MYH14_HUMAN
ID MYH14_HUMAN Reviewed; 1995 AA.
AC Q7Z406; B0I1S2; C3TTN4; Q5CZ75; Q6XYE4; Q76B62; Q8WV23; Q96I22; Q9BT27;
AC Q9BW35; Q9H882;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 2.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Myosin-14;
DE AltName: Full=Myosin heavy chain 14;
DE AltName: Full=Myosin heavy chain, non-muscle IIc;
DE AltName: Full=Non-muscle myosin heavy chain IIc;
DE Short=NMHC II-C;
GN Name=MYH14; Synonyms=KIAA2034; ORFNames=FP17425;
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), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Sciatic nerve;
RX PubMed=12909352; DOI=10.1016/s0378-1119(03)00613-9;
RA Leal A., Endele S., Stengel C., Huehne K., Loetterle J., Barrantes R.,
RA Winterpacht A., Rautenstrauss B.;
RT "A novel myosin heavy chain gene in human chromosome 19q13.3.";
RL Gene 312:165-171(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Yamakawa H., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP PROTEIN SEQUENCE OF 2-11; 190-204; 343-353; 403-413; 434-445; 607-613;
RP 669-675; 718-726; 839-845; 899-906; 957-963; 984-990; 1105-1115; 1244-1264;
RP 1469-1478; 1553-1562 AND 1686-1693, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Colon carcinoma;
RA Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.;
RL Submitted (NOV-2006) to UniProtKB.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 68-998 AND 1740-1995 (ISOFORM 1),
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1297-1995 (ISOFORM 4), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1297-1995 (ISOFORM 5), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 209-477 (ISOFORM 6).
RC TISSUE=Colon, Lung, Muscle, and Placenta;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 590-773 (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=19240025; DOI=10.1074/jbc.m806574200;
RA Jana S.S., Kim K.Y., Mao J., Kawamoto S., Sellers J.R., Adelstein R.S.;
RT "An alternatively spliced isoform of non-muscle myosin II-C is not
RT regulated by myosin light chain phosphorylation.";
RL J. Biol. Chem. 284:11563-11571(2009).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 964-1995 (ISOFORM 1).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1335-1995 (ISOFORM 1).
RC TISSUE=Lymph node;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1431-1995 (ISOFORM 1).
RC TISSUE=Thyroid;
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 [10]
RP IDENTIFICATION.
RX PubMed=11919279; DOI=10.1093/oxfordjournals.molbev.a004093;
RA Desjardins P.R., Burkman J.M., Shrager J.B., Allmond L.A., Stedman H.H.;
RT "Evolutionary implications of three novel members of the human sarcomeric
RT myosin heavy chain gene family.";
RL Mol. Biol. Evol. 19:375-393(2002).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=14594953; DOI=10.1074/jbc.m309981200;
RA Golomb E., Ma X., Jana S.S., Preston Y.A., Kawamoto S., Shoham N.G.,
RA Goldin E., Conti M.A., Sellers J.R., Adelstein R.S.;
RT "Identification and characterization of nonmuscle myosin II-C, a new member
RT of the myosin II family.";
RL J. Biol. Chem. 279:2800-2808(2004).
RN [12]
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 [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-1969 AND SER-1989, 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 THR-1194, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
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-60; SER-1969; SER-1980;
RP SER-1983 AND SER-1989, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 VARIANTS DFNA4A CYS-376; SER-726 AND PHE-976, AND VARIANTS VAL-266 AND
RP SER-1559.
RX PubMed=15015131; DOI=10.1086/383285;
RA Donaudy F., Snoeckx R., Pfister M., Zenner H.-P., Blin N., Di Stazio M.,
RA Ferrara A., Lanzara C., Ficarella R., Declau F., Pusch C.M., Nuernberg P.,
RA Melchionda S., Zelante L., Ballana E., Estivill X., Van Camp G.,
RA Gasparini P., Savoia A.;
RT "Nonmuscle myosin heavy-chain gene MYH14 is expressed in cochlea and
RT mutated in patients affected by autosomal dominant hearing impairment
RT (DFNA4).";
RL Am. J. Hum. Genet. 74:770-776(2004).
RN [18]
RP VARIANT DFNA4A LEU-120.
RX PubMed=16222661; DOI=10.1002/ajmg.a.30989;
RA Yang T., Pfister M., Blin N., Zenner H.P., Pusch C.M., Smith R.J.H.;
RT "Genetic heterogeneity of deafness phenotypes linked to DFNA4.";
RL Am. J. Med. Genet. A 139:9-12(2005).
RN [19]
RP VARIANT PNMHH LEU-933, AND VARIANT VAL-1154.
RX PubMed=21480433; DOI=10.1002/humu.21488;
RA Choi B.O., Kang S.H., Hyun Y.S., Kanwal S., Park S.W., Koo H., Kim S.B.,
RA Choi Y.C., Yoo J.H., Kim J.W., Park K.D., Choi K.G., Kim S.J., Zuchner S.,
RA Chung K.W.;
RT "A complex phenotype of peripheral neuropathy, myopathy, hoarseness, and
RT hearing loss is linked to an autosomal dominant mutation in MYH14.";
RL Hum. Mutat. 32:669-677(2011).
CC -!- FUNCTION: Cellular myosin that appears to play a role in cytokinesis,
CC cell shape, and specialized functions such as secretion and capping.
CC {ECO:0000250}.
CC -!- SUBUNIT: Myosin is a hexameric protein that consists of 2 heavy chain
CC subunits (MHC), 2 alkali light chain subunits (MLC) and 2 regulatory
CC light chain subunits (MLC-2). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q7Z406-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z406-2; Sequence=VSP_040881, VSP_040882;
CC Name=4;
CC IsoId=Q7Z406-4; Sequence=VSP_014628;
CC Name=5;
CC IsoId=Q7Z406-5; Sequence=VSP_014629, VSP_014630;
CC Name=6;
CC IsoId=Q7Z406-6; Sequence=VSP_040881;
CC -!- TISSUE SPECIFICITY: High levels of expression are found in brain
CC (highest in corpus callosum), heart, kidney, liver, lung, small
CC intestine, colon and skeletal muscle. Expression is low in organs
CC composed mainly of smooth muscle, such as aorta, uterus and urinary
CC bladder. No detectable expression is found in thymus, spleen, placenta
CC and lymphocytes. {ECO:0000269|PubMed:12909352,
CC ECO:0000269|PubMed:14594953, ECO:0000269|PubMed:19240025}.
CC -!- DOMAIN: The rodlike tail sequence is highly repetitive, showing cycles
CC of a 28-residue repeat pattern composed of 4 heptapeptides,
CC characteristic for alpha-helical coiled coils. {ECO:0000250}.
CC -!- DISEASE: Deafness, autosomal dominant, 4A (DFNA4A) [MIM:600652]: A form
CC of non-syndromic sensorineural hearing loss. Sensorineural deafness
CC results from damage to the neural receptors of the inner ear, the nerve
CC pathways to the brain, or the area of the brain that receives sound
CC information. {ECO:0000269|PubMed:15015131,
CC ECO:0000269|PubMed:16222661}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Peripheral neuropathy, myopathy, hoarseness, and hearing loss
CC (PNMHH) [MIM:614369]: A complex phenotype of progressive peripheral
CC neuropathy and distal myopathy, with later onset of hoarseness and
CC hearing loss. Affected individuals develop distal muscle weakness at a
CC mean age of 10.6 years, followed by progressive atrophy of these
CC muscles. The lower limbs are more severely affected than the upper
CC limbs, and the muscle weakness first affects anterior leg muscles and
CC later posterior leg muscles. {ECO:0000269|PubMed:21480433}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO39147.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAP34449.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP34449.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB14735.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BG468611; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY165122; AAO39147.1; ALT_FRAME; mRNA.
DR EMBL; AB111886; BAC98374.1; -; mRNA.
DR EMBL; AB290169; BAG06723.1; -; mRNA.
DR EMBL; AC008655; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC010515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC020906; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000676; AAH00676.2; -; mRNA.
DR EMBL; BC004396; AAH04396.1; -; mRNA.
DR EMBL; BC007877; AAH07877.2; -; mRNA.
DR EMBL; BC018933; AAH18933.2; -; mRNA.
DR EMBL; FJ041910; ACM78630.1; -; mRNA.
DR EMBL; BG468611; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AY203926; AAP34449.1; ALT_SEQ; mRNA.
DR EMBL; CR936653; CAI56791.1; -; mRNA.
DR EMBL; AK023943; BAB14735.1; ALT_INIT; mRNA.
DR CCDS; CCDS46151.1; -. [Q7Z406-6]
DR CCDS; CCDS54295.1; -. [Q7Z406-2]
DR CCDS; CCDS59411.1; -. [Q7Z406-1]
DR RefSeq; NP_001070654.1; NM_001077186.1. [Q7Z406-6]
DR RefSeq; NP_001139281.1; NM_001145809.1. [Q7Z406-2]
DR RefSeq; NP_079005.3; NM_024729.3. [Q7Z406-1]
DR RefSeq; XP_006723449.1; XM_006723386.3. [Q7Z406-6]
DR RefSeq; XP_011525625.1; XM_011527323.2. [Q7Z406-6]
DR PDB; 5I4E; X-ray; 2.25 A; A=47-784.
DR PDB; 5JLH; EM; 3.90 A; F/G=1-799.
DR PDBsum; 5I4E; -.
DR PDBsum; 5JLH; -.
DR AlphaFoldDB; Q7Z406; -.
DR SMR; Q7Z406; -.
DR BioGRID; 122884; 151.
DR DIP; DIP-33170N; -.
DR IntAct; Q7Z406; 59.
DR MINT; Q7Z406; -.
DR STRING; 9606.ENSP00000470298; -.
DR ChEMBL; CHEMBL4105888; -.
DR DrugBank; DB07470; (3aS)-3a-hydroxy-1-phenyl-1,2,3,3a-tetrahydro-4H-pyrrolo[2,3-b]quinolin-4-one.
DR DrugBank; DB07468; (3aS)-3a-hydroxy-5-methyl-1-phenyl-1,2,3,3a-tetrahydro-4H-pyrrolo[2,3-b]quinolin-4-one.
DR DrugBank; DB07469; (3aS)-3a-hydroxy-7-methyl-1-phenyl-1,2,3,3a-tetrahydro-4H-pyrrolo[2,3-b]quinolin-4-one.
DR DrugBank; DB01944; (S)-blebbistatin.
DR DrugBank; DB03126; Mant-Adp.
DR DrugBank; DB04444; Tetrafluoroaluminate Ion.
DR DrugBank; DB08276; trifluoro-[hydroxy-[hydroxy-[2-(N-methyl-2-nitro-anilino)ethoxy]phosphoryl]oxy-phosphoryl]oxy-beryllium(1-).
DR GlyGen; Q7Z406; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q7Z406; -.
DR PhosphoSitePlus; Q7Z406; -.
DR SwissPalm; Q7Z406; -.
DR BioMuta; MYH14; -.
DR DMDM; 327478526; -.
DR CPTAC; CPTAC-240; -.
DR CPTAC; CPTAC-241; -.
DR EPD; Q7Z406; -.
DR jPOST; Q7Z406; -.
DR MassIVE; Q7Z406; -.
DR MaxQB; Q7Z406; -.
DR PaxDb; Q7Z406; -.
DR PeptideAtlas; Q7Z406; -.
DR PRIDE; Q7Z406; -.
DR ProteomicsDB; 69113; -. [Q7Z406-1]
DR ProteomicsDB; 69114; -. [Q7Z406-2]
DR ProteomicsDB; 69115; -. [Q7Z406-4]
DR ProteomicsDB; 69116; -. [Q7Z406-5]
DR ProteomicsDB; 69117; -. [Q7Z406-6]
DR Antibodypedia; 32261; 268 antibodies from 33 providers.
DR DNASU; 79784; -.
DR Ensembl; ENST00000376970.6; ENSP00000366169.3; ENSG00000105357.20. [Q7Z406-1]
DR Ensembl; ENST00000425460.6; ENSP00000407879.1; ENSG00000105357.20. [Q7Z406-6]
DR Ensembl; ENST00000596571.5; ENSP00000472819.1; ENSG00000105357.20. [Q7Z406-1]
DR Ensembl; ENST00000598205.5; ENSP00000472543.1; ENSG00000105357.20. [Q7Z406-6]
DR Ensembl; ENST00000642316.2; ENSP00000493594.1; ENSG00000105357.20. [Q7Z406-2]
DR GeneID; 79784; -.
DR KEGG; hsa:79784; -.
DR MANE-Select; ENST00000642316.2; ENSP00000493594.1; NM_001145809.2; NP_001139281.1. [Q7Z406-2]
DR UCSC; uc002prq.2; human. [Q7Z406-1]
DR CTD; 79784; -.
DR DisGeNET; 79784; -.
DR GeneCards; MYH14; -.
DR GeneReviews; MYH14; -.
DR HGNC; HGNC:23212; MYH14.
DR HPA; ENSG00000105357; Tissue enhanced (skeletal).
DR MalaCards; MYH14; -.
DR MIM; 600652; phenotype.
DR MIM; 608568; gene.
DR MIM; 614369; phenotype.
DR neXtProt; NX_Q7Z406; -.
DR OpenTargets; ENSG00000105357; -.
DR Orphanet; 90635; Autosomal dominant non-syndromic sensorineural deafness type DFNA.
DR Orphanet; 397744; Peripheral neuropathy-myopathy-hoarseness-hearing loss syndrome.
DR PharmGKB; PA134935217; -.
DR VEuPathDB; HostDB:ENSG00000105357; -.
DR eggNOG; KOG0161; Eukaryota.
DR GeneTree; ENSGT00940000158808; -.
DR HOGENOM; CLU_000192_4_1_1; -.
DR InParanoid; Q7Z406; -.
DR OrthoDB; 47111at2759; -.
DR PhylomeDB; Q7Z406; -.
DR TreeFam; TF333601; -.
DR PathwayCommons; Q7Z406; -.
DR Reactome; R-HSA-3928663; EPHA-mediated growth cone collapse.
DR Reactome; R-HSA-416572; Sema4D induced cell migration and growth-cone collapse.
DR Reactome; R-HSA-5625740; RHO GTPases activate PKNs.
DR Reactome; R-HSA-5625900; RHO GTPases activate CIT.
DR Reactome; R-HSA-5627117; RHO GTPases Activate ROCKs.
DR Reactome; R-HSA-5627123; RHO GTPases activate PAKs.
DR SignaLink; Q7Z406; -.
DR BioGRID-ORCS; 79784; 9 hits in 1074 CRISPR screens.
DR ChiTaRS; MYH14; human.
DR GeneWiki; MYH14; -.
DR GenomeRNAi; 79784; -.
DR Pharos; Q7Z406; Tchem.
DR PRO; PR:Q7Z406; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q7Z406; protein.
DR Bgee; ENSG00000105357; Expressed in mucosa of transverse colon and 153 other tissues.
DR ExpressionAtlas; Q7Z406; baseline and differential.
DR Genevisible; Q7Z406; HS.
DR GO; GO:0042641; C:actomyosin; IDA:UniProtKB.
DR GO; GO:0005903; C:brush border; IEA:Ensembl.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032982; C:myosin filament; IBA:GO_Central.
DR GO; GO:0016460; C:myosin II complex; IDA:UniProtKB.
DR GO; GO:0097513; C:myosin II filament; IDA:UniProtKB.
DR GO; GO:0001725; C:stress fiber; IEA:Ensembl.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IEA:Ensembl.
DR GO; GO:0030048; P:actin filament-based movement; IEA:Ensembl.
DR GO; GO:0031032; P:actomyosin structure organization; IDA:UniProtKB.
DR GO; GO:0070584; P:mitochondrion morphogenesis; IMP:UniProtKB.
DR GO; GO:0019228; P:neuronal action potential; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0007605; P:sensory perception of sound; IMP:UniProtKB.
DR GO; GO:0003009; P:skeletal muscle contraction; IMP:UniProtKB.
DR GO; GO:0007519; P:skeletal muscle tissue development; IMP:UniProtKB.
DR GO; GO:0071625; P:vocalization behavior; IMP:UniProtKB.
DR Gene3D; 2.30.30.360; -; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR004009; Myosin_N.
DR InterPro; IPR008989; Myosin_S1_N.
DR InterPro; IPR002928; Myosin_tail.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF02736; Myosin_N; 1.
DR Pfam; PF01576; Myosin_tail_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51844; SH3_LIKE; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Actin-binding; Alternative splicing;
KW ATP-binding; Calmodulin-binding; Cell shape; Coiled coil; Deafness;
KW Direct protein sequencing; Disease variant; Motor protein; Myosin;
KW Neuropathy; Non-syndromic deafness; Nucleotide-binding; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.4"
FT CHAIN 2..1995
FT /note="Myosin-14"
FT /id="PRO_0000123431"
FT DOMAIN 51..101
FT /note="Myosin N-terminal SH3-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01190"
FT DOMAIN 105..800
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 803..832
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..700
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT REGION 1371..1415
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1905..1942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1958..1995
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 862..1947
FT /evidence="ECO:0000255"
FT COMPBIAS 1392..1415
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1905..1932
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 198..205
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.4"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1194
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1969
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 1980
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1983
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1989
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 231
FT /note="P -> PASVSTVSY (in isoform 2 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:19240025, ECO:0000303|Ref.2"
FT /id="VSP_040881"
FT VAR_SEQ 640
FT /note="D -> DEHGGFQQFSFLGSFPPSPPGSAERCSSAISPPG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:19240025, ECO:0000303|Ref.2"
FT /id="VSP_040882"
FT VAR_SEQ 1317..1532
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014628"
FT VAR_SEQ 1451..1478
FT /note="MDLEQQRQLVSTLEKKQRKFDQLLAEEK -> LSPDALTDGAQPPSSLDPTG
FT PCPRNPAL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014629"
FT VAR_SEQ 1479..1995
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_014630"
FT VARIANT 120
FT /note="S -> L (in DFNA4A; dbSNP:rs119103281)"
FT /evidence="ECO:0000269|PubMed:16222661"
FT /id="VAR_037302"
FT VARIANT 266
FT /note="I -> V (in dbSNP:rs200424400)"
FT /evidence="ECO:0000269|PubMed:15015131"
FT /id="VAR_022866"
FT VARIANT 334
FT /note="P -> A (in dbSNP:rs34498817)"
FT /id="VAR_056176"
FT VARIANT 376
FT /note="G -> C (in DFNA4A; dbSNP:rs119103280)"
FT /evidence="ECO:0000269|PubMed:15015131"
FT /id="VAR_022867"
FT VARIANT 726
FT /note="R -> S (in DFNA4A; dbSNP:rs28940307)"
FT /evidence="ECO:0000269|PubMed:15015131"
FT /id="VAR_022868"
FT VARIANT 933
FT /note="R -> L (in PNMHH; dbSNP:rs113993956)"
FT /evidence="ECO:0000269|PubMed:21480433"
FT /id="VAR_066338"
FT VARIANT 976
FT /note="L -> F (in DFNA4A; dbSNP:rs28940306)"
FT /evidence="ECO:0000269|PubMed:15015131"
FT /id="VAR_022869"
FT VARIANT 1154
FT /note="A -> V (in dbSNP:rs910420638)"
FT /evidence="ECO:0000269|PubMed:21480433"
FT /id="VAR_066339"
FT VARIANT 1209
FT /note="A -> E (in dbSNP:rs11669191)"
FT /id="VAR_056177"
FT VARIANT 1540
FT /note="V -> I (in dbSNP:rs680446)"
FT /id="VAR_056178"
FT VARIANT 1559
FT /note="N -> S (in dbSNP:rs769482601)"
FT /evidence="ECO:0000269|PubMed:15015131"
FT /id="VAR_022870"
FT CONFLICT 411
FT /note="F -> S (in Ref. 5; BG468611)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="A -> G (in Ref. 5; BG468611)"
FT /evidence="ECO:0000305"
FT CONFLICT 446
FT /note="A -> D (in Ref. 5; BG468611)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="R -> S (in Ref. 5; BG468611)"
FT /evidence="ECO:0000305"
FT CONFLICT 466
FT /note="S -> D (in Ref. 5; BG468611)"
FT /evidence="ECO:0000305"
FT CONFLICT 473
FT /note="F -> L (in Ref. 5; BG468611)"
FT /evidence="ECO:0000305"
FT CONFLICT 997
FT /note="M -> I (in Ref. 5; AAH18933)"
FT /evidence="ECO:0000305"
FT HELIX 51..53
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 61..63
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 75..82
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 156..162
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 174..188
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 204..218
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 233..249
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 259..270
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 276..284
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 288..291
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 302..310
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 313..318
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 324..326
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 340..354
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 359..374
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 388..390
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 395..404
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 408..416
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 433..463
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 473..477
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 490..519
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 520..522
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 535..542
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 545..547
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 550..558
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 565..576
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 587..589
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 592..598
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 601..605
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 610..615
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 620..627
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 632..637
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 670..686
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 688..696
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 709..719
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 721..730
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 734..737
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 738..745
FT /evidence="ECO:0007829|PDB:5I4E"
FT TURN 746..748
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 760..771
FT /evidence="ECO:0007829|PDB:5I4E"
FT HELIX 775..777
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 778..780
FT /evidence="ECO:0007829|PDB:5I4E"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:5I4E"
SQ SEQUENCE 1995 AA; 227871 MW; C77AAB26817B773B CRC64;
MAAVTMSVPG RKAPPRPGPV PEAAQPFLFT PRGPSAGGGP GSGTSPQVEW TARRLVWVPS
ELHGFEAAAL RDEGEEEAEV ELAESGRRLR LPRDQIQRMN PPKFSKAEDM AELTCLNEAS
VLHNLRERYY SGLIYTYSGL FCVVINPYKQ LPIYTEAIVE MYRGKKRHEV PPHVYAVTEG
AYRSMLQDRE DQSILCTGES GAGKTENTKK VIQYLAHVAS SPKGRKEPGV PGELERQLLQ
ANPILEAFGN AKTVKNDNSS RFGKFIRINF DVAGYIVGAN IETYLLEKSR AIRQAKDECS
FHIFYQLLGG AGEQLKADLL LEPCSHYRFL TNGPSSSPGQ ERELFQETLE SLRVLGFSHE
EIISMLRMVS AVLQFGNIAL KRERNTDQAT MPDNTAAQKL CRLLGLGVTD FSRALLTPRI
KVGRDYVQKA QTKEQADFAL EALAKATYER LFRWLVLRLN RALDRSPRQG ASFLGILDIA
GFEIFQLNSF EQLCINYTNE KLQQLFNHTM FVLEQEEYQR EGIPWTFLDF GLDLQPCIDL
IERPANPPGL LALLDEECWF PKATDKSFVE KVAQEQGGHP KFQRPRHLRD QADFSVLHYA
GKVDYKANEW LMKNMDPLND NVAALLHQST DRLTAEIWKD VEGIVGLEQV SSLGDGPPGG
RPRRGMFRTV GQLYKESLSR LMATLSNTNP SFVRCIVPNH EKRAGKLEPR LVLDQLRCNG
VLEGIRICRQ GFPNRILFQE FRQRYEILTP NAIPKGFMDG KQACEKMIQA LELDPNLYRV
GQSKIFFRAG VLAQLEEERD LKVTDIIVSF QAAARGYLAR RAFQKRQQQQ SALRVMQRNC
AAYLKLRHWQ WWRLFTKVKP LLQVTRQDEV LQARAQELQK VQELQQQSAR EVGELQGRVA
QLEEERARLA EQLRAEAELC AEAEETRGRL AARKQELELV VSELEARVGE EEECSRQMQT
EKKRLQQHIQ ELEAHLEAEE GARQKLQLEK VTTEAKMKKF EEDLLLLEDQ NSKLSKERKL
LEDRLAEFSS QAAEEEEKVK SLNKLRLKYE ATIADMEDRL RKEEKGRQEL EKLKRRLDGE
SSELQEQMVE QQQRAEELRA QLGRKEEELQ AALARAEDEG GARAQLLKSL REAQAALAEA
QEDLESERVA RTKAEKQRRD LGEELEALRG ELEDTLDSTN AQQELRSKRE QEVTELKKTL
EEETRIHEAA VQELRQRHGQ ALGELAEQLE QARRGKGAWE KTRLALEAEV SELRAELSSL
QTARQEGEQR RRRLELQLQE VQGRAGDGER ARAEAAEKLQ RAQAELENVS GALNEAESKT
IRLSKELSST EAQLHDAQEL LQEETRAKLA LGSRVRAMEA EAAGLREQLE EEAAARERAG
RELQTAQAQL SEWRRRQEEE AGALEAGEEA RRRAAREAEA LTQRLAEKTE TVDRLERGRR
RLQQELDDAT MDLEQQRQLV STLEKKQRKF DQLLAEEKAA VLRAVEERER AEAEGREREA
RALSLTRALE EEQEAREELE RQNRALRAEL EALLSSKDDV GKSVHELERA CRVAEQAAND
LRAQVTELED ELTAAEDAKL RLEVTVQALK TQHERDLQGR DEAGEERRRQ LAKQLRDAEV
ERDEERKQRT LAVAARKKLE GELEELKAQM ASAGQGKEEA VKQLRKMQAQ MKELWREVEE
TRTSREEIFS QNRESEKRLK GLEAEVLRLQ EELAASDRAR RQAQQDRDEM ADEVANGNLS
KAAILEEKRQ LEGRLGQLEE ELEEEQSNSE LLNDRYRKLL LQVESLTTEL SAERSFSAKA
ESGRQQLERQ IQELRGRLGE EDAGARARHK MTIAALESKL AQAEEQLEQE TRERILSGKL
VRRAEKRLKE VVLQVEEERR VADQLRDQLE KGNLRVKQLK RQLEEAEEEA SRAQAGRRRL
QRELEDVTES AESMNREVTT LRNRLRRGPL TFTTRTVRQV FRLEEGVASD EEAEEAQPGS
GPSPEPEGSP PAHPQ
