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A1A4K3 (DDB1_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA damage-binding protein 1
Alternative name(s):
Damage-specific DNA-binding protein 1
Gene names
Name:DDB1
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length1140 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Required for DNA repair. Binds to DDB2 to form the UV-damaged DNA-binding protein complex (the UV-DDB complex). The UV-DDB complex may recognize UV-induced DNA damage and recruit proteins of the nucleotide excision repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also appears to function as a component of numerous distinct DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. The functional specificity of the DCX E3 ubiquitin-protein ligase complex is determined by the variable substrate recognition component recruited by DDB1. DCX(DDB2) (also known as DDB1-CUL4-ROC1, CUL4-DDB-ROC1 and CUL4-DDB-RBX1) may ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-induced DNA damage. The ubiquitination of histones may facilitate their removal from the nucleosome and promote subsequent DNA repair. DCX(DDB2) also ubiquitinates XPC, which may enhance DNA-binding by XPC and promote NER. 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. DCX(ERCC8) (the CSA complex) plays a role in transcription-coupled repair (TCR). May also play a role in ubiquitination of CDKN1B/p27kip when associated with CUL4 and SKP2 By similarity.

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Component of the UV-DDB complex which includes DDB1 and DDB2. The UV-DDB complex interacts with monoubiquitinated histone H2A and binds to XPC via the DDB2 subunit. Component of numerous DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complexes which consist of a core of DDB1, CUL4A or CUL4B and RBX1. DDB1 may recruit specific substrate targeting subunits to the DCX complex. These substrate targeting subunits are generally known as DCAF (DDB1- and CUL4-associated factor) or CDW (CUL4-DDB1-associated WD40-repeat) proteins. Interacts with AMBRA1, ATG16L1, BTRC, DCAF17, DCAF16, DCAF15, DDA1, DET1, DTL, ERCC8, FBXW5, FBXW8, GRWD1, DCAF6, KATNB1, NLE1, NUP43, PAFAH1B1, PHIP, PWP1, RBBP4, RBBP5, RBBP7, RFWD2, SNRNP40, VPRBP, WDR5, WDR5B, WDR12, DCAF4, DCAF5, DCAF11, WDR26, DCAF10, WDR39, DCAF12, WDR42, DCAF8, WDR53, WDR59, WDR61, DCAF7, WSB1, WSB2, LRWD1 and WDTC1. DCX complexes may associate with the COP9 signalosome, and this inhibits the E3 ubiquitin-protein ligase activity of the complex. Interacts with NF2, TSC1 and TSC2. Interacts with AGO1 and AGO2. Associates with the E3 ligase complex containing DYRK2, EDD/UBR5, DDB1 and VPRBP proteins (EDVP complex). Interacts directly with DYRK2 By similarity.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity. Note: Primarily cytoplasmic. Translocates to the nucleus following UV irradiation and subsequently accumulates at sites of DNA damage By similarity.

Post-translational modification

Ubiquitinated by CUL4A. Subsequently degraded by ubiquitin-dependent proteolysis By similarity.

Sequence similarities

Belongs to the DDB1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 11401139DNA damage-binding protein 1
PRO_0000281035

Regions

Region2 – 768767Interaction with CDT1 By similarity
Region391 – 709319Interaction with CUL4A By similarity
Region771 – 1140370Interaction with CDT1 and CUL4A By similarity

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue10671N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
A1A4K3 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 8E4A2A0859180271

FASTA1,140126,930
        10         20         30         40         50         60 
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK 

        70         80         90        100        110        120 
IAVMELFRPK GESKDLLFIL TAKYNACILE YKQSGESIDI ITRAHGNVQD RIGRPSETGI 

       130        140        150        160        170        180 
IGIIDPECRM IGLRLYDGLF KVIPLDRDNK ELKAFNIRLE ELHVIDVKFL YGCQAPTICF 

       190        200        210        220        230        240 
VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH 

       250        260        270        280        290        300 
NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL 

       310        320        330        340        350        360 
RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV 

       370        380        390        400        410        420 
DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDPNRE 

       430        440        450        460        470        480 
TDDTLVLSFV GQTRVLMLNG EEVEETELMG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS 

       490        500        510        520        530        540 
QEPKALVSEW KEPQGKNISV ASCNSSQVVV AVGRALYYLQ IHPQELRQIS HTEMEHEVAC 

       550        560        570        580        590        600 
LDITPLGDSN GMSPLCAIGL WTDISARIAK LPSFELLHKE MLGGEIIPRS ILMTTFESSH 

       610        620        630        640        650        660 
YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY 

       670        680        690        700        710        720 
SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES 

       730        740        750        760        770        780 
PRKICYQEVS QCFGVLSSRI EVQDTSGGTT ALRPSASTQA LSSSVSSSKL FSSSTAPHET 

       790        800        810        820        830        840 
SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE 

       850        860        870        880        890        900 
AEPKQGRIVV FQYSDGKLQT VAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTTEKELR 

       910        920        930        940        950        960 
TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL 

       970        980        990       1000       1010       1020 
DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLFHL GEFVNVFCHG SLVMQNLGET 

      1030       1040       1050       1060       1070       1080 
STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER 

      1090       1100       1110       1120       1130       1140 
KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQYDDGSGM KREATADDLI KVVEELTRIH 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Fetal muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC126629 mRNA. Translation: AAI26630.1.
RefSeqNP_001073731.1. NM_001080262.1.
UniGeneBt.62917.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000028740.

Proteomic databases

PaxDbA1A4K3.
PRIDEA1A4K3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000028740; ENSBTAP00000028740; ENSBTAG00000021569.
GeneID511951.
KEGGbta:511951.

Organism-specific databases

CTD1642.

Phylogenomic databases

eggNOGNOG247734.
GeneTreeENSGT00530000063396.
HOGENOMHOG000007241.
HOVERGENHBG005460.
InParanoidA1A4K3.
KOK10610.
OMAMCPLNSE.
OrthoDBEOG7X0VG9.
TreeFamTF105840.

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

Gene3D2.130.10.10. 4 hits.
InterProIPR004871. Cleavage/polyA-sp_fac_asu_C.
IPR011047. Quinonprotein_ADH-like_supfam.
IPR015943. WD40/YVTN_repeat-like_dom.
[Graphical view]
PfamPF03178. CPSF_A. 1 hit.
[Graphical view]
SUPFAMSSF50998. SSF50998. 2 hits.
ProtoNetSearch...

Other

NextBio20870176.

Entry information

Entry nameDDB1_BOVIN
AccessionPrimary (citable) accession number: A1A4K3
Entry history
Integrated into UniProtKB/Swiss-Prot: March 20, 2007
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways