SMT3_YEAST
ID SMT3_YEAST Reviewed; 101 AA.
AC Q12306; D6VTD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Ubiquitin-like protein SMT3;
DE Flags: Precursor;
GN Name=SMT3; OrderedLocusNames=YDR510W; ORFNames=D9719.15;
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=YPH1/YNN214;
RA Meluh P.B., Koshland D.E.;
RL Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP INTERACTION WITH AOS1 AND UBA2.
RX PubMed=9312010; DOI=10.1093/emboj/16.18.5509;
RA Johnson E.S., Schwienhorst I., Dohmen R.J., Blobel G.;
RT "The ubiquitin-like protein Smt3p is activated for conjugation to other
RT proteins by an Aos1p/Uba2p heterodimer.";
RL EMBO J. 16:5509-5519(1997).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2 AND SER-4, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE
RP ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=17287358; DOI=10.1073/pnas.0607084104;
RA Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
RA Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
RT "Analysis of phosphorylation sites on proteins from Saccharomyces
RT cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [10]
RP STRUCTURE BY NMR.
RX PubMed=12021447; DOI=10.1110/ps.0201602;
RA Sheng W., Liao X.;
RT "Solution structure of a yeast ubiquitin-like protein Smt3: the role of
RT structurally less defined sequences in protein-protein recognitions.";
RL Protein Sci. 11:1482-1491(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 13-98 IN COMPLEX WITH ULP1.
RX PubMed=10882122; DOI=10.1016/s1097-2765(00)80326-3;
RA Mossessova E., Lima C.D.;
RT "Ulp1-SUMO crystal structure and genetic analysis reveal conserved
RT interactions and a regulatory element essential for cell growth in yeast.";
RL Mol. Cell 5:865-876(2000).
CC -!- FUNCTION: Not known; suppressor of MIF2 mutations.
CC -!- SUBUNIT: Activated by a E1 ligase composed of AOS1 and UBA2.
CC {ECO:0000269|PubMed:10882122}.
CC -!- INTERACTION:
CC Q12306; P32797: CDC13; NbExp=3; IntAct=EBI-17490, EBI-4187;
CC Q12306; P25694: CDC48; NbExp=3; IntAct=EBI-17490, EBI-4308;
CC Q12306; Q12050: ELG1; NbExp=11; IntAct=EBI-17490, EBI-32195;
CC Q12306; P29469: MCM2; NbExp=2; IntAct=EBI-17490, EBI-10533;
CC Q12306; P24279: MCM3; NbExp=2; IntAct=EBI-17490, EBI-10541;
CC Q12306; P30665: MCM4; NbExp=2; IntAct=EBI-17490, EBI-4326;
CC Q12306; P29496: MCM5; NbExp=3; IntAct=EBI-17490, EBI-10549;
CC Q12306; P53091: MCM6; NbExp=2; IntAct=EBI-17490, EBI-10556;
CC Q12306; P38132: MCM7; NbExp=2; IntAct=EBI-17490, EBI-4300;
CC Q12306; P43124: NSE4; NbExp=2; IntAct=EBI-17490, EBI-14410;
CC Q12306; P07271: PIF1; NbExp=2; IntAct=EBI-17490, EBI-13404;
CC Q12306; P15873: POL30; NbExp=6; IntAct=EBI-17490, EBI-12993;
CC Q12306; P06778: RAD52; NbExp=2; IntAct=EBI-17490, EBI-14719;
CC Q12306; P14291: RED1; NbExp=9; IntAct=EBI-17490, EBI-14909;
CC Q12306; P35187: SGS1; NbExp=3; IntAct=EBI-17490, EBI-17059;
CC Q12306; P32908: SMC1; NbExp=2; IntAct=EBI-17490, EBI-17402;
CC Q12306; Q08204: SMC5; NbExp=5; IntAct=EBI-17490, EBI-34125;
CC Q12306; Q12306: SMT3; NbExp=3; IntAct=EBI-17490, EBI-17490;
CC Q12306; P12954: SRS2; NbExp=4; IntAct=EBI-17490, EBI-18110;
CC Q12306; P52488: UBA2; NbExp=2; IntAct=EBI-17490, EBI-19710;
CC Q12306; P50623: UBC9; NbExp=3; IntAct=EBI-17490, EBI-19760;
CC Q12306; P53044: UFD1; NbExp=3; IntAct=EBI-17490, EBI-19997;
CC Q12306; P32807: YKU70; NbExp=2; IntAct=EBI-17490, EBI-8214;
CC Q12306; Q04437: YKU80; NbExp=2; IntAct=EBI-17490, EBI-8224;
CC -!- MISCELLANEOUS: Present with 2940 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
CC {ECO:0000305}.
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DR EMBL; U27233; AAB01675.1; -; Genomic_DNA.
DR EMBL; U33057; AAB64951.1; -; Genomic_DNA.
DR EMBL; AY558174; AAS56500.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12341.1; -; Genomic_DNA.
DR PIR; S63999; S63999.
DR RefSeq; NP_010798.1; NM_001180818.1.
DR PDB; 1EUV; X-ray; 1.60 A; B=13-98.
DR PDB; 1L2N; NMR; -; A=1-101.
DR PDB; 2EKE; X-ray; 1.90 A; C/D=13-98.
DR PDB; 3PGE; X-ray; 2.80 A; A=1-98.
DR PDB; 3QHT; X-ray; 2.40 A; A/B=2-98.
DR PDB; 3TIX; X-ray; 2.90 A; A/C=1-98.
DR PDB; 3UF8; X-ray; 1.50 A; A=13-98.
DR PDB; 3UQA; X-ray; 1.55 A; A=13-98.
DR PDB; 3UQB; X-ray; 1.90 A; A=13-98.
DR PDB; 3V60; X-ray; 2.60 A; A=20-98.
DR PDB; 3V61; X-ray; 2.80 A; A=20-98.
DR PDB; 3V62; X-ray; 2.90 A; A/D=20-98.
DR PDB; 3VAW; X-ray; 1.55 A; A=13-98.
DR PDB; 4FN2; X-ray; 1.95 A; A/B=13-98.
DR PDB; 4G50; X-ray; 1.75 A; A/B=13-98.
DR PDB; 4GGQ; X-ray; 1.95 A; A/B/C/D=13-98.
DR PDB; 4GIV; X-ray; 2.45 A; A/B=13-98.
DR PDB; 5D6J; X-ray; 2.25 A; B=21-94.
DR PDB; 5JNE; X-ray; 2.85 A; A/E=20-98, C/G=19-98.
DR PDB; 5KLX; X-ray; 2.45 A; A/B/C/D=13-98.
DR PDB; 5V8T; X-ray; 2.10 A; A/B=13-97.
DR PDB; 5YC2; X-ray; 2.70 A; A/C=20-93.
DR PDB; 5YCA; X-ray; 1.57 A; A=20-93.
DR PDB; 6CFP; X-ray; 2.45 A; A=13-98.
DR PDB; 6O4A; X-ray; 2.10 A; A/B/C/D=13-98.
DR PDB; 6P81; X-ray; 1.75 A; A=13-98.
DR PDB; 6Q2S; EM; 3.80 A; A/B=1-98.
DR PDB; 6RPQ; X-ray; 2.65 A; A=2-98.
DR PDB; 6UKM; X-ray; 1.74 A; A=2-98.
DR PDB; 6UKU; X-ray; 1.68 A; A=2-98.
DR PDB; 6UKV; X-ray; 1.83 A; A/B=2-98.
DR PDB; 6UKW; X-ray; 1.97 A; A/B=2-98.
DR PDB; 6UKX; X-ray; 1.93 A; A/B=2-98.
DR PDB; 6UKY; X-ray; 1.95 A; A=2-98.
DR PDB; 6UKZ; X-ray; 1.52 A; A/B=2-98.
DR PDB; 6UL0; X-ray; 1.76 A; A=2-98.
DR PDB; 6VEL; X-ray; 2.65 A; C=1-98.
DR PDB; 6VW2; EM; 3.40 A; A/B/C/D/E/F/G/H/I/J=1-97.
DR PDB; 7LTO; EM; 3.20 A; B=1-98.
DR PDB; 7O2W; EM; -; A=2-96.
DR PDB; 7P47; X-ray; 3.31 A; D/E=1-98.
DR PDB; 7SDE; EM; 3.20 A; B=1-98.
DR PDBsum; 1EUV; -.
DR PDBsum; 1L2N; -.
DR PDBsum; 2EKE; -.
DR PDBsum; 3PGE; -.
DR PDBsum; 3QHT; -.
DR PDBsum; 3TIX; -.
DR PDBsum; 3UF8; -.
DR PDBsum; 3UQA; -.
DR PDBsum; 3UQB; -.
DR PDBsum; 3V60; -.
DR PDBsum; 3V61; -.
DR PDBsum; 3V62; -.
DR PDBsum; 3VAW; -.
DR PDBsum; 4FN2; -.
DR PDBsum; 4G50; -.
DR PDBsum; 4GGQ; -.
DR PDBsum; 4GIV; -.
DR PDBsum; 5D6J; -.
DR PDBsum; 5JNE; -.
DR PDBsum; 5KLX; -.
DR PDBsum; 5V8T; -.
DR PDBsum; 5YC2; -.
DR PDBsum; 5YCA; -.
DR PDBsum; 6CFP; -.
DR PDBsum; 6O4A; -.
DR PDBsum; 6P81; -.
DR PDBsum; 6Q2S; -.
DR PDBsum; 6RPQ; -.
DR PDBsum; 6UKM; -.
DR PDBsum; 6UKU; -.
DR PDBsum; 6UKV; -.
DR PDBsum; 6UKW; -.
DR PDBsum; 6UKX; -.
DR PDBsum; 6UKY; -.
DR PDBsum; 6UKZ; -.
DR PDBsum; 6UL0; -.
DR PDBsum; 6VEL; -.
DR PDBsum; 6VW2; -.
DR PDBsum; 7LTO; -.
DR PDBsum; 7O2W; -.
DR PDBsum; 7P47; -.
DR PDBsum; 7SDE; -.
DR AlphaFoldDB; Q12306; -.
DR SMR; Q12306; -.
DR BioGRID; 32561; 716.
DR DIP; DIP-1364N; -.
DR IntAct; Q12306; 80.
DR MINT; Q12306; -.
DR STRING; 4932.YDR510W; -.
DR iPTMnet; Q12306; -.
DR MaxQB; Q12306; -.
DR PaxDb; Q12306; -.
DR PRIDE; Q12306; -.
DR EnsemblFungi; YDR510W_mRNA; YDR510W; YDR510W.
DR GeneID; 852122; -.
DR KEGG; sce:YDR510W; -.
DR SGD; S000002918; SMT3.
DR VEuPathDB; FungiDB:YDR510W; -.
DR eggNOG; KOG1769; Eukaryota.
DR HOGENOM; CLU_148322_0_1_1; -.
DR InParanoid; Q12306; -.
DR OMA; AYCDRVG; -.
DR BioCyc; YEAST:G3O-30030-MON; -.
DR Reactome; R-SCE-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
DR Reactome; R-SCE-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
DR Reactome; R-SCE-3065679; SUMO is proteolytically processed.
DR Reactome; R-SCE-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-SCE-3108232; SUMO E3 ligases SUMOylate target proteins.
DR Reactome; R-SCE-3232118; SUMOylation of transcription factors.
DR Reactome; R-SCE-3232142; SUMOylation of ubiquitinylation proteins.
DR Reactome; R-SCE-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-SCE-4085377; SUMOylation of SUMOylation proteins.
DR Reactome; R-SCE-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-SCE-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-SCE-4615885; SUMOylation of DNA replication proteins.
DR Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-SCE-9615933; Postmitotic nuclear pore complex (NPC) reformation.
DR EvolutionaryTrace; Q12306; -.
DR PRO; PR:Q12306; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; Q12306; protein.
DR GO; GO:0000794; C:condensed nuclear chromosome; IDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005940; C:septin ring; IDA:SGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0031386; F:protein tag; IDA:SGD.
DR GO; GO:0044389; F:ubiquitin-like protein ligase binding; IBA:GO_Central.
DR GO; GO:0016925; P:protein sumoylation; IDA:SGD.
DR DisProt; DP02264; -.
DR InterPro; IPR022617; Rad60/SUMO-like_dom.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF11976; Rad60-SLD; 1.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation pathway.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CHAIN 2..98
FT /note="Ubiquitin-like protein SMT3"
FT /id="PRO_0000035963"
FT PROPEP 99..101
FT /id="PRO_0000035964"
FT DOMAIN 22..98
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358,
FT ECO:0007744|PubMed:17330950"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17287358"
FT CROSSLNK 98
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT STRAND 22..29
FT /evidence="ECO:0007829|PDB:3UF8"
FT STRAND 34..40
FT /evidence="ECO:0007829|PDB:3UF8"
FT HELIX 46..56
FT /evidence="ECO:0007829|PDB:3UF8"
FT HELIX 60..62
FT /evidence="ECO:0007829|PDB:3UF8"
FT STRAND 64..67
FT /evidence="ECO:0007829|PDB:3UF8"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:3V60"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:3UF8"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:3UF8"
SQ SEQUENCE 101 AA; 11597 MW; A2790DE7F315E1A7 CRC64;
MSDSEVNQEA KPEVKPEVKP ETHINLKVSD GSSEIFFKIK KTTPLRRLME AFAKRQGKEM
DSLRFLYDGI RIQADQTPED LDMEDNDIIE AHREQIGGAT Y
