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   27-MAR-2024, entry version 164.
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 CMYP4, 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: Congenital myopathy 24 (CMYP4) [MIM:617336]: An autosomal
CC       recessive muscular disorder characterized by slowly progressive muscle
CC       weakness and atrophy, mainly affecting the lower limbs and neck. Some
CC       patients may have mild cardiac or respiratory involvement, but they do
CC       not have respiratory failure. Muscle biopsy shows nemaline bodies.
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)
CC       [MIM:615248]: A hereditary heart disorder characterized by ventricular
CC       hypertrophy, which is usually asymmetric and often involves the
CC       interventricular septum. The symptoms include dyspnea, syncope,
CC       collapse, palpitations, and chest pain. They can be readily provoked by
CC       exercise. The disorder has inter- and intrafamilial variability ranging
CC       from benign to malignant forms with high risk of cardiac failure and
CC       sudden cardiac death. {ECO:0000269|PubMed:22286171}. Note=The disease
CC       is caused by 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};
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; 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; 33.
DR   IntAct; Q86TC9; 10.
DR   MINT; Q86TC9; -.
DR   STRING; 9606.ENSP00000351790; -.
DR   GlyGen; Q86TC9; 11 sites, 1 O-linked glycan (11 sites).
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; 9606-ENSP00000351790; -.
DR   PeptideAtlas; Q86TC9; -.
DR   ProteomicsDB; 69683; -. [Q86TC9-1]
DR   ProteomicsDB; 69684; -. [Q86TC9-2]
DR   Pumba; Q86TC9; -.
DR   Antibodypedia; 28426; 140 antibodies from 22 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   AGR; HGNC:23246; -.
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; DEMDHKP; -.
DR   OrthoDB; 5356884at2759; -.
DR   PhylomeDB; Q86TC9; -.
DR   TreeFam; TF343193; -.
DR   PathwayCommons; Q86TC9; -.
DR   SignaLink; Q86TC9; -.
DR   BioGRID-ORCS; 84665; 18 hits in 1158 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 cell types or tissues.
DR   ExpressionAtlas; Q86TC9; baseline and differential.
DR   GO; GO:0030424; C:axon; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0031674; C:I band; IDA:BHF-UCL.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; Immunoglobulins; 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   PANTHER; PTHR47633:SF7; IG-LIKE DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR47633; IMMUNOGLOBULIN; 1.
DR   Pfam; PF07679; I-set; 5.
DR   SMART; SM00409; IG; 5.
DR   SMART; SM00408; IGc2; 5.
DR   SUPFAM; SSF48726; Immunoglobulin; 5.
DR   PROSITE; PS50835; IG_LIKE; 5.
DR   Genevisible; Q86TC9; HS.
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; uncertain significance;
FT                   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
//