CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016191
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 LIM domain-binding protein 1 
Protein Synonyms/Alias
 LDB-1; Carboxyl-terminal LIM domain-binding protein 2; CLIM-2; LIM domain-binding factor CLIM2; hLdb1; Nuclear LIM interactor 
Gene Name
 LDB1 
Gene Synonyms/Alias
 CLIM2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
76YRIFELNKRLQNWTEubiquitination[1, 2]
144TELYYVLKHPKEAFHubiquitination[3]
271LSPRDCLKTCLFQKWubiquitination[1, 4]
277LKTCLFQKWQRMVAPubiquitination[1]
393ANSPWNSKPPSSQESacetylation[5]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377] 
Functional Description
 Binds to the LIM domain of a wide variety of LIM domain- containing transcription factors. May regulate the transcriptional activity of LIM-containing proteins by determining specific partner interactions. Play a role in the development of interneurons and motor neurons in cooperation with LHX3 and ISL1. Acts synergistically with LHX1/LIM1 in axis formation and activation of gene expression. Acts with LMO2 in the regulation of red blood cell development, maintaining erythroid precursors in an immature state (By similarity). 
Sequence Annotation
 REGION 336 374 LIM-binding domain (LID) (By similarity).
 MOD_RES 2 2 N-acetylserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Developmental protein; Nucleus; Polymorphism; Reference proteome; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 411 AA 
Protein Sequence
MSVGCACPGC SSKSFKLYSP KEPPNGNAFP PFHPGTMLDR DVGPTPMYPP TYLEPGIGRH 60
TPYGNQTDYR IFELNKRLQN WTEECDNLWW DAFTTEFFED DAMLTITFCL EDGPKRYTIG 120
RTLIPRYFRS IFEGGATELY YVLKHPKEAF HSNFVSLDCD QGSMVTQHGK PMFTQVCVEG 180
RLYLEFMFDD MMRIKTWHFS IRQHRELIPR SILAMHAQDP QMLDQLSKNI TRCGLSNSTL 240
NYLRLCVILE PMQELMSRHK TYSLSPRDCL KTCLFQKWQR MVAPPAEPTR QQPSKRRKRK 300
MSGGSTMSSG GGNTNNSNSK KKSPASTFAL SSQVPDVMVV GEPTLMGGEF GDEDERLITR 360
LENTQFDAAN GIDDEDSFNN SPALGANSPW NSKPPSSQES KSENPTSQAS Q 411 
Gene Ontology
 GO:0005911; C:cell-cell junction; IEA:Compara.
 GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
 GO:0005667; C:transcription factor complex; IDA:BHF-UCL.
 GO:0003682; F:chromatin binding; IEA:Compara.
 GO:0001158; F:enhancer sequence-specific DNA binding; IEA:Compara.
 GO:0030274; F:LIM domain binding; ISS:UniProtKB.
 GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
 GO:0003714; F:transcription corepressor activity; TAS:ProtInc.
 GO:0009948; P:anterior/posterior axis specification; IEA:Compara.
 GO:0022607; P:cellular component assembly; IEA:Compara.
 GO:0021702; P:cerebellar Purkinje cell differentiation; IEA:Compara.
 GO:0010669; P:epithelial structure maintenance; IEA:Compara.
 GO:0001702; P:gastrulation with mouth forming second; IEA:Compara.
 GO:0001942; P:hair follicle development; IEA:Compara.
 GO:0060322; P:head development; IEA:Compara.
 GO:0043973; P:histone H3-K4 acetylation; ISS:BHF-UCL.
 GO:0045647; P:negative regulation of erythrocyte differentiation; ISS:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0030182; P:neuron differentiation; ISS:UniProtKB.
 GO:0045785; P:positive regulation of cell adhesion; IEA:Compara.
 GO:0046985; P:positive regulation of hemoglobin biosynthetic process; ISS:BHF-UCL.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IMP:BHF-UCL.
 GO:0032784; P:regulation of DNA-dependent transcription, elongation; ISS:BHF-UCL.
 GO:0035019; P:somatic stem cell maintenance; IEA:Compara.
 GO:0006366; P:transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; NAS:UniProtKB.
 GO:0000972; P:transcription-dependent tethering of RNA polymerase II gene DNA at nuclear periphery; ISS:BHF-UCL.
 GO:0016055; P:Wnt receptor signaling pathway; IEA:Compara. 
Interpro
 IPR002691; LIM-dom-bd. 
Pfam
  
SMART
  
PROSITE
  
PRINTS