HTF4_HUMAN
ID HTF4_HUMAN Reviewed; 682 AA.
AC Q99081; B4E1W1; Q7Z3D9; Q86TC1; Q86VM2;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Transcription factor 12;
DE Short=TCF-12;
DE AltName: Full=Class B basic helix-loop-helix protein 20;
DE Short=bHLHb20;
DE AltName: Full=DNA-binding protein HTF4;
DE AltName: Full=E-box-binding protein;
DE AltName: Full=Transcription factor HTF-4;
GN Name=TCF12; Synonyms=BHLHB20, HEB, HTF4;
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] (ISOFORM 1).
RX PubMed=1446075; DOI=10.3109/10425179209020819;
RA Zhang Y., Bina M.;
RT "The nucleotide sequence of the human transcription factor HTF4a cDNA.";
RL DNA Seq. 2:397-403(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Skeletal muscle;
RX PubMed=1312219; DOI=10.1128/mcb.12.3.1031-1042.1992;
RA Hu J.S., Olson E.N., Kingston R.E.;
RT "HEB, a helix-loop-helix protein related to E2A and ITF2 that can modulate
RT the DNA-binding ability of myogenic regulatory factors.";
RL Mol. Cell. Biol. 12:1031-1042(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Trachea;
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 MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Endometrium, and Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 352-682.
RX PubMed=1886779; DOI=10.1093/nar/19.16.4555;
RA Zhang Y., Babin J., Feldhaus A.L., Singh H., Sharp P.A., Bina M.;
RT "HTF4: a new human helix-loop-helix protein.";
RL Nucleic Acids Res. 19:4555-4555(1991).
RN [9]
RP GENE ORGANIZATION, AND ALTERNATIVE SPLICING.
RX PubMed=12826747; DOI=10.1159/000071042;
RA Gan T.I., Rowen L., Nesbitt R., Roe B.A., Wu H., Hu P., Yao Z., Kim U.J.,
RA O'Sickey T., Bina M.;
RT "Genomic organization of human TCF12 gene and spliced mRNA variants
RT producing isoforms of transcription factor HTF4.";
RL Cytogenet. Genome Res. 98:245-248(2002).
RN [10]
RP INTERACTION WITH RUNX1T1.
RX PubMed=16616331; DOI=10.1016/j.ccr.2006.03.012;
RA Liu Y., Cheney M.D., Gaudet J.J., Chruszcz M., Lukasik S.M., Sugiyama D.,
RA Lary J., Cole J., Dauter Z., Minor W., Speck N.A., Bushweller J.H.;
RT "The tetramer structure of the Nervy homology two domain, NHR2, is critical
RT for AML1/ETO's activity.";
RL Cancer Cell 9:249-260(2006).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-313, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-333 AND THR-557, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-67; SER-79; SER-98;
RP SER-116; THR-313; SER-333; SER-540; SER-558 AND SER-559, AND IDENTIFICATION
RP 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 [20]
RP IDENTIFICATION BY 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 [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-519 AND LYS-550, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-519, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-110; LYS-181; LYS-519; LYS-609
RP AND LYS-653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [24]
RP X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 177-200 IN COMPLEX WITH RUNX1T1,
RP INTERACTION WITH AML1-MTG8/ETO, AND MUTAGENESIS OF PRO-187; PRO-191 AND
RP SER-192.
RX PubMed=23812588; DOI=10.1038/nature12287;
RA Sun X.J., Wang Z., Wang L., Jiang Y., Kost N., Soong T.D., Chen W.Y.,
RA Tang Z., Nakadai T., Elemento O., Fischle W., Melnick A., Patel D.J.,
RA Nimer S.D., Roeder R.G.;
RT "A stable transcription factor complex nucleated by oligomeric AML1-ETO
RT controls leukaemogenesis.";
RL Nature 500:93-97(2013).
RN [25]
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 [26]
RP STRUCTURE BY NMR OF 11-28 IN COMPLEX WITH RUNX1T1, AND SUBUNIT.
RX PubMed=19204326; DOI=10.1182/blood-2008-06-161307;
RA Park S., Chen W., Cierpicki T., Tonelli M., Cai X., Speck N.A.,
RA Bushweller J.H.;
RT "Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its
RT contribution to AML1-ETO activity.";
RL Blood 113:3558-3567(2009).
RN [27]
RP VARIANTS CRS3 PRO-600 AND GLU-614.
RX PubMed=23354436; DOI=10.1038/ng.2531;
RG 500 Whole-Genome Sequences (WGS500) Consortium;
RA Sharma V.P., Fenwick A.L., Brockop M.S., McGowan S.J., Goos J.A.,
RA Hoogeboom A.J., Brady A.F., Jeelani N.O., Lynch S.A., Mulliken J.B.,
RA Murray D.J., Phipps J.M., Sweeney E., Tomkins S.E., Wilson L.C.,
RA Bennett S., Cornall R.J., Broxholme J., Kanapin A., Johnson D., Wall S.A.,
RA van der Spek P.J., Mathijssen I.M., Maxson R.E., Twigg S.R., Wilkie A.O.;
RT "Mutations in TCF12, encoding a basic helix-loop-helix partner of TWIST1,
RT are a frequent cause of coronal craniosynostosis.";
RL Nat. Genet. 45:304-307(2013).
RN [28]
RP VARIANT CRS3 ARG-483.
RX PubMed=25271085; DOI=10.1038/ejhg.2014.205;
RA Paumard-Hernandez B., Berges-Soria J., Barroso E., Rivera-Pedroza C.I.,
RA Perez-Carrizosa V., Benito-Sanz S., Lopez-Messa E., Santos F.,
RA Garcia-Recuero I.I., Romance A., Ballesta-Martinez J.M., Lopez-Gonzalez V.,
RA Campos-Barros A., Cruz J., Guillen-Navarro E., Sanchez Del Pozo J.,
RA Lapunzina P., Garcia-Minaur S., Heath K.E.;
RT "Expanding the mutation spectrum in 182 Spanish probands with
RT craniosynostosis: identification and characterization of novel TCF12
RT variants.";
RL Eur. J. Hum. Genet. 23:907-914(2015).
CC -!- FUNCTION: Transcriptional regulator. Involved in the initiation of
CC neuronal differentiation. Activates transcription by binding to the E
CC box (5'-CANNTG-3').
CC -!- SUBUNIT: Efficient DNA binding requires dimerization with another bHLH
CC protein. Forms homo- or heterooligomers with myogenin, E12 and ITF2
CC proteins. Interacts with PTF1A. Interacts with NEUROD2 (By similarity).
CC Interacts with RUNX1T1. Interacts with AML1-MTG8/ETO (via nervy
CC homology region 2 in oligomerized form) (PubMed:23812588). Interacts
CC with BHLHA9 (PubMed:25466284). {ECO:0000250|UniProtKB:Q61286,
CC ECO:0000269|PubMed:16616331, ECO:0000269|PubMed:19204326,
CC ECO:0000269|PubMed:23812588, ECO:0000269|PubMed:25466284}.
CC -!- INTERACTION:
CC Q99081; Q8IUR7: ARMC8; NbExp=3; IntAct=EBI-722877, EBI-1049469;
CC Q99081; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-722877, EBI-10254793;
CC Q99081; Q96MC5: BMERB1; NbExp=3; IntAct=EBI-722877, EBI-718468;
CC Q99081; Q9NX04: C1orf109; NbExp=3; IntAct=EBI-722877, EBI-8643161;
CC Q99081; P42773: CDKN2C; NbExp=5; IntAct=EBI-722877, EBI-711290;
CC Q99081; Q8IYR0: CFAP206; NbExp=3; IntAct=EBI-722877, EBI-749051;
CC Q99081; O75575: CRCP; NbExp=3; IntAct=EBI-722877, EBI-2654687;
CC Q99081; Q3B7T1-5: EDRF1; NbExp=3; IntAct=EBI-722877, EBI-10240074;
CC Q99081; O75593: FOXH1; NbExp=2; IntAct=EBI-722877, EBI-1759806;
CC Q99081; Q96MH2: HEXIM2; NbExp=4; IntAct=EBI-722877, EBI-5460660;
CC Q99081; Q9BPY8: HOPX; NbExp=3; IntAct=EBI-722877, EBI-10295883;
CC Q99081; P41134: ID1; NbExp=3; IntAct=EBI-722877, EBI-1215527;
CC Q99081; Q02363: ID2; NbExp=2; IntAct=EBI-722877, EBI-713450;
CC Q99081; Q02535: ID3; NbExp=5; IntAct=EBI-722877, EBI-1387094;
CC Q99081; Q96S90: LYSMD1; NbExp=3; IntAct=EBI-722877, EBI-10293291;
CC Q99081; O60336: MAPKBP1; NbExp=3; IntAct=EBI-722877, EBI-947402;
CC Q99081; Q6P2C6: MLLT6; NbExp=3; IntAct=EBI-722877, EBI-5773143;
CC Q99081; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-722877, EBI-10269566;
CC Q99081; Q8WVZ3: MORN4; NbExp=3; IntAct=EBI-722877, EBI-10277137;
CC Q99081; Q9UJ70: NAGK; NbExp=3; IntAct=EBI-722877, EBI-372578;
CC Q99081; Q9Y4Z2: NEUROG3; NbExp=4; IntAct=EBI-722877, EBI-10328570;
CC Q99081; Q9UJX0: OSGIN1; NbExp=4; IntAct=EBI-722877, EBI-9057006;
CC Q99081; P25786: PSMA1; NbExp=4; IntAct=EBI-722877, EBI-359352;
CC Q99081; P47897: QARS1; NbExp=4; IntAct=EBI-722877, EBI-347462;
CC Q99081; P47897-2: QARS1; NbExp=3; IntAct=EBI-722877, EBI-10209725;
CC Q99081; Q1RLL8: RNASEL; NbExp=3; IntAct=EBI-722877, EBI-10239181;
CC Q99081; Q9NZD8: SPG21; NbExp=4; IntAct=EBI-722877, EBI-742688;
CC Q99081; P30626: SRI; NbExp=3; IntAct=EBI-722877, EBI-750459;
CC Q99081; P42229: STAT5A; NbExp=3; IntAct=EBI-722877, EBI-749537;
CC Q99081; O75716: STK16; NbExp=3; IntAct=EBI-722877, EBI-749295;
CC Q99081; P17542: TAL1; NbExp=6; IntAct=EBI-722877, EBI-1753878;
CC Q99081; Q6ZMU5: TRIM72; NbExp=3; IntAct=EBI-722877, EBI-2341648;
CC Q99081; Q99598: TSNAX; NbExp=3; IntAct=EBI-722877, EBI-742638;
CC Q99081; Q8WVJ9: TWIST2; NbExp=3; IntAct=EBI-722877, EBI-1797313;
CC Q99081; Q548N1: VPS28; NbExp=3; IntAct=EBI-722877, EBI-10243107;
CC Q99081-3; Q0P5N6: ARL16; NbExp=3; IntAct=EBI-11952764, EBI-10186132;
CC Q99081-3; Q9NQ33: ASCL3; NbExp=3; IntAct=EBI-11952764, EBI-12108222;
CC Q99081-3; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-11952764, EBI-10254793;
CC Q99081-3; P51946: CCNH; NbExp=3; IntAct=EBI-11952764, EBI-741406;
CC Q99081-3; Q86Y33-5: CDC20B; NbExp=3; IntAct=EBI-11952764, EBI-11983537;
CC Q99081-3; P42773: CDKN2C; NbExp=4; IntAct=EBI-11952764, EBI-711290;
CC Q99081-3; P61024: CKS1B; NbExp=3; IntAct=EBI-11952764, EBI-456371;
CC Q99081-3; P51800-3: CLCNKA; NbExp=3; IntAct=EBI-11952764, EBI-11980535;
CC Q99081-3; P26196: DDX6; NbExp=3; IntAct=EBI-11952764, EBI-351257;
CC Q99081-3; O15197-2: EPHB6; NbExp=3; IntAct=EBI-11952764, EBI-10182490;
CC Q99081-3; Q8IYI6: EXOC8; NbExp=3; IntAct=EBI-11952764, EBI-742102;
CC Q99081-3; Q9Y247: FAM50B; NbExp=3; IntAct=EBI-11952764, EBI-742802;
CC Q99081-3; Q6QHK4: FIGLA; NbExp=3; IntAct=EBI-11952764, EBI-11976617;
CC Q99081-3; Q14451-3: GRB7; NbExp=3; IntAct=EBI-11952764, EBI-11991632;
CC Q99081-3; Q969Y2: GTPBP3; NbExp=3; IntAct=EBI-11952764, EBI-740290;
CC Q99081-3; O96004: HAND1; NbExp=3; IntAct=EBI-11952764, EBI-11320290;
CC Q99081-3; P61296-2: HAND2; NbExp=3; IntAct=EBI-11952764, EBI-13086076;
CC Q99081-3; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-11952764, EBI-14103818;
CC Q99081-3; Q96MH2: HEXIM2; NbExp=4; IntAct=EBI-11952764, EBI-5460660;
CC Q99081-3; P41134: ID1; NbExp=3; IntAct=EBI-11952764, EBI-1215527;
CC Q99081-3; Q02535: ID3; NbExp=4; IntAct=EBI-11952764, EBI-1387094;
CC Q99081-3; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-11952764, EBI-739832;
CC Q99081-3; Q8NDC4: MORN4; NbExp=3; IntAct=EBI-11952764, EBI-10269566;
CC Q99081-3; O60682: MSC; NbExp=3; IntAct=EBI-11952764, EBI-740310;
CC Q99081-3; A6NI15: MSGN1; NbExp=3; IntAct=EBI-11952764, EBI-11991020;
CC Q99081-3; Q9HC98-4: NEK6; NbExp=3; IntAct=EBI-11952764, EBI-11750983;
CC Q99081-3; Q13562: NEUROD1; NbExp=4; IntAct=EBI-11952764, EBI-3908303;
CC Q99081-3; Q92886: NEUROG1; NbExp=3; IntAct=EBI-11952764, EBI-10279647;
CC Q99081-3; Q9Y4Z2: NEUROG3; NbExp=7; IntAct=EBI-11952764, EBI-10328570;
CC Q99081-3; Q96IV0: NGLY1; NbExp=3; IntAct=EBI-11952764, EBI-6165879;
CC Q99081-3; Q02577: NHLH2; NbExp=3; IntAct=EBI-11952764, EBI-5378683;
CC Q99081-3; Q13526: PIN1; NbExp=3; IntAct=EBI-11952764, EBI-714158;
CC Q99081-3; O43741: PRKAB2; NbExp=3; IntAct=EBI-11952764, EBI-1053424;
CC Q99081-3; Q9Y5S9: RBM8A; NbExp=3; IntAct=EBI-11952764, EBI-447231;
CC Q99081-3; Q06455-4: RUNX1T1; NbExp=2; IntAct=EBI-11952764, EBI-10224192;
CC Q99081-3; O14796: SH2D1B; NbExp=3; IntAct=EBI-11952764, EBI-3923013;
CC Q99081-3; Q8IYX1: TBC1D21; NbExp=3; IntAct=EBI-11952764, EBI-12018146;
CC Q99081-3; O43680: TCF21; NbExp=3; IntAct=EBI-11952764, EBI-723267;
CC Q99081-3; Q7RTU1: TCF23; NbExp=3; IntAct=EBI-11952764, EBI-12127592;
CC Q99081-3; Q6ZMU5: TRIM72; NbExp=3; IntAct=EBI-11952764, EBI-2341648;
CC Q99081-3; Q99598: TSNAX; NbExp=3; IntAct=EBI-11952764, EBI-742638;
CC Q99081-3; Q9UNY4-2: TTF2; NbExp=3; IntAct=EBI-11952764, EBI-11980463;
CC Q99081-3; Q8WVJ9: TWIST2; NbExp=3; IntAct=EBI-11952764, EBI-1797313;
CC Q99081-3; Q9UK41: VPS28; NbExp=3; IntAct=EBI-11952764, EBI-727424;
CC Q99081-3; Q15007: WTAP; NbExp=3; IntAct=EBI-11952764, EBI-751647;
CC Q99081-3; A0A0S2Z6P0: ZNF688; NbExp=3; IntAct=EBI-11952764, EBI-16429989;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=a;
CC IsoId=Q99081-1; Sequence=Displayed;
CC Name=2; Synonyms=b;
CC IsoId=Q99081-2; Sequence=VSP_039109, VSP_039110;
CC Name=3; Synonyms=c;
CC IsoId=Q99081-3; Sequence=VSP_040024;
CC Name=4;
CC IsoId=Q99081-4; Sequence=VSP_057419, VSP_057420;
CC -!- TISSUE SPECIFICITY: Expressed in several tissues and cell types
CC including skeletal muscle, thymus, and a B-cell line.
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: Craniosynostosis 3 (CRS3) [MIM:615314]: A primary abnormality
CC of skull growth involving premature fusion of one or more cranial
CC sutures. The growth velocity of the skull often cannot match that of
CC the developing brain resulting in an abnormal head shape and, in some
CC cases, increased intracranial pressure, which must be treated promptly
CC to avoid permanent neurodevelopmental disability.
CC {ECO:0000269|PubMed:23354436, ECO:0000269|PubMed:25271085}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TCF12ID406.html";
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DR EMBL; M83233; AAB62389.1; -; mRNA.
DR EMBL; M80627; AAA58632.1; -; mRNA.
DR EMBL; AL831981; CAD89914.1; -; mRNA.
DR EMBL; AK304007; BAG64923.1; -; mRNA.
DR EMBL; BX537967; CAD97931.1; -; mRNA.
DR EMBL; AC010999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC016525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471082; EAW77512.1; -; Genomic_DNA.
DR EMBL; BC050556; AAH50556.1; -; mRNA.
DR EMBL; M65209; AAC37571.1; -; mRNA.
DR EMBL; BK001049; DAA01129.1; -; mRNA.
DR CCDS; CCDS10159.1; -. [Q99081-1]
DR CCDS; CCDS10160.1; -. [Q99081-3]
DR CCDS; CCDS42042.1; -. [Q99081-2]
DR CCDS; CCDS76761.1; -. [Q99081-4]
DR PIR; A42121; A42121.
DR RefSeq; NP_001293149.1; NM_001306220.2. [Q99081-4]
DR RefSeq; NP_001309080.1; NM_001322151.1. [Q99081-3]
DR RefSeq; NP_001309086.1; NM_001322157.1. [Q99081-1]
DR RefSeq; NP_001309088.1; NM_001322159.1. [Q99081-3]
DR RefSeq; NP_001309091.1; NM_001322162.1. [Q99081-3]
DR RefSeq; NP_001309094.1; NM_001322165.1. [Q99081-1]
DR RefSeq; NP_003196.1; NM_003205.3. [Q99081-1]
DR RefSeq; NP_996919.1; NM_207036.1. [Q99081-3]
DR RefSeq; NP_996920.1; NM_207037.1. [Q99081-3]
DR RefSeq; NP_996921.1; NM_207038.1. [Q99081-1]
DR RefSeq; NP_996923.1; NM_207040.1. [Q99081-2]
DR PDB; 2KNH; NMR; -; B=11-28.
DR PDB; 4JOL; X-ray; 2.91 A; E/F/G/H=177-200.
DR PDBsum; 2KNH; -.
DR PDBsum; 4JOL; -.
DR AlphaFoldDB; Q99081; -.
DR BMRB; Q99081; -.
DR SMR; Q99081; -.
DR BioGRID; 112798; 123.
DR CORUM; Q99081; -.
DR DIP; DIP-29403N; -.
DR IntAct; Q99081; 104.
DR MINT; Q99081; -.
DR STRING; 9606.ENSP00000388940; -.
DR GlyGen; Q99081; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q99081; -.
DR PhosphoSitePlus; Q99081; -.
DR BioMuta; TCF12; -.
DR DMDM; 1708332; -.
DR EPD; Q99081; -.
DR jPOST; Q99081; -.
DR MassIVE; Q99081; -.
DR MaxQB; Q99081; -.
DR PaxDb; Q99081; -.
DR PeptideAtlas; Q99081; -.
DR PRIDE; Q99081; -.
DR ProteomicsDB; 5790; -.
DR ProteomicsDB; 78231; -. [Q99081-1]
DR ProteomicsDB; 78232; -. [Q99081-2]
DR ProteomicsDB; 78233; -. [Q99081-3]
DR Antibodypedia; 913; 413 antibodies from 35 providers.
DR DNASU; 6938; -.
DR Ensembl; ENST00000267811.9; ENSP00000267811.5; ENSG00000140262.18. [Q99081-1]
DR Ensembl; ENST00000333725.10; ENSP00000331057.6; ENSG00000140262.18. [Q99081-3]
DR Ensembl; ENST00000343827.7; ENSP00000342459.3; ENSG00000140262.18. [Q99081-2]
DR Ensembl; ENST00000438423.6; ENSP00000388940.2; ENSG00000140262.18. [Q99081-3]
DR Ensembl; ENST00000537840.5; ENSP00000444696.1; ENSG00000140262.18. [Q99081-4]
DR Ensembl; ENST00000557843.5; ENSP00000453737.1; ENSG00000140262.18. [Q99081-1]
DR GeneID; 6938; -.
DR KEGG; hsa:6938; -.
DR MANE-Select; ENST00000333725.10; ENSP00000331057.6; NM_207037.2; NP_996920.1. [Q99081-3]
DR UCSC; uc002aea.4; human. [Q99081-1]
DR UCSC; uc010ugo.3; human.
DR CTD; 6938; -.
DR DisGeNET; 6938; -.
DR GeneCards; TCF12; -.
DR HGNC; HGNC:11623; TCF12.
DR HPA; ENSG00000140262; Low tissue specificity.
DR MalaCards; TCF12; -.
DR MIM; 600480; gene.
DR MIM; 615314; phenotype.
DR neXtProt; NX_Q99081; -.
DR OpenTargets; ENSG00000140262; -.
DR Orphanet; 209916; Extraskeletal myxoid chondrosarcoma.
DR Orphanet; 35099; Non-syndromic bicoronal craniosynostosis.
DR PharmGKB; PA36381; -.
DR VEuPathDB; HostDB:ENSG00000140262; -.
DR eggNOG; KOG3910; Eukaryota.
DR GeneTree; ENSGT00940000155047; -.
DR HOGENOM; CLU_021099_2_0_1; -.
DR InParanoid; Q99081; -.
DR OMA; XKTSERG; -.
DR OrthoDB; 571132at2759; -.
DR PhylomeDB; Q99081; -.
DR TreeFam; TF321672; -.
DR PathwayCommons; Q99081; -.
DR Reactome; R-HSA-525793; Myogenesis.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9031628; NGF-stimulated transcription.
DR SignaLink; Q99081; -.
DR SIGNOR; Q99081; -.
DR BioGRID-ORCS; 6938; 20 hits in 1104 CRISPR screens.
DR ChiTaRS; TCF12; human.
DR EvolutionaryTrace; Q99081; -.
DR GeneWiki; TCF12; -.
DR GenomeRNAi; 6938; -.
DR Pharos; Q99081; Tbio.
DR PRO; PR:Q99081; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q99081; protein.
DR Bgee; ENSG00000140262; Expressed in periodontal ligament and 202 other tissues.
DR ExpressionAtlas; Q99081; baseline and differential.
DR Genevisible; Q99081; HS.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0035497; F:cAMP response element binding; IEA:Ensembl.
DR GO; GO:0000987; F:cis-regulatory region sequence-specific DNA binding; IC:BHF-UCL.
DR GO; GO:0001228; F:DNA-binding transcription activator activity, RNA polymerase II-specific; IDA:NTNU_SB.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; ISA:NTNU_SB.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0070888; F:E-box binding; IEA:Ensembl.
DR GO; GO:0071837; F:HMG box domain binding; IEA:Ensembl.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; IDA:ARUK-UCL.
DR GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0010467; P:gene expression; IEA:Ensembl.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR GO; GO:0045666; P:positive regulation of neuron differentiation; IEA:Ensembl.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:NTNU_SB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR Gene3D; 4.10.280.10; -; 1.
DR IDEAL; IID00222; -.
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; Alternative splicing; Craniosynostosis;
KW Developmental protein; Differentiation; Disease variant; DNA-binding;
KW Isopeptide bond; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..682
FT /note="Transcription factor 12"
FT /id="PRO_0000127228"
FT DOMAIN 577..630
FT /note="bHLH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00981"
FT REGION 25..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..140
FT /note="Leucine-zipper"
FT REGION 140..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..196
FT /note="Interaction with RUNX1T1"
FT /evidence="ECO:0000269|PubMed:23812588"
FT REGION 281..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..395
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..580
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 632..655
FT /note="Class A specific domain"
FT REGION 651..682
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 19..27
FT /note="9aaTAD"
FT COMPBIAS 29..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..122
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..167
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..550
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 557..580
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..682
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 313
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 557
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 181
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 519
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 550
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT CROSSLNK 609
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 653
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039109"
FT VAR_SEQ 1..39
FT /note="MNPQQQRMAAIGTDKELSDLLDFSAMFSPPVNSGKTRPT -> MGKRYMHHP
FT QIQMISTVNLLVIHLLSHQPVCSLALSLCK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057419"
FT VAR_SEQ 40..275
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057420"
FT VAR_SEQ 171..193
FT /note="DSAALDPLQAKKVRKVPPGLPSS -> MYCAYPVPGMGSNSLMYYYNGKT
FT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_039110"
FT VAR_SEQ 396
FT /note="L -> LKNRVEQQLHEHLQDAMSFLKDVCE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040024"
FT VARIANT 300
FT /note="G -> S (in dbSNP:rs12442879)"
FT /id="VAR_049543"
FT VARIANT 483
FT /note="L -> R (in CRS3; dbSNP:rs36060670)"
FT /evidence="ECO:0000269|PubMed:25271085"
FT /id="VAR_072271"
FT VARIANT 600
FT /note="L -> P (in CRS3)"
FT /evidence="ECO:0000269|PubMed:23354436"
FT /id="VAR_070096"
FT VARIANT 614
FT /note="Q -> E (in CRS3; dbSNP:rs886037641)"
FT /evidence="ECO:0000269|PubMed:23354436"
FT /id="VAR_070097"
FT MUTAGEN 187
FT /note="P->A: Decreases interaction with RUNX1T1."
FT /evidence="ECO:0000269|PubMed:23812588"
FT MUTAGEN 191
FT /note="P->A: Decreases interaction with RUNX1T1."
FT /evidence="ECO:0000269|PubMed:23812588"
FT MUTAGEN 192
FT /note="S->A: Decreases interaction with RUNX1T1."
FT /evidence="ECO:0000269|PubMed:23812588"
FT CONFLICT 523
FT /note="K -> E (in Ref. 4; CAD89914)"
FT /evidence="ECO:0000305"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2KNH"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:2KNH"
SQ SEQUENCE 682 AA; 72965 MW; 9736113D9361D3F5 CRC64;
MNPQQQRMAA IGTDKELSDL LDFSAMFSPP VNSGKTRPTT LGSSQFSGSG IDERGGTTSW
GTSGQPSPSY DSSRGFTDSP HYSDHLNDSR LGAHEGLSPT PFMNSNLMGK TSERGSFSLY
SRDTGLPGCQ SSLLRQDLGL GSPAQLSSSG KPGTAYYSFS ATSSRRRPLH DSAALDPLQA
KKVRKVPPGL PSSVYAPSPN SDDFNRESPS YPSPKPPTSM FASTFFMQDG THNSSDLWSS
SNGMSQPGFG GILGTSTSHM SQSSSYGNLH SHDRLSYPPH SVSPTDINTS LPPMSSFHRG
STSSSPYVAA SHTPPINGSD SILGTRGNAA GSSQTGDALG KALASIYSPD HTSSSFPSNP
STPVGSPSPL TGTSQWPRPG GQAPSSPSYE NSLHSLQSRM EDRLDRLDDA IHVLRNHAVG
PSTSLPAGHS DIHSLLGPSH NAPIGSLNSN YGGSSLVASS RSASMVGTHR EDSVSLNGNH
SVLSSTVTTS STDLNHKTQE NYRGGLQSQS GTVVTTEIKT ENKEKDENLH EPPSSDDMKS
DDESSQKDIK VSSRGRTSST NEDEDLNPEQ KIEREKERRM ANNARERLRV RDINEAFKEL
GRMCQLHLKS EKPQTKLLIL HQAVAVILSL EQQVRERNLN PKAACLKRRE EEKVSAVSAE
PPTTLPGTHP GLSETTNPMG HM
