SKO1_YEAST - dbPTM
SKO1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKO1_YEAST
UniProt AC Q02100
Protein Name CRE-binding bZIP protein SKO1
Gene Name SKO1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 647
Subcellular Localization Nucleus.
Protein Description Binds to the CRE motif 5'-TGACGTCA-3' and acts as a repressor of transcription of the SUC2 gene and most probably other genes..
Protein Sequence MSSEERSRQPSTVSTFDLEPNPFEQSFASSKKALSLPGTISHPSLPKELSRNNSTSTITQHSQRSTHSLNSIPEENGNSTVTDNSNHNDVKKDSPSFLPGQQRPTIISPPILTPGGSKRLPPLLLSPSILYQANSTTNPSQNSHSVSVSNSNPSAIGVSSTSGSLYPNSSSPSGTSLIRQPRNSNVTTSNSGNGFPTNDSQMPGFLLNLSKSGLTPNESNIRTGLTPGILTQSYNYPVLPSINKNTITGSKNVNKSVTVNGSIENHPHVNIMHPTVNGTPLTPGLSSLLNLPSTGVLANPVFKSTPTTNTTDGTVNNSISNSNFSPNTSTKAAVKMDNPAEFNAIEHSAHNHKENENLTTQIENNDQFNNKTRKRKRRMSSTSSTSKASRKNSISRKNSAVTTAPAQKDDVENNKISNNVTLDENEEQERKRKEFLERNRVAASKFRKRKKEYIKKIENDLQFYESEYDDLTQVIGKLCGIIPSSSSNSQFNVNVSTPSSSSPPSTSLIALLESSISRSDYSSAMSVLSNMKQLICETNFYRRGGKNPRDDMDGQEDSFNKDTNVVKSENAGYPSVNSRPIILDKKYSLNSGANISKSNTTTNNVGNSAQNIINSCYSVTNPLVINANSDTHDTNKHDVLSTLPHNN
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
35PhosphorylationASSKKALSLPGTISH
HHCCCHHCCCCCCCC		37.0630377154
47AcetylationISHPSLPKELSRNNS
CCCCCCCHHHHCCCC		76.2724489116
54PhosphorylationKELSRNNSTSTITQH
HHHHCCCCCCCHHCC		27.5522369663
55PhosphorylationELSRNNSTSTITQHS
HHHCCCCCCCHHCCH		31.8222369663
56PhosphorylationLSRNNSTSTITQHSQ
HHCCCCCCCHHCCHH		20.0322369663
57PhosphorylationSRNNSTSTITQHSQR
HCCCCCCCHHCCHHC		28.2922369663
59PhosphorylationNNSTSTITQHSQRST
CCCCCCHHCCHHCCC		21.9622369663
62PhosphorylationTSTITQHSQRSTHSL
CCCHHCCHHCCCCCC		19.9223749301
66PhosphorylationTQHSQRSTHSLNSIP
HCCHHCCCCCCCCCC		20.0630377154
68PhosphorylationHSQRSTHSLNSIPEE
CHHCCCCCCCCCCCC		29.3630377154
71PhosphorylationRSTHSLNSIPEENGN
CCCCCCCCCCCCCCC		44.8330377154
94PhosphorylationHNDVKKDSPSFLPGQ
CCCCCCCCCCCCCCC		31.1822369663
96PhosphorylationDVKKDSPSFLPGQQR
CCCCCCCCCCCCCCC		43.2820377248
105PhosphorylationLPGQQRPTIISPPIL
CCCCCCCEEECCCEE		32.8820377248
108PhosphorylationQQRPTIISPPILTPG
CCCCEEECCCEECCC		22.2922369663
113PhosphorylationIISPPILTPGGSKRL
EECCCEECCCCCCCC		22.1722369663
117PhosphorylationPILTPGGSKRLPPLL
CEECCCCCCCCCCCE		22.1022369663
126PhosphorylationRLPPLLLSPSILYQA
CCCCCEECHHHEEEC		19.3011230135
212PhosphorylationFLLNLSKSGLTPNES
EEEHHHHCCCCCCHH		35.3428132839
215PhosphorylationNLSKSGLTPNESNIR
HHHHCCCCCCHHHCC		27.8222369663
223PhosphorylationPNESNIRTGLTPGIL
CCHHHCCCCCCCCEE		32.5230377154
320PhosphorylationGTVNNSISNSNFSPN
CCCCCCCCCCCCCCC		33.7419823750
322PhosphorylationVNNSISNSNFSPNTS
CCCCCCCCCCCCCCC		32.2524961812
325PhosphorylationSISNSNFSPNTSTKA
CCCCCCCCCCCCCCE		22.8419823750
328PhosphorylationNSNFSPNTSTKAAVK
CCCCCCCCCCCEEEE		40.9519823750
329PhosphorylationSNFSPNTSTKAAVKM
CCCCCCCCCCEEEEC		34.2523749301
330PhosphorylationNFSPNTSTKAAVKMD
CCCCCCCCCEEEECC		23.7528889911
380PhosphorylationRKRKRRMSSTSSTSK
HHHHHHHHCCHHCCH		28.7521440633
381PhosphorylationKRKRRMSSTSSTSKA
HHHHHHHCCHHCCHH		23.9821440633
382PhosphorylationRKRRMSSTSSTSKAS
HHHHHHCCHHCCHHH		21.2721440633
383PhosphorylationKRRMSSTSSTSKASR
HHHHHCCHHCCHHHH		33.3021440633
384PhosphorylationRRMSSTSSTSKASRK
HHHHCCHHCCHHHHH		36.4721440633
385PhosphorylationRMSSTSSTSKASRKN
HHHCCHHCCHHHHHH		33.7319823750
386PhosphorylationMSSTSSTSKASRKNS
HHCCHHCCHHHHHHC		28.3319823750
393PhosphorylationSKASRKNSISRKNSA
CHHHHHHCCCCCCCC		25.6121440633
395PhosphorylationASRKNSISRKNSAVT
HHHHHCCCCCCCCCC		36.7020377248
399PhosphorylationNSISRKNSAVTTAPA
HCCCCCCCCCCCCCC		27.4422369663
402PhosphorylationSRKNSAVTTAPAQKD
CCCCCCCCCCCCCHH		19.5622890988
403PhosphorylationRKNSAVTTAPAQKDD
CCCCCCCCCCCCHHH		24.8422890988
445AcetylationRNRVAASKFRKRKKE
HHHHHHHHHHHHHHH		44.4525381059
558PhosphorylationDMDGQEDSFNKDTNV
CCCCCCCCCCCCCCC		29.9321551504
563PhosphorylationEDSFNKDTNVVKSEN
CCCCCCCCCCCCCCC		31.3623749301
585AcetylationSRPIILDKKYSLNSG
CCCEEECCCEECCCC		50.6024489116
586AcetylationRPIILDKKYSLNSGA
CCEEECCCEECCCCC		39.4725381059
587PhosphorylationPIILDKKYSLNSGAN
CEEECCCEECCCCCC		24.9128889911
588PhosphorylationIILDKKYSLNSGANI
EEECCCEECCCCCCC		29.9223749301
591PhosphorylationDKKYSLNSGANISKS
CCCEECCCCCCCCCC		44.5717563356
596PhosphorylationLNSGANISKSNTTTN
CCCCCCCCCCCCCCC		29.8228889911
598PhosphorylationSGANISKSNTTTNNV
CCCCCCCCCCCCCCC		32.3928889911
601PhosphorylationNISKSNTTTNNVGNS
CCCCCCCCCCCCHHH		31.6028889911
602PhosphorylationISKSNTTTNNVGNSA
CCCCCCCCCCCHHHH		23.8228889911
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 SKO1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKO1_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 SKO1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HOG1_YEASTHOG1physical
11230135
HOG1_YEASTHOG1physical
12086627
SKO1_YEASTSKO1physical
11500510
TUP1_YEASTTUP1physical
11500510
CYC8_YEASTCYC8physical
11230135
TUP1_YEASTTUP1physical
11230135
STE2_YEASTSTE2genetic
18617996
GBB_YEASTSTE4genetic
18617996
STE5_YEASTSTE5genetic
18617996
STE20_YEASTSTE20genetic
18617996
STE11_YEASTSTE11genetic
18617996
FAR1_YEASTFAR1genetic
18617996
KAR4_YEASTKAR4genetic
18617996
SWI5_YEASTSWI5genetic
20831804
SMP1_YEASTSMP1physical
21193057
FUS3_YEASTFUS3genetic
21127252
CG11_YEASTCLN1genetic
21127252
SLT2_YEASTSLT2genetic
21127252
PP2C1_YEASTPTC1genetic
21127252
VMS1_YEASTVMS1genetic
21127252
CTK3_YEASTCTK3genetic
21127252
ACA2_YEASTCST6genetic
23300865
KPC1_YEASTPKC1genetic
27708008
GPI18_YEASTGPI18genetic
27708008
APC11_YEASTAPC11genetic
27708008
TIM22_YEASTTIM22genetic
27708008
SNU56_YEASTSNU56genetic
27708008
ACT_YEASTACT1genetic
27708008
CTF8_YEASTCTF8genetic
27708008
PAN1_YEASTPAN1genetic
27708008
CDC11_YEASTCDC11genetic
27708008
NOP2_YEASTNOP2genetic
27708008
SMP3_YEASTSMP3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKO1_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-94; SER-399 AND SER-558,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-94; SER-108; THR-113 ANDSER-591, AND MASS SPECTROMETRY.

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