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Protein

Ubiquitin-conjugating enzyme spm2

Gene

spm2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Has a role in the DNA error-free postreplication repair (PRR) pathway. Lacks catalytic activity by itself. The ubc13/spm2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.1 Publication

GO - Molecular functioni

GO - Biological processi

  • postreplication repair Source: PomBase
  • protein K63-linked ubiquitination Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme spm2
Alternative name(s):
Ubiquitin-conjugating enzyme variant MMS2 homolog
Short name:
UEV MMS2
Gene namesi
Name:spm2
ORF Names:SPCC338.05c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome III

Organism-specific databases

EuPathDBiFungiDB:SPCC338.05c.
PomBaseiSPCC338.05c.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 139139Ubiquitin-conjugating enzyme spm2PRO_0000082599Add
BLAST

Proteomic databases

MaxQBiO74983.

Interactioni

Subunit structurei

Heterodimer with ubc13.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi275304. 7 interactions.
MINTiMINT-4682250.

Structurei

3D structure databases

ProteinModelPortaliO74983.
SMRiO74983. Positions 3-138.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000036561.
InParanoidiO74983.
KOiK10704.
OMAiLANWQRQ.
OrthoDBiEOG77WWRD.
PhylomeDBiO74983.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O74983-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAKVPRNFKL LEELEKGEKG LGESSCSYGL TNADDITLSD WNATILGPAH
60 70 80 90 100
SVHENRIYSL KIHCDANYPD APPIVTFVSR INLPGVDGET GKVNPHKIDC
110 120 130
LRHWKREYSM ETVLLDLKKE MASSSNRKLP QPPEGSTFF
Length:139
Mass (Da):15,555
Last modified:November 1, 1998 - v1
Checksum:iBB247264D23F9BB2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF470233 mRNA. Translation: AAL79845.1.
CU329672 Genomic DNA. Translation: CAA19336.1.
PIRiT41737.
RefSeqiNP_588162.1. NM_001023151.2.

Genome annotation databases

EnsemblFungiiSPCC338.05c.1; SPCC338.05c.1:pep; SPCC338.05c.
GeneIDi2538720.
KEGGispo:SPCC338.05c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF470233 mRNA. Translation: AAL79845.1.
CU329672 Genomic DNA. Translation: CAA19336.1.
PIRiT41737.
RefSeqiNP_588162.1. NM_001023151.2.

3D structure databases

ProteinModelPortaliO74983.
SMRiO74983. Positions 3-138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi275304. 7 interactions.
MINTiMINT-4682250.

Proteomic databases

MaxQBiO74983.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPCC338.05c.1; SPCC338.05c.1:pep; SPCC338.05c.
GeneIDi2538720.
KEGGispo:SPCC338.05c.

Organism-specific databases

EuPathDBiFungiDB:SPCC338.05c.
PomBaseiSPCC338.05c.

Phylogenomic databases

HOGENOMiHOG000036561.
InParanoidiO74983.
KOiK10704.
OMAiLANWQRQ.
OrthoDBiEOG77WWRD.
PhylomeDBiO74983.

Miscellaneous databases

PROiO74983.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural and functional conservation of error-free DNA postreplication repair in Schizosaccharomyces pombe."
    Brown M., Zhu Y., Hemmingsen S.M., Xiao W.
    DNA Repair 1:869-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH UBC13.
  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.

Entry informationi

Entry nameiMMS2_SCHPO
AccessioniPrimary (citable) accession number: O74983
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: November 1, 1998
Last modified: July 6, 2016
This is version 115 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. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.