FHL1_HUMAN
ID FHL1_HUMAN Reviewed; 323 AA.
AC Q13642; B7Z5T4; B7Z793; O95212; Q13230; Q13645; Q5JXI7; Q5M7Y6; Q6IB30;
AC Q9NZ40; Q9UKZ8; Q9Y630;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 211.
DE RecName: Full=Four and a half LIM domains protein 1;
DE Short=FHL-1;
DE AltName: Full=Skeletal muscle LIM-protein 1;
DE Short=SLIM;
DE Short=SLIM-1;
GN Name=FHL1; Synonyms=SLIM1;
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).
RC TISSUE=Skeletal muscle;
RX PubMed=8753811; DOI=10.1006/bbrc.1996.1222;
RA Morgan M.J., Madgwick A.J.A.;
RT "Slim defines a novel family of LIM-proteins expressed in skeletal
RT muscle.";
RL Biochem. Biophys. Res. Commun. 225:632-638(1996).
RN [2]
RP SEQUENCE REVISION.
RA Morgan M.J.;
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=9714789; DOI=10.1016/s0378-1119(98)00302-3;
RA Lee S.M.Y., Tsui S.K.W., Chan K.K., Garcia-Barcelo M., Waye M.M.Y.,
RA Fung K.P., Liew C.C., Lee C.Y.;
RT "Chromosomal mapping, tissue distribution and cDNA sequence of four-and-a-
RT half LIM domain protein 1 (FHL1).";
RL Gene 216:163-170(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RX PubMed=10352231; DOI=10.1016/s0378-1119(99)00125-0;
RA Greene W.K., Baker E., Rabbitts T.H., Kees U.R.;
RT "Genomic structure, tissue expression and chromosomal location of the LIM-
RT only gene, SLIM1.";
RL Gene 232:203-207(1999).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10524257; DOI=10.1016/s0378-1119(99)00251-6;
RA Lee S.M.Y., Li H.-Y., Ng E.K.O., Or S.M.W., Chan K.K., Kotaka M.,
RA Chim S.S.C., Tsui S.K.W., Waye M.M.Y., Fung K.-P., Lee C.-Y.;
RT "Characterization of a brain-specific nuclear LIM domain protein (FHL1B)
RT which is an alternatively spliced variant of FHL1.";
RL Gene 237:253-263(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Bone marrow;
RX PubMed=10480922; DOI=10.1074/jbc.274.38.27083;
RA Brown S., McGrath M.J., Ooms L.M., Gurung R., Maimone M.M., Mitchell C.A.;
RT "Characterization of two isoforms of the skeletal muscle LIM protein 1,
RT SLIM1. Localization of SLIM1 at focal adhesions and the isoform slimmer in
RT the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles
RT in the cytoskeleton and in nuclear-cytoplasmic communication.";
RL J. Biol. Chem. 274:27083-27091(1999).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=11400158; DOI=10.1002/jcb.1110;
RA Ng E.K.O., Lee S.M.Y., Li H.-Y., Ngai S.-M., Tsui S.K.W., Waye M.M.Y.,
RA Lee C.-Y., Fung K.-P.;
RT "Characterization of tissue-specific LIM domain protein (FHL1C) which is an
RT alternatively spliced isoform of a human LIM-only protein (FHL1).";
RL J. Cell. Biochem. 82:1-10(2001).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 4 AND 5).
RC TISSUE=Esophagus, Thalamus, and Tongue;
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [11]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [12]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung, and Muscle;
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 [13]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 106-255 (ISOFORM 1), AND DEVELOPMENTAL STAGE.
RC TISSUE=Muscle;
RX PubMed=7626119; DOI=10.1006/bbrc.1995.2045;
RA Morgan M.J., Madgwick A.J.A., Charleston B., Pell J.M., Loughna P.T.;
RT "The developmental regulation of a novel muscle LIM-protein.";
RL Biochem. Biophys. Res. Commun. 212:840-846(1995).
RN [14]
RP PROTEIN SEQUENCE OF 2-11.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 [16]
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 [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-86, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP INVOLVEMENT IN FCMSU.
RX PubMed=26933038; DOI=10.1161/circgenetics.115.001193;
RA Xue Y., Schoser B., Rao A.R., Quadrelli R., Vaglio A., Rupp V.,
RA Beichler C., Nelson S.F., Schapacher-Tilp G., Windpassinger C.,
RA Wilcox W.R.;
RT "Exome sequencing identified a splice site mutation in FHL1 that causes
RT Uruguay Syndrome, an X-linked disorder with skeletal muscle hypertrophy and
RT premature cardiac death.";
RL Circ. Cardiovasc. Genet. 9:130-135(2016).
RN [19]
RP STRUCTURE BY NMR OF 40-280 IN COMPLEXES WITH ZINC IONS.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of LIM domains from human four and a half LIM domains
RT 1.";
RL Submitted (SEP-2007) to the PDB data bank.
RN [20]
RP VARIANTS XMPMA ILE-128 INS AND TRP-224.
RX PubMed=18179888; DOI=10.1016/j.ajhg.2007.09.004;
RA Windpassinger C., Schoser B., Straub V., Hochmeister S., Noor A.,
RA Lohberger B., Farra N., Petek E., Schwarzbraun T., Ofner L., Loescher W.N.,
RA Wagner K., Lochmueller H., Vincent J.B., Quasthoff S.;
RT "An X-linked myopathy with postural muscle atrophy and generalized
RT hypertrophy, termed XMPMA, is caused by mutations in FHL1.";
RL Am. J. Hum. Genet. 82:88-99(2008).
RN [21]
RP VARIANT SPM SER-122.
RX PubMed=18179901; DOI=10.1016/j.ajhg.2007.09.013;
RA Quinzii C.M., Vu T.H., Min K.C., Tanji K., Barral S., Grewal R.P.,
RA Kattah A., Camano P., Otaegui D., Kunimatsu T., Blake D.M.,
RA Wilhelmsen K.C., Rowland L.P., Hays A.P., Bonilla E., Hirano M.;
RT "X-linked dominant scapuloperoneal myopathy is due to a mutation in the
RT gene encoding four-and-a-half-LIM protein 1.";
RL Am. J. Hum. Genet. 82:208-213(2008).
RN [22]
RP INVOLVEMENT IN RBMX1A, INVOLVEMENT IN RBMX1B, VARIANTS RBMX1A TYR-123 AND
RP PHE-132, AND VARIANTS RBMX1B TYR-153 AND ARG-153.
RX PubMed=18274675; DOI=10.1172/jci34450;
RA Schessl J., Zou Y., McGrath M.J., Cowling B.S., Maiti B., Chin S.S.,
RA Sewry C., Battini R., Hu Y., Cottle D.L., Rosenblatt M., Spruce L.,
RA Ganguly A., Kirschner J., Judkins A.R., Golden J.A., Goebel H.-H.,
RA Muntoni F., Flanigan K.M., Mitchell C.A., Boennemann C.G.;
RT "Proteomic identification of FHL1 as the protein mutated in human reducing
RT body myopathy.";
RL J. Clin. Invest. 118:904-912(2008).
RN [23]
RP VARIANTS EDMD6 ARG-209 AND TYR-276, AND CHARACTERIZATION OF VARIANT EDMD6
RP TYR-276.
RX PubMed=19716112; DOI=10.1016/j.ajhg.2009.07.015;
RA Gueneau L., Bertrand A.T., Jais J.P., Salih M.A., Stojkovic T., Wehnert M.,
RA Hoeltzenbein M., Spuler S., Saitoh S., Verschueren A., Tranchant C.,
RA Beuvin M., Lacene E., Romero N.B., Heath S., Zelenika D., Voit T.,
RA Eymard B., Ben Yaou R., Bonne G.;
RT "Mutations of the FHL1 gene cause Emery-Dreifuss muscular dystrophy.";
RL Am. J. Hum. Genet. 85:338-353(2009).
RN [24]
RP VARIANTS RBMX1A GLN-123; LEU-123; TYR-123 AND PHE-132, AND VARIANTS RBMX1B
RP ARG-153 AND TYR-153.
RX PubMed=19181672; DOI=10.1093/brain/awn325;
RA Schessl J., Taratuto A.L., Sewry C., Battini R., Chin S.S., Maiti B.,
RA Dubrovsky A.L., Erro M.G., Espada G., Robertella M., Saccoliti M.,
RA Olmos P., Bridges L.R., Standring P., Hu Y., Zou Y., Swoboda K.J.,
RA Scavina M., Goebel H.H., Mitchell C.A., Flanigan K.M., Muntoni F.,
RA Boennemann C.G.;
RT "Clinical, histological and genetic characterization of reducing body
RT myopathy caused by mutations in FHL1.";
RL Brain 132:452-464(2009).
RN [25]
RP INTERACTION WITH CHIKUNGUNYA VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION).
RX PubMed=31554973; DOI=10.1038/s41586-019-1578-4;
RA Meertens L., Hafirassou M.L., Couderc T., Bonnet-Madin L., Kril V.,
RA Kuemmerer B.M., Labeau A., Brugier A., Simon-Loriere E.,
RA Burlaud-Gaillard J., Doyen C., Pezzi L., Goupil T., Rafasse S.,
RA Vidalain P.O., Bertrand-Legout A., Gueneau L., Juntas-Morales R.,
RA Ben Yaou R., Bonne G., de Lamballerie X., Benkirane M., Roingeard P.,
RA Delaugerre C., Lecuit M., Amara A.;
RT "FHL1 is a major host factor for chikungunya virus infection.";
RL Nature 574:259-263(2019).
RN [26]
RP INTERACTION WITH CHIKUNGUNYA VIRUS NON-STRUCTURAL PROTEIN 3 (MICROBIAL
RP INFECTION).
RX PubMed=33055253; DOI=10.1128/jvi.01672-20;
RA Lukash T., Agback T., Dominguez F., Shiliaev N., Meshram C., Frolova E.I.,
RA Agback P., Frolov I.;
RT "Structural and Functional Characterization of Host FHL1 Protein
RT Interaction with Hypervariable Domain of Chikungunya Virus nsP3 Protein.";
RL J. Virol. 95:0-0(2020).
RN [27]
RP VARIANTS RBMX1A PHE-101 AND TYR-150, AND VARIANTS RBMX1B 102-LYS--CYS-104
RP DEL AND ARG-104.
RX PubMed=19171836; DOI=10.1212/01.wnl.0000341311.84347.a0;
RA Shalaby S., Hayashi Y.K., Nonaka I., Noguchi S., Nishino I.;
RT "Novel FHL1 mutations in fatal and benign reducing body myopathy.";
RL Neurology 72:375-376(2009).
RN [28]
RP VARIANTS XMPMA TRP-224 AND MET-280, VARIANT XMPMA TYR-246 (ISOFORM 1), AND
RP VARIANT ASN-275 (ISOFORM 1).
RX PubMed=19687455; DOI=10.1212/wnl.0b013e3181b2a4b3;
RA Schoser B., Goebel H.H., Janisch I., Quasthoff S., Rother J., Bergmann M.,
RA Mueller-Felber W., Windpassinger C.;
RT "Consequences of mutations within the C terminus of the FHL1 gene.";
RL Neurology 73:543-551(2009).
RN [29]
RP VARIANT EDMD6 ARG-209.
RX PubMed=20186852; DOI=10.1002/ana.21839;
RA Knoblauch H., Geier C., Adams S., Budde B., Rudolph A., Zacharias U.,
RA Schulz-Menger J., Spuler A., Yaou R.B., Nuernberg P., Voit T., Bonne G.,
RA Spuler S.;
RT "Contractures and hypertrophic cardiomyopathy in a novel FHL1 mutation.";
RL Ann. Neurol. 67:136-140(2010).
RN [30]
RP VARIANT RBMX1B SER-150.
RX PubMed=23169582; DOI=10.1002/mus.23500;
RA Schreckenbach T., Henn W., Kress W., Roos A., Maschke M., Feiden W.,
RA Dillmann U., Schulz J.B., Weis J., Claeys K.G.;
RT "Novel FHL1 mutation in a family with reducing body myopathy.";
RL Muscle Nerve 47:127-134(2013).
RN [31]
RP VARIANT SPM PRO-154.
RX PubMed=27234031; DOI=10.1111/cge.12810;
RA Fattahi Z., Kalhor Z., Fadaee M., Vazehan R., Parsimehr E., Abolhassani A.,
RA Beheshtian M., Zamani G., Nafissi S., Nilipour Y., Akbari M.R., Kahrizi K.,
RA Kariminejad A., Najmabadi H.;
RT "Improved diagnostic yield of neuromuscular disorders applying clinical
RT exome sequencing in patients arising from a consanguineous population.";
RL Clin. Genet. 91:386-402(2017).
CC -!- FUNCTION: May have an involvement in muscle development or hypertrophy.
CC -!- SUBUNIT: (Microbial infection) Interacts (via LIM domain 1) with
CC Chikungunya virus non-structural protein 3 (via C-terminus); this
CC interaction is required for viral RNA replication.
CC {ECO:0000269|PubMed:31554973, ECO:0000269|PubMed:33055253}.
CC -!- INTERACTION:
CC Q13642; P48552: NRIP1; NbExp=6; IntAct=EBI-912547, EBI-746484;
CC Q13642; P04156: PRNP; NbExp=3; IntAct=EBI-912547, EBI-977302;
CC Q13642-2; P62714: PPP2CB; NbExp=3; IntAct=EBI-8477209, EBI-1044367;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. Cytoplasm, cytosol.
CC Note=Predominantly nuclear in myoblasts but is cytosolic in
CC differentiated myotubes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=2; Synonyms=FHL1B, SLIMMER;
CC IsoId=Q13642-2; Sequence=Displayed;
CC Name=1; Synonyms=FHL1, FHL1A, SLIM1;
CC IsoId=Q13642-1; Sequence=VSP_010694;
CC Name=3; Synonyms=FHL1C;
CC IsoId=Q13642-3; Sequence=VSP_010693;
CC Name=4;
CC IsoId=Q13642-4; Sequence=VSP_043162, VSP_010694;
CC Name=5;
CC IsoId=Q13642-5; Sequence=VSP_043404, VSP_010694;
CC -!- TISSUE SPECIFICITY: Isoform 1 is highly expressed in skeletal muscle
CC and to a lesser extent in heart, placenta, ovary, prostate, testis,
CC small intestine, colon and spleen. Expression is barely detectable in
CC brain, lung, liver, kidney, pancreas, thymus and peripheral blood
CC leukocytes. Isoform 2 is expressed in brain, skeletal muscle and to a
CC lesser extent in heart, colon, prostate and small intestine. Isoform 3
CC is expressed in testis, heart and skeletal muscle.
CC {ECO:0000269|PubMed:10352231, ECO:0000269|PubMed:10480922,
CC ECO:0000269|PubMed:10524257, ECO:0000269|PubMed:11400158,
CC ECO:0000269|PubMed:9714789}.
CC -!- DEVELOPMENTAL STAGE: Elevated levels during postnatal muscle growth.
CC {ECO:0000269|PubMed:7626119}.
CC -!- DISEASE: Emery-Dreifuss muscular dystrophy 6, X-linked (EDMD6)
CC [MIM:300696]: A form of Emery-Dreifuss muscular dystrophy, a
CC degenerative myopathy characterized by weakness and atrophy of muscle
CC without involvement of the nervous system, early contractures of the
CC elbows, Achilles tendons and spine, and cardiomyopathy associated with
CC cardiac conduction defects. {ECO:0000269|PubMed:19716112,
CC ECO:0000269|PubMed:20186852}. Note=The disease is caused by variants
CC affecting distinct genetic loci, including the gene represented in this
CC entry.
CC -!- DISEASE: Scapuloperoneal myopathy, X-linked dominant (SPM)
CC [MIM:300695]: A disease characterized by progressive muscle weakness
CC and wasting, upper and lower limbs weakness, foot drop, scapular
CC winging, and myopathic changes on muscle biopsy. Most affected
CC individuals become wheelchair-bound. {ECO:0000269|PubMed:18179901,
CC ECO:0000269|PubMed:27234031}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Myopathy, X-linked, with postural muscle atrophy (XMPMA)
CC [MIM:300696]: A progressive muscular dystrophy with onset in adulthood.
CC Affected individuals develop a proximal myopathy characterized by
CC specific atrophy of postural muscles, limited neck flexion, bent spine,
CC contractures of the Achilles tendon, respiratory problems, and
CC cardiomyopathy. Patients may show muscle hypertrophy in the early
CC stages of the disorder. {ECO:0000269|PubMed:18179888,
CC ECO:0000269|PubMed:19687455}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Reducing body myopathy, X-linked 1A, severe, with infantile or
CC early childhood onset (RBMX1A) [MIM:300717]: A rare myopathy clinically
CC characterized by rapidly progressive muscular weakness, and
CC pathologically by the presence of intracytoplasmic inclusion bodies
CC strongly stained by menadione-linked alpha-glycerophosphate
CC dehydrogenase in the absence of substrate, alpha-glycerophosphate. The
CC term 'reducing body' refers to the reducing activity of the inclusions
CC to nitroblue tetrazolium in the absence of substrate. This condition is
CC also commonly associated with rimmed vacuoles and cytoplasmic bodies.
CC Death in childhood is frequent in the severe form of the disease, due
CC to respiratory failure. {ECO:0000269|PubMed:18274675,
CC ECO:0000269|PubMed:19171836, ECO:0000269|PubMed:19181672}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Reducing body myopathy, X-linked 1B, with late childhood or
CC adult onset (RBMX1B) [MIM:300718]: A rare myopathy clinically
CC characterized by rapidly progressive muscular weakness, and
CC pathologically by the presence of intracytoplasmic inclusion bodies
CC strongly stained by menadione-linked alpha-glycerophosphate
CC dehydrogenase in the absence of substrate, alpha-glycerophosphate. The
CC term 'reducing body' refers to the reducing activity of the inclusions
CC to nitroblue tetrazolium in the absence of substrate. This condition is
CC also commonly associated with rimmed vacuoles and cytoplasmic bodies.
CC {ECO:0000269|PubMed:18274675, ECO:0000269|PubMed:19171836,
CC ECO:0000269|PubMed:19181672, ECO:0000269|PubMed:23169582}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Uruguay faciocardiomusculoskeletal syndrome (FCMSU)
CC [MIM:300280]: An X-linked recessive syndrome characterized by
CC brachyturricephaly, pugilistic coarse facies, a muffled voice,
CC cardiomyopathy, muscular hypertrophy, broad hands, wide feet with
CC progressive pes cavus deformities, dislocation of toes, variable
CC congenital hip dislocation, and scoliosis.
CC {ECO:0000269|PubMed:26933038}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH88369.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U60115; AAC52021.1; -; mRNA.
DR EMBL; U29538; AAC35421.1; -; mRNA.
DR EMBL; AF110763; AAD21579.1; -; Genomic_DNA.
DR EMBL; AF098518; AAC72390.1; -; mRNA.
DR EMBL; AF063002; AAC72886.1; -; mRNA.
DR EMBL; AF220153; AAF32351.1; -; mRNA.
DR EMBL; AK122708; BAG53680.1; -; mRNA.
DR EMBL; AK289411; BAF82100.1; -; mRNA.
DR EMBL; AK299381; BAH13020.1; -; mRNA.
DR EMBL; AK301642; BAH13529.1; -; mRNA.
DR EMBL; CR456974; CAG33255.1; -; mRNA.
DR EMBL; AL078638; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471150; EAW88476.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88478.1; -; Genomic_DNA.
DR EMBL; CH471150; EAW88479.1; -; Genomic_DNA.
DR EMBL; BC010998; AAH10998.1; -; mRNA.
DR EMBL; BC088369; AAH88369.1; ALT_INIT; mRNA.
DR EMBL; U60118; AAC50795.1; -; mRNA.
DR CCDS; CCDS14655.1; -. [Q13642-1]
DR CCDS; CCDS55505.1; -. [Q13642-4]
DR CCDS; CCDS55506.1; -. [Q13642-5]
DR CCDS; CCDS55507.1; -. [Q13642-2]
DR CCDS; CCDS76036.1; -. [Q13642-3]
DR PIR; G01884; G01884.
DR PIR; JC4893; G02741.
DR RefSeq; NP_001153171.1; NM_001159699.1. [Q13642-5]
DR RefSeq; NP_001153172.1; NM_001159700.1. [Q13642-1]
DR RefSeq; NP_001153173.1; NM_001159701.1. [Q13642-4]
DR RefSeq; NP_001153174.1; NM_001159702.2. [Q13642-2]
DR RefSeq; NP_001153175.1; NM_001159703.1. [Q13642-3]
DR RefSeq; NP_001153176.1; NM_001159704.1. [Q13642-1]
DR RefSeq; NP_001161291.1; NM_001167819.1. [Q13642-1]
DR RefSeq; NP_001440.2; NM_001449.4. [Q13642-1]
DR RefSeq; XP_006724807.1; XM_006724744.2.
DR RefSeq; XP_006724808.1; XM_006724745.3.
DR RefSeq; XP_006724809.1; XM_006724746.2. [Q13642-2]
DR RefSeq; XP_006724810.1; XM_006724747.2.
DR RefSeq; XP_016884846.1; XM_017029357.1.
DR PDB; 1X63; NMR; -; A=91-159.
DR PDB; 2CUP; NMR; -; A=40-127.
DR PDB; 2CUR; NMR; -; A=162-217.
DR PDB; 2EGQ; NMR; -; A=211-280.
DR PDBsum; 1X63; -.
DR PDBsum; 2CUP; -.
DR PDBsum; 2CUR; -.
DR PDBsum; 2EGQ; -.
DR AlphaFoldDB; Q13642; -.
DR SMR; Q13642; -.
DR BioGRID; 108564; 99.
DR CORUM; Q13642; -.
DR IntAct; Q13642; 41.
DR MINT; Q13642; -.
DR STRING; 9606.ENSP00000377710; -.
DR iPTMnet; Q13642; -.
DR PhosphoSitePlus; Q13642; -.
DR SwissPalm; Q13642; -.
DR BioMuta; FHL1; -.
DR DMDM; 59800384; -.
DR EPD; Q13642; -.
DR jPOST; Q13642; -.
DR MassIVE; Q13642; -.
DR MaxQB; Q13642; -.
DR PaxDb; Q13642; -.
DR PeptideAtlas; Q13642; -.
DR PRIDE; Q13642; -.
DR ProteomicsDB; 59642; -. [Q13642-2]
DR ProteomicsDB; 59643; -. [Q13642-1]
DR ProteomicsDB; 59644; -. [Q13642-3]
DR ProteomicsDB; 59645; -. [Q13642-4]
DR ProteomicsDB; 59646; -. [Q13642-5]
DR TopDownProteomics; Q13642-1; -. [Q13642-1]
DR ABCD; Q13642; 1 sequenced antibody.
DR Antibodypedia; 16643; 503 antibodies from 37 providers.
DR CPTC; Q13642; 1 antibody.
DR DNASU; 2273; -.
DR Ensembl; ENST00000370683.6; ENSP00000359717.1; ENSG00000022267.19. [Q13642-5]
DR Ensembl; ENST00000394153.6; ENSP00000377709.2; ENSG00000022267.19. [Q13642-1]
DR Ensembl; ENST00000394155.8; ENSP00000377710.2; ENSG00000022267.19. [Q13642-2]
DR Ensembl; ENST00000535737.5; ENSP00000444815.1; ENSG00000022267.19. [Q13642-1]
DR Ensembl; ENST00000539015.5; ENSP00000437673.1; ENSG00000022267.19. [Q13642-4]
DR Ensembl; ENST00000543669.5; ENSP00000443333.1; ENSG00000022267.19. [Q13642-1]
DR Ensembl; ENST00000618438.4; ENSP00000477609.1; ENSG00000022267.19. [Q13642-3]
DR Ensembl; ENST00000628568.1; ENSP00000486782.1; ENSG00000022267.19. [Q13642-1]
DR Ensembl; ENST00000628919.3; ENSP00000487147.2; ENSG00000022267.19. [Q13642-1]
DR Ensembl; ENST00000629039.2; ENSP00000486439.1; ENSG00000022267.19. [Q13642-1]
DR Ensembl; ENST00000630084.2; ENSP00000485897.1; ENSG00000022267.19. [Q13642-1]
DR Ensembl; ENST00000651089.1; ENSP00000498684.1; ENSG00000022267.19. [Q13642-2]
DR Ensembl; ENST00000651929.2; ENSP00000499016.1; ENSG00000022267.19. [Q13642-1]
DR GeneID; 2273; -.
DR KEGG; hsa:2273; -.
DR MANE-Select; ENST00000370683.6; ENSP00000359717.1; NM_001159699.2; NP_001153171.1. [Q13642-5]
DR UCSC; uc004ezl.3; human. [Q13642-2]
DR CTD; 2273; -.
DR DisGeNET; 2273; -.
DR GeneCards; FHL1; -.
DR GeneReviews; FHL1; -.
DR HGNC; HGNC:3702; FHL1.
DR HPA; ENSG00000022267; Group enriched (skeletal muscle, tongue).
DR MalaCards; FHL1; -.
DR MIM; 300163; gene.
DR MIM; 300280; phenotype.
DR MIM; 300695; phenotype.
DR MIM; 300696; phenotype.
DR MIM; 300717; phenotype.
DR MIM; 300718; phenotype.
DR neXtProt; NX_Q13642; -.
DR OpenTargets; ENSG00000022267; -.
DR Orphanet; 155; NON RARE IN EUROPE: Familial isolated hypertrophic cardiomyopathy.
DR Orphanet; 97239; Reducing body myopathy.
DR Orphanet; 98863; X-linked Emery-Dreifuss muscular dystrophy.
DR Orphanet; 178461; X-linked myopathy with postural muscle atrophy.
DR Orphanet; 431272; X-linked scapuloperoneal muscular dystrophy.
DR PharmGKB; PA28141; -.
DR VEuPathDB; HostDB:ENSG00000022267; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000154833; -.
DR HOGENOM; CLU_860421_0_0_1; -.
DR InParanoid; Q13642; -.
DR OMA; EKDGHHC; -.
DR OrthoDB; 642235at2759; -.
DR PhylomeDB; Q13642; -.
DR TreeFam; TF318571; -.
DR PathwayCommons; Q13642; -.
DR SignaLink; Q13642; -.
DR SIGNOR; Q13642; -.
DR BioGRID-ORCS; 2273; 13 hits in 703 CRISPR screens.
DR ChiTaRS; FHL1; human.
DR EvolutionaryTrace; Q13642; -.
DR GeneWiki; FHL1; -.
DR GenomeRNAi; 2273; -.
DR Pharos; Q13642; Tbio.
DR PRO; PR:Q13642; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q13642; protein.
DR Bgee; ENSG00000022267; Expressed in skeletal muscle tissue of rectus abdominis and 210 other tissues.
DR ExpressionAtlas; Q13642; baseline and differential.
DR Genevisible; Q13642; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0044325; F:transmembrane transporter binding; IPI:BHF-UCL.
DR GO; GO:0009887; P:animal organ morphogenesis; NAS:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0007517; P:muscle organ development; NAS:UniProtKB.
DR GO; GO:0030308; P:negative regulation of cell growth; IDA:UniProtKB.
DR GO; GO:2000134; P:negative regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; IDA:UniProtKB.
DR GO; GO:0043268; P:positive regulation of potassium ion transport; IDA:BHF-UCL.
DR GO; GO:0003254; P:regulation of membrane depolarization; IDA:BHF-UCL.
DR GO; GO:1901016; P:regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
DR InterPro; IPR042997; Fhl1.
DR InterPro; IPR001781; Znf_LIM.
DR PANTHER; PTHR47029; PTHR47029; 1.
DR Pfam; PF00412; LIM; 3.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 3.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cytoplasm;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Disease variant; Emery-Dreifuss muscular dystrophy; Isopeptide bond;
KW LIM domain; Metal-binding; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation; Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801"
FT CHAIN 2..323
FT /note="Four and a half LIM domains protein 1"
FT /id="PRO_0000075735"
FT DOMAIN 40..92
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 101..153
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 162..212
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT ZN_FING 7..31
FT /note="C4-type"
FT /evidence="ECO:0000255"
FT MOD_RES 4
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P97447"
FT CROSSLNK 86
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
FT VAR_SEQ 1
FT /note="M -> MTFYVASLALELIWMLSSPAGPSSYKVGTM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043162"
FT VAR_SEQ 1
FT /note="M -> MASHRHSGPSSYKVGTM (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043404"
FT VAR_SEQ 168..296
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:11400158"
FT /id="VSP_010693"
FT VAR_SEQ 231..323
FT /note="KRTVSRVSHPVSKARKPPVCHGKRLPLTLFPSANLRGRHPGGERTCPSWVVV
FT LYRKNRSLAAPRGPGLVKAPVWWPMKDNPGTTTASTAKNAP -> FGKGSSVVAYEGQS
FT WHDYCFHCKKCSVNLANKRFVFHQEQVYCPDCAKKL (in isoform 1, isoform
FT 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7626119,
FT ECO:0000303|PubMed:8753811, ECO:0000303|PubMed:9714789,
FT ECO:0000303|Ref.9"
FT /id="VSP_010694"
FT VARIANT 101
FT /note="C -> F (in RBMX1A; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19171836"
FT /id="VAR_075350"
FT VARIANT 102..104
FT /note="Missing (in RBMX1B; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19171836"
FT /id="VAR_075351"
FT VARIANT 104
FT /note="C -> R (in RBMX1B; unknown pathological
FT significance; dbSNP:rs122459147)"
FT /evidence="ECO:0000269|PubMed:19171836"
FT /id="VAR_075352"
FT VARIANT 122
FT /note="W -> S (in SPM; dbSNP:rs122458140)"
FT /evidence="ECO:0000269|PubMed:18179901"
FT /id="VAR_042603"
FT VARIANT 123
FT /note="H -> L (in RBMX1A; dbSNP:rs267606812)"
FT /evidence="ECO:0000269|PubMed:19181672"
FT /id="VAR_075353"
FT VARIANT 123
FT /note="H -> Q (in RBMX1A; dbSNP:rs267606813)"
FT /evidence="ECO:0000269|PubMed:19181672"
FT /id="VAR_075354"
FT VARIANT 123
FT /note="H -> Y (in RBMX1A; the mutant protein initiates
FT aggregation of the FHL1 protein causing reducing bodies
FT formation; dominant-negative effect; dbSNP:rs122458142)"
FT /evidence="ECO:0000269|PubMed:18274675,
FT ECO:0000269|PubMed:19181672"
FT /id="VAR_045999"
FT VARIANT 128
FT /note="T -> TI (in XMPMA)"
FT /evidence="ECO:0000269|PubMed:18179888"
FT /id="VAR_042604"
FT VARIANT 132
FT /note="C -> F (in RBMX1A; the mutant protein initiates
FT aggregation of the FHL1 protein causing reducing bodies
FT formation; dominant-negative effect; dbSNP:rs122458143)"
FT /evidence="ECO:0000269|PubMed:18274675,
FT ECO:0000269|PubMed:19181672"
FT /id="VAR_046000"
FT VARIANT 150
FT /note="C -> S (in RBMX1B)"
FT /evidence="ECO:0000269|PubMed:23169582"
FT /id="VAR_075355"
FT VARIANT 150
FT /note="C -> Y (in RBMX1A; unknown pathological
FT significance; dbSNP:rs122459146)"
FT /evidence="ECO:0000269|PubMed:19171836"
FT /id="VAR_075356"
FT VARIANT 153
FT /note="C -> R (in RBMX1B; dbSNP:rs122458144)"
FT /evidence="ECO:0000269|PubMed:18274675,
FT ECO:0000269|PubMed:19181672"
FT /id="VAR_046001"
FT VARIANT 153
FT /note="C -> Y (in RBMX1B; dbSNP:rs122458145)"
FT /evidence="ECO:0000269|PubMed:18274675,
FT ECO:0000269|PubMed:19181672"
FT /id="VAR_046002"
FT VARIANT 154
FT /note="H -> P (in SPM)"
FT /evidence="ECO:0000269|PubMed:27234031"
FT /id="VAR_076566"
FT VARIANT 209
FT /note="C -> R (in EDMD6; dbSNP:rs122459149)"
FT /evidence="ECO:0000269|PubMed:19716112,
FT ECO:0000269|PubMed:20186852"
FT /id="VAR_075357"
FT VARIANT 224
FT /note="C -> W (in XMPMA; dbSNP:rs122458141)"
FT /evidence="ECO:0000269|PubMed:18179888,
FT ECO:0000269|PubMed:19687455"
FT /id="VAR_042605"
FT VARIANT 276
FT /note="C -> Y (in EDMD6; drastically reduced protein levels
FT in muscle)"
FT /evidence="ECO:0000269|PubMed:19716112"
FT /id="VAR_075358"
FT VARIANT 280
FT /note="V -> M (in XMPMA; dbSNP:rs267606811)"
FT /evidence="ECO:0000269|PubMed:19687455"
FT /id="VAR_075359"
FT CONFLICT 73
FT /note="H -> Q (in Ref. 1; AAC52021)"
FT /evidence="ECO:0000305"
FT CONFLICT 81..91
FT /note="VAKDNKILCNK -> CGQGQQRSCAQ (in Ref. 4; AAD21579)"
FT /evidence="ECO:0000305"
FT CONFLICT 98
FT /note="S -> F (in Ref. 1 and 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="F -> L (in Ref. 1 and 13)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="H -> R (in Ref. 5; AAC72390)"
FT /evidence="ECO:0000305"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:2CUP"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:2CUP"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2CUP"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:2CUP"
FT TURN 63..65
FT /evidence="ECO:0007829|PDB:2CUP"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:2CUP"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2CUP"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2CUP"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:2CUP"
FT STRAND 102..104
FT /evidence="ECO:0007829|PDB:1X63"
FT STRAND 110..112
FT /evidence="ECO:0007829|PDB:1X63"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1X63"
FT STRAND 121..123
FT /evidence="ECO:0007829|PDB:1X63"
FT TURN 124..126
FT /evidence="ECO:0007829|PDB:1X63"
FT STRAND 130..132
FT /evidence="ECO:0007829|PDB:1X63"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:1X63"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1X63"
FT HELIX 151..157
FT /evidence="ECO:0007829|PDB:1X63"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:2CUR"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:2CUR"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:2CUR"
FT TURN 183..186
FT /evidence="ECO:0007829|PDB:2CUR"
FT TURN 189..191
FT /evidence="ECO:0007829|PDB:2CUR"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:2CUR"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:2CUR"
FT HELIX 210..217
FT /evidence="ECO:0007829|PDB:2CUR"
FT VARIANT Q13642-1:246
FT /note="H -> Y (in XMPMA; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:19687455"
FT /id="VAR_082844"
FT VARIANT Q13642-1:275
FT /note="D -> N"
FT /evidence="ECO:0000269|PubMed:19687455"
FT /id="VAR_082845"
SQ SEQUENCE 323 AA; 36263 MW; 50FD17F7B2606823 CRC64;
MAEKFDCHYC RDPLQGKKYV QKDGHHCCLK CFDKFCANTC VECRKPIGAD SKEVHYKNRF
WHDTCFRCAK CLHPLANETF VAKDNKILCN KCTTREDSPK CKGCFKAIVA GDQNVEYKGT
VWHKDCFTCS NCKQVIGTGS FFPKGEDFYC VTCHETKFAK HCVKCNKAIT SGGITYQDQP
WHADCFVCVT CSKKLAGQRF TAVEDQYYCV DCYKNFVAKK CAGCKNPITG KRTVSRVSHP
VSKARKPPVC HGKRLPLTLF PSANLRGRHP GGERTCPSWV VVLYRKNRSL AAPRGPGLVK
APVWWPMKDN PGTTTASTAK NAP
