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RAD10_YEAST
ID   RAD10_YEAST             Reviewed;         210 AA.
AC   P06838; D6W0J0;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 181.
DE   RecName: Full=DNA repair protein RAD10;
GN   Name=RAD10; OrderedLocusNames=YML095C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3896774; DOI=10.1002/j.1460-2075.1985.tb03819.x;
RA   Weiss W.A., Friedberg E.C.;
RT   "Molecular cloning and characterization of the yeast RAD10 gene and
RT   expression of RAD10 protein in E. coli.";
RL   EMBO J. 4:1575-1582(1985).
RN   [2]
RP   ERRATUM OF PUBMED:3896774, AND SEQUENCE REVISION.
RA   Weiss W.A., Friedberg E.C.;
RL   EMBO J. 4:3907-3907(1985).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3912171; DOI=10.1002/j.1460-2075.1985.tb04115.x;
RA   Reynolds P., Prakash L., Dumais D., Perozzi G., Prakash S.;
RT   "Nucleotide sequence of the RAD10 gene of Saccharomyces cerevisiae.";
RL   EMBO J. 4:3549-3552(1985).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169872;
RA   Bowman S., Churcher C.M., Badcock K., Brown D., Chillingworth T.,
RA   Connor R., Dedman K., Devlin K., Gentles S., Hamlin N., Hunt S., Jagels K.,
RA   Lye G., Moule S., Odell C., Pearson D., Rajandream M.A., Rice P.,
RA   Skelton J., Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIII.";
RL   Nature 387:90-93(1997).
RN   [5]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [6]
RP   FUNCTION, AND INTERACTION WITH RAD1.
RX   PubMed=8479526; DOI=10.1038/362860a0;
RA   Tomkinson A.E., Bardwell A.J., Bardwell L., Tappe N.J., Friedberg E.C.;
RT   "Yeast DNA repair and recombination proteins Rad1 and Rad10 constitute a
RT   single-stranded-DNA endonuclease.";
RL   Nature 362:860-862(1993).
RN   [7]
RP   IDENTIFICATION IN THE NEF1 COMPLEX.
RX   PubMed=8621533; DOI=10.1074/jbc.271.15.8903;
RA   Guzder S.N., Sung P., Prakash L., Prakash S.;
RT   "Nucleotide excision repair in yeast is mediated by sequential assembly of
RT   repair factors and not by a pre-assembled repairosome.";
RL   J. Biol. Chem. 271:8903-8910(1996).
RN   [8]
RP   INTERACTION WITH SAW1.
RX   PubMed=17989249; DOI=10.1101/gr.6667007;
RA   Suter B., Fetchko M.J., Imhof R., Graham C.I., Stoffel-Studer I.,
RA   Zbinden C., Raghavan M., Lopez L., Beneti L., Hort J., Fillingham J.,
RA   Greenblatt J.F., Giaever G., Nislow C., Stagljar I.;
RT   "Examining protein protein interactions using endogenously tagged yeast
RT   arrays: the cross-and-capture system.";
RL   Genome Res. 17:1774-1782(2007).
CC   -!- FUNCTION: Involved in nucleotide excision repair of DNA damaged with UV
CC       light, bulky adducts, or cross-linking agents. Along with RAD1 forms an
CC       endonuclease that specifically degrades single-stranded DNA.
CC       {ECO:0000269|PubMed:8479526}.
CC   -!- SUBUNIT: Component of the nucleotide excision repair factor 1 (NEF1)
CC       complex consisting of RAD1, RAD10 and RAD14. Interacts with SAW1.
CC       {ECO:0000269|PubMed:17989249, ECO:0000269|PubMed:8479526,
CC       ECO:0000269|PubMed:8621533}.
CC   -!- INTERACTION:
CC       P06838; P06777: RAD1; NbExp=11; IntAct=EBI-14637, EBI-14752;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- SIMILARITY: Belongs to the ERCC1/RAD10/SWI10 family. {ECO:0000305}.
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DR   EMBL; X02591; CAA26433.1; -; Genomic_DNA.
DR   EMBL; X05225; CAA28856.1; -; Genomic_DNA.
DR   EMBL; Z46660; CAA86642.1; -; Genomic_DNA.
DR   EMBL; BK006946; DAA09804.1; -; Genomic_DNA.
DR   PIR; A24576; A24576.
DR   RefSeq; NP_013614.1; NM_001182454.1.
DR   AlphaFoldDB; P06838; -.
DR   SMR; P06838; -.
DR   BioGRID; 35048; 157.
DR   ComplexPortal; CPX-1362; SLX4-RAD1-RAD10 endonuclease complex.
DR   ComplexPortal; CPX-1363; SAW1-RAD1-RAD10 endonuclease complex.
DR   ComplexPortal; CPX-1708; Nucleotide-excision repair factor 1 complex.
DR   DIP; DIP-1545N; -.
DR   IntAct; P06838; 24.
DR   MINT; P06838; -.
DR   STRING; 4932.YML095C; -.
DR   MaxQB; P06838; -.
DR   PaxDb; P06838; -.
DR   PRIDE; P06838; -.
DR   EnsemblFungi; YML095C_mRNA; YML095C; YML095C.
DR   GeneID; 854878; -.
DR   KEGG; sce:YML095C; -.
DR   SGD; S000004560; RAD10.
DR   VEuPathDB; FungiDB:YML095C; -.
DR   eggNOG; KOG2841; Eukaryota.
DR   GeneTree; ENSGT00390000011275; -.
DR   HOGENOM; CLU_1267070_0_0_1; -.
DR   InParanoid; P06838; -.
DR   OMA; LTYHKLY; -.
DR   BioCyc; YEAST:G3O-32680-MON; -.
DR   PRO; PR:P06838; -.
DR   Proteomes; UP000002311; Chromosome XIII.
DR   RNAct; P06838; protein.
DR   GO; GO:1905348; C:endonuclease complex; IPI:ComplexPortal.
DR   GO; GO:0070522; C:ERCC4-ERCC1 complex; IBA:GO_Central.
DR   GO; GO:0000110; C:nucleotide-excision repair factor 1 complex; IPI:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IDA:SGD.
DR   GO; GO:0006277; P:DNA amplification; IMP:SGD.
DR   GO; GO:0000736; P:double-strand break repair via single-strand annealing, removal of nonhomologous ends; IMP:SGD.
DR   GO; GO:0000710; P:meiotic mismatch repair; IMP:SGD.
DR   GO; GO:0006312; P:mitotic recombination; IMP:SGD.
DR   GO; GO:0006289; P:nucleotide-excision repair; IDA:SGD.
DR   GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IDA:ComplexPortal.
DR   GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; IBA:GO_Central.
DR   GO; GO:0000735; P:removal of nonhomologous ends; IMP:SGD.
DR   GO; GO:0070914; P:UV-damage excision repair; IBA:GO_Central.
DR   InterPro; IPR004579; ERCC1/RAD10/SWI10.
DR   InterPro; IPR011335; Restrct_endonuc-II-like.
DR   PANTHER; PTHR12749; PTHR12749; 1.
DR   Pfam; PF03834; Rad10; 1.
DR   SUPFAM; SSF52980; SSF52980; 1.
DR   TIGRFAMs; TIGR00597; rad10; 1.
PE   1: Evidence at protein level;
KW   DNA damage; DNA repair; DNA-binding; Endonuclease; Hydrolase; Nuclease;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..210
FT                   /note="DNA repair protein RAD10"
FT                   /id="PRO_0000097149"
FT   DNA_BIND        133..153
FT                   /evidence="ECO:0000255"
FT   REGION          20..89
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           17..23
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        26..68
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..84
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   210 AA;  24311 MW;  26891AD9CA1E3E2B CRC64;
     MNNTDPTSFE SILAGVAKLR KEKSGADTTG SQSLEIDASK LQQQEPQTSR RINSNQVINA
     FNQQKPEEWT DSKATDDYNR KRPFRSTRPG KTVLVNTTQK ENPLLNHLKS TNWRYVSSTG
     INMIYYDYLV RGRSVLFLTL TYHKLYVDYI SRRMQPLSRN ENNILIFIVD DNNSEDTLND
     ITKLCMFNGF TLLLAFNFEQ AAKYIEYLNL
 
 
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