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Q9Y818

- UBC15_SCHPO

UniProt

Q9Y818 - UBC15_SCHPO

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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

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
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 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
Complete GO annotation...

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. 31 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.
InParanoidiQ9Y818.
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

        10         20         30         40         50
MPSSASEQLL RKQLKEIQKN PPQGFSVGLV DDKSIFEWEV MIIGPEDTLY
60 70 80 90 100
EGGFFHATLS FPQDYPLMPP KMKFTTEIWH PNVHPNGEVC ISILHPPGDD
110 120 130 140 150
KYGYEDAGER WLPVHSPETI LISVISMLSS PNDESPANID AAKEFRENPQ
160
EFKKRVRRLV RRSIEMI
Length:167
Mass (Da):19,106
Last modified:November 1, 1999 - v1
Checksum:i2289FD04069E1707
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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. 31 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.
InParanoidi Q9Y818.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 97 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