TFPT_MOUSE
ID TFPT_MOUSE Reviewed; 259 AA.
AC Q3U1J1; Q9EP77;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=TCF3 fusion partner homolog;
DE AltName: Full=Protein FB1;
DE AltName: Full=Protein amida;
GN Name=Tfpt; Synonyms=Amida;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6 X CBA; TISSUE=Lung;
RA Brambillasca F., Mosna G., Privitera E.;
RT "Mouse ortholog of human FB1.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC STRAIN=ddY; TISSUE=Brain;
RA Miki N., Miyamoto K., Taira E.;
RT "Molecular cloning and functional analysis of mouse Amida.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=NOD; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180 AND SER-188, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Appears to promote apoptosis in a p53/TP53-independent
CC manner. {ECO:0000250}.
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. Component of the
CC chromatin remodeling INO80 complex; specifically part of a complex
CC module associated with the N-terminus of INO80 (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9JMG6}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3U1J1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3U1J1-2; Sequence=VSP_021243;
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DR EMBL; AF267988; AAG48243.1; -; mRNA.
DR EMBL; AB035134; BAB17318.1; -; mRNA.
DR EMBL; AK155925; BAE33506.1; -; mRNA.
DR EMBL; BC024356; AAH24356.1; -; mRNA.
DR CCDS; CCDS20720.1; -. [Q3U1J1-2]
DR CCDS; CCDS71873.1; -. [Q3U1J1-1]
DR RefSeq; NP_001277310.1; NM_001290381.1. [Q3U1J1-1]
DR RefSeq; NP_076013.1; NM_023524.2. [Q3U1J1-2]
DR AlphaFoldDB; Q3U1J1; -.
DR SMR; Q3U1J1; -.
DR BioGRID; 213632; 1.
DR ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR IntAct; Q3U1J1; 1.
DR STRING; 10090.ENSMUSP00000104281; -.
DR iPTMnet; Q3U1J1; -.
DR PhosphoSitePlus; Q3U1J1; -.
DR EPD; Q3U1J1; -.
DR jPOST; Q3U1J1; -.
DR MaxQB; Q3U1J1; -.
DR PaxDb; Q3U1J1; -.
DR PeptideAtlas; Q3U1J1; -.
DR PRIDE; Q3U1J1; -.
DR ProteomicsDB; 262804; -. [Q3U1J1-1]
DR ProteomicsDB; 262805; -. [Q3U1J1-2]
DR Antibodypedia; 32793; 153 antibodies from 27 providers.
DR DNASU; 69714; -.
DR Ensembl; ENSMUST00000108641; ENSMUSP00000104281; ENSMUSG00000006335. [Q3U1J1-1]
DR Ensembl; ENSMUST00000155592; ENSMUSP00000123636; ENSMUSG00000006335. [Q3U1J1-2]
DR GeneID; 69714; -.
DR KEGG; mmu:69714; -.
DR UCSC; uc009evf.2; mouse. [Q3U1J1-2]
DR UCSC; uc009evg.2; mouse. [Q3U1J1-1]
DR CTD; 29844; -.
DR MGI; MGI:1916964; Tfpt.
DR VEuPathDB; HostDB:ENSMUSG00000006335; -.
DR eggNOG; ENOG502RHUP; Eukaryota.
DR GeneTree; ENSGT00390000016605; -.
DR HOGENOM; CLU_096140_0_0_1; -.
DR InParanoid; Q3U1J1; -.
DR OMA; NERMLNR; -.
DR OrthoDB; 1308382at2759; -.
DR PhylomeDB; Q3U1J1; -.
DR TreeFam; TF338152; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR BioGRID-ORCS; 69714; 10 hits in 114 CRISPR screens.
DR PRO; PR:Q3U1J1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3U1J1; protein.
DR Bgee; ENSMUSG00000006335; Expressed in aortic valve and 246 other tissues.
DR ExpressionAtlas; Q3U1J1; baseline and differential.
DR Genevisible; Q3U1J1; MM.
DR GO; GO:0005884; C:actin filament; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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; ISS:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISS:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
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; ISO:MGI.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
DR InterPro; IPR033555; TFPT.
DR PANTHER; PTHR35084; PTHR35084; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; DNA damage; DNA recombination; DNA repair;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..259
FT /note="TCF3 fusion partner homolog"
FT /id="PRO_0000254582"
FT REGION 50..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 141..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..72
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 165..179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 167
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C1Z6"
FT MOD_RES 172
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0C1Z6"
FT MOD_RES 180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 203
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0C1Z6"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C1Z6"
FT CROSSLNK 222
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P0C1Z6"
FT VAR_SEQ 211..220
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1,
FT ECO:0000303|Ref.2"
FT /id="VSP_021243"
SQ SEQUENCE 259 AA; 28954 MW; C5A0094DC93B356A CRC64;
MELEQREGTM AAVGFEEFSA PPGSELALPP LFGGHILESE LETEVEFVSG GLGDSGLRER
DEEEEAARGR RRRQRELNRR KYQALGRRCR EIEQVNERVL NRLHQVQRIT RRLQQERRFL
MRVLDSYGDD YRDSQFTIVL EDDGSQGTDV PTPGNAENEP PEKEGLSPSQ RTTATLDPTS
PAPGEGPSGR KRRRAPRVGA SLTPELAPVQ VGAEGWGQGV IKVEEDFGFE ADEALDSSWV
SREPDKLLPY PTLASPPFD
