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Protein

Ubiquitin-conjugating enzyme variant MMS2

Gene

MMS2

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's 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/MMS2 heterodimer catalyzes the synthesis of non-canonical poly-ubiquitin chains that are linked through 'Lys-63'.

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • ubiquitin-protein transferase activity Source: SGD

GO - Biological processi

  • free ubiquitin chain polymerization Source: SGD
  • postreplication repair Source: SGD
  • protein polyubiquitination Source: SGD
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciYEAST:G3O-30588-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme variant MMS2
Short name:
UEV MMS2
Gene namesi
Name:MMS2
Ordered Locus Names:YGL087C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome VII

Organism-specific databases

EuPathDBiFungiDB:YGL087C.
SGDiS000003055. MMS2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: SGD
  • nucleus Source: SGD
  • ubiquitin conjugating enzyme complex Source: SGD
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi8 – 81F → A: Strongly reduces UBC13 binding and interferes with error-free DNA repair. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 137137Ubiquitin-conjugating enzyme variant MMS2PRO_0000082598Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei71 – 711PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP53152.
PeptideAtlasiP53152.
PRIDEiP53152.

PTM databases

iPTMnetiP53152.

Interactioni

Subunit structurei

Heterodimer with UBC13.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
UBC13P524904EBI-11035,EBI-19777

Protein-protein interaction databases

BioGridi33163. 131 interactions.
DIPiDIP-5829N.
IntActiP53152. 6 interactions.
MINTiMINT-580773.

Structurei

Secondary structure

1
137
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 1813Combined sources
Beta strandi26 – 327Combined sources
Beta strandi40 – 467Combined sources
Beta strandi49 – 513Combined sources
Turni52 – 554Combined sources
Beta strandi57 – 637Combined sources
Turni66 – 705Combined sources
Beta strandi74 – 796Combined sources
Beta strandi84 – 863Combined sources
Turni88 – 903Combined sources
Helixi98 – 1014Combined sources
Helixi109 – 12012Combined sources
Helixi123 – 1264Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JATX-ray1.60B1-137[»]
2GMIX-ray2.50B1-137[»]
ProteinModelPortaliP53152.
SMRiP53152. Positions 3-137.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP53152.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00740000115534.
HOGENOMiHOG000036561.
InParanoidiP53152.
KOiK10704.
OMAiLANWQRQ.
OrthoDBiEOG77WWRD.

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.

P53152-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKVPRNFRL LEELEKGEKG FGPESCSYGL ADSDDITMTK WNGTILGPPH
60 70 80 90 100
SNHENRIYSL SIDCGPNYPD SPPKVTFISK INLPCVNPTT GEVQTDFHTL
110 120 130
RDWKRAYTME TLLLDLRKEM ATPANKKLRQ PKEGETF
Length:137
Mass (Da):15,545
Last modified:October 1, 1996 - v1
Checksum:iE1DA713C94378795
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66724 Genomic DNA. Translation: AAC24241.1.
Z72609 Genomic DNA. Translation: CAA96792.1.
BK006941 Genomic DNA. Translation: DAA08018.1.
PIRiS64094.
RefSeqiNP_011428.1. NM_001180952.1.

Genome annotation databases

EnsemblFungiiYGL087C; YGL087C; YGL087C.
GeneIDi852793.
KEGGisce:YGL087C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U66724 Genomic DNA. Translation: AAC24241.1.
Z72609 Genomic DNA. Translation: CAA96792.1.
BK006941 Genomic DNA. Translation: DAA08018.1.
PIRiS64094.
RefSeqiNP_011428.1. NM_001180952.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JATX-ray1.60B1-137[»]
2GMIX-ray2.50B1-137[»]
ProteinModelPortaliP53152.
SMRiP53152. Positions 3-137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi33163. 131 interactions.
DIPiDIP-5829N.
IntActiP53152. 6 interactions.
MINTiMINT-580773.

PTM databases

iPTMnetiP53152.

Proteomic databases

MaxQBiP53152.
PeptideAtlasiP53152.
PRIDEiP53152.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYGL087C; YGL087C; YGL087C.
GeneIDi852793.
KEGGisce:YGL087C.

Organism-specific databases

EuPathDBiFungiDB:YGL087C.
SGDiS000003055. MMS2.

Phylogenomic databases

GeneTreeiENSGT00740000115534.
HOGENOMiHOG000036561.
InParanoidiP53152.
KOiK10704.
OMAiLANWQRQ.
OrthoDBiEOG77WWRD.

Enzyme and pathway databases

BioCyciYEAST:G3O-30588-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP53152.
PROiP53152.

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. "MMS2, encoding a ubiquitin-conjugating-enzyme-like protein, is a member of the yeast error-free postreplication repair pathway."
    Broomfield S., Chow B.L., Xiao W.
    Proc. Natl. Acad. Sci. U.S.A. 95:5678-5683(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
  2. "Sequence analysis of 203 kilobases from Saccharomyces cerevisiae chromosome VII."
    Rieger M., Brueckner M., Schaefer M., Mueller-Auer S.
    Yeast 13:1077-1090(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII."
    Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E.
    , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K.
    Nature 387:81-84(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  4. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  5. "The products of the yeast MMS2 and two human homologs (hMMS2 and CROC-1) define a structurally and functionally conserved Ubc-like protein family."
    Xiao W., Lin S.L., Broomfield S., Chow B.L., Wei Y.-F.
    Nucleic Acids Res. 26:3908-3914(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  6. "Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair."
    Hofmann R.M., Pickart C.M.
    Cell 96:645-653(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  8. "A multidimensional chromatography technology for in-depth phosphoproteome analysis."
    Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
    Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-71, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer."
    VanDemark A.P., Hofmann R.M., Tsui C., Pickart C.M., Wolberger C.
    Cell 105:711-720(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH UBC13, MUTAGENESIS OF PHE-8.

Entry informationi

Entry nameiMMS2_YEAST
AccessioniPrimary (citable) accession number: P53152
Secondary accession number(s): D6VU57
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2760 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome VII
    Yeast (Saccharomyces cerevisiae) chromosome VII: entries and gene names

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.