ID   CABIN_HUMAN             Reviewed;        2220 AA.
AC   Q9Y6J0; G5E9F3; Q6PHY0; Q9Y460;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   24-JAN-2024, entry version 202.
DE   RecName: Full=Calcineurin-binding protein cabin-1;
DE   AltName: Full=Calcineurin inhibitor;
DE            Short=CAIN;
GN   Name=CABIN1; Synonyms=KIAA0330;
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, INTERACTION WITH
RP   CALCINEURIN, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC   TISSUE=Kidney;
RX   PubMed=9655484; DOI=10.1016/s1074-7613(00)80575-0;
RA   Sun L., Youn H.-D., Loh C., Stolow M., He W., Liu J.O.;
RT   "Cabin 1, a negative regulator for calcineurin signaling in T
RT   lymphocytes.";
RL   Immunity 8:703-711(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10591208; DOI=10.1038/990031;
RA   Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA   Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA   Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA   Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA   Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA   Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA   Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA   Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA   Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA   Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA   Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA   Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA   Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA   Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA   Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA   Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA   Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA   Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA   Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA   Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA   Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA   Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA   Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA   Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA   Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA   Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA   Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA   Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA   Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA   Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA   Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA   Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA   Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA   McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA   Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA   Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA   Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA   Wright H.;
RT   "The DNA sequence of human chromosome 22.";
RL   Nature 402:489-495(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-853.
RC   TISSUE=Testis;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 319-2220 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA   Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA   Tanaka A., Kotani H., Nomura N., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. VII. The
RT   complete sequences of 100 new cDNA clones from brain which can code for
RT   large proteins in vitro.";
RL   DNA Res. 4:141-150(1997).
RN   [6]
RP   FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A
RP   COMPLEX WITH ASF1A; HIRA; HISTONE H3.3 AND UBN1.
RX   PubMed=14718166; DOI=10.1016/s0092-8674(03)01064-x;
RA   Tagami H., Ray-Gallet D., Almouzni G., Nakatani Y.;
RT   "Histone H3.1 and H3.3 complexes mediate nucleosome assembly pathways
RT   dependent or independent of DNA synthesis.";
RL   Cell 116:51-61(2004).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA   Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA   Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2151 AND THR-2154, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66 AND SER-1439, 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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10; SER-11; THR-12; SER-20;
RP   SER-66; SER-433; SER-450; SER-673; SER-1439; THR-1924 AND SER-2094, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma, and 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   [11]
RP   PHOSPHORYLATION BY ATM AND CHK2, AND UBIQUITINATION.
RX   PubMed=23303793; DOI=10.1093/nar/gks1319;
RA   Choi S.Y., Jang H., Roe J.S., Kim S.T., Cho E.J., Youn H.D.;
RT   "Phosphorylation and ubiquitination-dependent degradation of CABIN1
RT   releases p53 for transactivation upon genotoxic stress.";
RL   Nucleic Acids Res. 41:2180-2190(2013).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [13]
RP   X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2156-2190 IN COMPLEX WITH MEF2B
RP   AND DNA, AND MUTAGENESIS OF LEU-2172.
RX   PubMed=12700764; DOI=10.1038/nature01555;
RA   Han A., Pan F., Stroud J.C., Youn H.-D., Liu J.O., Chen L.;
RT   "Sequence-specific recruitment of transcriptional co-repressor Cabin1 by
RT   myocyte enhancer factor-2.";
RL   Nature 422:730-734(2003).
CC   -!- FUNCTION: May be required for replication-independent chromatin
CC       assembly. May serve as a negative regulator of T-cell receptor (TCR)
CC       signaling via inhibition of calcineurin. Inhibition of activated
CC       calcineurin is dependent on both PKC and calcium signals. Acts as a
CC       negative regulator of p53/TP53 by keeping p53 in an inactive state on
CC       chromatin at promoters of a subset of it's target genes.
CC       {ECO:0000269|PubMed:14718166, ECO:0000269|PubMed:9655484}.
CC   -!- SUBUNIT: Component of a complex that includes at least ASF1A, CABIN1,
CC       HIRA, histone H3.3 and UBN1. Interacts with calcineurin. Interacts with
CC       MEF2B. {ECO:0000269|PubMed:12700764, ECO:0000269|PubMed:14718166,
CC       ECO:0000269|PubMed:9655484}.
CC   -!- INTERACTION:
CC       Q9Y6J0; Q02080: MEF2B; NbExp=4; IntAct=EBI-2795712, EBI-6427785;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9655484}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y6J0-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9Y6J0-2; Sequence=VSP_054161, VSP_054162;
CC   -!- TISSUE SPECIFICITY: Widely expressed in different tissues.
CC       {ECO:0000269|PubMed:9655484}.
CC   -!- PTM: Activated through PKC-mediated hyperphosphorylation.
CC       Phosphorylation by the DNA damage kinases ATM and CHK2 enhances
CC       ubiquitination. {ECO:0000269|PubMed:23303793,
CC       ECO:0000269|PubMed:9655484}.
CC   -!- PTM: Upon genotoxic stress, ubiquitination by the DCX(DDB2) E3
CC       ubiquitin-protein ligase complex targets CABIN1 for proteasomal
CC       degradation, leading to the release of p53/TP53.
CC       {ECO:0000269|PubMed:23303793}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA20788.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF072441; AAD40846.1; -; mRNA.
DR   EMBL; AP000351; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP000352; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP000353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471095; EAW59639.1; -; Genomic_DNA.
DR   EMBL; BC054497; AAH54497.1; -; mRNA.
DR   EMBL; Z92546; CAB62954.1; -; Genomic_DNA.
DR   EMBL; AB002328; BAA20788.2; ALT_INIT; mRNA.
DR   CCDS; CCDS13823.1; -. [Q9Y6J0-1]
DR   RefSeq; NP_001186210.1; NM_001199281.1. [Q9Y6J0-1]
DR   RefSeq; NP_001188358.1; NM_001201429.1.
DR   RefSeq; NP_036427.1; NM_012295.3. [Q9Y6J0-1]
DR   RefSeq; XP_016884172.1; XM_017028683.1. [Q9Y6J0-2]
DR   PDB; 1N6J; X-ray; 2.20 A; G=2156-2190.
DR   PDBsum; 1N6J; -.
DR   AlphaFoldDB; Q9Y6J0; -.
DR   SMR; Q9Y6J0; -.
DR   BioGRID; 117070; 72.
DR   CORUM; Q9Y6J0; -.
DR   IntAct; Q9Y6J0; 24.
DR   MINT; Q9Y6J0; -.
DR   STRING; 9606.ENSP00000381364; -.
DR   GlyGen; Q9Y6J0; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y6J0; -.
DR   MetOSite; Q9Y6J0; -.
DR   PhosphoSitePlus; Q9Y6J0; -.
DR   SwissPalm; Q9Y6J0; -.
DR   BioMuta; CABIN1; -.
DR   DMDM; 6685261; -.
DR   EPD; Q9Y6J0; -.
DR   jPOST; Q9Y6J0; -.
DR   MassIVE; Q9Y6J0; -.
DR   MaxQB; Q9Y6J0; -.
DR   PaxDb; 9606-ENSP00000381364; -.
DR   PeptideAtlas; Q9Y6J0; -.
DR   ProteomicsDB; 33920; -.
DR   ProteomicsDB; 86699; -. [Q9Y6J0-1]
DR   Pumba; Q9Y6J0; -.
DR   Antibodypedia; 23901; 106 antibodies from 21 providers.
DR   DNASU; 23523; -.
DR   Ensembl; ENST00000263119.10; ENSP00000263119.5; ENSG00000099991.18. [Q9Y6J0-1]
DR   Ensembl; ENST00000398319.6; ENSP00000381364.2; ENSG00000099991.18. [Q9Y6J0-1]
DR   Ensembl; ENST00000405822.6; ENSP00000384694.2; ENSG00000099991.18. [Q9Y6J0-2]
DR   GeneID; 23523; -.
DR   KEGG; hsa:23523; -.
DR   MANE-Select; ENST00000263119.10; ENSP00000263119.5; NM_012295.4; NP_036427.1.
DR   UCSC; uc002zzi.1; human. [Q9Y6J0-1]
DR   AGR; HGNC:24187; -.
DR   CTD; 23523; -.
DR   DisGeNET; 23523; -.
DR   GeneCards; CABIN1; -.
DR   HGNC; HGNC:24187; CABIN1.
DR   HPA; ENSG00000099991; Low tissue specificity.
DR   MIM; 604251; gene.
DR   neXtProt; NX_Q9Y6J0; -.
DR   OpenTargets; ENSG00000099991; -.
DR   PharmGKB; PA164717549; -.
DR   VEuPathDB; HostDB:ENSG00000099991; -.
DR   eggNOG; ENOG502QPUI; Eukaryota.
DR   GeneTree; ENSGT00390000008529; -.
DR   InParanoid; Q9Y6J0; -.
DR   OrthoDB; 8630at2759; -.
DR   PhylomeDB; Q9Y6J0; -.
DR   TreeFam; TF323227; -.
DR   PathwayCommons; Q9Y6J0; -.
DR   Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR   SignaLink; Q9Y6J0; -.
DR   SIGNOR; Q9Y6J0; -.
DR   BioGRID-ORCS; 23523; 128 hits in 1192 CRISPR screens.
DR   ChiTaRS; CABIN1; human.
DR   EvolutionaryTrace; Q9Y6J0; -.
DR   GeneWiki; CABIN1; -.
DR   GenomeRNAi; 23523; -.
DR   Pharos; Q9Y6J0; Tbio.
DR   PRO; PR:Q9Y6J0; -.
DR   Proteomes; UP000005640; Chromosome 22.
DR   RNAct; Q9Y6J0; Protein.
DR   Bgee; ENSG00000099991; Expressed in right hemisphere of cerebellum and 205 other cell types or tissues.
DR   ExpressionAtlas; Q9Y6J0; baseline and differential.
DR   GO; GO:0016235; C:aggresome; IDA:HPA.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0004864; F:protein phosphatase inhibitor activity; NAS:UniProtKB.
DR   GO; GO:0007166; P:cell surface receptor signaling pathway; NAS:UniProtKB.
DR   GO; GO:0006334; P:nucleosome assembly; IDA:GO_Central.
DR   CDD; cd13839; MEF2_binding; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   IDEAL; IID00183; -.
DR   InterPro; IPR033053; Hir3/CABIN1.
DR   InterPro; IPR015134; MEF2-bd.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR15502; CALCINEURIN-BINDING PROTEIN CABIN 1-RELATED; 1.
DR   PANTHER; PTHR15502:SF7; CALCINEURIN-BINDING PROTEIN CABIN-1; 1.
DR   Pfam; PF09047; MEF2_binding; 1.
DR   SMART; SM00028; TPR; 5.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50005; TPR; 4.
DR   PROSITE; PS50293; TPR_REGION; 2.
DR   Genevisible; Q9Y6J0; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Chromatin regulator; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; TPR repeat; Ubl conjugation.
FT   CHAIN           1..2220
FT                   /note="Calcineurin-binding protein cabin-1"
FT                   /id="PRO_0000106275"
FT   REPEAT          36..69
FT                   /note="TPR 1"
FT   REPEAT          90..123
FT                   /note="TPR 2"
FT   REPEAT          125..157
FT                   /note="TPR 3"
FT   REPEAT          615..648
FT                   /note="TPR 4"
FT   REPEAT          1055..1088
FT                   /note="TPR 5"
FT   REPEAT          1106..1139
FT                   /note="TPR 6"
FT   REGION          361..400
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1299..1476
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1668..1845
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1916..2165
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          2116..2153
FT                   /note="Required for interaction with calcineurin"
FT                   /evidence="ECO:0000250"
FT   REGION          2197..2220
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        371..400
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1299..1321
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1329..1348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1357..1371
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1372..1403
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1410..1424
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1428..1444
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1741..1756
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1798..1812
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1977..1991
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2070..2084
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2086..2108
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        2206..2220
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         10
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         11
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         12
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         20
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         66
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         433
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         450
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         673
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1439
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1924
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2094
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         2151
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         2154
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   VAR_SEQ         220..269
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054161"
FT   VAR_SEQ         1344..1372
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_054162"
FT   VARIANT         56
FT                   /note="A -> T (in dbSNP:rs5760185)"
FT                   /id="VAR_052607"
FT   VARIANT         225
FT                   /note="D -> N (in dbSNP:rs17004823)"
FT                   /id="VAR_052608"
FT   VARIANT         517
FT                   /note="S -> R (in dbSNP:rs9624393)"
FT                   /id="VAR_052609"
FT   VARIANT         660
FT                   /note="R -> S (in dbSNP:rs9624395)"
FT                   /id="VAR_052610"
FT   VARIANT         853
FT                   /note="R -> Q (in dbSNP:rs17854874)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_052611"
FT   VARIANT         921
FT                   /note="Q -> E (in dbSNP:rs12166151)"
FT                   /id="VAR_052612"
FT   MUTAGEN         2172
FT                   /note="L->A,K,W: Abrogates binding to MEF2B."
FT                   /evidence="ECO:0000269|PubMed:12700764"
FT   HELIX           2166..2177
FT                   /evidence="ECO:0007829|PDB:1N6J"
SQ   SEQUENCE   2220 AA;  246352 MW;  BA4AD1741056C233 CRC64;
     MIRIAALNAS STIEDDHEGS FKSHKTQTKE AQEAEAFALY HKALDLQKHD RFEESAKAYH
     ELLEASLLRE AVSSGDEKEG LKHPGLILKY STYKNLAQLA AQREDLETAM EFYLEAVMLD
     STDVNLWYKI GHVALRLIRI PLARHAFEEG LRCNPDHWPC LDNLITVLYT LSDYTTCLYF
     ICKALEKDCR YSKGLVLKEK IFEEQPCLRK DSLRMFLKCD MSIHDVSVSA AETQAIVDEA
     LGLRKKRQAL IVREKEPDLK LVQPIPFFTW KCLGESLLAM YNHLTTCEPP RPSLGKRIDL
     SDYQDPSQPL ESSMVVTPVN VIQPSTVSTN PAVAVAEPVV SYTSVATTSF PLHSPGLLET
     GAPVGDISGG DKSKKGVKRK KISEESGETA KRRSARVRNT KCKKEEKVDF QELLMKFLPS
     RLRKLDPEEE DDSFNNYEVQ SEAKLESFPS IGPQRLSFDS ATFMESEKQD VHEFLLENLT
     NGGILELMMR YLKAMGHKFL VRWPPGLAEV VLSVYHSWRR HSTSLPNPLL RDCSNKHIKD
     MMLMSLSCME LQLDQWLLTK GRSSAVSPRN CPAGMVNGRF GPDFPGTHCL GDLLQLSFAS
     SQRDLFEDGW LEFVVRVYWL KARFLALQGD MEQALENYDI CTEMLQSSTA IQVEAGAERR
     DIVIRLPNLH NDSVVSLEEI DKNLKSLERC QSLEEIQRLY EAGDYKAVVH LLRPTLCTSG
     FDRAKHLEFM TSIPERPAQL LLLQDSLLRL KDYRQCFECS DVALNEAVQQ MVNSGEAAAK
     EEWVATVTQL LMGIEQALSA DSSGSILKVS SSTTGLVRLT NNLIQVIDCS MAVQEEAKEP
     HVSSVLPWII LHRIIWQEED TFHSLCHQQQ LQNPAEEGMS ETPMLPSSLM LLNTAHEYLG
     RRSWCCNSDG ALLRFYVRVL QKELAASTSE DTHPYKEELE TALEQCFYCL YSFPSKKSKA
     RYLEEHSAQQ VDLIWEDALF MFEYFKPKTL PEFDSYKTST VSADLANLLK RIATIVPRTE
     RPALSLDKVS AYIEGTSTEV PCLPEGADPS PPVVNELYYL LADYHFKNKE QSKAIKFYMH
     DICICPNRFD SWAGMALARA SRIQDKLNSN ELKSDGPIWK HATPVLNCFR RALEIDSSNL
     SLWIEYGTMS YALHSFASRQ LKQWRGELPP ELVQQMEGRR DSMLETAKHC FTSAARCEGD
     GDEEEWLIHY MLGKVAEKQQ QPPTVYLLHY RQAGHYLHEE AARYPKKIHY HNPPELAMEA
     LEVYFRLHAS ILKLLGKPDS GVGAEVLVNF MKEAAEGPFA RGEEKNTPKA SEKEKACLVD
     EDSHSSAGTL PGPGASLPSS SGPGLTSPPY TATPIDHDYV KCKKPHQQAT PDDRSQDSTA
     VALSDSSSTQ DFFNEPTSLL EGSRKSYTEK RLPILSSQAG ATGKDLQGAT EERGKNEESL
     ESTEGFRAAE QGVQKPAAET PASACIPGKP SASTPTLWDG KKRGDLPGEP VAFPQGLPAG
     AEEQRQFLTE QCIASFRLCL SRFPQHYKSL YRLAFLYTYS KTHRNLQWAR DVLLGSSIPW
     QQLQHMPAQG LFCERNKTNF FNGIWRIPVD EIDRPGSFAW HMNRSIVLLL KVLAQLRDHS
     TLLKVSSMLQ RTPDQGKKYL RDADRQVLAQ RAFILTVKVL EDTLSELAEG SERPGPKVCG
     LPGARMTTDV SHKASPEDGQ EGLPQPKKPP LADGSGPGPE PGGKVGLLNH RPVAMDAGDS
     ADQSGERKDK ESPRAGPTEP MDTSEATVCH SDLERTPPLL PGRPARDRGP ESRPTELSLE
     ELSISARQQP TPLTPAQPAP APAPATTTGT RAGGHPEEPL SRLSRKRKLL EDTESGKTLL
     LDAYRVWQQG QKGVAYDLGR VERIMSETYM LIKQVDEEAA LEQAVKFCQV HLGAAAQRQA
     SGDTPTTPKH PKDSRENFFP VTVVPTAPDP VPADSVQRPS DAHTKPRPAL AAATTIITCP
     PSASASTLDQ SKDPGPPRPH RPEATPSMAS LGPEGEELAR VAEGTSFPPQ EPRHSPQVKM
     APTSSPAEPH CWPAEAALGT GAEPTCSQEG KLRPEPRRDG EAQEAASETQ PLSSPPTAAS
     SKAPSSGSAQ PPEGHPGKPE PSRAKSRPLP NMPKLVIPSA ATKFPPEITV TPPTPTLLSP
     KGSISEETKQ KLKSAILSAQ SAANVRKESL CQPALEVLET SSQESSLESE TDEDDDYMDI
//