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P50623 (UBC9_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:UBC9
Ordered Locus Names:YDL064W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length157 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.4 Ref.5

Catalytic activity

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

Pathway

Protein modification; protein sumoylation.

Subunit structure

Interacts with SIZ1. Ref.5 Ref.6

Subcellular location

Nucleus Ref.7.

Miscellaneous

Present with 2600 molecules/cell in log phase SD medium. Ref.8

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 157157SUMO-conjugating enzyme UBC9
PRO_0000082556

Sites

Active site931Glycyl thioester intermediate By similarity

Secondary structure

1 ......................... 157
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50623 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: D74EE9845BB677B4

FASTA15717,911
        10         20         30         40         50         60 
MSSLCLQRLQ EERKKWRKDH PFGFYAKPVK KADGSMDLQK WEAGIPGKEG TNWAGGVYPI 

        70         80         90        100        110        120 
TVEYPNEYPS KPPKVKFPAG FYHPNVYPSG TICLSILNED QDWRPAITLK QIVLGVQDLL 

       130        140        150 
DSPNPNSPAQ EPAWRSFSRN KAEYDKKVLL QAKQYSK

« Hide

References

« Hide 'large scale' references
[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: 7800043] [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. expand/collapse author list , 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: 9169867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[3]Saccharomyces Genome Database
Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
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: 9341106] [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: 11572779] [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: 11587849] [Abstract]
Cited for: INTERACTION WITH SIZ1.
[7]"Global analysis of protein localization in budding yeast."
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W., Weissman J.S., O'Shea E.K.
Nature 425:686-691(2003) [PubMed: 14562095] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
[8]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed: 14562106] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X82538 Genomic DNA. Translation: CAA57888.1.
Z74112 Genomic DNA. Translation: CAA98629.1.
BK006938 Genomic DNA. Translation: DAA11793.1.
PIRS52414.
RefSeqNP_010219.1. NM_001180123.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EKEX-ray1.90A/B1-157[»]
2GJDX-ray1.75A/B/C/D1-157[»]
3ONGX-ray2.30B/D1-157[»]
ProteinModelPortalP50623.
SMRP50623. Positions 2-157.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-1531N.
IntActP50623. 7 interactions.
MINTMINT-400021.
STRINGP50623.

Proteomic databases

PeptideAtlasP50623.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYDL064W; YDL064W; YDL064W.
GeneID851495.
KEGGsce:YDL064W.
NMPDRfig|4932.3.peg.959.

Organism-specific databases

CYGDYDL064w.
SGDS000002222. UBC9.

Phylogenomic databases

eggNOGfuNOG08815.
GeneTreeEFGT00050000001509.
HOGENOMHBG756483.
OMAKQWRKDH.
OrthoDBEOG4X0R2S.

Gene expression databases

ArrayExpressP50623.
GenevestigatorP50623.
GermOnlineYDL064W. Saccharomyces cerevisiae.

Family and domain databases

InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
Gene3DG3DSA:3.10.110.10. UBQ-conjugat_E2. 1 hit.
KOK10577.
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio968831.

Entry information

Entry nameUBC9_YEAST
AccessionPrimary (citable) accession number: P50623
Secondary accession number(s): D6VRT3
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: January 25, 2012
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents