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Protein

E3 SUMO-protein ligase MMS21

Gene

MMS21

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts as an E3 ligase mediating SUMO/Smt3 attachment to SMC5 and YKU70. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks.1 Publication

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 24678SP-RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • ligase activity Source: UniProtKB-KW
  • protein serine/threonine kinase inhibitor activity Source: SGD
  • SUMO transferase activity Source: SGD
  • zinc ion binding Source: InterPro

GO - Biological processi

  • DNA repair Source: SGD
  • double-strand break repair via homologous recombination Source: InterPro
  • negative regulation of protein serine/threonine kinase activity Source: GOC
  • protein sumoylation Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Ubl conjugation pathway

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciYEAST:G3O-30144-MONOMER.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase MMS21 (EC:6.3.2.-)
Alternative name(s):
Methyl methanesulfonate-sensitivity protein 21
Non-structural maintenance of chromosome element 2
Short name:
Non-SMC element 2
Gene namesi
Name:MMS21
Synonyms:NSE2
Ordered Locus Names:YEL019C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome V

Organism-specific databases

EuPathDBiFungiDB:YEL019C.
SGDiS000000745. MMS21.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB-SubCell
  • nuclear envelope Source: SGD
  • Smc5-Smc6 complex Source: SGD
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 267267E3 SUMO-protein ligase MMS21PRO_0000218991Add
BLAST

Proteomic databases

MaxQBiP38632.
PeptideAtlasiP38632.

PTM databases

iPTMnetiP38632.

Interactioni

Subunit structurei

Component of the Smc5-Smc6 complex which consists of KRE29, NSE1, NSE2/MMS21, NSE3, NSE4, NSE5, SMC5 and SMC6.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
KAP114P530672EBI-11017,EBI-9174

Protein-protein interaction databases

BioGridi36711. 51 interactions.
DIPiDIP-4100N.
IntActiP38632. 4 interactions.
MINTiMINT-535631.

Structurei

Secondary structure

1
267
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi16 – 183Combined sources
Helixi19 – 246Combined sources
Helixi31 – 5121Combined sources
Helixi60 – 9940Combined sources
Helixi108 – 1147Combined sources
Beta strandi115 – 1173Combined sources
Helixi122 – 1276Combined sources
Helixi142 – 15514Combined sources
Beta strandi177 – 1793Combined sources
Turni185 – 1873Combined sources
Beta strandi188 – 1903Combined sources
Beta strandi192 – 2009Combined sources
Beta strandi203 – 2053Combined sources
Helixi206 – 2127Combined sources
Helixi223 – 2253Combined sources
Helixi232 – 2343Combined sources
Beta strandi235 – 2373Combined sources
Helixi239 – 25618Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HTKX-ray2.31C1-267[»]
ProteinModelPortaliP38632.
SMRiP38632. Positions 5-258.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP38632.

Family & Domainsi

Sequence similaritiesi

Belongs to the NSE2 family.Curated
Contains 1 SP-RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri169 – 24678SP-RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000000837.
InParanoidiP38632.
OMAiCPITCKP.
OrthoDBiEOG7F255T.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR026846. Nse2(Mms21).
IPR004181. Znf_MIZ.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR21330. PTHR21330. 1 hit.
PfamiPF11789. zf-Nse. 1 hit.
[Graphical view]
PROSITEiPS51044. ZF_SP_RING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P38632-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALNDNPIPK SVPLHPKSGK YFHNLHARDL SNIYQQCYKQ IDETINQLVD
60 70 80 90 100
STSPSTIGIE EQVADITSTY KLLSTYESES NSFDEHIKDL KKNFKQSSDA
110 120 130 140 150
CPQIDLSTWD KYRTGELTAP KLSELYLNMP TPEPATMVNN TDTLKILKVL
160 170 180 190 200
PYIWNDPTCV IPDLQNPADE DDLQIEGGKI ELTCPITCKP YEAPLISRKC
210 220 230 240 250
NHVFDRDGIQ NYLQGYTTRD CPQAACSQVV SMRDFVRDPI MELRCKIAKM
260
KESQEQDKRS SQAIDVL
Length:267
Mass (Da):30,354
Last modified:September 27, 2004 - v2
Checksum:iF200378289B1CEE4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241E → D in AAA20471 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12311 Genomic DNA. Translation: AAA20471.1.
U18530 Genomic DNA. Translation: AAB64496.1.
AY558441 Genomic DNA. Translation: AAS56767.1.
BK006939 Genomic DNA. Translation: DAA07634.1.
PIRiS50440.
RefSeqiNP_010896.3. NM_001178834.3.

Genome annotation databases

EnsemblFungiiYEL019C; YEL019C; YEL019C.
GeneIDi856695.
KEGGisce:YEL019C.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U12311 Genomic DNA. Translation: AAA20471.1.
U18530 Genomic DNA. Translation: AAB64496.1.
AY558441 Genomic DNA. Translation: AAS56767.1.
BK006939 Genomic DNA. Translation: DAA07634.1.
PIRiS50440.
RefSeqiNP_010896.3. NM_001178834.3.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3HTKX-ray2.31C1-267[»]
ProteinModelPortaliP38632.
SMRiP38632. Positions 5-258.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi36711. 51 interactions.
DIPiDIP-4100N.
IntActiP38632. 4 interactions.
MINTiMINT-535631.

PTM databases

iPTMnetiP38632.

Proteomic databases

MaxQBiP38632.
PeptideAtlasiP38632.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiYEL019C; YEL019C; YEL019C.
GeneIDi856695.
KEGGisce:YEL019C.

Organism-specific databases

EuPathDBiFungiDB:YEL019C.
SGDiS000000745. MMS21.

Phylogenomic databases

HOGENOMiHOG000000837.
InParanoidiP38632.
OMAiCPITCKP.
OrthoDBiEOG7F255T.

Enzyme and pathway databases

UniPathwayiUPA00886.
BioCyciYEAST:G3O-30144-MONOMER.

Miscellaneous databases

EvolutionaryTraceiP38632.
PROiP38632.

Family and domain databases

Gene3Di3.30.40.10. 1 hit.
InterProiIPR026846. Nse2(Mms21).
IPR004181. Znf_MIZ.
IPR013083. Znf_RING/FYVE/PHD.
[Graphical view]
PANTHERiPTHR21330. PTHR21330. 1 hit.
PfamiPF11789. zf-Nse. 1 hit.
[Graphical view]
PROSITEiPS51044. ZF_SP_RING. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequence analysis of the MMS21 gene of yeast."
    Williams T.L., Montelone B.A.
    Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: D7.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  3. Cited for: GENOME REANNOTATION.
    Strain: ATCC 204508 / S288c.
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 204508 / S288c.
  5. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  6. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
  7. "A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization."
    Zhao X., Blobel G.
    Proc. Natl. Acad. Sci. U.S.A. 102:4777-4782(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

Entry informationi

Entry nameiNSE2_YEAST
AccessioniPrimary (citable) accession number: P38632
Secondary accession number(s): D3DLN0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: September 27, 2004
Last modified: June 8, 2016
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Miscellaneous

Present with 2800 molecules/cell in log phase SD medium.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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