LDB1_HUMAN
ID LDB1_HUMAN Reviewed; 411 AA.
AC Q86U70; B4DUC4; O75479; O96010; Q1EQX1; Q9UGM4;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 2.
DT 03-AUG-2022, entry version 171.
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=hLdb1;
DE AltName: Full=Nuclear LIM interactor;
GN Name=LDB1; Synonyms=CLIM2;
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 3).
RC TISSUE=Craniofacial;
RX PubMed=9799849; DOI=10.1007/s003359900899;
RA Semina E.V., Altherr M.R., Murray J.C.;
RT "Cloning and chromosomal localization of two novel human genes encoding
RT LIM-domain binding factors CLIM1 and CLIM2/LDB1/NLI.";
RL Mamm. Genome 9:921-924(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10640831; DOI=10.1159/000015377;
RA Drechsler M., Schumacher V., Friedrich S., Wildhardt G., Giesler S.,
RA Schroth A., Bodem J., Royer-Pokora B.;
RT "Genomic structure, alternative transcripts and chromosome location of the
RT human LIM domain binding protein gene LDB1.";
RL Cytogenet. Cell Genet. 87:119-124(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10083735; DOI=10.1007/s100380050120;
RA Ueki N., Seki N., Yano K., Ohira M., Saito T., Masuho Y., Muramatsu M.;
RT "Isolation and chromosomal assignment of human genes encoding cofactor of
RT LIM homeodomain proteins, CLIM1 and CLIM2.";
RL J. Hum. Genet. 44:112-115(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Fetal brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Fetal brain;
RA Phillips J.C., Goldman D.A., Wiggs J.L.;
RT "Cloning, characterization, and physical mapping of the human homologs of
RT the mouse C-LIM gene.";
RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
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 [10]
RP INTERACTION WITH YWHAZ.
RX PubMed=16959763; DOI=10.1074/mcp.m600147-mcp200;
RA Angrand P.O., Segura I., Voelkel P., Ghidelli S., Terry R., Brajenovic M.,
RA Vintersten K., Klein R., Superti-Furga G., Drewes G., Kuster B.,
RA Bouwmeester T., Acker-Palmer A.;
RT "Transgenic mouse proteomics identifies new 14-3-3-associated proteins
RT involved in cytoskeletal rearrangements and cell signaling.";
RL Mol. Cell. Proteomics 5:2211-2227(2006).
RN [11]
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=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP INTERACTION WITH ESR1, MUTAGENESIS OF 245-LEU--LEU-249, AND MISCELLANEOUS.
RX PubMed=19117995; DOI=10.1158/0008-5472.can-08-1630;
RA Johnsen S.A., Guengoer C., Prenzel T., Riethdorf S., Riethdorf L.,
RA Taniguchi-Ishigaki N., Rau T., Tursun B., Furlow J.D., Sauter G.,
RA Scheffner M., Pantel K., Gannon F., Bach I.;
RT "Regulation of estrogen-dependent transcription by the LIM cofactors CLIM
RT and RLIM in breast cancer.";
RL Cancer Res. 69:128-136(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [16]
RP INTERACTION WITH PRDM1.
RX PubMed=32417234; DOI=10.1016/j.bbagrm.2020.194577;
RA Fong H.T., Hagen T., Inoue T.;
RT "LDB1 and the SWI/SNF complex participate in both transcriptional
RT activation and repression by Caenorhabditis elegans BLIMP1/PRDM1.";
RL Biochim. Biophys. Acta 1863:194577-194577(2020).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 334-368 ALONE AND IN COMPLEX WITH
RP LMO2, AND SUBUNIT.
RX PubMed=21076045; DOI=10.1182/blood-2010-07-293357;
RA El Omari K., Hoosdally S.J., Tuladhar K., Karia D., Vyas P., Patient R.,
RA Porcher C., Mancini E.J.;
RT "Structure of the leukemia oncogene LMO2: implications for the assembly of
RT a hematopoietic transcription factor complex.";
RL Blood 117:2146-2156(2011).
RN [18]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-299.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
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 (By similarity).
CC {ECO:0000250|UniProtKB:P70662}.
CC -!- SUBUNIT: Forms homodimers and heterodimers. Interacts with and
CC activates LHX1/LIM1. Interacts with the LIM domains of ISL1 and LMO2.
CC Can assemble in a complex with LMO2 and TAL1/SCL but does not interact
CC with TAL1/SCL directly. Strongly interacts with the LIM2 domain of
CC LMX1A and more weakly with the LIM1 domain. Homodimerization is not
CC required for, and does not effect, LMX1A-binding. Component of a
CC nuclear TAL-1 complex composed at least of CBFA2T3, LDB1, TAL1 and
CC TCF3. Interacts with LHX6 and LHX9. At neuronal promoters, forms a
CC complex with LHX3 involved in the specification of interneurons, in
CC motor neurons, it is displaced by ISL1 to form a ternary complex in
CC which ISL1 contacts both LHX3 and LDB1 (By similarity). Interacts with
CC ESR1. Interacts with SLK; leading to negatively regulate SLK kinase
CC activity (By similarity). Interacts with YWHAZ (PubMed:16959763).
CC Interacts with PRDM1/BLIMP1 (PubMed:32417234).
CC {ECO:0000250|UniProtKB:P70662, ECO:0000269|PubMed:16959763,
CC ECO:0000269|PubMed:19117995, ECO:0000269|PubMed:21076045,
CC ECO:0000269|PubMed:32417234}.
CC -!- INTERACTION:
CC Q86U70; P50458: LHX2; NbExp=3; IntAct=EBI-677177, EBI-12179869;
CC Q86U70; Q9UPM6: LHX6; NbExp=5; IntAct=EBI-677177, EBI-10258746;
CC Q86U70; Q68G74: LHX8; NbExp=5; IntAct=EBI-677177, EBI-8474075;
CC Q86U70; P25800: LMO1; NbExp=5; IntAct=EBI-677177, EBI-8639312;
CC Q86U70; P25791: LMO2; NbExp=6; IntAct=EBI-677177, EBI-739696;
CC Q86U70; P61968: LMO4; NbExp=6; IntAct=EBI-677177, EBI-2798728;
CC Q86U70; O60663-2: LMX1B; NbExp=3; IntAct=EBI-677177, EBI-10258690;
CC Q86U70; Q9BWW4: SSBP3; NbExp=4; IntAct=EBI-677177, EBI-2902395;
CC Q86U70-2; P42858: HTT; NbExp=3; IntAct=EBI-11979761, EBI-466029;
CC Q86U70-2; Q9BXS1: IDI2; NbExp=4; IntAct=EBI-11979761, EBI-766127;
CC Q86U70-2; P61371: ISL1; NbExp=7; IntAct=EBI-11979761, EBI-3906896;
CC Q86U70-2; Q96A47: ISL2; NbExp=3; IntAct=EBI-11979761, EBI-18560216;
CC Q86U70-2; P48742: LHX1; NbExp=3; IntAct=EBI-11979761, EBI-11990598;
CC Q86U70-2; P50458: LHX2; NbExp=3; IntAct=EBI-11979761, EBI-12179869;
CC Q86U70-2; Q9UBR4-2: LHX3; NbExp=5; IntAct=EBI-11979761, EBI-12039345;
CC Q86U70-2; Q969G2: LHX4; NbExp=4; IntAct=EBI-11979761, EBI-2865388;
CC Q86U70-2; Q9UPM6: LHX6; NbExp=5; IntAct=EBI-11979761, EBI-10258746;
CC Q86U70-2; Q68G74: LHX8; NbExp=6; IntAct=EBI-11979761, EBI-8474075;
CC Q86U70-2; Q9NQ69: LHX9; NbExp=3; IntAct=EBI-11979761, EBI-10175218;
CC Q86U70-2; P25800: LMO1; NbExp=6; IntAct=EBI-11979761, EBI-8639312;
CC Q86U70-2; P25791-3: LMO2; NbExp=7; IntAct=EBI-11979761, EBI-11959475;
CC Q86U70-2; Q8TAP4-4: LMO3; NbExp=6; IntAct=EBI-11979761, EBI-11742507;
CC Q86U70-2; P61968: LMO4; NbExp=8; IntAct=EBI-11979761, EBI-2798728;
CC Q86U70-2; O60663-2: LMX1B; NbExp=4; IntAct=EBI-11979761, EBI-10258690;
CC Q86U70-2; Q9BWW4: SSBP3; NbExp=5; IntAct=EBI-11979761, EBI-2902395;
CC Q86U70-2; Q9BWG4: SSBP4; NbExp=4; IntAct=EBI-11979761, EBI-744719;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q86U70-1; Sequence=Displayed;
CC Name=2; Synonyms=b;
CC IsoId=Q86U70-3; Sequence=VSP_027830, VSP_027831, VSP_027832;
CC Name=3; Synonyms=a;
CC IsoId=Q86U70-2; Sequence=VSP_027830;
CC -!- TISSUE SPECIFICITY: Expressed in a wide range of adult tissues
CC including brain, heart, skeletal muscle, colon, thymus, spleen, kidney,
CC liver, small intestine, lung and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:16815859}.
CC -!- DOMAIN: The dimerization domain is located in the N-terminus.
CC {ECO:0000250}.
CC -!- PTM: Ubiquitinated by RLIM/RNF12, leading to its degradation by the
CC proteasome. {ECO:0000250}.
CC -!- MISCELLANEOUS: Acts as a negative coregulator of ESR1-mediated
CC transcription in breast cancer cells.
CC -!- MISCELLANEOUS: [Isoform 2]: Due to intron retention. Lacks LIM-binding
CC domain. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the LDB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45409.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/LDB1ID41135ch10q24.html";
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DR EMBL; AF068652; AAC77818.1; -; mRNA.
DR EMBL; AJ243098; CAB45409.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB016485; BAA31991.1; -; mRNA.
DR EMBL; AB250384; BAE95402.1; -; mRNA.
DR EMBL; AF064491; AAC28341.1; -; mRNA.
DR EMBL; BT007054; AAP35703.1; -; mRNA.
DR EMBL; AK300588; BAG62286.1; -; mRNA.
DR EMBL; AL500527; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000482; AAH00482.1; -; mRNA.
DR EMBL; BC009246; AAH09246.1; -; mRNA.
DR CCDS; CCDS44472.1; -. [Q86U70-1]
DR CCDS; CCDS7528.1; -. [Q86U70-2]
DR RefSeq; NP_001106878.1; NM_001113407.2. [Q86U70-1]
DR RefSeq; NP_003884.1; NM_003893.4. [Q86U70-2]
DR PDB; 2XJY; X-ray; 2.40 A; B=334-368.
DR PDB; 2XJZ; X-ray; 2.80 A; I/J/K/L/M=334-368.
DR PDB; 2YPA; X-ray; 2.80 A; D=336-375.
DR PDB; 6TYD; X-ray; 2.80 A; V=56-285.
DR PDBsum; 2XJY; -.
DR PDBsum; 2XJZ; -.
DR PDBsum; 2YPA; -.
DR PDBsum; 6TYD; -.
DR AlphaFoldDB; Q86U70; -.
DR SMR; Q86U70; -.
DR BioGRID; 114384; 84.
DR CORUM; Q86U70; -.
DR DIP; DIP-31826N; -.
DR IntAct; Q86U70; 63.
DR MINT; Q86U70; -.
DR STRING; 9606.ENSP00000392466; -.
DR iPTMnet; Q86U70; -.
DR PhosphoSitePlus; Q86U70; -.
DR BioMuta; LDB1; -.
DR DMDM; 158518615; -.
DR EPD; Q86U70; -.
DR jPOST; Q86U70; -.
DR MassIVE; Q86U70; -.
DR MaxQB; Q86U70; -.
DR PaxDb; Q86U70; -.
DR PeptideAtlas; Q86U70; -.
DR PRIDE; Q86U70; -.
DR ProteomicsDB; 69771; -. [Q86U70-1]
DR ProteomicsDB; 69772; -. [Q86U70-2]
DR ProteomicsDB; 69773; -. [Q86U70-3]
DR Antibodypedia; 17969; 280 antibodies from 30 providers.
DR DNASU; 8861; -.
DR Ensembl; ENST00000361198.9; ENSP00000354616.5; ENSG00000198728.11. [Q86U70-2]
DR Ensembl; ENST00000673968.1; ENSP00000501277.1; ENSG00000198728.11. [Q86U70-1]
DR GeneID; 8861; -.
DR KEGG; hsa:8861; -.
DR MANE-Select; ENST00000673968.1; ENSP00000501277.1; NM_001113407.3; NP_001106878.1.
DR UCSC; uc001kuk.6; human. [Q86U70-1]
DR CTD; 8861; -.
DR DisGeNET; 8861; -.
DR GeneCards; LDB1; -.
DR HGNC; HGNC:6532; LDB1.
DR HPA; ENSG00000198728; Low tissue specificity.
DR MIM; 603451; gene.
DR neXtProt; NX_Q86U70; -.
DR OpenTargets; ENSG00000198728; -.
DR PharmGKB; PA30316; -.
DR VEuPathDB; HostDB:ENSG00000198728; -.
DR eggNOG; KOG2181; Eukaryota.
DR GeneTree; ENSGT00390000005639; -.
DR HOGENOM; CLU_032597_0_0_1; -.
DR InParanoid; Q86U70; -.
DR OMA; KMSVGCA; -.
DR OrthoDB; 849287at2759; -.
DR PhylomeDB; Q86U70; -.
DR TreeFam; TF319923; -.
DR PathwayCommons; Q86U70; -.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9752946; Expression and translocation of olfactory receptors.
DR SignaLink; Q86U70; -.
DR SIGNOR; Q86U70; -.
DR BioGRID-ORCS; 8861; 110 hits in 1101 CRISPR screens.
DR ChiTaRS; LDB1; human.
DR EvolutionaryTrace; Q86U70; -.
DR GeneWiki; LDB1; -.
DR GenomeRNAi; 8861; -.
DR Pharos; Q86U70; Tbio.
DR PRO; PR:Q86U70; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q86U70; protein.
DR Bgee; ENSG00000198728; Expressed in right uterine tube and 151 other tissues.
DR ExpressionAtlas; Q86U70; baseline and differential.
DR Genevisible; Q86U70; HS.
DR GO; GO:1990907; C:beta-catenin-TCF complex; IDA:FlyBase.
DR GO; GO:0031252; C:cell leading edge; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; ISS:UniProtKB.
DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; IPI:UniProtKB.
DR GO; GO:0030274; F:LIM domain binding; IPI:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR GO; GO:0043621; F:protein self-association; IEA:Ensembl.
DR GO; GO:0061629; F:RNA polymerase II-specific DNA-binding transcription factor binding; IPI:BHF-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IEA:InterPro.
DR GO; GO:0009948; P:anterior/posterior axis specification; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0022607; P:cellular component assembly; IEA:Ensembl.
DR GO; GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Ensembl.
DR GO; GO:0010669; P:epithelial structure maintenance; IEA:Ensembl.
DR GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
DR GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR GO; GO:0043973; P:histone H3-K4 acetylation; ISS:BHF-UCL.
DR GO; GO:0048382; P:mesendoderm development; IEA:Ensembl.
DR GO; GO:0045647; P:negative regulation of erythrocyte differentiation; ISS: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; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0030182; P:neuron differentiation; ISS:UniProtKB.
DR GO; GO:0045785; P:positive regulation of cell adhesion; IEA:Ensembl.
DR GO; GO:0046985; P:positive regulation of hemoglobin biosynthetic process; ISS:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0051893; P:regulation of focal adhesion assembly; ISS:UniProtKB.
DR GO; GO:0043549; P:regulation of kinase activity; ISS:UniProtKB.
DR GO; GO:0034243; P:regulation of transcription elongation from RNA polymerase II promoter; ISS:BHF-UCL.
DR GO; GO:0035019; P:somatic stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; ISS:BHF-UCL.
DR GO; GO:0016055; P:Wnt signaling pathway; IEA:Ensembl.
DR IDEAL; IID00282; -.
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:0007744|PubMed:19413330"
FT CHAIN 2..411
FT /note="LIM domain-binding protein 1"
FT /id="PRO_0000084384"
FT DOMAIN 336..375
FT /note="LIM interaction domain (LID)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01302"
FT REGION 283..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:0007744|PubMed:19413330"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P70662"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P70662"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:10083735,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16815859, ECO:0000303|PubMed:9799849,
FT ECO:0000303|Ref.5, ECO:0000303|Ref.6"
FT /id="VSP_027830"
FT VAR_SEQ 336..352
FT /note="DVMVVGEPTLMGGEFGD -> VSISAFFSLLGCPTTHP (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16815859"
FT /id="VSP_027831"
FT VAR_SEQ 353..411
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:16815859"
FT /id="VSP_027832"
FT VARIANT 299
FT /note="R -> Q (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs990101456)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036366"
FT MUTAGEN 245..249
FT /note="LCVIL->ACVAA: Abolishes interaction with ESR1."
FT /evidence="ECO:0000269|PubMed:19117995"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 68..78
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 87..97
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 98..108
FT /evidence="ECO:0007829|PDB:6TYD"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 115..119
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 124..133
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 152..168
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 175..191
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 194..207
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:6TYD"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 220..223
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 232..235
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 237..261
FT /evidence="ECO:0007829|PDB:6TYD"
FT HELIX 266..281
FT /evidence="ECO:0007829|PDB:6TYD"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:2XJZ"
FT TURN 346..349
FT /evidence="ECO:0007829|PDB:2XJY"
FT STRAND 355..357
FT /evidence="ECO:0007829|PDB:2XJZ"
FT STRAND 359..362
FT /evidence="ECO:0007829|PDB:2XJY"
SQ SEQUENCE 411 AA; 46533 MW; 5BB5348A36044580 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 MVAPPAEPTR QQPSKRRKRK
MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF GDEDERLITR
LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES KSENPTSQAS Q
