CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014471
UniProt Accession
Genbank Protein ID
 U48247 
Genbank Nucleotide ID
Protein Name
 PDZ and LIM domain protein 5 
Protein Synonyms/Alias
 Enigma homolog; Enigma-like PDZ and LIM domains protein 
Gene Name
 Pdlim5 
Gene Synonyms/Alias
 Enh 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
22GFRLQGGKDFNMPLTacetylation[1]
34PLTISSLKDGGKASQacetylation[1]
261PTHSDASKKRLIEDTacetylation[1]
346LRSAAAFKPVGSTSVacetylation[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 an important role in the heart development by scaffolding PKC to the Z-disk region. May play a role in the regulation of cardiomyocyte expansion. Isoforms lacking the LIM domains may negatively modulate the scaffolding activity of isoform 1. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May restrain postsynaptic growth of excitatory synapses. 
Sequence Annotation
 DOMAIN 1 85 PDZ.
 DOMAIN 413 472 LIM zinc-binding 1.
 DOMAIN 472 531 LIM zinc-binding 2.
 DOMAIN 531 591 LIM zinc-binding 3.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 111 111 Phosphoserine (By similarity).
 MOD_RES 137 137 Phosphoserine (By similarity).
 MOD_RES 228 228 Phosphoserine (By similarity).
 MOD_RES 313 313 Phosphoserine (By similarity).
 MOD_RES 331 331 Phosphoserine (By similarity).  
Keyword
 Acetylation; Alternative splicing; Cell junction; Cell membrane; Complete proteome; Cytoplasm; LIM domain; Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane; Reference proteome; Repeat; Synapse; Synaptosome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 591 AA 
Protein Sequence
MSNYNVSLVG PAPWGFRLQG GKDFNMPLTI SSLKDGGKAS QAHVRIGDVV LSIDGISAQG 60
MTHLEAQNKI KACTGSLNMT LQRASAAAKS EPVAVQKGEP KEVVKPVPIT SPAVSKVTST 120
TNMAYNKVPR PFGSVSSPKV TSIPSPSSAF TPAHAATSSH ASPPPVAAVT PPPLSASGLH 180
ASANPSAAQC SSPPNTGKPA VHVPRQPTVT SVCSESAQEL AEGQRRGSQG DIKQQNGPPR 240
KHIVERNTEF YHIPTHSDAS KKRLIEDTED WRPRTGTTQS RSFRILAQIT GTEHLKESEN 300
DNAKKANSTP EPSQQSASPL SAAESLESPG SNRPVVAGLR SAAAFKPVGS TSVKSPSWQR 360
PNQAAPSTGR ISNSASSSGT GAPMKPAVGP PQPSDQDTLV QRAEHIPAGK RTPMCAHCNQ 420
AIRGPFLVAL GKSWHPEEFN CAHCKNTMAY IGFVEEKGAL YCELCYEKFF APECGRCQRK 480
ILGEVINALK QTWHVSCFVC VACGKPIRNN VFHLEDGEPY CETDYYALFG TICRGCEFPI 540
EAGDMFLEAL GSTWHDTCFV CSVCCESLEG QTFFSKKDKP LCKKHAHSVN F 591 
Gene Ontology
 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0016020; C:membrane; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
 GO:0014069; C:postsynaptic density; IDA:UniProtKB.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
 GO:0030018; C:Z disc; IEA:Compara.
 GO:0003779; F:actin binding; IDA:UniProtKB.
 GO:0042805; F:actinin binding; IDA:UniProtKB.
 GO:0005080; F:protein kinase C binding; IDA:UniProtKB.
 GO:0047485; F:protein N-terminus binding; IMP:RGD.
 GO:0030159; F:receptor signaling complex scaffold activity; NAS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007507; P:heart development; NAS:UniProtKB.
 GO:0061001; P:regulation of dendritic spine morphogenesis; IDA:UniProtKB.
 GO:0051963; P:regulation of synapse assembly; IDA:UniProtKB. 
Interpro
 IPR001478; PDZ.
 IPR001781; Znf_LIM. 
Pfam
 PF00412; LIM
 PF00595; PDZ 
SMART
 SM00132; LIM
 SM00228; PDZ 
PROSITE
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2
 PS50106; PDZ 
PRINTS