CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014156
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
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
109QRGNPGGKTLEERRSacetylation[1]
163STPVTGHKRMVIPQQacetylation[1]
481QPFYAVEKKAYCEPCacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
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. 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 434 493 LIM zinc-binding 1.
 DOMAIN 494 554 LIM zinc-binding 2.
 DOMAIN 555 623 LIM zinc-binding 3.
 MOD_RES 241 241 Phosphotyrosine (By similarity).  
Keyword
 Activator; 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
 632 AA 
Protein Sequence
MSHPSWLPPR STGEPLGHVP ARMETTHSFG TPSISVSTQQ PPKKFAPVVA PKPKYNPYKQ 60
PGGEGDFLPP PPPPLEDPGT IPSGSGHFPP PPPLDEGAFI VQRGNPGGKT LEERRSSLDA 120
EIDSLTSILA DLECSSPYKP RAPPGSSSSI ASPPVSTPVT GHKRMVIPQQ PPLTATKKSA 180
TKPQAIPIPV TPIGTLKPQP QPVPASYSTA STSSRPAFNV QVKSAQPSTH YMTGSSSGQM 240
YGPGSRSYNT QQVPLSAQCP PPTTCAGTDY AYIPPSGQQA ESGFGYTSNQ GRYFEPFFAA 300
CPSYGGRNEA DPAYGQQVQP NTWKREPGYA APGAGNQNQP GMYSVSGPKK TYITDPVSAP 360
CAPPVQPKER LVKNQKVLQN VVDDRVHGLR KSGFPAPMGP PSVPPSFRPE DELEHLTKKM 420
LYDMENPPAD DYFGRCARCG ENVVGEGTGC TAMDQVFHVD CFTCMVCDIK LRGQPFYAVE 480
KKAYCEPCYI NTLEQCSVCS KPIMERILRA TGKAYHPHCF TCVMCHRSLD GIPFTVDACG 540
LIHCIEDFHK KFAPRCSVCK EPIMPAPGQE ETVRIVALDR DFHVHCYRCE DCGGLLSEGD 600
NQGCYPLDGH ILCKSCNSAR IRVLTAKAST DL 632 
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