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Transcription factor 12 (TCF-12) (Class B basic helix-loop-helix protein 20) (bHLHb20) (DNA-binding protein HTF4) (E-box-binding protein) (Transcription factor HTF-4)

 HTF4_HUMAN              Reviewed;         682 AA.
Q99081; B4E1W1; Q7Z3D9; Q86TC1; Q86VM2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
25-OCT-2017, entry version 166.
RecName: Full=Transcription factor 12;
Short=TCF-12;
AltName: Full=Class B basic helix-loop-helix protein 20;
Short=bHLHb20;
AltName: Full=DNA-binding protein HTF4;
AltName: Full=E-box-binding protein;
AltName: Full=Transcription factor HTF-4;
Name=TCF12; Synonyms=BHLHB20, HEB, HTF4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1446075; DOI=10.3109/10425179209020819;
Zhang Y., Bina M.;
"The nucleotide sequence of the human transcription factor HTF4a
cDNA.";
DNA Seq. 2:397-403(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Skeletal muscle;
PubMed=1312219; DOI=10.1128/MCB.12.3.1031;
Hu J.S., Olson E.N., Kingston R.E.;
"HEB, a helix-loop-helix protein related to E2A and ITF2 that can
modulate the DNA-binding ability of myogenic regulatory factors.";
Mol. Cell. Biol. 12:1031-1042(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Trachea;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Endometrium, and Skeletal muscle;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 352-682.
PubMed=1886779; DOI=10.1093/nar/19.16.4555;
Zhang Y., Babin J., Feldhaus A.L., Singh H., Sharp P.A., Bina M.;
"HTF4: a new human helix-loop-helix protein.";
Nucleic Acids Res. 19:4555-4555(1991).
[9]
GENE ORGANIZATION, AND ALTERNATIVE SPLICING.
PubMed=12826747; DOI=10.1159/000071042;
Gan T.I., Rowen L., Nesbitt R., Roe B.A., Wu H., Hu P., Yao Z.,
Kim U.J., O'Sickey T., Bina M.;
"Genomic organization of human TCF12 gene and spliced mRNA variants
producing isoforms of transcription factor HTF4.";
Cytogenet. Genome Res. 98:245-248(2002).
[10]
INTERACTION WITH RUNX1T1.
PubMed=16616331; DOI=10.1016/j.ccr.2006.03.012;
Liu Y., Cheney M.D., Gaudet J.J., Chruszcz M., Lukasik S.M.,
Sugiyama D., Lary J., Cole J., Dauter Z., Minor W., Speck N.A.,
Bushweller J.H.;
"The tetramer structure of the Nervy homology two domain, NHR2, is
critical for AML1/ETO's activity.";
Cancer Cell 9:249-260(2006).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[12]
DOMAIN.
PubMed=17467953; DOI=10.1016/j.ygeno.2007.02.003;
Piskacek S., Gregor M., Nemethova M., Grabner M., Kovarik P.,
Piskacek M.;
"Nine-amino-acid transactivation domain: establishment and prediction
utilities.";
Genomics 89:756-768(2007).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-313, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67; SER-333 AND THR-557,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-559, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-47; SER-67; SER-79;
SER-98; SER-116; THR-313; SER-333; SER-540; SER-558 AND SER-559, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-519 AND LYS-550, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-519, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-110; LYS-181; LYS-519;
LYS-609 AND LYS-653, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[24]
X-RAY CRYSTALLOGRAPHY (2.91 ANGSTROMS) OF 177-200 IN COMPLEX WITH
RUNX1T1, INTERACTION WITH AML1-MTG8/ETO, AND MUTAGENESIS OF PRO-187;
PRO-191 AND SER-192.
PubMed=23812588; DOI=10.1038/nature12287;
Sun X.J., Wang Z., Wang L., Jiang Y., Kost N., Soong T.D., Chen W.Y.,
Tang Z., Nakadai T., Elemento O., Fischle W., Melnick A., Patel D.J.,
Nimer S.D., Roeder R.G.;
"A stable transcription factor complex nucleated by oligomeric AML1-
ETO controls leukaemogenesis.";
Nature 500:93-97(2013).
[25]
INTERACTION WITH BHLHA9.
PubMed=25466284; DOI=10.1016/j.ajhg.2014.10.012;
Malik S., Percin F.E., Bornholdt D., Albrecht B., Percesepe A.,
Koch M.C., Landi A., Fritz B., Khan R., Mumtaz S., Akarsu N.A.,
Grzeschik K.H.;
"Mutations affecting the BHLHA9 DNA-binding domain cause MSSD,
mesoaxial synostotic syndactyly with phalangeal reduction, Malik-
Percin type.";
Am. J. Hum. Genet. 95:649-659(2014).
[26]
STRUCTURE BY NMR OF 11-28 IN COMPLEX WITH RUNX1T1, AND SUBUNIT.
PubMed=19204326; DOI=10.1182/blood-2008-06-161307;
Park S., Chen W., Cierpicki T., Tonelli M., Cai X., Speck N.A.,
Bushweller J.H.;
"Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its
contribution to AML1-ETO activity.";
Blood 113:3558-3567(2009).
[27]
VARIANTS CRS3 PRO-600 AND GLU-614.
PubMed=23354436; DOI=10.1038/ng.2531;
500 Whole-Genome Sequences (WGS500) Consortium;
Sharma V.P., Fenwick A.L., Brockop M.S., McGowan S.J., Goos J.A.,
Hoogeboom A.J., Brady A.F., Jeelani N.O., Lynch S.A., Mulliken J.B.,
Murray D.J., Phipps J.M., Sweeney E., Tomkins S.E., Wilson L.C.,
Bennett S., Cornall R.J., Broxholme J., Kanapin A., Johnson D.,
Wall S.A., van der Spek P.J., Mathijssen I.M., Maxson R.E.,
Twigg S.R., Wilkie A.O.;
"Mutations in TCF12, encoding a basic helix-loop-helix partner of
TWIST1, are a frequent cause of coronal craniosynostosis.";
Nat. Genet. 45:304-307(2013).
[28]
VARIANT CRS3 ARG-483.
PubMed=25271085; DOI=10.1038/ejhg.2014.205;
Paumard-Hernandez B., Berges-Soria J., Barroso E.,
Rivera-Pedroza C.I., Perez-Carrizosa V., Benito-Sanz S.,
Lopez-Messa E., Santos F., Garcia-Recuero I.I., Romance A.,
Ballesta-Martinez J.M., Lopez-Gonzalez V., Campos-Barros A., Cruz J.,
Guillen-Navarro E., Sanchez Del Pozo J., Lapunzina P.,
Garcia-Minaur S., Heath K.E.;
"Expanding the mutation spectrum in 182 Spanish probands with
craniosynostosis: identification and characterization of novel TCF12
variants.";
Eur. J. Hum. Genet. 23:907-914(2015).
-!- FUNCTION: Transcriptional regulator. Involved in the initiation of
neuronal differentiation. Activates transcription by binding to
the E box (5'-CANNTG-3').
-!- SUBUNIT: Efficient DNA binding requires dimerization with another
bHLH protein. Forms homo- or heterooligomers with myogenin, E12
and ITF2 proteins. Interacts with PTF1A. Interacts with NEUROD2
(By similarity). Interacts with RUNX1T1. Interacts with AML1-
MTG8/ETO (via nervy homology region 2 in oligomerized form)
(PubMed:23812588). Interacts with BHLHA9 (PubMed:25466284).
{ECO:0000250|UniProtKB:Q61286, ECO:0000269|PubMed:16616331,
ECO:0000269|PubMed:19204326, ECO:0000269|PubMed:23812588,
ECO:0000269|PubMed:25466284}.
-!- INTERACTION:
Q8IUR7:ARMC8; NbExp=3; IntAct=EBI-722877, EBI-1049469;
Q6XD76:ASCL4; NbExp=3; IntAct=EBI-722877, EBI-10254793;
Q96MC5:C16orf45; NbExp=3; IntAct=EBI-722877, EBI-718468;
Q9NX04:C1orf109; NbExp=3; IntAct=EBI-722877, EBI-8643161;
P42773:CDKN2C; NbExp=5; IntAct=EBI-11952764, EBI-711290;
Q8IYR0:CFAP206; NbExp=3; IntAct=EBI-722877, EBI-749051;
O75575:CRCP; NbExp=3; IntAct=EBI-722877, EBI-2654687;
Q3B7T1-5:EDRF1; NbExp=3; IntAct=EBI-722877, EBI-10240074;
O75593:FOXH1; NbExp=2; IntAct=EBI-722877, EBI-1759806;
Q96MH2:HEXIM2; NbExp=4; IntAct=EBI-722877, EBI-5460660;
Q9BPY8:HOPX; NbExp=3; IntAct=EBI-722877, EBI-10295883;
Q02363:ID2; NbExp=2; IntAct=EBI-722877, EBI-713450;
Q02535:ID3; NbExp=3; IntAct=EBI-722877, EBI-1387094;
Q96S90:LYSMD1; NbExp=3; IntAct=EBI-722877, EBI-10293291;
O60336:MAPKBP1; NbExp=3; IntAct=EBI-722877, EBI-947402;
Q6P2C6:MLLT6; NbExp=3; IntAct=EBI-722877, EBI-5773143;
Q8NDC4:MORN4; NbExp=3; IntAct=EBI-722877, EBI-10269566;
Q8WVZ3:MORN4; NbExp=3; IntAct=EBI-722877, EBI-10277137;
Q9UJ70:NAGK; NbExp=3; IntAct=EBI-722877, EBI-372578;
Q9Y4Z2:NEUROG3; NbExp=5; IntAct=EBI-11952764, EBI-10328570;
Q9UJX0:OSGIN1; NbExp=3; IntAct=EBI-722877, EBI-9057006;
P25786:PSMA1; NbExp=3; IntAct=EBI-722877, EBI-359352;
P47897:QARS; NbExp=3; IntAct=EBI-722877, EBI-347462;
P47897-2:QARS; NbExp=3; IntAct=EBI-722877, EBI-10209725;
Q9Y5S9:RBM8A; NbExp=4; IntAct=EBI-11952764, EBI-447231;
Q1RLL8:RNASEL; NbExp=3; IntAct=EBI-722877, EBI-10239181;
Q06455-4:RUNX1T1; NbExp=2; IntAct=EBI-11952764, EBI-10224192;
Q9NZD8:SPG21; NbExp=3; IntAct=EBI-722877, EBI-742688;
P30626:SRI; NbExp=3; IntAct=EBI-722877, EBI-750459;
P42229:STAT5A; NbExp=3; IntAct=EBI-722877, EBI-749537;
O75716:STK16; NbExp=3; IntAct=EBI-722877, EBI-749295;
P17542:TAL1; NbExp=4; IntAct=EBI-722877, EBI-1753878;
Q6ZMU5:TRIM72; NbExp=3; IntAct=EBI-722877, EBI-2341648;
Q99598:TSNAX; NbExp=3; IntAct=EBI-722877, EBI-742638;
Q8WVJ9:TWIST2; NbExp=3; IntAct=EBI-722877, EBI-1797313;
Q548N1:VPS28; NbExp=3; IntAct=EBI-722877, EBI-10243107;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=a;
IsoId=Q99081-1; Sequence=Displayed;
Name=2; Synonyms=b;
IsoId=Q99081-2; Sequence=VSP_039109, VSP_039110;
Name=3; Synonyms=c;
IsoId=Q99081-3; Sequence=VSP_040024;
Name=4;
IsoId=Q99081-4; Sequence=VSP_057419, VSP_057420;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in several tissues and cell types
including skeletal muscle, thymus, and a B-cell line.
-!- DOMAIN: the 9aaTAD motif is a transactivation domain present in a
large number of yeast and animal transcription factors.
{ECO:0000269|PubMed:17467953}.
-!- DISEASE: Craniosynostosis 3 (CRS3) [MIM:615314]: A primary
abnormality of skull growth involving premature fusion of one or
more cranial sutures. The growth velocity of the skull often
cannot match that of the developing brain resulting in an abnormal
head shape and, in some cases, increased intracranial pressure,
which must be treated promptly to avoid permanent
neurodevelopmental disability. {ECO:0000269|PubMed:23354436,
ECO:0000269|PubMed:25271085}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/TCF12ID406.html";
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EMBL; M83233; AAB62389.1; -; mRNA.
EMBL; M80627; AAA58632.1; -; mRNA.
EMBL; AL831981; CAD89914.1; -; mRNA.
EMBL; AK304007; BAG64923.1; -; mRNA.
EMBL; BX537967; CAD97931.1; -; mRNA.
EMBL; AC010999; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC016525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC090532; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF456057; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471082; EAW77512.1; -; Genomic_DNA.
EMBL; BC050556; AAH50556.1; -; mRNA.
EMBL; M65209; AAC37571.1; -; mRNA.
EMBL; BK001049; DAA01129.1; -; mRNA.
CCDS; CCDS10159.1; -. [Q99081-1]
CCDS; CCDS10160.1; -. [Q99081-3]
CCDS; CCDS42042.1; -. [Q99081-2]
CCDS; CCDS76761.1; -. [Q99081-4]
PIR; A42121; A42121.
RefSeq; NP_001293149.1; NM_001306220.2. [Q99081-4]
RefSeq; NP_001309080.1; NM_001322151.1. [Q99081-3]
RefSeq; NP_001309086.1; NM_001322157.1. [Q99081-1]
RefSeq; NP_001309088.1; NM_001322159.1. [Q99081-3]
RefSeq; NP_001309091.1; NM_001322162.1. [Q99081-3]
RefSeq; NP_001309094.1; NM_001322165.1. [Q99081-1]
RefSeq; NP_003196.1; NM_003205.3. [Q99081-1]
RefSeq; NP_996919.1; NM_207036.1. [Q99081-3]
RefSeq; NP_996920.1; NM_207037.1. [Q99081-3]
RefSeq; NP_996921.1; NM_207038.1. [Q99081-1]
RefSeq; NP_996923.1; NM_207040.1. [Q99081-2]
UniGene; Hs.511504; -.
PDB; 2KNH; NMR; -; B=11-28.
PDB; 4JOL; X-ray; 2.91 A; E/F/G/H=177-200.
PDBsum; 2KNH; -.
PDBsum; 4JOL; -.
ProteinModelPortal; Q99081; -.
SMR; Q99081; -.
BioGrid; 112798; 78.
CORUM; Q99081; -.
DIP; DIP-29403N; -.
IntAct; Q99081; 86.
MINT; MINT-4713897; -.
STRING; 9606.ENSP00000331057; -.
iPTMnet; Q99081; -.
PhosphoSitePlus; Q99081; -.
BioMuta; TCF12; -.
DMDM; 1708332; -.
EPD; Q99081; -.
MaxQB; Q99081; -.
PaxDb; Q99081; -.
PeptideAtlas; Q99081; -.
PRIDE; Q99081; -.
DNASU; 6938; -.
Ensembl; ENST00000267811; ENSP00000267811; ENSG00000140262. [Q99081-1]
Ensembl; ENST00000333725; ENSP00000331057; ENSG00000140262. [Q99081-3]
Ensembl; ENST00000343827; ENSP00000342459; ENSG00000140262. [Q99081-2]
Ensembl; ENST00000438423; ENSP00000388940; ENSG00000140262. [Q99081-3]
Ensembl; ENST00000537840; ENSP00000444696; ENSG00000140262. [Q99081-4]
Ensembl; ENST00000557843; ENSP00000453737; ENSG00000140262. [Q99081-1]
GeneID; 6938; -.
KEGG; hsa:6938; -.
UCSC; uc002aea.4; human. [Q99081-1]
UCSC; uc010ugo.3; human.
CTD; 6938; -.
DisGeNET; 6938; -.
EuPathDB; HostDB:ENSG00000140262.17; -.
GeneCards; TCF12; -.
HGNC; HGNC:11623; TCF12.
HPA; CAB004432; -.
HPA; HPA065827; -.
MalaCards; TCF12; -.
MIM; 600480; gene.
MIM; 615314; phenotype.
neXtProt; NX_Q99081; -.
OpenTargets; ENSG00000140262; -.
Orphanet; 209916; Extraskeletal myxoid chondrosarcoma.
Orphanet; 35099; Isolated brachycephaly.
Orphanet; 35098; Isolated plagiocephaly.
PharmGKB; PA36381; -.
eggNOG; KOG3910; Eukaryota.
eggNOG; ENOG410XYUA; LUCA.
GeneTree; ENSGT00510000046438; -.
HOGENOM; HOG000234180; -.
HOVERGEN; HBG003854; -.
InParanoid; Q99081; -.
KO; K15603; -.
OMA; YYSFSAT; -.
PhylomeDB; Q99081; -.
TreeFam; TF321672; -.
Reactome; R-HSA-375170; CDO in myogenesis.
Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
SIGNOR; Q99081; -.
ChiTaRS; TCF12; human.
EvolutionaryTrace; Q99081; -.
GeneWiki; TCF12; -.
GenomeRNAi; 6938; -.
PRO; PR:Q99081; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000140262; -.
CleanEx; HS_TCF12; -.
ExpressionAtlas; Q99081; baseline and differential.
Genevisible; Q99081; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:LIFEdb.
GO; GO:0090575; C:RNA polymerase II transcription factor complex; IDA:BHF-UCL.
GO; GO:0043425; F:bHLH transcription factor binding; IPI:BHF-UCL.
GO; GO:0035497; F:cAMP response element binding; IEA:Ensembl.
GO; GO:0070888; F:E-box binding; IEA:Ensembl.
GO; GO:0035326; F:enhancer binding; IC:BHF-UCL.
GO; GO:0071837; F:HMG box domain binding; IEA:Ensembl.
GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central.
GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central.
GO; GO:0000978; F:RNA polymerase II core promoter proximal region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0046332; F:SMAD binding; IPI:BHF-UCL.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0008134; F:transcription factor binding; IPI:BHF-UCL.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II core promoter proximal region sequence-specific binding; IDA:NTNU_SB.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
GO; GO:0045666; P:positive regulation of neuron differentiation; IBA:GO_Central.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:1902036; P:regulation of hematopoietic stem cell differentiation; TAS:Reactome.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
Pfam; PF00010; HLH; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Craniosynostosis; Developmental protein; Differentiation;
Disease mutation; DNA-binding; Isopeptide bond; Neurogenesis; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 682 Transcription factor 12.
/FTId=PRO_0000127228.
DOMAIN 577 630 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
REGION 119 140 Leucine-zipper.
REGION 182 196 Interaction with RUNX1T1.
{ECO:0000269|PubMed:23812588}.
REGION 632 655 Class A specific domain.
MOTIF 19 27 9aaTAD.
MOD_RES 47 47 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 67 67 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 79 79 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 98 98 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 116 116 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 313 313 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 333 333 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 557 557 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 559 559 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
CROSSLNK 110 110 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 181 181 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 519 519 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 550 550 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447}.
CROSSLNK 609 609 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 653 653 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 170 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_039109.
VAR_SEQ 1 39 MNPQQQRMAAIGTDKELSDLLDFSAMFSPPVNSGKTRPT
-> MGKRYMHHPQIQMISTVNLLVIHLLSHQPVCSLALSLC
K (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057419.
VAR_SEQ 40 275 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_057420.
VAR_SEQ 171 193 DSAALDPLQAKKVRKVPPGLPSS -> MYCAYPVPGMGSNS
LMYYYNGKT (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_039110.
VAR_SEQ 396 396 L -> LKNRVEQQLHEHLQDAMSFLKDVCE (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_040024.
VARIANT 300 300 G -> S (in dbSNP:rs12442879).
/FTId=VAR_049543.
VARIANT 483 483 L -> R (in CRS3; dbSNP:rs36060670).
{ECO:0000269|PubMed:25271085}.
/FTId=VAR_072271.
VARIANT 600 600 L -> P (in CRS3).
{ECO:0000269|PubMed:23354436}.
/FTId=VAR_070096.
VARIANT 614 614 Q -> E (in CRS3).
{ECO:0000269|PubMed:23354436}.
/FTId=VAR_070097.
MUTAGEN 187 187 P->A: Decreases interaction with RUNX1T1.
{ECO:0000269|PubMed:23812588}.
MUTAGEN 191 191 P->A: Decreases interaction with RUNX1T1.
{ECO:0000269|PubMed:23812588}.
MUTAGEN 192 192 S->A: Decreases interaction with RUNX1T1.
{ECO:0000269|PubMed:23812588}.
CONFLICT 523 523 K -> E (in Ref. 4; CAD89914).
{ECO:0000305}.
HELIX 15 18 {ECO:0000244|PDB:2KNH}.
TURN 24 26 {ECO:0000244|PDB:2KNH}.
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


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