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O00102

- UBC7_SCHPO

UniProt

O00102 - UBC7_SCHPO

Protein

Ubiquitin-conjugating enzyme E2-18 kDa

Gene

ubc7

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 2 (14 Aug 2001)
      Previous versions | rss
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    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 PublicationsPROSITE-ProRule annotation

    Catalytic activityi

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

    Pathwayi

    Sites

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

    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

    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

    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    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

    Experimental Info

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

    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

    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: October 1, 2014
    This is version 101 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