EID3_HUMAN
ID EID3_HUMAN Reviewed; 333 AA.
AC Q8N140;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=EP300-interacting inhibitor of differentiation 3;
DE Short=EID-3;
DE AltName: Full=E1A-like inhibitor of differentiation 3;
DE AltName: Full=EID-1-like inhibitor of differentiation 3;
DE AltName: Full=Non-structural maintenance of chromosomes element 4 homolog B;
DE Short=NS4EB;
DE Short=Non-SMC element 4 homolog B;
GN Name=EID3 {ECO:0000312|EMBL:AAH27612.1};
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] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CREBBP, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=15987788; DOI=10.1093/nar/gki667;
RA Bavner A., Matthews J., Sanyal S., Gustafsson J.-A., Treuter E.;
RT "EID3 is a novel EID family member and an inhibitor of CBP-dependent co-
RT activation.";
RL Nucleic Acids Res. 33:3561-3569(2005).
RN [2] {ECO:0000312|EMBL:BAC05385.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:BAC05385.1};
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] {ECO:0000312|EMBL:EAW97747.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000312|EMBL:AAH27612.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis {ECO:0000312|EMBL:AAH27612.1};
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 [5]
RP INTERACTION WITH SMC6 AND NSMCE1.
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 [6]
RP INTERACTION WITH NSMCE3.
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).
CC -!- FUNCTION: Tissue-specific component of the SMC5-SMC6 complex, a complex
CC involved in repair of DNA double-strand breaks by homologous
CC recombination. The complex may promote sister chromatid homologous
CC recombination by recruiting the SMC1-SMC3 cohesin complex to double-
CC strand breaks. The complex is required for telomere maintenance via
CC recombination and mediates sumoylation of shelterin complex (telosome)
CC components. {ECO:0000269|PubMed:15987788}.
CC -!- FUNCTION: Acts as a repressor of nuclear receptor-dependent
CC transcription possibly by interfering with CREBBP-dependent
CC coactivation. May function as a coinhibitor of other CREBBP/EP300-
CC dependent transcription factors. {ECO:0000269|PubMed:15987788}.
CC -!- SUBUNIT: Component of the SMC5-SMC6 complex which consists at least of
CC SMC5, SMC6, NSMCE2, NSMCE1, NSMCE4A or EID3 and NSMCE3; EID3 seems to
CC be a testis-specific subunit. NSMCE1, NSMCE4A or EID3 and NSMCE3
CC probably form a subcomplex that bridges the head domains of the
CC SMC5:SMC6 heterodimer. Homodimer, and heterodimer with EID2 (By
CC similarity). Interacts with the C-terminal region of CREBBP.
CC {ECO:0000250, ECO:0000269|PubMed:15987788, ECO:0000269|PubMed:18086888,
CC ECO:0000269|PubMed:21364888}.
CC -!- INTERACTION:
CC Q8N140; P43355: MAGEA1; NbExp=3; IntAct=EBI-744483, EBI-740978;
CC Q8N140; Q96MG7: NSMCE3; NbExp=8; IntAct=EBI-744483, EBI-2557356;
CC Q8N140; Q8IY18: SMC5; NbExp=4; IntAct=EBI-744483, EBI-605405;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:15987788}. Cytoplasm
CC {ECO:0000269|PubMed:15987788}. Chromosome, telomere
CC {ECO:0000305|PubMed:15987788}. Note=May shuttle between nucleus and
CC cytoplasm. {ECO:0000269|PubMed:15987788}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:15987788}.
CC -!- SIMILARITY: Belongs to the NSE4 family. {ECO:0000255}.
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DR EMBL; AK098698; BAC05385.1; -; mRNA.
DR EMBL; CH471054; EAW97747.1; -; Genomic_DNA.
DR EMBL; BC027612; AAH27612.1; -; mRNA.
DR CCDS; CCDS53822.1; -.
DR RefSeq; NP_001008395.1; NM_001008394.2.
DR AlphaFoldDB; Q8N140; -.
DR SMR; Q8N140; -.
DR BioGRID; 138924; 37.
DR ComplexPortal; CPX-5992; SMC5-SMC6 SUMO ligase complex, EID3 variant.
DR IntAct; Q8N140; 15.
DR STRING; 9606.ENSP00000435619; -.
DR iPTMnet; Q8N140; -.
DR PhosphoSitePlus; Q8N140; -.
DR BioMuta; EID3; -.
DR DMDM; 74728487; -.
DR jPOST; Q8N140; -.
DR MassIVE; Q8N140; -.
DR MaxQB; Q8N140; -.
DR PaxDb; Q8N140; -.
DR PeptideAtlas; Q8N140; -.
DR PRIDE; Q8N140; -.
DR ProteomicsDB; 71548; -.
DR Antibodypedia; 54643; 75 antibodies from 16 providers.
DR DNASU; 493861; -.
DR Ensembl; ENST00000527879.2; ENSP00000435619.1; ENSG00000255150.2.
DR GeneID; 493861; -.
DR KEGG; hsa:493861; -.
DR MANE-Select; ENST00000527879.2; ENSP00000435619.1; NM_001008394.3; NP_001008395.1.
DR UCSC; uc001tkw.4; human.
DR CTD; 493861; -.
DR DisGeNET; 493861; -.
DR GeneCards; EID3; -.
DR HGNC; HGNC:32961; EID3.
DR HPA; ENSG00000255150; Tissue enriched (testis).
DR MIM; 612986; gene.
DR neXtProt; NX_Q8N140; -.
DR OpenTargets; ENSG00000255150; -.
DR PharmGKB; PA162384552; -.
DR VEuPathDB; HostDB:ENSG00000255150; -.
DR eggNOG; KOG2866; Eukaryota.
DR GeneTree; ENSGT00940000165197; -.
DR HOGENOM; CLU_041037_3_0_1; -.
DR InParanoid; Q8N140; -.
DR OMA; TPVSYFE; -.
DR PhylomeDB; Q8N140; -.
DR TreeFam; TF313999; -.
DR PathwayCommons; Q8N140; -.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR SignaLink; Q8N140; -.
DR SIGNOR; Q8N140; -.
DR BioGRID-ORCS; 493861; 6 hits in 1070 CRISPR screens.
DR GenomeRNAi; 493861; -.
DR Pharos; Q8N140; Tdark.
DR PRO; PR:Q8N140; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8N140; protein.
DR Bgee; ENSG00000255150; Expressed in left testis and 128 other tissues.
DR ExpressionAtlas; Q8N140; baseline and differential.
DR Genevisible; Q8N140; HS.
DR GO; GO:0000781; C:chromosome, telomeric region; IC:ComplexPortal.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IBA:GO_Central.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IC:ComplexPortal.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR InterPro; IPR027786; Nse4/EID.
DR InterPro; IPR014854; Nse4_C.
DR InterPro; IPR029225; Nse4_Nse3-bd.
DR PANTHER; PTHR16140; PTHR16140; 1.
DR Pfam; PF15412; Nse4-Nse3_bdg; 1.
DR Pfam; PF08743; Nse4_C; 1.
PE 1: Evidence at protein level;
KW Chromosome; Cytoplasm; DNA damage; DNA recombination; DNA repair; Nucleus;
KW Reference proteome; Repressor; Telomere; Transcription;
KW Transcription regulation.
FT CHAIN 1..333
FT /note="EP300-interacting inhibitor of differentiation 3"
FT /id="PRO_0000315905"
SQ SEQUENCE 333 AA; 38168 MW; 3B35D08977C47C5A CRC64;
MKMDVSVRAA GCSDDLSSGE ADVDPKLLEL TADEEKCRSI RRQYRQLMYC VRQNREDIVS
SANNSLTEAL EEANVLFDGV SRTREAALDA RFLVMASDLG KEKAKQLNSD MNFFNQLAFC
DFLFLFVGLN WMEGDPDKLS DCDDSIALSF WKAIEKEATS WMVKAETFHF VFGSFKLERS
APKPRLEHQK KVRKMEENGN MPTKLQKLDL SSYPEATEKN VERILGLLQT YFRKYPDTPV
SYFEFVIDPN SFSRTVENIF YVSFIVRDGF ARIRLDEDRL PILEPMNVNQ MGEGNDSSCH
GRKQGVISLT LQEWKNIVAA FEISEAMITY SSY
