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FHL3_MOUSE
ID   FHL3_MOUSE              Reviewed;         289 AA.
AC   Q9R059; A6H6N4; Q9JLP5; Q9WUH3;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2012, sequence version 2.
DT   03-AUG-2022, entry version 140.
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;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
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 [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=10906474; DOI=10.1016/s0925-4773(00)00341-5;
RA   Chu P.-H., Ruiz-Lozano P., Zhou Q., Cai C., Chen J.;
RT   "Expression patterns of FHL/SLIM family members suggest important
RT   functional roles in skeletal muscle and cardiovascular system.";
RL   Mech. Dev. 95:259-265(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 11-228.
RA   Li H.Y., Lee S.M.Y., Tsui S.K.W., Chan K.K., Kotaka M., Chim S.S.C.,
RA   Lee C.Y., Fung K.P., Waye M.M.Y.;
RT   "The cloning, sequencing and characterization of a mouse FHL3, which
RT   contains four and a half LIM domains.";
RL   Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   FUNCTION, INTERACTION WITH SOX15, SUBCELLULAR LOCATION, AND TISSUE
RP   SPECIFICITY.
RX   PubMed=17363903; DOI=10.1038/sj.emboj.7601635;
RA   Meeson A.P., Shi X., Alexander M.S., Williams R.S., Allen R.E., Jiang N.,
RA   Adham I.M., Goetsch S.C., Hammer R.E., Garry D.J.;
RT   "Sox15 and Fhl3 transcriptionally coactivate Foxk1 and regulate myogenic
RT   progenitor cells.";
RL   EMBO J. 26:1902-1912(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Heart, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [8]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-157 AND LYS-244, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic fibroblast;
RX   PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA   Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA   Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT   "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT   pathways.";
RL   Mol. Cell 50:919-930(2013).
CC   -!- FUNCTION: Recruited by SOX15 to FOXK1 promoters where it acts as a
CC       transcriptional coactivator of FOXK1. {ECO:0000269|PubMed:17363903}.
CC   -!- SUBUNIT: Interacts with SOX15; the interaction recruits FHL3 to FOXK1
CC       promoters where it acts as a transcriptional coactivator of FOXK1.
CC       {ECO:0000269|PubMed:17363903}.
CC   -!- INTERACTION:
CC       Q9R059; P43267: Sox15; NbExp=7; IntAct=EBI-7332617, EBI-7332587;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17363903}. Cytoplasm
CC       {ECO:0000269|PubMed:17363903}.
CC   -!- TISSUE SPECIFICITY: Expressed in myogenic progenitor cells (at protein
CC       level) (PubMed:17363903). Expressed in skeletal striated muscle and the
CC       heart (PubMed:10906474, PubMed:17363903). Expressed to a lesser extent,
CC       in lung, and kidney (PubMed:10906474). Expressed in skin and skeletal
CC       muscles such as the masseter, tongue, tibialis anterior and plantar
CC       muscles (PubMed:10049693). {ECO:0000269|PubMed:10049693,
CC       ECO:0000269|PubMed:10906474, ECO:0000269|PubMed:17363903}.
CC   -!- DEVELOPMENTAL STAGE: Expressed ubiquitously at low levels during
CC       embryonic development. {ECO:0000269|PubMed:10906474}.
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DR   EMBL; AF134772; AAD32623.1; -; mRNA.
DR   EMBL; AF114382; AAD53231.1; -; mRNA.
DR   EMBL; AL606907; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC144903; AAI44904.1; -; mRNA.
DR   EMBL; BC145939; AAI45940.1; -; mRNA.
DR   EMBL; AF149826; AAF73159.1; -; mRNA.
DR   CCDS; CCDS38874.1; -.
DR   RefSeq; NP_034343.2; NM_010213.3.
DR   RefSeq; XP_006502831.1; XM_006502768.3.
DR   AlphaFoldDB; Q9R059; -.
DR   SMR; Q9R059; -.
DR   BioGRID; 199670; 5.
DR   IntAct; Q9R059; 1.
DR   MINT; Q9R059; -.
DR   STRING; 10090.ENSMUSP00000040150; -.
DR   iPTMnet; Q9R059; -.
DR   PhosphoSitePlus; Q9R059; -.
DR   EPD; Q9R059; -.
DR   MaxQB; Q9R059; -.
DR   PaxDb; Q9R059; -.
DR   PeptideAtlas; Q9R059; -.
DR   PRIDE; Q9R059; -.
DR   ProteomicsDB; 270989; -.
DR   Antibodypedia; 31823; 178 antibodies from 32 providers.
DR   DNASU; 14201; -.
DR   Ensembl; ENSMUST00000038684; ENSMUSP00000040150; ENSMUSG00000032643.
DR   GeneID; 14201; -.
DR   KEGG; mmu:14201; -.
DR   UCSC; uc008uqv.2; mouse.
DR   CTD; 2275; -.
DR   MGI; MGI:1341092; Fhl3.
DR   VEuPathDB; HostDB:ENSMUSG00000032643; -.
DR   eggNOG; KOG1704; Eukaryota.
DR   GeneTree; ENSGT00950000183028; -.
DR   InParanoid; Q9R059; -.
DR   OrthoDB; 642235at2759; -.
DR   PhylomeDB; Q9R059; -.
DR   TreeFam; TF314113; -.
DR   BioGRID-ORCS; 14201; 3 hits in 57 CRISPR screens.
DR   ChiTaRS; Fhl3; mouse.
DR   PRO; PR:Q9R059; -.
DR   Proteomes; UP000000589; Chromosome 4.
DR   RNAct; Q9R059; protein.
DR   Bgee; ENSMUSG00000032643; Expressed in hindlimb stylopod muscle and 62 other tissues.
DR   ExpressionAtlas; Q9R059; baseline and differential.
DR   Genevisible; Q9R059; MM.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0001725; C:stress fiber; IDA:MGI.
DR   GO; GO:0030018; C:Z disc; IDA:MGI.
DR   GO; GO:0003779; F:actin binding; IDA:MGI.
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; IDA:MGI.
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; 3.
DR   PROSITE; PS50023; LIM_DOMAIN_2; 4.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Cytoplasm; LIM domain; Metal-binding; Nucleus;
KW   Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW   Zinc-finger.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q13643"
FT   CHAIN           2..289
FT                   /note="Four and a half LIM domains protein 3"
FT                   /id="PRO_0000075741"
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:0000250|UniProtKB:Q13643"
FT   MOD_RES         157
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   MOD_RES         244
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0007744|PubMed:23806337"
FT   CONFLICT        77
FT                   /note="D -> G (in Ref. 1; AAD32623)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        91
FT                   /note="E -> D (in Ref. 1; AAD32623)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="T -> S (in Ref. 1; AAD32623)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        137
FT                   /note="G -> A (in Ref. 2; AAD53231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        157..159
FT                   /note="KFA -> NLT (in Ref. 5; AAF73159)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        192
FT                   /note="K -> Q (in Ref. 1; AAD32623)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="Q -> H (in Ref. 2; AAD53231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        205
FT                   /note="D -> E (in Ref. 1; AAD32623)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        225
FT                   /note="K -> N (in Ref. 2; AAD53231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        229..238
FT                   /note="TGGSGGGEGA -> V (in Ref. 1; AAD32623)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        235
FT                   /note="G -> A (in Ref. 2; AAD53231)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="S -> N (in Ref. 1; AAD32623)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   289 AA;  31795 MW;  38168919F5303237 CRC64;
     MSEAFDCAKC NESLYGRKYI QTDSGPYCVP CYDNTFANTC AECQQLIGHD SRELFYEDRH
     FHEGCFRCCR CQRSLADEPF TCQDSELLCN ECYCTAFSSQ CSACGETVMP GSRKLEYGGQ
     TWHEHCFLCS GCEQPLGSRS FVPDKGAHYC VPCYENKFAP RCARCSKTLT QGGVTYRDQP
     WHRECLVCTG CKTPLAGQQF TSRDDDPYCV ACFGELFAPK CSSCKRPITG GSGGGEGAGL
     GGGKYVSFED RHWHHSCFSC ARCSTSLVGQ GFVPDGDQVL CQGCSQAGP
 
 
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