ID LDB2_MOUSE Reviewed; 373 AA. AC O55203; O55205; Q3UHY1; Q6AXE6; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 11-SEP-2007, sequence version 2. DT 24-JAN-2024, entry version 150. DE RecName: Full=LIM domain-binding protein 2; DE Short=LDB-2; DE AltName: Full=Carboxyl-terminal LIM domain-binding protein 1; DE Short=CLIM-1; DE AltName: Full=LIM domain-binding factor CLIM1; GN Name=Ldb2; Synonyms=Clim1; 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] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH RP LHX3 AND PITX1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE. 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC STRAIN=C57BL/6J; TISSUE=Embryonic kidney; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J., RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; 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 [4] RP INTERACTION WITH LMO4, AND DEVELOPMENTAL STAGE. RX PubMed=9860983; DOI=10.1073/pnas.95.26.15418; RA Sugihara T.M., Bach I., Kioussi C., Rosenfeld M.G., Andersen B.; RT "Mouse deformed epidermal autoregulatory factor 1 recruits a LIM domain RT factor, LMO-4, and CLIM coregulators."; RL Proc. Natl. Acad. Sci. U.S.A. 95:15418-15423(1998). RN [5] 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 [6] 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 [7] RP ALTERNATIVE SPLICING. 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 [8] RP INTERACTION WITH SLK, SUBCELLULAR LOCATION, AND FUNCTION. 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). CC -!- FUNCTION: Transcription cofactor (PubMed:9192866). Binds to the LIM CC domain of a wide variety of LIM domain-containing transcription factors CC (PubMed:9192866). {ECO:0000269|PubMed:9192866}. CC -!- FUNCTION: [Isoform 1]: Regulates the transcriptional activity of LIM- CC containing proteins such as LHX3 or PITX1. CC {ECO:0000269|PubMed:9192866}. CC -!- SUBUNIT: Interacts with LHX9 (PubMed:10330499). Interacts with SLK; CC leading to negatively regulate SLK kinase activity (PubMed:19675209). CC Interacts with LMO4 (PubMed:9860983). {ECO:0000269|PubMed:10330499, CC ECO:0000269|PubMed:11882901, ECO:0000269|PubMed:19675209}. CC -!- SUBUNIT: [Isoform 1]: Interacts with PITX1 (PubMed:9192866). Interacts CC with LHX3 (PubMed:9192866). {ECO:0000269|PubMed:9192866}. CC -!- INTERACTION: CC O55203; Q9WTV7: Rlim; NbExp=2; IntAct=EBI-15657830, EBI-15657872; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. Note=Colocalizes with SLK CC at leading edges (PubMed:19675209). {ECO:0000269|PubMed:19675209}. CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus CC {ECO:0000305|PubMed:9192866}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=CLIM-1a; CC IsoId=O55203-1; Sequence=Displayed; CC Name=2; Synonyms=CLIM-1b; CC IsoId=O55203-2; Sequence=VSP_014369, VSP_014370; CC Name=3; CC IsoId=O55203-3; Sequence=VSP_027829, VSP_014369, VSP_014370; CC -!- TISSUE SPECIFICITY: Expressed in multiple tissues including heart, CC brain, liver, kidney, testis, lung and muscle, with expression highest CC in the brain, trigeminal ganglia, and lung. CC {ECO:0000269|PubMed:9192866}. CC -!- DEVELOPMENTAL STAGE: Expression in the embryo overlaps that of LIM CC domain-containing proteins (PubMed:9192866). Expressed widely in the CC embryo with highest expression in several regions of the brain, and the CC central nervous system ganglia (PubMed:9192866). CC {ECO:0000269|PubMed:9192866}. CC -!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the CC proteasome. {ECO:0000269|PubMed:11882901}. CC -!- MISCELLANEOUS: [Isoform 2]: Lacks LIM-binding domain. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the LDB family. {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; U89487; AAB96884.1; -; mRNA. DR EMBL; U89489; AAB96886.1; -; mRNA. DR EMBL; AK147160; BAE27725.1; -; mRNA. DR EMBL; AK146860; BAE27488.1; -; mRNA. DR EMBL; BC079611; AAH79611.1; -; mRNA. DR CCDS; CCDS19271.1; -. [O55203-1] DR CCDS; CCDS80276.1; -. [O55203-2] DR CCDS; CCDS80278.1; -. [O55203-3] DR RefSeq; NP_001070866.1; NM_001077398.2. [O55203-3] DR RefSeq; NP_001273277.1; NM_001286348.1. [O55203-2] DR RefSeq; NP_034828.3; NM_010698.4. [O55203-1] DR RefSeq; XP_006503817.1; XM_006503754.3. [O55203-2] DR RefSeq; XP_006503819.1; XM_006503756.3. DR AlphaFoldDB; O55203; -. DR SMR; O55203; -. DR BioGRID; 201126; 34. DR DIP; DIP-46444N; -. DR IntAct; O55203; 20. DR STRING; 10090.ENSMUSP00000067737; -. DR iPTMnet; O55203; -. DR PhosphoSitePlus; O55203; -. DR MaxQB; O55203; -. DR PaxDb; 10090-ENSMUSP00000067737; -. DR PeptideAtlas; O55203; -. DR ProteomicsDB; 265052; -. [O55203-1] DR ProteomicsDB; 265053; -. [O55203-2] DR ProteomicsDB; 265054; -. [O55203-3] DR Antibodypedia; 4310; 257 antibodies from 27 providers. DR DNASU; 16826; -. DR Ensembl; ENSMUST00000070748.10; ENSMUSP00000067737.6; ENSMUSG00000039706.12. [O55203-1] DR Ensembl; ENSMUST00000199256.5; ENSMUSP00000143775.2; ENSMUSG00000039706.12. [O55203-3] DR Ensembl; ENSMUST00000199534.5; ENSMUSP00000142442.2; ENSMUSG00000039706.12. [O55203-2] DR GeneID; 16826; -. DR KEGG; mmu:16826; -. DR UCSC; uc008xis.2; mouse. [O55203-3] DR UCSC; uc008xit.2; mouse. [O55203-1] DR UCSC; uc008xiu.2; mouse. [O55203-2] DR AGR; MGI:894670; -. DR CTD; 9079; -. DR MGI; MGI:894670; Ldb2. DR VEuPathDB; HostDB:ENSMUSG00000039706; -. DR eggNOG; KOG2181; Eukaryota. DR GeneTree; ENSGT00390000005639; -. DR HOGENOM; CLU_032597_0_0_1; -. DR InParanoid; O55203; -. DR OMA; TPWNSKP; -. DR OrthoDB; 1369602at2759; -. DR PhylomeDB; O55203; -. DR TreeFam; TF319923; -. DR BioGRID-ORCS; 16826; 2 hits in 76 CRISPR screens. DR ChiTaRS; Ldb2; mouse. DR PRO; PR:O55203; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; O55203; Protein. DR Bgee; ENSMUSG00000039706; Expressed in embryonic brain and 230 other cell types or tissues. DR ExpressionAtlas; O55203; baseline and differential. DR GO; GO:0031252; C:cell leading edge; IDA:UniProtKB. DR GO; GO:0005730; C:nucleolus; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISS:UniProtKB. DR GO; GO:0005886; C:plasma membrane; ISO:MGI. DR GO; GO:0005667; C:transcription regulator complex; IDA:MGI. DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB. DR GO; GO:0030274; F:LIM domain binding; ISS:UniProtKB. DR GO; GO:0044085; P:cellular component biogenesis; IGI:MGI. DR GO; GO:0010669; P:epithelial structure maintenance; IGI:MGI. DR GO; GO:0001942; P:hair follicle development; IGI:MGI. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IBA:GO_Central. DR GO; GO:0007399; P:nervous system development; IBA:GO_Central. DR GO; GO:0044089; P:positive regulation of cellular component biogenesis; IGI:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI. DR GO; GO:0030334; P:regulation of cell migration; IMP:UniProtKB. DR GO; GO:0043549; P:regulation of kinase activity; IDA:UniProtKB. DR GO; GO:0035019; P:somatic stem cell population maintenance; IGI:MGI. DR Gene3D; 2.10.110.10; Cysteine Rich Protein; 1. DR InterPro; IPR041363; LID. DR InterPro; IPR029005; LIM-bd/SEUSS. DR PANTHER; PTHR10378; LIM DOMAIN-BINDING PROTEIN; 1. DR PANTHER; PTHR10378:SF8; LIM DOMAIN-BINDING PROTEIN 2; 1. DR Pfam; PF17916; LID; 1. DR Pfam; PF01803; LIM_bind; 1. DR PROSITE; PS51957; LID; 1. DR Genevisible; O55203; MM. PE 1: Evidence at protein level; KW Alternative splicing; Nucleus; Reference proteome; Ubl conjugation. FT CHAIN 1..373 FT /note="LIM domain-binding protein 2" FT /id="PRO_0000084388" FT DOMAIN 298..337 FT /note="LIM interaction domain (LID)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01302" FT REGION 244..287 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 327..373 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 264..287 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 342..373 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT VAR_SEQ 296..297 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072" FT /id="VSP_027829" FT VAR_SEQ 298..331 FT /note="DVMVVGEPTLMGGEFGDEDERLITRLENTQYDAA -> GLGAIPNCSLNPGR FT DGDLCHSTAVTPSGQFKEKH (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9192866" FT /id="VSP_014369" FT VAR_SEQ 332..373 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:16141072, FT ECO:0000303|PubMed:9192866" FT /id="VSP_014370" FT CONFLICT 272 FT /note="A -> G (in Ref. 1; AAB96884/AAB96886)" FT /evidence="ECO:0000305" FT CONFLICT 279 FT /note="A -> S (in Ref. 1; AAB96884/AAB96886)" FT /evidence="ECO:0000305" SQ SEQUENCE 373 AA; 42691 MW; 0748DBAEB5586AB4 CRC64; MSSTPHDPFY SSPFGPFYRR HTPYMVQPEY RIYEMNKRLQ SRTEDSDNLW WDAFATEFFE DDATLTLSFC LEDGPKRYTI GRTLIPRYFS TVFEGGVTDL YYILKHSKES YHNSSITVDC DQCAMVTQHG KPMFTKVCTE GRLILEFTFD DLMRIKTWHF TIRQYRELVP RSILAMHAQD PQVLDQLSKN ITRMGLTNFT LNYLRLCVIL EPMQELMSRH KTYNLSPRDC LKTCLFQKWQ RMVAPPAEPT RQPTTKRRKR KNSTSSTSNS SAGNTTNSAG SKKKTPAASL SLATQVPDVM VVGEPTLMGG EFGDEDERLI TRLENTQYDA ANGMDDEEDF NNSPALGNNS PWNSKPPATQ ETKSENAPPQ ASQ //