CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-000408
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Zinc finger protein 185 
Protein Synonyms/Alias
 LIM domain protein ZNF185; P1-A 
Gene Name
 ZNF185 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
93IIRGVFTKPIDSSSQacetylation[1]
591ASEVSSGKPVSARYSubiquitination[2, 3, 4]
Reference
 [1] 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]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] 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]
 [4] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 May be involved in the regulation of cellular proliferation and/or differentiation. 
Sequence Annotation
 DOMAIN 627 689 LIM zinc-binding.  
Keyword
 Alternative splicing; Cell junction; Complete proteome; Cytoplasm; Cytoskeleton; LIM domain; Metal-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 689 AA 
Protein Sequence
MSISALGGRT KGKPLPPGEE ERNNVLKQMK VRTTLKGDKS WITKQDESEG RTIELPSGRS 60
RATSFSSAGE VPKPRPPSTR APTGYIIRGV FTKPIDSSSQ PQQQFPKANG TPKSAASLVR 120
TANAGPPRPS SSGYKMTTED YKKLAPYNIR RSSTSGDTEE EEEEEVVPFS SDEQKRRSEA 180
ASGVLRRTAP REHSYVLSAA KKSTGPTQET QAPFIAKRVE VVEEDGPSEK SQDPPALARS 240
TPGSNSADGG RTKASRAIWI ECLPSMPSPA GSQELSSRGE EIVRLQILTP RAGLRLVAPD 300
VEGMRSSPGN KDKEAPCSRE LQRDLAGEEA FRAPNTDAAR SSAQLSDGNV GSGATGSRPE 360
GLAAVDIGSE RGSSSATSVS AVPADRKSNS TAAQEDAKAD PKGALADYEG KDVATRVGEA 420
WQERPGAPRG GQGDPAVPAQ QPADPSTPER QSSPSGSEQL VRRESCGSSV LTDFEGKDVA 480
TKVGEAWQDR PGAPRGGQGD PAVPTQQPAD PSTPEQQNSP SGSEQFVRRE SCTSRVRSPS 540
SCMVTVTVTA TSEQPHIYIP APASELDSSS TTKGILFVKE YVNASEVSSG KPVSARYSNV 600
SSIEDSFAME KKPPCGSTPY SERTTGGICT YCNREIRDCP KITLEHLGIC CHEYCFKCGI 660
CSKPMGDLLD QIFIHRDTIH CGKCYEKLF 689 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005925; C:focal adhesion; IEA:UniProtKB-SubCell.
 GO:0008270; F:zinc ion binding; TAS:ProtInc. 
Interpro
 IPR001781; Znf_LIM. 
Pfam
  
SMART
 SM00132; LIM 
PROSITE
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2 
PRINTS