RCK2_YEAST - dbPTM
RCK2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RCK2_YEAST
UniProt AC P38623
Protein Name Serine/threonine-protein kinase RCK2
Gene Name RCK2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 610
Subcellular Localization Cytoplasm .
Protein Description Serine/threonine-protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment..
Protein Sequence MLKIKALFSKKKPDQADLSQESKKPFKGKTRSSGTNNKDVSQITSSPKKSFQDKNIVQYPSVVADDHHMKSLTDELVTTIDSDSSPSDNITTENVETVTSVPAIDVHESSEGQLSSDPLISDESLSEQSEIISDIQDDSTDDDNMEDEIPEKSFLEQKELIGYKLINKIGEGAFSKVFRAIPAKNSSNEFLTKNYKAVAIKVIKKADLSSINGDHRKKDKGKDSTKTSSRDQVLKEVALHKTVSAGCSQIVAFIDFQETDSYYYIIQELLTGGEIFGEIVRLTYFSEDLSRHVIKQLALAVKHMHSLGVVHRDIKPENLLFEPIEFTRSIKPKLRKSDDPQTKADEGIFTPGVGGGGIGIVKLADFGLSKQIFSKNTKTPCGTVGYTAPEVVKDEHYSMKVDMWGIGCVLYTMLCGFPPFYDEKIDTLTEKISRGEYTFLKPWWDEISAGAKNAVAKLLELEPSKRYDIDQFLDDPWLNTFDCLPKEGESSQKKAGTSERRHPHKKQFQLFQRDSSLLFSPAAVAMRDAFDIGNAVKRTEEDRMGTRGGLGSLAEDEELEDSYSGAQGDEQLEQNMFQLTLDTSTILQRRKKVQENDVGPTIPISATIRE
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
19PhosphorylationKPDQADLSQESKKPF
CCCCCCCCHHHCCCC		32.2330377154
30PhosphorylationKKPFKGKTRSSGTNN
CCCCCCCCCCCCCCC		44.4421440633
32PhosphorylationPFKGKTRSSGTNNKD
CCCCCCCCCCCCCCC		38.0528889911
33PhosphorylationFKGKTRSSGTNNKDV
CCCCCCCCCCCCCCH		46.4728889911
35PhosphorylationGKTRSSGTNNKDVSQ
CCCCCCCCCCCCHHH		37.2529136822
38UbiquitinationRSSGTNNKDVSQITS
CCCCCCCCCHHHHCC		62.6723749301
41PhosphorylationGTNNKDVSQITSSPK
CCCCCCHHHHCCCCC		26.4622369663
44PhosphorylationNKDVSQITSSPKKSF
CCCHHHHCCCCCHHC		18.6022369663
45PhosphorylationKDVSQITSSPKKSFQ
CCHHHHCCCCCHHCC		46.3925521595
46PhosphorylationDVSQITSSPKKSFQD
CHHHHCCCCCHHCCC		31.8922369663
50PhosphorylationITSSPKKSFQDKNIV
HCCCCCHHCCCCCCC		33.9821082442
59PhosphorylationQDKNIVQYPSVVADD
CCCCCCCCCCCCCCC		6.1321440633
61PhosphorylationKNIVQYPSVVADDHH
CCCCCCCCCCCCCHH		25.0421440633
158AcetylationEKSFLEQKELIGYKL
CCHHHHHHHHHCHHH		45.1524489116
164AcetylationQKELIGYKLINKIGE
HHHHHCHHHHHHHCC		37.3624489116
168AcetylationIGYKLINKIGEGAFS
HCHHHHHHHCCCHHH		45.1324489116
176AcetylationIGEGAFSKVFRAIPA
HCCCHHHHHHHHCCC		38.6524489116
186PhosphorylationRAIPAKNSSNEFLTK
HHCCCCCCCCCHHCC		33.5622369663
187PhosphorylationAIPAKNSSNEFLTKN
HCCCCCCCCCHHCCC		50.1822369663
193SuccinylationSSNEFLTKNYKAVAI
CCCCHHCCCCEEEEE		61.5023954790
2012-HydroxyisobutyrylationNYKAVAIKVIKKADL
CCEEEEEEEHHHCCH		28.33-
229PhosphorylationKDSTKTSSRDQVLKE
CCCCCCCCHHHHHHH		45.1428889911
235AcetylationSSRDQVLKEVALHKT
CCHHHHHHHHHHHHH		51.8124489116
350PhosphorylationKADEGIFTPGVGGGG
CHHCCCCCCCCCCCC		19.7428889911
370AcetylationLADFGLSKQIFSKNT
HHHHCCCHHHHCCCC		53.0824489116
370UbiquitinationLADFGLSKQIFSKNT
HHHHCCCHHHHCCCC		53.0824961812
375UbiquitinationLSKQIFSKNTKTPCG
CCHHHHCCCCCCCCC		58.8622817900
379PhosphorylationIFSKNTKTPCGTVGY
HHCCCCCCCCCCCCC		23.0522890988
383PhosphorylationNTKTPCGTVGYTAPE
CCCCCCCCCCCCCCH		19.9222890988
393AcetylationYTAPEVVKDEHYSMK
CCCCHHHCCCCCCCC		63.6824489116
431UbiquitinationKIDTLTEKISRGEYT
HHHHHHHHHHCCCCC		40.5223749301
515PhosphorylationFQLFQRDSSLLFSPA
HHHHHCCCHHHCCHH		25.6922369663
516PhosphorylationQLFQRDSSLLFSPAA
HHHHCCCHHHCCHHH		33.1222369663
520PhosphorylationRDSSLLFSPAAVAMR
CCCHHHCCHHHHHHH		17.3822890988
537UbiquitinationFDIGNAVKRTEEDRM
HHHCHHHHCCHHHHC		51.7124961812
605PhosphorylationVGPTIPISATIRE--
CCCCCCCCCEECC--		17.6325752575
607PhosphorylationPTIPISATIRE----
CCCCCCCEECC----		17.4921440633
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 RCK2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
520SPhosphorylation

10805732
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 RCK2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FET4_YEASTFET4physical
11805837
HOG1_YEASTHOG1physical
11805837
VPS41_YEASTVPS41physical
11805837
HOG1_YEASTHOG1physical
14735355
HOG1_YEASTHOG1physical
10805732
ZRC1_YEASTZRC1physical
15341652
ROD1_YEASTROD1physical
15341652
IRC6_YEASTIRC6physical
15341652
TRS65_YEASTTRS65physical
15341652
RCK2_YEASTRCK2physical
8939941
ZRC1_YEASTZRC1genetic
15341652
HOG1_YEASTHOG1physical
16554755
SLA1_YEASTSLA1physical
16319894
VCX1_YEASTVCX1physical
16319894
YN11A_YEASTYNL284C-Aphysical
16319894
SEC2_YEASTSEC2physical
16319894
IRC8_YEASTIRC8physical
16319894
RPA12_YEASTRPA12physical
16319894
YP150_YEASTYPL150Wphysical
16319894
VHS2_YEASTVHS2physical
16319894
STB3_YEASTSTB3physical
16319894
FPK1_YEASTFPK1physical
16319894
ADD37_YEASTADD37physical
16319894
KKQ8_YEASTKKQ8physical
16319894
MLF3_YEASTMLF3physical
16319894
AIM3_YEASTAIM3physical
16319894
RRM3_YEASTRRM3physical
16319894
YP091_YEASTNVJ2physical
16319894
YHT1_YEASTYHR131Cphysical
16319894
ROD1_YEASTROD1physical
16319894
YL257_YEASTYLR257Wphysical
16319894
ROG3_YEASTROG3physical
16319894
HSP42_YEASTHSP42physical
16319894
PHSG_YEASTGPH1physical
16319894
GLO3_YEASTGLO3physical
16319894
PIK1_YEASTPIK1physical
16319894
FAL1_YEASTFAL1physical
16319894
HOG1_YEASTHOG1physical
18212044
SET2_YEASTSET2genetic
19269370
SWI6_YEASTSWI6genetic
19269370
PIG1_YEASTPIG1genetic
19269370
ATPF_YEASTATP4physical
20489023
ACK1_YEASTACK1physical
21460040
APN1_YEASTAPN1physical
21460040
AVO2_YEASTAVO2physical
21460040
YM44_YEASTYMR178Wphysical
21460040
IPL1_YEASTIPL1physical
21460040
CG13_YEASTCLN3genetic
21127252
CTK1_YEASTCTK1genetic
21127252
DAL81_YEASTDAL81genetic
27708008
COXM1_YEASTCMC1genetic
27708008
ERG6_YEASTERG6genetic
27708008
SCS7_YEASTSCS7genetic
27708008
HOG1_YEASTHOG1physical
26775127
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of RCK2_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-45; SER-46; SER-50;SER-187; THR-350; SER-516 AND SER-605, 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-45; SER-46 AND SER-50,AND MASS 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-46, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46, AND MASSSPECTROMETRY.
"Rck2 kinase is a substrate for the osmotic stress-activated mitogen-activated protein kinase Hog1.";
Bilsland-Marchesan E., Arino J., Saito H., Sunnerhagen P., Posas F.;
Mol. Cell. Biol. 20:3887-3895(2000).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-520, ENZYME REGULATION, ANDINTERACTION WITH HOG1.

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