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Protein

Small ubiquitin-related modifier 2

Gene

SUMO2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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, CBX4 or ZNF451 (PubMed:26524494). 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 (PubMed:18408734, PubMed:18538659, PubMed:21965678, PubMed:9556629). Plays a role in the regulation of sumoylation status of SETX (PubMed:24105744).6 Publications

GO - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • protein tag Source: GO_Central
  • SUMO transferase activity Source: Ensembl
  • ubiquitin protein ligase binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

BioCyciZFISH:G66-32943-MONOMER.
ReactomeiR-HSA-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-HSA-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-HSA-3065679. SUMO is proteolytically processed.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3232118. SUMOylation of transcription factors.
R-HSA-4551638. SUMOylation of chromatin organization proteins.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-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):
HSMT31 Publication
SMT3 homolog 2Imported
SUMO-31 Publication
Sentrin-21 Publication
Ubiquitin-like protein SMT3BCurated
Short name:
Smt3B1 Publication
Gene namesi
Name:SUMO2Imported
Synonyms:SMT3B1 PublicationImported, SMT3H2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:11125. SUMO2.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • PML body Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi11K → R: Abolishes the formation of poly(SUMO) chains. 1 Publication1
Mutagenesisi33K → E: Significantly impairs sumoylation of MTA1. 1 Publication1
Mutagenesisi35K → E: Significantly impairs sumoylation of MTA1. 1 Publication1
Mutagenesisi42K → E: Significantly impairs sumoylation of MTA1. 1 Publication1

Organism-specific databases

DisGeNETi6613.
OpenTargetsiENSG00000188612.
PharmGKBiPA134914683.

Chemistry databases

ChEMBLiCHEMBL2146301.

Polymorphism and mutation databases

BioMutaiSUMO2.
DMDMi378405233.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000359491 – 93Small ubiquitin-related modifier 2Add BLAST93
PropeptideiPRO_000003595094 – 952

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki1Peptide (Met-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki5Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Cross-linki7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei11N6-acetyllysine; alternateCombined sources1
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateCombined sources
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki93Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

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 RNF4.2 Publications
Cleavage of precursor form by SENP1 or SENP2 is necessary for function.
Monoubiquitinated N-terminally by UBE2W, which primes it for RNF4-dependent polyubiquitination by the UBE2V1-UBE2N heterodimer.2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP61956.
MaxQBiP61956.
PaxDbiP61956.
PeptideAtlasiP61956.
PRIDEiP61956.
TopDownProteomicsiP61956-1. [P61956-1]
P61956-2. [P61956-2]

PTM databases

iPTMnetiP61956.
PhosphoSitePlusiP61956.

Miscellaneous databases

PMAP-CutDBP61956.

Expressioni

Tissue specificityi

Broadly expressed.1 Publication

Gene expression databases

BgeeiENSG00000188612.
CleanExiHS_SUMO2.
ExpressionAtlasiP61956. baseline and differential.
GenevisibleiP61956. HS.

Organism-specific databases

HPAiCAB037314.
HPA042123.
HPA048064.

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. Interacts with Epstein-barr virus BGLF4.Curated8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHD3Q128733EBI-473220,EBI-523590
HOMEZQ8IX15-33EBI-473220,EBI-10172004
MYBP102423EBI-473220,EBI-298355
PELP1Q8IZL84EBI-473220,EBI-716449
PIAS4Q8N2W93EBI-473220,EBI-473160
Rnf4O888462EBI-473220,EBI-7258907From a different organism.
SENP2Q9HC623EBI-473220,EBI-714881
TANKQ928443EBI-473220,EBI-356349
UBE2IP632796EBI-473220,EBI-80168
USP25Q9UHP35EBI-473220,EBI-2513462
USPL1Q5W0Q72EBI-473220,EBI-2513899
uspl1Q6DRC52EBI-473220,EBI-8018150From a different organism.

GO - Molecular functioni

  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi112497. 215 interactors.
DIPiDIP-29253N.
IntActiP61956. 66 interactors.
MINTiMINT-1373938.
STRINGi9606.ENSP00000405965.

Structurei

Secondary structure

195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi11 – 13Combined sources3
Turni14 – 16Combined sources3
Beta strandi18 – 23Combined sources6
Turni25 – 27Combined sources3
Beta strandi29 – 34Combined sources6
Helixi41 – 51Combined sources11
Turni55 – 57Combined sources3
Beta strandi59 – 62Combined sources4
Beta strandi65 – 67Combined sources3
Turni73 – 77Combined sources5
Beta strandi82 – 87Combined sources6
Beta strandi90 – 93Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WM2X-ray1.60A12-89[»]
1WM3X-ray1.20A17-88[»]
1WZ0NMR-A1-91[»]
1Z5Qmodel-B15-93[»]
2AWTNMR-A1-95[»]
2CKHX-ray3.20B15-93[»]
2D07X-ray2.10B1-93[»]
2IO0X-ray2.30B15-95[»]
2IO3X-ray3.20B15-93[»]
2IYDX-ray3.20B15-95[»]
2N1WNMR-A1-93[»]
2N9ENMR-B1-95[»]
2RPQNMR-A1-93[»]
3UINX-ray2.60B14-93[»]
3UIOX-ray2.60B14-93[»]
3ZO5X-ray2.15B16-95[»]
4BKGX-ray2.11A12-93[»]
4NPNX-ray1.63A12-93[»]
5D2MX-ray2.40B/E15-93[»]
ProteinModelPortaliP61956.
SMRiP61956.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP61956.

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
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOVERGENiHBG053025.
InParanoidiP61956.
KOiK12160.
OMAiLMQAYCD.
OrthoDBiEOG091G10ZQ.
PhylomeDBiP61956.
TreeFamiTF315116.

Family and domain databases

CDDicd01763. Sumo. 1 hit.
InterProiIPR022617. Rad60/SUMO-like_dom.
IPR033950. Sumo.
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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P61956-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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:February 22, 2012 - v3
Checksum:iF8F0426849BEF08B
GO
Isoform 2 (identifier: P61956-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     51-74: Missing.

Show »
Length:71
Mass (Da):8,111
Checksum:i96014B2763D7E899
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04750816D → N.1 PublicationCorresponds to variant rs17850328dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04235151 – 74Missing in isoform 2. 1 PublicationAdd BLAST24

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76416 mRNA. Translation: AAD45399.1.
X99585 mRNA. Translation: CAA67897.1.
AK311837 mRNA. Translation: BAG34779.1.
AC022211 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89249.1.
BC008450 mRNA. Translation: AAH08450.1.
BC016775 mRNA. Translation: AAH16775.1.
BC022340 mRNA. Translation: AAH22340.1.
BC062713 mRNA. Translation: AAH62713.1.
BC068465 mRNA. Translation: AAH68465.1.
BC070159 mRNA. Translation: AAH70159.1.
BC071645 mRNA. Translation: AAH71645.1.
BC071646 mRNA. Translation: AAH71646.1.
BC107853 mRNA. Translation: AAI07854.1.
BF978876 mRNA. No translation available.
CCDSiCCDS45773.1. [P61956-2]
CCDS45774.1. [P61956-1]
PIRiJC4760.
RefSeqiNP_001005849.1. NM_001005849.1. [P61956-2]
NP_008868.3. NM_006937.3. [P61956-1]
UniGeneiHs.380973.
Hs.546298.

Genome annotation databases

EnsembliENST00000314523; ENSP00000400886; ENSG00000188612. [P61956-2]
ENST00000420826; ENSP00000405965; ENSG00000188612. [P61956-1]
GeneIDi6613.
KEGGihsa:6613.
UCSCiuc002jne.4. human. [P61956-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

SUMO protein entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76416 mRNA. Translation: AAD45399.1.
X99585 mRNA. Translation: CAA67897.1.
AK311837 mRNA. Translation: BAG34779.1.
AC022211 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89249.1.
BC008450 mRNA. Translation: AAH08450.1.
BC016775 mRNA. Translation: AAH16775.1.
BC022340 mRNA. Translation: AAH22340.1.
BC062713 mRNA. Translation: AAH62713.1.
BC068465 mRNA. Translation: AAH68465.1.
BC070159 mRNA. Translation: AAH70159.1.
BC071645 mRNA. Translation: AAH71645.1.
BC071646 mRNA. Translation: AAH71646.1.
BC107853 mRNA. Translation: AAI07854.1.
BF978876 mRNA. No translation available.
CCDSiCCDS45773.1. [P61956-2]
CCDS45774.1. [P61956-1]
PIRiJC4760.
RefSeqiNP_001005849.1. NM_001005849.1. [P61956-2]
NP_008868.3. NM_006937.3. [P61956-1]
UniGeneiHs.380973.
Hs.546298.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WM2X-ray1.60A12-89[»]
1WM3X-ray1.20A17-88[»]
1WZ0NMR-A1-91[»]
1Z5Qmodel-B15-93[»]
2AWTNMR-A1-95[»]
2CKHX-ray3.20B15-93[»]
2D07X-ray2.10B1-93[»]
2IO0X-ray2.30B15-95[»]
2IO3X-ray3.20B15-93[»]
2IYDX-ray3.20B15-95[»]
2N1WNMR-A1-93[»]
2N9ENMR-B1-95[»]
2RPQNMR-A1-93[»]
3UINX-ray2.60B14-93[»]
3UIOX-ray2.60B14-93[»]
3ZO5X-ray2.15B16-95[»]
4BKGX-ray2.11A12-93[»]
4NPNX-ray1.63A12-93[»]
5D2MX-ray2.40B/E15-93[»]
ProteinModelPortaliP61956.
SMRiP61956.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112497. 215 interactors.
DIPiDIP-29253N.
IntActiP61956. 66 interactors.
MINTiMINT-1373938.
STRINGi9606.ENSP00000405965.

Chemistry databases

ChEMBLiCHEMBL2146301.

PTM databases

iPTMnetiP61956.
PhosphoSitePlusiP61956.

Polymorphism and mutation databases

BioMutaiSUMO2.
DMDMi378405233.

Proteomic databases

EPDiP61956.
MaxQBiP61956.
PaxDbiP61956.
PeptideAtlasiP61956.
PRIDEiP61956.
TopDownProteomicsiP61956-1. [P61956-1]
P61956-2. [P61956-2]

Protocols and materials databases

DNASUi6613.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000314523; ENSP00000400886; ENSG00000188612. [P61956-2]
ENST00000420826; ENSP00000405965; ENSG00000188612. [P61956-1]
GeneIDi6613.
KEGGihsa:6613.
UCSCiuc002jne.4. human. [P61956-1]

Organism-specific databases

CTDi6613.
DisGeNETi6613.
GeneCardsiSUMO2.
H-InvDBHIX0056267.
HGNCiHGNC:11125. SUMO2.
HPAiCAB037314.
HPA042123.
HPA048064.
MIMi603042. gene.
neXtProtiNX_P61956.
OpenTargetsiENSG00000188612.
PharmGKBiPA134914683.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1769. Eukaryota.
COG5227. LUCA.
GeneTreeiENSGT00390000018808.
HOVERGENiHBG053025.
InParanoidiP61956.
KOiK12160.
OMAiLMQAYCD.
OrthoDBiEOG091G10ZQ.
PhylomeDBiP61956.
TreeFamiTF315116.

Enzyme and pathway databases

BioCyciZFISH:G66-32943-MONOMER.
ReactomeiR-HSA-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-HSA-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-HSA-3065679. SUMO is proteolytically processed.
R-HSA-3108214. SUMOylation of DNA damage response and repair proteins.
R-HSA-3232118. SUMOylation of transcription factors.
R-HSA-4551638. SUMOylation of chromatin organization proteins.
R-HSA-4570464. SUMOylation of RNA binding proteins.
R-HSA-4615885. SUMOylation of DNA replication proteins.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5696395. Formation of Incision Complex in GG-NER.

Miscellaneous databases

EvolutionaryTraceiP61956.
GeneWikiiSUMO2.
GenomeRNAii6613.
PMAP-CutDBP61956.
PROiP61956.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000188612.
CleanExiHS_SUMO2.
ExpressionAtlasiP61956. baseline and differential.
GenevisibleiP61956. HS.

Family and domain databases

CDDicd01763. Sumo. 1 hit.
InterProiIPR022617. Rad60/SUMO-like_dom.
IPR033950. Sumo.
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_HUMAN
AccessioniPrimary (citable) accession number: P61956
Secondary accession number(s): B2R4I2
, P55855, Q32Q42, Q6IPZ6, Q96HK1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: February 22, 2012
Last modified: November 30, 2016
This is version 148 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.