TFPT_RAT
ID TFPT_RAT Reviewed; 259 AA.
AC Q9JMG6;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=TCF3 fusion partner homolog;
DE AltName: Full=Protein amida;
GN Name=Tfpt; Synonyms=Amida;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 10-259, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, POSSIBLE FUNCTION IN APOPTOSIS, AND INTERACTION WITH NOL3.
RX PubMed=10644725; DOI=10.1074/jbc.275.4.2647;
RA Irie Y., Yamagata K., Gan Y., Miyamoto K., Do E., Kuo C.H., Taira E.,
RA Miki N.;
RT "Molecular cloning and characterization of Amida, a novel protein which
RT interacts with a neuron-specific immediate early gene product arc, contains
RT novel nuclear localization signals, and causes cell death in cultured
RT cells.";
RL J. Biol. Chem. 275:2647-2653(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-180, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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. {ECO:0000250}.
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:0000269|PubMed:10644725}.
CC -!- INTERACTION:
CC Q9JMG6; Q62627: Pawr; NbExp=8; IntAct=EBI-1767101, EBI-1187240;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10644725}.
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Abundant in the brain.
CC {ECO:0000269|PubMed:10644725}.
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DR EMBL; AC103574; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AB029495; BAA90702.1; -; mRNA.
DR RefSeq; NP_620225.1; NM_138870.1.
DR RefSeq; XP_006228098.1; XM_006228036.3.
DR AlphaFoldDB; Q9JMG6; -.
DR SMR; Q9JMG6; -.
DR BioGRID; 250095; 2.
DR IntAct; Q9JMG6; 1.
DR STRING; 10116.ENSRNOP00000018913; -.
DR iPTMnet; Q9JMG6; -.
DR PhosphoSitePlus; Q9JMG6; -.
DR PaxDb; Q9JMG6; -.
DR PRIDE; Q9JMG6; -.
DR Ensembl; ENSRNOT00000089713; ENSRNOP00000075123; ENSRNOG00000056098.
DR GeneID; 85423; -.
DR KEGG; rno:85423; -.
DR UCSC; RGD:620839; rat.
DR CTD; 29844; -.
DR RGD; 620839; Tfpt.
DR eggNOG; ENOG502RHUP; Eukaryota.
DR GeneTree; ENSGT00390000016605; -.
DR InParanoid; Q9JMG6; -.
DR OrthoDB; 1308382at2759; -.
DR PhylomeDB; Q9JMG6; -.
DR TreeFam; TF338152; -.
DR Reactome; R-RNO-5689603; UCH proteinases.
DR Reactome; R-RNO-5696394; DNA Damage Recognition in GG-NER.
DR PRO; PR:Q9JMG6; -.
DR Proteomes; UP000002494; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0031011; C:Ino80 complex; ISO:RGD.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IDA:RGD.
DR GO; GO:0006915; P:apoptotic process; IDA:UniProtKB.
DR GO; GO:0097190; P:apoptotic signaling pathway; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
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; IEP:RGD.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:RGD.
DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:RGD.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; ISO:RGD.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:RGD.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:RGD.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:RGD.
DR GO; GO:0006282; P:regulation of DNA repair; ISO:RGD.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:RGD.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:RGD.
DR GO; GO:0045995; P:regulation of embryonic development; ISO:RGD.
DR GO; GO:0000723; P:telomere maintenance; ISO:RGD.
DR InterPro; IPR033555; TFPT.
DR PANTHER; PTHR35084; PTHR35084; 1.
PE 1: Evidence at protein level;
KW Apoptosis; DNA damage; DNA recombination; DNA repair; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT CHAIN 1..259
FT /note="TCF3 fusion partner homolog"
FT /id="PRO_0000254583"
FT REGION 51..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 REGION 240..259
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 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:22673903"
FT MOD_RES 188
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C1Z6"
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"
SQ SEQUENCE 259 AA; 28908 MW; 674408B3F3FB6863 CRC64;
MELEQREGTM AAVGFEEFSA PPGSELALPP LFGGHILESE LETEVEFVSG GLGDSGLRER
DEEEEAARGR RRRQRELNRR KYQALGRRCR EIEQVNERVL NRLHQVQRIT RRLQQERRFL
MRVLDSYGDD YRDSQFTIVL EDDGSQGTDV PTPGNVENEP PEKEGLSPPQ RTTATLDPSS
PAPGEGPSGR KRRRAPRAAS SLTPELAPVQ VGAEGWGQGV IKVEEDFGFE ADEALDSSWV
SRGPDKLLPY PTLASPPFD
