CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-013010
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 PDZ and LIM domain protein 7 
Protein Synonyms/Alias
 LIM mineralization protein; LMP; Protein enigma 
Gene Name
 Pdlim7 
Gene Synonyms/Alias
 Enigma 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
22GFRLQGGKDFNVPLSubiquitination[1]
238AERYAPDKTSTVLTRacetylation[2]
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] 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
Functional Description
 May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity). 
Sequence Annotation
 DOMAIN 1 85 PDZ.
 DOMAIN 280 338 LIM zinc-binding 1.
 DOMAIN 339 398 LIM zinc-binding 2.
 DOMAIN 399 457 LIM zinc-binding 3.
 MOD_RES 247 247 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; LIM domain; Metal-binding; Osteogenesis; Phosphoprotein; Reference proteome; Repeat; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 457 AA 
Protein Sequence
MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LNIDGENAGS 60
LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKALTPPAD PPRYTFAPSA SLNKTARPFG 120
APPPTDSTLR QNGQLLRQPV PDASKQRLME DTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ 180
DPDEEFMKKS SQVPRTEAPA PASTIPQESW PGPTTPSPTS RPPWAVDPAF AERYAPDKTS 240
TVLTRHSQPA TPTPLQNRTS IVQAAAGGGT GGGSNNGKTP VCHQCHKIIR GRYLVALGHA 300
YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP SCYDVRYAPN CAKCKKKITG EIMHALKMTW 360
HVHCFTCAAC KTPIRNRAFY MEEGAPYCER DYEKMFGTKC RGCDFKIDAG DRFLEALGFS 420
WHDTCFVCAI CQINLEGKTF YSKKDKPLCK SHAFSHV 457 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:MGI.
 GO:0005925; C:focal adhesion; IEA:Compara.
 GO:0001726; C:ruffle; IDA:MGI.
 GO:0001725; C:stress fiber; IDA:MGI.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0030036; P:actin cytoskeleton organization; IPI:MGI.
 GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
 GO:0007275; P:multicellular organismal development; IEA:UniProtKB-KW.
 GO:0001503; P:ossification; IEA:UniProtKB-KW.
 GO:0045669; P:positive regulation of osteoblast differentiation; IEA:Compara. 
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