TREF1_HUMAN
ID TREF1_HUMAN Reviewed; 1200 AA.
AC Q96PN7; Q05GC6; Q7Z6T2; Q7Z6T3; Q9NQ72; Q9NQ73; Q9NUN9;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Transcriptional-regulating factor 1;
DE AltName: Full=Breast cancer anti-estrogen resistance 2;
DE AltName: Full=Transcriptional-regulating protein 132;
DE AltName: Full=Zinc finger protein rapa;
DE AltName: Full=Zinc finger transcription factor TReP-132;
GN Name=TRERF1; Synonyms=BCAR2, RAPA, TREP132;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND INTERACTION WITH CREBBP AND EP300.
RC TISSUE=Adrenal gland;
RX PubMed=11349124; DOI=10.1074/jbc.m100113200;
RA Gizard F., Lavallee B., DeWitte F., Hum D.W.;
RT "A novel zinc finger protein TReP-132 interacts with CBP/p300 to regulate
RT human CYP11A1 gene expression.";
RL J. Biol. Chem. 276:33881-33892(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA Mauch S., Sedlacek R., Krawinkel U.;
RT "The cDNA sequences of rapa-1 and -2, two zinc finger proteins with unique
RT structural characteristics.";
RL Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=18351453; DOI=10.1007/s10549-008-9969-5;
RA van Agthoven T., Veldscholte J., Smid M., van Agthoven T.L., Vreede L.,
RA Broertjes M., de Vries I., de Jong D., Sarwari R., Dorssers L.C.J.;
RT "Functional identification of genes causing estrogen independence of human
RT breast cancer cells.";
RL Breast Cancer Res. Treat. 114:23-30(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 900-1200 (ISOFORMS 1/2/4).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [6]
RP INTERACTION WITH DNTTIP1 AND DNTT, SUBCELLULAR LOCATION, AND FUNCTION IN
RP DNA-BINDING.
RX PubMed=16371131; DOI=10.1111/j.1365-2443.2005.00916.x;
RA Fujisaki S., Sato A., Toyomoto T., Hayano T., Sugai M., Kubota T.,
RA Koiwai O.;
RT "Direct binding of TReP-132 with TdT results in reduction of TdT
RT activity.";
RL Genes Cells 11:47-57(2006).
RN [7]
RP IDENTIFICATION BY 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-767, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP INTERACTION WITH DNTTIP1, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=21573134; DOI=10.1371/journal.pgen.1002065;
RA Hao Y., Xu N., Box A.C., Schaefer L., Kannan K., Zhang Y., Florens L.,
RA Seidel C., Washburn M.P., Wiegraebe W., Mak H.Y.;
RT "Nuclear cGMP-dependent kinase regulates gene expression via activity-
RT dependent recruitment of a conserved histone deacetylase complex.";
RL PLoS Genet. 7:E1002065-E1002065(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-954 AND SER-955, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-491, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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).
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:0000269|PubMed:11349124,
CC ECO:0000269|PubMed:16371131}.
CC -!- SUBUNIT: Interacts with CREBBP and EP300 (PubMed:11349124). Interacts
CC with DNTTIP1 (PubMed:16371131, PubMed:21573134). Interacts with DNTT
CC (PubMed:16371131). {ECO:0000269|PubMed:11349124,
CC ECO:0000269|PubMed:16371131, ECO:0000269|PubMed:21573134}.
CC -!- INTERACTION:
CC Q96PN7; P62508-3: ESRRG; NbExp=3; IntAct=EBI-3505166, EBI-12001340;
CC Q96PN7; Q14145: KEAP1; NbExp=2; IntAct=EBI-3505166, EBI-751001;
CC Q96PN7; P46934: NEDD4; NbExp=2; IntAct=EBI-3505166, EBI-726944;
CC Q96PN7; P46937: YAP1; NbExp=2; IntAct=EBI-3505166, EBI-1044059;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00512,
CC ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:11349124,
CC ECO:0000269|PubMed:16371131}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q96PN7-1; Sequence=Displayed;
CC Name=2; Synonyms=Rapa-1;
CC IsoId=Q96PN7-2; Sequence=VSP_015644, VSP_015645;
CC Name=3; Synonyms=Rapa-2;
CC IsoId=Q96PN7-3; Sequence=VSP_015644, VSP_015645, VSP_015646;
CC Name=4;
CC IsoId=Q96PN7-4; Sequence=VSP_015645;
CC Name=5;
CC IsoId=Q96PN7-5; Sequence=VSP_015645, VSP_015646;
CC -!- TISSUE SPECIFICITY: Highest expression was seen in thymus, testis and
CC adrenal cortex, expressed also in the adrenal medulla, thyroid, and
CC stomach. Highly expressed in steroidogenic JEG-3 and MCF-7 cells, low
CC expression was seen in non-steroidogenic Hep-G2 and HEK293 cells.
CC {ECO:0000269|PubMed:11349124}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA92082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF297872; AAL01653.1; -; mRNA.
DR EMBL; AJ277275; CAB88206.1; -; mRNA.
DR EMBL; AJ277276; CAB88207.1; -; mRNA.
DR EMBL; AM404259; CAL49295.1; -; mRNA.
DR EMBL; AM404183; CAL49297.1; -; mRNA.
DR EMBL; AL096814; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK002096; BAA92082.1; ALT_INIT; mRNA.
DR CCDS; CCDS4867.1; -. [Q96PN7-1]
DR RefSeq; NP_001284502.1; NM_001297573.1.
DR RefSeq; NP_277037.1; NM_033502.3. [Q96PN7-1]
DR RefSeq; XP_016866538.1; XM_017011049.1. [Q96PN7-1]
DR RefSeq; XP_016866541.1; XM_017011052.1. [Q96PN7-5]
DR RefSeq; XP_016866542.1; XM_017011053.1. [Q96PN7-5]
DR RefSeq; XP_016866543.1; XM_017011054.1. [Q96PN7-4]
DR AlphaFoldDB; Q96PN7; -.
DR SMR; Q96PN7; -.
DR BioGRID; 120919; 21.
DR IntAct; Q96PN7; 9.
DR MINT; Q96PN7; -.
DR STRING; 9606.ENSP00000439689; -.
DR iPTMnet; Q96PN7; -.
DR PhosphoSitePlus; Q96PN7; -.
DR BioMuta; TRERF1; -.
DR DMDM; 74762683; -.
DR EPD; Q96PN7; -.
DR jPOST; Q96PN7; -.
DR MassIVE; Q96PN7; -.
DR MaxQB; Q96PN7; -.
DR PaxDb; Q96PN7; -.
DR PeptideAtlas; Q96PN7; -.
DR PRIDE; Q96PN7; -.
DR ProteomicsDB; 77718; -. [Q96PN7-1]
DR ProteomicsDB; 77719; -. [Q96PN7-2]
DR ProteomicsDB; 77720; -. [Q96PN7-3]
DR ProteomicsDB; 77721; -. [Q96PN7-4]
DR ProteomicsDB; 77722; -. [Q96PN7-5]
DR Antibodypedia; 30153; 213 antibodies from 29 providers.
DR DNASU; 55809; -.
DR Ensembl; ENST00000340840.6; ENSP00000339438.2; ENSG00000124496.12. [Q96PN7-5]
DR Ensembl; ENST00000354325.2; ENSP00000346285.2; ENSG00000124496.12. [Q96PN7-4]
DR Ensembl; ENST00000372917.8; ENSP00000362008.5; ENSG00000124496.12. [Q96PN7-2]
DR Ensembl; ENST00000372922.8; ENSP00000362013.4; ENSG00000124496.12. [Q96PN7-1]
DR GeneID; 55809; -.
DR KEGG; hsa:55809; -.
DR UCSC; uc003osc.3; human. [Q96PN7-1]
DR CTD; 55809; -.
DR DisGeNET; 55809; -.
DR GeneCards; TRERF1; -.
DR HGNC; HGNC:18273; TRERF1.
DR HPA; ENSG00000124496; Low tissue specificity.
DR MIM; 610322; gene.
DR neXtProt; NX_Q96PN7; -.
DR OpenTargets; ENSG00000124496; -.
DR PharmGKB; PA134923539; -.
DR VEuPathDB; HostDB:ENSG00000124496; -.
DR eggNOG; KOG4167; Eukaryota.
DR GeneTree; ENSGT00940000160303; -.
DR HOGENOM; CLU_009800_0_0_1; -.
DR InParanoid; Q96PN7; -.
DR OrthoDB; 165439at2759; -.
DR PhylomeDB; Q96PN7; -.
DR TreeFam; TF106431; -.
DR PathwayCommons; Q96PN7; -.
DR SignaLink; Q96PN7; -.
DR BioGRID-ORCS; 55809; 28 hits in 1096 CRISPR screens.
DR ChiTaRS; TRERF1; human.
DR GeneWiki; TRERF1; -.
DR GenomeRNAi; 55809; -.
DR Pharos; Q96PN7; Tbio.
DR PRO; PR:Q96PN7; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q96PN7; protein.
DR Bgee; ENSG00000124496; Expressed in mucosa of paranasal sinus and 148 other tissues.
DR ExpressionAtlas; Q96PN7; baseline and differential.
DR Genevisible; Q96PN7; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0000118; C:histone deacetylase complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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; IPI:ARUK-UCL.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:ARUK-UCL.
DR GO; GO:0001223; F:transcription coactivator binding; IPI:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IBA:GO_Central.
DR GO; GO:0071393; P:cellular response to progesterone stimulus; IDA:ARUK-UCL.
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; IDA:ARUK-UCL.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0050847; P:progesterone receptor signaling pathway; IDA:ARUK-UCL.
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..1200
FT /note="Transcriptional-regulating factor 1"
FT /id="PRO_0000197134"
FT DOMAIN 779..870
FT /note="ELM2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00512"
FT DOMAIN 885..936
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 1013..1037
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1086..1108
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 192..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 333..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..503
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..1200
FT /note="Interaction with CREBBP"
FT /evidence="ECO:0000269|PubMed:11349124"
FT REGION 529..577
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 650..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 954..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1036..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 256..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 333..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 438..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..576
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..612
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 954..973
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1081
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 633
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXJ2"
FT MOD_RES 640
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8BXJ2"
FT MOD_RES 767
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 954
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 955
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 1..161
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_015644"
FT VAR_SEQ 546..628
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_015645"
FT VAR_SEQ 1022
FT /note="A -> ADCRCHVTPFLPQ (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_015646"
FT VARIANT 431
FT /note="T -> A (in dbSNP:rs35162277)"
FT /id="VAR_050197"
FT VARIANT 766
FT /note="V -> I (in dbSNP:rs59159203)"
FT /id="VAR_061362"
FT VARIANT 834
FT /note="C -> S (in dbSNP:rs2295275)"
FT /id="VAR_050198"
FT VARIANT 1019
FT /note="N -> T (in dbSNP:rs35978318)"
FT /id="VAR_050199"
FT VARIANT 1187
FT /note="D -> N (in dbSNP:rs11751765)"
FT /id="VAR_050200"
FT CONFLICT 658
FT /note="P -> S (in Ref. 2; CAB88206/CAB88207)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1200 AA; 132256 MW; B77057F46A73404F CRC64;
MGDQQLYKTN HVAHGSENLF YQQPPLGVHS GLNHNYGNAV TGGGMDAPQA SPISPHFPQD
TRDGLGLPVG SKNLGQMDTS RQGGWGSHAG PGNHVQLRGN LANSNMMWGA PAQAEPTDGY
QYTYSQASEI RTQKLTSGVL HKLDSFTQVF ANQNLRIQVN NMAQVLHTQS AVMDGAPDSA
LRQLLSQKPM EPPAPAIPSR YQQVPQQPHP GFTGGLSKPA LQVGQHPTQG HLYYDYQQPL
AQVPVQGGQP LQAPQMLSQH MQQMQQHQYY PPQQQQQAGQ QRISMQEIQT QPQQIRPSQP
QPPPQQQQPQ QLQLQQRQGS MQIPQYYQPQ PMMQHLQEQQ QQQMHLQPPS YHRDPHQYTP
EQAHTVQLIP LGSMSQYYYQ EPQQPYSHPL YQQSHLSQHQ QREDSQLKTY SSDRQAQAML
SSHGDLGPPD TGMGDPASSD LTRVSSTLPH RPLLSPSGIH LNNMGPQHQQ LSPSAMWPQM
HLPDGRAQPG SPESSGQPKG AFGEQFDAKN KLTCSICLKE FKNLPALNGH MRSHGGMRAS
PNLKQEEGEK VLPPQPQPPL PPPPPPPPPP QLPPEAESLT PMVMPVSVPV KLLPPKPSSQ
GFTNSTVAAP SARDKPASSM SDDEMPVLEI PRKHQPSVPK AEEPLKTVQE KKKFRHRPEP
LFIPPPPSYN PNPAASYSGA TLYQSQLRSP RVLGDHLLLD PTHELPPYTP PPMLSPVRQG
SGLFSNVLIS GHGPGAHPQL PLTPLTPTPR VLLCRSNSID GSNVTVTPGP GEQTVDVEPR
INIGLRFQAE IPELQDISAL AQDTHKATLV WKPWPELENH DLQQRVENLL NLCCSSALPG
GGTNSEFALH SLFEAKGDVM VALEMLLLRK PVRLKCHPLA NYHYAGSDKW TSLERKLFNK
ALATYSKDFI FVQKMVKSKT VAQCVEYYYT WKKIMRLGRK HRTRLAEIID DCVTSEEEEE
LEEEEEEDPE EDRKSTKEEE SEVPKSPEPP PVPVLAPTEG PPLQALGQPS GSFICEMPNC
GAVFSSRQAL NGHARIHGGT NQVTKARGAI PSGKQKPGGT QSGYCSVKSS PSHSTTSGET
DPTTIFPCKE CGKVFFKIKS RNAHMKTHRQ QEEQQRQKAQ KAAFAAEMAA TIERTTGPVG
APGLLPLDQL SLIKPIKDVD ILDDDVVQQL GGVMEEAEVV DTDLLLDDQD SVLLQGDAEL
