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FHL3_HUMAN
ID   FHL3_HUMAN              Reviewed;         280 AA.
AC   Q13643; D3DPT6; Q6I9T0; Q9BVA2;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 4.
DT   03-AUG-2022, entry version 188.
DE   RecName: Full=Four and a half LIM domains protein 3;
DE            Short=FHL-3;
DE   AltName: Full=Skeletal muscle LIM-protein 2;
DE            Short=SLIM-2;
GN   Name=FHL3; Synonyms=SLIM2;
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].
RC   TISSUE=Skeletal muscle;
RX   PubMed=10049693; DOI=10.1006/bbrc.1999.0179;
RA   Morgan M.J., Madgwick A.J.A.;
RT   "The LIM proteins FHL1 and FHL3 are expressed differently in skeletal
RT   muscle.";
RL   Biochem. Biophys. Res. Commun. 255:245-250(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16710414; DOI=10.1038/nature04727;
RA   Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA   Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA   Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA   Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA   Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA   Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA   Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA   Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA   Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA   Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA   Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA   Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA   Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA   Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA   Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA   Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA   Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA   Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA   McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA   Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA   Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA   Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA   Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA   Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA   White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA   Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA   Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA   Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT   "The DNA sequence and biological annotation of human chromosome 1.";
RL   Nature 441:315-321(2006).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   [8]
RP   PRELIMINARY NUCLEOTIDE SEQUENCE [MRNA] OF 16-280.
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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [10]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [12]
RP   STRUCTURE BY NMR OF 98-218 IN COMPLEX WITH ZINC IONS.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of LIM domains from human skeletal muscle LIM-protein
RT   2.";
RL   Submitted (AUG-2005) to the PDB data bank.
CC   -!- FUNCTION: Recruited by SOX15 to FOXK1 promoters where it acts as a
CC       transcriptional coactivator of FOXK1. {ECO:0000250|UniProtKB:Q9R059}.
CC   -!- SUBUNIT: Interacts with SOX15; the interaction recruits FHL3 to FOXK1
CC       promoters where it acts as a transcriptional coactivator of FOXK1.
CC       {ECO:0000250|UniProtKB:Q9R059}.
CC   -!- INTERACTION:
CC       Q13643; Q9NQ94: A1CF; NbExp=3; IntAct=EBI-741101, EBI-2809489;
CC       Q13643; Q13444: ADAM15; NbExp=3; IntAct=EBI-741101, EBI-77818;
CC       Q13643; Q13155: AIMP2; NbExp=13; IntAct=EBI-741101, EBI-745226;
CC       Q13643; P02760: AMBP; NbExp=3; IntAct=EBI-741101, EBI-2115136;
CC       Q13643; A0A0A0MQZ8: ANKHD1; NbExp=4; IntAct=EBI-741101, EBI-11531560;
CC       Q13643; Q03989: ARID5A; NbExp=3; IntAct=EBI-741101, EBI-948603;
CC       Q13643; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-741101, EBI-10254793;
CC       Q13643; Q9UMQ3: BARX2; NbExp=3; IntAct=EBI-741101, EBI-12053927;
CC       Q13643; Q9BTE2: C16orf35; NbExp=3; IntAct=EBI-741101, EBI-10298364;
CC       Q13643; Q6P1W5: C1orf94; NbExp=5; IntAct=EBI-741101, EBI-946029;
CC       Q13643; Q5BN46: C9orf116; NbExp=3; IntAct=EBI-741101, EBI-10243636;
CC       Q13643; Q5BN46-2: C9orf116; NbExp=3; IntAct=EBI-741101, EBI-12305735;
CC       Q13643; Q9NQ75-2: CASS4; NbExp=5; IntAct=EBI-741101, EBI-12270182;
CC       Q13643; Q9HC52: CBX8; NbExp=5; IntAct=EBI-741101, EBI-712912;
CC       Q13643; E9PSE9: CCDC198; NbExp=3; IntAct=EBI-741101, EBI-11748295;
CC       Q13643; Q9NVL8: CCDC198; NbExp=3; IntAct=EBI-741101, EBI-10238351;
CC       Q13643; A0A0S2Z364: CLCN2; NbExp=3; IntAct=EBI-741101, EBI-16435545;
CC       Q13643; Q8NE01: CNNM3; NbExp=9; IntAct=EBI-741101, EBI-741032;
CC       Q13643; Q8NE01-3: CNNM3; NbExp=3; IntAct=EBI-741101, EBI-10269984;
CC       Q13643; Q02930-3: CREB5; NbExp=3; IntAct=EBI-741101, EBI-10192698;
CC       Q13643; Q6Q6R5-3: CRIP3; NbExp=3; IntAct=EBI-741101, EBI-12925520;
CC       Q13643; P53672: CRYBA2; NbExp=3; IntAct=EBI-741101, EBI-750444;
CC       Q13643; P09603: CSF1; NbExp=3; IntAct=EBI-741101, EBI-2872294;
CC       Q13643; P56545: CTBP2; NbExp=4; IntAct=EBI-741101, EBI-741533;
CC       Q13643; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-741101, EBI-3867333;
CC       Q13643; A2VCK2: DCDC2B; NbExp=6; IntAct=EBI-741101, EBI-10173222;
CC       Q13643; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-741101, EBI-12000556;
CC       Q13643; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-741101, EBI-9679045;
CC       Q13643; A0AVK6: E2F8; NbExp=3; IntAct=EBI-741101, EBI-7779316;
CC       Q13643; Q6NXP0: EFCAB12; NbExp=3; IntAct=EBI-741101, EBI-10251535;
CC       Q13643; Q5JZY3-3: EPHA10; NbExp=3; IntAct=EBI-741101, EBI-10244652;
CC       Q13643; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-741101, EBI-6255981;
CC       Q13643; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-741101, EBI-3943864;
CC       Q13643; Q9BQ89: FAM110A; NbExp=3; IntAct=EBI-741101, EBI-1752811;
CC       Q13643; Q9BYI3: FAM126A; NbExp=3; IntAct=EBI-741101, EBI-11065686;
CC       Q13643; Q8WU58: FAM222B; NbExp=3; IntAct=EBI-741101, EBI-2807642;
CC       Q13643; Q8NEG0: FAM71C; NbExp=3; IntAct=EBI-741101, EBI-752049;
CC       Q13643; Q86YD7: FAM90A1; NbExp=7; IntAct=EBI-741101, EBI-6658203;
CC       Q13643; Q96D16: FBXL18; NbExp=3; IntAct=EBI-741101, EBI-744419;
CC       Q13643; P15408: FOSL2; NbExp=4; IntAct=EBI-741101, EBI-3893419;
CC       Q13643; Q96NZ1: FOXN4; NbExp=4; IntAct=EBI-741101, EBI-11749712;
CC       Q13643; P15976-2: GATA1; NbExp=4; IntAct=EBI-741101, EBI-9090198;
CC       Q13643; P23769: GATA2; NbExp=5; IntAct=EBI-741101, EBI-2806671;
CC       Q13643; O75603: GCM2; NbExp=11; IntAct=EBI-741101, EBI-10188645;
CC       Q13643; Q96NT3-2: GUCD1; NbExp=3; IntAct=EBI-741101, EBI-11978177;
CC       Q13643; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-741101, EBI-11956675;
CC       Q13643; Q86Z02: HIPK1; NbExp=4; IntAct=EBI-741101, EBI-692891;
CC       Q13643; Q86Z02-4: HIPK1; NbExp=3; IntAct=EBI-741101, EBI-12025238;
CC       Q13643; P49639: HOXA1; NbExp=3; IntAct=EBI-741101, EBI-740785;
CC       Q13643; O75031: HSF2BP; NbExp=3; IntAct=EBI-741101, EBI-7116203;
CC       Q13643; P42858: HTT; NbExp=9; IntAct=EBI-741101, EBI-466029;
CC       Q13643; Q12891: HYAL2; NbExp=3; IntAct=EBI-741101, EBI-2806068;
CC       Q13643; Q8IYA8: IHO1; NbExp=4; IntAct=EBI-741101, EBI-8638439;
CC       Q13643; Q9UKT9: IKZF3; NbExp=4; IntAct=EBI-741101, EBI-747204;
CC       Q13643; P18084: ITGB5; NbExp=5; IntAct=EBI-741101, EBI-1223434;
CC       Q13643; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-741101, EBI-2556193;
CC       Q13643; Q9ULH0-2: KIDINS220; NbExp=3; IntAct=EBI-741101, EBI-11046235;
CC       Q13643; Q6UWL6: KIRREL2; NbExp=3; IntAct=EBI-741101, EBI-10254473;
CC       Q13643; Q6UWL6-5: KIRREL2; NbExp=3; IntAct=EBI-741101, EBI-12794590;
CC       Q13643; Q9Y4X4: KLF12; NbExp=3; IntAct=EBI-741101, EBI-750750;
CC       Q13643; P57682: KLF3; NbExp=11; IntAct=EBI-741101, EBI-8472267;
CC       Q13643; Q5T749: KPRP; NbExp=4; IntAct=EBI-741101, EBI-10981970;
CC       Q13643; P59990: KRTAP12-1; NbExp=6; IntAct=EBI-741101, EBI-10210845;
CC       Q13643; P59991: KRTAP12-2; NbExp=6; IntAct=EBI-741101, EBI-10176379;
CC       Q13643; Q96EK9: KTI12; NbExp=3; IntAct=EBI-741101, EBI-7951092;
CC       Q13643; Q9NRM7: LATS2; NbExp=4; IntAct=EBI-741101, EBI-3506895;
CC       Q13643; P01229: LHB; NbExp=3; IntAct=EBI-741101, EBI-11659791;
CC       Q13643; P25791: LMO2; NbExp=3; IntAct=EBI-741101, EBI-739696;
CC       Q13643; P61968: LMO4; NbExp=3; IntAct=EBI-741101, EBI-2798728;
CC       Q13643; Q8N448: LNX2; NbExp=4; IntAct=EBI-741101, EBI-2340947;
CC       Q13643; P50281: MMP14; NbExp=3; IntAct=EBI-741101, EBI-992788;
CC       Q13643; Q9HC36: MRM3; NbExp=8; IntAct=EBI-741101, EBI-1045440;
CC       Q13643; Q9P0M9: MRPL27; NbExp=6; IntAct=EBI-741101, EBI-5325236;
CC       Q13643; Q96E11: MRRF; NbExp=3; IntAct=EBI-741101, EBI-2855755;
CC       Q13643; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-741101, EBI-10699187;
CC       Q13643; A2RUH7: MYBPHL; NbExp=3; IntAct=EBI-741101, EBI-9088235;
CC       Q13643; Q8TDC0: MYOZ3; NbExp=3; IntAct=EBI-741101, EBI-5662487;
CC       Q13643; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-741101, EBI-2858213;
CC       Q13643; O14561: NDUFAB1; NbExp=5; IntAct=EBI-741101, EBI-1246261;
CC       Q13643; A8MYP8: ODF3B; NbExp=3; IntAct=EBI-741101, EBI-12010090;
CC       Q13643; O15460-2: P4HA2; NbExp=3; IntAct=EBI-741101, EBI-10182841;
CC       Q13643; Q86TB9: PATL1; NbExp=8; IntAct=EBI-741101, EBI-2562092;
CC       Q13643; Q96BD5: PHF21A; NbExp=7; IntAct=EBI-741101, EBI-745085;
CC       Q13643; Q99959-2: PKP2; NbExp=3; IntAct=EBI-741101, EBI-10987518;
CC       Q13643; Q96PX9: PLEKHG4B; NbExp=4; IntAct=EBI-741101, EBI-11741362;
CC       Q13643; Q7Z5V6-2: PPP1R32; NbExp=3; IntAct=EBI-741101, EBI-12000762;
CC       Q13643; P0CG20: PRR35; NbExp=3; IntAct=EBI-741101, EBI-11986293;
CC       Q13643; Q6MZQ0: PRR5L; NbExp=3; IntAct=EBI-741101, EBI-1567866;
CC       Q13643; P29350: PTPN6; NbExp=3; IntAct=EBI-741101, EBI-78260;
CC       Q13643; Q2TAL8: QRICH1; NbExp=6; IntAct=EBI-741101, EBI-2798044;
CC       Q13643; O60216: RAD21; NbExp=4; IntAct=EBI-741101, EBI-80739;
CC       Q13643; Q9NYN1: RASL12; NbExp=3; IntAct=EBI-741101, EBI-12917066;
CC       Q13643; P48380: RFX3; NbExp=4; IntAct=EBI-741101, EBI-742557;
CC       Q13643; Q8TAI7: RHEBL1; NbExp=3; IntAct=EBI-741101, EBI-746555;
CC       Q13643; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-741101, EBI-748350;
CC       Q13643; Q9UHR5: SAP30BP; NbExp=6; IntAct=EBI-741101, EBI-751683;
CC       Q13643; Q8IYX7: SAXO1; NbExp=9; IntAct=EBI-741101, EBI-3957636;
CC       Q13643; Q86WG5: SBF2; NbExp=3; IntAct=EBI-741101, EBI-2683289;
CC       Q13643; O00560: SDCBP; NbExp=3; IntAct=EBI-741101, EBI-727004;
CC       Q13643; Q5VZ18: SHE; NbExp=3; IntAct=EBI-741101, EBI-3956977;
CC       Q13643; Q8ND83: SLAIN1; NbExp=6; IntAct=EBI-741101, EBI-10269374;
CC       Q13643; Q96AG3: SLC25A46; NbExp=6; IntAct=EBI-741101, EBI-10281975;
CC       Q13643; Q8N4M1: SLC44A3; NbExp=3; IntAct=EBI-741101, EBI-10265585;
CC       Q13643; O95391: SLU7; NbExp=3; IntAct=EBI-741101, EBI-750559;
CC       Q13643; P14678-2: SNRPB; NbExp=3; IntAct=EBI-741101, EBI-372475;
CC       Q13643; P09234: SNRPC; NbExp=3; IntAct=EBI-741101, EBI-766589;
CC       Q13643; P62308: SNRPG; NbExp=6; IntAct=EBI-741101, EBI-624585;
CC       Q13643; Q9NU19: TBC1D22B; NbExp=3; IntAct=EBI-741101, EBI-8787464;
CC       Q13643; Q9BT49: THAP7; NbExp=3; IntAct=EBI-741101, EBI-741350;
CC       Q13643; Q9P2T0: THEG; NbExp=4; IntAct=EBI-741101, EBI-751020;
CC       Q13643; Q08117-2: TLE5; NbExp=4; IntAct=EBI-741101, EBI-11741437;
CC       Q13643; Q6UXF1: TMEM108; NbExp=3; IntAct=EBI-741101, EBI-7100456;
CC       Q13643; P62328: TMSB4X; NbExp=3; IntAct=EBI-741101, EBI-712598;
CC       Q13643; Q96JJ7: TMX3; NbExp=3; IntAct=EBI-741101, EBI-2514069;
CC       Q13643; G5E9N2: TRO; NbExp=3; IntAct=EBI-741101, EBI-10178070;
CC       Q13643; Q3SY00: TSGA10IP; NbExp=5; IntAct=EBI-741101, EBI-10241197;
CC       Q13643; Q6ZVT0: TTLL10; NbExp=3; IntAct=EBI-741101, EBI-7844656;
CC       Q13643; Q6ZVT0-3: TTLL10; NbExp=3; IntAct=EBI-741101, EBI-11979997;
CC       Q13643; Q6PEY2: TUBA3E; NbExp=3; IntAct=EBI-741101, EBI-2551023;
CC       Q13643; P29597: TYK2; NbExp=6; IntAct=EBI-741101, EBI-1383454;
CC       Q13643; Q8TAI1: TYMSOS; NbExp=3; IntAct=EBI-741101, EBI-742060;
CC       Q13643; Q7Z7E8-2: UBE2Q1; NbExp=3; IntAct=EBI-741101, EBI-10258181;
CC       Q13643; B2RUY7: VWC2L; NbExp=4; IntAct=EBI-741101, EBI-11747707;
CC       Q13643; Q64LD2-2: WDR25; NbExp=3; IntAct=EBI-741101, EBI-12032042;
CC       Q13643; Q8WYQ9: ZCCHC14; NbExp=3; IntAct=EBI-741101, EBI-3937908;
CC       Q13643; P26651: ZFP36; NbExp=4; IntAct=EBI-741101, EBI-374248;
CC       Q13643; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-741101, EBI-740727;
CC       Q13643; Q96KM6: ZNF512B; NbExp=8; IntAct=EBI-741101, EBI-1049952;
CC       Q13643; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-741101, EBI-6427977;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9R059}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9R059}.
CC   -!- TISSUE SPECIFICITY: Expressed only in skeletal muscle.
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DR   EMBL; U60116; AAC04466.2; -; mRNA.
DR   EMBL; AK290641; BAF83330.1; -; mRNA.
DR   EMBL; BT007052; AAP35701.1; -; mRNA.
DR   EMBL; CR457425; CAG33706.1; -; mRNA.
DR   EMBL; AL603790; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471059; EAX07301.1; -; Genomic_DNA.
DR   EMBL; CH471059; EAX07302.1; -; Genomic_DNA.
DR   EMBL; BC001351; AAH01351.1; -; mRNA.
DR   EMBL; BC011697; AAH11697.1; -; mRNA.
DR   CCDS; CCDS30678.1; -.
DR   PIR; T09504; T09504.
DR   RefSeq; NP_001230807.1; NM_001243878.1.
DR   RefSeq; NP_004459.2; NM_004468.4.
DR   PDB; 1WYH; NMR; -; A=101-159.
DR   PDB; 2CUQ; NMR; -; A=152-218.
DR   PDB; 2EHE; NMR; -; A=30-99.
DR   PDBsum; 1WYH; -.
DR   PDBsum; 2CUQ; -.
DR   PDBsum; 2EHE; -.
DR   AlphaFoldDB; Q13643; -.
DR   SMR; Q13643; -.
DR   BioGRID; 108566; 267.
DR   CORUM; Q13643; -.
DR   DIP; DIP-42030N; -.
DR   IntAct; Q13643; 173.
DR   MINT; Q13643; -.
DR   STRING; 9606.ENSP00000362107; -.
DR   GlyGen; Q13643; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q13643; -.
DR   PhosphoSitePlus; Q13643; -.
DR   BioMuta; FHL3; -.
DR   DMDM; 209572768; -.
DR   EPD; Q13643; -.
DR   jPOST; Q13643; -.
DR   MassIVE; Q13643; -.
DR   MaxQB; Q13643; -.
DR   PaxDb; Q13643; -.
DR   PeptideAtlas; Q13643; -.
DR   PRIDE; Q13643; -.
DR   ProteomicsDB; 59647; -.
DR   Antibodypedia; 31823; 178 antibodies from 32 providers.
DR   DNASU; 2275; -.
DR   Ensembl; ENST00000373016.4; ENSP00000362107.3; ENSG00000183386.10.
DR   GeneID; 2275; -.
DR   KEGG; hsa:2275; -.
DR   MANE-Select; ENST00000373016.4; ENSP00000362107.3; NM_004468.5; NP_004459.2.
DR   UCSC; uc001cck.4; human.
DR   CTD; 2275; -.
DR   DisGeNET; 2275; -.
DR   GeneCards; FHL3; -.
DR   HGNC; HGNC:3704; FHL3.
DR   HPA; ENSG00000183386; Group enriched (skeletal muscle, tongue).
DR   MIM; 602790; gene.
DR   neXtProt; NX_Q13643; -.
DR   OpenTargets; ENSG00000183386; -.
DR   PharmGKB; PA28142; -.
DR   VEuPathDB; HostDB:ENSG00000183386; -.
DR   eggNOG; KOG1704; Eukaryota.
DR   GeneTree; ENSGT00950000183028; -.
DR   HOGENOM; CLU_001357_2_0_1; -.
DR   InParanoid; Q13643; -.
DR   OMA; RILCRDC; -.
DR   OrthoDB; 642235at2759; -.
DR   PhylomeDB; Q13643; -.
DR   TreeFam; TF314113; -.
DR   PathwayCommons; Q13643; -.
DR   SignaLink; Q13643; -.
DR   BioGRID-ORCS; 2275; 16 hits in 1093 CRISPR screens.
DR   ChiTaRS; FHL3; human.
DR   EvolutionaryTrace; Q13643; -.
DR   GeneWiki; FHL3; -.
DR   GenomeRNAi; 2275; -.
DR   Pharos; Q13643; Tbio.
DR   PRO; PR:Q13643; -.
DR   Proteomes; UP000005640; Chromosome 1.
DR   RNAct; Q13643; protein.
DR   Bgee; ENSG00000183386; Expressed in hindlimb stylopod muscle and 118 other tissues.
DR   Genevisible; Q13643; HS.
DR   GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0001725; C:stress fiber; IBA:GO_Central.
DR   GO; GO:0030018; C:Z disc; IBA:GO_Central.
DR   GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR   GO; GO:0030036; P:actin cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0007517; P:muscle organ development; TAS:ProtInc.
DR   InterPro; IPR037987; FHL2/3/5.
DR   InterPro; IPR001781; Znf_LIM.
DR   PANTHER; PTHR24205; PTHR24205; 1.
DR   Pfam; PF00412; LIM; 4.
DR   SMART; SM00132; LIM; 4.
DR   PROSITE; PS00478; LIM_DOMAIN_1; 4.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Activator; Cytoplasm; LIM domain; Metal-binding;
KW   Nucleus; Reference proteome; Repeat; Transcription;
KW   Transcription regulation; Zinc; Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..280
FT                   /note="Four and a half LIM domains protein 3"
FT                   /id="PRO_0000075740"
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   DOMAIN          221..275
FT                   /note="LIM zinc-binding 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT   ZN_FING         7..31
FT                   /note="C4-type"
FT                   /evidence="ECO:0000255"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         157
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R059"
FT   MOD_RES         235
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9R059"
FT   CONFLICT        82
FT                   /note="C -> R (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        130
FT                   /note="S -> I (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        140
FT                   /note="S -> P (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157
FT                   /note="K -> N (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        166
FT                   /note="S -> T (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        174
FT                   /note="V -> L (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        179
FT                   /note="Q -> L (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        183..184
FT                   /note="RE -> PK (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        250..252
FT                   /note="SCA -> TCD (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        252
FT                   /note="A -> D (in Ref. 4; CAG33706)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="T -> N (in Ref. 1; AAC04466)"
FT                   /evidence="ECO:0000305"
FT   TURN            41..43
FT                   /evidence="ECO:0007829|PDB:2EHE"
FT   TURN            63..65
FT                   /evidence="ECO:0007829|PDB:2EHE"
FT   TURN            69..71
FT                   /evidence="ECO:0007829|PDB:2EHE"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:2EHE"
FT   STRAND          86..89
FT                   /evidence="ECO:0007829|PDB:2EHE"
FT   TURN            90..92
FT                   /evidence="ECO:0007829|PDB:2EHE"
FT   STRAND          102..104
FT                   /evidence="ECO:0007829|PDB:1WYH"
FT   STRAND          110..112
FT                   /evidence="ECO:0007829|PDB:1WYH"
FT   TURN            124..126
FT                   /evidence="ECO:0007829|PDB:1WYH"
FT   TURN            130..132
FT                   /evidence="ECO:0007829|PDB:1WYH"
FT   TURN            136..138
FT                   /evidence="ECO:0007829|PDB:1WYH"
FT   STRAND          141..144
FT                   /evidence="ECO:0007829|PDB:1WYH"
FT   STRAND          147..150
FT                   /evidence="ECO:0007829|PDB:1WYH"
FT   HELIX           151..157
FT                   /evidence="ECO:0007829|PDB:1WYH"
FT   TURN            163..165
FT                   /evidence="ECO:0007829|PDB:2CUQ"
FT   STRAND          174..181
FT                   /evidence="ECO:0007829|PDB:2CUQ"
FT   TURN            183..185
FT                   /evidence="ECO:0007829|PDB:2CUQ"
FT   STRAND          189..191
FT                   /evidence="ECO:0007829|PDB:2CUQ"
FT   STRAND          200..202
FT                   /evidence="ECO:0007829|PDB:2CUQ"
FT   STRAND          204..209
FT                   /evidence="ECO:0007829|PDB:2CUQ"
FT   HELIX           210..216
FT                   /evidence="ECO:0007829|PDB:2CUQ"
SQ   SEQUENCE   280 AA;  31192 MW;  D1A037C260370DFD CRC64;
     MSESFDCAKC NESLYGRKYI QTDSGPYCVP CYDNTFANTC AECQQLIGHD SRELFYEDRH
     FHEGCFRCCR CQRSLADEPF TCQDSELLCN DCYCSAFSSQ CSACGETVMP GSRKLEYGGQ
     TWHEHCFLCS GCEQPLGSRS FVPDKGAHYC VPCYENKFAP RCARCSKTLT QGGVTYRDQP
     WHRECLVCTG CQTPLAGQQF TSRDEDPYCV ACFGELFAPK CSSCKRPIVG LGGGKYVSFE
     DRHWHHNCFS CARCSTSLVG QGFVPDGDQV LCQGCSQAGP
 
 
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