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 27-MAR-2024, entry version 220. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; 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; 129. DR CORUM; Q13642; -. DR IntAct; Q13642; 44. DR MINT; Q13642; -. DR STRING; 9606.ENSP00000498684; -. DR GlyGen; Q13642; 1 site, 1 O-linked glycan (1 site). 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; 9606-ENSP00000377710; -. DR PeptideAtlas; 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 Pumba; Q13642; -. DR TopDownProteomics; Q13642-1; -. [Q13642-1] DR ABCD; Q13642; 1 sequenced antibody. DR Antibodypedia; 16643; 557 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 AGR; HGNC:3702; -. 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; HCKQPIS; -. DR OrthoDB; 370973at2759; -. DR PhylomeDB; Q13642; -. DR TreeFam; TF318571; -. DR PathwayCommons; Q13642; -. DR SignaLink; Q13642; -. DR SIGNOR; Q13642; -. DR BioGRID-ORCS; 2273; 13 hits in 777 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 212 other cell types or tissues. DR ExpressionAtlas; Q13642; baseline and differential. 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 CDD; cd09344; LIM1_FHL1; 1. DR CDD; cd09424; LIM2_FHL1; 1. DR CDD; cd09429; LIM3_FHL1; 1. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 3. DR InterPro; IPR042997; Fhl1. DR InterPro; IPR001781; Znf_LIM. DR PANTHER; PTHR47029; FOUR AND A HALF LIM DOMAINS PROTEIN 1; 1. DR PANTHER; PTHR47029:SF4; FOUR AND A HALF LIM DOMAINS PROTEIN 1; 1. DR Pfam; PF00412; LIM; 3. DR SMART; SM00132; LIM; 3. DR SUPFAM; SSF57716; Glucocorticoid receptor-like (DNA-binding domain); 4. DR PROSITE; PS00478; LIM_DOMAIN_1; 3. DR PROSITE; PS50023; LIM_DOMAIN_2; 3. DR Genevisible; Q13642; HS. 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; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19171836" FT /id="VAR_075350" FT VARIANT 102..104 FT /note="Missing (in RBMX1B; uncertain significance)" FT /evidence="ECO:0000269|PubMed:19171836" FT /id="VAR_075351" FT VARIANT 104 FT /note="C -> R (in RBMX1B; uncertain significance; FT 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; uncertain significance; FT 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; uncertain 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 //