KCC2_YEAST - dbPTM
KCC2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC2_YEAST
UniProt AC P22517
Protein Name Calcium/calmodulin-dependent protein kinase II
Gene Name CMK2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 447
Subcellular Localization
Protein Description Important in cellular regulation..
Protein Sequence MPKESEVINSEFHVDVQDPERLNGHPVAKFINKLSGQPESYVNRTNYIFGRTLGAGSFGVVRQARKLSTNEDVAIKILLKKALQGNNVQLQMLYEELSILQKLSHPNIVSFKDWFESKDKFYIVTQLATGGELFDRILSRGKFTEVDAVEIIVQILGAVEYMHSKNVVHRDLKPENVLYVDKSENSPLVIADFGIAKQLKGEEDLIYKAAGSLGYVAPEVLTQDGHGKPCDIWSIGVITYTLLCGYSPFIAESVEGFMEECTASRYPVTFHMPYWDNISIDVKRFILKALRLNPADRPTATELLDDPWITSKRVETSNILPDVKKGFSLRKKLRDAIEIVKLNNRIKRLRNMYSLGDDGDNDIEENSLNESLLDGVTHSLDDLRLQSQKKGGELTEEQMKLKSALTKDAFVQIVKAATKNKHKVLAGEEEDDSKKTLHDDRESKSED
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
29AcetylationLNGHPVAKFINKLSG
HCCCHHHHHHHHHCC		47.1925381059
33AcetylationPVAKFINKLSGQPES
HHHHHHHHHCCCCHH		38.9324489116
68PhosphorylationVRQARKLSTNEDVAI
HHHHHCCCCCHHHHH		32.0222369663
69PhosphorylationRQARKLSTNEDVAIK
HHHHCCCCCHHHHHH		53.7322369663
112AcetylationHPNIVSFKDWFESKD
CCCCCCHHHHHHCCC		46.6924489116
173UbiquitinationNVVHRDLKPENVLYV
CCCCCCCCHHHEEEE		55.3523749301
200AcetylationFGIAKQLKGEEDLIY
CCHHHHHCCCHHHHH		62.8824489116
299PhosphorylationLNPADRPTATELLDD
CCCCCCCCHHHHCCC		47.2929688323
301PhosphorylationPADRPTATELLDDPW
CCCCCCHHHHCCCCC		29.6429688323
310PhosphorylationLLDDPWITSKRVETS
HCCCCCCCCCCEECC		25.0729688323
316PhosphorylationITSKRVETSNILPDV
CCCCCEECCCCCCCH		24.98-
353PhosphorylationIKRLRNMYSLGDDGD
HHHHHHHHHCCCCCC		12.3222369663
354PhosphorylationKRLRNMYSLGDDGDN
HHHHHHHHCCCCCCC		18.3322369663
367PhosphorylationDNDIEENSLNESLLD
CCCCCCCCCCHHHHH		35.5322369663
371PhosphorylationEENSLNESLLDGVTH
CCCCCCHHHHHHHCC		32.9122369663
377PhosphorylationESLLDGVTHSLDDLR
HHHHHHHCCCHHHHH		15.9822369663
379PhosphorylationLLDGVTHSLDDLRLQ
HHHHHCCCHHHHHHH		24.9122369663
387PhosphorylationLDDLRLQSQKKGGEL
HHHHHHHHHHCCCCC		48.86-
403PhosphorylationEEQMKLKSALTKDAF
HHHHHHHHHHCHHHH		38.6628889911
406PhosphorylationMKLKSALTKDAFVQI
HHHHHHHCHHHHHHH		26.9617330950
407AcetylationKLKSALTKDAFVQIV
HHHHHHCHHHHHHHH		48.1624489116
443PhosphorylationTLHDDRESKSED---
CCCCCCHHCCCC---		42.2317287358
445PhosphorylationHDDRESKSED-----
CCCCHHCCCC-----		57.1727214570
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of KCC2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCC2_YEAST !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of KCC2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CALM_YEASTCMD1physical
16554755
YMD7_YEASTYML037Cphysical
16319894
VHR2_YEASTVHR2physical
16319894
YP013_YEASTCMR3physical
16319894
AKR1_YEASTAKR1physical
16319894
ASND1_YEASTYML096Wphysical
16319894
PAH1_YEASTPAH1physical
16319894
NSR1_YEASTNSR1physical
16319894
HSF_YEASTHSF1physical
18793336
OCA1_YEASTOCA1genetic
19269370
KIN4_YEASTKIN4genetic
19269370
VCX1_YEASTVCX1genetic
18806210
CANB_YEASTCNB1genetic
18806210
EDE1_YEASTEDE1physical
20489023
SYP1_YEASTSYP1physical
20489023
ARPC3_YEASTARC18physical
21460040
ATG29_YEASTATG29physical
21460040
AVT6_YEASTAVT6physical
21460040
TCPD_YEASTCCT4physical
21460040
CDA1_YEASTCDA1physical
21460040
DBR1_YEASTDBR1physical
21460040
DSE3_YEASTDSE3physical
21460040
ERS1_YEASTERS1physical
21460040
GRE3_YEASTGRE3physical
21460040
GLRX4_YEASTGRX4physical
21460040
JIP5_YEASTJIP5physical
21460040
LSM1_YEASTLSM1physical
21460040
MAG_YEASTMAG1physical
21460040
MRC1_YEASTMRC1physical
21460040
RM49_YEASTMRP49physical
21460040
MRP8_YEASTMRP8physical
21460040
MSN5_YEASTMSN5physical
21460040
NET1_YEASTNET1physical
21460040
NUP53_YEASTNUP53physical
21460040
OPY1_YEASTOPY1physical
21460040
OXA1_YEASTOXA1physical
21460040
PIR1_YEASTPIR1physical
21460040
PP4R3_YEASTPSY2physical
21460040
RAD2_YEASTRAD2physical
21460040
RFC5_YEASTRFC5physical
21460040
GPP1_YEASTGPP1physical
21460040
RIM13_YEASTRIM13physical
21460040
RL17B_YEASTRPL17Bphysical
21460040
RPAB2_YEASTRPO26physical
21460040
SGT1_YEASTSGT1physical
21460040
SODM_YEASTSOD2physical
21460040
SPP1_YEASTSPP1physical
21460040
SYF1_YEASTSYF1physical
21460040
TBG_YEASTTUB4physical
21460040
TVP18_YEASTTVP18physical
21460040
VATH_YEASTVMA13physical
21460040
YBS1_YEASTYBR071Wphysical
21460040
YB70_YEASTYBR220Cphysical
21460040
VFA1_YEASTVFA1physical
21460040
TDA10_YEASTTDA10physical
21460040
CG11_YEASTCLN1genetic
21127252
RPD3_YEASTRPD3genetic
21127252
BUB1_YEASTBUB1genetic
21127252
KAPA_YEASTTPK1genetic
21127252
CTK3_YEASTCTK3genetic
21127252
ATM_YEASTTEL1genetic
21127252
RSC2_YEASTRSC2genetic
21127252
EDE1_YEASTEDE1genetic
22511765
PSB6_YEASTPRE7genetic
27708008
GPI10_YEASTGPI10genetic
27708008
SMD1_YEASTSMD1genetic
27708008
MED6_YEASTMED6genetic
27708008
SPC97_YEASTSPC97genetic
27708008
FNTA_YEASTRAM2genetic
27708008
GPI12_YEASTGPI12genetic
27708008
DBP6_YEASTDBP6genetic
27708008
TBF1_YEASTTBF1genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
PHB2_YEASTPHB2genetic
27708008
SNF6_YEASTSNF6genetic
27708008
VPS53_YEASTVPS53genetic
27708008
YJ24_YEASTKCH1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
NCBP2_YEASTCBC2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KCC2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-68; SER-371; SER-379 ANDSER-443, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-379, ANDMASS SPECTROMETRY.
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-443, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-371, ANDMASS SPECTROMETRY.

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