ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q9Y818


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name UBC15_SCHPO
Primary accession number Q9Y818
Secondary accession numbers None
Integrated into Swiss-Prot on May 23, 2003
Sequence was last modified on November 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 50)
Name and origin of the protein
Protein name Ubiquitin-conjugating enzyme E2 15
Synonyms EC 6.3.2.19
Ubiquitin-protein ligase 15
Ubiquitin carrier protein 15
Gene name
Name: ubc15
ORFNames: SPBC1105.09
From
Schizosaccharomyces pombe (Fission yeast) [TaxID: 4896] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 38366 / 972;
DOI=10.1038/nature724; PubMed=11859360 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
FUNCTION.
DOI=10.1128/EC.1.4.613-625.2002; PubMed=12456009 [NCBI, ExPASy, EBI, Israel, Japan]
Nielsen I.S., Nielsen O., Murray J.M., Thon G.;
"The fission yeast ubiquitin-conjugating enzymes UbcP3, Ubc15, and Rhp6 affect transcriptional silencing of the mating-type region.";
Eukaryot. Cell 1:613-625(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
CU329671; CAB50972.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR T39286; T39286.
RefSeq NP_596465.1; -.
3D structure databases
HSSP P34477; 1PZV. [HSSP ENTRY / PDB]
ModBase Q9Y818.
Enzyme and pathway databases
BioCyc SPOM-XXX-01:SPOM-XXX-01-004466-MON; -.
Organism-specific databases
GeneDB_Spombe SPBC1105.09; -.
Gene expression databases
ArrayExpress Q9Y818; -.
Ontologies
GO
GO:0004842; Molecular function: ubiquitin-protein ligase activity (inferred from electronic annotation from EC).
GO:0030466; Biological process: chromatin silencing at silent mating-type cassette (inferred from mutant phenotype from GeneDB_SPombe).
GO:0043687; Biological process: post-translational protein modification (inferred from electronic annotation from InterPro).
GO:0051246; Biological process: regulation of protein metabolic process (inferred from electronic annotation from InterPro).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR016135; UBQ-conjugat/RWD-like.
IPR000608; UBQ-conjugat_E2.
Graphical view of domain structure.
Gene3D G3DSA:3.10.110.10; UBQ-conjugat_E2; 1.
PANTHER PTHR11621; UBQ-conjugat_E2; 1.
Pfam PF00179; UQ_con; 1.
Pfam graphical view of domain structure.
ProDom PD000461; UBQ_conjugat; 1.
[Domain structure / List of seq. sharing at least 1 domain]
SMART SM00212; UBCc; 1.
SMART graphical view of domain structure.
PROSITE PS00183; UBIQUITIN_CONJUGAT_1; 1.
PS50127; UBIQUITIN_CONJUGAT_2; 1.
PROSITE graphical view of domain structure (profiles).
ProtoNet Q9Y818.
Genome annotation databases
GeneID 2539995; -.
KEGG spo:SPBC1105.09; -.
NMPDR fig|4896.1.peg.2331; -.
Other
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Ligase; Ubl conjugation pathway.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
CHAIN   1   167  167     Ubiquitin-conjugating enzyme E2 15. PRO_0000082589
ACT_SITE   90    90        Glycyl thioester intermediate (By similarity). 
Sequence information
Length: 167 AA [This is the length of the unprocessed precursor] Molecular weight: 19106 Da [This is the MW of the unprocessed precursor] CRC64: 2289FD04069E1707 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MPSSASEQLL RKQLKEIQKN PPQGFSVGLV DDKSIFEWEV MIIGPEDTLY EGGFFHATLS 

        70         80         90        100        110        120 
FPQDYPLMPP KMKFTTEIWH PNVHPNGEVC ISILHPPGDD KYGYEDAGER WLPVHSPETI 

       130        140        150        160 
LISVISMLSS PNDESPANID AAKEFRENPQ EFKKRVRRLV RRSIEMI 

Q9Y818 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!