ID DESM_MOUSE Reviewed; 469 AA. AC P31001; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 27-MAR-2024, entry version 197. DE RecName: Full=Desmin; GN Name=Des; 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=8120103; DOI=10.1083/jcb.124.5.827; RA Li H., Choudhary S.K., Milner D.J., Munir M.I., Kuisk I.R., Capetanaki Y.; RT "Inhibition of desmin expression blocks myoblast fusion and interferes with RT the myogenic regulators MyoD and myogenin."; RL J. Cell Biol. 124:827-841(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Colon; 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 [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-40. RC STRAIN=BALB/cJ; TISSUE=Spleen; RX PubMed=8382796; DOI=10.1093/nar/21.2.335; RA Li H., Capetanaki Y.; RT "Regulation of the mouse desmin gene: transactivated by MyoD, myogenin, RT MRF4 and Myf5."; RL Nucleic Acids Res. 21:335-343(1993). RN [4] RP INTERACTION WITH DST. RX PubMed=10357897; DOI=10.1006/dbio.1999.9263; RA Dalpe G., Mathieu M., Comtois A., Zhu E., Wasiak S., De Repentigny Y., RA Leclerc N., Kothary R.; RT "Dystonin-deficient mice exhibit an intrinsic muscle weakness and an RT instability of skeletal muscle cytoarchitecture."; RL Dev. Biol. 210:367-380(1999). RN [5] RP INTERACTION WITH PKP1. RX PubMed=10852826; DOI=10.1242/jcs.113.13.2471; RA Hofmann I., Mertens C., Brettel M., Nimmrich V., Schnoelzer M., RA Herrmann H.; RT "Interaction of plakophilins with desmoplakin and intermediate filament RT proteins: an in vitro analysis."; RL J. Cell Sci. 113:2471-2483(2000). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=17242355; DOI=10.1073/pnas.0609836104; RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; RT "Large-scale phosphorylation analysis of mouse liver."; RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-17; SER-25; SER-28; SER-31; RP SER-32; SER-68 AND SER-423, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen, RC 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 [8] RP INTERACTION WITH PLEC. RX PubMed=24940650; DOI=10.1038/jid.2014.255; RA Bouameur J.E., Favre B., Fontao L., Lingasamy P., Begre N., Borradori L.; RT "Interaction of plectin with keratins 5 and 14: dependence on several RT plectin domains and keratin quaternary structure."; RL J. Invest. Dermatol. 134:2776-2783(2014). RN [9] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-16; ARG-37 AND ARG-70, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, and Embryo; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [10] RP FUNCTION, MUTAGENESIS OF ARG-349, AND SUBCELLULAR LOCATION. RX PubMed=25394388; DOI=10.1007/s00401-014-1363-2; RA Clemen C.S., Stoeckigt F., Strucksberg K.H., Chevessier F., Winter L., RA Schuetz J., Bauer R., Thorweihe J.M., Wenzel D., Schloetzer-Schrehardt U., RA Rasche V., Krsmanovic P., Katus H.A., Rottbauer W., Just S., Mueller O.J., RA Friedrich O., Meyer R., Herrmann H., Schrickel J.W., Schroeder R.; RT "The toxic effect of R350P mutant desmin in striated muscle of man and RT mouse."; RL Acta Neuropathol. 129:297-315(2015). RN [11] RP INTERACTION WITH ASB2, SUBCELLULAR LOCATION, AND PROTEASOMAL DEGRADATION. RX PubMed=26343497; DOI=10.1016/j.yjmcc.2015.08.020; RA Thottakara T., Friedrich F.W., Reischmann S., Braumann S., Schlossarek S., RA Kraemer E., Juhr D., Schlueter H., van der Velden J., Muench J., Patten M., RA Eschenhagen T., Moog-Lutz C., Carrier L.; RT "The E3 ubiquitin ligase Asb2beta is downregulated in a mouse model of RT hypertrophic cardiomyopathy and targets desmin for proteasomal RT degradation."; RL J. Mol. Cell. Cardiol. 87:214-224(2015). RN [12] RP PHOSPHORYLATION AT SER-7; SER-28; SER-32; SER-60 AND THR-76, AND RP MUTAGENESIS OF SER-7; SER-28; SER-32; SER-60 AND THR-76. RX PubMed=27565725; DOI=10.1016/j.bbrc.2016.08.122; RA Makihara H., Inaba H., Enomoto A., Tanaka H., Tomono Y., Ushida K., RA Goto M., Kurita K., Nishida Y., Kasahara K., Goto H., Inagaki M.; RT "Desmin phosphorylation by Cdk1 is required for efficient separation of RT desmin intermediate filaments in mitosis and detected in murine RT embryonic/newborn muscle and human rhabdomyosarcoma tissues."; RL Biochem. Biophys. Res. Commun. 478:1323-1329(2016). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=26787680; DOI=10.1242/bio.014993; RA Fuchs C., Gawlas S., Heher P., Nikouli S., Paar H., Ivankovic M., RA Schultheis M., Klammer J., Gottschamel T., Capetanaki Y., Weitzer G.; RT "Desmin enters the nucleus of cardiac stem cells and modulates Nkx2.5 RT expression by participating in transcription factor complexes that interact RT with the nkx2.5 gene."; RL Biol. Open 5:140-153(2016). RN [14] RP FUNCTION, AND DISRUPTION PHENOTYPE. RX PubMed=27733623; DOI=10.1091/mbc.e16-04-0237; RA Hernandez D.A., Bennett C.M., Dunina-Barkovskaya L., Wedig T., RA Capetanaki Y., Herrmann H., Conover G.M.; RT "Nebulette is a powerful cytolinker organizing desmin and actin in mouse RT hearts."; RL Mol. Biol. Cell 27:3869-3882(2016). RN [15] RP FUNCTION, AND INTERACTION WITH TUBULIN. RX PubMed=27102488; DOI=10.1126/science.aaf0659; RA Robison P., Caporizzo M.A., Ahmadzadeh H., Bogush A.I., Chen C.Y., RA Margulies K.B., Shenoy V.B., Prosser B.L.; RT "Detyrosinated microtubules buckle and bear load in contracting RT cardiomyocytes."; RL Science 352:417-428(2016). RN [16] RP MUTAGENESIS OF ARG-349, AND SUBCELLULAR LOCATION. RX PubMed=28469177; DOI=10.1038/s41598-017-01485-x; RA Diermeier S., Iberl J., Vetter K., Haug M., Pollmann C., Reischl B., RA Buttgereit A., Schuermann S., Spoerrer M., Goldmann W.H., Fabry B., RA Elhamine F., Stehle R., Pfitzer G., Winter L., Clemen C.S., Herrmann H., RA Schroeder R., Friedrich O.; RT "Early signs of architectural and biomechanical failure in isolated RT myofibers and immortalized myoblasts from desmin-mutant knock-in mice."; RL Sci. Rep. 7:1391-1391(2017). RN [17] RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=35959657; DOI=10.1161/circulationaha.122.060454; RA Perez-Hernandez M., van Opbergen C.J.M., Bagwan N., Vissing C.R., RA Marron-Linares G.M., Zhang M., Torres Vega E., Sorrentino A., Drici L., RA Sulek K., Zhai R., Hansen F.B., Christensen A.H., Boesgaard S., RA Gustafsson F., Rossing K., Small E.M., Davies M.J., Rothenberg E., RA Sato P.Y., Cerrone M., Jensen T.H.L., Qvortrup K., Bundgaard H., Delmar M., RA Lundby A.; RT "Loss of Nuclear Envelope Integrity and Increased Oxidant Production Cause RT DNA Damage in Adult Hearts Deficient in PKP2: A Molecular Substrate of RT ARVC."; RL Circulation 146:851-867(2022). CC -!- FUNCTION: Muscle-specific type III intermediate filament essential for CC proper muscular structure and function. Plays a crucial role in CC maintaining the structure of sarcomeres, inter-connecting the Z-disks CC and forming the myofibrils, linking them not only to the sarcolemmal CC cytoskeleton, but also to the nucleus and mitochondria, thus providing CC strength for the muscle fiber during activity (By similarity). In adult CC striated muscle they form a fibrous network connecting myofibrils to CC each other and to the plasma membrane from the periphery of the Z-line CC structures (PubMed:25394388). May act as a sarcomeric microtubule- CC anchoring protein: specifically associates with detyrosinated tubulin- CC alpha chains, leading to buckled microtubules and mechanical resistance CC to contraction (PubMed:27102488). Required for nuclear membrane CC integrity, via anchoring at the cell tip and nuclear envelope, CC resulting in maintenance of microtubule-derived intracellular CC mechanical forces (PubMed:35959657). Contributes to the transcriptional CC regulation of the NKX2-5 gene in cardiac progenitor cells during a CC short period of cardiomyogenesis and in cardiac side population stem CC cells in the adult. Plays a role in maintaining an optimal conformation CC of nebulette (NEB) on heart muscle sarcomeres to bind and recruit CC cardiac alpha-actin (PubMed:27733623). {ECO:0000250|UniProtKB:P17661, CC ECO:0000269|PubMed:25394388, ECO:0000269|PubMed:27102488, CC ECO:0000269|PubMed:27733623, ECO:0000269|PubMed:35959657}. CC -!- SUBUNIT: Homomer (By similarity). Interacts with MTM1 (By similarity). CC Interacts with DST (PubMed:10357897). Interacts with tubulin-alpha; CC specifically associates with detyrosinated tubulin-alpha CC (PubMed:27102488). Interacts with EPPK1; interaction is dependent of CC higher-order structure of intermediate filament. Interacts with CRYAB CC (By similarity). Interacts with NEB (via nebulin repeats 160-164) (By CC similarity). Interacts (via rod region) with NEBL (via nebulin repeats CC 1-5) (By similarity). Interacts with ASB2 isoform 1; the interaction CC targets DES for proteasomal degradation (PubMed:26343497). Interacts CC with PLEC isoform 1C (PubMed:24940650). Interacts with PKP1 CC (PubMed:10852826). {ECO:0000250|UniProtKB:P17661, CC ECO:0000269|PubMed:10357897, ECO:0000269|PubMed:10852826, CC ECO:0000269|PubMed:24940650, ECO:0000269|PubMed:26343497, CC ECO:0000269|PubMed:27102488}. CC -!- INTERACTION: CC P31001; Q9Z2C5: Mtm1; NbExp=4; IntAct=EBI-298565, EBI-6861578; CC P31001; Q9UBX2: DUX4; Xeno; NbExp=2; IntAct=EBI-298565, EBI-11600078; CC P31001; Q13496: MTM1; Xeno; NbExp=4; IntAct=EBI-298565, EBI-2864109; CC -!- SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line CC {ECO:0000269|PubMed:26343497, ECO:0000269|PubMed:26787680, CC ECO:0000269|PubMed:28469177}. Cytoplasm {ECO:0000269|PubMed:25394388, CC ECO:0000269|PubMed:26787680}. Cell membrane, sarcolemma CC {ECO:0000269|PubMed:25394388}. Nucleus {ECO:0000269|PubMed:26787680}. CC Cell tip {ECO:0000269|PubMed:35959657}. Nucleus envelope CC {ECO:0000269|PubMed:35959657}. Note=Localizes in the intercalated disks CC which occur at the Z line of cardiomyocytes (By similarity). Localizes CC in the nucleus exclusively in differentiating cardiac progenitor cells CC and premature cardiomyocytes (PubMed:26787680). PKP2 is required for CC correct anchoring of DES at the cell tip and nuclear envelope CC (PubMed:35959657). {ECO:0000250|UniProtKB:P17661, CC ECO:0000269|PubMed:26787680, ECO:0000269|PubMed:35959657}. CC -!- TISSUE SPECIFICITY: Expressed in mature cardiomyocytes, immature CC cardiomyocytes and cardiac progenitor cells (at protein level). CC {ECO:0000269|PubMed:26787680, ECO:0000269|PubMed:35959657}. CC -!- PTM: ADP-ribosylation prevents ability to form intermediate filaments. CC {ECO:0000250|UniProtKB:P48675}. CC -!- PTM: Phosphorylation at Ser-7, Ser-28 and Ser-32 by CDK1, CC phosphorylation at Ser-60 by AURKB and phosphorylation at Thr-76 by CC ROCK1 contribute to efficient separation of desmin intermediate CC filaments during mitosis. {ECO:0000269|PubMed:27565725}. CC -!- PTM: Ubiquitination by a SCF-like complex containing ASB2 isoform 1 CC leads to proteasomal degradation. {ECO:0000269|PubMed:26343497}. CC -!- DISRUPTION PHENOTYPE: Mice hearts have reduced nebulette (NEB) and CC elevated actin levels, with intact myofibers showing disordered NEB CC organization. {ECO:0000269|PubMed:27733623}. CC -!- SIMILARITY: Belongs to the intermediate filament family. CC {ECO:0000255|PROSITE-ProRule:PRU01188}. 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; L22550; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC031760; AAH31760.1; -; mRNA. DR EMBL; Z18892; CAA79330.1; -; Genomic_DNA. DR CCDS; CCDS15071.1; -. DR PIR; A54104; A54104. DR RefSeq; NP_034173.1; NM_010043.2. DR AlphaFoldDB; P31001; -. DR SMR; P31001; -. DR BioGRID; 199210; 11. DR DIP; DIP-256N; -. DR IntAct; P31001; 15. DR MINT; P31001; -. DR STRING; 10090.ENSMUSP00000027409; -. DR GlyGen; P31001; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P31001; -. DR PhosphoSitePlus; P31001; -. DR EPD; P31001; -. DR jPOST; P31001; -. DR PaxDb; 10090-ENSMUSP00000027409; -. DR PeptideAtlas; P31001; -. DR ProteomicsDB; 277981; -. DR Pumba; P31001; -. DR Antibodypedia; 3503; 1795 antibodies from 53 providers. DR DNASU; 13346; -. DR Ensembl; ENSMUST00000027409.10; ENSMUSP00000027409.10; ENSMUSG00000026208.10. DR GeneID; 13346; -. DR KEGG; mmu:13346; -. DR UCSC; uc007box.2; mouse. DR AGR; MGI:94885; -. DR CTD; 1674; -. DR MGI; MGI:94885; Des. DR VEuPathDB; HostDB:ENSMUSG00000026208; -. DR eggNOG; KOG0977; Eukaryota. DR GeneTree; ENSGT00940000155522; -. DR HOGENOM; CLU_012560_7_4_1; -. DR InParanoid; P31001; -. DR OMA; AWMCCLW; -. DR OrthoDB; 4640531at2759; -. DR PhylomeDB; P31001; -. DR TreeFam; TF330122; -. DR Reactome; R-MMU-390522; Striated Muscle Contraction. DR BioGRID-ORCS; 13346; 5 hits in 78 CRISPR screens. DR PRO; PR:P31001; -. DR Proteomes; UP000000589; Chromosome 1. DR RNAct; P31001; Protein. DR Bgee; ENSMUSG00000026208; Expressed in hindlimb stylopod muscle and 162 other cell types or tissues. DR ExpressionAtlas; P31001; baseline and differential. DR GO; GO:0097512; C:cardiac myofibril; ISO:MGI. DR GO; GO:0005911; C:cell-cell junction; IDA:MGI. DR GO; GO:0043292; C:contractile fiber; IDA:MGI. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IDA:MGI. DR GO; GO:0005916; C:fascia adherens; IDA:MGI. DR GO; GO:0005921; C:gap junction; ISO:MGI. DR GO; GO:0014704; C:intercalated disc; ISO:MGI. DR GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI. DR GO; GO:0031594; C:neuromuscular junction; IDA:MGI. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0042383; C:sarcolemma; IDA:UniProtKB. DR GO; GO:0045098; C:type III intermediate filament; ISO:MGI. DR GO; GO:0030018; C:Z disc; IDA:UniProtKB. DR GO; GO:0008092; F:cytoskeletal protein binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:MGI. DR GO; GO:0045109; P:intermediate filament organization; ISS:UniProtKB. DR GO; GO:0007517; P:muscle organ development; TAS:MGI. DR GO; GO:0060538; P:skeletal muscle organ development; IBA:GO_Central. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 1.20.5.500; Single helix bin; 1. DR Gene3D; 1.20.5.1160; Vasodilator-stimulated phosphoprotein; 1. DR InterPro; IPR018039; IF_conserved. DR InterPro; IPR039008; IF_rod_dom. DR InterPro; IPR006821; Intermed_filament_DNA-bd. DR PANTHER; PTHR45652:SF2; DESMIN; 1. DR PANTHER; PTHR45652; GLIAL FIBRILLARY ACIDIC PROTEIN; 1. DR Pfam; PF00038; Filament; 1. DR Pfam; PF04732; Filament_head; 1. DR SMART; SM01391; Filament; 1. DR SUPFAM; SSF64593; Intermediate filament protein, coiled coil region; 2. DR PROSITE; PS00226; IF_ROD_1; 1. DR PROSITE; PS51842; IF_ROD_2; 1. DR SWISS-2DPAGE; P31001; -. DR Genevisible; P31001; MM. PE 1: Evidence at protein level; KW ADP-ribosylation; Cell membrane; Coiled coil; Cytoplasm; KW Intermediate filament; Membrane; Methylation; Muscle protein; Nucleus; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:P02542" FT CHAIN 2..469 FT /note="Desmin" FT /id="PRO_0000063773" FT DOMAIN 107..415 FT /note="IF rod" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01188" FT REGION 2..108 FT /note="Head" FT REGION 109..140 FT /note="Coil 1A" FT REGION 141..150 FT /note="Linker 1" FT REGION 151..251 FT /note="Coil 1B" FT REGION 252..267 FT /note="Linker 12" FT REGION 267..414 FT /note="Interaction with NEB" FT /evidence="ECO:0000250|UniProtKB:P17661" FT REGION 268..286 FT /note="Coil 2A" FT REGION 287..294 FT /note="Linker 2" FT REGION 295..411 FT /note="Coil 2B" FT REGION 412..469 FT /note="Tail" FT REGION 437..452 FT /note="Interaction with CRYAB" FT /evidence="ECO:0000250|UniProtKB:P17661" FT SITE 353 FT /note="Stutter" FT MOD_RES 7 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:27565725" FT MOD_RES 12 FT /note="Phosphoserine; by AURKB" FT /evidence="ECO:0000250|UniProtKB:P17661" FT MOD_RES 16 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 17 FT /note="Phosphothreonine; by AURKB and ROCK1" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 25 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 28 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:27565725, FT ECO:0007744|PubMed:21183079" FT MOD_RES 31 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 32 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000269|PubMed:27565725, FT ECO:0007744|PubMed:21183079" FT MOD_RES 37 FT /note="Asymmetric dimethylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 37 FT /note="Omega-N-methylarginine; alternate" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 45 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48675" FT MOD_RES 58 FT /note="ADP-ribosylarginine" FT /evidence="ECO:0000250|UniProtKB:P48675" FT MOD_RES 60 FT /note="Phosphoserine; by AURKB" FT /evidence="ECO:0000269|PubMed:27565725" FT MOD_RES 68 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17242355, FT ECO:0007744|PubMed:21183079" FT MOD_RES 70 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 76 FT /note="Phosphothreonine; by ROCK1" FT /evidence="ECO:0000269|PubMed:27565725" FT MOD_RES 77 FT /note="Phosphothreonine; by ROCK1" FT /evidence="ECO:0000250|UniProtKB:P17661" FT MOD_RES 81 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48675" FT MOD_RES 289 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48675" FT MOD_RES 357 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P48675" FT MOD_RES 423 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MUTAGEN 7 FT /note="S->A: Reduced phosphorylation. Almost complete loss FT of phosphorylation; when associated with A-28 and A-32." FT /evidence="ECO:0000269|PubMed:27565725" FT MUTAGEN 28 FT /note="S->A: Reduced phosphorylation. Almost complete loss FT of phosphorylation; when associated with A-7 and A-32." FT /evidence="ECO:0000269|PubMed:27565725" FT MUTAGEN 32 FT /note="S->A: Reduced phosphorylation and formation of FT unusual long bridge-like intermediate filament structures FT between two daughter cells during cytokinesis. Almost FT complete loss of phosphorylation; when associated with A-7 FT and A-28. Increased formation of unusual long bridge-like FT intermediate filament structures between two daughter cells FT during cytokinesis; when associated with A-60 and A-76." FT /evidence="ECO:0000269|PubMed:27565725" FT MUTAGEN 60 FT /note="S->A: Formation of unusual long bridge-like FT intermediate filament structures between two daughter cells FT during cytokinesis; when associated with A-76. Increased FT formation of unusual long bridge-like intermediate filament FT structures between two daughter cells during cytokinesis; FT when associated with A-32 and A-76." FT /evidence="ECO:0000269|PubMed:27565725" FT MUTAGEN 76 FT /note="T->A: Formation of unusual long bridge-like FT intermediate filament structures between two daughter cells FT during cytokinesis; when associated with A-60. Increased FT formation of unusual long bridge-like intermediate filament FT structures between two daughter cells during cytokinesis; FT when associated with A-32 and A-60." FT /evidence="ECO:0000269|PubMed:27565725" FT MUTAGEN 349 FT /note="R->P: Increases protein decay. forms subsarcolemmal FT aggregates. Changes the subcellular localization and FT turnover of its direct, extrasarcomeric binding partners. FT Knockin mice develop age-dependent desmin-positive protein FT aggregation pathology, skeletal muscle weakness, dilated FT cardiomyopathy, as well as cardiac arrhythmias and FT conduction defects. Knockin mice exhibit altered axial FT myofibrillar lattice arrangement in fast- and slow-twitch FT muscle fibers, increased axial stiffness and FT stretch-induced vulnerability in soleus muscle fiber FT bundles, reduced Ca(2+)-sensitivity in heterozygous fiber FT bundles and increased Ca(2+)-sensitivity in homozygous FT fiber bundles." FT /evidence="ECO:0000269|PubMed:25394388" SQ SEQUENCE 469 AA; 53498 MW; 58A8A13C7CC11EEF CRC64; MSQAYSSSQR VSSYRRTFGG APGFSLGSPL SSPVFPRAGF GTKGSSSSMT SRVYQVSRTS GGAGGLGSLR SSRLGTTRAP SYGAGELLDF SLADAVNQEF LATRTNEKVE LQELNDRFAN YIEKVRFLEQ QNAALAAEVN RLKGREPTRV AELYEEEMRE LRRQVEVLTN QRARVDVERD NLIDDLQRLK AKLQEEIQLR EEAENNLAAF RADVDAATLA RIDLERRIES LNEEIAFLKK VHEEEIRELQ AQLQEQQVQV EMDMSKPDLT AALRDIRAQY ETIAAKNISE AEEWYKSKVS DLTQAANKNN DALRQAKQEM MEYRHQIQSY TCEIDALKGT NDSLMRQMRE LEDRFASEAN GYQDNIARLE EEIRHLKDEM ARHLREYQDL LNVKMALDVE IATYRKLLEG EESRINLPIQ TFSALNFRET SPEQRGSEVH TKKTVMIKTI ETRDGEVVSE ATQQQHEVL //