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DNA damage-binding protein 1 (DDB p127 subunit) (Damage-specific DNA-binding protein 1) (UV-damaged DNA-binding factor)

 DDB1_CHICK              Reviewed;        1140 AA.
Q805F9;
20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
01-JUN-2003, sequence version 1.
27-SEP-2017, entry version 87.
RecName: Full=DNA damage-binding protein 1;
AltName: Full=DDB p127 subunit;
AltName: Full=Damage-specific DNA-binding protein 1;
AltName: Full=UV-damaged DNA-binding factor;
Name=DDB1; ORFNames=RCJMB04_6h2;
Gallus gallus (Chicken).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes;
Phasianidae; Phasianinae; Gallus.
NCBI_TaxID=9031;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND SUBCELLULAR LOCATION.
PubMed=12773817; DOI=10.1266/ggs.78.169;
Fu D., Wakasugi M., Ishigaki Y., Nikaido O., Matsunaga T.;
"cDNA cloning of the chicken DDB1 gene encoding the p127 subunit of
damaged DNA-binding protein.";
Genes Genet. Syst. 78:169-177(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=CB; TISSUE=Bursa of Fabricius;
PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J.,
Fiedler P., Kutter S., Blagodatski A., Kostovska D., Koter M.,
Plachy J., Carninci P., Hayashizaki Y., Buerstedde J.-M.;
"Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
function analysis.";
Genome Biol. 6:R6.1-R6.9(2005).
[3]
INTERACTION WITH CRBN.
PubMed=25043012; DOI=10.1038/nature13527;
Fischer E.S., Bohm K., Lydeard J.R., Yang H., Stadler M.B.,
Cavadini S., Nagel J., Serluca F., Acker V., Lingaraju G.M.,
Tichkule R.B., Schebesta M., Forrester W.C., Schirle M., Hassiepen U.,
Ottl J., Hild M., Beckwith R.E., Harper J.W., Jenkins J.L.,
Thoma N.H.;
"Structure of the DDB1-CRBN E3 ubiquitin ligase in complex with
thalidomide.";
Nature 512:49-53(2014).
-!- 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 (By similarity). 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.
{ECO:0000250|UniProtKB:Q16531, ECO:0000305|PubMed:25043012}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000305|PubMed:25043012}.
-!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and
DDB2 (By similarity). 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, and a substrate receptor, such as
CRBN (PubMed:25043012). 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.
{ECO:0000250|UniProtKB:Q16531, ECO:0000269|PubMed:25043012,
ECO:0000305}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12773817}.
Nucleus {ECO:0000269|PubMed:12773817}.
-!- DOMAIN: The core of the protein consists of three WD40 beta-
propeller domains. {ECO:0000250}.
-!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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EMBL; AB074298; BAC56999.1; -; mRNA.
EMBL; AJ719779; CAG31438.1; -; mRNA.
RefSeq; NP_989547.1; NM_204216.3.
UniGene; Gga.12977; -.
SMR; Q805F9; -.
STRING; 9031.ENSGALP00000039807; -.
PaxDb; Q805F9; -.
PRIDE; Q805F9; -.
Ensembl; ENSGALT00000064678; ENSGALP00000058261; ENSGALG00000042333.
GeneID; 374050; -.
KEGG; gga:374050; -.
CTD; 1642; -.
eggNOG; KOG1897; Eukaryota.
eggNOG; ENOG410XPF6; LUCA.
GeneTree; ENSGT00530000063396; -.
HOGENOM; HOG000007241; -.
HOVERGEN; HBG005460; -.
InParanoid; Q805F9; -.
KO; K10610; -.
PhylomeDB; Q805F9; -.
Reactome; R-GGA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-GGA-353303; Nucleotide Excision Repair.
Reactome; R-GGA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-GGA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-GGA-5696400; Dual Incision in GG-NER.
Reactome; R-GGA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-GGA-6782135; Dual incision in TC-NER.
Reactome; R-GGA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-GGA-8951664; Neddylation.
UniPathway; UPA00143; -.
PRO; PR:Q805F9; -.
Proteomes; UP000000539; Chromosome 5.
GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0031464; C:Cul4A-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0031465; C:Cul4B-RING E3 ubiquitin ligase complex; ISS:UniProtKB.
GO; GO:0031461; C:cullin-RING ubiquitin ligase complex; IBA:GO_Central.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0000784; C:nuclear chromosome, telomeric region; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0097602; F:cullin family protein binding; IEA:Ensembl.
GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
GO; GO:0030674; F:protein binding, bridging; IEA:Ensembl.
GO; GO:0032403; F:protein complex binding; IEA:Ensembl.
GO; GO:0071987; F:WD40-repeat domain binding; IEA:Ensembl.
GO; GO:0006281; P:DNA repair; TAS:Reactome.
GO; GO:0035518; P:histone H2A monoubiquitination; IEA:Ensembl.
GO; GO:0051702; P:interaction with symbiont; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0006289; P:nucleotide-excision repair; IBA:GO_Central.
GO; GO:0046726; P:positive regulation by virus of viral protein levels in host cell; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0045070; P:positive regulation of viral genome replication; IEA:Ensembl.
GO; GO:1902188; P:positive regulation of viral release from host cell; IEA:Ensembl.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IEA:Ensembl.
GO; GO:1901990; P:regulation of mitotic cell cycle phase transition; IEA:Ensembl.
GO; GO:0070914; P:UV-damage excision repair; IEA:Ensembl.
GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
Gene3D; 2.130.10.10; -; 2.
InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
InterPro; IPR031297; DDB1.
InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom.
PANTHER; PTHR10644:SF11; PTHR10644:SF11; 1.
Pfam; PF03178; CPSF_A; 1.
SUPFAM; SSF50998; SSF50998; 3.
1: Evidence at protein level;
Complete proteome; Cytoplasm; DNA damage; DNA repair; DNA-binding;
Nucleus; Reference proteome; Repeat; Ubl conjugation pathway.
CHAIN 1 1140 DNA damage-binding protein 1.
/FTId=PRO_0000281039.
REGION 13 356 WD repeat beta-propeller A.
{ECO:0000250}.
REGION 391 708 WD repeat beta-propeller B; Interaction
with CUL4A. {ECO:0000250}.
REGION 709 1043 WD repeat beta-propeller C.
{ECO:0000250}.
SEQUENCE 1140 AA; 126955 MW; 70F3AB4C64E27B95 CRC64;
MSYNYVVTAQ KPTAVNGCVT GHFTSAEDLN LLIAKNTRLE IYVVTAEGLR PVKEVGMYGK
TAVMELFRPK GESKDLLFIL TAKYNACILE YKQNGDNIDI ITRAHGNVQD RIGRPSETGI
IGIIDPECRM IGLRLYDGLF KVIPLDRENK ELKAFNIRLE ELQVIDVKFL YGCQAPTICF
VYQDPQGRHV KTYEVSLREK EFNKGPWKQE NVEAEASMVI AVPEPFGGAI IIGQESITYH
NGDKYLAIAP PIIKQSTIVC HNRVDPNGSR YLLGDMEGRL FMLLLEKEEQ MDGTVTLKDL
RVELLGETSI AECLTYLDNG VVFVGSRLGD SQLVKLNVDS NEQGSYVVAM ETFTNLGPIV
DMCVVDLERQ GQGQLVTCSG AFKEGSLRII RNGIGIHEHA SIDLPGIKGL WPLRSDSHRE
MDNMLVLSFV GQTRVLMLNG EEVEETELTG FVDDQQTFFC GNVAHQQLIQ ITSASVRLVS
QEPKALVSEW KEPNGKNISV ASCNSNQVVV AVGRALYYLE IRPQELRQIN CTEMEHEVAC
LDITPLGDTN GMSPLCAIGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH
YLLCALGDGA LFYFGLSLET GLLSDRKKVT LGTQPTVLRT FRSLSTTNVF ACSDRPTVIY
SSNHKLVFSN VNLKEVNYMC PLNSDGYPDS LALANNSTLT IGTIDEIQKL HIRTVPLYES
PRKICYQEVS QCFGVLSSRI EVQDASGGTT ALRPSASTQA LSSSVSTSKL FSSSTAPHET
SFGEEVEVHN LLIIDQHTFE VLHAHQFLQN EYALSLVSCK LGKDPNTYFI VGTAMVYPEE
AEPKQGRIVV FHYSDGKLQS LAEKEVKGAV YSMVEFNGKL LASINSTVRL YEWTAEKELR
TECNHYNNIM ALYLKTKGDF ILVGDLMRSV LLLAYKPMEG NFEEIARDFN PNWMSAVEIL
DDDNFLGAEN AFNLFVCQKD SAATTDEERQ HLQEVGLSHL GEFVNVFCHG SLVMQNLGET
STPTQGSVLF GTVNGMIGLV TSLSESWYNL LLDMQNRLNK VIKSVGKIEH SFWRSFHTER
KTEPATGFID GDLIESFLDI SRPKMQEVVA NLQIDDGSGM KREATVDDLI KIVEELTRIH


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