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Protein

SUMO-conjugating enzyme UBC9

Gene

UBC9

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

E2 ubiquitin-like--protein ligase mediating SUMO/Smt3 attachment to septins and PCNA. Seems to be involved in degradation of S- (CLB5) and M-phase cyclins (CLB2).2 Publications

Catalytic activityi

ATP + SUMO + protein lysine = AMP + diphosphate + protein N-SUMOyllysine.

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ligase activity Source: UniProtKB-KW
  • SUMO transferase activity Source: SGD

GO - Biological processi

  • cell division Source: UniProtKB-KW
  • mitotic spindle elongation Source: SGD
  • protein sumoylation Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciYEAST:G3O-29479-MONOMER.
BRENDAi2.3.2.B5. 984.
ReactomeiR-SCE-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-SCE-3108214. SUMOylation of DNA damage response and repair proteins.
R-SCE-4570464. SUMOylation of RNA binding proteins.
R-SCE-4615885. SUMOylation of DNA replication proteins.
R-SCE-5696395. Formation of Incision Complex in GG-NER.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
SUMO-conjugating enzyme UBC9 (EC:6.3.2.-)
Alternative name(s):
Ubiquitin carrier protein 9
Ubiquitin-conjugating enzyme E2-18 kDa
Ubiquitin-protein ligase
Gene namesi
Name:UBC9
Ordered Locus Names:YDL064W
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDL064W.
SGDiS000002222. UBC9.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 157156SUMO-conjugating enzyme UBC9PRO_0000082556Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP50623.
PeptideAtlasiP50623.

Interactioni

Subunit structurei

Interacts with SIZ1.2 Publications

Protein-protein interaction databases

BioGridi31995. 159 interactions.
DIPiDIP-1531N.
IntActiP50623. 6 interactions.
MINTiMINT-400021.

Structurei

Secondary structure

1
157
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Beta strandi25 – 306Combined sources
Beta strandi36 – 4611Combined sources
Turni52 – 554Combined sources
Beta strandi56 – 638Combined sources
Turni66 – 705Combined sources
Beta strandi74 – 763Combined sources
Beta strandi90 – 923Combined sources
Helixi95 – 973Combined sources
Turni99 – 1024Combined sources
Helixi109 – 12012Combined sources
Helixi131 – 1399Combined sources
Helixi141 – 15414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKEX-ray1.90A/B1-157[»]
2GJDX-ray1.75A/B/C/D1-157[»]
3ONGX-ray2.30B/D1-157[»]
ProteinModelPortaliP50623.
SMRiP50623. Positions 2-157.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP50623.

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
InParanoidiP50623.
KOiK10577.
OMAiDLKRWEC.
OrthoDBiEOG7SBP18.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P50623-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLCLQRLQ EERKKWRKDH PFGFYAKPVK KADGSMDLQK WEAGIPGKEG
60 70 80 90 100
TNWAGGVYPI TVEYPNEYPS KPPKVKFPAG FYHPNVYPSG TICLSILNED
110 120 130 140 150
QDWRPAITLK QIVLGVQDLL DSPNPNSPAQ EPAWRSFSRN KAEYDKKVLL

QAKQYSK
Length:157
Mass (Da):17,911
Last modified:October 1, 1996 - v1
Checksum:iD74EE9845BB677B4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82538 Genomic DNA. Translation: CAA57888.1.
Z74112 Genomic DNA. Translation: CAA98629.1.
BK006938 Genomic DNA. Translation: DAA11793.1.
PIRiS52414.
RefSeqiNP_010219.1. NM_001180123.1.

Genome annotation databases

EnsemblFungiiYDL064W; YDL064W; YDL064W.
GeneIDi851495.
KEGGisce:YDL064W.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X82538 Genomic DNA. Translation: CAA57888.1.
Z74112 Genomic DNA. Translation: CAA98629.1.
BK006938 Genomic DNA. Translation: DAA11793.1.
PIRiS52414.
RefSeqiNP_010219.1. NM_001180123.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKEX-ray1.90A/B1-157[»]
2GJDX-ray1.75A/B/C/D1-157[»]
3ONGX-ray2.30B/D1-157[»]
ProteinModelPortaliP50623.
SMRiP50623. Positions 2-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi31995. 159 interactions.
DIPiDIP-1531N.
IntActiP50623. 6 interactions.
MINTiMINT-400021.

Proteomic databases

MaxQBiP50623.
PeptideAtlasiP50623.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYDL064W; YDL064W; YDL064W.
GeneIDi851495.
KEGGisce:YDL064W.

Organism-specific databases

EuPathDBiFungiDB:YDL064W.
SGDiS000002222. UBC9.

Phylogenomic databases

GeneTreeiENSGT00550000075088.
HOGENOMiHOG000233454.
InParanoidiP50623.
KOiK10577.
OMAiDLKRWEC.
OrthoDBiEOG7SBP18.

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciYEAST:G3O-29479-MONOMER.
BRENDAi2.3.2.B5. 984.
ReactomeiR-SCE-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-SCE-3108214. SUMOylation of DNA damage response and repair proteins.
R-SCE-4570464. SUMOylation of RNA binding proteins.
R-SCE-4615885. SUMOylation of DNA replication proteins.
R-SCE-5696395. Formation of Incision Complex in GG-NER.

Miscellaneous databases

EvolutionaryTraceiP50623.
PROiP50623.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins."
    Seufert W., Futcher B., Jentsch S.
    Nature 373:78-81(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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. "Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p."
    Johnson E.S., Blobel G.
    J. Biol. Chem. 272:26799-26802(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  5. "An E3-like factor that promotes SUMO conjugation to the yeast septins."
    Johnson E.S., Gupta A.A.
    Cell 106:735-744(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIZ1, FUNCTION.
  6. "A novel factor required for the SUMO1/Smt3 conjugation of yeast septins."
    Takahashi Y., Toh-e A., Kikuchi Y.
    Gene 275:223-231(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SIZ1.
  7. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  8. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiUBC9_YEAST
AccessioniPrimary (citable) accession number: P50623
Secondary accession number(s): D6VRT3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 144 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 2600 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.