CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031667
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 LIM domain kinase 2 
Protein Synonyms/Alias
  
Gene Name
 LIMK2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
194ALSTLDTKENLEGTLubiquitination[1]
214RRSNSISKSPGPSSPubiquitination[1]
222SPGPSSPKEPLLFSRubiquitination[1]
269GFFGQAIKVTHKATGubiquitination[1]
277VTHKATGKVMVMKELubiquitination[1]
282TGKVMVMKELIRCDEubiquitination[1]
293RCDEETQKTFLTEVKubiquitination[1]
300KTFLTEVKVMRSLDHubiquitination[1, 2]
321IGVLYKDKKLNLLTEubiquitination[1]
350DPFPWQQKVRFAKGIubiquitination[1]
596DAWASRVKELLVDCYubiquitination[1, 2, 3]
604ELLVDCYKPTEAFISubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [3] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931
Functional Description
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; LIM domain; Metal-binding; Nucleotide-binding; Reference proteome; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 629 AA 
Protein Sequence
MTGPFMVAGE FKYHPECFAC MSCKVIIEDG DAYALVQHAT LYCGKCHNEV VLAPMFERLS 60
TESVQEQLPY SVTLISMPAT TEGRRGFSVS VESACSNYAT TVQVKEVNRM HISPNNRNAI 120
HPGDRILEIN GTPVRTLRVE EVEDAISQTS QTLQLLIEHD PVSQRLDQLR LEARLAPHMQ 180
NAGHPHALST LDTKENLEGT LRRRSLRRSN SISKSPGPSS PKEPLLFSRD ISRSESLRCS 240
SSYSQQIFRP CDLIHGEVLG KGFFGQAIKV THKATGKVMV MKELIRCDEE TQKTFLTEVK 300
VMRSLDHPNV LKFIGVLYKD KKLNLLTEYI EGGTLKDFLR SMDPFPWQQK VRFAKGIASG 360
MAYLHSMCII HRDLNSHNCL IKLDKTVVVA DFGLSRLIVE ERKRAPMEKA TTKKRTLRKN 420
DRKKRYTVVG NPYWMAPEML NGKSYDETVD IFSFGIVLCE IIGQVYADPD CLPRTLDFGL 480
NVKLFWEKFV PTDCPPAFFP LAAICCRLEP ESRAPPGAAG EGPGCADDEG PVRRQGKVTI 540
KYDPKELRKH LNLEEWILEQ LTRLYDCQEE EISELEIDVD ELLDMESDDA WASRVKELLV 600
DCYKPTEAFI SGLLDKIRAM QKLSTPQKK 629 
Gene Ontology
 GO:0005801; C:cis-Golgi network; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0042325; P:regulation of phosphorylation; IEA:InterPro.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR001478; PDZ.
 IPR008025; PP1_inhibitor.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR001781; Znf_LIM. 
Pfam
 PF00412; LIM
 PF00595; PDZ
 PF00069; Pkinase
 PF05361; PP1_inhibitor 
SMART
 SM00132; LIM
 SM00228; PDZ 
PROSITE
 PS50023; LIM_DOMAIN_2
 PS50106; PDZ
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM 
PRINTS