LDB1_MOUSE
ID LDB1_MOUSE Reviewed; 411 AA.
AC P70662; O55204; Q1EQX2; Q71V68;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=LIM domain-binding protein 1;
DE Short=LDB-1;
DE AltName: Full=Carboxyl-terminal LIM domain-binding protein 2;
DE Short=CLIM-2;
DE AltName: Full=LIM domain-binding factor CLIM2;
DE Short=mLdb1;
DE AltName: Full=Nuclear LIM interactor;
GN Name=Ldb1; Synonyms=Nli;
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] (ISOFORM 3), FUNCTION, INTERACTION WITH LHX1,
RP AND TISSUE SPECIFICITY.
RC STRAIN=Swiss Webster; TISSUE=Embryo;
RX PubMed=8918878; DOI=10.1038/384270a0;
RA Agulnick A.D., Taira M., Breen J.J., Tanaka T., Dawid I.B., Westphal H.;
RT "Interactions of the LIM-domain-binding factor Ldb1 with LIM homeodomain
RT proteins.";
RL Nature 384:270-272(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND SUBCELLULAR LOCATION.
RC TISSUE=Embryo;
RX PubMed=8876198; DOI=10.1073/pnas.93.21.11693;
RA Jurata L.W., Kenny D.A., Gill G.N.;
RT "Nuclear LIM interactor, a rhombotin and LIM homeodomain interacting
RT protein, is expressed early in neuronal development.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:11693-11698(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Embryonic head;
RX PubMed=9192866; DOI=10.1101/gad.11.11.1370;
RA Bach I., Carriere C., Ostendorff H.P., Andersen B., Rosenfeld M.G.;
RT "A family of LIM domain-associated cofactors confer transcriptional
RT synergism between LIM and Otx homeodomain proteins.";
RL Genes Dev. 11:1370-1380(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, INTERACTION WITH LMO2, AND IDENTIFICATION IN A COMPLEX
RP WITH LMO2 AND TAL1.
RC TISSUE=Yolk sac;
RX PubMed=9391090; DOI=10.1073/pnas.94.25.13707;
RA Visvader J.E., Mao X., Fujiwara Y., Hahm K., Orkin S.H.;
RT "The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative
RT regulators of erythroid differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:13707-13712(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv;
RX PubMed=9503020; DOI=10.1006/geno.1997.5163;
RA Yamashita T., Agulnick A.D., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Westphal H.;
RT "Genomic structure and chromosomal localization of the mouse LIM domain-
RT binding protein 1 gene, Ldb1.";
RL Genomics 48:87-92(1998).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, ALTERNATIVE SPLICING, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Heart;
RX PubMed=16815859; DOI=10.1093/jb/mvj134;
RA Tran Y.H., Xu Z., Kato A., Mistry A.C., Goya Y., Taira M., Brandt S.J.,
RA Hirose S.;
RT "Spliced isoforms of LIM-domain-binding protein (CLIM/NLI/Ldb) lacking the
RT LIM-interaction domain.";
RL J. Biochem. 140:105-119(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 FUNCTION, INTERACTION WITH ISL1; LMO2 AND LMX1A, HOMODIMERIZATION,
RP SUBCELLULAR LOCATION, AND IDENTIFICATION OF LIM-BINDING DOMAIN.
RX PubMed=9315627; DOI=10.1128/mcb.17.10.5688;
RA Jurata L.W., Gill G.N.;
RT "Functional analysis of the nuclear LIM domain interactor NLI.";
RL Mol. Cell. Biol. 17:5688-5698(1997).
RN [9]
RP INTERACTION WITH LHX1, DOMAIN, AND HOMODIMERIZATION.
RX PubMed=9468533; DOI=10.1074/jbc.273.8.4712;
RA Breen J.J., Agulnick A.D., Westphal H., Dawid I.B.;
RT "Interactions between LIM domains and the LIM domain-binding protein
RT Ldb1.";
RL J. Biol. Chem. 273:4712-4717(1998).
RN [10]
RP INTERACTION WITH LHX6.
RC TISSUE=Fetal brain;
RX PubMed=10393337; DOI=10.1093/oxfordjournals.jbchem.a022420;
RA Kimura N., Ueno M., Nakashima K., Taga T.;
RT "A brain region-specific gene product Lhx6.1 interacts with Ldb1 through
RT tandem LIM-domains.";
RL J. Biochem. 126:180-187(1999).
RN [11]
RP INTERACTION WITH LHX9.
RX PubMed=10330499; DOI=10.1016/s0925-4773(98)00233-0;
RA Bertuzzi S., Porter F.D., Pitts A., Kumar M., Agulnick A., Wassif C.,
RA Westphal H.;
RT "Characterization of Lhx9, a novel LIM/homeobox gene expressed by the
RT pioneer neurons in the mouse cerebral cortex.";
RL Mech. Dev. 81:193-198(1999).
RN [12]
RP FUNCTION, AND INTERACTION WITH LHX3 AND ISL1.
RX PubMed=12150931; DOI=10.1016/s0092-8674(02)00823-1;
RA Thaler J.P., Lee S.K., Jurata L.W., Gill G.N., Pfaff S.L.;
RT "LIM factor Lhx3 contributes to the specification of motor neuron and
RT interneuron identity through cell-type-specific protein-protein
RT interactions.";
RL Cell 110:237-249(2002).
RN [13]
RP INTERACTION WITH RLIM, AND UBIQUITINATION.
RX PubMed=11882901; DOI=10.1038/416099a;
RA Ostendorff H.P., Peirano R.I., Peters M.A., Schluter A., Bossenz M.,
RA Scheffner M., Bach I.;
RT "Ubiquitination-dependent cofactor exchange on LIM homeodomain
RT transcription factors.";
RL Nature 416:99-103(2002).
RN [14]
RP IDENTIFICATION IN A NUCLEAR TAL-1 COMPLEX.
RX PubMed=16407974; DOI=10.1038/sj.emboj.7600934;
RA Goardon N., Lambert J.A., Rodriguez P., Nissaire P., Herblot S.,
RA Thibault P., Dumenil D., Strouboulis J., Romeo P.-H., Hoang T.;
RT "ETO2 coordinates cellular proliferation and differentiation during
RT erythropoiesis.";
RL EMBO J. 25:357-366(2006).
RN [15]
RP INTERACTION WITH SLK, AND SUBCELLULAR LOCATION.
RX PubMed=19675209; DOI=10.1091/mbc.e08-07-0707;
RA Storbeck C.J., Wagner S., O'Reilly P., McKay M., Parks R.J., Westphal H.,
RA Sabourin L.A.;
RT "The Ldb1 and Ldb2 transcriptional cofactors interact with the Ste20-like
RT kinase SLK and regulate cell migration.";
RL Mol. Biol. Cell 20:4174-4182(2009).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-61 AND SER-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Lung, Pancreas, 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 [17]
RP STRUCTURE BY NMR OF 336-375 IN COMPLEXES WITH LMO2 AND LMO4.
RX PubMed=12727888; DOI=10.1093/emboj/cdg196;
RA Deane J.E., Mackay J.P., Kwan A.H.Y., Sum E.Y.M., Visvader J.E.,
RA Matthews J.M.;
RT "Structural basis for the recognition of ldb1 by the N-terminal LIM domains
RT of LMO2 and LMO4.";
RL EMBO J. 22:2224-2233(2003).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 336-375 IN COMPLEX WITH LMO4.
RX PubMed=15343268; DOI=10.1038/sj.emboj.7600376;
RA Deane J.E., Ryan D.P., Sunde M., Maher M.J., Guss J.M., Visvader J.E.,
RA Matthews J.M.;
RT "Tandem LIM domains provide synergistic binding in the LMO4:Ldb1 complex.";
RL EMBO J. 23:3589-3598(2004).
CC -!- FUNCTION: Binds to the LIM domain of a wide variety of LIM domain-
CC containing transcription factors. May regulate the transcriptional
CC activity of LIM-containing proteins by determining specific partner
CC interactions. Plays a role in the development of interneurons and motor
CC neurons in cooperation with LHX3 and ISL1. Acts synergistically with
CC LHX1/LIM1 in axis formation and activation of gene expression. Acts
CC with LMO2 in the regulation of red blood cell development, maintaining
CC erythroid precursors in an immature state.
CC {ECO:0000269|PubMed:12150931, ECO:0000269|PubMed:16815859,
CC ECO:0000269|PubMed:8876198, ECO:0000269|PubMed:8918878,
CC ECO:0000269|PubMed:9192866, ECO:0000269|PubMed:9315627,
CC ECO:0000269|PubMed:9391090}.
CC -!- SUBUNIT: Interacts with ESR1 (By similarity). Forms homodimers and
CC heterodimers. Interacts with and activates LHX1/LIM1. Interacts with
CC the LIM domains of ISL1 and LMO2. Can assemble in a complex with LMO2
CC and TAL1/SCL but does not interact with TAL1/SCL directly. Strongly
CC interacts with the LIM2 domain of LMX1A and more weakly with the LIM1
CC domain. Homodimerization is not required for, and does not effect,
CC LMX1A-binding. Component of a nuclear TAL-1 complex composed at least
CC of CBFA2T3, LDB1, TAL1 and TCF3. Interacts with LHX6 and LHX9. At
CC neuronal promoters, forms a complex with LHX3 involved in the
CC specification of interneurons, in motor neurons, it is displaced by
CC ISL1 to form a ternary complex in which ISL1 contacts both LHX3 and
CC LDB1. Interacts with SLK; leading to negatively regulate SLK kinase
CC activity (PubMed:19675209). Interacts with YWHAZ (By similarity).
CC Interacts with PRDM1/BLIMP1 (By similarity). {ECO:0000250,
CC ECO:0000250|UniProtKB:Q86U70, ECO:0000269|PubMed:10330499,
CC ECO:0000269|PubMed:10393337, ECO:0000269|PubMed:11882901,
CC ECO:0000269|PubMed:12150931, ECO:0000269|PubMed:15343268,
CC ECO:0000269|PubMed:16407974, ECO:0000269|PubMed:19675209,
CC ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9315627,
CC ECO:0000269|PubMed:9391090, ECO:0000269|PubMed:9468533}.
CC -!- INTERACTION:
CC P70662; O54972: Cbfa2t3; NbExp=2; IntAct=EBI-6272082, EBI-8006703;
CC P70662; P61372: Isl1; NbExp=4; IntAct=EBI-6272082, EBI-7988215;
CC P70662; P50481: Lhx3; NbExp=5; IntAct=EBI-6272082, EBI-7988290;
CC P70662; P22091: Tal1; NbExp=4; IntAct=EBI-6272082, EBI-8006437;
CC P70662; Q60722: Tcf4; NbExp=2; IntAct=EBI-6272082, EBI-310070;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8876198,
CC ECO:0000269|PubMed:9315627, ECO:0000269|PubMed:9391090}.
CC Note=Colocalizes with SLK at leading edges (PubMed:19675209).
CC {ECO:0000269|PubMed:19675209}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Visvader-a;
CC IsoId=P70662-1; Sequence=Displayed;
CC Name=2; Synonyms=Tran-b;
CC IsoId=P70662-2; Sequence=VSP_027833, VSP_027834, VSP_027835;
CC Name=3; Synonyms=Tran-a;
CC IsoId=P70662-3; Sequence=VSP_027833;
CC -!- TISSUE SPECIFICITY: Expression overlaps that of LIM domain-containing
CC proteins. Expressed widely in the embryo with highest expression in
CC several regions of the brain the central nervous system ganglia. Also
CC expressed in fetal liver, lung, kidney, thymus and olfactory
CC epithelium. Expressed in multiple adult tissues including heart, brain,
CC liver, kidney, testis, lung and muscle and a diverse range of neuronal
CC cell types, with expression highest in the pituitary gland and skin.
CC Expressed in both embryonic and adult hemopoietic cells, including the
CC erythroid lineage. {ECO:0000269|PubMed:16815859,
CC ECO:0000269|PubMed:8918878, ECO:0000269|PubMed:9192866,
CC ECO:0000269|PubMed:9391090}.
CC -!- DOMAIN: The dimerization domain is located in the N-terminus.
CC {ECO:0000269|PubMed:9468533}.
CC -!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the
CC proteasome. {ECO:0000269|PubMed:11882901}.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. Lacks LIM-binding
CC domain. Lacks ability to activate LIM domain-dependent transcription.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDB family. {ECO:0000305}.
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DR EMBL; U70375; AAC52933.1; -; mRNA.
DR EMBL; U69270; AAC52887.1; -; mRNA.
DR EMBL; U89488; AAB96885.1; -; mRNA.
DR EMBL; AF030333; AAB94131.1; -; mRNA.
DR EMBL; AF024524; AAC40064.1; -; Genomic_DNA.
DR EMBL; AB250383; BAE95401.1; -; mRNA.
DR EMBL; BC013624; AAH13624.1; -; mRNA.
DR CCDS; CCDS29870.1; -. [P70662-3]
DR CCDS; CCDS50455.1; -. [P70662-1]
DR RefSeq; NP_001106879.1; NM_001113408.1. [P70662-1]
DR RefSeq; NP_034827.1; NM_010697.1. [P70662-3]
DR RefSeq; XP_011245459.1; XM_011247157.1.
DR PDB; 1J2O; NMR; -; A=336-375.
DR PDB; 1M3V; NMR; -; A=336-375.
DR PDB; 1RUT; X-ray; 1.30 A; X=336-375.
DR PDB; 2JTN; NMR; -; A=331-375.
DR PDB; 2L6Y; NMR; -; B=336-348.
DR PDB; 2L6Z; NMR; -; C=336-348.
DR PDB; 2LXD; NMR; -; A=336-375.
DR PDB; 4JCJ; X-ray; 3.00 A; A/B/C=336-366.
DR PDB; 6PTL; X-ray; 2.50 A; A=50-236.
DR PDBsum; 1J2O; -.
DR PDBsum; 1M3V; -.
DR PDBsum; 1RUT; -.
DR PDBsum; 2JTN; -.
DR PDBsum; 2L6Y; -.
DR PDBsum; 2L6Z; -.
DR PDBsum; 2LXD; -.
DR PDBsum; 4JCJ; -.
DR PDBsum; 6PTL; -.
DR AlphaFoldDB; P70662; -.
DR SASBDB; P70662; -.
DR SMR; P70662; -.
DR BioGRID; 201125; 32.
DR CORUM; P70662; -.
DR DIP; DIP-42842N; -.
DR IntAct; P70662; 30.
DR MINT; P70662; -.
DR STRING; 10090.ENSMUSP00000118546; -.
DR iPTMnet; P70662; -.
DR PhosphoSitePlus; P70662; -.
DR EPD; P70662; -.
DR MaxQB; P70662; -.
DR PaxDb; P70662; -.
DR PRIDE; P70662; -.
DR ProteomicsDB; 264922; -. [P70662-1]
DR ProteomicsDB; 264923; -. [P70662-2]
DR ProteomicsDB; 264924; -. [P70662-3]
DR Antibodypedia; 17969; 280 antibodies from 30 providers.
DR DNASU; 16825; -.
DR Ensembl; ENSMUST00000026252; ENSMUSP00000026252; ENSMUSG00000025223. [P70662-3]
DR Ensembl; ENSMUST00000056931; ENSMUSP00000053680; ENSMUSG00000025223. [P70662-3]
DR Ensembl; ENSMUST00000137771; ENSMUSP00000114667; ENSMUSG00000025223. [P70662-2]
DR Ensembl; ENSMUST00000156585; ENSMUSP00000118546; ENSMUSG00000025223. [P70662-1]
DR Ensembl; ENSMUST00000185355; ENSMUSP00000139562; ENSMUSG00000025223. [P70662-1]
DR GeneID; 16825; -.
DR KEGG; mmu:16825; -.
DR UCSC; uc008hrz.1; mouse. [P70662-1]
DR UCSC; uc008hsa.1; mouse. [P70662-2]
DR CTD; 8861; -.
DR MGI; MGI:894762; Ldb1.
DR VEuPathDB; HostDB:ENSMUSG00000025223; -.
DR eggNOG; KOG2181; Eukaryota.
DR GeneTree; ENSGT00390000005639; -.
DR HOGENOM; CLU_032597_0_0_1; -.
DR InParanoid; P70662; -.
DR OrthoDB; 849287at2759; -.
DR PhylomeDB; P70662; -.
DR TreeFam; TF319923; -.
DR Reactome; R-MMU-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR BioGRID-ORCS; 16825; 8 hits in 73 CRISPR screens.
DR ChiTaRS; Ldb1; mouse.
DR EvolutionaryTrace; P70662; -.
DR PRO; PR:P70662; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; P70662; protein.
DR Bgee; ENSMUSG00000025223; Expressed in embryonic brain and 255 other tissues.
DR ExpressionAtlas; P70662; baseline and differential.
DR Genevisible; P70662; MM.
DR GO; GO:1990907; C:beta-catenin-TCF complex; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0090575; C:RNA polymerase II transcription regulator complex; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0030274; F:LIM domain binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IPI:MGI.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0009948; P:anterior/posterior axis specification; IMP:MGI.
DR GO; GO:0007155; P:cell adhesion; IGI:MGI.
DR GO; GO:0030154; P:cell differentiation; TAS:MGI.
DR GO; GO:0022607; P:cellular component assembly; IGI:MGI.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IMP:MGI.
DR GO; GO:0021549; P:cerebellum development; IMP:MGI.
DR GO; GO:0010669; P:epithelial structure maintenance; IGI:MGI.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IMP:MGI.
DR GO; GO:0001942; P:hair follicle development; IGI:MGI.
DR GO; GO:0060322; P:head development; IGI:UniProtKB.
DR GO; GO:0043973; P:histone H3-K4 acetylation; IMP:BHF-UCL.
DR GO; GO:0048382; P:mesendoderm development; IMP:MGI.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; IEP:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IGI:MGI.
DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; TAS:BHF-UCL.
DR GO; GO:0030334; P:regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; IDA:UniProtKB.
DR GO; GO:0043549; P:regulation of kinase activity; IDA:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; IMP:BHF-UCL.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; IMP:BHF-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IMP:MGI.
DR IDEAL; IID50049; -.
DR InterPro; IPR030167; LDB1.
DR InterPro; IPR041363; LID.
DR InterPro; IPR029005; LIM-bd/SEUSS.
DR PANTHER; PTHR10378; PTHR10378; 1.
DR PANTHER; PTHR10378:SF7; PTHR10378:SF7; 1.
DR Pfam; PF17916; LID; 1.
DR Pfam; PF01803; LIM_bind; 2.
DR PROSITE; PS51957; LID; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Developmental protein;
KW Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q86U70"
FT CHAIN 2..411
FT /note="LIM domain-binding protein 1"
FT /id="PRO_0000084385"
FT DOMAIN 336..375
FT /note="LIM interaction domain (LID)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01302"
FT REGION 284..330
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 367..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U70"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86U70"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16815859, ECO:0000303|PubMed:8876198,
FT ECO:0000303|PubMed:8918878, ECO:0000303|PubMed:9192866"
FT /id="VSP_027833"
FT VAR_SEQ 336..355
FT /note="DVMVVGEPTLMGGEFGDEDE -> VSISAFFSSGLPHCSPLTPV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:16815859"
FT /id="VSP_027834"
FT VAR_SEQ 356..411
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16815859"
FT /id="VSP_027835"
FT CONFLICT 262
FT /note="Y -> C (in Ref. 3; AAB96885)"
FT /evidence="ECO:0000305"
FT CONFLICT 334
FT /note="V -> A (in Ref. 3; AAB96885)"
FT /evidence="ECO:0000305"
FT CONFLICT 389..390
FT /note="PW -> QR (in Ref. 3; AAB96885)"
FT /evidence="ECO:0000305"
FT HELIX 68..77
FT /evidence="ECO:0007829|PDB:6PTL"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:6PTL"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:6PTL"
FT STRAND 98..107
FT /evidence="ECO:0007829|PDB:6PTL"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:6PTL"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6PTL"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:6PTL"
FT STRAND 137..145
FT /evidence="ECO:0007829|PDB:6PTL"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:6PTL"
FT STRAND 152..167
FT /evidence="ECO:0007829|PDB:6PTL"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:6PTL"
FT STRAND 175..191
FT /evidence="ECO:0007829|PDB:6PTL"
FT STRAND 194..207
FT /evidence="ECO:0007829|PDB:6PTL"
FT STRAND 336..344
FT /evidence="ECO:0007829|PDB:1M3V"
FT STRAND 346..349
FT /evidence="ECO:0007829|PDB:1J2O"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:1RUT"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:1RUT"
SQ SEQUENCE 411 AA; 46503 MW; 47C53DFA23044580 CRC64;
MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP TYLEPGIGRH
TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED DAMLTITFCL EDGPKRYTIG
RTLIPRYFRS IFEGGATELY YVLKHPKEAF HSNFVSLDCD QGSMVTQHGK PMFTQVCVEG
RLYLEFMFDD MMRIKTWHFS IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL
NYLRLCVILE PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPAR QQPSKRRKRK
MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF GDEDERLITR
LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES KSENPTSQAS Q
