CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-018039
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Serine/threonine-protein kinase 35 
Protein Synonyms/Alias
 CLP-36-interacting kinase 1; CLIK-1; PDLIM1-interacting kinase 1; Serine/threonine-protein kinase 35 L1 
Gene Name
 STK35 
Gene Synonyms/Alias
 CLIK1; PDIK1; STK35L1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
297RLVETSLKGERILGYubiquitination[1]
362HIVHRDLKPDNILITubiquitination[1]
378RSGTPILKVADFGLSubiquitination[1]
386VADFGLSKVCAGLAPubiquitination[1, 2]
503TSMSEGIKQLLKDMLubiquitination[3, 4]
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] 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]
 [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
  
Sequence Annotation
 DOMAIN 202 530 Protein kinase.
 NP_BIND 208 216 ATP (By similarity).
 ACT_SITE 360 360 Proton acceptor (By similarity).
 BINDING 231 231 ATP (Probable).  
Keyword
 ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome; Serine/threonine-protein kinase; Transferase. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 534 AA 
Protein Sequence
MGHQESPLAR APAGGAAYVK RLCKGLSWRE HVESHGSLGA QASPASAAAA EGSATRRARA 60
ATSRAARSRR QPGPGADHPQ AGAPGGKRAA RKWRCAGQVT IQGPAPPRPR AGRRDEAGGA 120
RAAPLLLPPP PAAMETGKDG ARRGTQSPER KRRSPVPRAP STKLRPAAAA RAMDPVAAEA 180
PGEAFLARRR PEGGGGSARP RYSLLAEIGR GSYGVVYEAV AGRSGARVAV KKIRCDAPEN 240
VELALAEFWA LTSLKRRHQN VVQFEECVLQ RNGLAQRMSH GNKSSQLYLR LVETSLKGER 300
ILGYAEEPCY LWFVMEFCEG GDLNQYVLSR RPDPATNKSF MLQLTSAIAF LHKNHIVHRD 360
LKPDNILITE RSGTPILKVA DFGLSKVCAG LAPRGKEGNQ DNKNVNVNKY WLSSACGSDF 420
YMAPEVWEGH YTAKADIFAL GIIIWAMIER ITFIDSETKK ELLGTYIKQG TEIVPVGEAL 480
LENPKMELHI PQKRRTSMSE GIKQLLKDML AANPQDRPDA FELETRMDQV TCAA 534 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. 
Interpro
 IPR011009; Kinase-like_dom.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00069; Pkinase 
SMART
  
PROSITE
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST 
PRINTS