MYPN_HUMAN
ID MYPN_HUMAN Reviewed; 1320 AA.
AC Q86TC9; Q5VV35; Q5VV36; Q86T37; Q8N3L4; Q96K90; Q96KF5;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Myopalladin;
DE AltName: Full=145 kDa sarcomeric protein;
GN Name=MYPN; Synonyms=MYOP;
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 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH NEB; NEBL; ACTN2 AND CARP, AND
RP VARIANTS ASN-691; ASN-707 AND ARG-803.
RC TISSUE=Skeletal muscle;
RX PubMed=11309420; DOI=10.1083/jcb.153.2.413;
RA Bang M.-L., Mudry R.E., McElhinny A.S., Trombitas K., Geach A.J.,
RA Yamasaki R., Sorimachi H., Granzier H., Gregorio C.C., Labeit S.;
RT "Myopalladin, a novel 145-kilodalton sarcomeric protein with multiple roles
RT in Z-disc and I-band protein assemblies.";
RL J. Cell Biol. 153:413-427(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-494 (ISOFORM 1).
RC TISSUE=Embryo;
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 INTERACTION WITH TTN.
RX PubMed=12482578; DOI=10.1016/s0014-5793(02)03655-4;
RA Ma K., Wang K.;
RT "Interaction of nebulin SH3 domain with titin PEVK and myopalladin:
RT implications for the signaling and assembly role of titin and nebulin.";
RL FEBS Lett. 532:273-278(2002).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-928, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-251; SER-759; SER-813;
RP SER-818 AND SER-928, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-101; SER-813 AND SER-928, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [9]
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 [10]
RP INVOLVEMENT IN RCM4, VARIANTS CMH22 CYS-20; ARG-153; GLU-217; ALA-410;
RP THR-841; LEU-1112 AND PRO-1265, VARIANTS CMD1KK CYS-20; VAL-213; PHE-339;
RP THR-611; THR-882 AND LEU-954, VARIANTS ALA-393; LYS-467; LYS-614; LEU-628;
RP ASN-691; ASN-707; ARG-803; ARG-804; GLN-955; THR-1135; ILE-1161 AND
RP GLY-1306, AND CHARACTERIZATION OF VARIANT CMH22 CYS-20.
RX PubMed=22286171; DOI=10.1093/hmg/dds022;
RA Purevjav E., Arimura T., Augustin S., Huby A.C., Takagi K., Nunoda S.,
RA Kearney D.L., Taylor M.D., Terasaki F., Bos J.M., Ommen S.R., Shibata H.,
RA Takahashi M., Itoh-Satoh M., McKenna W.J., Murphy R.T., Labeit S.,
RA Yamanaka Y., Machida N., Park J.E., Alexander P.M., Weintraub R.G.,
RA Kitaura Y., Ackerman M.J., Kimura A., Towbin J.A.;
RT "Molecular basis for clinical heterogeneity in inherited cardiomyopathies
RT due to myopalladin mutations.";
RL Hum. Mol. Genet. 21:2039-2053(2012).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-644; SER-813; SER-867;
RP SER-907 AND SER-928, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [12]
RP INVOLVEMENT IN NEM11, AND SUBCELLULAR LOCATION.
RX PubMed=28017374; DOI=10.1016/j.ajhg.2016.11.017;
RA Miyatake S., Mitsuhashi S., Hayashi Y.K., Purevjav E., Nishikawa A.,
RA Koshimizu E., Suzuki M., Yatabe K., Tanaka Y., Ogata K., Kuru S.,
RA Shiina M., Tsurusaki Y., Nakashima M., Mizuguchi T., Miyake N., Saitsu H.,
RA Ogata K., Kawai M., Towbin J., Nonaka I., Nishino I., Matsumoto N.;
RT "Biallelic Mutations in MYPN, Encoding Myopalladin, Are Associated with
RT Childhood-Onset, Slowly Progressive Nemaline Myopathy.";
RL Am. J. Hum. Genet. 100:169-178(2017).
RN [13]
RP VARIANTS CMD1KK HIS-1088; LEU-1112 AND MET-1195, AND CHARACTERIZATION OF
RP VARIANTS CMD1KK LEU-1112 AND MET-1195.
RX PubMed=18006477; DOI=10.1093/cvr/cvm015;
RA Duboscq-Bidot L., Xu P., Charron P., Neyroud N., Dilanian G., Millaire A.,
RA Bors V., Komajda M., Villard E.;
RT "Mutations in the Z-band protein myopalladin gene and idiopathic dilated
RT cardiomyopathy.";
RL Cardiovasc. Res. 77:118-125(2008).
RN [14]
RP VARIANTS CMD1KK TRP-955 AND LEU-961, AND VARIANTS ALA-393; LEU-628;
RP ASN-691; ASN-707; ARG-803 AND THR-1135.
RX PubMed=22892539; DOI=10.1038/ejhg.2012.173;
RG German Competence Network Heart Failure;
RA Meyer T., Ruppert V., Ackermann S., Richter A., Perrot A., Sperling S.R.,
RA Posch M.G., Maisch B., Pankuweit S.;
RT "Novel mutations in the sarcomeric protein myopalladin in patients with
RT dilated cardiomyopathy.";
RL Eur. J. Hum. Genet. 21:294-300(2013).
RN [15]
RP VARIANT SER-698.
RX PubMed=25787250; DOI=10.1073/pnas.1503696112;
RA Cromer M.K., Choi M., Nelson-Williams C., Fonseca A.L., Kunstman J.W.,
RA Korah R.M., Overton J.D., Mane S., Kenney B., Malchoff C.D., Stalberg P.,
RA Akerstroem G., Westin G., Hellman P., Carling T., Bjoerklund P.,
RA Lifton R.P.;
RT "Neomorphic effects of recurrent somatic mutations in Yin Yang 1 in
RT insulin-producing adenomas.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:4062-4067(2015).
RN [16]
RP VARIANT ILE-1161.
RX PubMed=27535533; DOI=10.1038/nature19057;
RG Exome Aggregation Consortium;
RA Lek M., Karczewski K.J., Minikel E.V., Samocha K.E., Banks E., Fennell T.,
RA O'Donnell-Luria A.H., Ware J.S., Hill A.J., Cummings B.B., Tukiainen T.,
RA Birnbaum D.P., Kosmicki J.A., Duncan L.E., Estrada K., Zhao F., Zou J.,
RA Pierce-Hoffman E., Berghout J., Cooper D.N., Deflaux N., DePristo M.,
RA Do R., Flannick J., Fromer M., Gauthier L., Goldstein J., Gupta N.,
RA Howrigan D., Kiezun A., Kurki M.I., Moonshine A.L., Natarajan P.,
RA Orozco L., Peloso G.M., Poplin R., Rivas M.A., Ruano-Rubio V., Rose S.A.,
RA Ruderfer D.M., Shakir K., Stenson P.D., Stevens C., Thomas B.P., Tiao G.,
RA Tusie-Luna M.T., Weisburd B., Won H.H., Yu D., Altshuler D.M.,
RA Ardissino D., Boehnke M., Danesh J., Donnelly S., Elosua R., Florez J.C.,
RA Gabriel S.B., Getz G., Glatt S.J., Hultman C.M., Kathiresan S., Laakso M.,
RA McCarroll S., McCarthy M.I., McGovern D., McPherson R., Neale B.M.,
RA Palotie A., Purcell S.M., Saleheen D., Scharf J.M., Sklar P.,
RA Sullivan P.F., Tuomilehto J., Tsuang M.T., Watkins H.C., Wilson J.G.,
RA Daly M.J., MacArthur D.G.;
RT "Analysis of protein-coding genetic variation in 60,706 humans.";
RL Nature 536:285-291(2016).
CC -!- FUNCTION: Component of the sarcomere that tethers together nebulin
CC (skeletal muscle) and nebulette (cardiac muscle) to alpha-actinin, at
CC the Z lines. {ECO:0000269|PubMed:11309420}.
CC -!- SUBUNIT: Interacts with TTN/titin, NEB, NEBL, ACTN2 and CARP.
CC {ECO:0000269|PubMed:11309420, ECO:0000269|PubMed:12482578}.
CC -!- INTERACTION:
CC Q86TC9; P20929: NEB; NbExp=2; IntAct=EBI-2562606, EBI-1049657;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11309420}. Nucleus
CC {ECO:0000269|PubMed:11309420}. Cytoplasm, myofibril, sarcomere
CC {ECO:0000269|PubMed:11309420}. Cytoplasm, myofibril, sarcomere, Z line
CC {ECO:0000269|PubMed:11309420, ECO:0000269|PubMed:28017374}. Note=Bound
CC to sarcomere both at the Z-line periphery and in the central I-band
CC region. {ECO:0000269|PubMed:11309420}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q86TC9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q86TC9-2; Sequence=VSP_019384, VSP_019385;
CC -!- TISSUE SPECIFICITY: Expressed in adult skeletal muscle and fetal heart.
CC {ECO:0000269|PubMed:11309420}.
CC -!- DISEASE: Nemaline myopathy 11 (NEM11) [MIM:617336]: An autosomal
CC recessive form of nemaline myopathy. Nemaline myopathies are muscular
CC disorders characterized by muscle weakness of varying severity and
CC onset, and abnormal thread-like or rod-shaped structures in muscle
CC fibers on histologic examination. NEM11 is characterized by slowly
CC progressive muscle weakness and atrophy, mainly affecting the lower
CC limbs and neck. Some patients may have mild cardiac or respiratory
CC involvement, but they do not have respiratory failure.
CC {ECO:0000269|PubMed:28017374}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, dilated 1KK (CMD1KK) [MIM:615248]: A disorder
CC characterized by ventricular dilation and impaired systolic function,
CC resulting in congestive heart failure and arrhythmia. Patients are at
CC risk of premature death. {ECO:0000269|PubMed:18006477,
CC ECO:0000269|PubMed:22286171, ECO:0000269|PubMed:22892539}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Cardiomyopathy, familial hypertrophic 22 (CMH22) [MIM:615248]:
CC A hereditary heart disorder characterized by ventricular hypertrophy,
CC which is usually asymmetric and often involves the interventricular
CC septum. The symptoms include dyspnea, syncope, collapse, palpitations,
CC and chest pain. They can be readily provoked by exercise. The disorder
CC has inter- and intrafamilial variability ranging from benign to
CC malignant forms with high risk of cardiac failure and sudden cardiac
CC death. {ECO:0000269|PubMed:22286171}. Note=The disease is caused by
CC variants affecting the gene represented in this entry.
CC -!- DISEASE: Cardiomyopathy, familial restrictive 4 (RCM4) [MIM:615248]: A
CC heart disorder characterized by impaired filling of the ventricles with
CC reduced diastolic volume, in the presence of normal or near normal wall
CC thickness and systolic function. {ECO:0000269|PubMed:22286171}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the myotilin/palladin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55048.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
CC Sequence=CAD38923.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF328296; AAK50625.1; -; mRNA.
DR EMBL; AL832002; CAD89906.1; -; mRNA.
DR EMBL; AL832379; CAD91155.1; -; mRNA.
DR EMBL; AL834247; CAD38923.2; ALT_INIT; mRNA.
DR EMBL; AC016395; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC024258; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL512429; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK027343; BAB55048.1; ALT_SEQ; mRNA.
DR CCDS; CCDS7275.1; -. [Q86TC9-1]
DR RefSeq; NP_001243196.1; NM_001256267.1. [Q86TC9-1]
DR RefSeq; NP_115967.2; NM_032578.3. [Q86TC9-1]
DR RefSeq; XP_016872323.1; XM_017016834.1. [Q86TC9-1]
DR AlphaFoldDB; Q86TC9; -.
DR BioGRID; 124185; 30.
DR IntAct; Q86TC9; 11.
DR MINT; Q86TC9; -.
DR STRING; 9606.ENSP00000351790; -.
DR iPTMnet; Q86TC9; -.
DR PhosphoSitePlus; Q86TC9; -.
DR BioMuta; MYPN; -.
DR DMDM; 109892761; -.
DR EPD; Q86TC9; -.
DR jPOST; Q86TC9; -.
DR MassIVE; Q86TC9; -.
DR MaxQB; Q86TC9; -.
DR PaxDb; Q86TC9; -.
DR PeptideAtlas; Q86TC9; -.
DR PRIDE; Q86TC9; -.
DR ProteomicsDB; 69683; -. [Q86TC9-1]
DR ProteomicsDB; 69684; -. [Q86TC9-2]
DR Antibodypedia; 28426; 116 antibodies from 21 providers.
DR DNASU; 84665; -.
DR Ensembl; ENST00000354393.7; ENSP00000346369.2; ENSG00000138347.17. [Q86TC9-2]
DR Ensembl; ENST00000358913.10; ENSP00000351790.5; ENSG00000138347.17. [Q86TC9-1]
DR Ensembl; ENST00000613327.5; ENSP00000480757.2; ENSG00000138347.17. [Q86TC9-1]
DR GeneID; 84665; -.
DR KEGG; hsa:84665; -.
DR MANE-Select; ENST00000358913.10; ENSP00000351790.5; NM_032578.4; NP_115967.2.
DR UCSC; uc001jnm.6; human. [Q86TC9-1]
DR CTD; 84665; -.
DR DisGeNET; 84665; -.
DR GeneCards; MYPN; -.
DR HGNC; HGNC:23246; MYPN.
DR HPA; ENSG00000138347; Tissue enhanced (heart muscle, skeletal muscle, tongue).
DR MalaCards; MYPN; -.
DR MIM; 608517; gene.
DR MIM; 615248; phenotype.
DR MIM; 617336; phenotype.
DR neXtProt; NX_Q86TC9; -.
DR OpenTargets; ENSG00000138347; -.
DR Orphanet; 171881; Cap myopathy.
DR Orphanet; 171439; Childhood-onset nemaline myopathy.
DR Orphanet; 154; Familial isolated dilated cardiomyopathy.
DR Orphanet; 75249; Familial isolated restrictive cardiomyopathy.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR PharmGKB; PA134944534; -.
DR VEuPathDB; HostDB:ENSG00000138347; -.
DR eggNOG; ENOG502QSRV; Eukaryota.
DR GeneTree; ENSGT00940000153441; -.
DR HOGENOM; CLU_024873_0_0_1; -.
DR InParanoid; Q86TC9; -.
DR OMA; RSHQQEY; -.
DR OrthoDB; 100208at2759; -.
DR PhylomeDB; Q86TC9; -.
DR TreeFam; TF343193; -.
DR PathwayCommons; Q86TC9; -.
DR SignaLink; Q86TC9; -.
DR BioGRID-ORCS; 84665; 18 hits in 1080 CRISPR screens.
DR ChiTaRS; MYPN; human.
DR GeneWiki; MYPN; -.
DR GenomeRNAi; 84665; -.
DR Pharos; Q86TC9; Tbio.
DR PRO; PR:Q86TC9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86TC9; protein.
DR Bgee; ENSG00000138347; Expressed in hindlimb stylopod muscle and 86 other tissues.
DR ExpressionAtlas; Q86TC9; baseline and differential.
DR Genevisible; Q86TC9; HS.
DR GO; GO:0030424; C:axon; IBA:GO_Central.
DR GO; GO:0031674; C:I band; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030018; C:Z disc; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0098632; F:cell-cell adhesion mediator activity; IBA:GO_Central.
DR GO; GO:0008092; F:cytoskeletal protein binding; IPI:BHF-UCL.
DR GO; GO:0051371; F:muscle alpha-actinin binding; IPI:BHF-UCL.
DR GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
DR GO; GO:0007411; P:axon guidance; IBA:GO_Central.
DR GO; GO:0070593; P:dendrite self-avoidance; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IBA:GO_Central.
DR GO; GO:0045214; P:sarcomere organization; IMP:BHF-UCL.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF07679; I-set; 5.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 5.
DR PROSITE; PS50835; IG_LIKE; 5.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Cardiomyopathy; Coiled coil;
KW Cytoplasm; Disease variant; Disulfide bond; Immunoglobulin domain;
KW Nemaline myopathy; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1320
FT /note="Myopalladin"
FT /id="PRO_0000240489"
FT DOMAIN 269..359
FT /note="Ig-like 1"
FT DOMAIN 435..531
FT /note="Ig-like 2"
FT DOMAIN 945..1029
FT /note="Ig-like 3"
FT DOMAIN 1073..1162
FT /note="Ig-like 4"
FT DOMAIN 1172..1262
FT /note="Ig-like 5"
FT REGION 1..522
FT /note="Interaction with CARP"
FT /evidence="ECO:0000269|PubMed:11309420"
FT REGION 19..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 165..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 554..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..677
FT /note="Interaction with NEB"
FT /evidence="ECO:0000269|PubMed:11309420"
FT REGION 763..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 844..876
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 945..1320
FT /note="Interaction with ACTN"
FT COILED 219..248
FT /evidence="ECO:0000255"
FT COMPBIAS 86..104
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..261
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..574
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 763..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 785..799
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 857..876
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 101
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5DTJ9"
FT MOD_RES 251
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 644
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 813
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 818
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 867
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 928
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT DISULFID 290..341
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 456..515
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 1094..1146
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 1..275
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019384"
FT VAR_SEQ 276..301
FT /note="RSREVPEGTRVQLDCIVVGIPPPQVR -> MLTVQVKTSSAIELPDSLAFLW
FT IIPM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019385"
FT VARIANT 20
FT /note="Y -> C (in CMH22 and CMD1KK; perturbs MYPN nuclear
FT shuttling and leads to disruption of intercalated disks;
FT dbSNP:rs140148105)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069642"
FT VARIANT 153
FT /note="K -> R (in CMH22; dbSNP:rs199476401)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069643"
FT VARIANT 213
FT /note="I -> V (in CMD1KK; dbSNP:rs199476402)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069644"
FT VARIANT 217
FT /note="A -> E (in CMH22; dbSNP:rs199476403)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069645"
FT VARIANT 339
FT /note="Y -> F (in CMD1KK; dbSNP:rs199476404)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069646"
FT VARIANT 393
FT /note="V -> A (in dbSNP:rs11596653)"
FT /evidence="ECO:0000269|PubMed:22286171,
FT ECO:0000269|PubMed:22892539"
FT /id="VAR_049911"
FT VARIANT 410
FT /note="V -> A (in CMH22; dbSNP:rs199476406)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069647"
FT VARIANT 467
FT /note="E -> K (in dbSNP:rs74143030)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069648"
FT VARIANT 611
FT /note="A -> T (in CMD1KK; dbSNP:rs199476409)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069649"
FT VARIANT 614
FT /note="E -> K (in dbSNP:rs143338091)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069650"
FT VARIANT 628
FT /note="F -> L (in dbSNP:rs10823148)"
FT /evidence="ECO:0000269|PubMed:22286171,
FT ECO:0000269|PubMed:22892539"
FT /id="VAR_049912"
FT VARIANT 691
FT /note="S -> N (in dbSNP:rs10997975)"
FT /evidence="ECO:0000269|PubMed:11309420,
FT ECO:0000269|PubMed:22286171, ECO:0000269|PubMed:22892539"
FT /id="VAR_026727"
FT VARIANT 698
FT /note="N -> S (in dbSNP:rs181355189)"
FT /evidence="ECO:0000269|PubMed:25787250"
FT /id="VAR_074186"
FT VARIANT 707
FT /note="S -> N (in dbSNP:rs7916821)"
FT /evidence="ECO:0000269|PubMed:11309420,
FT ECO:0000269|PubMed:22286171, ECO:0000269|PubMed:22892539"
FT /id="VAR_026728"
FT VARIANT 803
FT /note="S -> R (in dbSNP:rs3814182)"
FT /evidence="ECO:0000269|PubMed:11309420,
FT ECO:0000269|PubMed:22286171, ECO:0000269|PubMed:22892539"
FT /id="VAR_026729"
FT VARIANT 804
FT /note="G -> R (in dbSNP:rs62620248)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069651"
FT VARIANT 841
FT /note="P -> T (in CMH22; dbSNP:rs199476410)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069652"
FT VARIANT 882
FT /note="A -> T (in CMD1KK; dbSNP:rs199476411)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069653"
FT VARIANT 954
FT /note="F -> L (in CMD1KK; dbSNP:rs199476413)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069654"
FT VARIANT 955
FT /note="R -> Q (in dbSNP:rs199476414)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069655"
FT VARIANT 955
FT /note="R -> W (in CMD1KK; unknown pathological
FT significance; dbSNP:rs149887823)"
FT /evidence="ECO:0000269|PubMed:22892539"
FT /id="VAR_069656"
FT VARIANT 961
FT /note="P -> L (in CMD1KK; dbSNP:rs864621995)"
FT /evidence="ECO:0000269|PubMed:22892539"
FT /id="VAR_069657"
FT VARIANT 1088
FT /note="R -> H (in CMD1KK; dbSNP:rs71584501)"
FT /evidence="ECO:0000269|PubMed:18006477"
FT /id="VAR_069658"
FT VARIANT 1112
FT /note="P -> L (in CMD1KK and CMH22; results in sarcomere
FT disorganization and premature cell death;
FT dbSNP:rs71534278)"
FT /evidence="ECO:0000269|PubMed:18006477,
FT ECO:0000269|PubMed:22286171"
FT /id="VAR_069659"
FT VARIANT 1135
FT /note="P -> T (in dbSNP:rs7079481)"
FT /evidence="ECO:0000269|PubMed:22286171,
FT ECO:0000269|PubMed:22892539"
FT /id="VAR_049913"
FT VARIANT 1161
FT /note="L -> I (in dbSNP:rs138313730)"
FT /evidence="ECO:0000269|PubMed:22286171,
FT ECO:0000269|PubMed:27535533"
FT /id="VAR_069660"
FT VARIANT 1195
FT /note="V -> M (in CMD1KK; results in sarcomere
FT disorganization and premature cell death;
FT dbSNP:rs71534280)"
FT /evidence="ECO:0000269|PubMed:18006477"
FT /id="VAR_069661"
FT VARIANT 1265
FT /note="A -> P (in CMH22; dbSNP:rs199476416)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069662"
FT VARIANT 1306
FT /note="V -> G (in dbSNP:rs199476417)"
FT /evidence="ECO:0000269|PubMed:22286171"
FT /id="VAR_069663"
FT CONFLICT 139
FT /note="Q -> R (in Ref. 2; CAD89906)"
FT /evidence="ECO:0000305"
FT CONFLICT 484
FT /note="L -> S (in Ref. 2; CAD89906)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="D -> G (in Ref. 2; CAD89906)"
FT /evidence="ECO:0000305"
FT CONFLICT 601
FT /note="N -> D (in Ref. 2; CAD89906)"
FT /evidence="ECO:0000305"
FT CONFLICT 677
FT /note="L -> S (in Ref. 2; CAD89906)"
FT /evidence="ECO:0000305"
FT CONFLICT 908
FT /note="F -> L (in Ref. 2; CAD89906)"
FT /evidence="ECO:0000305"
FT CONFLICT 991
FT /note="H -> R (in Ref. 2; CAD38923)"
FT /evidence="ECO:0000305"
FT CONFLICT 1078
FT /note="A -> T (in Ref. 2; CAD91155)"
FT /evidence="ECO:0000305"
FT CONFLICT 1118
FT /note="S -> P (in Ref. 2; CAD38923)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1320 AA; 145257 MW; FD59508CB611A9A9 CRC64;
MQDDSIEAST SISQLLRESY LAETRHRGNN ERSRAEPSSN PCHFGSPSGA AEGGGGQDDL
PDLSAFLSQE ELDESVNLAR LAINYDPLEK ADETQARKRL SPDQMKHSPN LSFEPNFCQD
NPRSPTSSKE SPQEAKRPQY CSETQSKKVF LNKAADFIEE LSSLFKSHSS KRIRPRACKN
HKSKLESQNK VMQENSSSFS DLSERRERSS VPIPIPADTR DNEVNHALEQ QEAKRREAEQ
AASEAAGGDT TPGSSPSSLY YEEPLGQPPR FTQKLRSREV PEGTRVQLDC IVVGIPPPQV
RWYCEGKELE NSPDIHIVQA GNLHSLTIAE AFEEDTGRYS CFASNIYGTD STSAEIYIEG
VSSSDSEGDP NKEEMNRIQK PNEVSSPPTT SAVIPPAVPQ AQHLVAQPRV ATIQQCQSPT
NYLQGLDGKP IIAAPVFTKM LQNLSASEGQ LVVFECRVKG APSPKVEWYR EGTLIEDSPD
FRILQKKPRS MAEPEEICTL VIAEVFAEDS GCFTCTASNK YGTVSSIAQL HVRGNEDLSN
NGSLHSANST TNLAAIEPQP SPPHSEPPSV EQPPKPKLEG VLVNHNEPRS SSRIGLRVHF
NLPEDDKGSE ASSEAGVVTT RQTRPDSFQE RFNGQATKTP EPSSPVKEPP PVLAKPKLDS
TQLQQLHNQV LLEQHQLQNP PPSSPKEFPF SMTVLNSNAP PAVTTSSKQV KAPSSQTFSL
ARPKYFFPST NTTAATVAPS SSPVFTLSST PQTIQRTVSK ESLLVSHPSV QTKSPGGLSI
QNEPLPPGPT EPTPPPFTFS IPSGNQFQPR CVSPIPVSPT SRIQNPVAFL SSVLPSLPAI
PPTNAMGLPR SAPSMPSQGL AKKNTKSPQP VNDDNIRETK NAVIRDLGKK ITFSDVRPNQ
QEYKISSFEQ RLMNEIEFRL ERTPVDESDD EIQHDEIPTG KCIAPIFDKR LKHFRVTEGS
PVTFTCKIVG IPVPKVYWFK DGKQISKRNE HCKMRREGDG TCSLHIESTT SDDDGNYTIM
AANPQGRISC SGHLMVQSLP IRSRLTSAGQ SHRGRSRVQE RDKEPLQERF FRPHFLQAPG
DMVAHEGRLC RLDCKVSGLP PPELTWLLNG QPVLPDASHK MLVRETGVHS LLIDPLTQRD
AGTYKCIATN KTGQNSFSLE LSVVAKEVKK APVILEKLQN CGVPEGHPVR LECRVIGMPP
PVFYWKKDNE TIPCTRERIS MHQDTTGYAC LLIQPAKKSD AGWYTLSAKN EAGIVSCTAR
LDIYAQWHHQ IPPPMSVRPS GSRYGSLTSK GLDIFSAFSS MESTMVYSCS SRSVVESDEL
