Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-3702-00688
Entry Name
UniProt Accession
Theoretical PI
5.83
Molecular Weight
60362.56
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Calcium-dependent protein kinase 9
Protein Synonyms/Alias
2.7.11.1; Calmodulin-domain protein kinase CDPK isoform 9;
Gene Name
CPK9
Gene Synonyms/Alias
At3g20410; MQC12.23;
Created Date
10-FEB-2009
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
2
Canonical
******MGNCFAKNH
[1]
N-Myristoylation
Organism
Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxa ID
3702
Reference
[1] 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: 91 349 Protein kinase.
Domain: 392 427 EF-hand 1.
Domain: 428 463 EF-hand 2.
Domain: 464 499 EF-hand 3.
Domain: 500 534 EF-hand 4.
Nucleotide-binding: 97 105 ATP.
Region: 355 385 Autoinhibitory domain.
Active site: 215 215 Proton acceptor.
Binding site: 120 120 ATP.
Modified residue: 69 69 Phosphoserine.
Protein Length
541 AA.
Protein Sequence
(Canonical)
MGNCFAKNHG LMKPQQNGNT TRSVEVGVTN QDPPSYTPQA RTTQQPEKPG SVNSQPPPWR  60
AAAAAPGLSP KTTTKSNSIL ENAFEDVKLF YTLGKELGRG QFGVTYLCTE NSTGKKYACK  120
SISKKKLVTK ADKDDMRREI QIMQHLSGQP NIVEFKGAYE DEKAVNLVME LCAGGELFDR  180
IIAKGHYTER AAASVCRQIV NVVKICHFMG VLHRDLKPEN FLLSSKDEKA LIKATDFGLS  240
VFIEEGKVYR DIVGSAYYVA PEVLRRRYGK EVDIWSAGII LYILLSGVPP FWAETEKGIF  300
DAILEGHIDF ESQPWPSISS SAKDLVRRML TADPKRRISA ADVLQHPWLR EGGEASDKPI  360
DSAVLSRMKQ FRAMNKLKKL ALKVIAENID TEEIQGLKAM FANIDTDNSG TITYEELKEG  420
LAKLGSKLTE AEVKQLMDAA DVDGNGSIDY IEFITATMHR HRLESNENLY KAFQHFDKDS  480
SGYITIDELE SALKEYGMGD DATIKEVLSD VDSDNDGRIN YEEFCAMMRS GNPQQQQPRL  540
F                                                                  541
FASTA
(Canonical)
>LipidDB-3702-00688|Q38868
MGNCFAKNHGLMKPQQNGNTTRSVEVGVTNQDPPSYTPQARTTQQPEKPGSVNSQPPPWR
AAAAAPGLSPKTTTKSNSILENAFEDVKLFYTLGKELGRGQFGVTYLCTENSTGKKYACK
SISKKKLVTKADKDDMRREIQIMQHLSGQPNIVEFKGAYEDEKAVNLVMELCAGGELFDR
IIAKGHYTERAAASVCRQIVNVVKICHFMGVLHRDLKPENFLLSSKDEKALIKATDFGLS
VFIEEGKVYRDIVGSAYYVAPEVLRRRYGKEVDIWSAGIILYILLSGVPPFWAETEKGIF
DAILEGHIDFESQPWPSISSSAKDLVRRMLTADPKRRISAADVLQHPWLREGGEASDKPI
DSAVLSRMKQFRAMNKLKKLALKVIAENIDTEEIQGLKAMFANIDTDNSGTITYEELKEG
LAKLGSKLTEAEVKQLMDAADVDGNGSIDYIEFITATMHRHRLESNENLYKAFQHFDKDS
SGYITIDELESALKEYGMGDDATIKEVLSDVDSDNDGRINYEEFCAMMRSGNPQQQQPRL
F
Gene Ontology
GO:0005886; C:plasma membrane; IDA:TAIR
GO:0005524; F:ATP binding; IEA:UniProtKB-KW
GO:0005509; F:calcium ion binding; IEA:InterPro
GO:0004683; F:calmodulin-dependent protein kinase activity; ISS:TAIR
GO:0007165; P:signal transduction; TAS:TAIR
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; PF00036; EF-hand_1;
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