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HUMAN:SUMO2

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) SUMO2 (ECO:0000312 with HGNC:HGNC:11125)
Protein Name(s) Small ubiquitin-related modifier 2 (ECO:0000305)

SUMO-2 (ECO:0000305) HSMT3 (ECO:0000303 with PMID:8630065[1]) SMT3 homolog 2 (ECO:0000312 with HGNC:HGNC:11125) SUMO-3 (ECO:0000303 with PMID:10692421[2]) Sentrin-2 (ECO:0000303 with PMID:9556629[3]) Ubiquitin-like protein SMT3B (ECO:0000305) Smt3B (ECO:0000303 with PMID:10692421[2])

External Links
UniProt P61956
EMBL L76416
X99585
AK311837
AC022211
CH471099
BC008450
BC016775
BC022340
BC062713
BC068465
BC070159
BC071645
BC071646
BC107853
BF978876
CCDS CCDS45773.1
CCDS45774.1
PIR JC4760
RefSeq NP_001005849.1
NP_008868.3
UniGene Hs.380973
Hs.546298
PDB 1WM2
1WM3
1WZ0
1Z5Q
2AWT
2CKH
2D07
2IO0
2IO3
2IYD
2N1W
2N9E
2RPQ
3UIN
3UIO
3ZO5
4BKG
4NPN
5D2M
5ELU
5EQL
5GHB
5GHC
PDBsum 1WM2
1WM3
1WZ0
1Z5Q
2AWT
2CKH
2D07
2IO0
2IO3
2IYD
2N1W
2N9E
2RPQ
3UIN
3UIO
3ZO5
4BKG
4NPN
5D2M
5ELU
5EQL
5GHB
5GHC
ProteinModelPortal P61956
SMR P61956
BioGrid 112497
DIP DIP-29253N
ELM P61956
IntAct P61956
MINT MINT-1373938
STRING 9606.ENSP00000405965
ChEMBL CHEMBL2146301
iPTMnet P61956
PhosphoSitePlus P61956
BioMuta SUMO2
DMDM 378405233
EPD P61956
MaxQB P61956
PaxDb P61956
PeptideAtlas P61956
PRIDE P61956
TopDownProteomics P61956-1
P61956-2
DNASU 6613
Ensembl ENST00000314523
ENST00000420826
GeneID 6613
KEGG hsa:6613
UCSC uc002jne.4
CTD 6613
DisGeNET 6613
EuPathDB HostDB:ENSG00000188612.11
GeneCards SUMO2
H-InvDB HIX0056267
HGNC HGNC:11125
HPA CAB037314
HPA042123
HPA048064
MIM 603042
neXtProt NX_P61956
OpenTargets ENSG00000188612
PharmGKB PA134914683
eggNOG KOG1769
COG5227
GeneTree ENSGT00390000018808
HOVERGEN HBG053025
InParanoid P61956
KO K12160
OMA NDTIDVM
OrthoDB EOG091G10ZQ
PhylomeDB P61956
TreeFam TF315116
Reactome [www.reactome.org/content/detail/R-HSA-3065676 R-HSA-3065676]
[www.reactome.org/content/detail/R-HSA-3065678 R-HSA-3065678]
[www.reactome.org/content/detail/R-HSA-3065679 R-HSA-3065679]
[www.reactome.org/content/detail/R-HSA-3108214 R-HSA-3108214]
[www.reactome.org/content/detail/R-HSA-3232118 R-HSA-3232118]
[www.reactome.org/content/detail/R-HSA-4551638 R-HSA-4551638]
[www.reactome.org/content/detail/R-HSA-4570464 R-HSA-4570464]
[www.reactome.org/content/detail/R-HSA-4615885 R-HSA-4615885]
[www.reactome.org/content/detail/R-HSA-5693607 R-HSA-5693607]
[www.reactome.org/content/detail/R-HSA-5696395 R-HSA-5696395]
EvolutionaryTrace P61956
GeneWiki SUMO2
GenomeRNAi 6613
PMAP-CutDB P61956
PRO PR:P61956
Proteomes UP000005640
Bgee ENSG00000188612
CleanEx HS_SUMO2
ExpressionAtlas P61956
Genevisible P61956
GO GO:0005654
GO:0005634
GO:0016605
GO:0031386
GO:0003723
GO:0019789
GO:0001222
GO:0031625
GO:0070911
GO:0032436
GO:0045944
GO:0016925
CDD cd01763
InterPro IPR022617
IPR033950
IPR029071
IPR000626
Pfam PF11976
SMART SM00213
SUPFAM SSF54236
PROSITE PS50053

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status

enables

GO:0001222

transcription corepressor binding

PMID:17081986[4]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:Q9UER7

F

Seeded From UniProt

complete

involved_in

GO:0016925

protein sumoylation

PMID:17081986[4]

ECO:0000314

direct assay evidence used in manual assertion

P

has_direct_input:(UniProtKB:Q9UER7)

Seeded From UniProt

complete

involved_in

GO:0016925

protein sumoylation

PMID:24105744[5]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21965678[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0016925

protein sumoylation

PMID:21965678[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0003723

RNA binding

PMID:22681889[7]

ECO:0007005

high throughput direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0032436

positive regulation of proteasomal ubiquitin-dependent protein catabolic process

PMID:18408734[8]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0031625

ubiquitin protein ligase binding

PMID:18408734[8]

ECO:0000353

physical interaction evidence used in manual assertion

UniProtKB:O88846

F

Seeded From UniProt

complete

involved_in

GO:0016925

protein sumoylation

PMID:17696781[9]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0016605

PML body

PMID:22406621[10]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0044389

ubiquitin-like protein ligase binding

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000059492
UniProtKB:P61956
UniProtKB:P63165

F

Seeded From UniProt

complete

enables

GO:0031386

protein tag

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000059492
PomBase:SPBC365.06
SGD:S000002918
TAIR:locus:2116332
TAIR:locus:2161695
TAIR:locus:505006284
UniProtKB:Q59W54
UniProtKB:Q9FLP6

F

Seeded From UniProt

complete

involved_in

GO:0016925

protein sumoylation

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0264922
MGI:MGI:1197010
MGI:MGI:1336201
MGI:MGI:2158813
PANTHER:PTN000059492
PomBase:SPBC365.06
RGD:621761
SGD:S000002918
TAIR:locus:2116332
TAIR:locus:2161695
TAIR:locus:505006284
UniProtKB:P55854
UniProtKB:P61956
UniProtKB:P63165
UniProtKB:Q59W54
UniProtKB:Q9FLP6
WB:WBGene00004888
dictyBase:DDB_G0286189

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[11]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0264922
MGI:MGI:1197010
MGI:MGI:1336201
PANTHER:PTN000059492
PomBase:SPBC365.06
RGD:621761
SGD:S000002918
TAIR:locus:2116332
UniProtKB:P55854
UniProtKB:P61956
UniProtKB:Q5BE39
UniProtKB:Q8I444
UniProtKB:Q9FLP6
dictyBase:DDB_G0286189

C

Seeded From UniProt

complete

involved_in

GO:0045944

positive regulation of transcription by RNA polymerase II

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P61957
ensembl:ENSMUSP00000115044

P

Seeded From UniProt

complete

enables

GO:0019789

SUMO transferase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P61957
ensembl:ENSMUSP00000115044

F

Seeded From UniProt

complete

involved_in

GO:0016925

protein sumoylation

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:P61957
ensembl:ENSMUSP00000115044

P

Seeded From UniProt

complete

involved_in

GO:0016925

protein sumoylation

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR033950

P

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

Reactome:R-HSA-6804485
Reactome:R-HSA-6804468
Reactome:R-HSA-6790487
Reactome:R-HSA-6790454
Reactome:R-HSA-5684071
Reactome:R-HSA-5684052
Reactome:R-HSA-4720446
Reactome:R-HSA-4720432
Reactome:R-HSA-4719413
Reactome:R-HSA-4655355
Reactome:R-HSA-4641350
Reactome:R-HSA-4615987
Reactome:R-HSA-4615839
Reactome:R-HSA-4570553
Reactome:R-HSA-4570499
Reactome:R-HSA-4570489
Reactome:R-HSA-4570463
Reactome:R-HSA-4568914
Reactome:R-HSA-4551768
Reactome:R-HSA-4551738
Reactome:R-HSA-4551679
Reactome:R-HSA-4551616
Reactome:R-HSA-4546387
Reactome:R-HSA-4546385
Reactome:R-HSA-4341072
Reactome:R-HSA-4086059
Reactome:R-HSA-4085372
Reactome:R-HSA-3900194
Reactome:R-HSA-3465545
Reactome:R-HSA-3108203
Reactome:R-HSA-3000411
Reactome:R-HSA-3000348
Reactome:R-HSA-2997706
Reactome:R-HSA-2997616
Reactome:R-HSA-2990842

ECO:0000304

author statement supported by traceable reference used in manual assertion



































C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

part_of

GO:0016605

PML body

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0465

C

Seeded From UniProt

complete

edit table

Notes

References

See Help:References for how to manage references in GONUTS.

  1. ↑ Mannen, H et al. (1996) Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene. Biochem. Biophys. Res. Commun. 222 178-80 PubMed GONUTS page
  2. ↑ 2.0 2.1 Saitoh, H & Hinchey, J (2000) Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J. Biol. Chem. 275 6252-8 PubMed GONUTS page
  3. ↑ Kamitani, T et al. (1998) Characterization of a second member of the sentrin family of ubiquitin-like proteins. J. Biol. Chem. 273 11349-53 PubMed GONUTS page
  4. ↑ 4.0 4.1 Lin, DY et al. (2006) Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors. Mol. Cell 24 341-54 PubMed GONUTS page
  5. ↑ Richard, P et al. (2013) A SUMO-dependent interaction between Senataxin and the exosome, disrupted in the neurodegenerative disease AOA2, targets the exosome to sites of transcription-induced DNA damage. Genes Dev. 27 2227-32 PubMed GONUTS page
  6. ↑ 6.0 6.1 Cong, L et al. (2011) SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function. J. Biol. Chem. 286 43793-808 PubMed GONUTS page
  7. ↑ Baltz, AG et al. (2012) The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Mol. Cell 46 674-90 PubMed GONUTS page
  8. ↑ 8.0 8.1 Tatham, MH et al. (2008) RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat. Cell Biol. 10 538-46 PubMed GONUTS page
  9. ↑ Jambunathan, S & Fontes, JD (2007) Sumoylation of the zinc finger protein ZXDC enhances the function of its transcriptional activation domain. Biol. Chem. 388 965-72 PubMed GONUTS page
  10. ↑ Rabellino, A et al. (2012) The SUMO E3-ligase PIAS1 regulates the tumor suppressor PML and its oncogenic counterpart PML-RARA. Cancer Res. 72 2275-84 PubMed GONUTS page
  11. ↑ 11.0 11.1 11.2 11.3 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
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