TREF1_MOUSE
ID TREF1_MOUSE Reviewed; 1205 AA.
AC Q8BXJ2; Q32NY5; Q6PCQ4; Q80X25; Q810H8; Q8BY31;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Transcriptional-regulating factor 1;
DE AltName: Full=Transcriptional-regulating protein 132;
DE AltName: Full=Zinc finger transcription factor TReP-132;
GN Name=Trerf1;
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 4), TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12556907; DOI=10.1038/sj.mp.4001201;
RA Duguay Y., Lapointe A., Lavallee B., Hum D.W., Rivest S.;
RT "Cloning of murine TReP-132, a novel transcription factor expressed in
RT brain regions involved in behavioral and psychiatric disorders.";
RL Mol. Psychiatry 8:39-49(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Medulla oblongata;
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] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Pancreas;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-773, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-639 AND LYS-646, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- FUNCTION: Binds DNA and activates transcription of CYP11A1. Interaction
CC with CREBBP and EP300 results in a synergistic transcriptional
CC activation of CYP11A1. {ECO:0000250|UniProtKB:Q96PN7}.
CC -!- SUBUNIT: Interacts with CREBBP and EP300. Interacts with DNTTIP1 and
CC DNTT. {ECO:0000250|UniProtKB:Q96PN7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8BXJ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BXJ2-2; Sequence=VSP_015650;
CC Name=3;
CC IsoId=Q8BXJ2-3; Sequence=VSP_015647, VSP_015648, VSP_015649;
CC Name=4;
CC IsoId=Q8BXJ2-4; Sequence=VSP_015647, VSP_015651;
CC -!- TISSUE SPECIFICITY: Highly expressed in kidney, lung and brain. In the
CC brain, expression was seen in the basal ganglia, hippocampus, piriform
CC cortex, cerebral cortex, ventromedial nucleus of the hypothalamus and
CC the dorsal and superior central nuclei of the raphe.
CC {ECO:0000269|PubMed:12556907}.
CC -!- DEVELOPMENTAL STAGE: At 15.5 dpc, highly expressed in brain, lung,
CC adrenal, thymus and kidney. Expression was also seen in spinal cord,
CC retina and snout. {ECO:0000269|PubMed:12556907}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN02288.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AY081774; AAN02288.1; ALT_FRAME; mRNA.
DR EMBL; AK042320; BAC31222.1; -; mRNA.
DR EMBL; AK046822; BAC32884.1; -; mRNA.
DR EMBL; BC051645; AAH51645.1; -; mRNA.
DR EMBL; BC059215; AAH59215.1; -; mRNA.
DR EMBL; BC108416; AAI08417.1; -; mRNA.
DR RefSeq; NP_001091092.1; NM_001097623.2. [Q8BXJ2-2]
DR RefSeq; NP_766210.1; NM_172622.3. [Q8BXJ2-1]
DR AlphaFoldDB; Q8BXJ2; -.
DR SMR; Q8BXJ2; -.
DR BioGRID; 230328; 3.
DR IntAct; Q8BXJ2; 2.
DR iPTMnet; Q8BXJ2; -.
DR PhosphoSitePlus; Q8BXJ2; -.
DR EPD; Q8BXJ2; -.
DR jPOST; Q8BXJ2; -.
DR MaxQB; Q8BXJ2; -.
DR PaxDb; Q8BXJ2; -.
DR PeptideAtlas; Q8BXJ2; -.
DR PRIDE; Q8BXJ2; -.
DR ProteomicsDB; 258965; -. [Q8BXJ2-1]
DR ProteomicsDB; 258966; -. [Q8BXJ2-2]
DR ProteomicsDB; 258967; -. [Q8BXJ2-3]
DR ProteomicsDB; 258968; -. [Q8BXJ2-4]
DR DNASU; 224829; -.
DR Ensembl; ENSMUST00000190020; ENSMUSP00000159411; ENSMUSG00000064043. [Q8BXJ2-4]
DR Ensembl; ENSMUST00000190080; ENSMUSP00000159410; ENSMUSG00000064043. [Q8BXJ2-2]
DR GeneID; 224829; -.
DR KEGG; mmu:224829; -.
DR UCSC; uc008cur.1; mouse. [Q8BXJ2-1]
DR UCSC; uc008cus.1; mouse. [Q8BXJ2-2]
DR UCSC; uc008cut.1; mouse. [Q8BXJ2-3]
DR UCSC; uc008cuw.1; mouse. [Q8BXJ2-4]
DR CTD; 55809; -.
DR MGI; MGI:2442086; Trerf1.
DR GeneTree; ENSGT00940000160303; -.
DR InParanoid; Q8BXJ2; -.
DR OMA; MTYSPPC; -.
DR OrthoDB; 165439at2759; -.
DR PhylomeDB; Q8BXJ2; -.
DR TreeFam; TF106431; -.
DR BioGRID-ORCS; 224829; 3 hits in 21 CRISPR screens.
DR ChiTaRS; Trerf1; mouse.
DR PRO; PR:Q8BXJ2; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q8BXJ2; protein.
DR Bgee; ENSMUSG00000064043; Expressed in rostral migratory stream and 248 other tissues.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0033142; F:nuclear progesterone receptor binding; ISO:MGI.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR GO; GO:0001223; F:transcription coactivator binding; ISO:MGI.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0071393; P:cellular response to progesterone stimulus; ISO:MGI.
DR GO; GO:0016575; P:histone deacetylation; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; ISO:MGI.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR000949; ELM2_dom.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR Pfam; PF01448; ELM2; 1.
DR SMART; SM01189; ELM2; 1.
DR SMART; SM00717; SANT; 1.
DR SMART; SM00355; ZnF_C2H2; 3.
DR SUPFAM; SSF46689; SSF46689; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS51156; ELM2; 1.
DR PROSITE; PS51293; SANT; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 3.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; DNA-binding; Metal-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Zinc; Zinc-finger.
FT CHAIN 1..1205
FT /note="Transcriptional-regulating factor 1"
FT /id="PRO_0000197135"
FT DOMAIN 785..876
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 891..942
FT /note="SANT"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT ZN_FING 512..534
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1019..1043
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1092..1114
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 201..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 270..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 390..500
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 527..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 956..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 958..978
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1061..1087
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PN7"
FT MOD_RES 639
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 646
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 773
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 960
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96PN7"
FT MOD_RES 961
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96PN7"
FT VAR_SEQ 493
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12556907,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_015647"
FT VAR_SEQ 546..565
FT /note="EEGEKAPPPQPQPQPQPQQP -> VSREPAPSFPGHVLLALLCC (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015648"
FT VAR_SEQ 566..1205
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_015649"
FT VAR_SEQ 634
FT /note="L -> LVRMTLSPPHSPQGAAPRAPA (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015650"
FT VAR_SEQ 1028
FT /note="A -> ADCRCHVAPFLPQ (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:12556907"
FT /id="VSP_015651"
FT CONFLICT 89
FT /note="A -> V (in Ref. 3; AAH59215)"
FT /evidence="ECO:0000305"
FT CONFLICT 112
FT /note="T -> P (in Ref. 1; AAN02288)"
FT /evidence="ECO:0000305"
FT CONFLICT 308..309
FT /note="QQ -> HR (in Ref. 1; AAN02288)"
FT /evidence="ECO:0000305"
FT CONFLICT 368..369
FT /note="QL -> PA (in Ref. 1; AAN02288)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="S -> T (in Ref. 1; AAN02288)"
FT /evidence="ECO:0000305"
FT CONFLICT 659
FT /note="K -> E (in Ref. 1; AAN02288)"
FT /evidence="ECO:0000305"
FT CONFLICT 915
FT /note="F -> L (in Ref. 1; AAN02288)"
FT /evidence="ECO:0000305"
FT CONFLICT 1159
FT /note="M -> I (in Ref. 1; AAN02288)"
FT /evidence="ECO:0000305"
FT CONFLICT 1202
FT /note="D -> V (in Ref. 1; AAN02288)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1205 AA; 132402 MW; 322FCC31845A99E2 CRC64;
MGDQQLYKTN HVGHGGENLF YQQPPLGVHS GLGHSYGNTI SGAGMDAPQA SPISPHFPQD
TRDGLGLPIG SKNLGQMDTS RQGGWGSHAG PGNHVQLRSN LANSNMMWGT PTQVEPADGY
QYTYSQASEI RTQKLTSGVL HKLDSFTQVF ANQNLRIQVN NMAQVLHTQS AVMDGASDSA
LRQLLSQKPV EPSASAIASR YQQVPQQPHP GFTGGLPKPA LPVGQHAPQG HLYYDYQQPL
AQMSMQGGQP LQAPQVLSGH MQQLQQHQYY PQPPPQQQQA GLQRISVQEM QQQQQPQQIR
PSPPQQQQQL QLQQRQSSLQ IPQYYQPQPM MQHLQEQQQP SMHLQPPSYH RDPHQYTPEQ
AHAVQLIQLG SMPQYYYQEP QQAYSHPLYP QSHLSQHQQR EDGQLKTYSS DRQTPAMLSS
HGDMGTSDTG VADPASSEMT RVTSTLPHQP LLSPSGIHLN NMGSQHQQPP SPSAMWPQMH
LPDGRAQSGS PESSSGQTKG VFGEQFDAKN KLTCSICLKE FKSLPALNGH MRSHGGMRAS
PSLKQEEGEK APPPQPQPQP QPQQPLPPPP PPPPPPQLPP EAERLTPMVM PVSVPVKLIP
PKPSSQGFTN SVAATPAARD KPASSMSDDE MPVLEIPRKH PPIAAKVEEP LKNLPEKKKF
RHRPEPLFIP PPPSSYTPNP TSYSGATLYQ SQLRSPRILG DHLLLDPAHE LPPYTPPPML
SPVRQGSGLF SNVLISGHGP GVHPQLPLTP LTPTPRVLLC RSSSIDGSNV TVTPGPGEQT
VDVEPRINIG LRFQAEIPEL QDVSALAQDT HRATLVWKPW PELENQALQQ QVENLLNLCC
SSALPGGGTN SEFALHSLFE AKGDVMATLE MLLLRKPVRL KCHPLANYHY AGSDKWTSLE
RKLFNKALAT YSKDFIFVQK MVKSKTVAQC VEYYYTWKKI MRLGRKHRTR LAEIIDDCMT
SEEEEEAEEE EEDPEEDRKS IKEEESEVAK SPEPPPAPAL APTEGPPMQA VGQQPSGNFI
CEMPNCGAVF SSRQALNGHA RIHGGTNQVA KTRGAIPSGK QKPGGTQSGY CSVKSSPSHS
TTSGETDPTT IFPCKECGKV FFKIKSRNAH MKTHRQQEEQ QRQKAQKAAF AAEMAATIER
TTGPVGAPEL LPLDQLSLMK PVKDVDILDD DVVQQLGVMD EAEVVGTDLL LDDQDSVLLQ
GDTEL
