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MADEGPRKGS VSALMGRTNG LTKPAALAGG PAKPGGTGGS RKLVIKNFRD
60 70 80 90 100
RPRLPDNYTQ DTWRKLHEAV KAIQSSTSIR YNLEELYQAV ENLCSHKVSP
110 120 130 140 150
TLYKQLRQVC EDHVQAQILP FREDSLDSVL FLKKINTCWQ DHCRQMIMIR
160 170 180 190 200
SIFLFLDRTY VLQNSMLPSI WDMGLELFRN HIISDRMVQS KTIDGILLLI
210 220 230 240 250
GRERSGEAVD RSLLRSLLSM LSDLQVYKDS FELKFLEETN CLYAAEGQRL
260 270 280 290 300
MQDREVPEYL NHVSKRLEEE ADRVITYLDH STQKPLIACV EKQLLGEHLT
310 320 330 340 350
AILQKGLEHL LDENRVPDLT QMYQLFSRVK GGQHALLQHW SEYIKTFGTT
360 370 380 390 400
IVINPEKDKD MVQDLLDFKD KVDHVVEVCF QRNERFINLM KESFETFINK
410 420 430 440 450
RPNKPAELIA KHVDSKLRAG NKEATDEELE RILDKIMILF RFIHGKDVFE
460 470 480 490 500
AFYKKDLAKR LLVGKSASVD AEKSMLSKLK HECGAAFTSK LEGMFKDMEL
510 520 530 540 550
SKDIMVHFKQ HMQNQSAPGP IDLTVNILTM GYWPTYTPME VHLPPEMVRL
560 570 580 590 600
QEVFKTFYLG KHSGRKLQWQ TTLGHAVLKA DFKEGKKEFQ VSLFQTLVLL
610 620 630 640 650
MFNEGDGFSF EEIKMATGIE DSELRRTLQS LACGKARVLI KSPKGKEVED
660 670 680 690 700
GDKFIFNADF KHKLFRIKIN QIQMKETVEE QVSTTERVFQ DRQYQIDAAI
710 720 730 740 750
VRIMKMRKTL GHNLLVSELY NQLKFPVKPG DLKKRIESLI DRDYMERDKD

SPNQYHYVA
Length:759
Mass (Da):87,753
Last modified:October 11, 2005 - v1
Checksum:i464271E22FB65F2D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti756 – 7561H → R in BAE40173. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK168215 mRNA. Translation: BAE40173.1.
AK170722 mRNA. Translation: BAE41979.1.
BC010211 mRNA. Translation: AAH10211.2.
CCDSiCCDS52485.1.
RefSeqiNP_666319.2. NM_146207.2.
UniGeneiMm.212861.

Genome annotation databases

EnsembliENSMUST00000016680; ENSMUSP00000016680; ENSMUSG00000031446.
GeneIDi99375.
KEGGimmu:99375.
UCSCiuc009kww.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK168215 mRNA. Translation: BAE40173.1 .
AK170722 mRNA. Translation: BAE41979.1 .
BC010211 mRNA. Translation: AAH10211.2 .
CCDSi CCDS52485.1.
RefSeqi NP_666319.2. NM_146207.2.
UniGenei Mm.212861.

3D structure databases

ProteinModelPortali Q3TCH7.
SMRi Q3TCH7. Positions 41-759.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 221235. 13 interactions.
IntActi Q3TCH7. 5 interactions.
MINTi MINT-4122171.

PTM databases

PhosphoSitei Q3TCH7.

Proteomic databases

MaxQBi Q3TCH7.
PaxDbi Q3TCH7.
PRIDEi Q3TCH7.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000016680 ; ENSMUSP00000016680 ; ENSMUSG00000031446 .
GeneIDi 99375.
KEGGi mmu:99375.
UCSCi uc009kww.2. mouse.

Organism-specific databases

CTDi 8451.
MGIi MGI:1914487. Cul4a.

Phylogenomic databases

eggNOGi COG5647.
GeneTreei ENSGT00760000119212.
HOGENOMi HOG000176712.
HOVERGENi HBG003619.
InParanoidi Q3TCH7.
KOi K10609.
OMAi HVVEVCF.
OrthoDBi EOG75TMB5.
PhylomeDBi Q3TCH7.
TreeFami TF101153.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

ChiTaRSi Cul4a. mouse.
NextBioi 353901.
PROi Q3TCH7.
SOURCEi Search...

Gene expression databases

Bgeei Q3TCH7.
CleanExi MM_CUL4A.
ExpressionAtlasi Q3TCH7. baseline and differential.
Genevestigatori Q3TCH7.

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 transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: BALB/c and NOD.
  2. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  3. "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 MURINE CYTOMEGALOVIRUS M48, DENEDDYLATION BY MURINE CYTOMEGALOVIRUS M48.

Entry informationi

Entry nameiCUL4A_MOUSE
AccessioniPrimary (citable) accession number: Q3TCH7
Secondary accession number(s): Q3THM3, Q91Z44
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 11, 2005
Last modified: November 26, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3