CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-030908
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein kinase C eta type 
Protein Synonyms/Alias
 Protein kinase C, eta, isoform CRA_a; cDNA FLJ57944, highly similar to Protein kinase C eta type (EC 2.7.11.13) 
Gene Name
 PRKCH 
Gene Synonyms/Alias
 hCG_22361 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
73NINKVDSKIAEQRFGubiquitination[1]
160GNISPTSKLVSRSTLubiquitination[1, 2, 3]
176RQGKESSKEGNGIGVubiquitination[1, 3]
202EFIRVLGKGSFGKVMubiquitination[1, 3]
214KVMLARVKETGDLYAubiquitination[3]
243VECTMTEKRILSLARubiquitination[1, 3]
320GIIYRDLKLDNVLLDubiquitination[3]
430ILKSFMTKNPTMRLGubiquitination[3]
454ILRHPFFKEIDWAQLubiquitination[2, 3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
  
Sequence Annotation
  
Keyword
 ATP-binding; Complete proteome; Kinase; Metal-binding; Nucleotide-binding; Reference proteome; Serine/threonine-protein kinase; Transferase; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 522 AA 
Protein Sequence
MRRRVHQING HKFMATYLRQ PTYCSHCREF IWGVFGKQGY QCQVCTCVVH KRCHHLIVTA 60
CTCQNNINKV DSKIAEQRFG INIPHKFSIH NYKVPTFCDH CGSLLWGIMR QGLQCKICKM 120
NVHIRCQANV APNCGVNAVE LAKTLAGMGL QPGNISPTSK LVSRSTLRRQ GKESSKEGNG 180
IGVNSSNRLG IDNFEFIRVL GKGSFGKVML ARVKETGDLY AVKVLKKDVI LQDDDVECTM 240
TEKRILSLAR NHPFLTQLFC CFQTPDRLFF VMEFVNGGDL MFHIQKSRRF DEARARFYAA 300
EIISALMFLH DKGIIYRDLK LDNVLLDHEG HCKLADFGMC KEGICNGVTT ATFCGTPDYI 360
APEILQEMLY GPAVDWWAMG VLLYEMLCGH APFEAENEDD LFEAILNDEV VYPTWLHEDA 420
TGILKSFMTK NPTMRLGSLT QGGEHAILRH PFFKEIDWAQ LNHRQIEPPF RPRIKSREDV 480
SNFDPDFIKE EPVLTPIDEG HLPMINQDEF RNFSYVSPEL QP 522 
Gene Ontology
 GO:0005829; C:cytosol; IEA:Compara.
 GO:0005886; C:plasma membrane; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0004699; F:calcium-independent protein kinase C activity; IEA:Compara.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Compara.
 GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; IEA:Compara.
 GO:0070528; P:protein kinase C signaling cascade; IEA:Compara. 
Interpro
 IPR000961; AGC-kinase_C.
 IPR020454; DAG/PE-bd.
 IPR011009; Kinase-like_dom.
 IPR017892; Pkinase_C.
 IPR002219; Prot_Kinase_C-like_PE/DAG-bd.
 IPR000719; Prot_kinase_cat_dom.
 IPR017441; Protein_kinase_ATP_BS.
 IPR002290; Ser/Thr_dual-sp_kinase_dom.
 IPR008271; Ser/Thr_kinase_AS. 
Pfam
 PF00130; C1_1
 PF00069; Pkinase
 PF00433; Pkinase_C 
SMART
 SM00109; C1
 SM00133; S_TK_X
 SM00220; S_TKc 
PROSITE
 PS51285; AGC_KINASE_CTER
 PS00107; PROTEIN_KINASE_ATP
 PS50011; PROTEIN_KINASE_DOM
 PS00108; PROTEIN_KINASE_ST
 PS00479; ZF_DAG_PE_1
 PS50081; ZF_DAG_PE_2 
PRINTS
 PR00008; DAGPEDOMAIN.