CABIN_HUMAN
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 03-AUG-2022, entry version 194.
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=3; 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; 67.
DR CORUM; Q9Y6J0; -.
DR IntAct; Q9Y6J0; 23.
DR MINT; Q9Y6J0; -.
DR STRING; 9606.ENSP00000381364; -.
DR iPTMnet; Q9Y6J0; -.
DR MetOSite; Q9Y6J0; -.
DR PhosphoSitePlus; Q9Y6J0; -.
DR BioMuta; CABIN1; -.
DR DMDM; 6685261; -.
DR EPD; Q9Y6J0; -.
DR jPOST; Q9Y6J0; -.
DR MassIVE; Q9Y6J0; -.
DR MaxQB; Q9Y6J0; -.
DR PaxDb; Q9Y6J0; -.
DR PeptideAtlas; Q9Y6J0; -.
DR PRIDE; Q9Y6J0; -.
DR ProteomicsDB; 33920; -.
DR ProteomicsDB; 86699; -. [Q9Y6J0-1]
DR Antibodypedia; 23901; 97 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 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; 56555at2759; -.
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; 113 hits in 1092 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 203 other tissues.
DR ExpressionAtlas; Q9Y6J0; baseline and differential.
DR Genevisible; Q9Y6J0; HS.
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:0006336; P:DNA replication-independent chromatin assembly; IDA:UniProtKB.
DR CDD; cd13839; MEF2_binding; 1.
DR Gene3D; 1.25.40.10; -; 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; PTHR15502; 1.
DR Pfam; PF09047; MEF2_binding; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
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
