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O42646 (UBC6_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 96. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Ubiquitin-conjugating enzyme E2 6
EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein 6
Ubiquitin-protein ligase 6
Gene names
Name:ubc6
ORF Names:SPAC10F6.05c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Taphrinomycotina › Schizosaccharomycetes › Schizosaccharomycetales › Schizosaccharomycetaceae › Schizosaccharomyces ›

Protein attributes

Sequence length227 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 By similarity.

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Endoplasmic reticulum membrane By similarity.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentEndoplasmic reticulum
Membrane
   DomainTransmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processER-associated protein catabolic process

Inferred from sequence orthology. Source: PomBase

   Cellular_componentendoplasmic reticulum membrane

Inferred from sequence orthology. Source: PomBase

integral to membrane

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from sequence orthology. Source: PomBase

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 227227Ubiquitin-conjugating enzyme E2 6
PRO_0000082551

Regions

Topological domain1 – 206206Cytoplasmic Potential
Transmembrane207 – 22519Helical; Potential

Sites

Active site871Glycyl thioester intermediate By similarity

Experimental info

Sequence conflict221V → F in BAA13909. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O42646 [UniParc].

Last modified June 1, 1998. Version 1.
Checksum: 58BE058326D843AC

FASTA22725,659
        10         20         30         40         50         60 
MASKGAYKRL MKEYLALQKN PVELVDAKPA TENILEWHYI ITGPPDTPYE GGQYHGTLIF 

        70         80         90        100        110        120 
PPDYPFKPPA IRMITPSGRF QTNTRLCLSF SDFHPKSWNP SWMVSTILVG LVSFMTSDEI 

       130        140        150        160        170        180 
TTGGIVTSES TRRTYAKDTK RFNIMDNPKF LIMFPELIDK NREDIAKAAA EAALIEPQQI 

       190        200        210        220 
HSTPVSSNEC KKNEPFNSKQ SWVKSRWSIA VLVFFALALA RFFGADS

« Hide

References

[1]"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.
[2]"Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-227.
Strain: PR745.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329670 Genomic DNA. Translation: CAA15718.1.
D89248 mRNA. Translation: BAA13909.1.
PIRT37499.
T43159.
RefSeqNP_593256.1. NM_001018653.2.

3D structure databases

ProteinModelPortalO42646.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPAC10F6.05c-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC10F6.05c.1; SPAC10F6.05c.1:pep; SPAC10F6.05c.
GeneID2541642.
KEGGspo:SPAC10F6.05c.

Organism-specific databases

PomBaseSPAC10F6.05c.

Phylogenomic databases

HOGENOMHOG000170329.
KOK04554.
OMASFMTGDE.
OrthoDBEOG441TMP.

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMSSF54495. UBQ-conjugat/RWD-like. 1 hit.
PROSITEPS00183. UBIQUITIN_CONJUGAT_1. False negative.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio20802735.

Entry information

Entry nameUBC6_SCHPO
AccessionPrimary (citable) accession number: O42646
Secondary accession number(s): P78897, Q1L844
Entry history
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: June 1, 1998
Last modified: May 1, 2013
This is version 96 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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