TCF25_HUMAN
ID TCF25_HUMAN Reviewed; 676 AA.
AC Q9BQ70; Q2MK75; Q9UPV3;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Transcription factor 25;
DE Short=TCF-25;
DE AltName: Full=Nuclear localized protein 1;
GN Name=TCF25; Synonyms=KIAA1049, NULP1; ORFNames=FKSG26;
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], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DOMAIN.
RX PubMed=16574069; DOI=10.1016/j.bbrc.2006.02.187;
RA Cai Z., Wang Y., Yu W., Xiao J., Li Y., Liu L., Zhu C., Tan K., Deng Y.,
RA Yuan W., Liu M., Wu X.;
RT "hnulp1, a basic helix-loop-helix protein with a novel transcriptional
RT repressive domain, inhibits transcriptional activity of serum response
RT factor.";
RL Biochem. Biophys. Res. Commun. 343:973-981(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Wang Y.-G., Gong L.;
RT "Characterization of FKSG26, a novel gene located on human chromosome
RT 16q24.3.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Lymph, and Muscle;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 127-676.
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=18068114; DOI=10.1016/j.bbrc.2007.11.146;
RA Steen H., Lindholm D.;
RT "Nuclear localized protein-1 (Nulp1) increases cell death of human
RT osteosarcoma cells and binds the X-linked inhibitor of apoptosis protein.";
RL Biochem. Biophys. Res. Commun. 366:432-437(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION BY
RP 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 [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [10]
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).
CC -!- FUNCTION: May play a role in cell death control. Acts as a
CC transcriptional repressor. Has been shown to repress transcription of
CC SRF in vitro and so may play a role in heart development.
CC {ECO:0000269|PubMed:16574069}.
CC -!- SUBUNIT: Interacts with XIAP. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9BQ70; Q92624: APPBP2; NbExp=3; IntAct=EBI-745182, EBI-743771;
CC Q9BQ70; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-745182, EBI-398977;
CC Q9BQ70; Q96D09: GPRASP2; NbExp=8; IntAct=EBI-745182, EBI-473189;
CC Q9BQ70; Q96SL4: GPX7; NbExp=3; IntAct=EBI-745182, EBI-749411;
CC Q9BQ70; Q8N6L0: KASH5; NbExp=3; IntAct=EBI-745182, EBI-749265;
CC Q9BQ70; O60333-2: KIF1B; NbExp=3; IntAct=EBI-745182, EBI-10975473;
CC Q9BQ70; Q5S007: LRRK2; NbExp=3; IntAct=EBI-745182, EBI-5323863;
CC Q9BQ70; P43364: MAGEA11; NbExp=5; IntAct=EBI-745182, EBI-739552;
CC Q9BQ70; P43364-2: MAGEA11; NbExp=3; IntAct=EBI-745182, EBI-10178634;
CC Q9BQ70; P21673: SAT1; NbExp=11; IntAct=EBI-745182, EBI-711613;
CC Q9BQ70; O76024: WFS1; NbExp=3; IntAct=EBI-745182, EBI-720609;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16574069,
CC ECO:0000269|PubMed:18068114}. Note=Some staining in the cytosol.
CC -!- TISSUE SPECIFICITY: In the embryo, widely expressed with highest levels
CC in brain. In the adult, highest expression is found in the heart.
CC {ECO:0000269|PubMed:16574069}.
CC -!- DOMAIN: The C-terminal region mediates transcriptional repression.
CC {ECO:0000269|PubMed:16574069}.
CC -!- SIMILARITY: Belongs to the TCF25 family. {ECO:0000305}.
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DR EMBL; DQ321703; ABC55265.1; -; mRNA.
DR EMBL; AF322111; AAG50276.1; -; mRNA.
DR EMBL; BC000959; AAH00959.1; -; mRNA.
DR EMBL; BC009349; AAH09349.1; -; mRNA.
DR EMBL; BC011884; AAH11884.1; -; mRNA.
DR EMBL; AB028972; BAA83001.1; -; mRNA.
DR CCDS; CCDS10987.1; -.
DR RefSeq; NP_055787.1; NM_014972.2.
DR AlphaFoldDB; Q9BQ70; -.
DR SMR; Q9BQ70; -.
DR BioGRID; 116629; 74.
DR IntAct; Q9BQ70; 45.
DR MINT; Q9BQ70; -.
DR STRING; 9606.ENSP00000263346; -.
DR GlyGen; Q9BQ70; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQ70; -.
DR MetOSite; Q9BQ70; -.
DR PhosphoSitePlus; Q9BQ70; -.
DR BioMuta; TCF25; -.
DR DMDM; 23396596; -.
DR EPD; Q9BQ70; -.
DR jPOST; Q9BQ70; -.
DR MassIVE; Q9BQ70; -.
DR MaxQB; Q9BQ70; -.
DR PaxDb; Q9BQ70; -.
DR PeptideAtlas; Q9BQ70; -.
DR PRIDE; Q9BQ70; -.
DR ProteomicsDB; 78638; -.
DR Antibodypedia; 30955; 200 antibodies from 26 providers.
DR DNASU; 22980; -.
DR Ensembl; ENST00000263346.13; ENSP00000263346.8; ENSG00000141002.20.
DR Ensembl; ENST00000640279.1; ENSP00000491638.1; ENSG00000141002.20.
DR GeneID; 22980; -.
DR KEGG; hsa:22980; -.
DR MANE-Select; ENST00000263346.13; ENSP00000263346.8; NM_014972.3; NP_055787.1.
DR UCSC; uc002fpb.3; human.
DR CTD; 22980; -.
DR DisGeNET; 22980; -.
DR GeneCards; TCF25; -.
DR HGNC; HGNC:29181; TCF25.
DR HPA; ENSG00000141002; Low tissue specificity.
DR MIM; 612326; gene.
DR neXtProt; NX_Q9BQ70; -.
DR OpenTargets; ENSG00000141002; -.
DR PharmGKB; PA145007492; -.
DR VEuPathDB; HostDB:ENSG00000141002; -.
DR eggNOG; KOG2422; Eukaryota.
DR GeneTree; ENSGT00390000005563; -.
DR HOGENOM; CLU_008321_3_2_1; -.
DR InParanoid; Q9BQ70; -.
DR OMA; WPPLTKN; -.
DR OrthoDB; 1428505at2759; -.
DR PhylomeDB; Q9BQ70; -.
DR TreeFam; TF106155; -.
DR PathwayCommons; Q9BQ70; -.
DR SignaLink; Q9BQ70; -.
DR BioGRID-ORCS; 22980; 14 hits in 1082 CRISPR screens.
DR ChiTaRS; TCF25; human.
DR GenomeRNAi; 22980; -.
DR Pharos; Q9BQ70; Tbio.
DR PRO; PR:Q9BQ70; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BQ70; protein.
DR Bgee; ENSG00000141002; Expressed in sural nerve and 200 other tissues.
DR ExpressionAtlas; Q9BQ70; baseline and differential.
DR Genevisible; Q9BQ70; HS.
DR GO; GO:0005634; C:nucleus; IDA:GO_Central.
DR GO; GO:1990112; C:RQC complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:GO_Central.
DR GO; GO:0007507; P:heart development; NAS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:GO_Central.
DR Gene3D; 1.25.40.10; -; 1.
DR InterPro; IPR006994; TCF25/Rqc1.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR22684; PTHR22684; 1.
DR Pfam; PF04910; Tcf25; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW DNA-binding; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Transcription; Transcription regulation.
FT CHAIN 1..676
FT /note="Transcription factor 25"
FT /id="PRO_0000087265"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 85..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..48
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
SQ SEQUENCE 676 AA; 76667 MW; 6ECF8A1C78141296 CRC64;
MSRRALRRLR GEQRGQEPLG PGALHFDLRD DDDAEEEGPK RELGVRRPGG AGKEGVRVNN
RFELINIDDL EDDPVVNGER SGCALTDAVA PGNKGRGQRG NTESKTDGDD TETVPSEQSH
ASGKLRKKKK KQKNKKSSTG EASENGLEDI DRILERIEDS TGLNRPGPAP LSSRKHVLYV
EHRHLNPDTE LKRYFGARAI LGEQRPRQRQ RVYPKCTWLT TPKSTWPRYS KPGLSMRLLE
SKKGLSFFAF EHSEEYQQAQ HKFLVAVESM EPNNIVVLLQ TSPYHVDSLL QLSDACRFQE
DQEMARDLVE RALYSMECAF HPLFSLTSGA CRLDYRRPEN RSFYLALYKQ MSFLEKRGCP
RTALEYCKLI LSLEPDEDPL CMLLLIDHLA LRARNYEYLI RLFQEWEAHR NLSQLPNFAF
SVPLAYFLLS QQTDLPECEQ SSARQKASLL IQQALTMFPG VLLPLLESCS VRPDASVSSH
RFFGPNAEIS QPPALSQLVN LYLGRSHFLW KEPATMSWLE ENVHEVLQAV DAGDPAVEAC
ENRRKVLYQR APRNIHRHVI LSEIKEAVAA LPPDVTTQSV MGFDPLPPSD TIYSYVRPER
LSPISHGNTI ALFFRSLLPN YTMEGERPEE GVAGGLNRNQ GLNRLMLAVR DMMANFHLND
LEAPHEDDAE GEGEWD
