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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

Complete GO annotation...

Keywords - Biological processi

Ubl 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

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 9393Small ubiquitin-related modifier 2PRO_0000035951Add
BLAST
Propeptidei94 – 952By similarityPRO_0000035952

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki1 – 1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki5 – 5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei11 – 111N6-acetyllysine; alternateCombined sources
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternateBy similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki93 – 93Glycyl 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.
PhosphoSiteiP61957.

Expressioni

Gene expression databases

BgeeiENSMUSG00000020738.
CleanExiMM_SUMO2.
ExpressionAtlasiP61957. baseline.
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 interactions.
STRINGi10090.ENSMUSP00000115044.

Structurei

3D structure databases

ProteinModelPortaliP61957.
SMRiP61957. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 9580Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family. SUMO subfamily.Curated
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

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

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR027218. SUMO_chordates.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

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. Positions 1-95.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi228466. 13 interactions.
STRINGi10090.ENSMUSP00000115044.

PTM databases

iPTMnetiP61957.
PhosphoSiteiP61957.

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.
GenevisibleiP61957. MM.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR027218. SUMO_chordates.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PANTHERiPTHR10562:SF10. PTHR10562:SF10. 1 hit.
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSUMO2_MOUSE
AccessioniPrimary (citable) accession number: P61957
Secondary accession number(s): A2A9X2, P55855, Q542L8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: September 7, 2016
This is version 122 of the entry and version 1 of the sequence. [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.