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DDB1_CAEEL
ID   DDB1_CAEEL              Reviewed;        1134 AA.
AC   Q21554;
DT   23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 2.
DT   03-AUG-2022, entry version 148.
DE   RecName: Full=DNA damage-binding protein 1;
DE   AltName: Full=Damage-specific DNA-binding protein 1;
GN   Name=ddb-1; ORFNames=M18.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   SEQUENCE REVISION.
RG   WormBase consortium;
RL   Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   FUNCTION, INTERACTION WITH CDT-1 AND CUL-4, TISSUE SPECIFICITY, AND
RP   DEVELOPMENTAL STAGE.
RX   PubMed=17145765; DOI=10.1128/mcb.00736-06;
RA   Kim Y., Kipreos E.T.;
RT   "The Caenorhabditis elegans replication licensing factor CDT-1 is targeted
RT   for degradation by the CUL-4/DDB-1 complex.";
RL   Mol. Cell. Biol. 27:1394-1406(2007).
CC   -!- FUNCTION: Plays a role in DNA repair. May be a component of an E3
CC       ubiquitin-protein ligase which promotes histone ubiquitination in
CC       response to UV irradiation. Histone ubiquitination may be important for
CC       subsequent DNA repair (By similarity). Promotes the degradation of the
CC       replication licensing factor cdt-1 during S-phase, thereby preventing
CC       rereplication of DNA during a single round of cell division.
CC       {ECO:0000250, ECO:0000269|PubMed:17145765}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: Interacts with cdt-1 and cul-4. {ECO:0000269|PubMed:17145765}.
CC   -!- INTERACTION:
CC       Q21554; Q86S68: cdt-1; NbExp=3; IntAct=EBI-325461, EBI-3902879;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Expressed at high levels in the spermatheca of
CC       adult hermaphrodites. {ECO:0000269|PubMed:17145765}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in proliferating larval blast cells
CC       including seam cells in the lateral hypodermis, P cells in the ventral
CC       hypodermis, and intestinal cells. Within the P cell lineage expression
CC       levels correlate with the proliferative state, being low in newly
CC       hatched larvae and then increasing in L1 as P cells begin to
CC       proliferate. Not expressed in the adult cells of the P lineage which
CC       are postmitotic. Also expressed in some non-proliferating cells such as
CC       the lateral hyp7 hypodermal cells, rectal gland and epithelial cells,
CC       and a subset of neuronal cells in the head and tail regions.
CC       {ECO:0000269|PubMed:17145765}.
CC   -!- SIMILARITY: Belongs to the DDB1 family. {ECO:0000305}.
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DR   EMBL; Z68507; CAA92824.2; -; Genomic_DNA.
DR   PIR; A88855; A88855.
DR   PIR; T23798; T23798.
DR   RefSeq; NP_502299.1; NM_069898.7.
DR   AlphaFoldDB; Q21554; -.
DR   SMR; Q21554; -.
DR   BioGRID; 43249; 16.
DR   DIP; DIP-25884N; -.
DR   IntAct; Q21554; 5.
DR   STRING; 6239.M18.5; -.
DR   EPD; Q21554; -.
DR   PaxDb; Q21554; -.
DR   PeptideAtlas; Q21554; -.
DR   EnsemblMetazoa; M18.5.1; M18.5.1; WBGene00010890.
DR   GeneID; 178156; -.
DR   KEGG; cel:CELE_M18.5; -.
DR   UCSC; M18.5; c. elegans.
DR   CTD; 178156; -.
DR   WormBase; M18.5; CE23880; WBGene00010890; ddb-1.
DR   eggNOG; KOG1897; Eukaryota.
DR   GeneTree; ENSGT00950000183151; -.
DR   HOGENOM; CLU_002893_0_1_1; -.
DR   InParanoid; Q21554; -.
DR   OMA; CTEMEHE; -.
DR   OrthoDB; 146622at2759; -.
DR   PhylomeDB; Q21554; -.
DR   Reactome; R-CEL-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-CEL-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-CEL-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-CEL-5696400; Dual Incision in GG-NER.
DR   Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-CEL-6782135; Dual incision in TC-NER.
DR   Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-CEL-8951664; Neddylation.
DR   UniPathway; UPA00143; -.
DR   PRO; PR:Q21554; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00010890; Expressed in embryo and 4 other tissues.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0035861; C:site of double-strand break; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR   GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IGI:WormBase.
DR   GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.130.10.10; -; 3.
DR   InterPro; IPR004871; Cleavage/polyA-sp_fac_asu_C.
DR   InterPro; IPR018846; Cleavage/polyA-sp_fac_asu_N.
DR   InterPro; IPR031297; DDB1.
DR   InterPro; IPR011047; Quinoprotein_ADH-like_supfam.
DR   InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR   PANTHER; PTHR10644:SF3; PTHR10644:SF3; 1.
DR   Pfam; PF03178; CPSF_A; 1.
DR   Pfam; PF10433; MMS1_N; 1.
DR   SUPFAM; SSF50998; SSF50998; 1.
PE   1: Evidence at protein level;
KW   Cell cycle; Cytoplasm; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..1134
FT                   /note="DNA damage-binding protein 1"
FT                   /id="PRO_0000351087"
SQ   SEQUENCE   1134 AA;  125718 MW;  56366EE0FB4D9139 CRC64;
     MPISYCVSAK KASVVVESVV GNFTGHENVN LIVARGNRID VQLVSPEGLK NVCEIPIYGQ
     VLTIALVKCK RDKRHSLIVV TEKWHMAILA YRDGKVVTRA AGCIADPTGR ATDNLFSLTI
     HRNGLIAIRA FEGSVKMIQW ESGTDLRHFN VRFDYPNVSD FKFVDTGEDD VYRVAFIYDD
     DHGKHLQFSD LNMHDKEFRT YSRQASIAAD SSVLIPVPHA IGGVIVLGSN SVLYKPNDNL
     GEVVPYTCSL LENTTFTCHG IVDASGERFL LSDTDGRLLM LLLNVTESQS GYTVKEMRID
     YLGETSIADS INYIDNGVVF VGSRLGDSQL IRLMTEPNGG SYSVILETYS NIGPIRDMVM
     VESDGQPQLV TCTGADKDGS LRVIRNGIGI DELASVDLAG VVGIFPIRLD SNADNYVIVS
     LSDETHVLQI TGEELEDVKL LEINTDLPTI FASTLFGPND SGIILQATEK QIRLMSSSGL
     SKFWEPTNGE IISKVSVNAA NGQIVLAARD TVYLLTCIVD EMGALDIQLT AEKKFENEIA
     CLDLSNEGDD PNNKATFLVL AFWSTFAMEV IQLPDLITVC HTDLPTKIIP RSIIATCIEE
     VHYLLVAFGD GALVYYVFDI KTGTHGEPKK SNVGTRPPSL HRVRNKNRQH LFVCSDRPVI
     IFSASKKLVF SNVNVKLVDT VCSLSSSAYR DCLVISDGNS MVFGTVDDIQ KIHVRSIPMG
     ESVLRIAYQK STSTYGVCSN RTESKAERVF ASKNALVTSQ SRPKVASTRA DMDESPPNTT
     SSFMVLDQNT FQVLHSHEFG PWETALSCIS GQFTNDSSTY YVVGTGLIYP DETETKIGRI
     VVFEVDDVER SKLRRVHELV VRGSPLAIRI LNGKLVAAIN SSIRLFEWTT DKELRLECSS
     FNHVIALDLK VMNEEVAVAD VMRSVSLLSY RMLEGNFEEV AKDWNSQWMV TCEFITAESI
     LGGEAHLNLF TVEVDKTRPI TDDGRYVLEP TGYWYLGELP KVMTRSTLVI QPEDSIIQYS
     QPIMFGTNQG TIGMIVQIDD KWKKFLIAIE KAIADSVKNC MHIEHSSYRT FVFQKRAEPP
     SGFVDGDLVE SILDMDRSVA MDILSKVSDK GWDPSLPRDP VEILKVIEDL ARMH
 
 
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