ID CALD1_HUMAN Reviewed; 793 AA.
AC Q05682; A8K0X1; Q13978; Q13979; Q14741; Q14742; Q9UD91;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 3.
DT 27-MAR-2024, entry version 212.
DE RecName: Full=Caldesmon;
DE Short=CDM;
GN Name=CALD1; Synonyms=CAD, CDM;
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 4).
RC TISSUE=Lung fibroblast;
RX PubMed=1885618; DOI=10.1016/s0021-9258(18)55390-4;
RA Novy R.E., Lin J.L.-C., Lin J.J.-C.;
RT "Characterization of cDNA clones encoding a human fibroblast caldesmon
RT isoform and analysis of caldesmon expression in normal and transformed
RT cells.";
RL J. Biol. Chem. 266:16917-16924(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), AND VARIANT ARG-397.
RC TISSUE=Aorta;
RX PubMed=1555769; DOI=10.1016/0378-1119(92)90376-z;
RA Humphrey M.B., Herrera-Sosa H., Gonzalez G., Lee R., Bryan J.;
RT "Cloning of cDNAs encoding human caldesmons.";
RL Gene 112:197-204(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3 AND 5).
RX PubMed=1465449; DOI=10.1073/pnas.89.24.12122;
RA Hayashi K., Yano H., Hashida T., Takeuchi R., Takeda O., Asada K.,
RA Takahashi E., Kato I., Sobue K.;
RT "Genomic structure of the human caldesmon gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:12122-12126(1992).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Amygdala;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Skin;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 497-793, AND FUNCTION.
RC TISSUE=Fetal liver;
RX PubMed=8227296; DOI=10.1007/bf00121289;
RA Huber P.A.J., Redwood C.S., Avent N.D., Tanner M.J.A., Marston S.B.;
RT "Identification of functioning regulatory sites and a new myosin binding
RT site in the C-terminal 288 amino acids of caldesmon expressed from a human
RT clone.";
RL J. Muscle Res. Cell Motil. 14:385-391(1993).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-730, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6), PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-730, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-730; THR-753 AND
RP SER-789, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 (ISOFORMS 3 AND
RP 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-724; THR-730 AND THR-753,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; TYR-21 AND SER-196
RP (ISOFORMS 3 AND 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643 AND SER-789,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-656; THR-730; THR-753 AND
RP SER-759, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129 AND THR-753,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202 (ISOFORMS 2; 4 AND 6),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-196 (ISOFORMS 3 AND 5), AND
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-459 AND LYS-645, SUMOYLATION
RP [LARGE SCALE ANALYSIS] AT LYS-209 (ISOFORM 4), SUMOYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-203 (ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Actin- and myosin-binding protein implicated in the
CC regulation of actomyosin interactions in smooth muscle and nonmuscle
CC cells (could act as a bridge between myosin and actin filaments).
CC Stimulates actin binding of tropomyosin which increases the
CC stabilization of actin filament structure. In muscle tissues, inhibits
CC the actomyosin ATPase by binding to F-actin. This inhibition is
CC attenuated by calcium-calmodulin and is potentiated by tropomyosin.
CC Interacts with actin, myosin, two molecules of tropomyosin and with
CC calmodulin. Also plays an essential role during cellular mitosis and
CC receptor capping. Involved in Schwann cell migration during peripheral
CC nerve regeneration (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:8227296}.
CC -!- INTERACTION:
CC Q05682; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-1642116, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P13505}. Cytoplasm, myofibril
CC {ECO:0000250|UniProtKB:P13505}. Cytoplasm, cytoskeleton, stress fiber
CC {ECO:0000250|UniProtKB:P13505}. Note=On thin filaments in smooth muscle
CC and on stress fibers in fibroblasts (nonmuscle).
CC {ECO:0000250|UniProtKB:P13505}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=H-CAD;
CC IsoId=Q05682-1; Sequence=Displayed;
CC Name=2; Synonyms=WI-38 L-CAD I;
CC IsoId=Q05682-2; Sequence=VSP_004155;
CC Name=3; Synonyms=HELA L-CAD I;
CC IsoId=Q05682-3; Sequence=VSP_004154, VSP_004155;
CC Name=4; Synonyms=WI-38 L-CAD II, 1-CAD;
CC IsoId=Q05682-4; Sequence=VSP_004156;
CC Name=5; Synonyms=HELA L-CAD II;
CC IsoId=Q05682-5; Sequence=VSP_004154, VSP_004156;
CC Name=6;
CC IsoId=Q05682-6; Sequence=VSP_004155, VSP_043292;
CC -!- TISSUE SPECIFICITY: High-molecular-weight caldesmon (isoform 1) is
CC predominantly expressed in smooth muscles, whereas low-molecular-weight
CC caldesmon (isoforms 2, 3, 4 and 5) are widely distributed in non-muscle
CC tissues and cells. Not expressed in skeletal muscle or heart.
CC -!- DOMAIN: The N-terminal part seems to be a myosin/calmodulin-binding
CC domain, and the C-terminal a tropomyosin/actin/calmodulin-binding
CC domain. These two domains are separated by a central helical region in
CC the smooth-muscle form.
CC -!- PTM: In non-muscle cells, phosphorylation by CDK1 during mitosis causes
CC caldesmon to dissociate from microfilaments. Phosphorylation reduces
CC caldesmon binding to actin, myosin, and calmodulin as well as its
CC inhibition of actomyosin ATPase activity. Phosphorylation also occurs
CC in both quiescent and dividing smooth muscle cells with similar effects
CC on the interaction with actin and calmodulin and on microfilaments
CC reorganization. CDK1-mediated phosphorylation promotes Schwann cell
CC migration during peripheral nerve regeneration (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the caldesmon family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M64110; AAA35636.1; -; mRNA.
DR EMBL; M83216; AAA58420.1; -; mRNA.
DR EMBL; M83216; AAA58419.1; -; mRNA.
DR EMBL; D90452; BAA14418.1; -; mRNA.
DR EMBL; D90453; BAA14419.1; -; mRNA.
DR EMBL; AK289686; BAF82375.1; -; mRNA.
DR EMBL; AC019014; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC083870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC040354; AAH40354.1; -; mRNA.
DR CCDS; CCDS47716.1; -. [Q05682-3]
DR CCDS; CCDS47717.1; -. [Q05682-5]
DR CCDS; CCDS5834.1; -. [Q05682-4]
DR CCDS; CCDS5835.1; -. [Q05682-1]
DR CCDS; CCDS5836.2; -. [Q05682-6]
DR PIR; JH0628; JH0628.
DR RefSeq; NP_004333.1; NM_004342.6. [Q05682-4]
DR RefSeq; NP_149129.2; NM_033138.3. [Q05682-1]
DR RefSeq; NP_149130.1; NM_033139.3. [Q05682-3]
DR RefSeq; NP_149131.1; NM_033140.3. [Q05682-5]
DR RefSeq; NP_149347.2; NM_033157.3. [Q05682-6]
DR RefSeq; XP_016868140.1; XM_017012651.1.
DR RefSeq; XP_016868141.1; XM_017012652.1. [Q05682-4]
DR AlphaFoldDB; Q05682; -.
DR BMRB; Q05682; -.
DR SMR; Q05682; -.
DR BioGRID; 107251; 250.
DR IntAct; Q05682; 63.
DR MINT; Q05682; -.
DR STRING; 9606.ENSP00000354826; -.
DR GlyGen; Q05682; 5 sites, 1 O-linked glycan (5 sites).
DR iPTMnet; Q05682; -.
DR MetOSite; Q05682; -.
DR PhosphoSitePlus; Q05682; -.
DR SwissPalm; Q05682; -.
DR BioMuta; CALD1; -.
DR DMDM; 338817891; -.
DR OGP; Q05682; -.
DR CPTAC; CPTAC-323; -.
DR CPTAC; CPTAC-324; -.
DR EPD; Q05682; -.
DR jPOST; Q05682; -.
DR MassIVE; Q05682; -.
DR MaxQB; Q05682; -.
DR PaxDb; 9606-ENSP00000354826; -.
DR PeptideAtlas; Q05682; -.
DR ProteomicsDB; 58344; -. [Q05682-1]
DR ProteomicsDB; 58345; -. [Q05682-2]
DR ProteomicsDB; 58346; -. [Q05682-3]
DR ProteomicsDB; 58347; -. [Q05682-4]
DR ProteomicsDB; 58348; -. [Q05682-5]
DR ProteomicsDB; 58349; -. [Q05682-6]
DR Antibodypedia; 1954; 1492 antibodies from 46 providers.
DR DNASU; 800; -.
DR Ensembl; ENST00000361675.7; ENSP00000354826.2; ENSG00000122786.20. [Q05682-1]
DR Ensembl; ENST00000361901.6; ENSP00000354513.2; ENSG00000122786.20. [Q05682-4]
DR Ensembl; ENST00000393118.7; ENSP00000376826.2; ENSG00000122786.20. [Q05682-3]
DR Ensembl; ENST00000417172.5; ENSP00000398826.1; ENSG00000122786.20. [Q05682-4]
DR Ensembl; ENST00000422748.5; ENSP00000395710.1; ENSG00000122786.20. [Q05682-6]
DR Ensembl; ENST00000424922.5; ENSP00000393621.1; ENSG00000122786.20. [Q05682-5]
DR GeneID; 800; -.
DR KEGG; hsa:800; -.
DR MANE-Select; ENST00000361675.7; ENSP00000354826.2; NM_033138.4; NP_149129.2.
DR UCSC; uc003vrz.4; human. [Q05682-1]
DR AGR; HGNC:1441; -.
DR CTD; 800; -.
DR DisGeNET; 800; -.
DR GeneCards; CALD1; -.
DR HGNC; HGNC:1441; CALD1.
DR HPA; ENSG00000122786; Tissue enhanced (intestine).
DR MIM; 114213; gene.
DR neXtProt; NX_Q05682; -.
DR OpenTargets; ENSG00000122786; -.
DR PharmGKB; PA26034; -.
DR VEuPathDB; HostDB:ENSG00000122786; -.
DR eggNOG; ENOG502QSYB; Eukaryota.
DR GeneTree; ENSGT00940000153901; -.
DR HOGENOM; CLU_017579_1_0_1; -.
DR InParanoid; Q05682; -.
DR OMA; NGERFQE; -.
DR OrthoDB; 4273102at2759; -.
DR PhylomeDB; Q05682; -.
DR TreeFam; TF331771; -.
DR PathwayCommons; Q05682; -.
DR Reactome; R-HSA-445355; Smooth Muscle Contraction.
DR SignaLink; Q05682; -.
DR SIGNOR; Q05682; -.
DR BioGRID-ORCS; 800; 20 hits in 1152 CRISPR screens.
DR ChiTaRS; CALD1; human.
DR GeneWiki; Caldesmon; -.
DR GenomeRNAi; 800; -.
DR Pharos; Q05682; Tbio.
DR PRO; PR:Q05682; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q05682; Protein.
DR Bgee; ENSG00000122786; Expressed in blood vessel layer and 220 other cell types or tissues.
DR ExpressionAtlas; Q05682; baseline and differential.
DR Genevisible; Q05682; HS.
DR GO; GO:0030478; C:actin cap; IEA:Ensembl.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030016; C:myofibril; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001725; C:stress fiber; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0005516; F:calmodulin binding; TAS:ProtInc.
DR GO; GO:0017022; F:myosin binding; IBA:GO_Central.
DR GO; GO:0005523; F:tropomyosin binding; TAS:ProtInc.
DR GO; GO:0051017; P:actin filament bundle assembly; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; IBA:GO_Central.
DR GO; GO:0006936; P:muscle contraction; IEA:InterPro.
DR InterPro; IPR006017; Caldesmon.
DR InterPro; IPR006018; Caldesmon_LSP.
DR PANTHER; PTHR18949; CALDESMON; 1.
DR PANTHER; PTHR18949:SF0; CALDESMON; 1.
DR Pfam; PF02029; Caldesmon; 2.
DR PRINTS; PR01076; CALDESMON.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Calmodulin-binding; Cytoplasm;
KW Cytoskeleton; Isopeptide bond; Muscle protein; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..793
FT /note="Caldesmon"
FT /id="PRO_0000089288"
FT REPEAT 319..332
FT /note="1"
FT REPEAT 333..346
FT /note="2"
FT REPEAT 347..360
FT /note="3"
FT REGION 26..207
FT /note="Myosin and calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 26..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 108..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 319..375
FT /note="3 X 14 AA tandem repeats of E-E-E-K-R-A-A-E-E-R-Q-R-
FT I-K"
FT REGION 434..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 492..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 564..621
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000255"
FT REGION 653..686
FT /note="Strong actin-binding"
FT /evidence="ECO:0000250"
FT REGION 664..674
FT /note="Tropomyosin-binding"
FT /evidence="ECO:0000255"
FT REGION 687..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 716..722
FT /note="Calmodulin-binding"
FT /evidence="ECO:0000250"
FT REGION 721..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 747..793
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 768..793
FT /note="Weak actin-binding"
FT /evidence="ECO:0000250"
FT COMPBIAS 26..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..123
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..203
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..407
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 492..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..640
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 643
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 730
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 753
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 789
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT CROSSLNK 459
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 645
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..24
FT /note="MDDFERRRELRRQKREEMRLEAER -> MLGGSGSHGRRSLAALSQ (in
FT isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:1465449"
FT /id="VSP_004154"
FT VAR_SEQ 208..462
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:1465449,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:1555769,
FT ECO:0000303|PubMed:1885618"
FT /id="VSP_004156"
FT VAR_SEQ 208..436
FT /note="Missing (in isoform 2, isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:1465449,
FT ECO:0000303|PubMed:14702039"
FT /id="VSP_004155"
FT VAR_SEQ 660
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043292"
FT VARIANT 397
FT /note="H -> R (in dbSNP:rs6973420)"
FT /evidence="ECO:0000269|PubMed:1555769"
FT /id="VAR_065254"
FT CONFLICT 530
FT /note="V -> M (in Ref. 1; AAA35636)"
FT /evidence="ECO:0000305"
FT MOD_RES Q05682-2:202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES Q05682-3:12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q05682-3:21
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q05682-3:196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES Q05682-4:202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK Q05682-4:209
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MOD_RES Q05682-5:12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES Q05682-5:21
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES Q05682-5:196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK Q05682-5:203
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT MOD_RES Q05682-6:202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
SQ SEQUENCE 793 AA; 93231 MW; 7468E2C3E40BF697 CRC64;
MDDFERRREL RRQKREEMRL EAERIAYQRN DDDEEEAARE RRRRARQERL RQKQEEESLG
QVTDQVEVNA QNSVPDEEAK TTTTNTQVEG DDEAAFLERL ARREERRQKR LQEALERQKE
FDPTITDASL SLPSRRMQND TAENETTEKE EKSESRQERY EIEETETVTK SYQKNDWRDA
EENKKEDKEK EEEEEEKPKR GSIGENQVEV MVEEKTTESQ EETVVMSLKN GQISSEEPKQ
EEEREQGSDE ISHHEKMEEE DKERAEAERA RLEAEERERI KAEQDKKIAD ERARIEAEEK
AAAQERERRE AEERERMREE EKRAAEERQR IKEEEKRAAE ERQRIKEEEK RAAEERQRIK
EEEKRAAEER QRARAEEEEK AKVEEQKRNK QLEEKKHAMQ ETKIKGEKVE QKIEGKWVNE
KKAQEDKLQT AVLKKQGEEK GTKVQAKREK LQEDKPTFKK EEIKDEKIKK DKEPKEEVKS
FMDRKKGFTE VKSQNGEFMT HKLKHTENTF SRPGGRASVD TKEAEGAPQV EAGKRLEELR
RRRGETESEE FEKLKQKQQE AALELEELKK KREERRKVLE EEEQRRKQEE ADRKLREEEE
KRRLKEEIER RRAEAAEKRQ KMPEDGLSDD KKPFKCFTPK GSSLKIEERA EFLNKSVQKS
SGVKSTHQAA IVSKIDSRLE QYTSAIEGTK SAKPTKPAAS DLPVPAEGVR NIKSMWEKGN
VFSSPTAAGT PNKETAGLKV GVSSRINEWL TKTPDGNKSP APKPSDLRPG DVSSKRNLWE
KQSVDKVTSP TKV
//
