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Protein

Ubiquitin-like protein SMT3

Gene

SMT3

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

Functioni

Not known; suppressor of MIF2 mutations.

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • protein tag Source: SGD

GO - Biological processi

  • protein sumoylation Source: SGD
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-30030-MONOMER.
ReactomeiREACT_325765. SUMO is proteolytically processed.
REACT_326849. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_338960. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_357266. SUMOylation of DNA damage response and repair proteins.

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 Componenti: Chromosome IV

Organism-specific databases

CYGDiYDR510w.
EuPathDBiFungiDB:YDR510W.
SGDiS000002918. SMT3.

Subcellular locationi

GO - Cellular componenti

  • condensed nuclear chromosome Source: SGD
  • nucleus Source: SGD
  • septin ring Source: SGD
Complete GO annotation...

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.

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. 1019 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 – 298Combined sources
Beta strandi34 – 407Combined sources
Helixi46 – 5611Combined sources
Helixi60 – 623Combined sources
Beta strandi64 – 674Combined sources
Beta strandi70 – 723Combined sources
Turni78 – 825Combined sources
Beta strandi87 – 926Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiQ12306.
KOiK12160.
OMAiQRINDDQ.
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

        10         20         30         40         50
MSDSEVNQEA KPEVKPEVKP ETHINLKVSD GSSEIFFKIK KTTPLRRLME
60 70 80 90 100
AFAKRQGKEM DSLRFLYDGI RIQADQTPED LDMEDNDIIE AHREQIGGAT

Y
Length:101
Mass (Da):11,597
Last modified:November 1, 1996 - v1
Checksum:iA2790DE7F315E1A7
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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...

Protein-protein interaction databases

BioGridi32561. 1019 interactions.
DIPiDIP-1364N.
IntActiQ12306. 50 interactions.
MINTiMINT-390217.
STRINGi4932.YDR510W.

Proteomic databases

MaxQBiQ12306.
PaxDbiQ12306.
PeptideAtlasiQ12306.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CYGDiYDR510w.
EuPathDBiFungiDB:YDR510W.
SGDiS000002918. SMT3.

Phylogenomic databases

eggNOGiCOG5227.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
InParanoidiQ12306.
KOiK12160.
OMAiQRINDDQ.
OrthoDBiEOG7SR514.

Enzyme and pathway databases

BioCyciYEAST:G3O-30030-MONOMER.
ReactomeiREACT_325765. SUMO is proteolytically processed.
REACT_326849. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
REACT_338960. SUMO is conjugated to E1 (UBA2:SAE1).
REACT_357266. SUMOylation of DNA damage response and repair proteins.

Miscellaneous databases

EvolutionaryTraceiQ12306.
NextBioi970504.
PMAP-CutDBQ12306.
PROiQ12306.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: June 24, 2015
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.