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 27-MAR-2024, entry version 167. 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}; GN 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 45. 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; 14. 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; 9606-ENSP00000330694; -. DR PeptideAtlas; Q96MG7; -. DR ProteomicsDB; 77353; -. DR Pumba; Q96MG7; -. DR Antibodypedia; 41882; 61 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 AGR; HGNC:7677; -. 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; HQSSGCP; -. DR OrthoDB; 3128316at2759; -. 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; 652 hits in 1160 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 100 other cell types or tissues. DR GO; GO:0000781; C:chromosome, telomeric region; NAS: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:0140588; P:chromatin looping; NAS:ComplexPortal. DR GO; GO:0006281; P:DNA repair; IMP:UniProtKB. DR GO; GO:0000724; P:double-strand break repair via homologous recombination; NAS: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; NAS:ComplexPortal. DR GO; GO:0032204; P:regulation of telomere maintenance; NAS:ComplexPortal. DR Gene3D; 1.10.10.1200; MAGE homology domain, winged helix WH1 motif; 1. DR Gene3D; 1.10.10.1210; MAGE homology domain, winged helix WH2 motif; 1. DR InterPro; IPR037445; MAGE. DR InterPro; IPR041898; MAGE_WH1. DR InterPro; IPR041899; MAGE_WH2. DR InterPro; IPR002190; MHD_dom. DR PANTHER; PTHR11736; MELANOMA-ASSOCIATED ANTIGEN MAGE ANTIGEN; 1. DR PANTHER; PTHR11736:SF165; NON-STRUCTURAL MAINTENANCE OF CHROMOSOMES ELEMENT 3 HOMOLOG; 1. DR Pfam; PF01454; MAGE; 1. DR SMART; SM01373; MAGE; 1. DR PROSITE; PS50838; MAGE; 1. DR Genevisible; Q96MG7; HS. 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 //