Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9Y818

- UBC15_SCHPO

UniProt

Q9Y818 - UBC15_SCHPO

Protein

Ubiquitin-conjugating enzyme E2 15

Gene

ubc15

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 95 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the covalent attachment of ubiquitin to other proteins. Has a role in the formation of chromatin structures that influence the localization of transcriptional silencing factors.1 PublicationPROSITE-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

    GO - Biological processi

    1. chromatin silencing at silent mating-type cassette Source: PomBase
    2. 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 15 (EC:6.3.2.19)
    Alternative name(s):
    Ubiquitin carrier protein 15
    Ubiquitin-protein ligase 15
    Gene namesi
    Name:ubc15
    ORF Names:SPBC1105.09
    OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
    Taxonomic identifieri284812 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
    ProteomesiUP000002485: Chromosome II

    Organism-specific databases

    PomBaseiSPBC1105.09.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: PomBase

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 167167Ubiquitin-conjugating enzyme E2 15PRO_0000082589Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y818.

    Interactioni

    Protein-protein interaction databases

    BioGridi276539. 30 interactions.
    STRINGi4896.SPBC1105.09-1.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y818.
    SMRiQ9Y818. Positions 6-165.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG5078.
    HOGENOMiHOG000233454.
    KOiK10575.
    OMAiFYSPNEE.
    OrthoDBiEOG7SBP18.
    PhylomeDBiQ9Y818.

    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.

    Q9Y818-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSSASEQLL RKQLKEIQKN PPQGFSVGLV DDKSIFEWEV MIIGPEDTLY    50
    EGGFFHATLS FPQDYPLMPP KMKFTTEIWH PNVHPNGEVC ISILHPPGDD 100
    KYGYEDAGER WLPVHSPETI LISVISMLSS PNDESPANID AAKEFRENPQ 150
    EFKKRVRRLV RRSIEMI 167
    Length:167
    Mass (Da):19,106
    Last modified:November 1, 1999 - v1
    Checksum:i2289FD04069E1707
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB50972.1.
    PIRiT39286.
    RefSeqiNP_596465.1. NM_001022384.2.

    Genome annotation databases

    EnsemblFungiiSPBC1105.09.1; SPBC1105.09.1:pep; SPBC1105.09.
    GeneIDi2539995.
    KEGGispo:SPBC1105.09.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    CU329671 Genomic DNA. Translation: CAB50972.1 .
    PIRi T39286.
    RefSeqi NP_596465.1. NM_001022384.2.

    3D structure databases

    ProteinModelPortali Q9Y818.
    SMRi Q9Y818. Positions 6-165.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 276539. 30 interactions.
    STRINGi 4896.SPBC1105.09-1.

    Proteomic databases

    MaxQBi Q9Y818.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii SPBC1105.09.1 ; SPBC1105.09.1:pep ; SPBC1105.09 .
    GeneIDi 2539995.
    KEGGi spo:SPBC1105.09.

    Organism-specific databases

    PomBasei SPBC1105.09.

    Phylogenomic databases

    eggNOGi COG5078.
    HOGENOMi HOG000233454.
    KOi K10575.
    OMAi FYSPNEE.
    OrthoDBi EOG7SBP18.
    PhylomeDBi Q9Y818.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 20801138.
    PROi Q9Y818.

    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. "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.
    2. "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.

    Entry informationi

    Entry nameiUBC15_SCHPO
    AccessioniPrimary (citable) accession number: Q9Y818
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 23, 2003
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 95 of the entry and version 1 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