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NHP10_YEAST
ID   NHP10_YEAST             Reviewed;         203 AA.
AC   Q03435; D6VRY6;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 184.
DE   RecName: Full=Non-histone protein 10;
DE   AltName: Full=High mobility group protein 2;
GN   Name=NHP10; Synonyms=HMO2; OrderedLocusNames=YDL002C; ORFNames=YD8119.05C;
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 [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169867;
RA   Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA   Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA   Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA   Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA   Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA   Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA   Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA   Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA   Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA   Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA   Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA   Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA   Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA   Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA   Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA   Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA   Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA   Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA   Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA   Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA   Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA   Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA   Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA   Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA   Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA   Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA   Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA   Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA   Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA   Mewes H.-W., Zollner A., Zaccaria P.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL   Nature 387:75-78(1997).
RN   [2]
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   [3]
RP   IDENTIFICATION.
RX   PubMed=8969238; DOI=10.1074/jbc.271.52.33678;
RA   Lu J., Kobayashi R., Brill S.J.;
RT   "Characterization of a high mobility group 1/2 homolog in yeast.";
RL   J. Biol. Chem. 271:33678-33685(1996).
RN   [4]
RP   IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY.
RX   PubMed=12887900; DOI=10.1016/s1097-2765(03)00264-8;
RA   Shen X., Ranallo R., Choi E., Wu C.;
RT   "Involvement of actin-related proteins in ATP-dependent chromatin
RT   remodeling.";
RL   Mol. Cell 12:147-155(2003).
RN   [5]
RP   SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [6]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [7]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC   -!- FUNCTION: Probably involved in transcription regulation via its
CC       interaction with the INO80 complex, a chromatin remodeling complex.
CC   -!- SUBUNIT: Component of the chromatin-remodeling INO80 complex, at least
CC       composed of ARP4, ARP5, ARP8, RVB1, RVB2, TAF14, NHP10, IES1, IES3,
CC       IES4, IES6, ACT1, IES2, IES5 and INO80. {ECO:0000269|PubMed:12887900}.
CC   -!- INTERACTION:
CC       Q03435; P43579: IES1; NbExp=4; IntAct=EBI-12010, EBI-22775;
CC       Q03435; P40060: IES5; NbExp=4; IntAct=EBI-12010, EBI-22617;
CC       Q03435; P53115: INO80; NbExp=10; IntAct=EBI-12010, EBI-24019;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC       ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 1750 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
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DR   EMBL; Z48008; CAA88059.1; -; Genomic_DNA.
DR   EMBL; BK006938; DAA11846.1; -; Genomic_DNA.
DR   PIR; S50980; S50980.
DR   RefSeq; NP_010282.3; NM_001180061.3.
DR   AlphaFoldDB; Q03435; -.
DR   SMR; Q03435; -.
DR   BioGRID; 32052; 688.
DR   ComplexPortal; CPX-863; INO80 chromatin remodeling complex.
DR   DIP; DIP-1387N; -.
DR   IntAct; Q03435; 28.
DR   MINT; Q03435; -.
DR   STRING; 4932.YDL002C; -.
DR   iPTMnet; Q03435; -.
DR   MaxQB; Q03435; -.
DR   PaxDb; Q03435; -.
DR   PRIDE; Q03435; -.
DR   EnsemblFungi; YDL002C_mRNA; YDL002C; YDL002C.
DR   GeneID; 851562; -.
DR   KEGG; sce:YDL002C; -.
DR   SGD; S000002160; NHP10.
DR   VEuPathDB; FungiDB:YDL002C; -.
DR   eggNOG; KOG0381; Eukaryota.
DR   HOGENOM; CLU_066251_0_1_1; -.
DR   InParanoid; Q03435; -.
DR   OMA; RWREAPM; -.
DR   BioCyc; YEAST:G3O-29433-MON; -.
DR   Reactome; R-SCE-140342; Apoptosis induced DNA fragmentation.
DR   Reactome; R-SCE-163282; Mitochondrial transcription initiation.
DR   PRO; PR:Q03435; -.
DR   Proteomes; UP000002311; Chromosome IV.
DR   RNAct; Q03435; protein.
DR   GO; GO:0031011; C:Ino80 complex; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR   GO; GO:0008301; F:DNA binding, bending; IBA:GO_Central.
DR   GO; GO:0045027; F:DNA end binding; IDA:SGD.
DR   GO; GO:0000404; F:heteroduplex DNA loop binding; IDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR   GO; GO:0006281; P:DNA repair; IC:ComplexPortal.
DR   GO; GO:0006302; P:double-strand break repair; IMP:SGD.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR   GO; GO:0000722; P:telomere maintenance via recombination; IGI:SGD.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
DR   InterPro; IPR030483; Nhp10.
DR   PANTHER; PTHR48112:SF13; PTHR48112:SF13; 2.
DR   Pfam; PF00505; HMG_box; 1.
DR   SMART; SM00398; HMG; 1.
DR   SUPFAM; SSF47095; SSF47095; 1.
DR   PROSITE; PS50118; HMG_BOX_2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..203
FT                   /note="Non-histone protein 10"
FT                   /id="PRO_0000048567"
FT   DNA_BIND        94..158
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          78..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          161..203
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        161..189
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
SQ   SEQUENCE   203 AA;  23857 MW;  EE6F488F78D32415 CRC64;
     MSVEEKKRRL EELKDQNVVL GLAIQRSRLS VKRLKLEYGV LLERLESRIE LDPELNCEDP
     LPTLASFKQE LLTKPFRKSK TKRHKVKERD PNMPKRPTNA YLLYCEMNKE RIRQNGSLDV
     TRDLAEGWKN LNEQDRKPYY KLYSEDRERY QMEMEIYNKK ISNIDADDDK EENEQKIKNN
     EEGSSTKVAD SKGGEDGSLV SSN
 
 
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