Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00707
Entry Name
UniProt Accession
Theoretical PI
5.3
Molecular Weight
72254.06
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calcium-dependent protein kinase 2
Protein Synonyms/Alias
2.7.11.1; Calmodulin-domain protein kinase CDPK isoform 2;
Gene Name
CPK2
Gene Synonyms/Alias
At3g10660; F13M14.5; F18K10.28;
Created Date
10-FEB-2009
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNACVGPN
[1][2]
N-Myristoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] Lu SX, Hrabak EM. An Arabidopsis calcium-dependent protein kinase isassociated with the endoplasmic reticulum. Plant Physiol. 2002Mar;128(3):1008-21.[PMID:11891256]
[2] Benetka W, Mehlmer N, Maurer-Stroh S, Sammer M, Koranda M, Neumüller R,Betschinger J, Knoblich JA, Teige M, Eisenhaber F. Experimental testing ofpredicted myristoylation targets involved in asymmetric cell division andcalcium-dependent signalling. Cell Cycle. 2008 Dec;7(23):3709-19. Epub 2008 Dec13. Erratum in: Cell Cycle. 2009 Feb 1;8(3):508-9.[PMID:19029837]
Functional Description
May play a role in signal transduction pathways that involve calcium as a second messenger.
Sequence Annotation
Domain: 186 444 Protein kinase.
Domain: 487 522 EF-hand 1.
Domain: 523 558 EF-hand 2.
Domain: 559 594 EF-hand 3.
Domain: 595 628 EF-hand 4.
Nucleotide-binding: 192 200 ATP.
Region: 450 480 Autoinhibitory domain.
Active site: 310 310 Proton acceptor.
Binding site: 215 215 ATP.
Modified residue: 3 3 Deamidated asparagine.
Protein Length
646 AA.
Protein Sequence
(Canonical)
MGNACVGPNI SGNGFLQTVT AAMWRPRIGA EQASSSSHGN GQVSKEAASE PATDQVQNKP  60
PEPITMPSSK TNPETKLKPD LEIQPEEKKE KVLAEETKQK VVPEESKQEV PPEESKREVV  120
VQPESAKPET KSESKPETTK PETTSETKPE TKAEPQKPKH MRRVSSAGLR TESVLQRKTE  180
NFKEFYSLGR KLGQGQFGTT FLCLEKGTGN EYACKSISKR KLLTDEDVED VRREIQIMHH  240
LAGHPNVISI KGAYEDVVAV HLVMELCSGG ELFDRIIQRG HYTERKAAEL ARTIVGVLEA  300
CHSLGVMHRD LKPENFLFVS REEDSLLKTI DFGLSMFFKP DEVFTDVVGS PYYVAPEVLR  360
KRYGPESDVW SAGVIVYILL SGVPPFWAET EQGIFEQVLH GDLDFSSDPW PSISESAKDL  420
VRKMLVRDPK RRLTAHQVLC HPWVQIDGVA PDKPLDSAVL SRMKQFSAMN KFKKMALRVI  480
AESLSEEEIA GLKQMFKMID ADNSGQITFE ELKAGLKRVG ANLKESEILD LMQAADVDNS  540
GTIDYKEFIA ATLHLNKIER EDHLFAAFSY FDKDESGFIT PDELQQACEE FGVEDARIEE  600
MMRDVDQDKD GRIDYNEFVA MMQKGSIMGG PVKMGLENSI SISLKH                 646
FASTA
(Canonical)
>LipidDB-3702-00707|Q38870
MGNACVGPNISGNGFLQTVTAAMWRPRIGAEQASSSSHGNGQVSKEAASEPATDQVQNKP
PEPITMPSSKTNPETKLKPDLEIQPEEKKEKVLAEETKQKVVPEESKQEVPPEESKREVV
VQPESAKPETKSESKPETTKPETTSETKPETKAEPQKPKHMRRVSSAGLRTESVLQRKTE
NFKEFYSLGRKLGQGQFGTTFLCLEKGTGNEYACKSISKRKLLTDEDVEDVRREIQIMHH
LAGHPNVISIKGAYEDVVAVHLVMELCSGGELFDRIIQRGHYTERKAAELARTIVGVLEA
CHSLGVMHRDLKPENFLFVSREEDSLLKTIDFGLSMFFKPDEVFTDVVGSPYYVAPEVLR
KRYGPESDVWSAGVIVYILLSGVPPFWAETEQGIFEQVLHGDLDFSSDPWPSISESAKDL
VRKMLVRDPKRRLTAHQVLCHPWVQIDGVAPDKPLDSAVLSRMKQFSAMNKFKKMALRVI
AESLSEEEIAGLKQMFKMIDADNSGQITFEELKAGLKRVGANLKESEILDLMQAADVDNS
GTIDYKEFIAATLHLNKIEREDHLFAAFSYFDKDESGFITPDELQQACEEFGVEDARIEE
MMRDVDQDKDGRIDYNEFVAMMQKGSIMGGPVKMGLENSISISLKH
Gene Ontology
GO:0005789; C:endoplasmic reticulum membrane; IDA:TAIR
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW
Interpro
InterPro; IPR011992; EF-hand-dom_pair
InterPro; IPR018247; EF_Hand_1_Ca_BS
InterPro; IPR002048; EF_hand_dom
InterPro; IPR011009; Kinase-like_dom
InterPro; IPR000719; Prot_kinase_dom
InterPro; IPR017441; Protein_kinase_ATP_BS
InterPro; IPR002290; Ser/Thr_dual-sp_kinase
InterPro; IPR008271; Ser/Thr_kinase_AS
Pfam
Pfam; PF13499; EF-hand_7;
Pfam; PF00069; Pkinase;
SMART
SMART; SM00054; EFh;
SMART; SM00220; S_TKc;
PROSITE
PROSITE; PS00018; EF_HAND_1;
PROSITE; PS50222; EF_HAND_2;
PROSITE; PS00107; PROTEIN_KINASE_ATP;
PROSITE; PS50011; PROTEIN_KINASE_DOM;
PROSITE; PS00108; PROTEIN_KINASE_ST;
PRINTS