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NHP6B_YEAST
ID   NHP6B_YEAST             Reviewed;          99 AA.
AC   P11633; A2TBM2; D6VQ90; P89500; P89501;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   27-JUL-2011, sequence version 3.
DT   03-AUG-2022, entry version 194.
DE   RecName: Full=Non-histone chromosomal protein 6B;
GN   Name=NHP6B; Synonyms=NHPB; OrderedLocusNames=YBR089C-A; ORFNames=YBR090BC;
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].
RC   STRAIN=DBY1091 / DKY1;
RX   PubMed=2406250; DOI=10.1016/s0021-9258(19)39758-3;
RA   Kolodrubetz D., Burgum A.;
RT   "Duplicated NHP6 genes of Saccharomyces cerevisiae encode proteins
RT   homologous to bovine high mobility group protein 1.";
RL   J. Biol. Chem. 265:3234-3239(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7900426; DOI=10.1002/yea.320101014;
RA   Mannhaupt G., Stucka R., Ehnle S., Vetter I., Feldmann H.;
RT   "Analysis of a 70 kb region on the right arm of yeast chromosome II.";
RL   Yeast 10:1363-1381(1994).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=7813418; DOI=10.1002/j.1460-2075.1994.tb06923.x;
RA   Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
RA   Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
RA   Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
RA   Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
RA   Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
RA   Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J., Glansdorff N.,
RA   Goffeau A., Grivell L.A., de Haan M., Hein C., Herbert C.J.,
RA   Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M., Jauniaux J.-C.,
RA   Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L., Koetter P.,
RA   Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J., Li Z.Y.,
RA   Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T., Molemans F.,
RA   Mueller S., Nasr F., Obermaier B., Perea J., Pierard A., Piravandi E.,
RA   Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B., Ramezani Rad M.,
RA   Rieger M., Rose M., Schaaff-Gerstenschlaeger I., Scherens B.,
RA   Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M., Souciet J.-L.,
RA   Steensma H.Y., Stucka R., Urrestarazu L.A., van der Aart Q.J.M.,
RA   Van Dyck L., Vassarotti A., Vetter I., Vierendeels F., Vissers S.,
RA   Wagner G., de Wergifosse P., Wolfe K.H., Zagulski M., Zimmermann F.K.,
RA   Mewes H.-W., Kleine K.;
RT   "Complete DNA sequence of yeast chromosome II.";
RL   EMBO J. 13:5795-5809(1994).
RN   [4]
RP   GENOME REANNOTATION, AND SEQUENCE REVISION TO 30.
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=17322287; DOI=10.1101/gr.6037607;
RA   Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA   Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA   Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA   Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA   LaBaer J.;
RT   "Approaching a complete repository of sequence-verified protein-encoding
RT   clones for Saccharomyces cerevisiae.";
RL   Genome Res. 17:536-543(2007).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 1-57.
RC   STRAIN=ATCC 201390 / BY4743;
RX   PubMed=17244705; DOI=10.1073/pnas.0610354104;
RA   Juneau K., Palm C., Miranda M., Davis R.W.;
RT   "High-density yeast-tiling array reveals previously undiscovered introns
RT   and extensive regulation of meiotic splicing.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1522-1527(2007).
RN   [7]
RP   FUNCTION.
RX   PubMed=7721780; DOI=10.1074/jbc.270.15.8744;
RA   Paull T.T., Johnson R.C.;
RT   "DNA looping by Saccharomyces cerevisiae high mobility group proteins
RT   NHP6A/B. Consequences for nucleoprotein complex assembly and chromatin
RT   condensation.";
RL   J. Biol. Chem. 270:8744-8754(1995).
RN   [8]
RP   FUNCTION.
RX   PubMed=8946917; DOI=10.1101/gad.10.21.2769;
RA   Paull T.T., Carey M., Johnson R.C.;
RT   "Yeast HMG proteins NHP6A/B potentiate promoter-specific transcriptional
RT   activation in vivo and assembly of preinitiation complexes in vitro.";
RL   Genes Dev. 10:2769-2781(1996).
RN   [9]
RP   FUNCTION.
RX   PubMed=11118215; DOI=10.1093/emboj/19.24.6804;
RA   Moreira J.M.A., Holmberg S.;
RT   "Chromatin-mediated transcriptional regulation by the yeast architectural
RT   factors NHP6A and NHP6B.";
RL   EMBO J. 19:6804-6813(2000).
RN   [10]
RP   ASSOCIATION WITH THE SPT16-POB3 DIMER AND NUCLEOSOMES, AND FUNCTION OF THE
RP   FACT COMPLEX.
RX   PubMed=11432837; DOI=10.1093/emboj/20.13.3506;
RA   Formosa T., Eriksson P., Wittmeyer J., Ginn J., Yu Y., Stillman D.J.;
RT   "Spt16-Pob3 and the HMG protein Nhp6 combine to form the nucleosome-binding
RT   factor SPN.";
RL   EMBO J. 20:3506-3517(2001).
RN   [11]
RP   FUNCTION.
RX   PubMed=11239460; DOI=10.1016/s1097-2765(01)00179-4;
RA   Kruppa M., Moir R.D., Kolodrubetz D., Willis I.M.;
RT   "Nhp6, an HMG1 protein, functions in SNR6 transcription by RNA polymerase
RT   III in S. cerevisiae.";
RL   Mol. Cell 7:309-318(2001).
RN   [12]
RP   ERRATUM OF PUBMED:11239460.
RA   Kruppa M., Moir R.D., Kolodrubetz D., Willis I.M.;
RL   Mol. Cell 8:727-727(2001).
RN   [13]
RP   FUNCTION.
RX   PubMed=11287614; DOI=10.1128/mcb.21.9.3096-3104.2001;
RA   Lopez S., Livingstone-Zatchej M., Jourdain S., Thoma F., Sentenac A.,
RA   Marsolier M.-C.;
RT   "High-mobility-group proteins NHP6A and NHP6B participate in activation of
RT   the RNA polymerase III SNR6 gene.";
RL   Mol. Cell. Biol. 21:3096-3104(2001).
RN   [14]
RP   ASSOCIATION WITH THE SPT16-POB3 DIMER.
RX   PubMed=11313475; DOI=10.1128/mcb.21.10.3491-3502.2001;
RA   Brewster N.K., Johnston G.C., Singer R.A.;
RT   "A bipartite yeast SSRP1 analog comprised of Pob3 and Nhp6 proteins
RT   modulates transcription.";
RL   Mol. Cell. Biol. 21:3491-3502(2001).
RN   [15]
RP   FUNCTION.
RX   PubMed=12952948; DOI=10.1074/jbc.m307291200;
RA   Ruone S., Rhoades A.R., Formosa T.;
RT   "Multiple Nhp6 molecules are required to recruit Spt16-Pob3 to form yFACT
RT   complexes and to reorganize nucleosomes.";
RL   J. Biol. Chem. 278:45288-45295(2003).
RN   [16]
RP   FUNCTION OF THE FACT COMPLEX.
RX   PubMed=14585989; DOI=10.1128/mcb.23.22.8323-8333.2003;
RA   Mason P.B., Struhl K.;
RT   "The FACT complex travels with elongating RNA polymerase II and is
RT   important for the fidelity of transcriptional initiation in vivo.";
RL   Mol. Cell. Biol. 23:8323-8333(2003).
RN   [17]
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   [18]
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   [19]
RP   FUNCTION.
RX   PubMed=16407207; DOI=10.1074/jbc.m512810200;
RA   Kassavetis G.A., Steiner D.F.;
RT   "Nhp6 is a transcriptional initiation fidelity factor for RNA polymerase
RT   III transcription in vitro and in vivo.";
RL   J. Biol. Chem. 281:7445-7451(2006).
RN   [20]
RP   IDENTIFICATION BY MASS SPECTROMETRY [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: DNA-binding protein that induces severe bending of DNA.
CC       Required for DNA-binding by the FACT complex, a general chromatin
CC       factor that acts to reorganize nucleosomes. The FACT complex is
CC       involved in multiple processes that require DNA as a template such as
CC       mRNA elongation, DNA replication and DNA repair. Also augments the
CC       fidelity of transcription by RNA polymerase III independently of any
CC       role in the FACT complex. Required for transcriptional initiation
CC       fidelity of some but not all tRNA genes. Seems to be functionally
CC       redundant with NHP6A. {ECO:0000269|PubMed:11118215,
CC       ECO:0000269|PubMed:11239460, ECO:0000269|PubMed:11287614,
CC       ECO:0000269|PubMed:11432837, ECO:0000269|PubMed:12952948,
CC       ECO:0000269|PubMed:14585989, ECO:0000269|PubMed:16407207,
CC       ECO:0000269|PubMed:7721780, ECO:0000269|PubMed:8946917}.
CC   -!- SUBUNIT: Weakly associates with the stable SPT16-POB3 heterodimer to
CC       form the FACT (yFACT or SNP) complex, which is associated with
CC       nucleosomes. Multiple molecules of NHP6 (NHP6A and/or NHP6B) are
CC       required to recruit the SPT16-POB3 heterodimer to DNA.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC       ECO:0000269|PubMed:14562095}. Chromosome {ECO:0000269|PubMed:14562095}.
CC   -!- MISCELLANEOUS: Present with 4590 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the NHP6 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=X78993; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X15318; CAA33378.1; -; Genomic_DNA.
DR   EMBL; X78993; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; Z35957; CAA85040.1; -; Genomic_DNA.
DR   EMBL; Z35959; CAA85042.1; -; Genomic_DNA.
DR   EMBL; AY558566; AAS56892.1; -; Genomic_DNA.
DR   EMBL; EF123125; ABM97469.1; -; mRNA.
DR   EMBL; BK006936; DAA07210.2; -; Genomic_DNA.
DR   PIR; S78076; S78076.
DR   RefSeq; NP_009647.2; NM_001180058.2.
DR   AlphaFoldDB; P11633; -.
DR   SMR; P11633; -.
DR   BioGRID; 32795; 165.
DR   DIP; DIP-6748N; -.
DR   IntAct; P11633; 23.
DR   STRING; 4932.YBR089C-A; -.
DR   iPTMnet; P11633; -.
DR   PaxDb; P11633; -.
DR   PRIDE; P11633; -.
DR   EnsemblFungi; YBR089C-A_mRNA; YBR089C-A; YBR089C-A.
DR   GeneID; 852386; -.
DR   KEGG; sce:YBR089C-A; -.
DR   SGD; S000002157; NHP6B.
DR   VEuPathDB; FungiDB:YBR089C-A; -.
DR   eggNOG; KOG0381; Eukaryota.
DR   GeneTree; ENSGT00940000176448; -.
DR   HOGENOM; CLU_082854_10_3_1; -.
DR   InParanoid; P11633; -.
DR   OMA; RAPGPYM; -.
DR   BioCyc; YEAST:G3O-29229-MON; -.
DR   Reactome; R-SCE-140342; Apoptosis induced DNA fragmentation.
DR   Reactome; R-SCE-163282; Mitochondrial transcription initiation.
DR   Reactome; R-SCE-5620971; Pyroptosis.
DR   Reactome; R-SCE-5686938; Regulation of TLR by endogenous ligand.
DR   Reactome; R-SCE-6798695; Neutrophil degranulation.
DR   ChiTaRS; NHP6B; yeast.
DR   PRO; PR:P11633; -.
DR   Proteomes; UP000002311; Chromosome II.
DR   RNAct; P11633; protein.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IDA:SGD.
DR   GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR   GO; GO:0043565; F:sequence-specific DNA binding; HDA:SGD.
DR   GO; GO:0006338; P:chromatin remodeling; IGI:SGD.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0001195; P:maintenance of transcriptional fidelity during DNA-templated transcription elongation from RNA polymerase III promoter; IDA:SGD.
DR   GO; GO:0070898; P:RNA polymerase III preinitiation complex assembly; IDA:SGD.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; IGI:SGD.
DR   Gene3D; 1.10.30.10; -; 1.
DR   InterPro; IPR009071; HMG_box_dom.
DR   InterPro; IPR036910; HMG_box_dom_sf.
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   Chromosome; DNA damage; DNA repair; DNA-binding; Nucleus;
KW   Reference proteome; Transcription; Transcription regulation.
FT   CHAIN           1..99
FT                   /note="Non-histone chromosomal protein 6B"
FT                   /id="PRO_0000048566"
FT   DNA_BIND        27..95
FT                   /note="HMG box"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT   REGION          1..31
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          69..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CONFLICT        30
FT                   /note="G -> R (in Ref. 2; X78993 and 3; CAA85042)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   99 AA;  11476 MW;  0243FDC7D19B8A59 CRC64;
     MAATKEAKQP KEPKKRTTRR KKDPNAPKRG LSAYMFFANE NRDIVRSENP DVTFGQVGRI
     LGERWKALTA EEKQPYESKA QADKKRYESE KELYNATRA
 
 
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