CACO1_HUMAN
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 03-AUG-2022, entry version 150.
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 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=3; 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: DUSP13; 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=4; 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 -!- 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};
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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_001143682.1. [Q9P1Z2-4]
DR RefSeq; NP_065949.1; NM_020898.2. [Q9P1Z2-1]
DR RefSeq; XP_016875196.1; XM_017019707.1. [Q9P1Z2-1]
DR AlphaFoldDB; Q9P1Z2; -.
DR SMR; Q9P1Z2; -.
DR BioGRID; 121692; 76.
DR DIP; DIP-47322N; -.
DR IntAct; Q9P1Z2; 47.
DR MINT; Q9P1Z2; -.
DR STRING; 9606.ENSP00000449960; -.
DR iPTMnet; Q9P1Z2; -.
DR PhosphoSitePlus; Q9P1Z2; -.
DR BioMuta; CALCOCO1; -.
DR DMDM; 160017736; -.
DR CPTAC; CPTAC-1234; -.
DR CPTAC; CPTAC-1235; -.
DR EPD; Q9P1Z2; -.
DR jPOST; Q9P1Z2; -.
DR MassIVE; Q9P1Z2; -.
DR MaxQB; Q9P1Z2; -.
DR PaxDb; Q9P1Z2; -.
DR PeptideAtlas; Q9P1Z2; -.
DR PRIDE; Q9P1Z2; -.
DR ProteomicsDB; 83683; -. [Q9P1Z2-1]
DR ProteomicsDB; 83684; -. [Q9P1Z2-2]
DR ProteomicsDB; 83685; -. [Q9P1Z2-3]
DR ProteomicsDB; 83686; -. [Q9P1Z2-4]
DR Antibodypedia; 27237; 107 antibodies from 22 providers.
DR DNASU; 57658; -.
DR Ensembl; ENST00000262059.8; ENSP00000262059.4; ENSG00000012822.16. [Q9P1Z2-3]
DR Ensembl; ENST00000430117.6; ENSP00000397189.2; ENSG00000012822.16. [Q9P1Z2-4]
DR Ensembl; ENST00000548263.5; ENSP00000447647.1; ENSG00000012822.16. [Q9P1Z2-2]
DR Ensembl; ENST00000550804.6; ENSP00000449960.1; ENSG00000012822.16. [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 CTD; 57658; -.
DR DisGeNET; 57658; -.
DR GeneCards; CALCOCO1; -.
DR HGNC; HGNC:29306; CALCOCO1.
DR HPA; ENSG00000012822; Low tissue specificity.
DR neXtProt; NX_Q9P1Z2; -.
DR OpenTargets; ENSG00000012822; -.
DR PharmGKB; PA128394699; -.
DR VEuPathDB; HostDB:ENSG00000012822; -.
DR eggNOG; ENOG502QR9J; Eukaryota.
DR GeneTree; ENSGT00950000183025; -.
DR HOGENOM; CLU_028857_0_0_1; -.
DR InParanoid; Q9P1Z2; -.
DR OMA; GLCEHGD; -.
DR OrthoDB; 179838at2759; -.
DR PhylomeDB; Q9P1Z2; -.
DR TreeFam; TF329501; -.
DR PathwayCommons; Q9P1Z2; -.
DR SignaLink; Q9P1Z2; -.
DR BioGRID-ORCS; 57658; 12 hits in 1082 CRISPR screens.
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 201 other tissues.
DR ExpressionAtlas; Q9P1Z2; baseline and differential.
DR Genevisible; Q9P1Z2; HS.
DR GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
DR GO; GO:0070016; F:armadillo repeat domain binding; IPI:UniProtKB.
DR GO; GO:0008013; F:beta-catenin binding; IPI:AgBase.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:AgBase.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
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:0000976; F:transcription cis-regulatory region binding; IDA:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:UniProtKB.
DR GO; GO:0003712; F:transcription coregulator activity; IDA:UniProtKB.
DR GO; GO:0030518; P:intracellular steroid hormone receptor signaling pathway; ISS:HGNC-UCL.
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:0045893; P:positive regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; ISS:HGNC-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:UniProtKB-KW.
DR InterPro; IPR012852; CALCOCO1-like.
DR InterPro; IPR041641; CALCOCO1/2_Zn_UBZ1.
DR InterPro; IPR041611; SKICH.
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; Reference proteome; Transcription;
KW Transcription regulation; Wnt signaling pathway; Zinc; 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..607
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
