ID CACO1_HUMAN Reviewed; 691 AA. AC Q9P1Z2; B3KVA8; Q6FI59; Q71RC3; Q86WF8; Q96JU3; Q9H090; DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot. DT 23-OCT-2007, sequence version 2. DT 28-JAN-2026, entry version 166. DE RecName: Full=Calcium-binding and coiled-coil domain-containing protein 1; DE AltName: Full=Calphoglin; DE AltName: Full=Coiled-coil coactivator protein; DE AltName: Full=Sarcoma antigen NY-SAR-3; GN Name=CALCOCO1; Synonyms=KIAA1536; ORFNames=PP13275, UNQ2436/PRO4996; 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, AND INTERACTION WITH RP PHOSPHOGLUCOMUTASE AND PPA1. RX DOI=10.1016/J.BBRC.2004.10.021; RA Takahashi K., Inuzuka M., Ingi T.; RT "Cellular signaling mediated by calphoglin-induced activation of IPP and RT PGM."; RL Biochem. Biophys. Res. Commun. 325:203-214(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain; RX PubMed=10819331; DOI=10.1093/dnares/7.2.143; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVII. The RT complete sequences of 100 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:143-150(2000). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND VARIANT RP LYS-393. RC TISSUE=Spleen, and Thyroid; 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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RX PubMed=15498874; DOI=10.1073/pnas.0404089101; RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X., RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.; RT "Large-scale cDNA transfection screening for genes related to cancer RT development and progression."; RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 147-455. RX PubMed=12601173; DOI=10.1073/pnas.0437972100; RA Lee S.-Y., Obata Y., Yoshida M., Stockert E., Williamson B., RA Jungbluth A.A., Chen Y.-T., Old L.J., Scanlan M.J.; RT "Immunomic analysis of human sarcoma."; RL Proc. Natl. Acad. Sci. U.S.A. 100:2651-2656(2003). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4, AND IDENTIFICATION BY MASS RP 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 [12] RP FUNCTION. RX PubMed=24245781; DOI=10.1111/gtc.12104; RA Mizuta S., Minami T., Fujita H., Kaminaga C., Matsui K., Ishino R., RA Fujita A., Oda K., Kawai A., Hasegawa N., Urahama N., Roeder R.G., Ito M.; RT "CCAR1/CoCoA pair-mediated recruitment of the Mediator defines a novel RT pathway for GATA1 function."; RL Genes Cells 19:28-51(2014). CC -!- FUNCTION: Functions as a coactivator for aryl hydrocarbon and nuclear CC receptors (NR). Recruited to promoters through its contact with the N- CC terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of CC transcription factors or coactivators, such as NCOA2. During ER- CC activation acts synergistically in combination with other NCOA2-binding CC proteins, such as EP300, CREBBP and CARM1. Involved in the CC transcriptional activation of target genes in the Wnt/CTNNB1 pathway. CC Functions as a secondary coactivator in LEF1-mediated transcriptional CC activation via its interaction with CTNNB1. Coactivator function for CC nuclear receptors and LEF1/CTNNB1 involves differential utilization of CC two different activation regions (By similarity). In association with CC CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from CC the gamma-globin promoter during erythroid differentiation of K562 CC erythroleukemia cells (PubMed:24245781). {ECO:0000250|UniProtKB:Q8CGU1, CC ECO:0000269|PubMed:24245781}. CC -!- FUNCTION: Seems to enhance inorganic pyrophosphatase thus activating CC phosphogluomutase (PMG). Probably functions as a component of the CC calphoglin complex, which is involved in linking cellular metabolism CC (phosphate and glucose metabolism) with other core functions including CC protein synthesis and degradation, calcium signaling and cell growth. CC {ECO:0000269|Ref.1}. CC -!- SUBUNIT: Part of a calphoglin complex consisting of CALCOCO1, PPA1 and CC PGM (Ref.1). Interacts with the bHLH-PAS domains of GRIP1, AHR and CC ARNT. Interacts with CTNNB1 via both its N- and C-terminal regions. CC Interacts with EP300. Interacts with CCAR1 (via N-terminus) and GATA1 CC (By similarity). {ECO:0000250|UniProtKB:Q8CGU1, ECO:0000269|Ref.1}. CC -!- INTERACTION: CC Q9P1Z2; Q13515: BFSP2; NbExp=5; IntAct=EBI-749920, EBI-10229433; CC Q9P1Z2; Q96LK0: CEP19; NbExp=6; IntAct=EBI-749920, EBI-741885; CC Q9P1Z2; Q2TBE0: CWF19L2; NbExp=6; IntAct=EBI-749920, EBI-5453285; CC Q9P1Z2; Q9UII6: DUSP13B; NbExp=6; IntAct=EBI-749920, EBI-749800; CC Q9P1Z2; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-749920, EBI-744099; CC Q9P1Z2; Q3B820: FAM161A; NbExp=3; IntAct=EBI-749920, EBI-719941; CC Q9P1Z2; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-749920, EBI-746969; CC Q9P1Z2; P60520: GABARAPL2; NbExp=3; IntAct=EBI-749920, EBI-720116; CC Q9P1Z2; Q96CN7: ISOC1; NbExp=3; IntAct=EBI-749920, EBI-2805787; CC Q9P1Z2; O14777: NDC80; NbExp=6; IntAct=EBI-749920, EBI-715849; CC Q9P1Z2; P54646: PRKAA2; NbExp=3; IntAct=EBI-749920, EBI-1383852; CC Q9P1Z2; O76064: RNF8; NbExp=3; IntAct=EBI-749920, EBI-373337; CC Q9P1Z2; Q8TC07: TBC1D15; NbExp=3; IntAct=EBI-749920, EBI-1048247; CC Q9P1Z2; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-749920, EBI-2682299; CC Q9P1Z2; P46678: BDP1; Xeno; NbExp=3; IntAct=EBI-749920, EBI-19164; CC Q9P1Z2; Q04264: PDS5; Xeno; NbExp=3; IntAct=EBI-749920, EBI-13077; CC Q9P1Z2; Q12208: USB1; Xeno; NbExp=3; IntAct=EBI-749920, EBI-31589; CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Shuttles between nucleus CC and cytoplasm. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=1; CC IsoId=Q9P1Z2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9P1Z2-2; Sequence=VSP_029053; CC Name=3; CC IsoId=Q9P1Z2-3; Sequence=VSP_029052; CC Name=4; CC IsoId=Q9P1Z2-4; Sequence=VSP_041471, VSP_041472; CC -!- DOMAIN: The C-terminal activation region (AD) is used for downstream CC signaling. Seems to be essential for coactivator function with nuclear CC receptors and with the aryl hydrocarbon receptor (By similarity). CC {ECO:0000250}. CC -!- DOMAIN: The N-terminal activation region (AD) is necessary and CC sufficient for synergistic activation of LEF1-mediated transcription by CC CTNNB1. Contains a EP3000 binding region which is important for CC synergistic cooperation (By similarity). {ECO:0000250}. CC -!- DOMAIN: Recruitment by nuclear receptors is accomplished by the CC interaction of the coiled-coiled domain with p160 coactivators. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CALCOCO family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA96060.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY563137; AAT68474.1; -; mRNA. DR EMBL; AB040969; BAA96060.1; ALT_INIT; mRNA. DR EMBL; AL136895; CAB66829.1; -; mRNA. DR EMBL; AY358397; AAQ88763.1; -; mRNA. DR EMBL; AK122773; BAG53720.1; -; mRNA. DR EMBL; AK027881; BAB55428.1; -; mRNA. DR EMBL; AF370415; AAQ15251.1; -; mRNA. DR EMBL; CR533567; CAG38598.1; -; mRNA. DR EMBL; CH471054; EAW96728.1; -; Genomic_DNA. DR EMBL; BC003177; AAH03177.1; -; mRNA. DR EMBL; AY211909; AAO65163.1; -; mRNA. DR CCDS; CCDS44908.1; -. [Q9P1Z2-4] DR CCDS; CCDS8864.1; -. [Q9P1Z2-1] DR RefSeq; NP_001137154.1; NM_001143682.2. [Q9P1Z2-4] DR RefSeq; NP_065949.1; NM_020898.3. [Q9P1Z2-1] DR AlphaFoldDB; Q9P1Z2; -. DR SMR; Q9P1Z2; -. DR BioGRID; 121692; 86. DR CORUM; Q9P1Z2; -. DR DIP; DIP-47322N; -. DR FunCoup; Q9P1Z2; 1726. DR IntAct; Q9P1Z2; 71. DR MINT; Q9P1Z2; -. DR STRING; 9606.ENSP00000449960; -. DR GlyGen; Q9P1Z2; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; Q9P1Z2; -. DR PhosphoSitePlus; Q9P1Z2; -. DR BioMuta; CALCOCO1; -. DR DMDM; 160017736; -. DR CPTAC; CPTAC-1234; -. DR CPTAC; CPTAC-1235; -. DR jPOST; Q9P1Z2; -. DR MassIVE; Q9P1Z2; -. DR PaxDb; 9606-ENSP00000449960; -. DR PeptideAtlas; Q9P1Z2; -. DR ProteomicsDB; 83683; -. [Q9P1Z2-1] DR ProteomicsDB; 83684; -. [Q9P1Z2-2] DR ProteomicsDB; 83685; -. [Q9P1Z2-3] DR ProteomicsDB; 83686; -. [Q9P1Z2-4] DR Pumba; Q9P1Z2; -. DR Antibodypedia; 27237; 106 antibodies from 22 providers. DR DNASU; 57658; -. DR Ensembl; ENST00000262059.8; ENSP00000262059.4; ENSG00000012822.17. [Q9P1Z2-3] DR Ensembl; ENST00000430117.6; ENSP00000397189.2; ENSG00000012822.17. [Q9P1Z2-4] DR Ensembl; ENST00000548263.5; ENSP00000447647.1; ENSG00000012822.17. [Q9P1Z2-2] DR Ensembl; ENST00000550804.6; ENSP00000449960.1; ENSG00000012822.17. [Q9P1Z2-1] DR GeneID; 57658; -. DR KEGG; hsa:57658; -. DR MANE-Select; ENST00000550804.6; ENSP00000449960.1; NM_020898.3; NP_065949.1. DR UCSC; uc001sef.4; human. [Q9P1Z2-1] DR AGR; HGNC:29306; -. DR ClinPGx; PA128394699; -. DR CTD; 57658; -. DR DisGeNET; 57658; -. DR GeneCards; CALCOCO1; -. DR HGNC; HGNC:29306; CALCOCO1. DR HPA; ENSG00000012822; Low tissue specificity. DR OpenTargets; ENSG00000012822; -. DR VEuPathDB; HostDB:ENSG00000012822; -. DR eggNOG; ENOG502QR9J; Eukaryota. DR GeneTree; ENSGT00950000183025; -. DR HOGENOM; CLU_028857_0_0_1; -. DR InParanoid; Q9P1Z2; -. DR OMA; HNWASND; -. DR OrthoDB; 10015001at2759; -. DR PAN-GO; Q9P1Z2; 2 GO annotations based on evolutionary models. DR PhylomeDB; Q9P1Z2; -. DR PathwayCommons; Q9P1Z2; -. DR SignaLink; Q9P1Z2; -. DR SIGNOR; Q9P1Z2; -. DR Agora; ENSG00000012822; -. DR BioGRID-ORCS; 57658; 12 hits in 1160 CRISPR screens. DR CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities. DR ChiTaRS; CALCOCO1; human. DR GeneWiki; CALCOCO1; -. DR GenomeRNAi; 57658; -. DR Pharos; Q9P1Z2; Tbio. DR PRO; PR:Q9P1Z2; -. DR Proteomes; UP000005640; Chromosome 12. DR RNAct; Q9P1Z2; protein. DR Bgee; ENSG00000012822; Expressed in mucosa of stomach and 203 other cell types or tissues. DR ExpressionAtlas; Q9P1Z2; baseline and differential. DR GO; GO:0000785; C:chromatin; IEA:Ensembl. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:LIFEdb. DR GO; GO:0008013; F:beta-catenin binding; IPI:AgBase. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:UniProtKB. DR GO; GO:0043565; F:sequence-specific DNA binding; IDA:AgBase. DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB. DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW. DR GO; GO:0030518; P:nuclear receptor-mediated steroid hormone signaling pathway; ISS:HGNC-UCL. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:UniProtKB. DR GO; GO:0010628; P:positive regulation of gene expression; IDA:AgBase. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:HGNC-UCL. DR GO; GO:0007165; P:signal transduction; ISS:HGNC-UCL. DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW. DR CDD; cd21967; Zn-C2H2_CALCOCO1; 1. DR FunFam; 2.60.40.2840:FF:000004; Calcium-binding and coiled-coil domain-containing protein 1; 1. DR Gene3D; 2.60.40.2840; -; 1. DR Gene3D; 6.20.250.40; -; 1. DR InterPro; IPR012852; CALCOCO1-like. DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1. DR InterPro; IPR041611; SKICH. DR InterPro; IPR051002; UBA_autophagy_assoc_protein. DR PANTHER; PTHR31915:SF5; CALCIUM-BINDING AND COILED-COIL DOMAIN-CONTAINING PROTEIN 1; 1. DR PANTHER; PTHR31915; SKICH DOMAIN-CONTAINING PROTEIN; 1. DR Pfam; PF07888; CALCOCO1; 1. DR Pfam; PF17751; SKICH; 1. DR Pfam; PF18112; Zn-C2H2_12; 1. DR PROSITE; PS51905; ZF_UBZ1; 1. PE 1: Evidence at protein level; KW Activator; Alternative splicing; Coiled coil; Cytoplasm; Metal-binding; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Transcription; Transcription regulation; Wnt signaling pathway; Zinc; KW Zinc-finger. FT CHAIN 1..691 FT /note="Calcium-binding and coiled-coil domain-containing FT protein 1" FT /id="PRO_0000308899" FT ZN_FING 653..679 FT /note="UBZ1-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253" FT REGION 1..190 FT /note="N-terminal AD (CTNNB1 binding site)" FT /evidence="ECO:0000250" FT REGION 1..30 FT /note="p300 KIX-binding" FT /evidence="ECO:0000250" FT REGION 45..125 FT /note="Interaction with GATA1" FT /evidence="ECO:0000250|UniProtKB:Q8CGU1" FT REGION 501..691 FT /note="C-terminal AD (CTNNB1 binding site); interaction FT with CCAR1" FT /evidence="ECO:0000250|UniProtKB:Q8CGU1" FT REGION 514..606 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 145..205 FT /evidence="ECO:0000255" FT COILED 232..339 FT /evidence="ECO:0000255" FT COILED 417..514 FT /evidence="ECO:0000255" FT BINDING 656 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253" FT BINDING 659 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253" FT BINDING 675 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253" FT BINDING 679 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01253" FT MOD_RES 4 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 87..119 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041471" FT VAR_SEQ 287..338 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_041472" FT VAR_SEQ 598 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_029052" FT VAR_SEQ 633..691 FT /note="SGFTVGTLSETSTGGPATPTWKECPICKERFPAESDKDALEDHMDGHFFFST FT QDPFTFE -> R (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10819331, FT ECO:0000303|PubMed:15498874" FT /id="VSP_029053" FT VARIANT 393 FT /note="R -> K (in dbSNP:rs3741659)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_036881" FT CONFLICT 381 FT /note="H -> R (in Ref. 5; BAG53720)" FT /evidence="ECO:0000305" FT CONFLICT 486 FT /note="K -> R (in Ref. 7; CAG38598)" FT /evidence="ECO:0000305" FT CONFLICT 660 FT /note="K -> E (in Ref. 7; CAG38598)" FT /evidence="ECO:0000305" SQ SEQUENCE 691 AA; 77336 MW; 06A4C6BAB896759F CRC64; MEESPLSRAP SRGGVNFLNV ARTYIPNTKV ECHYTLPPGT MPSASDWIGI FKVEAACVRD YHTFVWSSVP ESTTDGSPIH TSVQFQASYL PKPGAQLYQF RYVNRQGQVC GQSPPFQFRE PRPMDELVTL EEADGGSDIL LVVPKATVLQ NQLDESQQER NDLMQLKLQL EGQVTELRSR VQELERALAT ARQEHTELME QYKGISRSHG EITEERDILS RQQGDHVARI LELEDDIQTI SEKVLTKEVE LDRLRDTVKA LTREQEKLLG QLKEVQADKE QSEAELQVAQ QENHHLNLDL KEAKSWQEEQ SAQAQRLKDK VAQMKDTLGQ AQQRVAELEP LKEQLRGAQE LAASSQQKAT LLGEELASAA AARDRTIAEL HRSRLEVAEV NGRLAELGLH LKEEKCQWSK ERAGLLQSVE AEKDKILKLS AEILRLEKAV QEERTQNQVF KTELAREKDS SLVQLSESKR ELTELRSALR VLQKEKEQLQ EEKQELLEYM RKLEARLEKV ADEKWNEDAT TEDEEAAVGL SCPAALTDSE DESPEDMRLP PYGLCERGDP GSSPAGPREA SPLVVISQPA PISPHLSGPA EDSSSDSEAE DEKSVLMAAV QSGGEEANLL LPELGSAFYD MASGFTVGTL SETSTGGPAT PTWKECPICK ERFPAESDKD ALEDHMDGHF FFSTQDPFTF E //