CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019401
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Lymphokine-activated killer T-cell-originated protein kinase 
Protein Synonyms/Alias
 Cancer/testis antigen 84; CT84; MAPKK-like protein kinase; Nori-3; PDZ-binding kinase; Spermatogenesis-related protein kinase; SPK; T-LAK cell-originated protein kinase 
Gene Name
 PBK 
Gene Synonyms/Alias
 TOPK 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
8MEGISNFKTPSKLSEubiquitination[1]
12SNFKTPSKLSEKKKSacetylation[2]
64SHSPWAVKKINPICNacetylation[3]
65HSPWAVKKINPICNDubiquitination[1]
87KRLMDEAKILKSLHHubiquitination[1]
90MDEAKILKSLHHPNIubiquitination[1, 4]
132DLIEERYKASQDPFPubiquitination[1, 5]
155LNMARGLKYLHQEKKubiquitination[1]
169KLLHGDIKSSNVVIKubiquitination[1]
213YIGTEPWKPKEAVEEubiquitination[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] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [3] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [4] 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]
 [5] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724
Functional Description
 Phosphorylates MAP kinase p38. Seems to be active only in mitosis. May also play a role in the activation of lymphoid cells. When phosphorylated, forms a complex with TP53, leading to TP53 destabilization and attenuation of G2/M checkpoint during doxorubicin-induced DNA damage. 
Sequence Annotation
 DOMAIN 32 322 Protein kinase.
 NP_BIND 38 46 ATP (By similarity).
 REGION 320 322 PDZ-interaction.
 ACT_SITE 167 167 Proton acceptor (By similarity).
 BINDING 64 64 ATP (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 9 9 Phosphothreonine.
 MOD_RES 24 24 Phosphothreonine.
 MOD_RES 32 32 Phosphoserine.
 MOD_RES 59 59 Phosphoserine.  
Keyword
 Acetylation; ATP-binding; Complete proteome; Kinase; Nucleotide-binding; Phosphoprotein; Polymorphism; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 322 AA 
Protein Sequence
MEGISNFKTP SKLSEKKKSV LCSTPTINIP ASPFMQKLGF GTGVNVYLMK RSPRGLSHSP 60
WAVKKINPIC NDHYRSVYQK RLMDEAKILK SLHHPNIVGY RAFTEANDGS LCLAMEYGGE 120
KSLNDLIEER YKASQDPFPA AIILKVALNM ARGLKYLHQE KKLLHGDIKS SNVVIKGDFE 180
TIKICDVGVS LPLDENMTVT DPEACYIGTE PWKPKEAVEE NGVITDKADI FAFGLTLWEM 240
MTLSIPHINL SNDDDDEDKT FDESDFDDEA YYAALGTRPP INMEELDESY QKVIELFSVC 300
TNEDPKDRPS AAHIVEALET DV 322 
Gene Ontology
 GO:0005524; F:ATP binding; NAS:UniProtKB.
 GO:0004674; F:protein serine/threonine kinase activity; TAS:UniProtKB.
 GO:0007067; P:mitosis; NAS:UniProtKB. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
  
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS