UniProt Accession

 PDLI5_MOUSE; Q8CI51; Q3UGD0; Q9QYN0; Q9QYN1; Q9QYN2 

Genbank Protein ID

 AB016586; AB016587; AB016588; AK147999; BC037476 

Genbank Nucleotide ID

 BAA88827.1; BAA88828.1; BAA88829.1; BAE28279.1; AAH37476.1 

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

 Mus musculus (Mouse) 

NCBI Taxa ID

 10090 

Lysine Modification

Position	Peptide	Type	References
89	QRASAAAKSEPVSVQ	ubiquitination	[1]
105	GEPKEVVKPVPITSP	acetylation	[2, 3]
350	LRSAAAFKPVGSTSV	acetylation	[3, 4]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [4] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441] 

Functional Description

 May play an important role in the heart development by scaffolding PKC to the Z-disk region. Isoform 2 and isoform 3 may negatively modulate the scaffolding activity of isoform 1. May play a role in the regulation of cardiomyocyte expansion. Overexpression promotes the development of heart hypertrophy. Contributes to the regulation of dendritic spine morphogenesis in neurons. May restrain postsynaptic growth of excitatory synapses (By similarity). 

Sequence Annotation

 DOMAIN 2 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.
 MOD_RES 313 313 Phosphoserine (By similarity).
 MOD_RES 335 335 Phosphoserine.  

Keyword

 3D-structure; 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

Gene Ontology

 GO:0030054; C:cell junction; IEA:UniProtKB-KW.
 GO:0005829; C:cytosol; ISS:UniProtKB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
 GO:0014069; C:postsynaptic density; ISS:UniProtKB.
 GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-KW.
 GO:0030018; C:Z disc; IDA:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0061001; P:regulation of dendritic spine morphogenesis; ISS:UniProtKB.
 GO:0051963; P:regulation of synapse assembly; ISS: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