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O74810 (UBC1_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. 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 1
EC=6.3.2.19
Alternative name(s):
Ubiquitin carrier protein 1
Ubiquitin-protein ligase 1
Gene names
Name:ubc1
ORF Names:SPBC2D10.20
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 length217 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 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.

Catalytic activity

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

Pathway

Protein modification; protein ubiquitination.

Subcellular location

Cytoplasm. Nucleus Ref.2.

Sequence similarities

Belongs to the ubiquitin-conjugating enzyme family.

Ontologies

Keywords
   Biological processUbl conjugation pathway
   Cellular componentCytoplasm
Nucleus
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processprotein ubiquitination

Inferred from sequence orthology. Source: PomBase

   Cellular_componentcytosol

Inferred from direct assay Ref.2. Source: PomBase

nucleus

Inferred from direct assay Ref.2. Source: PomBase

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ubiquitin-protein ligase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 217217Ubiquitin-conjugating enzyme E2 1
PRO_0000310742

Sites

Active site891Glycyl thioester intermediate By similarity

Sequences

Sequence LengthMass (Da)Tools
O74810 [UniParc].

Last modified May 1, 2000. Version 2.
Checksum: 4ACDEC0648676BE4

FASTA21724,507
        10         20         30         40         50         60 
MSDNRSRRIA KELADVQQDK QAGIQVWTIN DDISHLKGMF RGPEGTPYEG GYFVVDIEIP 

        70         80         90        100        110        120 
IDYPFRPPKM NFDTKIYHPN VSSQTGAICL DILKDQWSPV YTMKSALISL QSLLCTPEPS 

       130        140        150        160        170        180 
NPQDAQVAQV YLQNYQQFVR TAREWTSSYA AAPAGVDLDA ENTEFGGIDP NIITNLQQFG 

       190        200        210 
FSTELIVRVL QREHIKSQED LKDYPNGING ILDQLLH

« 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]"ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CU329671 Genomic DNA. Translation: CAA21178.2.
PIRT40123.
RefSeqNP_596239.1. NM_001022159.2.

3D structure databases

HSSPHSSP built from PDB template 1FZY based on UniProtKB P21734.
ProteinModelPortalO74810.
SMRO74810. Positions 4-151.
ModBaseSearch...

Protein-protein interaction databases

STRING4896.SPBC2D10.20-1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPBC2D10.20.1; SPBC2D10.20.1:pep; SPBC2D10.20.
GeneID2540277.
KEGGspo:SPBC2D10.20.

Organism-specific databases

PomBaseSPBC2D10.20.

Phylogenomic databases

eggNOGCOG5078.
HOGENOMHOG000233455.
KOK04649.
OMASESDIHH.
OrthoDBEOG46HKM6.

Enzyme and pathway databases

UniPathwayUPA00143.

Family and domain databases

Gene3D3.10.110.10. 1 hit.
InterProIPR015368. UBA_C_fun.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamPF09288. UBA_3. 1 hit.
PF00179. 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

NextBio20801407.

Entry information

Entry nameUBC1_SCHPO
AccessionPrimary (citable) accession number: O74810
Entry history
Integrated into UniProtKB/Swiss-Prot: November 13, 2007
Last sequence update: May 1, 2000
Last modified: May 1, 2013
This is version 88 of the entry and version 2 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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