NSE2_HUMAN - dbPTM
NSE2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NSE2_HUMAN
UniProt AC Q96MF7
Protein Name E3 SUMO-protein ligase NSE2
Gene Name NSMCE2
Organism Homo sapiens (Human).
Sequence Length 247
Subcellular Localization Nucleus . Chromosome, telomere . Nucleus, PML body . Localizes to PML nuclear bodies in ALT cell lines.
Protein Description E3 SUMO-protein ligase component of the SMC5-SMC6 complex, a complex involved in DNA double-strand break repair by homologous recombination. Is not be required for the stability of the complex. The complex may promote sister chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. 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). Acts as an E3 ligase mediating SUMO attachment to various proteins such as SMC6L1 and TRAX, the shelterin complex subunits TERF1, TERF2, TINF2 and TERF2IP, and maybe the cohesin components RAD21 and STAG2. Required for recruitment of telomeres to PML nuclear bodies. 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. Required for sister chromatid cohesion during prometaphase and mitotic progression..
Protein Sequence MPGRSSSNSGSTGFISFSGVESALSSLKNFQACINSGMDTASSVALDLVESQTEVSSEYSMDKAMVEFATLDRQLNHYVKAVQSTINHVKEERPEKIPDLKLLVEKKFLALQSKNSDADFQNNEKFVQFKQQLKELKKQCGLQADREADGTEGVDEDIIVTQSQTNFTCPITKEEMKKPVKNKVCGHTYEEDAIVRMIESRQKRKKKAYCPQIGCSHTDIRKSDLIQDEALRRAIENHNKKRHRHSE
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
1Acetylation-------MPGRSSSN
-------CCCCCCCC		7.7720068231
5Phosphorylation---MPGRSSSNSGST
---CCCCCCCCCCCC		43.9924732914
6Phosphorylation--MPGRSSSNSGSTG
--CCCCCCCCCCCCC		31.9824732914
7Phosphorylation-MPGRSSSNSGSTGF
-CCCCCCCCCCCCCC		35.9428387310
9PhosphorylationPGRSSSNSGSTGFIS
CCCCCCCCCCCCCEE		35.7524732914
11PhosphorylationRSSSNSGSTGFISFS
CCCCCCCCCCCEEEC		25.7724732914
12PhosphorylationSSSNSGSTGFISFSG
CCCCCCCCCCEEECC		39.3728450419
16PhosphorylationSGSTGFISFSGVESA
CCCCCCEEECCHHHH		15.8824732914
18PhosphorylationSTGFISFSGVESALS
CCCCEEECCHHHHHH		34.8328634120
22PhosphorylationISFSGVESALSSLKN
EEECCHHHHHHHHHH		31.9120068231
25PhosphorylationSGVESALSSLKNFQA
CCHHHHHHHHHHHHH		33.0824719451
26PhosphorylationGVESALSSLKNFQAC
CHHHHHHHHHHHHHH		44.1820068231
80UbiquitinationRQLNHYVKAVQSTIN
HHHHHHHHHHHHHHH		35.3621890473
90SumoylationQSTINHVKEERPEKI
HHHHHHHHHHCCCCC		46.43-
90UbiquitinationQSTINHVKEERPEKI
HHHHHHHHHHCCCCC		46.43-
90SumoylationQSTINHVKEERPEKI
HHHHHHHHHHCCCCC		46.4328112733
96UbiquitinationVKEERPEKIPDLKLL
HHHHCCCCCCCHHHH		63.32-
101SumoylationPEKIPDLKLLVEKKF
CCCCCCHHHHHHHHH		47.34-
101UbiquitinationPEKIPDLKLLVEKKF
CCCCCCHHHHHHHHH		47.34-
101SumoylationPEKIPDLKLLVEKKF
CCCCCCHHHHHHHHH		47.34-
107AcetylationLKLLVEKKFLALQSK
HHHHHHHHHHHHHCC		31.9125953088
107MalonylationLKLLVEKKFLALQSK
HHHHHHHHHHHHHCC		31.9126320211
107UbiquitinationLKLLVEKKFLALQSK
HHHHHHHHHHHHHCC		31.91-
107SumoylationLKLLVEKKFLALQSK
HHHHHHHHHHHHHCC		31.9128112733
107SumoylationLKLLVEKKFLALQSK
HHHHHHHHHHHHHCC		31.91-
113PhosphorylationKKFLALQSKNSDADF
HHHHHHHCCCCCCCC		34.3521712546
114UbiquitinationKFLALQSKNSDADFQ
HHHHHHCCCCCCCCC		47.7321890473
116PhosphorylationLALQSKNSDADFQNN
HHHHCCCCCCCCCCH		37.6025159151
125SumoylationADFQNNEKFVQFKQQ
CCCCCHHHHHHHHHH		53.62-
125AcetylationADFQNNEKFVQFKQQ
CCCCCHHHHHHHHHH		53.6223954790
125UbiquitinationADFQNNEKFVQFKQQ
CCCCCHHHHHHHHHH		53.6221890473
125SumoylationADFQNNEKFVQFKQQ
CCCCCHHHHHHHHHH		53.6228112733
130UbiquitinationNEKFVQFKQQLKELK
HHHHHHHHHHHHHHH		21.7521890473
130SumoylationNEKFVQFKQQLKELK
HHHHHHHHHHHHHHH		21.75-
130SumoylationNEKFVQFKQQLKELK
HHHHHHHHHHHHHHH		21.7528112733
134UbiquitinationVQFKQQLKELKKQCG
HHHHHHHHHHHHHHC		57.57-
183UbiquitinationMKKPVKNKVCGHTYE
HCCCCCCCCCCCCCC		32.93-
207UbiquitinationSRQKRKKKAYCPQIG
HHHHHCCHHCCCCCC		47.85-
209PhosphorylationQKRKKKAYCPQIGCS
HHHCCHHCCCCCCCC		17.3417924679
216PhosphorylationYCPQIGCSHTDIRKS
CCCCCCCCCCCCCHH		24.9817924679
218PhosphorylationPQIGCSHTDIRKSDL
CCCCCCCCCCCHHHH		19.4828555341
222SumoylationCSHTDIRKSDLIQDE
CCCCCCCHHHHCCHH		48.97-
222SumoylationCSHTDIRKSDLIQDE
CCCCCCCHHHHCCHH		48.97-
222UbiquitinationCSHTDIRKSDLIQDE
CCCCCCCHHHHCCHH		48.97-
223PhosphorylationSHTDIRKSDLIQDEA
CCCCCCHHHHCCHHH		28.0030266825
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of NSE2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NSE2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of NSE2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD21_HUMANRAD21physical
22751501
STAG2_HUMANSTAG2physical
22751501
SMC5_HUMANSMC5physical
22751501
SMC6_HUMANSMC6physical
22751501
SMC1A_HUMANSMC1Aphysical
22751501
SMC3_HUMANSMC3physical
22751501
PDS5A_HUMANPDS5Aphysical
22751501
PDS5B_HUMANPDS5Bphysical
22751501
WAPL_HUMANWAPALphysical
22751501
ETV1_HUMANETV1physical
16055714
TSNAX_HUMANTSNAXphysical
16055714
UBP28_HUMANUSP28physical
25359778
NSE3_HUMANNDNL2physical
26344197
NSE1_HUMANNSMCE1physical
26344197
SMC5_HUMANSMC5physical
26344197
SMC6_HUMANSMC6physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NSE2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-209 AND SER-216, ANDMASS SPECTROMETRY.

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