HMO1_YEAST
ID HMO1_YEAST Reviewed; 246 AA.
AC Q03973; D6VSF6;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=High mobility group protein 1;
DE AltName: Full=High spontaneous mutagenesis protein 2;
GN Name=HMO1; Synonyms=HSM2; OrderedLocusNames=YDR174W; ORFNames=YD9395.07;
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 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 [4]
RP PROTEIN SEQUENCE OF 14-25; 51-84 AND 163-175, SUBCELLULAR LOCATION, AND
RP DNA-BINDING.
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 [5]
RP INTERACTION WITH FPR1.
RX PubMed=10049913; DOI=10.1093/genetics/151.3.935;
RA Dolinski K.J., Heitman J.;
RT "Hmo1p, a high mobility group 1/2 homolog, genetically and physically
RT interacts with the yeast FKBP12 prolyl isomerase.";
RL Genetics 151:935-944(1999).
RN [6]
RP FUNCTION.
RX PubMed=12509247; DOI=10.1016/s1568-7864(02)00005-8;
RA Alekseev S.Y., Kovaltsova S.V., Fedorova I.V., Gracheva L.M.,
RA Evstukhina T.A., Peshekhonov V.T., Korolev V.G.;
RT "HSM2 (HMO1) gene participates in mutagenesis control in yeast
RT Saccharomyces cerevisiae.";
RL DNA Repair 1:287-297(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12374750; DOI=10.1093/emboj/cdf539;
RA Gadal O., Labarre S., Boschiero C., Thuriaux P.;
RT "Hmo1, an HMG-box protein, belongs to the yeast ribosomal DNA transcription
RT system.";
RL EMBO J. 21:5498-5507(2002).
RN [8]
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 [9]
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).
CC -!- FUNCTION: DNA-binding protein that is probably part of the rDNA
CC transcription apparatus. Acts synergetically with the RPA49 subunit of
CC RNA polymerase I during rDNA transcription. May participate in
CC mutagenesis control. {ECO:0000269|PubMed:12374750,
CC ECO:0000269|PubMed:12509247}.
CC -!- SUBUNIT: Interacts with FPR1. Interacts with an unidentified DNA
CC helicase. Associates with rDNA. {ECO:0000269|PubMed:10049913}.
CC -!- INTERACTION:
CC Q03973; Q12050: ELG1; NbExp=2; IntAct=EBI-33047, EBI-32195;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12374750,
CC ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8969238}.
CC Note=Colocalizes with FOB1.
CC -!- MISCELLANEOUS: Present with 19000 molecules/cell in log phase SD
CC medium. {ECO:0000269|PubMed:14562106}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z46727; CAA86679.1; -; Genomic_DNA.
DR EMBL; AY557680; AAS56006.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12016.1; -; Genomic_DNA.
DR PIR; S49770; S49770.
DR RefSeq; NP_010459.1; NM_001180481.1.
DR AlphaFoldDB; Q03973; -.
DR SMR; Q03973; -.
DR BioGRID; 32227; 341.
DR DIP; DIP-1687N; -.
DR IntAct; Q03973; 50.
DR MINT; Q03973; -.
DR STRING; 4932.YDR174W; -.
DR iPTMnet; Q03973; -.
DR MaxQB; Q03973; -.
DR PaxDb; Q03973; -.
DR PRIDE; Q03973; -.
DR EnsemblFungi; YDR174W_mRNA; YDR174W; YDR174W.
DR GeneID; 851754; -.
DR KEGG; sce:YDR174W; -.
DR SGD; S000002581; HMO1.
DR VEuPathDB; FungiDB:YDR174W; -.
DR eggNOG; KOG0381; Eukaryota.
DR HOGENOM; CLU_076155_0_0_1; -.
DR InParanoid; Q03973; -.
DR OMA; DKWKQAY; -.
DR BioCyc; YEAST:G3O-29763-MON; -.
DR Reactome; R-SCE-140342; Apoptosis induced DNA fragmentation.
DR Reactome; R-SCE-163282; Mitochondrial transcription initiation.
DR PRO; PR:Q03973; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q03973; protein.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005730; C:nucleolus; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0033553; C:rDNA heterochromatin; IDA:SGD.
DR GO; GO:0032040; C:small-subunit processome; IDA:SGD.
DR GO; GO:0008301; F:DNA binding, bending; IDA:SGD.
DR GO; GO:0003690; F:double-stranded DNA binding; IDA:SGD.
DR GO; GO:0000400; F:four-way junction DNA binding; IDA:SGD.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:SGD.
DR GO; GO:0044804; P:autophagy of nucleus; IMP:SGD.
DR GO; GO:0006338; P:chromatin remodeling; IDA:SGD.
DR GO; GO:0030261; P:chromosome condensation; IMP:SGD.
DR GO; GO:0051276; P:chromosome organization; IDA:SGD.
DR GO; GO:0006265; P:DNA topological change; IMP:SGD.
DR GO; GO:2001034; P:positive regulation of double-strand break repair via nonhomologous end joining; IMP:CACAO.
DR GO; GO:0070550; P:rDNA chromatin condensation; IMP:SGD.
DR GO; GO:0060962; P:regulation of ribosomal protein gene transcription by RNA polymerase II; IMP:SGD.
DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; IMP:SGD.
DR GO; GO:0001174; P:transcriptional start site selection at RNA polymerase II promoter; IMP: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 Direct protein sequencing; DNA-binding; Nucleus; Reference proteome;
KW Transcription; Transcription regulation.
FT CHAIN 1..246
FT /note="High mobility group protein 1"
FT /id="PRO_0000048564"
FT DNA_BIND 106..179
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 179..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..229
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 246 AA; 27544 MW; 3D6DCD56A28B7D77 CRC64;
MTTDPSVKLK SAKDSLVSSL FELSKAANQT ASSIVDFYNA IGDDEEEKIE AFTTLTESLQ
TLTSGVNHLH GISSELVNPI DDDKDAIIAA PVKAVRRKIE RDPNAPKKPL TVFFAYSAYV
RQELREDRQK AGLPPLSSTE ITQEISKKWK ELSDNEKEKW KQAYNVELEN YQREKSKYLE
AKKNGTLPPA SLENGPTHAP VPIPFSLQHA AEPPVEKRPH DDDGSSEKKK KKKKKDKKKD
KSNSSI
