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DDB2_CHICK
ID   DDB2_CHICK              Reviewed;         507 AA.
AC   Q5ZJL7;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=DNA damage-binding protein 2;
DE   AltName: Full=Damage-specific DNA-binding protein 2;
GN   Name=DDB2; ORFNames=RCJMB04_17d21;
OS   Gallus gallus (Chicken).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC   Phasianinae; Gallus.
OX   NCBI_TaxID=9031;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=CB; TISSUE=Bursa of Fabricius;
RX   PubMed=15642098; DOI=10.1186/gb-2004-6-1-r6;
RA   Caldwell R.B., Kierzek A.M., Arakawa H., Bezzubov Y., Zaim J., Fiedler P.,
RA   Kutter S., Blagodatski A., Kostovska D., Koter M., Plachy J., Carninci P.,
RA   Hayashizaki Y., Buerstedde J.-M.;
RT   "Full-length cDNAs from chicken bursal lymphocytes to facilitate gene
RT   function analysis.";
RL   Genome Biol. 6:R6.1-R6.9(2005).
CC   -!- FUNCTION: Protein, which is both involved in DNA repair and protein
CC       ubiquitination, as part of the UV-DDB complex and DCX (DDB1-CUL4-X-box)
CC       complexes, respectively. Core component of the UV-DDB complex (UV-
CC       damaged DNA-binding protein complex), a complex that recognizes UV-
CC       induced DNA damage and recruit proteins of the nucleotide excision
CC       repair pathway (the NER pathway) to initiate DNA repair. The UV-DDB
CC       complex preferentially binds to cyclobutane pyrimidine dimers (CPD), 6-
CC       4 photoproducts (6-4 PP), apurinic sites and short mismatches. Also
CC       functions as the substrate recognition module for the DCX (DDB2-CUL4-X-
CC       box) E3 ubiquitin-protein ligase complex DDB2-CUL4-ROC1 (also known as
CC       CUL4-DDB-ROC1 and CUL4-DDB-RBX1). The DDB2-CUL4-ROC1 complex may
CC       ubiquitinate histone H2A, histone H3 and histone H4 at sites of UV-
CC       induced DNA damage. The ubiquitination of histones may facilitate their
CC       removal from the nucleosome and promote subsequent DNA repair.
CC       {ECO:0000250|UniProtKB:Q92466}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Component of the UV-DDB complex which includes DDB1 and DDB2
CC       (By similarity). Component of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-
CC       protein ligase complex DDB1-CUL4-ROC1 (also known as CUL4-DDB-ROC1 and
CC       CUL4-DDB-RBX1), which includes CUL4A or CUL4B, DDB1, DDB2 and RBX1.
CC       DDB2 may function as the substrate recognition module within this
CC       complex. A large number of other DCX complexes may also exist in which
CC       an alternate substrate targeting subunit replaces DDB2. These targeting
CC       subunits are generally known as DCAF (DDB1- and CUL4-associated factor)
CC       or CDW (CUL4-DDB1-associated WD40-repeat) proteins (By similarity).
CC       {ECO:0000250|UniProtKB:Q92466}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92466}.
CC       Chromosome {ECO:0000250|UniProtKB:Q92466}. Note=Accumulates at sites of
CC       DNA damage following UV irradiation. {ECO:0000250|UniProtKB:Q92466}.
CC   -!- DOMAIN: The DWD box is required for interaction with DDB1.
CC       {ECO:0000250|UniProtKB:Q92466}.
CC   -!- DOMAIN: Interblade loops of the WD repeat region mediate most of the
CC       interaction with DNA. A hairpin between blades 5 and 6 inserts into DNA
CC       minor groove and mediates recognition of lesions and separation of the
CC       damaged and undamaged strands (By similarity).
CC       {ECO:0000250|UniProtKB:Q92466}.
CC   -!- SIMILARITY: Belongs to the WD repeat DDB2/WDR76 family. {ECO:0000305}.
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DR   EMBL; AJ720417; CAG32076.1; -; mRNA.
DR   RefSeq; NP_001034390.1; NM_001039301.1.
DR   RefSeq; XP_015142508.1; XM_015287022.1.
DR   RefSeq; XP_015142509.1; XM_015287023.1.
DR   RefSeq; XP_015142510.1; XM_015287024.1.
DR   RefSeq; XP_015142511.1; XM_015287025.1.
DR   AlphaFoldDB; Q5ZJL7; -.
DR   SMR; Q5ZJL7; -.
DR   STRING; 9031.ENSGALP00000013362; -.
DR   PaxDb; Q5ZJL7; -.
DR   Ensembl; ENSGALT00000013377; ENSGALP00000013362; ENSGALG00000008218.
DR   GeneID; 423185; -.
DR   KEGG; gga:423185; -.
DR   CTD; 1643; -.
DR   VEuPathDB; HostDB:geneid_423185; -.
DR   eggNOG; KOG4328; Eukaryota.
DR   GeneTree; ENSGT00510000047881; -.
DR   HOGENOM; CLU_036401_0_0_1; -.
DR   InParanoid; Q5ZJL7; -.
DR   OMA; FIKGKGP; -.
DR   OrthoDB; 559605at2759; -.
DR   PhylomeDB; Q5ZJL7; -.
DR   Reactome; R-GGA-5689880; Ub-specific processing proteases.
DR   Reactome; R-GGA-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-GGA-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-GGA-5696400; Dual Incision in GG-NER.
DR   Reactome; R-GGA-8951664; Neddylation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q5ZJL7; -.
DR   Proteomes; UP000000539; Chromosome 5.
DR   Bgee; ENSGALG00000008218; Expressed in spermatid and 13 other tissues.
DR   ExpressionAtlas; Q5ZJL7; baseline and differential.
DR   GO; GO:0080008; C:Cul4-RING E3 ubiquitin ligase complex; IEA:InterPro.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0090734; C:site of DNA damage; ISS:UniProtKB.
DR   GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0006289; P:nucleotide-excision repair; ISS:UniProtKB.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009411; P:response to UV; IBA:GO_Central.
DR   Gene3D; 2.130.10.10; -; 1.
DR   InterPro; IPR033312; DDB2.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   InterPro; IPR001680; WD40_repeat.
DR   InterPro; IPR019775; WD40_repeat_CS.
DR   InterPro; IPR036322; WD40_repeat_dom_sf.
DR   PANTHER; PTHR15169; PTHR15169; 1.
DR   Pfam; PF00400; WD40; 1.
DR   SMART; SM00320; WD40; 4.
DR   SUPFAM; SSF50978; SSF50978; 1.
DR   PROSITE; PS00678; WD_REPEATS_1; 1.
DR   PROSITE; PS50082; WD_REPEATS_2; 1.
DR   PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE   2: Evidence at transcript level;
KW   Chromosome; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Reference proteome; Repeat; Ubl conjugation pathway; WD repeat.
FT   CHAIN           1..507
FT                   /note="DNA damage-binding protein 2"
FT                   /id="PRO_0000351089"
FT   REPEAT          129..164
FT                   /note="WD 1"
FT   REPEAT          172..207
FT                   /note="WD 2"
FT   REPEAT          223..258
FT                   /note="WD 3"
FT   REPEAT          264..307
FT                   /note="WD 4"
FT   REPEAT          310..350
FT                   /note="WD 5"
FT   REPEAT          364..407
FT                   /note="WD 6"
FT   REPEAT          417..441
FT                   /note="WD 7"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..92
FT                   /note="Required for interaction with DDB1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92466"
FT   REGION          100..111
FT                   /note="Required for interaction with DDB1"
FT                   /evidence="ECO:0000250|UniProtKB:Q92466"
FT   REGION          355..357
FT                   /note="Photolesion recognition"
FT                   /evidence="ECO:0000250|UniProtKB:Q92466"
FT   REGION          459..487
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           276..294
FT                   /note="DWD box"
FT   COMPBIAS        460..481
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   507 AA;  57312 MW;  F0137FA9B0BD8EB9 CRC64;
     MAPVNQPKDK KHEKAHEHRS EEAKSAGKRK LDYEGLENEP LAKKLFLRKT SKAQEKIGWN
     RGGTVMRNTR ALFHQPKWQC SIVHYVYQNM LGGSIRAQLR QCLQLPFLRS LTSYRLFRTA
     SPFDRRVTCL EWHPTHPSTV AVGSKGGDII LWDYEVLTKT CFIKGKGPGD SLGDIKFSPY
     EAVKLYVASG DGTLSLQDLE GRAVQVISRA PDCGHENHNV CCWYCSVDVS ASCRAVVTGD
     NLGNVVLLST SGEEIWKLKL HKKKVTHVEF NSRCEWLLAT ASVDQTVKIW DLRNIKDKAN
     FLHVLPHDKP VNAAYFSPTD GAKLLSTDQR NEIRVYSCSD WTKPQHLIPH PHRQFQHLTP
     IKATWHPRYD LIVVGRYPDP KFPGYTVNEL RTVDIFDGNT GEMVCQLYDP NASGIISLNK
     FNPMGDTLAS GMGFNILIWS REEMVMKKQE HLLKAMTEQG IGSRSLSRRG GQRQANPGTS
     KLKAKLLSWE VEEMGTKTKD SKSQGRK
 
 
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