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Q95017 (UBC9_CAEEL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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):
SUMO-protein ligase
Ubiquitin carrier protein 9
Ubiquitin-conjugating enzyme E2 9
Ubiquitin-protein ligase 9
Gene names
Name:ubc-9
ORF Names:F29B9.6
OrganismCaenorhabditis elegans
Taxonomic identifier6239 [NCBI]
Taxonomic lineageEukaryotaMetazoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis

Protein attributes

Sequence length166 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2 E1 complex and catalyzes its covalent attachment to other proteins with the help of an E3 ligase such as gei-17. Required to sumoylate the ETS transcription factor lin-1 and the Polycomb protein sop-2. Required for embryonic development, fertility, vulval morphogenesis and inhibition of vulval cell fates. Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8

Catalytic activity

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

Pathway

Protein modification; protein sumoylation.

Subunit structure

Interacts with brd-1 and rad-51. Interacts with smo-1 and sop-2. Ref.1 Ref.4

Disruption phenotype

Sterility, embryonic lethality and sensitivity to radiation. Ref.4

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   LigandATP-binding
Nucleotide-binding
   Molecular functionDevelopmental protein
Ligase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological processanterior/posterior pattern specification

Inferred from mutant phenotype Ref.5. Source: WormBase

cellular response to stress

Inferred from mutant phenotype Ref.4. Source: WormBase

embryo development ending in birth or egg hatching

Inferred from mutant phenotype Ref.3Ref.4Ref.5. Source: WormBase

growth

Inferred from mutant phenotype. Source: WormBase

hermaphrodite genitalia development

Inferred from mutant phenotype. Source: WormBase

locomotion

Inferred from mutant phenotype. Source: WormBase

morphogenesis of an epithelium

Inferred from mutant phenotype. Source: WormBase

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.5. Source: WormBase

negative regulation of vulval development

Inferred from mutant phenotype Ref.6Ref.7. Source: WormBase

oviposition

Inferred from mutant phenotype Ref.3. Source: WormBase

pharyngeal muscle development

Inferred from mutant phenotype Ref.8. Source: WormBase

positive regulation of growth rate

Inferred from mutant phenotype. Source: WormBase

protein sumoylation

Inferred from direct assay Ref.5. Source: WormBase

regulation of protein localization

Inferred from mutant phenotype Ref.8. Source: WormBase

vulval development

Inferred from mutant phenotype Ref.3. Source: WormBase

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA polymerase II transcription factor binding

Inferred from physical interaction Ref.8. Source: WormBase

SAM domain binding

Inferred from physical interaction Ref.5. Source: WormBase

SUMO ligase activity

Inferred from direct assay Ref.5. Source: WormBase

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 166166SUMO-conjugating enzyme UBC9
PRO_0000082517

Sites

Active site931Glycyl thioester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q95017 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: E5A5AFA773DE286C

FASTA16619,115
        10         20         30         40         50         60 
MSGIAAGRLA EERKHWRKDH PFGFIAKPVK NADGTLNLFN WECAIPGRKD TIWEGGLYRI 

        70         80         90        100        110        120 
RMLFKDDFPS TPPKCKFEPP LFHPNVYPSG TVCLSLLDEN KDWKPSISIK QLLIGIQDLL 

       130        140        150        160 
NHPNIEDPAQ AEAYQIYCQN RAEYEKRVKK EAVKYAAELV QKQMLE 

« Hide

References

« Hide 'large scale' references
[1]"Ubc-9 of Caenorhabditis elegans: identification, characterization and interaction with smt-3."
Li T., Sun B., Lee M.-K., Teo T.-S.
Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH SMO-1.
Strain: Bristol N2.
[2]"Genome sequence of the nematode C. elegans: a platform for investigating biology."
The C. elegans sequencing consortium
Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Bristol N2.
[3]"Functional and phylogenetic analysis of the ubiquitylation system in Caenorhabditis elegans: ubiquitin-conjugating enzymes, ubiquitin-activating enzymes, and ubiquitin-like proteins."
Jones D., Crowe E., Stevens T.A., Candido E.P.M.
Genome Biol. 3:RESEARCH0002.1-RESEARCH0002.15(2002) [PubMed: 11806825] [Abstract]
Cited for: FUNCTION.
[4]"BRCA1/BARD1 orthologs required for DNA repair in Caenorhabditis elegans."
Boulton S.J., Martin J.S., Polanowska J., Hill D.E., Gartner A., Vidal M.
Curr. Biol. 14:33-39(2004) [PubMed: 14711411] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH BRD-1 AND RAD-1.
[5]"SUMO modification is required for in vivo Hox gene regulation by the Caenorhabditis elegans Polycomb group protein SOP-2."
Zhang H., Smolen G.A., Palmer R., Christoforou A., van den Heuvel S., Haber D.A.
Nat. Genet. 36:507-511(2004) [PubMed: 15107848] [Abstract]
Cited for: FUNCTION.
[6]"Sumoylation of LIN-1 promotes transcriptional repression and inhibition of vulval cell fates."
Leight E.R., Glossip D., Kornfeld K.
Development 132:1047-1056(2005) [PubMed: 15689373] [Abstract]
Cited for: FUNCTION.
[7]"Chromatin regulation and sumoylation in the inhibition of Ras-induced vulval development in Caenorhabditis elegans."
Poulin G., Dong Y., Fraser A.G., Hopper N.A., Ahringer J.
EMBO J. 24:2613-2623(2005) [PubMed: 15990876] [Abstract]
Cited for: FUNCTION.
[8]"The T-box factor TBX-2 and the SUMO conjugating enzyme UBC-9 are required for ABa-derived pharyngeal muscle in C. elegans."
Roy Chowdhuri S., Crum T., Woollard A., Aslam S., Okkema P.G.
Dev. Biol. 295:664-677(2006) [PubMed: 16701625] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF106565 mRNA. Translation: AAC97374.1.
FO081255 Genomic DNA. Translation: CCD70229.1.
PIRT29929.
RefSeqNP_001023158.1. NM_001027987.2.
UniGeneCel.6281.

3D structure databases

ProteinModelPortalQ95017.
SMRQ95017. Positions 1-156.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-25778N.
IntActQ95017. 11 interactions.
MINTMINT-229351.
STRINGQ95017.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaF29B9.6.1; F29B9.6.1; F29B9.6.
F29B9.6.2; F29B9.6.2; F29B9.6.
GeneID3565767.
KEGGcel:F29B9.6.
UCSCF29B9.6.1. c. elegans.

Organism-specific databases

CTD3565767.
WormBaseF29B9.6; CE09784; WBGene00006706; ubc-9.

Phylogenomic databases

eggNOGmeNOG06611.
GeneTreeEMGT00070000025728.
HOGENOMHBG756483.
InParanoidQ95017.
OMAKQWRKDH.
PhylomeDBQ95017.

Gene expression databases

ArrayExpressQ95017.

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

NextBio957785.

Entry information

Entry nameUBC9_CAEEL
AccessionPrimary (citable) accession number: Q95017
Secondary accession number(s): Q9GYI5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Relevant documents

Caenorhabditis elegans

Caenorhabditis elegans: entries, gene names and cross-references to WormPep

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families