Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)DescriptionActionsGraphical viewLength
Active sitei93Glycyl thioester intermediatePROSITE-ProRule annotation1

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
  • cytoplasm Source: GO_Central
  • nucleus Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00000825562 – 157SUMO-conjugating enzyme UBC9Add BLAST156

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP50623.
PRIDEiP50623.

Interactioni

Subunit structurei

Interacts with SIZ1.2 Publications

Protein-protein interaction databases

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

Structurei

Secondary structure

1157
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi4 – 18Combined sources15
Beta strandi25 – 30Combined sources6
Beta strandi36 – 46Combined sources11
Turni52 – 55Combined sources4
Beta strandi56 – 63Combined sources8
Turni66 – 70Combined sources5
Beta strandi74 – 76Combined sources3
Beta strandi90 – 92Combined sources3
Helixi95 – 97Combined sources3
Turni99 – 102Combined sources4
Helixi109 – 120Combined sources12
Helixi131 – 139Combined sources9
Helixi141 – 154Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EKEX-ray1.90A/B1-157[»]
2GJDX-ray1.75A/B/C/D1-157[»]
3ONGX-ray2.30B/D1-157[»]
5JNEX-ray2.85B/F1-157[»]
ProteinModelPortaliP50623.
SMRiP50623.
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.
OrthoDBiEOG092C50OL.

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EKEX-ray1.90A/B1-157[»]
2GJDX-ray1.75A/B/C/D1-157[»]
3ONGX-ray2.30B/D1-157[»]
5JNEX-ray2.85B/F1-157[»]
ProteinModelPortaliP50623.
SMRiP50623.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

Proteomic databases

MaxQBiP50623.
PRIDEiP50623.

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.
OrthoDBiEOG092C50OL.

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...

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: November 30, 2016
This is version 149 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.