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CALD1_HUMAN
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   03-AUG-2022, entry version 203.
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}.
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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   BioGRID; 107251; 108.
DR   IntAct; Q05682; 57.
DR   MINT; Q05682; -.
DR   STRING; 9606.ENSP00000354826; -.
DR   GlyGen; Q05682; 1 site, 1 O-linked glycan (1 site).
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; Q05682; -.
DR   PeptideAtlas; Q05682; -.
DR   PRIDE; 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; 1322 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; ENST00000393118.6; 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   CTD; 800; -.
DR   DisGeNET; 800; -.
DR   GeneCards; CALD1; -.
DR   HGNC; HGNC:1441; CALD1.
DR   HPA; ENSG00000122786; Low tissue specificity.
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; NQVEAMV; -.
DR   OrthoDB; 1038798at2759; -.
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; 17 hits in 1074 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 218 other 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: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; PTHR18949; 2.
DR   PANTHER; PTHR18949:SF0; PTHR18949:SF0; 2.
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
 
 
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