SKS1_YEAST - dbPTM
SKS1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKS1_YEAST
UniProt AC Q12505
Protein Name Serine/threonine-protein kinase SKS1
Gene Name SKS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 502
Subcellular Localization
Protein Description May have a role in glucose regulation..
Protein Sequence MLSDCLLNNFRITAQIGSGAYGLVFHVVDILTSREYAVKTVFKSSSMDEFYNKNGLNNNSQVARTTLLQTQLYHFFKSFQKKLFLPSVDLDSILQLTENELNRLPHYREIAFQLRVQSHGNIVKIHQVLESSIATFIVMDYYDRDLFTSIVDDKHFVNHGILIKKVFLQLCSALDHCHRLGIYHCDIKPENVLLDRNDNAYLCDFGLSTKSKYLAPNVCVGSSYYMAPERILYCLNTTTNGIHVDECCSSLPTDTGDIWSLGIILINLTCIRNPWLKAHQKEDNTFQHFANDNNVLKKILPISDELFTVLTKILQLNPYTRIDMKTLMSEVSSLTSFTREGPLSQVPILSSEVYMTHIIRNENLFLSDLSHFSADQEQQQQQQQQQQQVQEQEQEQKQEQIQNQEQAQQQQEEEDAEPESDIPSTYNSDGSMEKYEYTNNHNNSTFLTSSMDSTPYQSDIDDVSASKDCKFQQDTLRNRLLCLQMNFSTLTDGPNEKWLPDY
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
77UbiquitinationTQLYHFFKSFQKKLF
HHHHHHHHHHHHHHC		49.7917644757
188UbiquitinationGIYHCDIKPENVLLD
CEECCCCCCHHEEEC		32.7817644757
210UbiquitinationCDFGLSTKSKYLAPN
CCCCCCCCCCCCCCC		41.3917644757
297UbiquitinationANDNNVLKKILPISD
CCCCCHHHHHHCCCH		33.2217644757
298UbiquitinationNDNNVLKKILPISDE
CCCCHHHHHHCCCHH		45.3617644757
312UbiquitinationELFTVLTKILQLNPY
HHHHHHHHHHCCCCC		36.9417644757
344PhosphorylationFTREGPLSQVPILSS
CCCCCCHHHCCCCCC		32.0627017623
350PhosphorylationLSQVPILSSEVYMTH
HHHCCCCCCEEHHHH		25.7727017623
351PhosphorylationSQVPILSSEVYMTHI
HHCCCCCCEEHHHHH		27.8627017623
354PhosphorylationPILSSEVYMTHIIRN
CCCCCEEHHHHHHHC		7.7027017623
356PhosphorylationLSSEVYMTHIIRNEN
CCCEEHHHHHHHCCC		7.7027017623
435PhosphorylationSDGSMEKYEYTNNHN
CCCCEEEEEECCCCC		10.8127017623
437PhosphorylationGSMEKYEYTNNHNNS
CCEEEEEECCCCCCC		16.2127017623
448PhosphorylationHNNSTFLTSSMDSTP
CCCCEEEECCCCCCC		17.9827017623
456PhosphorylationSSMDSTPYQSDIDDV
CCCCCCCCCCCCCCC		22.2727017623
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 SKS1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKS1_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 SKS1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
THIL_YEASTERG10physical
11805837
VPS53_YEASTVPS53physical
16319894
CDC15_YEASTCDC15physical
16319894
SYEC_YEASTGUS1physical
16319894
MTW1_YEASTMTW1physical
16319894
VHS2_YEASTVHS2physical
16319894
OSH2_YEASTOSH2physical
16319894
HPH2_YEASTFRT2physical
16319894
SAS10_YEASTSAS10physical
16319894
VHR2_YEASTVHR2physical
16319894
RCM1_YEASTRCM1physical
16319894
CH10_YEASTHSP10physical
16319894
SOL2_YEASTSOL2physical
16319894
AQR1_YEASTAQR1physical
16319894
YP013_YEASTCMR3physical
16319894
6P21_YEASTPFK26physical
16319894
RSC30_YEASTRSC30physical
16319894
SEF1_YEASTSEF1physical
16319894
ASND1_YEASTYML096Wphysical
16319894
PLP1_YEASTPLP1physical
16319894
IGD1_YEASTIGD1physical
16319894
AVT3_YEASTAVT3physical
16319894
TREA_YEASTNTH1physical
16319894
MGA1_YEASTMGA1physical
16319894
KAD2_YEASTADK1physical
16319894
PMT2_YEASTPMT2physical
16319894
UTR1_YEASTUTR1physical
16319894
SS100_YEASTSPS100physical
16319894
YMZ2_YEASTYMR102Cphysical
16319894
INP54_YEASTINP54physical
16319894
COQ8_YEASTCOQ8physical
16319894
DCOR_YEASTSPE1physical
16319894
AAD16_YEASTYPL088Wphysical
16319894
STE3_YEASTSTE3physical
16319894
VATC_YEASTVMA5physical
16319894
PMT6_YEASTPMT6physical
16319894
JJJ1_YEASTJJJ1physical
16319894
MDJ1_YEASTMDJ1physical
16319894
MBA1_YEASTMBA1genetic
20093466
VHC1_YEASTVHC1genetic
20093466
VPS41_YEASTVPS41genetic
20093466
UME6_YEASTUME6genetic
20093466
EAF1_YEASTEAF1genetic
20093466
PUS3_YEASTDEG1genetic
20093466
YGY5_YEASTYGL235Wgenetic
20093466
DBF2_YEASTDBF2genetic
20093466
VPS55_YEASTVPS55genetic
20093466
OAF3_YEASTOAF3genetic
20093466
AP1S1_YEASTAPS1genetic
20093466
RSC2_YEASTRSC2genetic
20093466
SGT2_YEASTSGT2genetic
20093466
YO08A_YEASTYOR008C-Agenetic
20093466
SNF3_YEASTSNF3genetic
9559544
HXT2_YEASTHXT2genetic
9559544
ACAC_YEASTACC1physical
20489023
BOP3_YEASTBOP3physical
20489023
NFS1_YEASTNFS1physical
20489023
SEF1_YEASTSEF1physical
20489023
UTR1_YEASTUTR1physical
20489023
ELP2_YEASTELP2physical
21460040
EMI2_YEASTEMI2physical
21460040
MTD1_YEASTMTD1physical
21460040
OYE3_YEASTOYE3physical
21460040
TRPG_YEASTTRP3physical
21460040
UBA1_YEASTUBA1physical
21460040
YCQ6_YEASTYCR016Wphysical
21460040
YKC3_YEASTYKL023Wphysical
21460040
RSC1_YEASTRSC1genetic
21127252
CG11_YEASTCLN1genetic
21127252
RAD5_YEASTRAD5genetic
21127252
CBF1_YEASTCBF1genetic
21127252
AP1S1_YEASTAPS1genetic
22282571
DBF2_YEASTDBF2genetic
22282571
SGT2_YEASTSGT2genetic
22282571
UME6_YEASTUME6genetic
22282571
YGY5_YEASTYGL235Wgenetic
22282571
VHC1_YEASTVHC1genetic
22282571
OAF3_YEASTOAF3genetic
22282571
MBA1_YEASTMBA1genetic
22282571
VPS55_YEASTVPS55genetic
22282571
YO08A_YEASTYOR008C-Agenetic
22282571
PUS3_YEASTDEG1genetic
22282571
VPS41_YEASTVPS41genetic
22282571
EAF1_YEASTEAF1genetic
22282571
RSC2_YEASTRSC2genetic
22282571
MBA1_YEASTMBA1genetic
27708008
DAL81_YEASTDAL81genetic
27708008
MRX5_YEASTYJL147Cgenetic
27708008
VAM3_YEASTVAM3genetic
27708008
COQ7_YEASTCAT5genetic
27708008
PALA_YEASTRIM20genetic
27708008
MNE1_YEASTMNE1genetic
27708008
MDL2_YEASTMDL2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKS1_YEAST

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Related Literatures of Post-Translational Modification

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