NSE3_HUMAN
ID NSE3_HUMAN Reviewed; 304 AA.
AC Q96MG7; Q8IW16; Q8TEI6; Q9H214;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 158.
DE RecName: Full=Non-structural maintenance of chromosomes element 3 homolog;
DE Short=Non-SMC element 3 homolog;
DE AltName: Full=Hepatocellular carcinoma-associated protein 4;
DE AltName: Full=MAGE-G1 antigen;
DE AltName: Full=Melanoma-associated antigen G1;
DE AltName: Full=Necdin-like protein 2;
GN Name=NSMCE3 {ECO:0000312|HGNC:HGNC:7677}; Synonyms=HCA4, MAGEG1, NDNL2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Dong X.-Y., Chen W.-F.;
RT "Identification of genes in the chromosome X that are differentially
RT expressed in hepatocellular carcinoma.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lung, Spleen, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 85-304.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 189-288.
RC TISSUE=Testis;
RA Lucas S., Boon T.;
RT "Identification of new genes of the MAGE family.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP TISSUE SPECIFICITY.
RX PubMed=11782285; DOI=10.1186/1471-2156-2-22;
RA Chibuk T.K., Bischof J.M., Wevrick R.;
RT "A necdin/MAGE-like gene in the chromosome 15 autism susceptibility region:
RT expression, imprinting, and mapping of the human and mouse orthologues.";
RL BMC Genet. 2:22-22(2001).
RN [7]
RP SUBCELLULAR LOCATION, INTERACTION WITH NSMCE1 AND SMC6, AND IDENTIFICATION
RP IN THE SMC5-SMC6 COMPLEX.
RX PubMed=18086888; DOI=10.1128/mcb.00767-07;
RA Taylor E.M., Copsey A.C., Hudson J.J., Vidot S., Lehmann A.R.;
RT "Identification of the proteins, including MAGEG1, that make up the human
RT SMC5-6 protein complex.";
RL Mol. Cell. Biol. 28:1197-1206(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP INTERACTION WITH EID3 AND NSMCE1, AND MUTAGENESIS OF MET-180; ILE-181;
RP LEU-185; PHE-266 AND VAL-270.
RX PubMed=21364888; DOI=10.1371/journal.pone.0017270;
RA Hudson J.J., Bednarova K., Kozakova L., Liao C., Guerineau M., Colnaghi R.,
RA Vidot S., Marek J., Bathula S.R., Lehmann A.R., Palecek J.;
RT "Interactions between the Nse3 and Nse4 components of the SMC5-6 complex
RT identify evolutionarily conserved interactions between MAGE and EID
RT Families.";
RL PLoS ONE 6:E17270-E17270(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57; SER-60 AND SER-64, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 78-294 IN COMPLEX WITH NSMCE1,
RP FUNCTION, INTERACTION WITH NSMCE1; NSMCE4A AND PJA1, AND MUTAGENESIS OF
RP 96-LEU-LEU-97.
RX PubMed=20864041; DOI=10.1016/j.molcel.2010.08.029;
RA Doyle J.M., Gao J., Wang J., Yang M., Potts P.R.;
RT "MAGE-RING protein complexes comprise a family of E3 ubiquitin ligases.";
RL Mol. Cell 39:963-974(2010).
RN [16]
RP VARIANTS LICS LEU-209 AND PHE-264, CHARACTERIZATION OF VARIANTS LICS
RP LEU-209 AND PHE-264, INVOLVEMENT IN LICS, FUNCTION, SUBUNIT, AND
RP INTERACTION WITH NSMCE1 AND NSMCE4.
RX PubMed=27427983; DOI=10.1172/jci82890;
RA van der Crabben S.N., Hennus M.P., McGregor G.A., Ritter D.I.,
RA Nagamani S.C., Wells O.S., Harakalova M., Chinn I.K., Alt A., Vondrova L.,
RA Hochstenbach R., van Montfrans J.M., Terheggen-Lagro S.W., van Lieshout S.,
RA van Roosmalen M.J., Renkens I., Duran K., Nijman I.J., Kloosterman W.P.,
RA Hennekam E., Orange J.S., van Hasselt P.M., Wheeler D.A., Palecek J.J.,
RA Lehmann A.R., Oliver A.W., Pearl L.H., Plon S.E., Murray J.M.,
RA van Haaften G.;
RT "Destabilized SMC5/6 complex leads to chromosome breakage syndrome with
RT severe lung disease.";
RL J. Clin. Invest. 126:2881-2892(2016).
CC -!- FUNCTION: Component of the SMC5-SMC6 complex, a complex involved in
CC repair of DNA double-strand breaks by homologous recombination
CC (PubMed:20864041, PubMed:27427983). The complex may promote sister
CC chromatid homologous recombination by recruiting the SMC1-SMC3 cohesin
CC complex to double-strand breaks. The complex is required for telomere
CC maintenance via recombination in ALT (alternative lengthening of
CC telomeres) cell lines and mediates sumoylation of shelterin complex
CC (telosome) components which is proposed to lead to shelterin complex
CC disassembly in ALT-associated PML bodies (APBs). In vitro enhances
CC ubiquitin ligase activity of NSMCE1. Proposed to act through
CC recruitment and/or stabilization of the Ubl-conjugating enzyme (E2) at
CC the E3:substrate complex (PubMed:20864041). May be a growth suppressor
CC that facilitates the entry of the cell into cell cycle arrest (By
CC similarity). {ECO:0000250|UniProtKB:Q9CPR8,
CC ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:27427983}.
CC -!- SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of
CC SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3. NSMCE1, NSMCE4A
CC or EID3 and NSMCE3 probably form a subcomplex that bridges the head
CC domains of the SMC5:SMC6 heterodimer (PubMed:18086888). Interacts with
CC PJA1 (PubMed:20864041). Interacts with E2F1 (via C-terminus) (By
CC similarity). Interacts with NGFR (via C-terminus) (By similarity).
CC Interacts with NSMCE1 (PubMed:18086888, PubMed:21364888,
CC PubMed:20864041, PubMed:27427983). Interacts with NSMCE4
CC (PubMed:20864041, PubMed:27427983). Interacts with SMC6
CC (PubMed:18086888). Interacts with EID3 (PubMed:21364888).
CC {ECO:0000250|UniProtKB:Q9CPR8, ECO:0000269|PubMed:18086888,
CC ECO:0000269|PubMed:20864041, ECO:0000269|PubMed:21364888,
CC ECO:0000269|PubMed:27427983}.
CC -!- INTERACTION:
CC Q96MG7; Q8N140: EID3; NbExp=8; IntAct=EBI-2557356, EBI-744483;
CC Q96MG7; Q8WV22: NSMCE1; NbExp=20; IntAct=EBI-2557356, EBI-2557372;
CC Q96MG7; Q9NXX6: NSMCE4A; NbExp=4; IntAct=EBI-2557356, EBI-2557393;
CC Q96MG7; Q8NG27: PJA1; NbExp=3; IntAct=EBI-2557356, EBI-714606;
CC Q96MG7; Q96SB8: SMC6; NbExp=5; IntAct=EBI-2557356, EBI-605415;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000269|PubMed:18086888}. Chromosome, telomere
CC {ECO:0000305|PubMed:18086888}.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:11782285}.
CC -!- DISEASE: Lung disease, immunodeficiency, and chromosome breakage
CC syndrome (LICS) [MIM:617241]: An autosomal recessive chromosome
CC breakage syndrome associated with severe, fatal lung disease in early
CC childhood, following viral pneumonia. LICS is characterized by combined
CC T and B-cell immunodeficiency. Some patients may have mild dysmorphic
CC features. {ECO:0000269|PubMed:27427983}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84964.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF490510; AAM08357.1; -; mRNA.
DR EMBL; AK056957; BAB71325.1; -; mRNA.
DR EMBL; BC041166; AAH41166.2; -; mRNA.
DR EMBL; BC053999; AAH53999.1; -; mRNA.
DR EMBL; AK074138; BAB84964.1; ALT_FRAME; mRNA.
DR EMBL; AF320911; AAG38607.1; -; Genomic_DNA.
DR CCDS; CCDS10023.1; -.
DR RefSeq; NP_619649.1; NM_138704.3.
DR PDB; 5HVQ; X-ray; 2.92 A; D=78-294.
DR PDB; 5WY5; X-ray; 2.92 A; B=78-294.
DR PDBsum; 5HVQ; -.
DR PDBsum; 5WY5; -.
DR AlphaFoldDB; Q96MG7; -.
DR SMR; Q96MG7; -.
DR BioGRID; 121094; 34.
DR ComplexPortal; CPX-5992; SMC5-SMC6 SUMO ligase complex, EID3 variant.
DR ComplexPortal; CPX-6086; SMC5-SMC6 SUMO ligase complex, NSE4EA variant.
DR IntAct; Q96MG7; 13.
DR STRING; 9606.ENSP00000330694; -.
DR iPTMnet; Q96MG7; -.
DR PhosphoSitePlus; Q96MG7; -.
DR BioMuta; NSMCE3; -.
DR DMDM; 46396494; -.
DR EPD; Q96MG7; -.
DR jPOST; Q96MG7; -.
DR MassIVE; Q96MG7; -.
DR MaxQB; Q96MG7; -.
DR PaxDb; Q96MG7; -.
DR PeptideAtlas; Q96MG7; -.
DR PRIDE; Q96MG7; -.
DR ProteomicsDB; 77353; -.
DR Antibodypedia; 41882; 53 antibodies from 19 providers.
DR DNASU; 56160; -.
DR Ensembl; ENST00000332303.6; ENSP00000330694.4; ENSG00000185115.6.
DR Ensembl; ENST00000631973.1; ENSP00000487893.1; ENSG00000282130.1.
DR GeneID; 56160; -.
DR KEGG; hsa:56160; -.
DR MANE-Select; ENST00000332303.6; ENSP00000330694.4; NM_138704.4; NP_619649.1.
DR UCSC; uc001zco.4; human.
DR CTD; 56160; -.
DR DisGeNET; 56160; -.
DR GeneCards; NSMCE3; -.
DR HGNC; HGNC:7677; NSMCE3.
DR HPA; ENSG00000185115; Low tissue specificity.
DR MalaCards; NSMCE3; -.
DR MIM; 608243; gene.
DR MIM; 617241; phenotype.
DR neXtProt; NX_Q96MG7; -.
DR OpenTargets; ENSG00000185115; -.
DR PharmGKB; PA31480; -.
DR VEuPathDB; HostDB:ENSG00000185115; -.
DR eggNOG; KOG4562; Eukaryota.
DR GeneTree; ENSGT00940000163627; -.
DR HOGENOM; CLU_039582_2_0_1; -.
DR InParanoid; Q96MG7; -.
DR OMA; YPTKKHL; -.
DR OrthoDB; 1195799at2759; -.
DR PhylomeDB; Q96MG7; -.
DR TreeFam; TF328505; -.
DR PathwayCommons; Q96MG7; -.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR SignaLink; Q96MG7; -.
DR SIGNOR; Q96MG7; -.
DR BioGRID-ORCS; 56160; 621 hits in 1079 CRISPR screens.
DR EvolutionaryTrace; Q96MG7; -.
DR GenomeRNAi; 56160; -.
DR Pharos; Q96MG7; Tbio.
DR PRO; PR:Q96MG7; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q96MG7; protein.
DR Bgee; ENSG00000185115; Expressed in islet of Langerhans and 99 other tissues.
DR Genevisible; Q96MG7; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:UniProtKB.
DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
DR GO; GO:0072711; P:cellular response to hydroxyurea; IMP:UniProtKB.
DR GO; GO:0071478; P:cellular response to radiation; IMP:UniProtKB.
DR GO; GO:0034644; P:cellular response to UV; IMP:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:UniProtKB.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0040008; P:regulation of growth; IEA:UniProtKB-KW.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR Gene3D; 1.10.10.1200; -; 1.
DR Gene3D; 1.10.10.1210; -; 1.
DR InterPro; IPR037445; MAGE.
DR InterPro; IPR041898; MAGE_WH1.
DR InterPro; IPR041899; MAGE_WH2.
DR InterPro; IPR002190; MHD_dom.
DR PANTHER; PTHR11736; PTHR11736; 1.
DR Pfam; PF01454; MAGE; 1.
DR SMART; SM01373; MAGE; 1.
DR PROSITE; PS50838; MAGE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Cytoplasm; Disease variant; DNA damage;
KW DNA recombination; DNA repair; Growth regulation; Nucleus; Phosphoprotein;
KW Reference proteome; Telomere; Tumor antigen; Ubl conjugation pathway.
FT CHAIN 1..304
FT /note="Non-structural maintenance of chromosomes element 3
FT homolog"
FT /id="PRO_0000156733"
FT DOMAIN 85..285
FT /note="MAGE"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00127"
FT REGION 1..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..304
FT /note="Interaction with NSMCE1"
FT REGION 285..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..67
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 64
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT VARIANT 209
FT /note="P -> L (in LICS; creates novel endoproteolytic
FT cleavage sites compared to wild-type; loss of interaction
FT with NSMCE4; loss of interaction with NSMCE1;
FT dbSNP:rs886037827)"
FT /evidence="ECO:0000269|PubMed:27427983"
FT /id="VAR_078021"
FT VARIANT 264
FT /note="L -> F (in LICS; no loss of protein stability; loss
FT of interaction with NSMCE4; decreased interaction with
FT NSMCE1; decreased association with the SMC5-SMC6 complex;
FT decreased DNA repair; dbSNP:rs199905054)"
FT /evidence="ECO:0000269|PubMed:27427983"
FT /id="VAR_078022"
FT MUTAGEN 96..97
FT /note="LL->AA: Decreases interaction with NSMCE1, no effect
FT on interaction with NSMCE4A, abolishes in vitro promotion
FT of NSMCE1 ubiquitin ligase activity."
FT /evidence="ECO:0000269|PubMed:20864041"
FT MUTAGEN 180
FT /note="M->A: Abolishes interaction with EID3."
FT /evidence="ECO:0000269|PubMed:21364888"
FT MUTAGEN 181
FT /note="I->A: Abolishes interaction with EID3."
FT /evidence="ECO:0000269|PubMed:21364888"
FT MUTAGEN 185
FT /note="L->A: Abolishes interaction with EID3."
FT /evidence="ECO:0000269|PubMed:21364888"
FT MUTAGEN 266
FT /note="F->A: Abolishes interaction with EID3."
FT /evidence="ECO:0000269|PubMed:21364888"
FT MUTAGEN 270
FT /note="V->A: Abolishes interaction with EID3."
FT /evidence="ECO:0000269|PubMed:21364888"
FT HELIX 82..102
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 108..114
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 117..122
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 123..138
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 140..146
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:5WY5"
FT TURN 166..169
FT /evidence="ECO:0007829|PDB:5HVQ"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:5WY5"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 195..204
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 220..230
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:5HVQ"
FT STRAND 247..249
FT /evidence="ECO:0007829|PDB:5HVQ"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 260..271
FT /evidence="ECO:0007829|PDB:5WY5"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:5WY5"
FT HELIX 278..293
FT /evidence="ECO:0007829|PDB:5WY5"
SQ SEQUENCE 304 AA; 34308 MW; C00E2FB2D2CCED7B CRC64;
MLQKPRNRGR SGGQAERDRD WSHSGNPGAS RAGEDARVLR DGFAEEAPST SRGPGGSQGS
QGPSPQGARR AQAAPAVGPR SQKQLELKVS ELVQFLLIKD QKKIPIKRAD ILKHVIGDYK
DIFPDLFKRA AERLQYVFGY KLVELEPKSN TYILINTLEP VEEDAEMRGD QGTPTTGLLM
IVLGLIFMKG NTIKETEAWD FLRRLGVYPT KKHLIFGDPK KLITEDFVRQ RYLEYRRIPH
TDPVDYEFQW GPRTNLETSK MKVLKFVAKV HNQDPKDWPA QYCEALADEE NRARPQPSGP
APSS
