# Small ubiquitin like modifier 2

> mammalian protein found in Homo sapiens

**Wikidata**: [Q21173586](https://www.wikidata.org/wiki/Q21173586)  
**Source**: https://4ort.xyz/entity/small-ubiquitin-like-modifier-2-q21173586


## References

1. UniProt
2. [InterPro Release 71.0](http://www.ebi.ac.uk/interpro/protein/P61956)
3. Q20641742
4. [SUMOylation and SUMO-interacting Motif (SIM) of Metastasis Tumor Antigen 1 (MTA1) Synergistically Regulate Its Transcriptional Repressor Function](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
5. [A Human Protein-Protein Interaction Network: A Resource for Annotating the Proteome](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
6. [A Directed Protein Interaction Network for Investigating Intracellular Signal Transduction](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
7. [Mammalian SUMO E3-ligases PIAS1 and PIAS4 promote responses to DNA double-strand breaks](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
8. [A functional SUMO-interacting motif in the transactivation domain of c-Myb regulates its myeloid transforming ability](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
9. [A Protein Interaction Network Links GIT1, an Enhancer of Huntingtin Aggregation, to Huntington's Disease](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
10. [SUMO protease SENP1 induces isomerization of the scissile peptide bond](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
11. [The SUMO modification pathway is involved in the BRCA1 response to genotoxic stress](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
12. [The SUMO system controls nucleolar partitioning of a novel mammalian ribosome biogenesis complex](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
13. [A Proteome-Scale Map of the Human Interactome Network](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
14. [Structural basis for SENP2 protease interactions with SUMO precursors and conjugated substrates](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
15. [Inducible SUMO modification of TANK alleviates its repression of TLR7 signalling](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
16. [Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
17. [Toward an understanding of the protein interaction network of the human liver](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
18. [Ubiquitin‐specific protease‐like 1 (USPL1) is a SUMO isopeptidase with essential, non‐catalytic functions](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
19. [Purification and identification of endogenous polySUMO conjugates](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
20. [Role of SUMO-Interacting Motif in Daxx SUMO Modification, Subnuclear Localization, and Repression of Sumoylated Transcription Factors](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
21. [RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
22. [Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
23. [The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts](http://www.ebi.ac.uk/QuickGO/annotations?protein=P61956&geneProductId=UniProtKB:P61956)
24. [GOA](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
25. [The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
26. [The SUMO E3-ligase PIAS1 Regulates the Tumor Suppressor PML and Its Oncogenic Counterpart PML-RARA](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
27. [GOA](http://www.ebi.ac.uk/QuickGO/annotations?protein=P61956&geneProductId=UniProtKB:P61956)
28. [SUMOylation and SUMO-interacting Motif (SIM) of Metastasis Tumor Antigen 1 (MTA1) Synergistically Regulate Its Transcriptional Repressor Function](http://www.ebi.ac.uk/QuickGO/annotations?protein=P61956&geneProductId=UniProtKB:P61956)
29. [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](http://www.ebi.ac.uk/QuickGO/annotations?protein=P61956&geneProductId=UniProtKB:P61956)
30. [Sumoylation of the zinc finger protein ZXDC enhances the function of its transcriptional activation domain](http://www.ebi.ac.uk/QuickGO/annotations?protein=P61956&geneProductId=UniProtKB:P61956)
31. [Role of SUMO-Interacting Motif in Daxx SUMO Modification, Subnuclear Localization, and Repression of Sumoylated Transcription Factors](http://www.ebi.ac.uk/QuickGO/annotations?protein=P61956&geneProductId=UniProtKB:P61956)
32. [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](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
33. [Sumoylation of the zinc finger protein ZXDC enhances the function of its transcriptional activation domain](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:P61956)
34. Ensembl Release 99