HSM3_YEAST
ID HSM3_YEAST Reviewed; 480 AA.
AC P38348; D6VQR8;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=DNA mismatch repair protein HSM3;
DE AltName: Full=Enhanced spontaneous mutability protein 3;
GN Name=HSM3; OrderedLocusNames=YBR272C; ORFNames=YBR1740;
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=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 [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 FUNCTION.
RX PubMed=9539417; DOI=10.1093/genetics/148.3.963;
RA Fedorova I.V., Gracheva L.M., Kovaltzova S.V., Evstuhina T.A.,
RA Alekseev S.Y., Korolev V.G.;
RT "The yeast HSM3 gene acts in one of the mismatch repair pathways.";
RL Genetics 148:963-973(1998).
RN [5]
RP FUNCTION.
RX PubMed=10681182; DOI=10.1093/genetics/154.1.491;
RA Merker J.D., Datta A., Kolodner R.D., Petes T.D.;
RT "The yeast HSM3 gene is not involved in DNA mismatch repair in rapidly
RT dividing cells.";
RL Genetics 154:491-493(2000).
RN [6]
RP FUNCTION.
RX PubMed=10681183; DOI=10.1093/genetics/154.1.495;
RA Fedorova I.V., Kovaltzova S.V., Korolev V.G.;
RT "The yeast HSM3 gene is involved in DNA mismatch repair in slowly dividing
RT cells.";
RL Genetics 154:495-496(2000).
RN [7]
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 [8]
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 [9]
RP FUNCTION.
RX PubMed=15450405; DOI=10.1016/j.mrfmmm.2004.03.003;
RA Fedorova I.V., Kovaltzova S.V., Gracheva L.M., Evstuhina T.A.,
RA Korolev V.G.;
RT "Requirement of HSM3 gene for spontaneous mutagenesis in Saccharomyces
RT cerevisiae.";
RL Mutat. Res. 554:67-75(2004).
RN [10]
RP FUNCTION AS PROTEASOME CHAPERONE.
RX PubMed=19446322; DOI=10.1016/j.cell.2009.04.061;
RA Funakoshi M., Tomko R.J. Jr., Kobayashi H., Hochstrasser M.;
RT "Multiple assembly chaperones govern biogenesis of the proteasome
RT regulatory particle base.";
RL Cell 137:887-899(2009).
RN [11]
RP FUNCTION AS PROTEASOME CHAPERONE, AND INTERACTION WITH RPT1; RPT2; RPT3;
RP RPT5; RPT6; RPN1 AND RPN2.
RX PubMed=19217412; DOI=10.1016/j.molcel.2009.01.010;
RA Le Tallec B., Barrault M.B., Guerois R., Carre T., Peyroche A.;
RT "Hsm3/S5b participates in the assembly pathway of the 19S regulatory
RT particle of the proteasome.";
RL Mol. Cell 33:389-399(2009).
RN [12]
RP FUNCTION AS PROTEASOME CHAPERONE, AND INTERACTION WITH RPT1.
RX PubMed=19412159; DOI=10.1038/nature08063;
RA Roelofs J., Park S., Haas W., Tian G., McAllister F.E., Huo Y., Lee B.H.,
RA Zhang F., Shi Y., Gygi S.P., Finley D.;
RT "Chaperone-mediated pathway of proteasome regulatory particle assembly.";
RL Nature 459:861-865(2009).
RN [13]
RP SUBUNIT.
RX PubMed=19412160; DOI=10.1038/nature08065;
RA Park S., Roelofs J., Kim W., Robert J., Schmidt M., Gygi S.P., Finley D.;
RT "Hexameric assembly of the proteasomal ATPases is templated through their C
RT termini.";
RL Nature 459:866-870(2009).
CC -!- FUNCTION: Involved in DNA mismatch repair in slow-growing cells. Acts
CC as a chaperone during the assembly of the 26S proteasome, specifically
CC of the base subcomplex of the 19S regulatory complex (RC).
CC {ECO:0000269|PubMed:10681182, ECO:0000269|PubMed:10681183,
CC ECO:0000269|PubMed:15450405, ECO:0000269|PubMed:19217412,
CC ECO:0000269|PubMed:19412159, ECO:0000269|PubMed:19446322,
CC ECO:0000269|PubMed:9539417}.
CC -!- SUBUNIT: Interacts with RPT1, RPT2, RPT3, RPT5, RPT6, RPN1 and RPN2.
CC Part of transient complex (BP1) containing HSM3, RPT1, RPT2 and RPT5
CC formed during the assembly of the 26S proteasome.
CC {ECO:0000269|PubMed:19217412, ECO:0000269|PubMed:19412159,
CC ECO:0000269|PubMed:19412160}.
CC -!- INTERACTION:
CC P38348; P50086: NAS6; NbExp=7; IntAct=EBI-21152, EBI-14028;
CC P38348; P53196: RPN14; NbExp=8; IntAct=EBI-21152, EBI-23691;
CC P38348; Q08723: RPN8; NbExp=4; IntAct=EBI-21152, EBI-36176;
CC P38348; P33299: RPT1; NbExp=9; IntAct=EBI-21152, EBI-13910;
CC P38348; P33297: RPT5; NbExp=6; IntAct=EBI-21152, EBI-13920;
CC P38348; O94742: SEM1; NbExp=2; IntAct=EBI-21152, EBI-31337;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}.
CC -!- MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the proteasome subunit S5B/HSM3 family.
CC {ECO:0000305}.
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DR EMBL; Z36141; CAA85235.1; -; Genomic_DNA.
DR EMBL; AY692825; AAT92844.1; -; Genomic_DNA.
DR EMBL; BK006936; DAA07388.1; -; Genomic_DNA.
DR PIR; S46153; S46153.
DR RefSeq; NP_009831.3; NM_001178620.3.
DR PDB; 3VLD; X-ray; 2.05 A; A/B=1-480.
DR PDB; 3VLE; X-ray; 2.41 A; A/B=1-480.
DR PDB; 3VLF; X-ray; 3.80 A; A/C=1-480.
DR PDB; 4A3T; X-ray; 2.10 A; A/B=2-480.
DR PDB; 4A3V; X-ray; 3.80 A; A/C=2-480.
DR PDB; 4FP7; X-ray; 2.20 A; A/B=1-480.
DR PDB; 4JPO; X-ray; 5.00 A; A/B=1-480.
DR PDBsum; 3VLD; -.
DR PDBsum; 3VLE; -.
DR PDBsum; 3VLF; -.
DR PDBsum; 4A3T; -.
DR PDBsum; 4A3V; -.
DR PDBsum; 4FP7; -.
DR PDBsum; 4JPO; -.
DR AlphaFoldDB; P38348; -.
DR SMR; P38348; -.
DR BioGRID; 32967; 111.
DR DIP; DIP-2748N; -.
DR IntAct; P38348; 42.
DR MINT; P38348; -.
DR STRING; 4932.YBR272C; -.
DR iPTMnet; P38348; -.
DR MaxQB; P38348; -.
DR PaxDb; P38348; -.
DR PRIDE; P38348; -.
DR EnsemblFungi; YBR272C_mRNA; YBR272C; YBR272C.
DR GeneID; 852575; -.
DR KEGG; sce:YBR272C; -.
DR SGD; S000000476; HSM3.
DR VEuPathDB; FungiDB:YBR272C; -.
DR eggNOG; ENOG502QWEK; Eukaryota.
DR HOGENOM; CLU_044760_0_0_1; -.
DR InParanoid; P38348; -.
DR OMA; YMEQMVL; -.
DR BioCyc; YEAST:G3O-29193-MON; -.
DR PRO; PR:P38348; -.
DR Proteomes; UP000002311; Chromosome II.
DR RNAct; P38348; protein.
DR GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR GO; GO:0005829; C:cytosol; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0006298; P:mismatch repair; IMP:SGD.
DR GO; GO:0070682; P:proteasome regulatory particle assembly; IMP:SGD.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR040752; HSM3_C.
DR InterPro; IPR041335; HSM3_N.
DR Pfam; PF18794; HSM3_C; 1.
DR Pfam; PF18795; HSM3_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; DNA damage; DNA repair;
KW Reference proteome.
FT CHAIN 1..480
FT /note="DNA mismatch repair protein HSM3"
FT /id="PRO_0000202532"
FT HELIX 10..21
FT /evidence="ECO:0007829|PDB:3VLD"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:4A3T"
FT HELIX 29..42
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 73..86
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 89..95
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 98..105
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 110..121
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 126..129
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 134..142
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 150..163
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 167..174
FT /evidence="ECO:0007829|PDB:3VLD"
FT TURN 175..177
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 178..187
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 190..204
FT /evidence="ECO:0007829|PDB:3VLD"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 214..217
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 221..227
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 231..250
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 254..256
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 257..260
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 261..263
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 264..272
FT /evidence="ECO:0007829|PDB:3VLD"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 285..295
FT /evidence="ECO:0007829|PDB:3VLD"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:4FP7"
FT HELIX 304..312
FT /evidence="ECO:0007829|PDB:3VLD"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:3VLE"
FT HELIX 320..322
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 323..329
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 332..338
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 340..346
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 351..353
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 354..360
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 364..368
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 376..380
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 384..394
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 398..407
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 409..416
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 421..423
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 427..441
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 449..451
FT /evidence="ECO:0007829|PDB:3VLD"
FT HELIX 452..464
FT /evidence="ECO:0007829|PDB:3VLD"
SQ SEQUENCE 480 AA; 55543 MW; 8B739BCC9A46A63E CRC64;
MSEKETNYVE NLLTQLENEL NEDNLPEDIN TLLRKCSLNL VTVVSLPDMD VKPLLATIKR
FLTSNVSYDS LNYDYLLDVV DKLVPMADFD DVLEVYSAED LVKALRSEID PLKVAACRVI
ENSQPKGLFA TSNIIDILLD ILFDEKVEND KLITAIEKAL ERLSTDELIR RRLFDNNLPY
LVSVKGRMET VSFVRLIDFL TIEFQFISGP EFKDIIFCFT KEEILKSVED ILVFIELVNY
YTKFLLEIRN QDKYWALRHV KKILPVFAQL FEDTENYPDV RAFSTNCLLQ LFAEVSRIEE
DEYSLFKTMD KDSLKIGSEA KLITEWLELI NPQYLVKYHK DVVENYFHVS GYSIGMLRNL
SADEECFNAI RNKFSAEIVL RLPYLEQMQV VETLTRYEYT SKFLLNEMPK VMGSLIGDGS
AGAIIDLETV HYRNSALRNL LDKGEEKLSV WYEPLLREYS KAVNGKNYST GSETKIADCR
