Overview
| Uniprot ID | Q96MF7 |
|---|
| Protein Name | E3 SUMO-protein ligase NSE2 |
|---|
| Gene Name | NSMCE2 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 183 |
MKKPVKNKVCGHTYE |
Function
E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination (PubMed:16055714, PubMed:16810316). Is not be required for the stability of the complex (PubMed:16055714, PubMed:16810316). The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks (PubMed:16055714, PubMed:16810316). The complex is required for telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines and mediates sumoylation of shelterin complex (telosome) components which is proposed to lead to shelterin complex disassembly in ALT-associated PML bodies (APBs) (PubMed:17589526). Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TSNAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, RAD51AP1, and maybe the cohesin components RAD21 and STAG2 (PubMed:16055714, PubMed:16810316, PubMed:17589526, PubMed:31400850). Required for recruitment of telomeres to PML nuclear bodies (PubMed:17589526). SUMO protein-ligase activity is required for the prevention of DNA damage-induced apoptosis by facilitating DNA repair, and for formation of APBs in ALT cell lines (PubMed:17589526). Required for sister chromatid cohesion during prometaphase and mitotic progression (PubMed:19502785)
Protein Sequence
10
MPGRSSSNSG
20
STGFISFSGV
30
ESALSSLKNF
40
QACINSGMDT
50
ASSVALDLVE
60
SQTEVSSEYS
70
MDKAMVEFAT
80
LDRQLNHYVK
90
AVQSTINHVK
100
EERPEKIPDL
110
KLLVEKKFLA
120
LQSKNSDADF
130
QNNEKFVQFK
140
QQLKELKKQC
150
GLQADREADG
160
TEGVDEDIIV
170
TQSQTNFTCP
180
ITKEEMKKPV
190
KNKVCGHTYE
200
EDAIVRMIES
210
RQKRKKKAYC
220
PQIGCSHTDI
230
RKSDLIQDEA
240
LRRAIENHNK
KRHRHSE
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0000781 |
chromosome, telomeric region |
| Cellular Component |
GO:0016604 |
nuclear body |
| Cellular Component |
GO:0005654 |
nucleoplasm |
| Cellular Component |
GO:0005634 |
nucleus |
| Cellular Component |
GO:0016605 |
PML body |
| Cellular Component |
GO:0030915 |
Smc5-Smc6 complex |
| Molecular Function |
GO:0061665 |
SUMO ligase activity |
| Molecular Function |
GO:0019789 |
SUMO transferase activity |
| Molecular Function |
GO:0008270 |
zinc ion binding |
| Biological Process |
GO:0051301 |
cell division |
| Biological Process |
GO:0090398 |
cellular senescence |
| Biological Process |
GO:0140588 |
chromatin looping |
| Biological Process |
GO:0000724 |
double-strand break repair via homologous recombination |
| Biological Process |
GO:0034184 |
positive regulation of maintenance of mitotic sister chromatid cohesion |
| Biological Process |
GO:0045842 |
positive regulation of mitotic metaphase/anaphase transition |
| Biological Process |
GO:0016925 |
protein sumoylation |
| Biological Process |
GO:0032204 |
regulation of telomere maintenance |
| Biological Process |
GO:0000722 |
telomere maintenance via recombination |
Reference
[1] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.