CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008728
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 LIM domain kinase 2 
Protein Synonyms/Alias
 LIMK-2 
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
251ALSTLDTKENLEGTLubiquitination[1]
271RRSNSISKSPGPSSPubiquitination[1]
279SPGPSSPKEPLLFSRubiquitination[1]
326GFFGQAIKVTHKATGubiquitination[1]
334VTHKATGKVMVMKELubiquitination[1]
339TGKVMVMKELIRCDEubiquitination[1]
350RCDEETQKTFLTEVKubiquitination[1]
357KTFLTEVKVMRSLDHubiquitination[1]
378IGVLYKDKKLNLLTEubiquitination[1]
407DPFPWQQKVRFAKGIubiquitination[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] 
Functional Description
 Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. 
Sequence Annotation
 DOMAIN 12 63 LIM zinc-binding 1.
 DOMAIN 72 124 LIM zinc-binding 2.
 DOMAIN 152 239 PDZ.
 DOMAIN 331 608 Protein kinase.
 NP_BIND 337 345 ATP (By similarity).
 ACT_SITE 451 451 By similarity.
 BINDING 360 360 ATP (By similarity).
 MOD_RES 210 210 Phosphothreonine.
 MOD_RES 293 293 Phosphoserine.
 MOD_RES 298 298 Phosphoserine.
 MOD_RES 505 505 Phosphothreonine; by ROCK1 and CDC42BP.  
Keyword
 3D-structure; Alternative splicing; ATP-binding; Complete proteome; Cytoplasm; Kinase; LIM domain; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Serine/threonine-protein kinase; Transferase; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 638 AA 
Protein Sequence
MGSYLSVPAY FTSRDLFRCS ECQDSLTNWY YEKDGKLYCP KDYWGKFGEF CHGCSLLMTG 60
PFMVAGEFKY HPECFACMSC KVIIEDGDAY ALVQHATLYC GKCHNEVVLA PMFERLSTES 120
VQEQLPYSVT LISMPATTEG RRGFSVSVES ACSNYATTVQ VKEVNRMHIS PNNRNAIHPG 180
DRILEINGTP VRTLRVEEVE DAISQTSQTL QLLIEHDPVS QRLDQLRLEA RLAPHMQNAG 240
HPHALSTLDT KENLEGTLRR RSLRRSNSIS KSPGPSSPKE PLLFSRDISR SESLRCSSSY 300
SQQIFRPCDL IHGEVLGKGF FGQAIKVTHK ATGKVMVMKE LIRCDEETQK TFLTEVKVMR 360
SLDHPNVLKF IGVLYKDKKL NLLTEYIEGG TLKDFLRSMD PFPWQQKVRF AKGIASGMAY 420
LHSMCIIHRD LNSHNCLIKL DKTVVVADFG LSRLIVEERK RAPMEKATTK KRTLRKNDRK 480
KRYTVVGNPY WMAPEMLNGK SYDETVDIFS FGIVLCEIIG QVYADPDCLP RTLDFGLNVK 540
LFWEKFVPTD CPPAFFPLAA ICCRLEPESR APPGAAGEGP GCADDEGPVR RQGKVTIKYD 600
PKELRKHLNL EEWILEQLTR LYDCQEEEIS ELEIDVDELL DMESDDAWAS RVKELLVDCY 660
KPTEAFISGL LDKIRAMQKL STPQKK 686 
Gene Ontology
 GO:0005801; C:cis-Golgi network; IEA:Compara.
 GO:0005737; C:cytoplasm; TAS:UniProtKB.
 GO:0005634; C:nucleus; TAS:UniProtKB.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; TAS:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0007283; P:spermatogenesis; IEA:Compara. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR001478; PDZ.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
 IPR001781; Znf_LIM. 
Pfam
 PF00412; LIM
 PF00595; PDZ
 PF07714; Pkinase_Tyr 
SMART
 SM00132; LIM
 SM00228; PDZ 
PROSITE
 PS00478; LIM_DOMAIN_1
 PS50023; LIM_DOMAIN_2
 PS50106; PDZ
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS