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O00102 (UBC7_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 99. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2-18 kDa

EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein
Ubiquitin-protein ligase
Gene names
Name:ubc7
Synonyms:ubcp3
ORF Names:SPBP16F5.04
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

Protein attributes

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

General annotation (Comments)

Function

Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the doa10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains, and of the hrd1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD-L), or ER-membrane proteins with misfolded transmembrane domains (ERAD-M) By similarity. Together with hrd1, required for the degradation of the transcription factor sre1 precursor in the absence of its binding partner scp1. Has a role in the formation of chromatin structures that influence the localization of transcriptional silencing factors. Ref.3 Ref.4

Catalytic activity

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.

Pathway

Protein modification; protein ubiquitination.

Post-translational modification

Autoubiquitinated at Cys-90; undergoes 'Lys-48'-linked polyubiquitination, which leads to proteasome-dependent protein degradation By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 166166Ubiquitin-conjugating enzyme E2-18 kDa
PRO_0000082553

Sites

Active site901Glycyl thioester intermediate By similarity

Amino acid modifications

Cross-link90Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict61A → P in BAA20373. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O00102 [UniParc].

Last modified August 14, 2001. Version 2.
Checksum: C376ACE52EF444EE

FASTA16618,720
        10         20         30         40         50         60 
MSKAMALRRL MKEYKELTEN GPDGITAGPS NEDDFFTWDC LIQGPDGTPF EGGLYPATLK 

        70         80         90        100        110        120 
FPSDYPLGPP TLKFECEFFH PNVYKDGTVC ISILHAPGDD PNMYESSSER WSPVQSVEKI 

       130        140        150        160 
LLSVMSMLAE PNDESGANID ACKMWREDRE EYCRVVRRLA RKTLGL 

« Hide

References

« Hide 'large scale' references
[1]"A ubiquitin-conjugating enzyme in fission yeast that is essential for the onset of anaphase in mitosis."
Osaka F., Seino H., Seno T., Yamao F.
Mol. Cell. Biol. 17:3388-3397(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: 972 / ATCC 24843.
[2]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
[3]"The fission yeast ubiquitin-conjugating enzymes UbcP3, Ubc15, and Rhp6 affect transcriptional silencing of the mating-type region."
Nielsen I.S., Nielsen O., Murray J.M., Thon G.
Eukaryot. Cell 1:613-625(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[4]"Degradation of sterol regulatory element-binding protein precursor requires the endoplasmic reticulum-associated degradation components Ubc7 and Hrd1 in fission yeast."
Hughes B.T., Nwosu C.C., Espenshade P.J.
J. Biol. Chem. 284:20512-20521(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D85544 mRNA. Translation: BAA20373.1.
CU329671 Genomic DNA. Translation: CAC08543.1.
PIRT43235.
RefSeqNP_595778.1. NM_001021678.2.

3D structure databases

ProteinModelPortalO00102.
SMRO00102. Positions 6-166.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-4666424.
STRING4896.SPBP16F5.04-1.

Proteomic databases

MaxQBO00102.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBP16F5.04.1; SPBP16F5.04.1:pep; SPBP16F5.04.
GeneID2541252.
KEGGspo:SPBP16F5.04.

Organism-specific databases

PomBaseSPBP16F5.04.

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233454.
KOK04555.
OMADMFHPNI.
OrthoDBEOG7SBP18.
PhylomeDBO00102.

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. SSF54495. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802364.
PROO00102.

Entry information

Entry nameUBC7_SCHPO
AccessionPrimary (citable) accession number: O00102
Secondary accession number(s): Q9HDP3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: May 14, 2014
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways