| Tag | Content |
|---|
| CPLM ID | CPLM-022040 |
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 | Homo sapiens (Human) |
NCBI Taxa ID | 9606 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 22 | GFRLQGGKDFNVPLS | ubiquitination | [1] | | 114 | APSVSLNKTARPFGA | ubiquitination | [1] | | 238 | AERYAPDKTSTVLTR | ubiquitination | [1] |
|
Reference | [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass. Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C. Nat Cell Biol. 2012 Oct;14(10):1089-98. [ PMID: 23000965] |
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. |
Keyword | 3D-structure; Alternative splicing; Complete proteome; Cytoplasm; Cytoskeleton; Developmental protein; Differentiation; Direct protein sequencing; LIM domain; Metal-binding; Osteogenesis; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Zinc. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 457 AA |
Protein Sequence | MDSFKVVLEG PAPWGFRLQG GKDFNVPLSI SRLTPGGKAA QAGVAVGDWV LSIDGENAGS 60
LTHIEAQNKI RACGERLSLG LSRAQPVQSK PQKASAPAAD PPRYTFAPSV SLNKTARPFG 120
APPPADSAPQ QNGQPLRPLV PDASKQRLME NTEDWRPRPG TGQSRSFRIL AHLTGTEFMQ 180
DPDEEHLKKS SQVPRTEAPA PASSTPQEPW PGPTAPSPTS RPPWAVDPAF AERYAPDKTS 240
TVLTRHSQPA TPTPLQSRTS IVQAAAGGVP GGGSNNGKTP VCHQCHKVIR GRYLVALGHA 300
YHPEEFVCSQ CGKVLEEGGF FEEKGAIFCP PCYDVRYAPS CAKCKKKITG EIMHALKMTW 360
HVHCFTCAAC KTPIRNRAFY MEEGVPYCER DYEKMFGTKC HGCDFKIDAG DRFLEALGFS 420
WHDTCFVCAI CQINLEGKTF YSKKDRPLCK SHAFSHV 457 |
Gene Ontology | GO:0015629; C:actin cytoskeleton; IDA:HPA. GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. GO:0005925; C:focal adhesion; IDA:HPA. GO:0001726; C:ruffle; IEA:Compara. GO:0001725; C:stress fiber; IEA:Compara. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0030036; P:actin cytoskeleton organization; IEA:Compara. 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. GO:0006898; P:receptor-mediated endocytosis; TAS:ProtInc. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |