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Protein

Ubiquitin-conjugating enzyme E2-18 kDa

Gene

ubc7

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

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.PROSITE-ProRule annotation2 Publications

Catalytic activityi

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

Pathway:iprotein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.PROSITE-ProRule annotation
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • chromatin silencing at silent mating-type cassette Source: PomBase
  • ER-associated ubiquitin-dependent protein catabolic process Source: PomBase
  • negative regulation of transcription by transcription factor catabolism Source: PomBase
  • protein polyubiquitination Source: GO_Central
  • protein ubiquitination Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2-18 kDa (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein
Ubiquitin-protein ligase
Gene namesi
Name:ubc7
Synonyms:ubcp3
ORF Names:SPBP16F5.04
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBP16F5.04.
PomBaseiSPBP16F5.04. ubc7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: PomBase
  • endoplasmic reticulum Source: GO_Central
  • nucleus Source: PomBase
  • ubiquitin ligase complex Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 166166Ubiquitin-conjugating enzyme E2-18 kDaPRO_0000082553Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki90 – 90Glycyl cysteine thioester (Cys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

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

Keywords - PTMi

Thioester bond, Ubl conjugation

Proteomic databases

MaxQBiO00102.

Interactioni

Protein-protein interaction databases

MINTiMINT-4666424.

Structurei

3D structure databases

ProteinModelPortaliO00102.
SMRiO00102. Positions 6-166.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233454.
InParanoidiO00102.
KOiK04555.
OMAiKMKFTCD.
OrthoDBiEOG7SBP18.
PhylomeDBiO00102.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O00102-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKAMALRRL MKEYKELTEN GPDGITAGPS NEDDFFTWDC LIQGPDGTPF
60 70 80 90 100
EGGLYPATLK FPSDYPLGPP TLKFECEFFH PNVYKDGTVC ISILHAPGDD
110 120 130 140 150
PNMYESSSER WSPVQSVEKI LLSVMSMLAE PNDESGANID ACKMWREDRE
160
EYCRVVRRLA RKTLGL
Length:166
Mass (Da):18,720
Last modified:August 14, 2001 - v2
Checksum:iC376ACE52EF444EE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61A → P in BAA20373 (PubMed:9154838).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85544 mRNA. Translation: BAA20373.1.
CU329671 Genomic DNA. Translation: CAC08543.1.
PIRiT43235.
RefSeqiNP_595778.1. NM_001021678.2.

Genome annotation databases

EnsemblFungiiSPBP16F5.04.1; SPBP16F5.04.1:pep; SPBP16F5.04.
GeneIDi2541252.
KEGGispo:SPBP16F5.04.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D85544 mRNA. Translation: BAA20373.1.
CU329671 Genomic DNA. Translation: CAC08543.1.
PIRiT43235.
RefSeqiNP_595778.1. NM_001021678.2.

3D structure databases

ProteinModelPortaliO00102.
SMRiO00102. Positions 6-166.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

MINTiMINT-4666424.

Proteomic databases

MaxQBiO00102.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBP16F5.04.1; SPBP16F5.04.1:pep; SPBP16F5.04.
GeneIDi2541252.
KEGGispo:SPBP16F5.04.

Organism-specific databases

EuPathDBiFungiDB:SPBP16F5.04.
PomBaseiSPBP16F5.04. ubc7.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233454.
InParanoidiO00102.
KOiK04555.
OMAiKMKFTCD.
OrthoDBiEOG7SBP18.
PhylomeDBiO00102.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi20802364.
PROiO00102.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiUBC7_SCHPO
AccessioniPrimary (citable) accession number: O00102
Secondary accession number(s): Q9HDP3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: August 14, 2001
Last modified: July 22, 2015
This is version 109 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.