CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019456
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 SUMO-protein ligase NSE2 
Protein Synonyms/Alias
 MMS21 homolog; hMMS21; Non-structural maintenance of chromosomes element 2 homolog; Non-SMC element 2 homolog 
Gene Name
 NSMCE2 
Gene Synonyms/Alias
 C8orf36; MMS21 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
80RQLNHYVKAVQSTINubiquitination[1, 2]
101PEKIPDLKLLVEKKFubiquitination[3]
107LKLLVEKKFLALQSKubiquitination[4]
114KFLALQSKNSDADFQubiquitination[3, 4]
125ADFQNNEKFVQFKQQubiquitination[1, 2, 3, 4, 5]
130NEKFVQFKQQLKELKubiquitination[1, 2, 4]
134VQFKQQLKELKKQCGubiquitination[4]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional 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 a 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. 
Sequence Annotation
 ZN_FING 154 236 SP-RING-type.
 MOD_RES 1 1 N-acetylmethionine.  
Keyword
 3D-structure; Acetylation; Cell cycle; Cell division; Chromosome; Complete proteome; DNA damage; DNA recombination; DNA repair; Ligase; Metal-binding; Mitosis; Nucleus; Polymorphism; Reference proteome; Telomere; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 247 AA 
Protein Sequence
MPGRSSSNSG STGFISFSGV ESALSSLKNF QACINSGMDT ASSVALDLVE SQTEVSSEYS 60
MDKAMVEFAT LDRQLNHYVK AVQSTINHVK EERPEKIPDL KLLVEKKFLA LQSKNSDADF 120
QNNEKFVQFK QQLKELKKQC GLQADREADG TEGVDEDIIV TQSQTNFTCP ITKEEMKKPV 180
KNKVCGHTYE EDAIVRMIES RQKRKKKAYC PQIGCSHTDI RKSDLIQDEA LRRAIENHNK 240
KRHRHSE 247 
Gene Ontology
 GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
 GO:0016605; C:PML body; IDA:UniProtKB.
 GO:0030915; C:Smc5-Smc6 complex; IDA:UniProtKB.
 GO:0019789; F:SUMO ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0090398; P:cellular senescence; IMP:UniProtKB.
 GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IMP:UniProtKB.
 GO:0045842; P:positive regulation of mitotic metaphase/anaphase transition; IMP:UniProtKB.
 GO:0016925; P:protein sumoylation; IEA:UniProtKB-UniPathway.
 GO:0000722; P:telomere maintenance via recombination; IMP:UniProtKB. 
Interpro
 IPR026846; Nse2(Mms21).
 IPR027370; zf-RING_LisH.
 IPR004181; Znf_MIZ.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF13445; zf-RING_LisH 
SMART
  
PROSITE
 PS51044; ZF_SP_RING 
PRINTS