Full text data of MATR3
MATR3
(KIAA0723)
[Confidence: low (only semi-automatic identification from reviews)]
Matrin-3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Matrin-3
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P43243
ID MATR3_HUMAN Reviewed; 847 AA.
AC P43243; B7ZAV5; D3DQC3; Q9UHW0; Q9UQ27;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 150.
DE RecName: Full=Matrin-3;
GN Name=MATR3; Synonyms=KIAA0723;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-12; 150-160; 187-207 AND 374-387, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Kolch W.;
RL Submitted (JUL-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 432-847 (ISOFORM 1).
RX PubMed=2033075;
RA Belgrader P., Dey R., Berezney R.;
RT "Molecular cloning of matrin 3. A 125-kilodalton protein of the
RT nuclear matrix contains an extensive acidic domain.";
RL J. Biol. Chem. 266:9893-9899(1991).
RN [9]
RP FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND
RP IDENTIFICATION IN A COMPLEX WITH SFPQ AND NONO.
RX PubMed=11525732; DOI=10.1016/S0092-8674(01)00466-4;
RA Zhang Z., Carmichael G.G.;
RT "The fate of dsRNA in the nucleus: a p54(nrb)-containing complex
RT mediates the nuclear retention of promiscuously A-to-I edited RNAs.";
RL Cell 106:465-475(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-
RT protein complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-206, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP IDENTIFICATION BY 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-195; SER-208;
RP SER-533; SER-596; SER-598 AND SER-604, AND MASS SPECTROMETRY.
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP IDENTIFICATION IN A COMPLEX WITH ZNF335; MKI67; C11ORF30; ZNF335;
RP HSPA8; TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
RX PubMed=19131338; DOI=10.1074/jbc.M805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A.,
RA Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein
RT complex involved in nuclear hormone receptor-mediated gene
RT regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-118, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-3; LYS-522; LYS-571
RP AND LYS-836, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-14; SER-41;
RP SER-188; SER-195; SER-206; SER-208; SER-533; SER-598; SER-604; SER-606
RP AND SER-766, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-9; SER-188;
RP SER-195; SER-206; SER-208; TYR-219; SER-533; SER-596; SER-598;
RP SER-604; THR-741; SER-747 AND SER-766, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP VARIANT MPD2 CYS-85.
RX PubMed=19344878; DOI=10.1016/j.ajhg.2009.03.006;
RA Senderek J., Garvey S.M., Krieger M., Guergueltcheva V.,
RA Urtizberea A., Roos A., Elbracht M., Stendel C., Tournev I.,
RA Mihailova V., Feit H., Tramonte J., Hedera P., Crooks K., Bergmann C.,
RA Rudnik-Schoeneborn S., Zerres K., Lochmueller H., Seboun E., Weis J.,
RA Beckmann J.S., Hauser M.A., Jackson C.E.;
RT "Autosomal-dominant distal myopathy associated with a recurrent
RT missense mutation in the gene encoding the nuclear matrix protein,
RT matrin 3.";
RL Am. J. Hum. Genet. 84:511-518(2009).
CC -!- FUNCTION: May play a role in transcription or may interact with
CC other nuclear matrix proteins to form the internal fibrogranular
CC network. In association with the SFPQ-NONO heteromer may play a
CC role in nuclear retention of defective RNAs.
CC -!- SUBUNIT: Part of complex consisting of SFPQ, NONO and MATR3.
CC Interacts with AGO1 and AGO2. Part of a complex composed at least
CC of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5,
CC TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-
CC specific methyltransferase activity.
CC -!- INTERACTION:
CC P22736:NR4A1; NbExp=2; IntAct=EBI-352602, EBI-721550;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43243-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43243-2; Sequence=VSP_042624;
CC Note=No experimental confirmation available;
CC -!- DISEASE: Myopathy, distal, 2 (MPD2) [MIM:606070]: A muscular
CC disorder characterized by distal weakness, with onset in hands and
CC feet, associated with vocal cord and pharyngeal weakness causing a
CC nasal voice and swallowing disorders. Note=The disease is caused
CC by mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Contains 1 matrin-type zinc finger.
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17217.1; Type=Frameshift; Positions=Several;
CC Sequence=BAA34443.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB018266; BAA34443.2; ALT_INIT; mRNA.
DR EMBL; AF117236; AAF17217.1; ALT_FRAME; mRNA.
DR EMBL; AK316420; BAH14791.1; -; mRNA.
DR EMBL; AC011404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62114.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62115.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62116.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62117.1; -; Genomic_DNA.
DR EMBL; BC015031; AAH15031.1; -; mRNA.
DR EMBL; M63483; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001181883.1; NM_001194954.1.
DR RefSeq; NP_001181884.1; NM_001194955.1.
DR RefSeq; NP_001181885.1; NM_001194956.1.
DR RefSeq; NP_001269207.1; NM_001282278.1.
DR RefSeq; NP_061322.2; NM_018834.5.
DR RefSeq; NP_954659.1; NM_199189.2.
DR UniGene; Hs.268939; -.
DR UniGene; Hs.595110; -.
DR ProteinModelPortal; P43243; -.
DR SMR; P43243; 390-576.
DR IntAct; P43243; 49.
DR MINT; MINT-4999417; -.
DR STRING; 9606.ENSP00000354346; -.
DR PhosphoSite; P43243; -.
DR DMDM; 12643409; -.
DR PaxDb; P43243; -.
DR PRIDE; P43243; -.
DR DNASU; 9782; -.
DR Ensembl; ENST00000361059; ENSP00000354346; ENSG00000015479.
DR Ensembl; ENST00000394805; ENSP00000378284; ENSG00000015479.
DR Ensembl; ENST00000503811; ENSP00000423587; ENSG00000015479.
DR Ensembl; ENST00000509990; ENSP00000423533; ENSG00000015479.
DR GeneID; 9782; -.
DR KEGG; hsa:9782; -.
DR UCSC; uc003ldt.3; human.
DR CTD; 9782; -.
DR GeneCards; GC05P138609; -.
DR HGNC; HGNC:6912; MATR3.
DR HPA; CAB033552; -.
DR HPA; HPA036564; -.
DR HPA; HPA036565; -.
DR MIM; 164015; gene.
DR MIM; 606070; phenotype.
DR neXtProt; NX_P43243; -.
DR Orphanet; 600; Distal myopathy with vocal cord weakness.
DR PharmGKB; PA30655; -.
DR eggNOG; NOG80010; -.
DR HOGENOM; HOG000015369; -.
DR HOVERGEN; HBG057347; -.
DR KO; K13213; -.
DR OrthoDB; EOG7GJ6C8; -.
DR PhylomeDB; P43243; -.
DR ChiTaRS; MATR3; human.
DR GeneWiki; MATR3; -.
DR GenomeRNAi; 9782; -.
DR NextBio; 36832; -.
DR PMAP-CutDB; P43243; -.
DR PRO; PR:P43243; -.
DR ArrayExpress; P43243; -.
DR Bgee; P43243; -.
DR CleanEx; HS_MATR3; -.
DR Genevestigator; P43243; -.
DR GO; GO:0005637; C:nuclear inner membrane; TAS:ProtInc.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR000690; Znf_C2H2_matrin.
DR InterPro; IPR003604; Znf_U1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SMART; SM00451; ZnF_U1; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Disease mutation; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 847 Matrin-3.
FT /FTId=PRO_0000081622.
FT DOMAIN 398 473 RRM 1.
FT DOMAIN 496 571 RRM 2.
FT ZN_FING 801 832 Matrin-type.
FT MOTIF 710 718 Nuclear localization signal (Potential).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 3 3 N6-acetyllysine.
FT MOD_RES 4 4 Phosphoserine.
FT MOD_RES 9 9 Phosphoserine.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 22 22 Phosphoserine.
FT MOD_RES 41 41 Phosphoserine.
FT MOD_RES 118 118 Phosphoserine.
FT MOD_RES 188 188 Phosphoserine.
FT MOD_RES 195 195 Phosphoserine.
FT MOD_RES 206 206 Phosphoserine.
FT MOD_RES 208 208 Phosphoserine.
FT MOD_RES 219 219 Phosphotyrosine.
FT MOD_RES 522 522 N6-acetyllysine.
FT MOD_RES 533 533 Phosphoserine.
FT MOD_RES 571 571 N6-acetyllysine.
FT MOD_RES 596 596 Phosphoserine.
FT MOD_RES 598 598 Phosphoserine.
FT MOD_RES 604 604 Phosphoserine.
FT MOD_RES 606 606 Phosphoserine.
FT MOD_RES 741 741 Phosphothreonine.
FT MOD_RES 747 747 Phosphoserine.
FT MOD_RES 766 766 Phosphoserine.
FT MOD_RES 836 836 N6-acetyllysine.
FT VAR_SEQ 1 304 MSKSFQQSSLSRDSQGHGRDLSAAGIGLLAAATQSLSMPAS
FT LGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHN
FT LQSIFNIGSRGPLPLSSQHRGDADQASNILASFGLSARDLD
FT ELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRS
FT ATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHG
FT SRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKF
FT DSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPK
FT GYPHLCSICDLPVHSNK -> MLGAQWRRNQPSRAAE (in
FT isoform 2).
FT /FTId=VSP_042624.
FT VARIANT 85 85 S -> C (in MPD2; dbSNP:rs121434591).
FT /FTId=VAR_063421.
FT CONFLICT 257 257 P -> S (in Ref. 2; AAF17217).
FT CONFLICT 274 274 P -> S (in Ref. 2; AAF17217).
FT CONFLICT 572 572 Y -> C (in Ref. 2; AAF17217 and 8;
FT M63483).
FT CONFLICT 691 691 G -> P (in Ref. 8; M63483).
FT CONFLICT 703 703 D -> H (in Ref. 8; M63483).
SQ SEQUENCE 847 AA; 94623 MW; 530AA49214BC1611 CRC64;
MSKSFQQSSL SRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDADQASN ILASFGLSAR
DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE
KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS
HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV
HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP
PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE
PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP
EGKPDQKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME
TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD
GKESPSDKKS KTDGSQKTES STEGKEQEEK SGEDGEKDTK DDQTEQEPNM LLESEDELLV
DEEEAAALLE SGSSVGDETD LANLGDVASD GKKEPSDKAV KKDGSASAAA KKKLKKVDKI
EELDQENEAA LENGIKNEEN TEPGAESSEN ADDPNKDTSE NADGQSDENK DDYTIPDEYR
IGPYQPNVPV GIDYVIPKTG FYCKLCSLFY TNEEVAKNTH CSSLPHYQKL KKFLNKLAEE
RRQKKET
//
ID MATR3_HUMAN Reviewed; 847 AA.
AC P43243; B7ZAV5; D3DQC3; Q9UHW0; Q9UQ27;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
read moreDT 24-JAN-2001, sequence version 2.
DT 22-JAN-2014, entry version 150.
DE RecName: Full=Matrin-3;
GN Name=MATR3; Synonyms=KIAA0723;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9872452; DOI=10.1093/dnares/5.5.277;
RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XI.
RT The complete sequences of 100 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 5:277-286(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP PROTEIN SEQUENCE OF 2-12; 150-160; 187-207 AND 374-387, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Mammary carcinoma;
RA Bienvenut W.V., Matallanas D., Kolch W.;
RL Submitted (JUL-2009) to UniProtKB.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 432-847 (ISOFORM 1).
RX PubMed=2033075;
RA Belgrader P., Dey R., Berezney R.;
RT "Molecular cloning of matrin 3. A 125-kilodalton protein of the
RT nuclear matrix contains an extensive acidic domain.";
RL J. Biol. Chem. 266:9893-9899(1991).
RN [9]
RP FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND
RP IDENTIFICATION IN A COMPLEX WITH SFPQ AND NONO.
RX PubMed=11525732; DOI=10.1016/S0092-8674(01)00466-4;
RA Zhang Z., Carmichael G.G.;
RT "The fate of dsRNA in the nucleus: a p54(nrb)-containing complex
RT mediates the nuclear retention of promiscuously A-to-I edited RNAs.";
RL Cell 106:465-475(2001).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [11]
RP INTERACTION WITH AGO1 AND AGO2.
RX PubMed=17932509; DOI=10.1038/sj.embor.7401088;
RA Hoeck J., Weinmann L., Ender C., Ruedel S., Kremmer E., Raabe M.,
RA Urlaub H., Meister G.;
RT "Proteomic and functional analysis of Argonaute-containing mRNA-
RT protein complexes in human cells.";
RL EMBO Rep. 8:1052-1060(2007).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa
RT cells and high confident phosphopeptide identification by cross-
RT validation of MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-206, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [15]
RP IDENTIFICATION BY 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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188; SER-195; SER-208;
RP SER-533; SER-596; SER-598 AND SER-604, AND MASS SPECTROMETRY.
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND MASS
RP SPECTROMETRY.
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by
RT enrichment and fractionation of phosphopeptides with strong anion
RT exchange chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [18]
RP IDENTIFICATION IN A COMPLEX WITH ZNF335; MKI67; C11ORF30; ZNF335;
RP HSPA8; TUBB2A; CCAR2; ASCL2; RBBP5 AND WDR5.
RX PubMed=19131338; DOI=10.1074/jbc.M805872200;
RA Garapaty S., Xu C.F., Trojer P., Mahajan M.A., Neubert T.A.,
RA Samuels H.H.;
RT "Identification and characterization of a novel nuclear protein
RT complex involved in nuclear hormone receptor-mediated gene
RT regulation.";
RL J. Biol. Chem. 284:7542-7552(2009).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-118, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2; LYS-3; LYS-522; LYS-571
RP AND LYS-836, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-14; SER-41;
RP SER-188; SER-195; SER-206; SER-208; SER-533; SER-598; SER-604; SER-606
RP AND SER-766, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [22]
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.,
RA Buerckstuemmer T., 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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4; SER-9; SER-188;
RP SER-195; SER-206; SER-208; TYR-219; SER-533; SER-596; SER-598;
RP SER-604; THR-741; SER-747 AND SER-766, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [24]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [25]
RP VARIANT MPD2 CYS-85.
RX PubMed=19344878; DOI=10.1016/j.ajhg.2009.03.006;
RA Senderek J., Garvey S.M., Krieger M., Guergueltcheva V.,
RA Urtizberea A., Roos A., Elbracht M., Stendel C., Tournev I.,
RA Mihailova V., Feit H., Tramonte J., Hedera P., Crooks K., Bergmann C.,
RA Rudnik-Schoeneborn S., Zerres K., Lochmueller H., Seboun E., Weis J.,
RA Beckmann J.S., Hauser M.A., Jackson C.E.;
RT "Autosomal-dominant distal myopathy associated with a recurrent
RT missense mutation in the gene encoding the nuclear matrix protein,
RT matrin 3.";
RL Am. J. Hum. Genet. 84:511-518(2009).
CC -!- FUNCTION: May play a role in transcription or may interact with
CC other nuclear matrix proteins to form the internal fibrogranular
CC network. In association with the SFPQ-NONO heteromer may play a
CC role in nuclear retention of defective RNAs.
CC -!- SUBUNIT: Part of complex consisting of SFPQ, NONO and MATR3.
CC Interacts with AGO1 and AGO2. Part of a complex composed at least
CC of ASCL2, C11orf30/EMSY, HCFC1, HSPA8, CCAR2, MATR3, MKI67, RBBP5,
CC TUBB2A, WDR5 and ZNF335; this complex may have a histone H3-
CC specific methyltransferase activity.
CC -!- INTERACTION:
CC P22736:NR4A1; NbExp=2; IntAct=EBI-352602, EBI-721550;
CC -!- SUBCELLULAR LOCATION: Nucleus matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P43243-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P43243-2; Sequence=VSP_042624;
CC Note=No experimental confirmation available;
CC -!- DISEASE: Myopathy, distal, 2 (MPD2) [MIM:606070]: A muscular
CC disorder characterized by distal weakness, with onset in hands and
CC feet, associated with vocal cord and pharyngeal weakness causing a
CC nasal voice and swallowing disorders. Note=The disease is caused
CC by mutations affecting the gene represented in this entry.
CC -!- SIMILARITY: Contains 1 matrin-type zinc finger.
CC -!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17217.1; Type=Frameshift; Positions=Several;
CC Sequence=BAA34443.2; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR EMBL; AB018266; BAA34443.2; ALT_INIT; mRNA.
DR EMBL; AF117236; AAF17217.1; ALT_FRAME; mRNA.
DR EMBL; AK316420; BAH14791.1; -; mRNA.
DR EMBL; AC011404; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471062; EAW62114.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62115.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62116.1; -; Genomic_DNA.
DR EMBL; CH471062; EAW62117.1; -; Genomic_DNA.
DR EMBL; BC015031; AAH15031.1; -; mRNA.
DR EMBL; M63483; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001181883.1; NM_001194954.1.
DR RefSeq; NP_001181884.1; NM_001194955.1.
DR RefSeq; NP_001181885.1; NM_001194956.1.
DR RefSeq; NP_001269207.1; NM_001282278.1.
DR RefSeq; NP_061322.2; NM_018834.5.
DR RefSeq; NP_954659.1; NM_199189.2.
DR UniGene; Hs.268939; -.
DR UniGene; Hs.595110; -.
DR ProteinModelPortal; P43243; -.
DR SMR; P43243; 390-576.
DR IntAct; P43243; 49.
DR MINT; MINT-4999417; -.
DR STRING; 9606.ENSP00000354346; -.
DR PhosphoSite; P43243; -.
DR DMDM; 12643409; -.
DR PaxDb; P43243; -.
DR PRIDE; P43243; -.
DR DNASU; 9782; -.
DR Ensembl; ENST00000361059; ENSP00000354346; ENSG00000015479.
DR Ensembl; ENST00000394805; ENSP00000378284; ENSG00000015479.
DR Ensembl; ENST00000503811; ENSP00000423587; ENSG00000015479.
DR Ensembl; ENST00000509990; ENSP00000423533; ENSG00000015479.
DR GeneID; 9782; -.
DR KEGG; hsa:9782; -.
DR UCSC; uc003ldt.3; human.
DR CTD; 9782; -.
DR GeneCards; GC05P138609; -.
DR HGNC; HGNC:6912; MATR3.
DR HPA; CAB033552; -.
DR HPA; HPA036564; -.
DR HPA; HPA036565; -.
DR MIM; 164015; gene.
DR MIM; 606070; phenotype.
DR neXtProt; NX_P43243; -.
DR Orphanet; 600; Distal myopathy with vocal cord weakness.
DR PharmGKB; PA30655; -.
DR eggNOG; NOG80010; -.
DR HOGENOM; HOG000015369; -.
DR HOVERGEN; HBG057347; -.
DR KO; K13213; -.
DR OrthoDB; EOG7GJ6C8; -.
DR PhylomeDB; P43243; -.
DR ChiTaRS; MATR3; human.
DR GeneWiki; MATR3; -.
DR GenomeRNAi; 9782; -.
DR NextBio; 36832; -.
DR PMAP-CutDB; P43243; -.
DR PRO; PR:P43243; -.
DR ArrayExpress; P43243; -.
DR Bgee; P43243; -.
DR CleanEx; HS_MATR3; -.
DR Genevestigator; P43243; -.
DR GO; GO:0005637; C:nuclear inner membrane; TAS:ProtInc.
DR GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR015880; Znf_C2H2-like.
DR InterPro; IPR000690; Znf_C2H2_matrin.
DR InterPro; IPR003604; Znf_U1.
DR SMART; SM00360; RRM; 2.
DR SMART; SM00355; ZnF_C2H2; 1.
DR SMART; SM00451; ZnF_U1; 2.
DR PROSITE; PS50102; RRM; 2.
DR PROSITE; PS50171; ZF_MATRIN; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Disease mutation; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Zinc;
KW Zinc-finger.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 847 Matrin-3.
FT /FTId=PRO_0000081622.
FT DOMAIN 398 473 RRM 1.
FT DOMAIN 496 571 RRM 2.
FT ZN_FING 801 832 Matrin-type.
FT MOTIF 710 718 Nuclear localization signal (Potential).
FT MOD_RES 2 2 N-acetylserine.
FT MOD_RES 3 3 N6-acetyllysine.
FT MOD_RES 4 4 Phosphoserine.
FT MOD_RES 9 9 Phosphoserine.
FT MOD_RES 14 14 Phosphoserine.
FT MOD_RES 22 22 Phosphoserine.
FT MOD_RES 41 41 Phosphoserine.
FT MOD_RES 118 118 Phosphoserine.
FT MOD_RES 188 188 Phosphoserine.
FT MOD_RES 195 195 Phosphoserine.
FT MOD_RES 206 206 Phosphoserine.
FT MOD_RES 208 208 Phosphoserine.
FT MOD_RES 219 219 Phosphotyrosine.
FT MOD_RES 522 522 N6-acetyllysine.
FT MOD_RES 533 533 Phosphoserine.
FT MOD_RES 571 571 N6-acetyllysine.
FT MOD_RES 596 596 Phosphoserine.
FT MOD_RES 598 598 Phosphoserine.
FT MOD_RES 604 604 Phosphoserine.
FT MOD_RES 606 606 Phosphoserine.
FT MOD_RES 741 741 Phosphothreonine.
FT MOD_RES 747 747 Phosphoserine.
FT MOD_RES 766 766 Phosphoserine.
FT MOD_RES 836 836 N6-acetyllysine.
FT VAR_SEQ 1 304 MSKSFQQSSLSRDSQGHGRDLSAAGIGLLAAATQSLSMPAS
FT LGRMNQGTARLASLMNLGMSSSLNQQGAHSALSSASTSSHN
FT LQSIFNIGSRGPLPLSSQHRGDADQASNILASFGLSARDLD
FT ELSRYPEDKITPENLPQILLQLKRRRTEEGPTLSYGRDGRS
FT ATREPPYRVPRDDWEEKRHFRRDSFDDRGPSLNPVLDYDHG
FT SRSQESGYYDRMDYEDDRLRDGERCRDDSFFGETSHNYHKF
FT DSEYERMGRGPGPLQERSLFEKKRGAPPSSNIEDFHGLLPK
FT GYPHLCSICDLPVHSNK -> MLGAQWRRNQPSRAAE (in
FT isoform 2).
FT /FTId=VSP_042624.
FT VARIANT 85 85 S -> C (in MPD2; dbSNP:rs121434591).
FT /FTId=VAR_063421.
FT CONFLICT 257 257 P -> S (in Ref. 2; AAF17217).
FT CONFLICT 274 274 P -> S (in Ref. 2; AAF17217).
FT CONFLICT 572 572 Y -> C (in Ref. 2; AAF17217 and 8;
FT M63483).
FT CONFLICT 691 691 G -> P (in Ref. 8; M63483).
FT CONFLICT 703 703 D -> H (in Ref. 8; M63483).
SQ SEQUENCE 847 AA; 94623 MW; 530AA49214BC1611 CRC64;
MSKSFQQSSL SRDSQGHGRD LSAAGIGLLA AATQSLSMPA SLGRMNQGTA RLASLMNLGM
SSSLNQQGAH SALSSASTSS HNLQSIFNIG SRGPLPLSSQ HRGDADQASN ILASFGLSAR
DLDELSRYPE DKITPENLPQ ILLQLKRRRT EEGPTLSYGR DGRSATREPP YRVPRDDWEE
KRHFRRDSFD DRGPSLNPVL DYDHGSRSQE SGYYDRMDYE DDRLRDGERC RDDSFFGETS
HNYHKFDSEY ERMGRGPGPL QERSLFEKKR GAPPSSNIED FHGLLPKGYP HLCSICDLPV
HSNKEWSQHI NGASHSRRCQ LLLEIYPEWN PDNDTGHTMG DPFMLQQSTN PAPGILGPPP
PSFHLGGPAV GPRGNLGAGN GNLQGPRHMQ KGRVETSRVV HIMDFQRGKN LRYQLLQLVE
PFGVISNHLI LNKINEAFIE MATTEDAQAA VDYYTTTPAL VFGKPVRVHL SQKYKRIKKP
EGKPDQKFDQ KQELGRVIHL SNLPHSGYSD SAVLKLAEPY GKIKNYILMR MKSQAFIEME
TREDAMAMVD HCLKKALWFQ GRCVKVDLSE KYKKLVLRIP NRGIDLLKKD KSRKRSYSPD
GKESPSDKKS KTDGSQKTES STEGKEQEEK SGEDGEKDTK DDQTEQEPNM LLESEDELLV
DEEEAAALLE SGSSVGDETD LANLGDVASD GKKEPSDKAV KKDGSASAAA KKKLKKVDKI
EELDQENEAA LENGIKNEEN TEPGAESSEN ADDPNKDTSE NADGQSDENK DDYTIPDEYR
IGPYQPNVPV GIDYVIPKTG FYCKLCSLFY TNEEVAKNTH CSSLPHYQKL KKFLNKLAEE
RRQKKET
//
MIM
164015
*RECORD*
*FIELD* NO
164015
*FIELD* TI
*164015 MATRIN 3; MATR3
*FIELD* TX
CLONING
Stuurman et al. (1990) showed that nuclear matrins, a group of proteins
read morein the nuclear matrix, are present in cultured cells from a variety of
tissues and are probably common to mammalian cells. Stuurman et al.
(1990) differentiated 2 nuclear matrix fractions: the peripheral nuclear
matrix (matrix proteins that remain insoluble after reduction), and the
internal nuclear matrix (matrix proteins released by reduction).
Nakayasu and Berezney (1991) identified several novel nuclear matrins
from a rat liver nuclear matrix and characterized them by peptide maps,
polyclonal antibodies generated against the individual matrins, and
indirect immunofluorescence microscopy. They designated the proteins
matrins 3, 4, D-G, 12, and 13.
Belgrader et al. (1991) cloned a full-length rat insulinoma cDNA that
encodes an acidic internal matrix protein designated matrin-3. The
deduced 845-amino acid protein has a calculated molecular mass of
approximately 95 kD. Its primary structure consists of 33% charged
residues and is generally hydrophilic. Like the lamins (see 150330),
matrin-3 has a positively charged N terminus that contains a large
number of amino acids with free hydroxyl groups. A highly acidic domain
near the C terminus, in which 32% of the amino acids are acidic, is a
characteristic found in other nuclear proteins.
Nagase et al. (1998) cloned and sequenced matrin-3, which they called
KIAA0723, from human brain cDNA libraries. The deduced protein contains
847 amino acids.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MATR3
gene to chromosome 5 (TMAP WI-15469).
Using genomic sequence analysis, Senderek et al. (2009) mapped the MATR3
gene to chromosome 5q31.
MOLECULAR GENETICS
In 2 unrelated families with a form of distal myopathy that included
vocal cord and pharyngeal weakness (MPD2; 606070), Senderek et al.
(2009) identified the same missense mutation in the MATR3 gene (S85C;
164015.0001).
*FIELD* AV
.0001
MYOPATHY, DISTAL, 2
MATR3, SER85CYS
In affected members of a North American family originally reported by
Feit et al. (1998) and in an unrelated Bulgarian family with distal
myopathy with vocal cord and pharyngeal weakness (MPD2; 606070),
Senderek et al. (2009) identified heterozygosity for a C-to-G
transversion at nucleotide 254 in exon 2 of the MATR3 gene that resulted
in a change from serine to cysteine at codon 85 (S85C).
*FIELD* RF
1. Belgrader, P.; Dey, R.; Berezney, R.: Molecular cloning of matrin
3: a 125-kilodalton protein of the nuclear matrix contains an extensive
acidic domain. J. Biol. Chem. 266: 9893-9899, 1991.
2. Feit, H.; Silbergleit, A.; Schneider, L. B.; Gutierrez, J. A.;
Fitoussi, R.-P.; Reyes, C.; Rouleau, G. A.; Brais, B.; Jackson, C.
E.; Beckmann, J. S.; Seboun, E.: Vocal cord and pharyngeal weakness
with autosomal dominant distal myopathy: clinical description and
gene localization to 5q31. Am. J. Hum. Genet. 63: 1732-1742, 1998.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
4. Nakayasu, H.; Berezney, R.: Nuclear matrins: identification of
the major nuclear matrix proteins. Proc. Nat. Acad. Sci. 88: 10312-10316,
1991.
5. Senderek, J.; Garvey, S. M.; Krieger, M.; Guergueltcheva, V.; Urtizberea,
A.; Roos, A.; Elbracht, M.; Stendel, C.; Tournev, I.; Mihailova, V.;
Feit, H.; Tramonte, J.; and 11 others: Autosomal-dominant distal
myopathy associated with a recurrent missense mutation in the gene
encoding the nuclear matrix protein, matrin 3. Am. J. Hum. Genet. 84:
511-518, 2009.
6. Stuurman, N.; Meijne, A. M. L.; van der Pol, A. J.; de Jong, L.;
van Driel, R.; van Renswoude, J.: The nuclear matrix from cells of
different origin: evidence for a common set of matrix proteins. J.
Biol. Chem. 265: 5460-5465, 1990.
*FIELD* CN
Anne M. Stumpf - updated: 10/20/2009
*FIELD* CD
Victor A. McKusick: 11/27/1991
*FIELD* ED
wwang: 07/01/2011
alopez: 10/20/2009
carol: 5/4/2007
supermim: 3/16/1992
carol: 11/27/1991
*RECORD*
*FIELD* NO
164015
*FIELD* TI
*164015 MATRIN 3; MATR3
*FIELD* TX
CLONING
Stuurman et al. (1990) showed that nuclear matrins, a group of proteins
read morein the nuclear matrix, are present in cultured cells from a variety of
tissues and are probably common to mammalian cells. Stuurman et al.
(1990) differentiated 2 nuclear matrix fractions: the peripheral nuclear
matrix (matrix proteins that remain insoluble after reduction), and the
internal nuclear matrix (matrix proteins released by reduction).
Nakayasu and Berezney (1991) identified several novel nuclear matrins
from a rat liver nuclear matrix and characterized them by peptide maps,
polyclonal antibodies generated against the individual matrins, and
indirect immunofluorescence microscopy. They designated the proteins
matrins 3, 4, D-G, 12, and 13.
Belgrader et al. (1991) cloned a full-length rat insulinoma cDNA that
encodes an acidic internal matrix protein designated matrin-3. The
deduced 845-amino acid protein has a calculated molecular mass of
approximately 95 kD. Its primary structure consists of 33% charged
residues and is generally hydrophilic. Like the lamins (see 150330),
matrin-3 has a positively charged N terminus that contains a large
number of amino acids with free hydroxyl groups. A highly acidic domain
near the C terminus, in which 32% of the amino acids are acidic, is a
characteristic found in other nuclear proteins.
Nagase et al. (1998) cloned and sequenced matrin-3, which they called
KIAA0723, from human brain cDNA libraries. The deduced protein contains
847 amino acids.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the MATR3
gene to chromosome 5 (TMAP WI-15469).
Using genomic sequence analysis, Senderek et al. (2009) mapped the MATR3
gene to chromosome 5q31.
MOLECULAR GENETICS
In 2 unrelated families with a form of distal myopathy that included
vocal cord and pharyngeal weakness (MPD2; 606070), Senderek et al.
(2009) identified the same missense mutation in the MATR3 gene (S85C;
164015.0001).
*FIELD* AV
.0001
MYOPATHY, DISTAL, 2
MATR3, SER85CYS
In affected members of a North American family originally reported by
Feit et al. (1998) and in an unrelated Bulgarian family with distal
myopathy with vocal cord and pharyngeal weakness (MPD2; 606070),
Senderek et al. (2009) identified heterozygosity for a C-to-G
transversion at nucleotide 254 in exon 2 of the MATR3 gene that resulted
in a change from serine to cysteine at codon 85 (S85C).
*FIELD* RF
1. Belgrader, P.; Dey, R.; Berezney, R.: Molecular cloning of matrin
3: a 125-kilodalton protein of the nuclear matrix contains an extensive
acidic domain. J. Biol. Chem. 266: 9893-9899, 1991.
2. Feit, H.; Silbergleit, A.; Schneider, L. B.; Gutierrez, J. A.;
Fitoussi, R.-P.; Reyes, C.; Rouleau, G. A.; Brais, B.; Jackson, C.
E.; Beckmann, J. S.; Seboun, E.: Vocal cord and pharyngeal weakness
with autosomal dominant distal myopathy: clinical description and
gene localization to 5q31. Am. J. Hum. Genet. 63: 1732-1742, 1998.
3. Nagase, T.; Ishikawa, K.; Suyama, M.; Kikuno, R.; Miyajima, N.;
Tanaka, A.; Kotani, H.; Nomura, N.; Ohara, O.: Prediction of the
coding sequences of unidentified human genes. XI. The complete sequences
of 100 new cDNA clones from brain which code for large proteins in
vitro. DNA Res. 5: 277-286, 1998.
4. Nakayasu, H.; Berezney, R.: Nuclear matrins: identification of
the major nuclear matrix proteins. Proc. Nat. Acad. Sci. 88: 10312-10316,
1991.
5. Senderek, J.; Garvey, S. M.; Krieger, M.; Guergueltcheva, V.; Urtizberea,
A.; Roos, A.; Elbracht, M.; Stendel, C.; Tournev, I.; Mihailova, V.;
Feit, H.; Tramonte, J.; and 11 others: Autosomal-dominant distal
myopathy associated with a recurrent missense mutation in the gene
encoding the nuclear matrix protein, matrin 3. Am. J. Hum. Genet. 84:
511-518, 2009.
6. Stuurman, N.; Meijne, A. M. L.; van der Pol, A. J.; de Jong, L.;
van Driel, R.; van Renswoude, J.: The nuclear matrix from cells of
different origin: evidence for a common set of matrix proteins. J.
Biol. Chem. 265: 5460-5465, 1990.
*FIELD* CN
Anne M. Stumpf - updated: 10/20/2009
*FIELD* CD
Victor A. McKusick: 11/27/1991
*FIELD* ED
wwang: 07/01/2011
alopez: 10/20/2009
carol: 5/4/2007
supermim: 3/16/1992
carol: 11/27/1991
MIM
606070
*RECORD*
*FIELD* NO
606070
*FIELD* TI
#606070 MYOPATHY, DISTAL, 2; MPD2
;;VOCAL CORD AND PHARYNGEAL DYSFUNCTION WITH DISTAL MYOPATHY; VCPDM
read more*FIELD* TX
A number sign (#) is used with this entry because this form of distal
myopathy is caused by mutation in the matrin-3 gene on chromosome 5q31
(MATR3; 164015).
CLINICAL FEATURES
Feit et al. (1998) described a large American family segregating an
autosomal dominant distal myopathy, with multiple affected individuals
in whom vocal cord and pharyngeal weakness may accompany the distal
myopathy, without involvement of the ocular muscles. From a
histopathologic standpoint, the lesion observed in these individuals was
a noninflammatory myopathy with rimmed vacuoles probably fitting into
the spectrum of the inclusion-bodied myopathies. Overall, the myopathy
was mild or moderate. They stated that this 'form of distal myopathy has
not been previously recognized and is distinct from other myopathies
with pharyngeal or vocal weakness.' They referred to the clinical
disorder as VCPDM (vocal cord and pharyngeal dysfunction with distal
myopathy).
Senderek et al. (2009) expanded the family described by Feit et al.
(1998) with 2 additional sibs from an additional branch of the family.
They also described a multigenerational Bulgarian family with a typical
VCPDM phenotype.
DIAGNOSIS
- Differential Diagnosis
Feit et al. (1998) commented on the possible confusion of the MPD2
phenotype with the axonal (neuronal) form of Charcot-Marie-tooth
disease, CMT2 (see CMT2A1; 118210), if EMG results show a neurogenic
disorder with normal nerve conduction velocities. Muscle biopsy would be
required to distinguish between the 2 disorders. They also noted that
the diagnosis of MPD2 does not require voice and pharyngeal changes,
since some affected individuals in the kindred they studied did not show
these changes at the time of examination. Two myopathies had already
been mapped to 5q, the autosomal recessive limb-girdle muscular
dystrophy (LGMD) 2F (601287) and the autosomal dominant LGMD1A (159000).
LGMD2F was excluded because it was found to lie outside the linkage
interval of MPD2. LGMD1A was encompassed by the linkage interval of
MPD2, but the phenotypes of the 2 disorders were clinically quite
different. Proximal weakness in LGMD1A is always much more severe than
the distal weakness, whereas the opposite is observed in MPD2.
Feit et al. (1998) noted that Young and Harper (1980) had described a
similar autosomal dominant disorder with distal atrophy and vocal cord
paralysis (158580) that mapped to chromosome 2.
MAPPING
By use of combined genome screening and DNA pooling adapted to
fluorescent markers, Feit et al. (1998) mapped the gene for the
disorder, which they designated MPD2, to 5q, within a 12-cM interval
between markers D5S458 and D5S1972 in this large pedigree (maximum lod
score = 12.94 at a recombination fraction of 0.0 for D5S393).
In the family originally described by Feit et al. (1998), Senderek et
al. (2009) reduced the candidate interval to a 5.37-Mb region on
chromosome 5q31, between short tandem repeat (STR) markers sara2AC and
AC008667C.
NOMENCLATURE
Feit et al. (1998) adopted the gene symbol MPD2 following the precedent
of Laing et al. (1995), who had designated a form of distal myopathy
that maps to 14q as MPD1 (160500).
MOLECULAR GENETICS
In the family described by Feit et al. (1998) and in an unrelated
Bulgarian family with vocal cord and pharyngeal weakness with distal
myopathy, Senderek et al. (2009) identified the same heterozygous
missense mutation in the MATR3 gene (S85C; 164015.0001), which encodes a
component of the nuclear matrix.
*FIELD* RF
1. Feit, H.; Silbergleit, A.; Schneider, L. B.; Gutierrez, J. A.;
Fitoussi, R.-P.; Reyes, C.; Rouleau, G. A.; Brais, B.; Jackson, C.
E.; Beckmann, J. S.; Seboun, E.: Vocal cord and pharyngeal weakness
with autosomal dominant distal myopathy: clinical description and
gene localization to 5q31. Am. J. Hum. Genet. 63: 1732-1742, 1998.
2. Laing, N. G.; Laing, B. A.; Meredith, C.; Wilton, S. D.; Robbins,
P.; Honeyman, K.; Dorosz, S.; Kozman, H.; Mastaglia, F. L.; Kakulas,
B. A.: Autosomal dominant distal myopathy: linkage to chromosome
14. Am. J. Hum. Genet. 56: 422-427, 1995.
3. Senderek, J.; Garvey, S. M.; Krieger, M.; Guergueltcheva, V.; Urtizberea,
A.; Roos, A.; Elbracht, M.; Stendel, C.; Tournev, I.; Mihailova, V.;
Feit, H.; Tramonte, J.; and 11 others: Autosomal-dominant distal
myopathy associated with a recurrent missense mutation in the gene
encoding the nuclear matrix protein, matrin 3. Am. J. Hum. Genet. 84:
511-518, 2009.
4. Young, I. D.; Harper, P. S.: Hereditary distal spinal muscular
atrophy with vocal cord paralysis. J. Neurol. Neurosurg. Psychiat. 43:
413-418, 1980.
*FIELD* CS
INHERITANCE:
Autosomal dominant
RESPIRATORY:
[Nasopharynx];
Pharyngeal muscle weakness;
[Larynx];
Vocal cord weakness;
Bowing of the vocal cords;
Incomplete closure of the glottis;
Aspiration
ABDOMEN:
[Gastrointestinal];
Dysphagia
MUSCLE, SOFT TISSUE:
Distal muscle weakness;
Onset of weakness in hands and feet;
Shoulder weakness
NEUROLOGIC:
[Central nervous system];
Distal muscle weakness;
Shoulder weakness
VOICE:
Hypophonic, breathy voice;
Wet, gurgling, hoarse voice
LABORATORY ABNORMALITIES:
Elevated serum creatine phosphokinase (CPK);
Nerve conduction velocity (NCV) slowing;
EMG shows neuropathic or myopathic changes;
Muscle biopsy shows noninflammatory myopathy with rimmed vacuoles
and atrophic fibers
MISCELLANEOUS:
Age of onset 35-57 years
MOLECULAR BASIS:
Caused by mutation in the matrin-3 gene (MATR3, 164017.0001)
*FIELD* CD
Cassandra L. Kniffin: 10/25/2002
*FIELD* ED
joanna: 10/22/2013
alopez: 10/20/2009
ckniffin: 11/12/2002
*FIELD* CD
Victor A. McKusick: 6/27/2001
*FIELD* ED
wwang: 07/01/2011
alopez: 10/20/2009
mgross: 3/15/2005
alopez: 3/18/2004
ckniffin: 5/2/2003
ckniffin: 4/29/2003
ckniffin: 4/14/2003
carol: 2/21/2003
carol: 6/27/2001
*RECORD*
*FIELD* NO
606070
*FIELD* TI
#606070 MYOPATHY, DISTAL, 2; MPD2
;;VOCAL CORD AND PHARYNGEAL DYSFUNCTION WITH DISTAL MYOPATHY; VCPDM
read more*FIELD* TX
A number sign (#) is used with this entry because this form of distal
myopathy is caused by mutation in the matrin-3 gene on chromosome 5q31
(MATR3; 164015).
CLINICAL FEATURES
Feit et al. (1998) described a large American family segregating an
autosomal dominant distal myopathy, with multiple affected individuals
in whom vocal cord and pharyngeal weakness may accompany the distal
myopathy, without involvement of the ocular muscles. From a
histopathologic standpoint, the lesion observed in these individuals was
a noninflammatory myopathy with rimmed vacuoles probably fitting into
the spectrum of the inclusion-bodied myopathies. Overall, the myopathy
was mild or moderate. They stated that this 'form of distal myopathy has
not been previously recognized and is distinct from other myopathies
with pharyngeal or vocal weakness.' They referred to the clinical
disorder as VCPDM (vocal cord and pharyngeal dysfunction with distal
myopathy).
Senderek et al. (2009) expanded the family described by Feit et al.
(1998) with 2 additional sibs from an additional branch of the family.
They also described a multigenerational Bulgarian family with a typical
VCPDM phenotype.
DIAGNOSIS
- Differential Diagnosis
Feit et al. (1998) commented on the possible confusion of the MPD2
phenotype with the axonal (neuronal) form of Charcot-Marie-tooth
disease, CMT2 (see CMT2A1; 118210), if EMG results show a neurogenic
disorder with normal nerve conduction velocities. Muscle biopsy would be
required to distinguish between the 2 disorders. They also noted that
the diagnosis of MPD2 does not require voice and pharyngeal changes,
since some affected individuals in the kindred they studied did not show
these changes at the time of examination. Two myopathies had already
been mapped to 5q, the autosomal recessive limb-girdle muscular
dystrophy (LGMD) 2F (601287) and the autosomal dominant LGMD1A (159000).
LGMD2F was excluded because it was found to lie outside the linkage
interval of MPD2. LGMD1A was encompassed by the linkage interval of
MPD2, but the phenotypes of the 2 disorders were clinically quite
different. Proximal weakness in LGMD1A is always much more severe than
the distal weakness, whereas the opposite is observed in MPD2.
Feit et al. (1998) noted that Young and Harper (1980) had described a
similar autosomal dominant disorder with distal atrophy and vocal cord
paralysis (158580) that mapped to chromosome 2.
MAPPING
By use of combined genome screening and DNA pooling adapted to
fluorescent markers, Feit et al. (1998) mapped the gene for the
disorder, which they designated MPD2, to 5q, within a 12-cM interval
between markers D5S458 and D5S1972 in this large pedigree (maximum lod
score = 12.94 at a recombination fraction of 0.0 for D5S393).
In the family originally described by Feit et al. (1998), Senderek et
al. (2009) reduced the candidate interval to a 5.37-Mb region on
chromosome 5q31, between short tandem repeat (STR) markers sara2AC and
AC008667C.
NOMENCLATURE
Feit et al. (1998) adopted the gene symbol MPD2 following the precedent
of Laing et al. (1995), who had designated a form of distal myopathy
that maps to 14q as MPD1 (160500).
MOLECULAR GENETICS
In the family described by Feit et al. (1998) and in an unrelated
Bulgarian family with vocal cord and pharyngeal weakness with distal
myopathy, Senderek et al. (2009) identified the same heterozygous
missense mutation in the MATR3 gene (S85C; 164015.0001), which encodes a
component of the nuclear matrix.
*FIELD* RF
1. Feit, H.; Silbergleit, A.; Schneider, L. B.; Gutierrez, J. A.;
Fitoussi, R.-P.; Reyes, C.; Rouleau, G. A.; Brais, B.; Jackson, C.
E.; Beckmann, J. S.; Seboun, E.: Vocal cord and pharyngeal weakness
with autosomal dominant distal myopathy: clinical description and
gene localization to 5q31. Am. J. Hum. Genet. 63: 1732-1742, 1998.
2. Laing, N. G.; Laing, B. A.; Meredith, C.; Wilton, S. D.; Robbins,
P.; Honeyman, K.; Dorosz, S.; Kozman, H.; Mastaglia, F. L.; Kakulas,
B. A.: Autosomal dominant distal myopathy: linkage to chromosome
14. Am. J. Hum. Genet. 56: 422-427, 1995.
3. Senderek, J.; Garvey, S. M.; Krieger, M.; Guergueltcheva, V.; Urtizberea,
A.; Roos, A.; Elbracht, M.; Stendel, C.; Tournev, I.; Mihailova, V.;
Feit, H.; Tramonte, J.; and 11 others: Autosomal-dominant distal
myopathy associated with a recurrent missense mutation in the gene
encoding the nuclear matrix protein, matrin 3. Am. J. Hum. Genet. 84:
511-518, 2009.
4. Young, I. D.; Harper, P. S.: Hereditary distal spinal muscular
atrophy with vocal cord paralysis. J. Neurol. Neurosurg. Psychiat. 43:
413-418, 1980.
*FIELD* CS
INHERITANCE:
Autosomal dominant
RESPIRATORY:
[Nasopharynx];
Pharyngeal muscle weakness;
[Larynx];
Vocal cord weakness;
Bowing of the vocal cords;
Incomplete closure of the glottis;
Aspiration
ABDOMEN:
[Gastrointestinal];
Dysphagia
MUSCLE, SOFT TISSUE:
Distal muscle weakness;
Onset of weakness in hands and feet;
Shoulder weakness
NEUROLOGIC:
[Central nervous system];
Distal muscle weakness;
Shoulder weakness
VOICE:
Hypophonic, breathy voice;
Wet, gurgling, hoarse voice
LABORATORY ABNORMALITIES:
Elevated serum creatine phosphokinase (CPK);
Nerve conduction velocity (NCV) slowing;
EMG shows neuropathic or myopathic changes;
Muscle biopsy shows noninflammatory myopathy with rimmed vacuoles
and atrophic fibers
MISCELLANEOUS:
Age of onset 35-57 years
MOLECULAR BASIS:
Caused by mutation in the matrin-3 gene (MATR3, 164017.0001)
*FIELD* CD
Cassandra L. Kniffin: 10/25/2002
*FIELD* ED
joanna: 10/22/2013
alopez: 10/20/2009
ckniffin: 11/12/2002
*FIELD* CD
Victor A. McKusick: 6/27/2001
*FIELD* ED
wwang: 07/01/2011
alopez: 10/20/2009
mgross: 3/15/2005
alopez: 3/18/2004
ckniffin: 5/2/2003
ckniffin: 4/29/2003
ckniffin: 4/14/2003
carol: 2/21/2003
carol: 6/27/2001