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UniProtKB/Swiss-Prot entry Q12306


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name SMT3_YEAST
Primary accession number Q12306
Secondary accession numbers None
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 77)
Name and origin of the protein
Protein name Ubiquitin-like protein SMT3 [Precursor]
Synonyms None
Gene name
Name: SMT3
OrderedLocusNames: YDR510W
ORFNames: D9719.15
From
Saccharomyces cerevisiae (Baker's yeast) [TaxID: 4932] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=YPH1/YNN214;
Meluh P.B., Koshland D.E.;
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867 [NCBI, ExPASy, EBI, Israel, Japan]
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K., Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
DOI=10.1101/gr.6037607; PubMed=17322287 [NCBI, ExPASy, EBI, Israel, Japan]
Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F., Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J., Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J., Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D., LaBaer J.;
"Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae.";
Genome Res. 17:536-543(2007).
[4]
INTERACTION WITH AOS1 AND UBA2.
DOI=10.1093/emboj/16.18.5509; PubMed=9312010 [NCBI, ExPASy, EBI, Israel, Japan]
Johnson E.S., Schwienhorst I., Dohmen R.J., Blobel G.;
"The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer.";
EMBO J. 16:5509-5519(1997).
[5]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
DOI=10.1038/nature02046; PubMed=14562106 [NCBI, ExPASy, EBI, Israel, Japan]
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
DOI=10.1021/pr060559j; PubMed=17330950 [NCBI, ExPASy, EBI, Israel, Japan]
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-4, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0607084104; PubMed=17287358 [NCBI, ExPASy, EBI, Israel, Japan]
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L., Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32 AND SER-33, AND MASS SPECTROMETRY.
DOI=10.1074/mcp.M700468-MCP200; PubMed=18407956 [NCBI, ExPASy, EBI, Israel, Japan]
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[9]
STRUCTURE BY NMR.
DOI=10.1110/ps.0201602; PubMed=12021447 [NCBI, ExPASy, EBI, Israel, Japan]
Sheng W., Liao X.;
"Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions.";
Protein Sci. 11:1482-1491(2002).
[10]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 13-98 IN COMPLEX WITH ULP1.
DOI=10.1016/S1097-2765(00)80326-3; PubMed=10882122 [NCBI, ExPASy, EBI, Israel, Japan]
Mossessova E., Lima C.D.;
"Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast.";
Mol. Cell 5:865-876(2000).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U27233; AAB01675.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U33057; AAB64951.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AY558174; AAS56500.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S63999; S63999.
RefSeq NP_010798.1; -.
3D structure databases
PDB
1EUV; X-ray; 1.60 A; B=13-98.[ExPASy / RCSB / EBI]
1L2N; NMR; -; A=1-101.[ExPASy / RCSB / EBI]
2EKE; X-ray; 1.90 A; C/D=13-98.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EUV; -.
1L2N; -.
2EKE; -.
ModBase Q12306.
Protein-protein interaction databases
DIP DIP:1364N; -.
IntAct Q12306; 30.
Organism-specific databases
CYGD YDR510w; -.
SGD S000002918; SMT3.
Yeast-GFP YDR510W.
Gene expression databases
GermOnline YDR510W; Saccharomyces cerevisiae.
Ontologies
GO
GO:0005634; Cellular component: nucleus (inferred from direct assay from SGD).
GO:0005940; Cellular component: septin ring (inferred from direct assay from SGD).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031386; Molecular function: protein tag (inferred from direct assay from SGD).
GO:0016925; Biological process: protein sumoylation (inferred from direct assay from SGD).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000626; Ubiquitin.
Graphical view of domain structure.
Pfam PF00240; ubiquitin; 1.
Pfam graphical view of domain structure.
SMART SM00213; UBQ; 1.
SMART graphical view of domain structure.
PROSITE PS50053; UBIQUITIN_2; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PeptideAtlas Q12306; -.
Genome annotation databases
Ensembl YDR510W; Saccharomyces cerevisiae. [Contig view]
GeneID 852122; -.
GenomeReviews Z71256_GR; YDR510W.
KEGG sce:YDR510W; -.
NMPDR fig|4932.3.peg.1571; -.
Phylogenomic databases
HOGENOM Q12306; -.
Other
LinkHub Q12306; -.
NextBio 970504; -.
ProtoNet Q12306.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Phosphoprotein; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom  To Length Description FTId
CHAIN   1    98  98     Ubiquitin-like protein SMT3. PRO_0000035963
PROPEP   99   101  3      PRO_0000035964
DOMAIN   22    98  77     Ubiquitin-like. 
MOD_RES   2     2        Phosphoserine. 
MOD_RES   4     4        Phosphoserine. 
MOD_RES   32    32        Phosphoserine. 
MOD_RES   33    33        Phosphoserine. 
CROSSLNK   98    98        Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins). 
STRAND   22    32  11      
STRAND   34    40  7      
HELIX   46    55  10      
HELIX   60    62  3      
STRAND   63    67  5      
TURN   78    82  5      
STRAND   87    93  7      
Sequence information
Length: 101 AA [This is the length of the unprocessed precursor] Molecular weight: 11597 Da [This is the MW of the unprocessed precursor] CRC64: A2790DE7F315E1A7 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDSEVNQEA KPEVKPEVKP ETHINLKVSD GSSEIFFKIK KTTPLRRLME AFAKRQGKEM 

        70         80         90        100 
DSLRFLYDGI RIQADQTPED LDMEDNDIIE AHREQIGGAT Y 

Q12306 in FASTA format

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View entry in raw text format (no links)
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