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Protein

Small ubiquitin-related modifier 2

Gene

Sumo2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. Plays a role in the regulation of sumoylation status of SETX (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Biological processUbl conjugation pathway

Enzyme and pathway databases

ReactomeiR-MMU-3065679. SUMO is proteolytically processed.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3232118. SUMOylation of transcription factors.
R-MMU-4551638. SUMOylation of chromatin organization proteins.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5696395. Formation of Incision Complex in GG-NER.

Names & Taxonomyi

Protein namesi
Recommended name:
Small ubiquitin-related modifier 2Curated
Short name:
SUMO-2Curated
Alternative name(s):
SMT3 homolog 2Imported
Ubiquitin-like protein SMT3B1 Publication
Short name:
Smt3B1 Publication
Gene namesi
Name:Sumo2Imported
Synonyms:Smt3bImported, Smt3h2Imported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:2158813. Sumo2.

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000359511 – 93Small ubiquitin-related modifier 2Add BLAST93
PropeptideiPRO_000003595294 – 95By similarity2

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei11N6-acetyllysine; alternateCombined sources1
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Post-translational modificationi

Polymeric chains can be formed through Lys-11 cross-linking. Polymeric SUMO2 chains undergo 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 (By similarity).By similarity
Cleavage of precursor form by SENP1 or SENP2 is necessary for function.By similarity
Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP61957.
MaxQBiP61957.
PaxDbiP61957.
PeptideAtlasiP61957.
PRIDEiP61957.
TopDownProteomicsiP61957.

PTM databases

iPTMnetiP61957.
PhosphoSitePlusiP61957.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020738.
CleanExiMM_SUMO2.
ExpressionAtlasiP61957. baseline and differential.
GenevisibleiP61957. MM.

Interactioni

Subunit structurei

Interacts with SAE2 and UBE2I. Interacts with ZNF451. Identified in a complex with ZNF451 and UBE2I/UBC9, where one ZNF451 interacts with one UBE2I/UBC9 and two SUMO2 chains, one bound to the UBE2I/UBC9 active site and the other to another region of the same UBE2I/UBC9 molecule. Covalently attached to a number of proteins. Interacts with PELP1. Interacts with USP25; the interaction sumoylates USP25. Interacts with SIMC1, CASP8AP2, RNF111 AND SOBP (via SIM domains). Interacts with MTA1.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi228466. 13 interactors.
STRINGi10090.ENSMUSP00000115044.

Structurei

3D structure databases

ProteinModelPortaliP61957.
SMRiP61957.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 95Ubiquitin-likePROSITE-ProRule annotationAdd BLAST80

Sequence similaritiesi

Belongs to the ubiquitin family. SUMO subfamily.Curated

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP61957.
KOiK12160.
OMAiLMQAYCD.
OrthoDBiEOG091G10ZQ.
PhylomeDBiP61957.
TreeFamiTF315116.

Family and domain databases

CDDicd01763. Sumo. 1 hit.
InterProiView protein in InterPro
IPR022617. Rad60/SUMO-like_dom.
IPR033950. Sumo.
IPR027218. SUMO_2/3.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
PANTHERiPTHR10562:SF33. PTHR10562:SF33. 1 hit.
PfamiView protein in Pfam
PF11976. Rad60-SLD. 1 hit.
SMARTiView protein in SMART
SM00213. UBQ. 1 hit.
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiView protein in PROSITE
PS50053. UBIQUITIN_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P61957-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADEKPKEGV KTENNDHINL KVAGQDGSVV QFKIKRHTPL SKLMKAYCER
60 70 80 90
QGLSMRQIRF RFDGQPINET DTPAQLEMED EDTIDVFQQQ TGGVY
Length:95
Mass (Da):10,871
Last modified:June 7, 2004 - v1
Checksum:iF8F0426849BEF08B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L79948 mRNA. Translation: AAL40136.1.
AK012619 mRNA. Translation: BAB28360.1.
AK085238 mRNA. Translation: BAC39397.1.
AK132213 mRNA. Translation: BAE21037.1.
AK160404 mRNA. Translation: BAE35772.1.
AK167308 mRNA. Translation: BAE39412.1.
AL645470 Genomic DNA. Translation: CAM23014.1.
BC017522 mRNA. Translation: AAH17522.1.
BC083326 mRNA. Translation: AAH83326.1.
BC095930 mRNA. Translation: AAH95930.1.
CCDSiCCDS36374.1.
RefSeqiNP_579932.1. NM_133354.2.
UniGeneiMm.29923.

Genome annotation databases

EnsembliENSMUST00000153892; ENSMUSP00000115044; ENSMUSG00000020738.
GeneIDi170930.
KEGGimmu:170930.
UCSCiuc007mhw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L79948 mRNA. Translation: AAL40136.1.
AK012619 mRNA. Translation: BAB28360.1.
AK085238 mRNA. Translation: BAC39397.1.
AK132213 mRNA. Translation: BAE21037.1.
AK160404 mRNA. Translation: BAE35772.1.
AK167308 mRNA. Translation: BAE39412.1.
AL645470 Genomic DNA. Translation: CAM23014.1.
BC017522 mRNA. Translation: AAH17522.1.
BC083326 mRNA. Translation: AAH83326.1.
BC095930 mRNA. Translation: AAH95930.1.
CCDSiCCDS36374.1.
RefSeqiNP_579932.1. NM_133354.2.
UniGeneiMm.29923.

3D structure databases

ProteinModelPortaliP61957.
SMRiP61957.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228466. 13 interactors.
STRINGi10090.ENSMUSP00000115044.

PTM databases

iPTMnetiP61957.
PhosphoSitePlusiP61957.

Proteomic databases

EPDiP61957.
MaxQBiP61957.
PaxDbiP61957.
PeptideAtlasiP61957.
PRIDEiP61957.
TopDownProteomicsiP61957.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000153892; ENSMUSP00000115044; ENSMUSG00000020738.
GeneIDi170930.
KEGGimmu:170930.
UCSCiuc007mhw.1. mouse.

Organism-specific databases

CTDi6613.
MGIiMGI:2158813. Sumo2.

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOGENOMiHOG000207495.
HOVERGENiHBG053025.
InParanoidiP61957.
KOiK12160.
OMAiLMQAYCD.
OrthoDBiEOG091G10ZQ.
PhylomeDBiP61957.
TreeFamiTF315116.

Enzyme and pathway databases

ReactomeiR-MMU-3065679. SUMO is proteolytically processed.
R-MMU-3108214. SUMOylation of DNA damage response and repair proteins.
R-MMU-3232118. SUMOylation of transcription factors.
R-MMU-4551638. SUMOylation of chromatin organization proteins.
R-MMU-4570464. SUMOylation of RNA binding proteins.
R-MMU-4615885. SUMOylation of DNA replication proteins.
R-MMU-5693607. Processing of DNA double-strand break ends.
R-MMU-5696395. Formation of Incision Complex in GG-NER.

Miscellaneous databases

PROiP61957.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020738.
CleanExiMM_SUMO2.
ExpressionAtlasiP61957. baseline and differential.
GenevisibleiP61957. MM.

Family and domain databases

CDDicd01763. Sumo. 1 hit.
InterProiView protein in InterPro
IPR022617. Rad60/SUMO-like_dom.
IPR033950. Sumo.
IPR027218. SUMO_2/3.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
PANTHERiPTHR10562:SF33. PTHR10562:SF33. 1 hit.
PfamiView protein in Pfam
PF11976. Rad60-SLD. 1 hit.
SMARTiView protein in SMART
SM00213. UBQ. 1 hit.
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiView protein in PROSITE
PS50053. UBIQUITIN_2. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSUMO2_MOUSE
AccessioniPrimary (citable) accession number: P61957
Secondary accession number(s): A2A9X2, P55855, Q542L8
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: March 15, 2017
This is version 127 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.