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O00102

- UBC7_SCHPO

UniProt

O00102 - UBC7_SCHPO

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Protein

Ubiquitin-conjugating enzyme E2-18 kDa

Gene
ubc7, ubcp3, SPBP16F5.04
Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - 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.2 Publications

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei90 – 901Glycyl thioester intermediate By similarity

GO - Molecular functioni

  1. acid-amino acid ligase activity Source: InterPro
  2. ATP binding Source: UniProtKB-KW
  3. ubiquitin-protein transferase activity Source: PomBase

GO - Biological processi

  1. chromatin silencing at silent mating-type cassette Source: PomBase
  2. ER-associated ubiquitin-dependent protein catabolic process Source: PomBase
  3. negative regulation of transcription by transcription factor catabolism Source: PomBase
  4. 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: Chromosome II

Organism-specific databases

PomBaseiSPBP16F5.04.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. nucleus Source: PomBase
  3. 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.
STRINGi4896.SPBP16F5.04-1.

Structurei

3D structure databases

ProteinModelPortaliO00102.
SMRiO00102. Positions 6-166.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233454.
KOiK04555.
OMAiDMFHPNI.
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

MSKAMALRRL MKEYKELTEN GPDGITAGPS NEDDFFTWDC LIQGPDGTPF    50
EGGLYPATLK FPSDYPLGPP TLKFECEFFH PNVYKDGTVC ISILHAPGDD 100
PNMYESSSER WSPVQSVEKI LLSVMSMLAE PNDESGANID ACKMWREDRE 150
EYCRVVRRLA RKTLGL 166
Length:166
Mass (Da):18,720
Last modified:August 14, 2001 - v2
Checksum:iC376ACE52EF444EE
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61A → P in BAA20373. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
D85544 mRNA. Translation: BAA20373.1 .
CU329671 Genomic DNA. Translation: CAC08543.1 .
PIRi T43235.
RefSeqi NP_595778.1. NM_001021678.2.

3D structure databases

ProteinModelPortali O00102.
SMRi O00102. Positions 6-166.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-4666424.
STRINGi 4896.SPBP16F5.04-1.

Proteomic databases

MaxQBi O00102.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPBP16F5.04.1 ; SPBP16F5.04.1:pep ; SPBP16F5.04 .
GeneIDi 2541252.
KEGGi spo:SPBP16F5.04.

Organism-specific databases

PomBasei SPBP16F5.04.

Phylogenomic databases

eggNOGi COG5078.
HOGENOMi HOG000233454.
KOi K04555.
OMAi DMFHPNI.
OrthoDBi EOG7SBP18.
PhylomeDBi O00102.

Enzyme and pathway databases

UniPathwayi UPA00143 .

Miscellaneous databases

NextBioi 20802364.
PROi O00102.

Family and domain databases

Gene3Di 3.10.110.10. 1 hit.
InterProi IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view ]
Pfami PF00179. UQ_con. 1 hit.
[Graphical view ]
SUPFAMi SSF54495. SSF54495. 1 hit.
PROSITEi PS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 100 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

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