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CALM3_MOUSE
ID   CALM3_MOUSE             Reviewed;         149 AA.
AC   P0DP28; 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 38.
DE   RecName: Full=Calmodulin-3 {ECO:0000250|UniProtKB:P0DP25};
GN   Name=Calm3 {ECO:0000312|MGI:MGI:103249}; Synonyms=Cam3, 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 [MRNA].
RX   PubMed=3384819; DOI=10.1016/s0021-9258(19)81579-x;
RA   Bender P.K., Dedman J.R., Emerson C.P. Jr.;
RT   "The abundance of calmodulin mRNAs is regulated in phosphorylase kinase-
RT   deficient skeletal muscle.";
RL   J. Biol. Chem. 263:9733-9737(1988).
RN   [2]
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   [3]
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   [4]
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   [5]
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   [6]
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   [7]
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   [8]
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   [9]
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   [10]
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   [11]
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. Is
CC       a regulator of voltage-dependent L-type calcium channels. Among the
CC       enzymes to be stimulated by the calmodulin-calcium complex are a number
CC       of protein kinases and phosphatases. Together with CCP110 and centrin,
CC       is involved in a genetic pathway that regulates the centrosome cycle
CC       and progression through cytokinesis. {ECO:0000250|UniProtKB:P0DP25}.
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:P0DP25,
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:P0DP25}.
CC   -!- SIMILARITY: Belongs to the calmodulin family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC39089.2; Type=Erroneous translation; Note=Wrong CDS prediction.; Evidence={ECO:0000305};
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DR   EMBL; M19380; AAA66181.1; -; mRNA.
DR   EMBL; AK083996; BAC39089.2; ALT_SEQ; mRNA.
DR   EMBL; AK151610; BAE30549.1; -; mRNA.
DR   EMBL; AK152754; BAE31469.1; -; mRNA.
DR   EMBL; AK153179; BAE31782.1; -; mRNA.
DR   EMBL; BC050926; AAH50926.1; -; mRNA.
DR   CCDS; CCDS39789.1; -.
DR   PIR; S37707; S37707.
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; P0DP28; -.
DR   SMR; P0DP28; -.
DR   iPTMnet; P0DP28; -.
DR   jPOST; P0DP28; -.
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:103249; Calm3.
DR   VEuPathDB; HostDB:ENSMUSG00000001175; -.
DR   VEuPathDB; HostDB:ENSMUSG00000019370; -.
DR   VEuPathDB; HostDB:ENSMUSG00000036438; -.
DR   GeneTree; ENSGT00950000182980; -.
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; Calm3; mouse.
DR   PRO; PR:P0DP28; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   Proteomes; UP000000589; Chromosome 17.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; P0DP28; protein.
DR   Bgee; ENSMUSG00000001175; Expressed in ureter smooth muscle and 281 other tissues.
DR   ExpressionAtlas; P0DP28; 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; ISO:MGI.
DR   GO; GO:0030426; C:growth cone; ISO:MGI.
DR   GO; GO:0031966; C:mitochondrial membrane; ISO:MGI.
DR   GO; GO:0043209; C:myelin sheath; IDA:CAFA.
DR   GO; GO:0043005; C:neuron projection; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR   GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
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; ISO:MGI.
DR   GO; GO:0030235; F:nitric-oxide synthase regulator activity; ISO:MGI.
DR   GO; GO:0043548; F:phosphatidylinositol 3-kinase binding; ISO:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR   GO; GO:0047485; F:protein N-terminus 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; ISO:MGI.
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:1901842; P:negative regulation of high voltage-gated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; ISO:MGI.
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:0098901; P:regulation of cardiac muscle cell action potential; ISS:UniProtKB.
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: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.4"
FT   CHAIN           2..149
FT                   /note="Calmodulin-3"
FT                   /id="PRO_0000439937"
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:P0DP25"
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.4"
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:P0DP31"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DP25"
FT   MOD_RES         95
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DP25"
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:P0DP25"
FT   MOD_RES         116
FT                   /note="N6,N6,N6-trimethyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0DP25"
FT   MOD_RES         116
FT                   /note="N6-methyllysine; alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0DP25"
FT   MOD_RES         139
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:P0DP25"
FT   CROSSLNK        22
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P0DP25"
FT   CROSSLNK        22
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000250|UniProtKB:P62157"
FT   CONFLICT        142
FT                   /note="F -> S (in Ref. 2; BAC39089)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   149 AA;  16838 MW;  6B4BC3FCDE10727B CRC64;
     MADQLTEEQI AEFKEAFSLF DKDGDGTITT KELGTVMRSL GQNPTEAELQ DMINEVDADG
     NGTIDFPEFL TMMARKMKDT DSEEEIREAF RVFDKDGNGY ISAAELRHVM TNLGEKLTDE
     EVDEMIREAD IDGDGQVNYE EFVQMMTAK
 
 
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