TFPT_HUMAN
ID TFPT_HUMAN Reviewed; 253 AA.
AC P0C1Z6; G5E9B5;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=TCF3 fusion partner;
DE AltName: Full=INO80 complex subunit F;
DE AltName: Full=Protein FB1;
GN Name=TFPT; Synonyms=INO80F;
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), AND CHROMOSOMAL TRANSLOCATION WITH
RP TCF3.
RC TISSUE=Leukemia;
RX PubMed=10086727; DOI=10.1038/sj.leu.2401338;
RA Brambillasca F., Mosna G., Colombo M., Rivolta A., Caslini C., Minuzzo M.,
RA Giudici G., Mizzi L., Biondi A., Privitera E.;
RT "Identification of a novel molecular partner of the E2A gene in childhood
RT leukemia.";
RL Leukemia 13:369-375(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Retinoblastoma, Skin, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP IDENTIFICATION IN INO80 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.m509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P.,
RA Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the yeast
RT INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [6]
RP POSSIBLE FUNCTION IN APOPTOSIS.
RX PubMed=17041757; DOI=10.1007/s10495-006-0195-5;
RA Franchini C., Fontana F., Minuzzo M., Babbio F., Privitera E.;
RT "Apoptosis promoted by up-regulation of TFPT (TCF3 fusion partner) appears
RT p53 independent, cell type restricted and cell density influenced.";
RL Apoptosis 11:2217-2224(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-249 AND SER-252, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION IN THE INO80 COMPLEX, SUBCELLULAR LOCATION, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; SER-188; SER-249 AND
RP SER-252, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180; THR-207; SER-249 AND
RP SER-252, AND 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 [13]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-252, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-167; SER-180; THR-207;
RP SER-249 AND SER-252, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-172; SER-180 AND SER-252, AND
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-216, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE 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).
CC -!- FUNCTION: Appears to promote apoptosis in a p53/TP53-independent
CC manner.
CC -!- FUNCTION: Putative regulatory component of the chromatin remodeling
CC INO80 complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair.
CC -!- SUBUNIT: Interacts with NOL3; translocates NOL3 into the nucleus and
CC negatively regulated TFPT-induced cell death (By similarity). Component
CC of the chromatin remodeling INO80 complex; specifically part of a
CC complex module associated with the N-terminus of INO80. {ECO:0000250,
CC ECO:0000250|UniProtKB:Q9JMG6, ECO:0000269|PubMed:16230350,
CC ECO:0000269|PubMed:18922472, ECO:0000269|PubMed:21303910}.
CC -!- INTERACTION:
CC P0C1Z6; Q9UFG5: C19orf25; NbExp=3; IntAct=EBI-1245626, EBI-741214;
CC P0C1Z6; Q2TAC2-2: CCDC57; NbExp=3; IntAct=EBI-1245626, EBI-10961624;
CC P0C1Z6; Q96CJ1: EAF2; NbExp=4; IntAct=EBI-1245626, EBI-1245604;
CC P0C1Z6; Q13526: PIN1; NbExp=3; IntAct=EBI-1245626, EBI-714158;
CC P0C1Z6; P20618: PSMB1; NbExp=3; IntAct=EBI-1245626, EBI-372273;
CC P0C1Z6; Q13188: STK3; NbExp=3; IntAct=EBI-1245626, EBI-992580;
CC P0C1Z6; P09493-10: TPM1; NbExp=3; IntAct=EBI-1245626, EBI-12123928;
CC P0C1Z6; P07951-2: TPM2; NbExp=3; IntAct=EBI-1245626, EBI-10977815;
CC P0C1Z6; P06753: TPM3; NbExp=7; IntAct=EBI-1245626, EBI-355607;
CC P0C1Z6; Q9Y5K5: UCHL5; NbExp=3; IntAct=EBI-1245626, EBI-1051183;
CC P0C1Z6-2; Q504U0: C4orf46; NbExp=3; IntAct=EBI-10178002, EBI-6657981;
CC P0C1Z6-2; Q96GN5: CDCA7L; NbExp=3; IntAct=EBI-10178002, EBI-5278764;
CC P0C1Z6-2; Q05D60: DEUP1; NbExp=3; IntAct=EBI-10178002, EBI-748597;
CC P0C1Z6-2; Q8WWB3: DYDC1; NbExp=3; IntAct=EBI-10178002, EBI-740680;
CC P0C1Z6-2; Q96C92-2: ENTR1; NbExp=3; IntAct=EBI-10178002, EBI-10178036;
CC P0C1Z6-2; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-10178002, EBI-2514791;
CC P0C1Z6-2; P08727: KRT19; NbExp=3; IntAct=EBI-10178002, EBI-742756;
CC P0C1Z6-2; P25791: LMO2; NbExp=3; IntAct=EBI-10178002, EBI-739696;
CC P0C1Z6-2; P11309: PIM1; NbExp=3; IntAct=EBI-10178002, EBI-696621;
CC P0C1Z6-2; Q15311: RALBP1; NbExp=5; IntAct=EBI-10178002, EBI-749285;
CC P0C1Z6-2; Q96KN7: RPGRIP1; NbExp=3; IntAct=EBI-10178002, EBI-1050213;
CC P0C1Z6-2; Q59EK9: RUNDC3A; NbExp=3; IntAct=EBI-10178002, EBI-747225;
CC P0C1Z6-2; Q13188: STK3; NbExp=3; IntAct=EBI-10178002, EBI-992580;
CC P0C1Z6-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-10178002, EBI-1105213;
CC P0C1Z6-2; P09493-5: TPM1; NbExp=3; IntAct=EBI-10178002, EBI-10196387;
CC P0C1Z6-2; P06753: TPM3; NbExp=3; IntAct=EBI-10178002, EBI-355607;
CC P0C1Z6-2; Q5VU62: TPM3; NbExp=3; IntAct=EBI-10178002, EBI-10184033;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18922472}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P0C1Z6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P0C1Z6-2; Sequence=VSP_058937;
CC -!- DISEASE: Note=A chromosomal aberration involving TFPT is a cause of
CC pre-B-cell acute lymphoblastic leukemia (B-ALL). Inversion
CC inv(19)(p13;q13) with TCF3. {ECO:0000269|PubMed:10086727}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TFPTID495ch19q13.html";
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DR EMBL; AF052052; AAD45182.1; -; mRNA.
DR EMBL; AC012314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC245052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471135; EAW72186.1; -; Genomic_DNA.
DR EMBL; BC001728; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC004281; AAH04281.1; -; mRNA.
DR EMBL; BC007776; AAH07776.1; -; mRNA.
DR CCDS; CCDS12878.1; -. [P0C1Z6-1]
DR CCDS; CCDS82396.1; -. [P0C1Z6-2]
DR RefSeq; NP_001308721.1; NM_001321792.1. [P0C1Z6-2]
DR RefSeq; NP_037474.1; NM_013342.3. [P0C1Z6-1]
DR AlphaFoldDB; P0C1Z6; -.
DR SMR; P0C1Z6; -.
DR BioGRID; 118931; 180.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR IntAct; P0C1Z6; 44.
DR MINT; P0C1Z6; -.
DR STRING; 9606.ENSP00000375639; -.
DR iPTMnet; P0C1Z6; -.
DR PhosphoSitePlus; P0C1Z6; -.
DR BioMuta; TFPT; -.
DR DMDM; 126352246; -.
DR EPD; P0C1Z6; -.
DR jPOST; P0C1Z6; -.
DR MassIVE; P0C1Z6; -.
DR MaxQB; P0C1Z6; -.
DR PaxDb; P0C1Z6; -.
DR PeptideAtlas; P0C1Z6; -.
DR PRIDE; P0C1Z6; -.
DR ProteomicsDB; 33890; -.
DR ProteomicsDB; 52299; -.
DR Antibodypedia; 32793; 153 antibodies from 27 providers.
DR DNASU; 29844; -.
DR Ensembl; ENST00000391758.5; ENSP00000375638.1; ENSG00000105619.14. [P0C1Z6-2]
DR Ensembl; ENST00000391759.6; ENSP00000375639.1; ENSG00000105619.14. [P0C1Z6-1]
DR Ensembl; ENST00000611344.4; ENSP00000484338.1; ENSG00000276504.4. [P0C1Z6-2]
DR Ensembl; ENST00000611514.1; ENSP00000481443.1; ENSG00000278161.1. [P0C1Z6-1]
DR Ensembl; ENST00000611935.1; ENSP00000482185.1; ENSG00000276022.1. [P0C1Z6-1]
DR Ensembl; ENST00000614788.1; ENSP00000482785.1; ENSG00000273833.1. [P0C1Z6-1]
DR Ensembl; ENST00000615534.1; ENSP00000480353.1; ENSG00000274073.1. [P0C1Z6-1]
DR Ensembl; ENST00000615620.1; ENSP00000483971.1; ENSG00000276263.1. [P0C1Z6-1]
DR Ensembl; ENST00000616277.1; ENSP00000483417.1; ENSG00000276296.1. [P0C1Z6-1]
DR Ensembl; ENST00000616798.4; ENSP00000480169.1; ENSG00000276504.4. [P0C1Z6-1]
DR Ensembl; ENST00000617348.1; ENSP00000477775.1; ENSG00000275086.1. [P0C1Z6-1]
DR Ensembl; ENST00000619581.1; ENSP00000484685.1; ENSG00000276323.1. [P0C1Z6-1]
DR GeneID; 29844; -.
DR KEGG; hsa:29844; -.
DR MANE-Select; ENST00000391759.6; ENSP00000375639.1; NM_013342.4; NP_037474.1.
DR UCSC; uc010yej.1; human. [P0C1Z6-1]
DR UCSC; uc061cmq.1; human.
DR CTD; 29844; -.
DR DisGeNET; 29844; -.
DR GeneCards; TFPT; -.
DR HGNC; HGNC:13630; TFPT.
DR HPA; ENSG00000105619; Low tissue specificity.
DR MIM; 609519; gene.
DR neXtProt; NX_P0C1Z6; -.
DR OpenTargets; ENSG00000105619; -.
DR PharmGKB; PA37802; -.
DR VEuPathDB; HostDB:ENSG00000105619; -.
DR eggNOG; ENOG502RHUP; Eukaryota.
DR GeneTree; ENSGT00390000016605; -.
DR InParanoid; P0C1Z6; -.
DR OMA; NERMLNR; -.
DR PhylomeDB; P0C1Z6; -.
DR TreeFam; TF338152; -.
DR PathwayCommons; P0C1Z6; -.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR SignaLink; P0C1Z6; -.
DR BioGRID-ORCS; 29844; 79 hits in 1092 CRISPR screens.
DR ChiTaRS; TFPT; human.
DR GeneWiki; TFPT; -.
DR GenomeRNAi; 29844; -.
DR Pharos; P0C1Z6; Tbio.
DR PRO; PR:P0C1Z6; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P0C1Z6; protein.
DR Bgee; ENSG00000105619; Expressed in amygdala and 96 other tissues.
DR ExpressionAtlas; P0C1Z6; baseline and differential.
DR Genevisible; P0C1Z6; HS.
DR GO; GO:0005884; C:actin filament; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IEA:Ensembl.
DR GO; GO:0044877; F:protein-containing complex binding; IEA:Ensembl.
DR GO; GO:0097190; P:apoptotic signaling pathway; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:ComplexPortal.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IBA:GO_Central.
DR GO; GO:0045739; P:positive regulation of DNA repair; IEA:Ensembl.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR InterPro; IPR033555; TFPT.
DR PANTHER; PTHR35084; PTHR35084; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Chromosomal rearrangement; DNA damage;
KW DNA recombination; DNA repair; Isopeptide bond; Nucleus; Phosphoprotein;
KW Proto-oncogene; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..253
FT /note="TCF3 fusion partner"
FT /id="PRO_0000254581"
FT REGION 49..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 56..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..183
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 252
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform 2)"
FT /id="VSP_058937"
SQ SEQUENCE 253 AA; 28278 MW; C57CC8436F963F36 CRC64;
MELEQREGTM AAVGFEEFSA PPGSELALPP LFGGHILESE LETEVEFVSG GLGGSGLRER
DEEEEAARGR RRRQRELNRR KYQALGRRCR EIEQVNERVL NRLHQVQRIT RRLQQERRFL
MRVLDSYGDD YRASQFTIVL EDEGSQGTDA PTPGNAENEP PEKETLSPPR RTPAPPEPGS
PAPGEGPSGR KRRRVPRDGR RAGNALTPEL APVQIKVEED FGFEADEALD SSWVSRGPDK
LLPYPTLASP ASD
