CALM2_MOUSE
ID CALM2_MOUSE Reviewed; 149 AA.
AC P0DP27; P02593; P62204; P70667; P99014; Q3TEH7; Q3THK5; Q3U6Z5; Q3U7C7;
AC Q498A3; Q61379; Q61380; Q8BNC9; Q91VQ9; Q9D6G4;
DT 10-MAY-2017, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 1.
DT 03-AUG-2022, entry version 36.
DE RecName: Full=Calmodulin-2 {ECO:0000250|UniProtKB:P0DP24};
GN Name=Calm2 {ECO:0000312|MGI:MGI:103250}; Synonyms=Cam2, CamC;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
RX PubMed=2551780; DOI=10.1016/0378-1119(89)90259-x;
RA Danchin A., Sezer O., Glaser P., Chalon P., Caput D.;
RT "Cloning and expression of mouse-brain calmodulin as an activator of
RT Bordetella pertussis adenylate cyclase in Escherichia coli.";
RL Gene 80:145-149(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CAST/EiJ; TISSUE=Brain;
RX PubMed=16670015; DOI=10.1186/1471-2164-7-102;
RA Farber C.R., Corva P.M., Medrano J.F.;
RT "Genome-wide isolation of growth and obesity QTL using mouse speed congenic
RT strains.";
RL BMC Genomics 7:102-102(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD;
RC TISSUE=Amnion, Bone marrow, Colon, Hippocampus, Kidney, Liver, Lung,
RC Mammary gland, Ovary, Placenta, Stomach, Testis, Thymus, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=129, C57BL/6J, and Czech II;
RC TISSUE=Brain, Mammary tumor, Placenta, and Spinal ganglion;
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 [MRNA] OF 1-131.
RX PubMed=7828884; DOI=10.1016/0378-1119(94)90665-3;
RA Skinner T.L., Kerns R.T., Bender P.K.;
RT "Three different calmodulin-encoding cDNAs isolated by a modified 5'-RACE
RT using degenerate oligodeoxyribonucleotides.";
RL Gene 151:247-251(1994).
RN [6]
RP PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Liver;
RA Bienvenut W.V.;
RL Submitted (JUL-2005) to UniProtKB.
RN [7]
RP PROTEIN SEQUENCE OF 15-31; 79-87 AND 92-107, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
RA Lubec G., Klug S., Kang S.U.;
RL Submitted (APR-2007) to UniProtKB.
RN [8]
RP INTERACTION WITH RYR1 AND RYR2.
RX PubMed=18650434; DOI=10.1074/jbc.m804432200;
RA Wright N.T., Prosser B.L., Varney K.M., Zimmer D.B., Schneider M.F.,
RA Weber D.J.;
RT "S100A1 and calmodulin compete for the same binding site on ryanodine
RT receptor.";
RL J. Biol. Chem. 283:26676-26683(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-100 AND SER-102, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-22, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [12]
RP INTERACTION WITH IQCF1.
RX PubMed=25380116; DOI=10.1111/andr.296;
RA Fang P., Xu W., Li D., Zhao X., Dai J., Wang Z., Yan X., Qin M., Zhang Y.,
RA Xu C., Wang L., Qiao Z.;
RT "A novel acrosomal protein, IQCF1, involved in sperm capacitation and the
RT acrosome reaction.";
RL Andrology 3:332-344(2015).
RN [13]
RP INTERACTION WITH SYT7.
RX PubMed=24569478; DOI=10.7554/elife.01524;
RA Liu H., Bai H., Hui E., Yang L., Evans C.S., Wang Z., Kwon S.E.,
RA Chapman E.R.;
RT "Synaptotagmin 7 functions as a Ca2+-sensor for synaptic vesicle
RT replenishment.";
RL Elife 3:E01524-E01524(2014).
CC -!- FUNCTION: Calmodulin mediates the control of a large number of enzymes,
CC ion channels, aquaporins and other proteins through calcium-binding.
CC Among the enzymes to be stimulated by the calmodulin-calcium complex
CC are a number of protein kinases and phosphatases. Together with CCP110
CC and centrin, is involved in a genetic pathway that regulates the
CC centrosome cycle and progression through cytokinesis. Mediates calcium-
CC dependent inactivation of CACNA1C. Positively regulates calcium-
CC activated potassium channel activity of KCNN2.
CC {ECO:0000250|UniProtKB:P62158}.
CC -!- SUBUNIT: Interacts with CEP97, CCP110, MYO1C, TTN/titin and SRY.
CC Interacts with MYO10. Interacts with RRAD (By similarity). Interacts
CC with USP6; the interaction is calcium dependent (By similarity).
CC Interacts with CDK5RAP2. Interacts with SCN5A (By similarity).
CC Interacts with FCHO1. Interacts with MIP in a 1:2 stoichiometry; the
CC interaction with the cytoplasmic domains from two MIP subunits promotes
CC MIP water channel closure. Interacts with ORAI1; this may play a role
CC in the regulation of ORAI1-mediated calcium transport (By similarity).
CC Interacts with RYR1 (PubMed:18650434). Interacts with MYO5A (By
CC similarity). Interacts with IQCF1 (PubMed:25380116). Interacts with
CC SYT7 (PubMed:24569478). Interacts with CEACAM1 (via cytoplasmic
CC domain); this interaction is in a calcium dependent manner and reduces
CC homophilic cell adhesion through dissociation of dimer (By similarity).
CC Interacts with RYR2; regulates RYR2 calcium-release channel activity
CC (PubMed:18650434). Interacts with PCP4; regulates calmodulin calcium-
CC binding (By similarity). Interacts with the heterotetrameric KCNQ2 and
CC KCNQ3 channel; the interaction is calcium-independent, constitutive and
CC participates in the proper assembly of a functional heterotetrameric M
CC channel (By similarity). {ECO:0000250|UniProtKB:P0DP24,
CC ECO:0000250|UniProtKB:P0DP26, ECO:0000250|UniProtKB:P62161,
CC ECO:0000269|PubMed:18650434, ECO:0000269|PubMed:24569478,
CC ECO:0000269|PubMed:25380116}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Cytoplasm,
CC cytoskeleton, spindle pole. Note=Distributed throughout the cell during
CC interphase, but during mitosis becomes dramatically localized to the
CC spindle poles and the spindle microtubules. {ECO:0000250}.
CC -!- PTM: Ubiquitination results in a strongly decreased activity.
CC {ECO:0000250}.
CC -!- PTM: Phosphorylation results in a decreased activity. {ECO:0000250}.
CC -!- MISCELLANEOUS: This protein has four functional calcium-binding sites.
CC {ECO:0000250|UniProtKB:P0DP24}.
CC -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
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DR EMBL; M27844; AAA37365.1; -; Genomic_DNA.
DR EMBL; AY902353; AAY21063.1; -; Genomic_DNA.
DR EMBL; AK012247; BAB28116.1; -; mRNA.
DR EMBL; AK012564; BAB28319.1; -; mRNA.
DR EMBL; AK013068; BAB28631.1; -; mRNA.
DR EMBL; AK152303; BAE31109.1; -; mRNA.
DR EMBL; AK160636; BAE35930.1; -; mRNA.
DR EMBL; AK161268; BAE36280.1; -; mRNA.
DR EMBL; AK161984; BAE36667.1; -; mRNA.
DR EMBL; AK168741; BAE40582.1; -; mRNA.
DR EMBL; BC010730; AAH10730.1; -; mRNA.
DR EMBL; BC021347; AAH21347.1; -; mRNA.
DR EMBL; BC051444; AAH51444.1; -; mRNA.
DR EMBL; BC100301; AAI00302.1; -; mRNA.
DR EMBL; L31642; AAA65934.1; -; mRNA.
DR CCDS; CCDS37716.1; -.
DR RefSeq; NP_031615.1; NM_007589.5.
DR RefSeq; NP_031616.1; NM_007590.3.
DR RefSeq; NP_033920.1; NM_009790.5.
DR AlphaFoldDB; P0DP27; -.
DR SMR; P0DP27; -.
DR iPTMnet; P0DP27; -.
DR jPOST; P0DP27; -.
DR Antibodypedia; 39411; 188 antibodies from 17 providers.
DR Antibodypedia; 4344; 533 antibodies from 34 providers.
DR Antibodypedia; 53945; 72 antibodies from 14 providers.
DR DNASU; 12313; -.
DR Ensembl; ENSMUST00000019514; ENSMUSP00000019514; ENSMUSG00000019370.
DR Ensembl; ENSMUST00000040440; ENSMUSP00000048857; ENSMUSG00000036438.
DR Ensembl; ENSMUST00000110082; ENSMUSP00000105709; ENSMUSG00000001175.
DR GeneID; 12313; -.
DR GeneID; 12314; -.
DR GeneID; 12315; -.
DR KEGG; mmu:12313; -.
DR KEGG; mmu:12314; -.
DR KEGG; mmu:12315; -.
DR CTD; 801; -.
DR CTD; 805; -.
DR CTD; 808; -.
DR MGI; MGI:103250; Calm2.
DR VEuPathDB; HostDB:ENSMUSG00000001175; -.
DR VEuPathDB; HostDB:ENSMUSG00000019370; -.
DR VEuPathDB; HostDB:ENSMUSG00000036438; -.
DR OMA; SCDRHPP; -.
DR OrthoDB; 1386217at2759; -.
DR BioGRID-ORCS; 12313; 6 hits in 76 CRISPR screens.
DR BioGRID-ORCS; 12314; 4 hits in 69 CRISPR screens.
DR BioGRID-ORCS; 12315; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Calm2; mouse.
DR PRO; PR:P0DP27; -.
DR Proteomes; UP000000589; Chromosome 12.
DR Proteomes; UP000000589; Chromosome 17.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P0DP27; protein.
DR Bgee; ENSMUSG00000001175; Expressed in ureter smooth muscle and 281 other tissues.
DR ExpressionAtlas; P0DP27; baseline and differential.
DR GO; GO:0034704; C:calcium channel complex; ISO:MGI.
DR GO; GO:1902494; C:catalytic complex; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IDA:ARUK-UCL.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0043209; C:myelin sheath; IDA:CAFA.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0030017; C:sarcomere; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; ISO:MGI.
DR GO; GO:0000922; C:spindle pole; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; IDA:ARUK-UCL.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IGI:MGI.
DR GO; GO:0010856; F:adenylate cyclase activator activity; ISO:MGI.
DR GO; GO:0008179; F:adenylate cyclase binding; ISO:MGI.
DR GO; GO:0019855; F:calcium channel inhibitor activity; ISS:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:ARUK-UCL.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:MGI.
DR GO; GO:0030234; F:enzyme regulator activity; IBA:GO_Central.
DR GO; GO:0031997; F:N-terminal myristoylation domain binding; ISO:MGI.
DR GO; GO:0050998; F:nitric-oxide synthase binding; IEA:Ensembl.
DR GO; GO:0030235; F:nitric-oxide synthase regulator activity; IEA:Ensembl.
DR GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; IEA:Ensembl.
DR GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0072542; F:protein phosphatase activator activity; ISO:MGI.
DR GO; GO:0031432; F:titin binding; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0031800; F:type 3 metabotropic glutamate receptor binding; IEA:Ensembl.
DR GO; GO:0007190; P:activation of adenylate cyclase activity; IEA:Ensembl.
DR GO; GO:0016240; P:autophagosome membrane docking; IEA:Ensembl.
DR GO; GO:0019722; P:calcium-mediated signaling; IEA:Ensembl.
DR GO; GO:0005513; P:detection of calcium ion; ISO:MGI.
DR GO; GO:0090151; P:establishment of protein localization to mitochondrial membrane; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; IDA:MGI.
DR GO; GO:1990456; P:mitochondrion-endoplasmic reticulum membrane tethering; IEA:Ensembl.
DR GO; GO:1905913; P:negative regulation of calcium ion export across plasma membrane; IDA:ARUK-UCL.
DR GO; GO:1901020; P:negative regulation of calcium ion transmembrane transporter activity; IDA:ARUK-UCL.
DR GO; GO:1901842; P:negative regulation of high voltage-gated calcium channel activity; IEA:Ensembl.
DR GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISS:UniProtKB.
DR GO; GO:0051343; P:positive regulation of cyclic-nucleotide phosphodiesterase activity; ISO:MGI.
DR GO; GO:0051000; P:positive regulation of nitric-oxide synthase activity; IEA:Ensembl.
DR GO; GO:0032516; P:positive regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR GO; GO:0035307; P:positive regulation of protein dephosphorylation; ISO:MGI.
DR GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
DR GO; GO:0050848; P:regulation of calcium-mediated signaling; IGI:ARUK-UCL.
DR GO; GO:0098901; P:regulation of cardiac muscle cell action potential; IEA:Ensembl.
DR GO; GO:0055117; P:regulation of cardiac muscle contraction; ISO:MGI.
DR GO; GO:0032465; P:regulation of cytokinesis; ISO:MGI.
DR GO; GO:0002027; P:regulation of heart rate; ISO:MGI.
DR GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; ISO:MGI.
DR GO; GO:0060314; P:regulation of ryanodine-sensitive calcium-release channel activity; IBA:GO_Central.
DR GO; GO:1900242; P:regulation of synaptic vesicle endocytosis; IEA:Ensembl.
DR GO; GO:2000300; P:regulation of synaptic vesicle exocytosis; IEA:Ensembl.
DR GO; GO:0001975; P:response to amphetamine; IEA:Ensembl.
DR GO; GO:0051592; P:response to calcium ion; ISO:MGI.
DR GO; GO:0051412; P:response to corticosterone; IEA:Ensembl.
DR CDD; cd00051; EFh; 2.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 4.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Acetylation; Calcium; Cytoplasm; Cytoskeleton; Direct protein sequencing;
KW Isopeptide bond; Metal-binding; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.6"
FT CHAIN 2..149
FT /note="Calmodulin-2"
FT /id="PRO_0000439936"
FT DOMAIN 8..43
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 44..79
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 81..116
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 117..149
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REGION 77..149
FT /note="Necessary and sufficient for interaction with PCP4"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT BINDING 21
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 23
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 25
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 27
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 32
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 57
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 59
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 61
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 63
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 94
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 96
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 98
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 100
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 105
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 130
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 132
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 134
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 141
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.6"
FT MOD_RES 22
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 45
FT /note="Phosphothreonine; by CaMK4"
FT /evidence="ECO:0000250|UniProtKB:P0DP30"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 95
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 100
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 111
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 116
FT /note="N6,N6,N6-trimethyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 116
FT /note="N6-methyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT MOD_RES 139
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P0DP24"
FT CROSSLNK 22
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin); alternate"
FT /evidence="ECO:0000250|UniProtKB:P62157"
SQ SEQUENCE 149 AA; 16838 MW; 6B4BC3FCDE10727B CRC64;
MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
EVDEMIREAD IDGDGQVNYE EFVQMMTAK
