ITF2_HUMAN
ID ITF2_HUMAN Reviewed; 667 AA.
AC P15884; B3KT62; B3KUC0; B4DT37; B4DUG3; B7Z5M6; B7Z6Y1; G0LNT9; G0LNU0;
AC G0LNU1; G0LNU2; G0LNU4; G0LNU5; G0LNU8; G0LNU9; G0LNV0; G0LNV1; G0LNV2;
AC H3BPQ1; Q08AP2; Q08AP3; Q15439; Q15440; Q15441;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 3.
DT 03-AUG-2022, entry version 225.
DE RecName: Full=Transcription factor 4;
DE Short=TCF-4;
DE AltName: Full=Class B basic helix-loop-helix protein 19;
DE Short=bHLHb19;
DE AltName: Full=Immunoglobulin transcription factor 2;
DE Short=ITF-2;
DE AltName: Full=SL3-3 enhancer factor 2;
DE Short=SEF-2;
GN Name=TCF4; Synonyms=BHLHB19, ITF2, SEF2;
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] (ISOFORMS SEF2-1A; SEF2-1B AND SEF2-1D), AND
RP ALTERNATIVE SPLICING (ISOFORM SEF2-1C).
RC TISSUE=Thymocyte, and Thymus;
RX PubMed=1681116; DOI=10.1128/jvi.65.11.6084-6093.1991;
RA Corneliussen B., Thornell A., Hallberg B., Grundstroem T.;
RT "Helix-loop-helix transcriptional activators bind to a sequence in
RT glucocorticoid response elements of retrovirus enhancers.";
RL J. Virol. 65:6084-6093(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A-; B-DELTA; B+DELTA; C-; C-DELTA; D-;
RP E-; F-; G-; H-; I-; SEF2-1A; SEF2-1B AND SEF2-1D), AND ALTERNATIVE
RP SPLICING.
RX PubMed=21789225; DOI=10.1371/journal.pone.0022138;
RA Sepp M., Kannike K., Eesmaa A., Urb M., Timmusk T.;
RT "Functional diversity of human basic helix-loop-helix transcription factor
RT TCF4 isoforms generated by alternative 5' exon usage and splicing.";
RL PLoS ONE 6:E22138-E22138(2011).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SEF2-1A; C-; D-; F-; 11
RP AND 13).
RC TISSUE=Brain, Hippocampus, Spleen, and Teratocarcinoma;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16177791; DOI=10.1038/nature03983;
RA Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D.,
RA Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
RA Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J.,
RA Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L.,
RA Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A.,
RA Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C.,
RA Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K.,
RA Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R.,
RA Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 18.";
RL Nature 437:551-555(2005).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS SEF2-1B AND SEF2-1D).
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-278 (ISOFORM SEF2-1A).
RA Gu J., Zhao M., Huang Q., Xu X., Li Y., Peng Y., Song H., Xiao H., Gu Y.,
RA Li N., Qian B., Liu F., Qu J., Gao X., Cheng Z., Xu Z., Zeng L., Xu S.,
RA Gu W., Tu Y., Jia J., Fu G., Ren S., Zhong M., Lu G., Yang Y., Gao G.,
RA Zhang Q., Chen S., Han Z., Chen Z.;
RT "MDSDCE06_MDS Homo sapiens cDNA clone MDSDCE06 5',mRNA sequence.";
RL Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-48.
RC TISSUE=Skin fibroblast;
RX PubMed=9302263; DOI=10.1093/hmg/6.11.1855;
RA Breschel T.S., McInnis M.G., Margolis R.L., Sirugo G., Corneliussen B.,
RA Simpson S.G., McMahon F.J., Mackinnon D.F., Xu J.F., Pleasant N., Huo Y.,
RA Ashworth R.G., Grundstrom C., Grundstrom T., Kidd K.K., Depaulo J.R.,
RA Ross C.A.;
RT "A novel, heritable, expanding CTG repeat in an intron of the SEF2-1 gene
RT on chromosome 18q21.1.";
RL Hum. Mol. Genet. 6:1855-1863(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 46-667 (ISOFORM SEF2-1B).
RX PubMed=2308860; DOI=10.1093/nar/18.3.678;
RA Henthorn P., McCarrick-Walmsley R., Kadesch T.;
RT "Sequence of the cDNA encoding ITF-2, a positive-acting transcription
RT factor.";
RL Nucleic Acids Res. 18:678-678(1990).
RN [10]
RP DISCUSSION OF SEQUENCE.
RX PubMed=2105528; DOI=10.1126/science.2105528;
RA Henthorn P., Kiledjian M., Kadesch T.;
RT "Two distinct transcription factors that bind the immunoglobulin enhancer
RT microE5/kappa 2 motif.";
RL Science 247:467-470(1990).
RN [11]
RP DOMAIN.
RX PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
RA Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P., Piskacek M.;
RT "Nine-amino-acid transactivation domain: establishment and prediction
RT utilities.";
RL Genomics 89:756-768(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP 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 SUBCELLULAR LOCATION, AND CHARACTERIZATION OF VARIANTS PTHS VAL-358;
RP GLY-535; PRO-574; TRP-576 AND VAL-610.
RX PubMed=22777675; DOI=10.1002/humu.22160;
RA Forrest M., Chapman R.M., Doyle A.M., Tinsley C.L., Waite A., Blake D.J.;
RT "Functional analysis of TCF4 missense mutations that cause Pitt-Hopkins
RT syndrome.";
RL Hum. Mutat. 33:1676-1686(2012).
RN [14]
RP INTERACTION WITH AGBL1.
RX PubMed=24094747; DOI=10.1016/j.ajhg.2013.08.010;
RA Riazuddin S.A., Vasanth S., Katsanis N., Gottsch J.D.;
RT "Mutations in AGBL1 cause dominant late-onset Fuchs corneal dystrophy and
RT alter protein-protein interaction with TCF4.";
RL Am. J. Hum. Genet. 93:758-764(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66; SER-87 AND SER-92, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [16]
RP INTERACTION WITH BHLHA9.
RX PubMed=25466284; DOI=10.1016/j.ajhg.2014.10.012;
RA Malik S., Percin F.E., Bornholdt D., Albrecht B., Percesepe A., Koch M.C.,
RA Landi A., Fritz B., Khan R., Mumtaz S., Akarsu N.A., Grzeschik K.H.;
RT "Mutations affecting the BHLHA9 DNA-binding domain cause MSSD, mesoaxial
RT synostotic syndactyly with phalangeal reduction, Malik-Percin type.";
RL Am. J. Hum. Genet. 95:649-659(2014).
RN [17]
RP INVOLVEMENT IN FECD3.
RX PubMed=24255041; DOI=10.1167/iovs.13-12611;
RA Mootha V.V., Gong X., Ku H.C., Xing C.;
RT "Association and familial segregation of CTG18.1 trinucleotide repeat
RT expansion of TCF4 gene in Fuchs' endothelial corneal dystrophy.";
RL Invest. Ophthalmol. Vis. Sci. 55:33-42(2014).
RN [18]
RP INVOLVEMENT IN FECD3.
RX PubMed=25168903; DOI=10.1167/iovs.14-14958;
RA Wieben E.D., Aleff R.A., Eckloff B.W., Atkinson E.J., Baheti S., Middha S.,
RA Brown W.L., Patel S.V., Kocher J.P., Baratz K.H.;
RT "Comprehensive assessment of genetic variants within TCF4 in Fuchs'
RT endothelial corneal dystrophy.";
RL Invest. Ophthalmol. Vis. Sci. 55:6101-6107(2014).
RN [19]
RP INVOLVEMENT IN FECD3.
RX PubMed=25593321; DOI=10.1074/jbc.m114.621607;
RA Du J., Aleff R.A., Soragni E., Kalari K., Nie J., Tang X., Davila J.,
RA Kocher J.P., Patel S.V., Gottesfeld J.M., Baratz K.H., Wieben E.D.;
RT "RNA toxicity and missplicing in the common eye disease fuchs endothelial
RT corneal dystrophy.";
RL J. Biol. Chem. 290:5979-5990(2015).
RN [20]
RP POSSIBLE INVOLVEMENT IN SYMMETRICAL ACRAL KERATODERMA, AND VARIANT THR-29.
RX PubMed=28921696; DOI=10.1111/jdv.14591;
RA Chen P., Sun S., Zeng K., Li C., Wen J., Liang J., Tian X., Jiang Y.,
RA Zhang J., Zhang S., Han K., Han C., Zhang X.;
RT "Exome sequencing identifies a TCF4 mutation in a Chinese pedigree with
RT symmetrical acral keratoderma.";
RL J. Eur. Acad. Dermatol. Venereol. 32:1204-1208(2018).
RN [21]
RP VARIANTS PTHS TRP-576 AND GLN-576.
RX PubMed=17436254; DOI=10.1086/515582;
RA Amiel J., Rio M., de Pontual L., Redon R., Malan V., Boddaert N.,
RA Plouin P., Carter N.P., Lyonnet S., Munnich A., Colleaux L.;
RT "Mutations in TCF4, encoding a class I basic helix-loop-helix transcription
RT factor, are responsible for Pitt-Hopkins syndrome, a severe epileptic
RT encephalopathy associated with autonomic dysfunction.";
RL Am. J. Hum. Genet. 80:988-993(2007).
RN [22]
RP VARIANT PTHS TRP-576.
RX PubMed=17436255; DOI=10.1086/515583;
RA Zweier C., Peippo M.M., Hoyer J., Sousa S., Bottani A., Clayton-Smith J.,
RA Reardon W., Saraiva J., Cabral A., Goehring I., Devriendt K., de Ravel T.,
RA Bijlsma E.K., Hennekam R.C.M., Orrico A., Cohen M., Dreweke A., Reis A.,
RA Nuernberg P., Rauch A.;
RT "Haploinsufficiency of TCF4 causes syndromal mental retardation with
RT intermittent hyperventilation (Pitt-Hopkins syndrome).";
RL Am. J. Hum. Genet. 80:994-1001(2007).
RN [23]
RP VARIANTS PTHS VAL-358; PRO-574 AND HIS-578.
RX PubMed=18728071; DOI=10.1136/jmg.2008.060129;
RA Zweier C., Sticht H., Bijlsma E.K., Clayton-Smith J., Boonen S.E.,
RA Fryer A., Greally M.T., Hoffmann L., den Hollander N.S., Jongmans M.,
RA Kant S.G., King M.D., Lynch S.A., McKee S., Midro A.T., Park S.M.,
RA Ricotti V., Tarantino E., Wessels M., Peippo M., Rauch A.;
RT "Further delineation of Pitt-Hopkins syndrome: phenotypic and genotypic
RT description of 16 novel patients.";
RL J. Med. Genet. 45:738-744(2008).
RN [24]
RP VARIANTS PTHS GLY-535; GLY-572; GLN-576 AND VAL-610, AND CHARACTERIZATION
RP OF VARIANTS PTHS GLY-535; GLY-572; GLN-576 AND VAL-610.
RX PubMed=19235238; DOI=10.1002/humu.20935;
RA de Pontual L., Mathieu Y., Golzio C., Rio M., Malan V., Boddaert N.,
RA Soufflet C., Picard C., Durandy A., Dobbie A., Heron D., Isidor B.,
RA Motte J., Newburry-Ecob R., Pasquier L., Tardieu M., Viot G., Jaubert F.,
RA Munnich A., Colleaux L., Vekemans M., Etchevers H., Lyonnet S., Amiel J.;
RT "Mutational, functional, and expression studies of the TCF4 gene in Pitt-
RT Hopkins syndrome.";
RL Hum. Mutat. 30:669-676(2009).
RN [25]
RP VARIANT PTHS PRO-578.
RX PubMed=20184619; DOI=10.1111/j.1399-0004.2010.01380.x;
RA Takano K., Lyons M., Moyes C., Jones J., Schwartz C.E.;
RT "Two percent of patients suspected of having Angelman syndrome have TCF4
RT mutations.";
RL Clin. Genet. 78:282-288(2010).
RN [26]
RP VARIANTS PTHS TRP-565; GLY-572; GLN-572; HIS-574; PRO-574; TRP-576;
RP GLN-576; PRO-578; PRO-583 AND VAL-610.
RX PubMed=22045651; DOI=10.1002/humu.21639;
RA Whalen S., Heron D., Gaillon T., Moldovan O., Rossi M., Devillard F.,
RA Giuliano F., Soares G., Mathieu-Dramard M., Afenjar A., Charles P.,
RA Mignot C., Burglen L., Van Maldergem L., Piard J., Aftimos S., Mancini G.,
RA Dias P., Philip N., Goldenberg A., Le Merrer M., Rio M., Josifova D.,
RA Van Hagen J.M., Lacombe D., Edery P., Dupuis-Girod S., Putoux A.,
RA Sanlaville D., Fischer R., Drevillon L., Briand-Suleau A., Metay C.,
RA Goossens M., Amiel J., Jacquette A., Giurgea I.;
RT "Novel comprehensive diagnostic strategy in Pitt-Hopkins syndrome: clinical
RT score and further delineation of the TCF4 mutational spectrum.";
RL Hum. Mutat. 33:64-72(2012).
RN [27]
RP VARIANT PTHS 385-ARG--MET-667 DEL.
RX PubMed=25356899; DOI=10.1371/journal.pgen.1004772;
RA Hamdan F.F., Srour M., Capo-Chichi J.M., Daoud H., Nassif C., Patry L.,
RA Massicotte C., Ambalavanan A., Spiegelman D., Diallo O., Henrion E.,
RA Dionne-Laporte A., Fougerat A., Pshezhetsky A.V., Venkateswaran S.,
RA Rouleau G.A., Michaud J.L.;
RT "De novo mutations in moderate or severe intellectual disability.";
RL PLoS Genet. 10:E1004772-E1004772(2014).
CC -!- FUNCTION: Transcription factor that binds to the immunoglobulin
CC enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal
CC differentiation. Activates transcription by binding to the E box (5'-
CC CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2
CC initiator element (SSTR2-INR) to activate transcription (By
CC similarity). Preferentially binds to either 5'-ACANNTGT-3' or 5'-
CC CCANNTGG-3'. {ECO:0000250}.
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Forms homo- or heterooligomers with myogenin. Interacts with
CC HIVEP2. Interacts with NEUROD2 (By similarity). Interacts with AGBL1.
CC Interacts with BHLHA9. {ECO:0000250, ECO:0000269|PubMed:24094747,
CC ECO:0000269|PubMed:25466284}.
CC -!- INTERACTION:
CC P15884; P29972: AQP1; NbExp=3; IntAct=EBI-533224, EBI-745213;
CC P15884; Q92888: ARHGEF1; NbExp=3; IntAct=EBI-533224, EBI-465400;
CC P15884; Q9H6L4: ARMC7; NbExp=3; IntAct=EBI-533224, EBI-742909;
CC P15884; P50553: ASCL1; NbExp=7; IntAct=EBI-533224, EBI-957042;
CC P15884; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-533224, EBI-10254793;
CC P15884; Q9BZE9: ASPSCR1; NbExp=3; IntAct=EBI-533224, EBI-1993677;
CC P15884; P21281: ATP6V1B2; NbExp=3; IntAct=EBI-533224, EBI-4290814;
CC P15884; O75934: BCAS2; NbExp=4; IntAct=EBI-533224, EBI-1050106;
CC P15884; Q92843: BCL2L2; NbExp=3; IntAct=EBI-533224, EBI-707714;
CC P15884; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-533224, EBI-8643161;
CC P15884; Q9NP86: CABP5; NbExp=5; IntAct=EBI-533224, EBI-10311131;
CC P15884; P38936: CDKN1A; NbExp=3; IntAct=EBI-533224, EBI-375077;
CC P15884; P42773: CDKN2C; NbExp=4; IntAct=EBI-533224, EBI-711290;
CC P15884; Q6ZQR2: CFAP77; NbExp=3; IntAct=EBI-533224, EBI-10255140;
CC P15884; Q13111: CHAF1A; NbExp=3; IntAct=EBI-533224, EBI-1020839;
CC P15884; Q9Y6H1: CHCHD2; NbExp=3; IntAct=EBI-533224, EBI-2321769;
CC P15884; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-533224, EBI-741528;
CC P15884; P61024: CKS1B; NbExp=3; IntAct=EBI-533224, EBI-456371;
CC P15884; P35222: CTNNB1; NbExp=22; IntAct=EBI-533224, EBI-491549;
CC P15884; P26196: DDX6; NbExp=3; IntAct=EBI-533224, EBI-351257;
CC P15884; Q9H4E7: DEF6; NbExp=4; IntAct=EBI-533224, EBI-745369;
CC P15884; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-533224, EBI-9679045;
CC P15884; Q5JVL4: EFHC1; NbExp=7; IntAct=EBI-533224, EBI-743105;
CC P15884; O60573: EIF4E2; NbExp=3; IntAct=EBI-533224, EBI-398610;
CC P15884; Q13541: EIF4EBP1; NbExp=3; IntAct=EBI-533224, EBI-74090;
CC P15884; Q9Y2J2-3: EPB41L3; NbExp=3; IntAct=EBI-533224, EBI-10326138;
CC P15884; O15197-2: EPHB6; NbExp=3; IntAct=EBI-533224, EBI-10182490;
CC P15884; Q9Y3B2: EXOSC1; NbExp=4; IntAct=EBI-533224, EBI-371892;
CC P15884; P16930: FAH; NbExp=3; IntAct=EBI-533224, EBI-4397076;
CC P15884; Q9H5Z6: FAM124B; NbExp=3; IntAct=EBI-533224, EBI-741626;
CC P15884; Q5TZK3: FAM74A6; NbExp=3; IntAct=EBI-533224, EBI-10247271;
CC P15884; Q96RJ6: FERD3L; NbExp=4; IntAct=EBI-533224, EBI-10183007;
CC P15884; Q96AC1: FERMT2; NbExp=6; IntAct=EBI-533224, EBI-4399465;
CC P15884; Q8NFF5: FLAD1; NbExp=3; IntAct=EBI-533224, EBI-742815;
CC P15884; P21333-2: FLNA; NbExp=3; IntAct=EBI-533224, EBI-9641086;
CC P15884; O43559: FRS3; NbExp=3; IntAct=EBI-533224, EBI-725515;
CC P15884; P55040: GEM; NbExp=3; IntAct=EBI-533224, EBI-744104;
CC P15884; O76003: GLRX3; NbExp=3; IntAct=EBI-533224, EBI-374781;
CC P15884; P50151: GNG10; NbExp=3; IntAct=EBI-533224, EBI-10211741;
CC P15884; Q0D2H9: GOLGA8DP; NbExp=3; IntAct=EBI-533224, EBI-10181276;
CC P15884; Q08AF8: GOLGA8G; NbExp=3; IntAct=EBI-533224, EBI-10181260;
CC P15884; Q9H8Y8: GORASP2; NbExp=4; IntAct=EBI-533224, EBI-739467;
CC P15884; Q96NT3: GUCD1; NbExp=3; IntAct=EBI-533224, EBI-8293751;
CC P15884; P61296: HAND2; NbExp=3; IntAct=EBI-533224, EBI-10218584;
CC P15884; O14929: HAT1; NbExp=3; IntAct=EBI-533224, EBI-2339359;
CC P15884; V9HWF5: HEL-S-69p; NbExp=3; IntAct=EBI-533224, EBI-10330249;
CC P15884; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-533224, EBI-739361;
CC P15884; P41134: ID1; NbExp=3; IntAct=EBI-533224, EBI-1215527;
CC P15884; Q02363: ID2; NbExp=3; IntAct=EBI-533224, EBI-713450;
CC P15884; Q02535: ID3; NbExp=5; IntAct=EBI-533224, EBI-1387094;
CC P15884; I3WAC9: INS; NbExp=3; IntAct=EBI-533224, EBI-10178524;
CC P15884; Q92993: KAT5; NbExp=3; IntAct=EBI-533224, EBI-399080;
CC P15884; Q9BQ13: KCTD14; NbExp=3; IntAct=EBI-533224, EBI-10189448;
CC P15884; Q6P597: KLC3; NbExp=3; IntAct=EBI-533224, EBI-1643885;
CC P15884; Q5THT1: KLHL32; NbExp=3; IntAct=EBI-533224, EBI-10247181;
CC P15884; Q14847: LASP1; NbExp=3; IntAct=EBI-533224, EBI-742828;
CC P15884; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-533224, EBI-726510;
CC P15884; Q8TCE9: LGALS14; NbExp=4; IntAct=EBI-533224, EBI-10274069;
CC P15884; P25800: LMO1; NbExp=3; IntAct=EBI-533224, EBI-8639312;
CC P15884; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-533224, EBI-11742507;
CC P15884; P61968: LMO4; NbExp=3; IntAct=EBI-533224, EBI-2798728;
CC P15884; Q9UIQ6: LNPEP; NbExp=3; IntAct=EBI-533224, EBI-2805360;
CC P15884; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-533224, EBI-77889;
CC P15884; Q96A72: MAGOHB; NbExp=3; IntAct=EBI-533224, EBI-746778;
CC P15884; O60336: MAPKBP1; NbExp=3; IntAct=EBI-533224, EBI-947402;
CC P15884; O15232: MATN3; NbExp=3; IntAct=EBI-533224, EBI-6262458;
CC P15884; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-533224, EBI-1104564;
CC P15884; Q6P2C6: MLLT6; NbExp=3; IntAct=EBI-533224, EBI-5773143;
CC P15884; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-533224, EBI-10269566;
CC P15884; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-533224, EBI-748896;
CC P15884; Q7Z7H8: MRPL10; NbExp=3; IntAct=EBI-533224, EBI-723524;
CC P15884; Q8IXL7: MSRB3; NbExp=3; IntAct=EBI-533224, EBI-8634060;
CC P15884; Q9ULV0: MYO5B; NbExp=3; IntAct=EBI-533224, EBI-311356;
CC P15884; O43639: NCK2; NbExp=3; IntAct=EBI-533224, EBI-713635;
CC P15884; Q9UHB4: NDOR1; NbExp=4; IntAct=EBI-533224, EBI-10249760;
CC P15884; Q9HC98: NEK6; NbExp=4; IntAct=EBI-533224, EBI-740364;
CC P15884; Q86SG6: NEK8; NbExp=3; IntAct=EBI-533224, EBI-1752987;
CC P15884; Q8WWR8-2: NEU4; NbExp=3; IntAct=EBI-533224, EBI-10277551;
CC P15884; Q92886: NEUROG1; NbExp=3; IntAct=EBI-533224, EBI-10279647;
CC P15884; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-533224, EBI-744782;
CC P15884; Q9GZQ4: NMUR2; NbExp=3; IntAct=EBI-533224, EBI-10303844;
CC P15884; Q5SY16: NOL9; NbExp=3; IntAct=EBI-533224, EBI-1055462;
CC P15884; Q86WQ0: NR2C2AP; NbExp=3; IntAct=EBI-533224, EBI-10260040;
CC P15884; Q8NFP7: NUDT10; NbExp=3; IntAct=EBI-533224, EBI-726826;
CC P15884; O43929: ORC4; NbExp=3; IntAct=EBI-533224, EBI-374889;
CC P15884; Q9UJX0: OSGIN1; NbExp=4; IntAct=EBI-533224, EBI-9057006;
CC P15884; Q01804: OTUD4; NbExp=3; IntAct=EBI-533224, EBI-1054396;
CC P15884; Q8WXA2: PATE1; NbExp=3; IntAct=EBI-533224, EBI-10277790;
CC P15884; P30039: PBLD; NbExp=3; IntAct=EBI-533224, EBI-750589;
CC P15884; Q13526: PIN1; NbExp=3; IntAct=EBI-533224, EBI-714158;
CC P15884; Q494U1: PLEKHN1; NbExp=4; IntAct=EBI-533224, EBI-10241513;
CC P15884; O95602: POLR1A; NbExp=3; IntAct=EBI-533224, EBI-359472;
CC P15884; O15160: POLR1C; NbExp=3; IntAct=EBI-533224, EBI-1055079;
CC P15884; P62937-2: PPIA; NbExp=3; IntAct=EBI-533224, EBI-25884072;
CC P15884; Q9Y3C6: PPIL1; NbExp=3; IntAct=EBI-533224, EBI-2557649;
CC P15884; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-533224, EBI-2557469;
CC P15884; P54646: PRKAA2; NbExp=3; IntAct=EBI-533224, EBI-1383852;
CC P15884; P17252: PRKCA; NbExp=3; IntAct=EBI-533224, EBI-1383528;
CC P15884; P25786: PSMA1; NbExp=3; IntAct=EBI-533224, EBI-359352;
CC P15884; Q969U7: PSMG2; NbExp=3; IntAct=EBI-533224, EBI-723276;
CC P15884; P43115-12: PTGER3; NbExp=3; IntAct=EBI-533224, EBI-10234038;
CC P15884; Q5JT25: RAB41; NbExp=3; IntAct=EBI-533224, EBI-10244509;
CC P15884; P47224: RABIF; NbExp=3; IntAct=EBI-533224, EBI-713992;
CC P15884; Q6P9E2: RECK; NbExp=3; IntAct=EBI-533224, EBI-10253121;
CC P15884; Q04206-3: RELA; NbExp=3; IntAct=EBI-533224, EBI-10223388;
CC P15884; Q8IX06: REXO1L1P; NbExp=3; IntAct=EBI-533224, EBI-10262361;
CC P15884; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-533224, EBI-748350;
CC P15884; Q9UIL1: SCOC; NbExp=3; IntAct=EBI-533224, EBI-2686537;
CC P15884; Q9UDX3: SEC14L4; NbExp=3; IntAct=EBI-533224, EBI-10320311;
CC P15884; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-533224, EBI-9090795;
CC P15884; Q6NXQ0: SFRS2; NbExp=3; IntAct=EBI-533224, EBI-10251550;
CC P15884; Q96ES7: SGF29; NbExp=5; IntAct=EBI-533224, EBI-743117;
CC P15884; Q9NUL5: SHFL; NbExp=3; IntAct=EBI-533224, EBI-10313866;
CC P15884; O43699: SIGLEC6; NbExp=3; IntAct=EBI-533224, EBI-2814604;
CC P15884; Q96H72: SLC39A13; NbExp=3; IntAct=EBI-533224, EBI-10287091;
CC P15884; Q9BWU0: SLC4A1AP; NbExp=3; IntAct=EBI-533224, EBI-1999704;
CC P15884; P49901: SMCP; NbExp=3; IntAct=EBI-533224, EBI-750494;
CC P15884; Q9H4F8: SMOC1; NbExp=3; IntAct=EBI-533224, EBI-2801103;
CC P15884; Q9H0A9: SPATC1L; NbExp=3; IntAct=EBI-533224, EBI-372911;
CC P15884; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-533224, EBI-742688;
CC P15884; Q96FJ0: STAMBPL1; NbExp=3; IntAct=EBI-533224, EBI-745021;
CC P15884; O75716: STK16; NbExp=3; IntAct=EBI-533224, EBI-749295;
CC P15884; O75558: STX11; NbExp=3; IntAct=EBI-533224, EBI-714135;
CC P15884; Q5T011-5: SZT2; NbExp=3; IntAct=EBI-533224, EBI-10245139;
CC P15884; P17542: TAL1; NbExp=4; IntAct=EBI-533224, EBI-1753878;
CC P15884; Q16559: TAL2; NbExp=3; IntAct=EBI-533224, EBI-10237959;
CC P15884; Q15560: TCEA2; NbExp=3; IntAct=EBI-533224, EBI-710310;
CC P15884; P15884: TCF4; NbExp=3; IntAct=EBI-533224, EBI-533224;
CC P15884; P56279: TCL1A; NbExp=3; IntAct=EBI-533224, EBI-749995;
CC P15884; Q08117: TLE5; NbExp=3; IntAct=EBI-533224, EBI-717810;
CC P15884; P04637: TP53; NbExp=2; IntAct=EBI-533224, EBI-366083;
CC P15884; Q9UL33: TRAPPC2L; NbExp=3; IntAct=EBI-533224, EBI-747601;
CC P15884; Q96PN8: TSSK3; NbExp=3; IntAct=EBI-533224, EBI-3918381;
CC P15884; Q15672: TWIST1; NbExp=8; IntAct=EBI-533224, EBI-1797287;
CC P15884; Q8WVJ9: TWIST2; NbExp=4; IntAct=EBI-533224, EBI-1797313;
CC P15884; Q9NX01: TXNL4B; NbExp=4; IntAct=EBI-533224, EBI-10309345;
CC P15884; Q9BRU9: UTP23; NbExp=3; IntAct=EBI-533224, EBI-5457544;
CC P15884; Q548N1: VPS28; NbExp=3; IntAct=EBI-533224, EBI-10243107;
CC P15884; P61981: YWHAG; NbExp=3; IntAct=EBI-533224, EBI-359832;
CC P15884; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-533224, EBI-10254561;
CC P15884; Q15973: ZNF124; NbExp=3; IntAct=EBI-533224, EBI-2555767;
CC P15884; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-533224, EBI-740727;
CC P15884; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-533224, EBI-6427977;
CC P15884; Q53FW8; NbExp=3; IntAct=EBI-533224, EBI-10242473;
CC P15884; P26233: ctnnb1; Xeno; NbExp=2; IntAct=EBI-533224, EBI-7373758;
CC P15884; PRO_0000449627 [P0DTD1]: rep; Xeno; NbExp=3; IntAct=EBI-533224, EBI-25475877;
CC P15884; Q61473: Sox17; Xeno; NbExp=5; IntAct=EBI-533224, EBI-9106822;
CC P15884; Q06831: Sox4; Xeno; NbExp=2; IntAct=EBI-533224, EBI-6262177;
CC P15884-3; Q9NXW9: ALKBH4; NbExp=3; IntAct=EBI-13636688, EBI-8637516;
CC P15884-3; Q12774: ARHGEF5; NbExp=3; IntAct=EBI-13636688, EBI-602199;
CC P15884-3; Q0P5N6: ARL16; NbExp=3; IntAct=EBI-13636688, EBI-10186132;
CC P15884-3; Q8TDY4: ASAP3; NbExp=3; IntAct=EBI-13636688, EBI-2609717;
CC P15884-3; Q9NQ33: ASCL3; NbExp=3; IntAct=EBI-13636688, EBI-12108222;
CC P15884-3; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-13636688, EBI-10254793;
CC P15884-3; Q7Z3C6-3: ATG9A; NbExp=3; IntAct=EBI-13636688, EBI-12006308;
CC P15884-3; Q8N100: ATOH7; NbExp=3; IntAct=EBI-13636688, EBI-11976887;
CC P15884-3; A0A0C4DG94: ATP11B; NbExp=3; IntAct=EBI-13636688, EBI-11990784;
CC P15884-3; Q9H503-2: BANF2; NbExp=3; IntAct=EBI-13636688, EBI-11977289;
CC P15884-3; Q5TBC7: BCL2L15; NbExp=3; IntAct=EBI-13636688, EBI-10247136;
CC P15884-3; Q9BV19: C1orf50; NbExp=3; IntAct=EBI-13636688, EBI-2874661;
CC P15884-3; O43439-4: CBFA2T2; NbExp=3; IntAct=EBI-13636688, EBI-11954144;
CC P15884-3; P51946: CCNH; NbExp=3; IntAct=EBI-13636688, EBI-741406;
CC P15884-3; Q16543: CDC37; NbExp=3; IntAct=EBI-13636688, EBI-295634;
CC P15884-3; P42773: CDKN2C; NbExp=3; IntAct=EBI-13636688, EBI-711290;
CC P15884-3; Q13111: CHAF1A; NbExp=3; IntAct=EBI-13636688, EBI-1020839;
CC P15884-3; P61024: CKS1B; NbExp=3; IntAct=EBI-13636688, EBI-456371;
CC P15884-3; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-13636688, EBI-11980535;
CC P15884-3; Q86WW8: COA5; NbExp=3; IntAct=EBI-13636688, EBI-5458774;
CC P15884-3; Q96FN4: CPNE2; NbExp=3; IntAct=EBI-13636688, EBI-7097057;
CC P15884-3; P26196: DDX6; NbExp=3; IntAct=EBI-13636688, EBI-351257;
CC P15884-3; P04053: DNTT; NbExp=3; IntAct=EBI-13636688, EBI-1220259;
CC P15884-3; Q9BVJ7: DUSP23; NbExp=3; IntAct=EBI-13636688, EBI-724940;
CC P15884-3; Q68J44: DUSP29; NbExp=3; IntAct=EBI-13636688, EBI-1054321;
CC P15884-3; Q5JVL4: EFHC1; NbExp=6; IntAct=EBI-13636688, EBI-743105;
CC P15884-3; O15197-2: EPHB6; NbExp=3; IntAct=EBI-13636688, EBI-10182490;
CC P15884-3; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-13636688, EBI-742102;
CC P15884-3; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-13636688, EBI-1752811;
CC P15884-3; Q6QHK4: FIGLA; NbExp=3; IntAct=EBI-13636688, EBI-11976617;
CC P15884-3; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-13636688, EBI-14103818;
CC P15884-3; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-13636688, EBI-739361;
CC P15884-3; P41134: ID1; NbExp=3; IntAct=EBI-13636688, EBI-1215527;
CC P15884-3; Q02535: ID3; NbExp=3; IntAct=EBI-13636688, EBI-1387094;
CC P15884-3; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-13636688, EBI-6426443;
CC P15884-3; A0A0S2Z5S9: LHX4; NbExp=3; IntAct=EBI-13636688, EBI-16429099;
CC P15884-3; P61968: LMO4; NbExp=3; IntAct=EBI-13636688, EBI-2798728;
CC P15884-3; Q9UI95: MAD2L2; NbExp=3; IntAct=EBI-13636688, EBI-77889;
CC P15884-3; O60336: MAPKBP1; NbExp=3; IntAct=EBI-13636688, EBI-947402;
CC P15884-3; Q9Y4F3: MARF1; NbExp=3; IntAct=EBI-13636688, EBI-5235902;
CC P15884-3; O15232: MATN3; NbExp=3; IntAct=EBI-13636688, EBI-6262458;
CC P15884-3; Q9Y316: MEMO1; NbExp=3; IntAct=EBI-13636688, EBI-1104564;
CC P15884-3; Q9BUN1: MENT; NbExp=3; IntAct=EBI-13636688, EBI-12022316;
CC P15884-3; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-13636688, EBI-10269566;
CC P15884-3; O60682: MSC; NbExp=3; IntAct=EBI-13636688, EBI-740310;
CC P15884-3; A6NI15: MSGN1; NbExp=3; IntAct=EBI-13636688, EBI-11991020;
CC P15884-3; Q9ULV0-2: MYO5B; NbExp=3; IntAct=EBI-13636688, EBI-14093244;
CC P15884-3; Q9UHB4: NDOR1; NbExp=3; IntAct=EBI-13636688, EBI-10249760;
CC P15884-3; Q92692-2: NECTIN2; NbExp=3; IntAct=EBI-13636688, EBI-6979889;
CC P15884-3; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-13636688, EBI-11750983;
CC P15884-3; Q13562: NEUROD1; NbExp=3; IntAct=EBI-13636688, EBI-3908303;
CC P15884-3; Q9HD90: NEUROD4; NbExp=3; IntAct=EBI-13636688, EBI-3917781;
CC P15884-3; Q9Y4Z2: NEUROG3; NbExp=4; IntAct=EBI-13636688, EBI-10328570;
CC P15884-3; Q8NET5: NFAM1; NbExp=3; IntAct=EBI-13636688, EBI-11990542;
CC P15884-3; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-13636688, EBI-10271199;
CC P15884-3; Q02577: NHLH2; NbExp=3; IntAct=EBI-13636688, EBI-5378683;
CC P15884-3; Q9Y5B8: NME7; NbExp=3; IntAct=EBI-13636688, EBI-744782;
CC P15884-3; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-13636688, EBI-12025760;
CC P15884-3; Q9BRQ3: NUDT22; NbExp=3; IntAct=EBI-13636688, EBI-10297093;
CC P15884-3; Q96DL1-3: NXPE2; NbExp=3; IntAct=EBI-13636688, EBI-12128194;
CC P15884-3; Q9NPJ8-3: NXT2; NbExp=3; IntAct=EBI-13636688, EBI-10698339;
CC P15884-3; Q96PB7-3: OLFM3; NbExp=3; IntAct=EBI-13636688, EBI-12005356;
CC P15884-3; Q8WXA2-2: PATE1; NbExp=3; IntAct=EBI-13636688, EBI-12837654;
CC P15884-3; Q9Y3C6: PPIL1; NbExp=3; IntAct=EBI-13636688, EBI-2557649;
CC P15884-3; O75771: RAD51D; NbExp=3; IntAct=EBI-13636688, EBI-1055693;
CC P15884-3; Q6P9E2: RECK; NbExp=3; IntAct=EBI-13636688, EBI-10253121;
CC P15884-3; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-13636688, EBI-16428950;
CC P15884-3; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-13636688, EBI-748350;
CC P15884-3; Q7RTU7: SCX; NbExp=3; IntAct=EBI-13636688, EBI-17492262;
CC P15884-3; O00560: SDCBP; NbExp=3; IntAct=EBI-13636688, EBI-727004;
CC P15884-3; Q9UDX3: SEC14L4; NbExp=3; IntAct=EBI-13636688, EBI-10320311;
CC P15884-3; Q96ES7: SGF29; NbExp=3; IntAct=EBI-13636688, EBI-743117;
CC P15884-3; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-13636688, EBI-2872322;
CC P15884-3; Q9Y5K1-2: SPO11; NbExp=3; IntAct=EBI-13636688, EBI-12354035;
CC P15884-3; Q9BX59: TAPBPL; NbExp=3; IntAct=EBI-13636688, EBI-12017416;
CC P15884-3; Q7RTU1: TCF23; NbExp=3; IntAct=EBI-13636688, EBI-12127592;
CC P15884-3; Q7RTU0: TCF24; NbExp=3; IntAct=EBI-13636688, EBI-18239606;
CC P15884-3; Q9UL33-2: TRAPPC2L; NbExp=3; IntAct=EBI-13636688, EBI-11119202;
CC P15884-3; Q6AZZ1: TRIM68; NbExp=3; IntAct=EBI-13636688, EBI-2130449;
CC P15884-3; Q8N7C3: TRIML2; NbExp=3; IntAct=EBI-13636688, EBI-11059915;
CC P15884-3; Q5T7W7: TSTD2; NbExp=3; IntAct=EBI-13636688, EBI-8994397;
CC P15884-3; Q9UNY4-2: TTF2; NbExp=3; IntAct=EBI-13636688, EBI-11980463;
CC P15884-3; Q8TF42: UBASH3B; NbExp=3; IntAct=EBI-13636688, EBI-1380492;
CC P15884-3; Q6UX98: ZDHHC24; NbExp=3; IntAct=EBI-13636688, EBI-10254561;
CC P15884-3; O75800: ZMYND10; NbExp=3; IntAct=EBI-13636688, EBI-747061;
CC P15884-3; Q15973: ZNF124; NbExp=3; IntAct=EBI-13636688, EBI-2555767;
CC P15884-3; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-13636688, EBI-6427977;
CC P15884-3; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-13636688, EBI-16429014;
CC P15884-3; A0A0S2Z6P0: ZNF688; NbExp=3; IntAct=EBI-13636688, EBI-16429989;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981,
CC ECO:0000269|PubMed:22777675}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=16;
CC Comment=Additional isoforms seem to exist.;
CC Name=SEF2-1B; Synonyms=B-;
CC IsoId=P15884-1; Sequence=Displayed;
CC Name=SEF2-1A; Synonyms=A+;
CC IsoId=P15884-2; Sequence=VSP_030819, VSP_002111, VSP_002112;
CC Name=SEF2-1D; Synonyms=B+;
CC IsoId=P15884-3; Sequence=VSP_002112;
CC Name=B+delta;
CC IsoId=P15884-4; Sequence=VSP_044340, VSP_002112;
CC Name=B-delta;
CC IsoId=P15884-5; Sequence=VSP_044340;
CC Name=A-;
CC IsoId=P15884-6; Sequence=VSP_044336, VSP_044337, VSP_044340;
CC Name=G-;
CC IsoId=P15884-7; Sequence=VSP_044334, VSP_044338, VSP_044339;
CC Name=H-;
CC IsoId=P15884-8; Sequence=VSP_044335, VSP_057364;
CC Name=D-;
CC IsoId=P15884-9; Sequence=VSP_045149;
CC Name=F-;
CC IsoId=P15884-10; Sequence=VSP_045151;
CC Name=11;
CC IsoId=P15884-11; Sequence=VSP_045150, VSP_044339, VSP_002112;
CC Name=E-;
CC IsoId=P15884-12; Sequence=VSP_047082, VSP_047083;
CC Name=13;
CC IsoId=P15884-13; Sequence=VSP_047081, VSP_002112;
CC Name=C-;
CC IsoId=P15884-14; Sequence=VSP_047081;
CC Name=C-delta;
CC IsoId=P15884-15; Sequence=VSP_047081, VSP_044340;
CC Name=I-;
CC IsoId=P15884-16; Sequence=VSP_054279;
CC -!- TISSUE SPECIFICITY: Expressed in adult heart, brain, placenta, skeletal
CC muscle and to a lesser extent in the lung. In developing embryonic
CC tissues, expression mostly occurs in the brain.
CC -!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a large
CC number of yeast and animal transcription factors.
CC {ECO:0000269|PubMed:17467953}.
CC -!- DISEASE: Pitt-Hopkins syndrome (PTHS) [MIM:610954]: A syndrome
CC characterized by intellectual disability, wide mouth and distinctive
CC facial features, and intermittent hyperventilation followed by apnea.
CC Features include intellectual disability with severe speech impairment,
CC normal growth parameters at birth, postnatal microcephaly, breathing
CC anomalies, severe motor developmental delay, motor incoordination,
CC ocular anomalies, constipation, seizures, typical behavior and subtle
CC brain abnormalities. {ECO:0000269|PubMed:17436254,
CC ECO:0000269|PubMed:17436255, ECO:0000269|PubMed:18728071,
CC ECO:0000269|PubMed:19235238, ECO:0000269|PubMed:20184619,
CC ECO:0000269|PubMed:22045651, ECO:0000269|PubMed:22777675,
CC ECO:0000269|PubMed:25356899}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Corneal dystrophy, Fuchs endothelial, 3 (FECD3) [MIM:613267]:
CC A late-onset form of Fuchs endothelial corneal dystrophy, a disease
CC caused by loss of endothelium of the central cornea. It is
CC characterized by focal wart-like guttata that arise from Descemet
CC membrane and develop in the central cornea, epithelial blisters,
CC reduced vision and pain. Descemet membrane is thickened by abnormal
CC collagenous deposition. {ECO:0000269|PubMed:24255041,
CC ECO:0000269|PubMed:25168903, ECO:0000269|PubMed:25593321}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Causative mutations are heterozygous TCF4 intronic trinucleotide
CC repeat expansions (CTG)n. {ECO:0000269|PubMed:24255041,
CC ECO:0000269|PubMed:25168903, ECO:0000269|PubMed:25593321}.
CC -!- DISEASE: Note=Defects in TCF4 may cause autosomal dominant symmetrical
CC acral keratoderma (SAK)syndrome. Symmetrical acral keratodermadefines
CC is characterized by brown/black hyperkeratotic patches symmetrically
CC distributed on the acral regions, especially the wrists, ankles, dorsa
CC of hands, fingers and feet affects young and middle aged men. Patients
CC have epidermis thickened by acanthosis and compact stratum
CC corneum(PubMed:28921696). {ECO:0000269|PubMed:28921696}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA60310.1; Type=Miscellaneous discrepancy; Note=Incomplete and probable erroneous sequence.; Evidence={ECO:0000305};
CC Sequence=AAA60312.1; Type=Miscellaneous discrepancy; Note=Incomplete and probable erroneous sequence.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
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DR EMBL; M74718; AAA60310.1; ALT_SEQ; mRNA.
DR EMBL; M74719; AAA60311.1; -; mRNA.
DR EMBL; M74720; AAA60312.1; ALT_SEQ; mRNA.
DR EMBL; FR748210; CBY80189.1; -; mRNA.
DR EMBL; FR748211; CBY80190.1; -; mRNA.
DR EMBL; FR748212; CBY80191.1; -; mRNA.
DR EMBL; FR748213; CBY80192.1; -; mRNA.
DR EMBL; FR748214; CBY80193.1; -; mRNA.
DR EMBL; FR748215; CBY80194.1; -; mRNA.
DR EMBL; FR748216; CBY80195.1; -; mRNA.
DR EMBL; FR748217; CBY80196.1; -; mRNA.
DR EMBL; FR748218; CBY80197.1; -; mRNA.
DR EMBL; FR748219; CBY80198.1; -; mRNA.
DR EMBL; FR748220; CBY80199.1; -; mRNA.
DR EMBL; FR748221; CBY80200.1; -; mRNA.
DR EMBL; FR748222; CBY80201.1; -; mRNA.
DR EMBL; FR748223; CBY80202.1; -; mRNA.
DR EMBL; AK095041; BAG52974.1; -; mRNA.
DR EMBL; AK096862; BAG53382.1; -; mRNA.
DR EMBL; AK299169; BAH12962.1; -; mRNA.
DR EMBL; AK300636; BAG62325.1; -; mRNA.
DR EMBL; AK300038; BAG61849.1; -; mRNA.
DR EMBL; AK301144; BAH13417.1; -; mRNA.
DR EMBL; AK300612; BAH13314.1; -; mRNA.
DR EMBL; AK316165; BAH14536.1; -; mRNA.
DR EMBL; AC013587; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC018994; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090684; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC091103; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471096; EAW63017.1; -; Genomic_DNA.
DR EMBL; CH471096; EAW63018.1; -; Genomic_DNA.
DR EMBL; BC125084; AAI25085.1; -; mRNA.
DR EMBL; BC125085; AAI25086.1; -; mRNA.
DR EMBL; AV761952; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; U75701; AAC51824.1; -; Genomic_DNA.
DR EMBL; X52079; CAA36298.1; -; mRNA.
DR CCDS; CCDS11960.1; -. [P15884-1]
DR CCDS; CCDS42438.1; -. [P15884-3]
DR CCDS; CCDS58623.1; -. [P15884-8]
DR CCDS; CCDS58624.1; -. [P15884-2]
DR CCDS; CCDS58625.1; -. [P15884-6]
DR CCDS; CCDS58626.1; -. [P15884-9]
DR CCDS; CCDS58627.1; -. [P15884-11]
DR CCDS; CCDS58628.1; -. [P15884-10]
DR CCDS; CCDS58629.1; -. [P15884-13]
DR CCDS; CCDS59321.1; -. [P15884-12]
DR CCDS; CCDS77191.1; -. [P15884-7]
DR CCDS; CCDS77192.1; -. [P15884-14]
DR PIR; A41311; A41311.
DR RefSeq; NP_001077431.1; NM_001083962.1. [P15884-3]
DR RefSeq; NP_001230155.2; NM_001243226.2.
DR RefSeq; NP_001230156.1; NM_001243227.1. [P15884-13]
DR RefSeq; NP_001230157.1; NM_001243228.1.
DR RefSeq; NP_001230159.1; NM_001243230.1. [P15884-12]
DR RefSeq; NP_001230160.1; NM_001243231.1. [P15884-10]
DR RefSeq; NP_001230161.1; NM_001243232.1. [P15884-11]
DR RefSeq; NP_001230162.1; NM_001243233.1. [P15884-9]
DR RefSeq; NP_001230163.1; NM_001243234.1. [P15884-2]
DR RefSeq; NP_001230164.1; NM_001243235.1. [P15884-6]
DR RefSeq; NP_001230165.1; NM_001243236.1. [P15884-8]
DR RefSeq; NP_001293136.1; NM_001306207.1. [P15884-14]
DR RefSeq; NP_001293137.1; NM_001306208.1. [P15884-7]
DR RefSeq; NP_001335140.1; NM_001348211.1.
DR RefSeq; NP_001335141.1; NM_001348212.1. [P15884-9]
DR RefSeq; NP_001335142.1; NM_001348213.1.
DR RefSeq; NP_001335143.1; NM_001348214.1.
DR RefSeq; NP_001335144.1; NM_001348215.1.
DR RefSeq; NP_001335145.1; NM_001348216.1.
DR RefSeq; NP_001335146.1; NM_001348217.1. [P15884-13]
DR RefSeq; NP_001335147.1; NM_001348218.1. [P15884-13]
DR RefSeq; NP_001335148.1; NM_001348219.1. [P15884-14]
DR RefSeq; NP_001335149.1; NM_001348220.1.
DR RefSeq; NP_003190.1; NM_003199.2. [P15884-1]
DR RefSeq; XP_005266796.2; XM_005266739.3.
DR RefSeq; XP_006722599.1; XM_006722536.2.
DR RefSeq; XP_006722600.1; XM_006722537.2.
DR RefSeq; XP_016881425.1; XM_017025936.1.
DR RefSeq; XP_016881429.1; XM_017025940.1.
DR RefSeq; XP_016881430.1; XM_017025941.1.
DR RefSeq; XP_016881435.1; XM_017025946.1.
DR RefSeq; XP_016881445.1; XM_017025956.1. [P15884-9]
DR PDB; 2KWF; NMR; -; B=11-27.
DR PDB; 6OD3; X-ray; 1.49 A; A/B/E/F/G/H/I/J=565-624.
DR PDB; 6OD4; X-ray; 1.70 A; A/B/G/H=565-624.
DR PDB; 6OD5; X-ray; 2.05 A; A/B/C/D=565-624.
DR PDBsum; 2KWF; -.
DR PDBsum; 6OD3; -.
DR PDBsum; 6OD4; -.
DR PDBsum; 6OD5; -.
DR AlphaFoldDB; P15884; -.
DR BMRB; P15884; -.
DR SMR; P15884; -.
DR BioGRID; 112787; 282.
DR CORUM; P15884; -.
DR DIP; DIP-163N; -.
DR IntAct; P15884; 278.
DR MINT; P15884; -.
DR STRING; 9606.ENSP00000381382; -.
DR BindingDB; P15884; -.
DR ChEMBL; CHEMBL3885541; -.
DR GlyConnect; 2086; 1 N-Linked glycan (1 site).
DR GlyGen; P15884; 1 site, 2 N-linked glycans (1 site).
DR iPTMnet; P15884; -.
DR PhosphoSitePlus; P15884; -.
DR BioMuta; TCF4; -.
DR EPD; P15884; -.
DR jPOST; P15884; -.
DR MassIVE; P15884; -.
DR MaxQB; P15884; -.
DR PaxDb; P15884; -.
DR PeptideAtlas; P15884; -.
DR PRIDE; P15884; -.
DR ProteomicsDB; 32164; -.
DR ProteomicsDB; 32165; -.
DR ProteomicsDB; 32166; -.
DR ProteomicsDB; 32167; -.
DR ProteomicsDB; 32168; -.
DR ProteomicsDB; 3668; -.
DR ProteomicsDB; 3707; -.
DR ProteomicsDB; 41559; -.
DR ProteomicsDB; 5186; -.
DR ProteomicsDB; 53237; -. [P15884-1]
DR ProteomicsDB; 53238; -. [P15884-2]
DR ProteomicsDB; 53239; -. [P15884-3]
DR ProteomicsDB; 6700; -.
DR ProteomicsDB; 6818; -.
DR Antibodypedia; 9596; 425 antibodies from 36 providers.
DR DNASU; 6925; -.
DR Ensembl; ENST00000354452.8; ENSP00000346440.3; ENSG00000196628.20. [P15884-3]
DR Ensembl; ENST00000356073.8; ENSP00000348374.4; ENSG00000196628.20. [P15884-1]
DR Ensembl; ENST00000457482.7; ENSP00000409447.2; ENSG00000196628.20. [P15884-2]
DR Ensembl; ENST00000537578.5; ENSP00000440731.1; ENSG00000196628.20. [P15884-13]
DR Ensembl; ENST00000537856.7; ENSP00000439827.2; ENSG00000196628.20. [P15884-9]
DR Ensembl; ENST00000540999.5; ENSP00000445202.1; ENSG00000196628.20. [P15884-14]
DR Ensembl; ENST00000543082.5; ENSP00000439656.1; ENSG00000196628.20. [P15884-10]
DR Ensembl; ENST00000544241.6; ENSP00000441562.2; ENSG00000196628.20. [P15884-11]
DR Ensembl; ENST00000561831.7; ENSP00000457765.1; ENSG00000196628.20. [P15884-8]
DR Ensembl; ENST00000561992.5; ENSP00000455179.1; ENSG00000196628.20. [P15884-9]
DR Ensembl; ENST00000564228.5; ENSP00000455261.1; ENSG00000196628.20. [P15884-7]
DR Ensembl; ENST00000564999.5; ENSP00000457649.1; ENSG00000196628.20. [P15884-1]
DR Ensembl; ENST00000565018.6; ENSP00000455984.2; ENSG00000196628.20. [P15884-15]
DR Ensembl; ENST00000566279.5; ENSP00000456125.1; ENSG00000196628.20. [P15884-4]
DR Ensembl; ENST00000566286.5; ENSP00000455418.2; ENSG00000196628.20. [P15884-12]
DR Ensembl; ENST00000567880.5; ENSP00000454366.1; ENSG00000196628.20. [P15884-5]
DR Ensembl; ENST00000568673.5; ENSP00000455135.1; ENSG00000196628.20. [P15884-13]
DR Ensembl; ENST00000570177.6; ENSP00000454647.1; ENSG00000196628.20. [P15884-9]
DR Ensembl; ENST00000570287.6; ENSP00000455763.1; ENSG00000196628.20. [P15884-6]
DR Ensembl; ENST00000616053.4; ENSP00000478549.1; ENSG00000196628.20. [P15884-15]
DR Ensembl; ENST00000626584.2; ENSP00000486072.1; ENSG00000196628.20. [P15884-16]
DR Ensembl; ENST00000629387.2; ENSP00000486670.1; ENSG00000196628.20. [P15884-3]
DR Ensembl; ENST00000636400.2; ENSP00000490006.1; ENSG00000196628.20. [P15884-13]
DR GeneID; 6925; -.
DR KEGG; hsa:6925; -.
DR MANE-Select; ENST00000354452.8; ENSP00000346440.3; NM_001083962.2; NP_001077431.1. [P15884-3]
DR UCSC; uc002lfw.5; human. [P15884-1]
DR CTD; 6925; -.
DR DisGeNET; 6925; -.
DR GeneCards; TCF4; -.
DR GeneReviews; TCF4; -.
DR HGNC; HGNC:11634; TCF4.
DR HPA; ENSG00000196628; Tissue enhanced (brain).
DR MalaCards; TCF4; -.
DR MIM; 602272; gene.
DR MIM; 610954; phenotype.
DR MIM; 613267; phenotype.
DR neXtProt; NX_P15884; -.
DR OpenTargets; ENSG00000196628; -.
DR Orphanet; 178469; Autosomal dominant non-syndromic intellectual disability.
DR Orphanet; 98974; Fuchs endothelial corneal dystrophy.
DR Orphanet; 2896; Pitt-Hopkins syndrome.
DR Orphanet; 171; Primary sclerosing cholangitis.
DR PharmGKB; PA164742621; -.
DR VEuPathDB; HostDB:ENSG00000196628; -.
DR eggNOG; KOG3910; Eukaryota.
DR GeneTree; ENSGT00940000159129; -.
DR InParanoid; P15884; -.
DR OrthoDB; 571132at2759; -.
DR PhylomeDB; P15884; -.
DR TreeFam; TF321672; -.
DR BRENDA; 7.6.2.3; 2681.
DR PathwayCommons; P15884; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR SignaLink; P15884; -.
DR SIGNOR; P15884; -.
DR BioGRID-ORCS; 6925; 20 hits in 1103 CRISPR screens.
DR ChiTaRS; TCF4; human.
DR EvolutionaryTrace; P15884; -.
DR GeneWiki; TCF4; -.
DR GenomeRNAi; 6925; -.
DR Pharos; P15884; Tbio.
DR PRO; PR:P15884; -.
DR Proteomes; UP000005640; Chromosome 18.
DR RNAct; P15884; protein.
DR Bgee; ENSG00000196628; Expressed in endothelial cell and 212 other tissues.
DR ExpressionAtlas; P15884; baseline and differential.
DR Genevisible; P15884; HS.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IPI:FlyBase.
DR GO; GO:0070369; C:beta-catenin-TCF7L2 complex; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:ARUK-UCL.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; ISS:BHF-UCL.
DR GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; ISS:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISS:BHF-UCL.
DR GO; GO:0070888; F:E-box binding; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0001093; F:TFIIB-class transcription factor binding; ISS:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:BHF-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0065004; P:protein-DNA complex assembly; ISS:BHF-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR IDEAL; IID00622; -.
DR InterPro; IPR011598; bHLH_dom.
DR InterPro; IPR036638; HLH_DNA-bd_sf.
DR Pfam; PF00010; HLH; 1.
DR SMART; SM00353; HLH; 1.
DR SUPFAM; SSF47459; SSF47459; 1.
DR PROSITE; PS50888; BHLH; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Corneal dystrophy;
KW Differentiation; Disease variant; DNA-binding; Epilepsy;
KW Intellectual disability; Neurogenesis; Nucleus; Phosphoprotein;
KW Primary microcephaly; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..667
FT /note="Transcription factor 4"
FT /id="PRO_0000127256"
FT DOMAIN 564..617
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 1..83
FT /note="Essential for MYOD1 inhibition"
FT /evidence="ECO:0000250"
FT REGION 24..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..321
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..400
FT /note="Leucine-zipper"
FT REGION 466..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 619..642
FT /note="Class A specific domain"
FT REGION 634..667
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 18..26
FT /note="9aaTAD"
FT COMPBIAS 28..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..124
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..319
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..488
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 513..570
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 66
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q62655"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..216
FT /note="Missing (in isoform I-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_054279"
FT VAR_SEQ 1..160
FT /note="Missing (in isoform SEF2-1A)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1681116, ECO:0000303|PubMed:21789225,
FT ECO:0000303|Ref.7"
FT /id="VSP_030819"
FT VAR_SEQ 1..130
FT /note="Missing (in isoform D-)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:21789225"
FT /id="VSP_045149"
FT VAR_SEQ 1..102
FT /note="MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVED
FT RSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQS -> MKDIF
FT FQFIIARVRKCYSLSCLHTLPVVPTLR (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045150"
FT VAR_SEQ 1..49
FT /note="MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSN ->
FT MEEDSRD (in isoform F-)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:21789225"
FT /id="VSP_045151"
FT VAR_SEQ 1..32
FT /note="MHHQQRMAALGTDKELSDLLDFSAMFSPPVSS -> MKDIFFQFIIARVRKC
FT YSLSCLHTLPVVPTLR (in isoform G-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_044334"
FT VAR_SEQ 1..24
FT /note="Missing (in isoform 13, isoform C- and isoform C-
FT delta)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:21789225"
FT /id="VSP_047081"
FT VAR_SEQ 1..24
FT /note="MHHQQRMAALGTDKELSDLLDFSA -> MQRAKTELFRLQIVTDDLRKNE
FT (in isoform E-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_047082"
FT VAR_SEQ 1..23
FT /note="MHHQQRMAALGTDKELSDLLDFS -> MYCAYTIPGMGGNSLMYYYNGKA
FT (in isoform A-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_044336"
FT VAR_SEQ 1..23
FT /note="MHHQQRMAALGTDKELSDLLDFS -> MKFKQCRCSDTGLCCLDHEGKAE
FT (in isoform H-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_044335"
FT VAR_SEQ 24..183
FT /note="Missing (in isoform H-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_057364"
FT VAR_SEQ 24..123
FT /note="Missing (in isoform A-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_044337"
FT VAR_SEQ 33..102
FT /note="Missing (in isoform G-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_044338"
FT VAR_SEQ 123
FT /note="Missing (in isoform G- and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:21789225"
FT /id="VSP_044339"
FT VAR_SEQ 124..183
FT /note="Missing (in isoform A-, isoform B-delta, isoform
FT B+delta and isoform C-delta)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_044340"
FT VAR_SEQ 161..183
FT /note="LHSSAMEVQTKKVRKVPPGLPSS -> MYCAYTIPGMGGNSLMYYYNGKA
FT (in isoform SEF2-1A)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:1681116, ECO:0000303|PubMed:21789225,
FT ECO:0000303|Ref.7"
FT /id="VSP_002111"
FT VAR_SEQ 357
FT /note="Missing (in isoform E-)"
FT /evidence="ECO:0000303|PubMed:21789225"
FT /id="VSP_047083"
FT VAR_SEQ 545
FT /note="T -> TRSRS (in isoform B+delta, isoform SEF2-1A,
FT isoform SEF2-1D, isoform 11 and isoform 13)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1681116,
FT ECO:0000303|PubMed:21789225, ECO:0000303|Ref.7"
FT /id="VSP_002112"
FT VARIANT 29
FT /note="P -> T (probable disease-associated variant found in
FT a family with symmetrical acral keratoderma)"
FT /evidence="ECO:0000269|PubMed:28921696"
FT /id="VAR_079726"
FT VARIANT 358
FT /note="G -> V (in PTHS; also expressed in the nucleus with
FT a pattern indistinguishable from the wild-type; does not
FT have a major impact on homodimer formation; affects
FT transcriptional activity in a context-dependent manner)"
FT /evidence="ECO:0000269|PubMed:18728071,
FT ECO:0000269|PubMed:22777675"
FT /id="VAR_066839"
FT VARIANT 385..667
FT /note="Missing (in PTHS)"
FT /evidence="ECO:0000269|PubMed:25356899"
FT /id="VAR_078644"
FT VARIANT 450
FT /note="M -> I (in dbSNP:rs11660217)"
FT /id="VAR_049545"
FT VARIANT 535
FT /note="D -> G (in PTHS; loss of function; also expressed in
FT the nucleus with a pattern indistinguishable from the wild-
FT type; does not have a major impact on homodimer formation;
FT affects transcriptional activity in a context-dependent
FT manner)"
FT /evidence="ECO:0000269|PubMed:19235238,
FT ECO:0000269|PubMed:22777675"
FT /id="VAR_058632"
FT VARIANT 565
FT /note="R -> W (in PTHS)"
FT /evidence="ECO:0000269|PubMed:22045651"
FT /id="VAR_066970"
FT VARIANT 572
FT /note="R -> G (in PTHS; loss of function)"
FT /evidence="ECO:0000269|PubMed:19235238,
FT ECO:0000269|PubMed:22045651"
FT /id="VAR_058633"
FT VARIANT 572
FT /note="R -> Q (in PTHS; dbSNP:rs1057521070)"
FT /evidence="ECO:0000269|PubMed:22045651"
FT /id="VAR_066971"
FT VARIANT 574
FT /note="R -> H (in PTHS; dbSNP:rs121909123)"
FT /evidence="ECO:0000269|PubMed:22045651"
FT /id="VAR_066972"
FT VARIANT 574
FT /note="R -> P (in PTHS; mislocalized to small spherical
FT punctae that are dispersed throughout the nucleus; can
FT attenuate homo- and heterodimer formation; affects
FT transcriptional activity in a context-dependent manner;
FT dbSNP:rs121909123)"
FT /evidence="ECO:0000269|PubMed:18728071,
FT ECO:0000269|PubMed:22045651, ECO:0000269|PubMed:22777675"
FT /id="VAR_066840"
FT VARIANT 576
FT /note="R -> Q (in PTHS; loss of function;
FT dbSNP:rs121909121)"
FT /evidence="ECO:0000269|PubMed:17436254,
FT ECO:0000269|PubMed:19235238, ECO:0000269|PubMed:22045651"
FT /id="VAR_034704"
FT VARIANT 576
FT /note="R -> W (in PTHS; mislocalized to small spherical
FT punctae that are dispersed throughout the nucleus; can
FT attenuate homo- and heterodimer formation; affects
FT transcriptional activity in a context-dependent manner;
FT dbSNP:rs121909120)"
FT /evidence="ECO:0000269|PubMed:17436254,
FT ECO:0000269|PubMed:17436255, ECO:0000269|PubMed:22045651,
FT ECO:0000269|PubMed:22777675"
FT /id="VAR_034705"
FT VARIANT 578
FT /note="R -> H (in PTHS)"
FT /evidence="ECO:0000269|PubMed:18728071"
FT /id="VAR_066841"
FT VARIANT 578
FT /note="R -> P (in PTHS)"
FT /evidence="ECO:0000269|PubMed:20184619,
FT ECO:0000269|PubMed:22045651"
FT /id="VAR_066973"
FT VARIANT 583
FT /note="A -> P (in PTHS)"
FT /evidence="ECO:0000269|PubMed:22045651"
FT /id="VAR_066974"
FT VARIANT 610
FT /note="A -> V (in PTHS; loss of function; mislocalized to
FT small spherical punctae that are dispersed throughout the
FT nucleus; can attenuate homo- and heterodimer formation;
FT affects transcriptional activity in a context-dependent
FT manner)"
FT /evidence="ECO:0000269|PubMed:19235238,
FT ECO:0000269|PubMed:22045651, ECO:0000269|PubMed:22777675"
FT /id="VAR_058634"
FT CONFLICT 46..49
FT /note="TGSN -> EFGG (in Ref. 9; CAA36298)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="Missing (in Ref. 7; AV761952)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="P -> S (in Ref. 9; CAA36298)"
FT /evidence="ECO:0000305"
FT HELIX 15..25
FT /evidence="ECO:0007829|PDB:2KWF"
FT HELIX 565..594
FT /evidence="ECO:0007829|PDB:6OD3"
FT HELIX 603..622
FT /evidence="ECO:0007829|PDB:6OD3"
SQ SEQUENCE 667 AA; 71308 MW; 53459FC7989D9487 CRC64;
MHHQQRMAAL GTDKELSDLL DFSAMFSPPV SSGKNGPTSL ASGHFTGSNV EDRSSSGSWG
NGGHPSPSRN YGDGTPYDHM TSRDLGSHDN LSPPFVNSRI QSKTERGSYS SYGRESNLQG
CHQQSLLGGD MDMGNPGTLS PTKPGSQYYQ YSSNNPRRRP LHSSAMEVQT KKVRKVPPGL
PSSVYAPSAS TADYNRDSPG YPSSKPATST FPSSFFMQDG HHSSDPWSSS SGMNQPGYAG
MLGNSSHIPQ SSSYCSLHPH ERLSYPSHSS ADINSSLPPM STFHRSGTNH YSTSSCTPPA
NGTDSIMANR GSGAAGSSQT GDALGKALAS IYSPDHTNNS FSSNPSTPVG SPPSLSAGTA
VWSRNGGQAS SSPNYEGPLH SLQSRIEDRL ERLDDAIHVL RNHAVGPSTA MPGGHGDMHG
IIGPSHNGAM GGLGSGYGTG LLSANRHSLM VGTHREDGVA LRGSHSLLPN QVPVPQLPVQ
SATSPDLNPP QDPYRGMPPG LQGQSVSSGS SEIKSDDEGD ENLQDTKSSE DKKLDDDKKD
IKSITSNNDD EDLTPEQKAE REKERRMANN ARERLRVRDI NEAFKELGRM VQLHLKSDKP
QTKLLILHQA VAVILSLEQQ VRERNLNPKA ACLKRREEEK VSSEPPPLSL AGPHPGMGDA
SNHMGQM
