TCF25_MOUSE
ID TCF25_MOUSE Reviewed; 676 AA.
AC Q8R3L2; Q3THR8; Q3UBI7; Q3UD64; Q3UG75; Q80ZX3; Q8BR80; Q8C200; Q8C2M3;
AC Q8C6B4; Q9CUW0; Q9ER19;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Transcription factor 25;
DE Short=TCF-25;
DE AltName: Full=Nuclear localized protein 1;
GN Name=Tcf25; Synonyms=D8Ertd325e, Nulp1;
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), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Embryonic kidney;
RX PubMed=12107429; DOI=10.1007/s00441-002-0544-9;
RA Olsson M., Durbeej M., Ekblom P., Hjalt T.;
RT "Nulp1, a novel basic helix-loop-helix protein expressed broadly during
RT early embryonic organogenesis and prominently in developing dorsal root
RT ganglia.";
RL Cell Tissue Res. 308:361-370(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3; 4 AND 5), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 51-676 (ISOFORM 2).
RC STRAIN=BALB/cJ, C57BL/6J, and NOD;
RC TISSUE=Bone marrow, Corpora quadrigemina, Melanoma, Spleen, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Mammary gland;
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH XIAP.
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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
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: 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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:18068114}.
CC -!- SUBUNIT: Interacts with XIAP. {ECO:0000269|PubMed:18068114}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12107429,
CC ECO:0000269|PubMed:18068114}. Note=Some staining in the cytosol;
CC cytosolic localization is reduced in staurosporine-induced cell death.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q8R3L2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8R3L2-2; Sequence=VSP_020026, VSP_020027;
CC Name=3;
CC IsoId=Q8R3L2-3; Sequence=VSP_020023, VSP_020025, VSP_020028;
CC Name=4;
CC IsoId=Q8R3L2-4; Sequence=VSP_020024, VSP_020026, VSP_020027;
CC Name=5;
CC IsoId=Q8R3L2-5; Sequence=VSP_020025, VSP_020028;
CC -!- TISSUE SPECIFICITY: Broadly expressed in the embryo during the early
CC stages of organogenesis with highest levels in dorsal root ganglia and
CC little or no expression in liver and skin.
CC {ECO:0000269|PubMed:12107429}.
CC -!- DOMAIN: The C-terminal region mediates transcriptional repression.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TCF25 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB28983.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC32344.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC36220.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U94988; AAG27133.1; -; mRNA.
DR EMBL; AK013754; BAB28983.2; ALT_INIT; mRNA.
DR EMBL; AK045397; BAC32344.1; ALT_FRAME; mRNA.
DR EMBL; AK076151; BAC36220.1; ALT_INIT; mRNA.
DR EMBL; AK088360; BAC40301.1; -; mRNA.
DR EMBL; AK089964; BAC41018.1; -; mRNA.
DR EMBL; AK148082; BAE28334.1; -; mRNA.
DR EMBL; AK150232; BAE29397.1; -; mRNA.
DR EMBL; AK150918; BAE29956.1; -; mRNA.
DR EMBL; AK150942; BAE29977.1; -; mRNA.
DR EMBL; AK151143; BAE30150.1; -; mRNA.
DR EMBL; AK152178; BAE31009.1; -; mRNA.
DR EMBL; AK152494; BAE31265.1; -; mRNA.
DR EMBL; AK161627; BAE36500.1; -; mRNA.
DR EMBL; AK167837; BAE39858.1; -; mRNA.
DR EMBL; AK168167; BAE40128.1; -; mRNA.
DR EMBL; BC025071; AAH25071.1; -; mRNA.
DR EMBL; BC046768; AAH46768.2; -; mRNA.
DR CCDS; CCDS22755.1; -. [Q8R3L2-1]
DR CCDS; CCDS52700.1; -. [Q8R3L2-5]
DR CCDS; CCDS85630.1; -. [Q8R3L2-2]
DR CCDS; CCDS85631.1; -. [Q8R3L2-4]
DR RefSeq; NP_001032966.1; NM_001037877.3. [Q8R3L2-5]
DR RefSeq; NP_001032967.1; NM_001037878.3. [Q8R3L2-1]
DR RefSeq; NP_001273291.1; NM_001286362.1. [Q8R3L2-4]
DR RefSeq; NP_080080.2; NM_025804.3. [Q8R3L2-2]
DR AlphaFoldDB; Q8R3L2; -.
DR SMR; Q8R3L2; -.
DR BioGRID; 211765; 9.
DR STRING; 10090.ENSMUSP00000056485; -.
DR iPTMnet; Q8R3L2; -.
DR PhosphoSitePlus; Q8R3L2; -.
DR EPD; Q8R3L2; -.
DR MaxQB; Q8R3L2; -.
DR PaxDb; Q8R3L2; -.
DR PeptideAtlas; Q8R3L2; -.
DR PRIDE; Q8R3L2; -.
DR ProteomicsDB; 262965; -. [Q8R3L2-1]
DR ProteomicsDB; 262966; -. [Q8R3L2-2]
DR ProteomicsDB; 262967; -. [Q8R3L2-3]
DR ProteomicsDB; 262968; -. [Q8R3L2-4]
DR ProteomicsDB; 262969; -. [Q8R3L2-5]
DR Antibodypedia; 30955; 200 antibodies from 26 providers.
DR Ensembl; ENSMUST00000057934; ENSMUSP00000056485; ENSMUSG00000001472. [Q8R3L2-1]
DR Ensembl; ENSMUST00000108840; ENSMUSP00000104468; ENSMUSG00000001472. [Q8R3L2-5]
DR Ensembl; ENSMUST00000212470; ENSMUSP00000148344; ENSMUSG00000001472. [Q8R3L2-4]
DR Ensembl; ENSMUST00000212571; ENSMUSP00000148531; ENSMUSG00000001472. [Q8R3L2-2]
DR GeneID; 66855; -.
DR KEGG; mmu:66855; -.
DR UCSC; uc009nvl.2; mouse. [Q8R3L2-1]
DR UCSC; uc009nvn.2; mouse. [Q8R3L2-2]
DR UCSC; uc009nvo.2; mouse. [Q8R3L2-4]
DR UCSC; uc009nvp.2; mouse. [Q8R3L2-5]
DR CTD; 22980; -.
DR MGI; MGI:1914105; Tcf25.
DR VEuPathDB; HostDB:ENSMUSG00000001472; -.
DR eggNOG; KOG2422; Eukaryota.
DR GeneTree; ENSGT00390000005563; -.
DR HOGENOM; CLU_008321_3_2_1; -.
DR InParanoid; Q8R3L2; -.
DR OMA; WPPLTKN; -.
DR OrthoDB; 1428505at2759; -.
DR PhylomeDB; Q8R3L2; -.
DR TreeFam; TF106155; -.
DR BioGRID-ORCS; 66855; 1 hit in 74 CRISPR screens.
DR ChiTaRS; Tcf25; mouse.
DR PRO; PR:Q8R3L2; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8R3L2; protein.
DR Bgee; ENSMUSG00000001472; Expressed in pontine nuclear group and 300 other tissues.
DR ExpressionAtlas; Q8R3L2; baseline and differential.
DR Genevisible; Q8R3L2; MM.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
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; ISS:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repressor; Transcription; Transcription regulation.
FT CHAIN 1..676
FT /note="Transcription factor 25"
FT /id="PRO_0000087266"
FT REGION 1..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9BQ70"
FT VAR_SEQ 54..68
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020023"
FT VAR_SEQ 119..143
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020024"
FT VAR_SEQ 625..626
FT /note="GE -> QL (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020025"
FT VAR_SEQ 625
FT /note="G -> L (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12107429,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_020026"
FT VAR_SEQ 626..676
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12107429,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT /id="VSP_020027"
FT VAR_SEQ 627..676
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020028"
FT CONFLICT 129
FT /note="K -> E (in Ref. 2; BAE29956/BAE29977/BAE30150/
FT BAE31009/BAE31265)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="H -> L (in Ref. 1; AAG27133)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="Q -> E (in Ref. 1; AAG27133)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="L -> R (in Ref. 2; BAE39858/BAE40128)"
FT /evidence="ECO:0000305"
FT CONFLICT 243
FT /note="K -> E (in Ref. 2; BAE28334)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="I -> T (in Ref. 1; AAG27133)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="E -> V (in Ref. 1; AAG27133)"
FT /evidence="ECO:0000305"
FT CONFLICT 454
FT /note="A -> T (in Ref. 1; AAG27133)"
FT /evidence="ECO:0000305"
FT CONFLICT 539
FT /note="A -> V (in Ref. 2; BAE28334 and 3; AAH25071)"
FT /evidence="ECO:0000305"
FT CONFLICT 560
FT /note="I -> M (in Ref. 1; AAG27133)"
FT /evidence="ECO:0000305"
FT CONFLICT 597
FT /note="R -> G (in Ref. 2; BAE39858/BAE40128)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 676 AA; 76685 MW; 095539BBAA3E8535 CRC64;
MSRRALRRLR GEQRGQEPLG PDALKFVLLD DDDAEEEGPK PGLGGRRPGG AGKEGVRVNN
RFELINTEDL EDDLVVNGER SDCTLPDSVS SGNKGRAKHG NAETKQDGGA TKAGSSEQSN
ASGKLRKKKK KQKNKKSCTG ESSENGLEDI DRILERIEDS SGFSHPGPPP LSSRKHVLYV
EHRHLNPDTE LKRYFGARAV LGEQRPRQRQ RVYPKCTWLT TPKSTWPRYS KPGLSMRLLE
SKKGLSFFAF DHNEEYQQAQ HKFLVAVESM EPNNIVVLLQ TSPYHVDSLL QLSDACRFQE
DQEMARDLIE RALYSMECAF HPLFSLTSGT CRLDYRRPEN RSFYLTLYKQ MSFLEKRGCP
RTALEYCKLI LSLEPDEDPL CMLLLIDHLA LRARNYEYLI RLFQEWEAHR NLSQLPNFAF
SVPLAYFLLS QQTDLPEHEL SSARQQASLL IQQALTMFPG VLMPLLEYCS VRPDATVSNH
RFFGPDAEIS QPPALGQLVS LYLGRSHFLW KEPAIMSWLE ENVHEVLQAV DAGDPAVEAC
ENRRKVLYQR APRNIHRHVI LSEIKEAVAA LPSDVTTQSV MGFDPLPPLD TIYSYVRPER
LSPVSHGNTI ALFFRSLLPN YTTEGERLEE GVAGGPNRNQ GLNRLMLAVR DMMANFHFND
LEVPREDNPE GEGDWD
