CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016365
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lipoma-preferred partner homolog 
Protein Synonyms/Alias
  
Gene Name
 Lpp 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
109QQGNPGGKTLEERRSacetylation[1]
109QQGNPGGKTLEERRSubiquitination[2]
328QVQPNTWKREAAYAPubiquitination[2]
400ELEHLTKKMLYDMENubiquitination[2]
462QPFYAVEKKAYCEPCubiquitination[2]
Reference
 [1] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 May play a structural role at sites of cell adhesion in maintaining cell shape and motility. In addition to these structural functions, it may also be implicated in signaling events and activation of gene transcription. May be involved in signal transduction from cell adhesion sites to the nucleus allowing successful integration of signals arising from soluble factors and cell-cell adhesion sites. Also suggested to serve as a scaffold protein upon which distinct protein complexes are assembled in the cytoplasm and in the nucleus (By similarity). 
Sequence Annotation
 DOMAIN 415 474 LIM zinc-binding 1.
 DOMAIN 475 535 LIM zinc-binding 2.
 DOMAIN 536 604 LIM zinc-binding 3.
 MOD_RES 245 245 Phosphotyrosine.
 MOD_RES 302 302 Phosphotyrosine.  
Keyword
 Activator; Alternative splicing; Cell adhesion; Cell junction; Complete proteome; Cytoplasm; LIM domain; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 613 AA 
Protein Sequence
MSHPSWLPPK STGEPLGHVP ARMETTHSFG NPSISVSTQQ PPKKYAPVVA PKPKYNPYKQ 60
PGGEGDLLPP PPPPLEDPGT IPPGPGHFPP PPPLDEGAFK VQQGNPGGKT LEERRSSLDA 120
EIDSLTSILA DLECSSPYKP RPPQGSASSI ASPPVSTPVT GHKRMVIPQQ PPLTATKKSA 180
TKPQPAPQAA PIPVTPIGTL KPQPQPVPAS YTTASTSSRP TFNVQVKSAQ PSPHYMAGPS 240
SGQIYGPGPR GYNNQPVPVS GQCPPPPTCV GTDYAYIPPS GHPPESGYGY TSNQGRYYEP 300
YYAAGPSYGG RSEGDTAYGQ QVQPNTWKRE AAYAPPASGN QNHPGMYPVS GPKKTYITDP 360
VSAPCAPPLQ PKGGYPGPMG PPSIPPSFRP EDELEHLTKK MLYDMENPPA DDYFGRCARC 420
GENVVGEGTG CTAMDQVFHV DCFTCIVCDV KLRGQPFYAV EKKAYCEPCY INTLEQCSVC 480
SKPIMERILR ATGKAYHPHC FTCVMCHRSL DGIPFTVDAC GLIHCIEDFH KKFAPRCSVC 540
KEPIMPAPGQ EETVRIVALD RDFHVHCYRC EDCGGLLSEG DNQGCYPLDG HILCKTCNSA 600
RIRVLTAKAS TDL 613 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. 
Interpro
 IPR001781; Znf_LIM. 
Pfam
 PF00412; LIM 
SMART
 SM00132; LIM 
PROSITE
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2 
PRINTS