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Q12306

- SMT3_YEAST

UniProt

Q12306 - SMT3_YEAST

Protein

Ubiquitin-like protein SMT3

Gene

SMT3

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Not known; suppressor of MIF2 mutations.

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. protein binding Source: IntAct
    3. protein tag Source: SGD

    GO - Biological processi

    1. protein sumoylation Source: SGD

    Keywords - Biological processi

    Ubl conjugation pathway

    Enzyme and pathway databases

    BioCyciYEAST:G3O-30030-MONOMER.
    ReactomeiREACT_188767. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_188903. SUMO is conjugated to E1 (UBA2:SAE1).

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Ubiquitin-like protein SMT3
    Gene namesi
    Name:SMT3
    Ordered Locus Names:YDR510W
    ORF Names:D9719.15
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome IV

    Organism-specific databases

    CYGDiYDR510w.
    SGDiS000002918. SMT3.

    Subcellular locationi

    GO - Cellular componenti

    1. condensed nuclear chromosome Source: SGD
    2. nucleus Source: SGD
    3. septin ring Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 9897Ubiquitin-like protein SMT3PRO_0000035963Add
    BLAST
    Propeptidei99 – 1013PRO_0000035964

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserine1 Publication
    Modified residuei2 – 21Phosphoserine1 Publication
    Modified residuei4 – 41Phosphoserine1 Publication
    Cross-linki98 – 98Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein

    Proteomic databases

    MaxQBiQ12306.
    PaxDbiQ12306.
    PeptideAtlasiQ12306.

    Miscellaneous databases

    PMAP-CutDBQ12306.

    Expressioni

    Gene expression databases

    GenevestigatoriQ12306.

    Interactioni

    Subunit structurei

    Activated by a E1 ligase composed of AOS1 and UBA2.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-17490,EBI-17490
    ELG1Q1205011EBI-17490,EBI-32195
    POL30P158736EBI-17490,EBI-12993
    RED1P142916EBI-17490,EBI-14909
    SGS1P351873EBI-17490,EBI-17059
    SRS2P129544EBI-17490,EBI-18110

    Protein-protein interaction databases

    BioGridi32561. 1011 interactions.
    DIPiDIP-1364N.
    IntActiQ12306. 50 interactions.
    MINTiMINT-390217.
    STRINGi4932.YDR510W.

    Structurei

    Secondary structure

    1
    101
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi22 – 298
    Beta strandi34 – 407
    Helixi46 – 5611
    Helixi60 – 623
    Beta strandi64 – 674
    Beta strandi70 – 723
    Turni78 – 825
    Beta strandi87 – 926

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1EUVX-ray1.60B13-98[»]
    1L2NNMR-A1-101[»]
    2EKEX-ray1.90C/D13-98[»]
    3PGEX-ray2.80A1-98[»]
    3QHTX-ray2.40A/B2-98[»]
    3TIXX-ray2.90A/C1-98[»]
    3UF8X-ray1.50A13-98[»]
    3UQAX-ray1.55A13-98[»]
    3UQBX-ray1.90A13-98[»]
    3V60X-ray2.60A20-98[»]
    3V61X-ray2.80A20-98[»]
    3V62X-ray2.90A/D20-98[»]
    3VAWX-ray1.55A13-98[»]
    4FN2X-ray1.95A/B13-98[»]
    4G50X-ray1.75A/B13-98[»]
    4GGQX-ray1.95A/B/C/D13-98[»]
    4GIVX-ray2.45A/B13-98[»]
    ProteinModelPortaliQ12306.
    SMRiQ12306. Positions 20-98.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12306.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 9877Ubiquitin-likePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ubiquitin family. SUMO subfamily.Curated
    Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5227.
    GeneTreeiENSGT00390000018808.
    HOGENOMiHOG000207495.
    KOiK12160.
    OMAiSTENRII.
    OrthoDBiEOG7SR514.

    Family and domain databases

    InterProiIPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view]
    PfamiPF00240. ubiquitin. 1 hit.
    [Graphical view]
    SMARTiSM00213. UBQ. 1 hit.
    [Graphical view]
    SUPFAMiSSF54236. SSF54236. 1 hit.
    PROSITEiPS50053. UBIQUITIN_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q12306-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDSEVNQEA KPEVKPEVKP ETHINLKVSD GSSEIFFKIK KTTPLRRLME    50
    AFAKRQGKEM DSLRFLYDGI RIQADQTPED LDMEDNDIIE AHREQIGGAT 100
    Y 101
    Length:101
    Mass (Da):11,597
    Last modified:November 1, 1996 - v1
    Checksum:iA2790DE7F315E1A7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27233 Genomic DNA. Translation: AAB01675.1.
    U33057 Genomic DNA. Translation: AAB64951.1.
    AY558174 Genomic DNA. Translation: AAS56500.1.
    BK006938 Genomic DNA. Translation: DAA12341.1.
    PIRiS63999.
    RefSeqiNP_010798.1. NM_001180818.1.

    Genome annotation databases

    EnsemblFungiiYDR510W; YDR510W; YDR510W.
    GeneIDi852122.
    KEGGisce:YDR510W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U27233 Genomic DNA. Translation: AAB01675.1 .
    U33057 Genomic DNA. Translation: AAB64951.1 .
    AY558174 Genomic DNA. Translation: AAS56500.1 .
    BK006938 Genomic DNA. Translation: DAA12341.1 .
    PIRi S63999.
    RefSeqi NP_010798.1. NM_001180818.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1EUV X-ray 1.60 B 13-98 [» ]
    1L2N NMR - A 1-101 [» ]
    2EKE X-ray 1.90 C/D 13-98 [» ]
    3PGE X-ray 2.80 A 1-98 [» ]
    3QHT X-ray 2.40 A/B 2-98 [» ]
    3TIX X-ray 2.90 A/C 1-98 [» ]
    3UF8 X-ray 1.50 A 13-98 [» ]
    3UQA X-ray 1.55 A 13-98 [» ]
    3UQB X-ray 1.90 A 13-98 [» ]
    3V60 X-ray 2.60 A 20-98 [» ]
    3V61 X-ray 2.80 A 20-98 [» ]
    3V62 X-ray 2.90 A/D 20-98 [» ]
    3VAW X-ray 1.55 A 13-98 [» ]
    4FN2 X-ray 1.95 A/B 13-98 [» ]
    4G50 X-ray 1.75 A/B 13-98 [» ]
    4GGQ X-ray 1.95 A/B/C/D 13-98 [» ]
    4GIV X-ray 2.45 A/B 13-98 [» ]
    ProteinModelPortali Q12306.
    SMRi Q12306. Positions 20-98.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 32561. 1011 interactions.
    DIPi DIP-1364N.
    IntActi Q12306. 50 interactions.
    MINTi MINT-390217.
    STRINGi 4932.YDR510W.

    Proteomic databases

    MaxQBi Q12306.
    PaxDbi Q12306.
    PeptideAtlasi Q12306.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YDR510W ; YDR510W ; YDR510W .
    GeneIDi 852122.
    KEGGi sce:YDR510W.

    Organism-specific databases

    CYGDi YDR510w.
    SGDi S000002918. SMT3.

    Phylogenomic databases

    eggNOGi COG5227.
    GeneTreei ENSGT00390000018808.
    HOGENOMi HOG000207495.
    KOi K12160.
    OMAi STENRII.
    OrthoDBi EOG7SR514.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-30030-MONOMER.
    Reactomei REACT_188767. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
    REACT_188903. SUMO is conjugated to E1 (UBA2:SAE1).

    Miscellaneous databases

    EvolutionaryTracei Q12306.
    NextBioi 970504.
    PMAP-CutDB Q12306.

    Gene expression databases

    Genevestigatori Q12306.

    Family and domain databases

    InterProi IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    [Graphical view ]
    Pfami PF00240. ubiquitin. 1 hit.
    [Graphical view ]
    SMARTi SM00213. UBQ. 1 hit.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 1 hit.
    PROSITEi PS50053. UBIQUITIN_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Meluh P.B., Koshland D.E.
      Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: YPH1/YNN214.
    2. "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."
      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.
      Nature 387:75-78(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    3. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. "The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer."
      Johnson E.S., Schwienhorst I., Dohmen R.J., Blobel G.
      EMBO J. 16:5509-5519(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH AOS1 AND UBA2.
    6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    7. "Large-scale phosphorylation analysis of alpha-factor-arrested Saccharomyces cerevisiae."
      Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J., Elias J.E., Gygi S.P.
      J. Proteome Res. 6:1190-1197(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Strain: ADR376.
    8. "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry."
      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.
      Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-4, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    9. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
      Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
      Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Solution structure of a yeast ubiquitin-like protein Smt3: the role of structurally less defined sequences in protein-protein recognitions."
      Sheng W., Liao X.
      Protein Sci. 11:1482-1491(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR.
    11. "Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast."
      Mossessova E., Lima C.D.
      Mol. Cell 5:865-876(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 13-98 IN COMPLEX WITH ULP1.

    Entry informationi

    Entry nameiSMT3_YEAST
    AccessioniPrimary (citable) accession number: Q12306
    Secondary accession number(s): D6VTD1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 2940 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome IV
      Yeast (Saccharomyces cerevisiae) chromosome IV: entries and gene names

    External Data

    Dasty 3