SKG6_YEAST - dbPTM
SKG6_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SKG6_YEAST
UniProt AC P32900
Protein Name Protein SKG6
Gene Name SKG6
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 734
Subcellular Localization Membrane
Single-pass membrane protein . Localizes primarily to the growing sites, such as an incipient bud site in the cells with emerging buds, a bud tip in small- or medium-budded cells, or a cell periphery in large-budded cells.
Protein Description May be involved in the polarity establishment process. Suppresses the lethality of KEX2-GAS1 double null mutant when overexpressed..
Protein Sequence MYHTHMHESLISVTSTVSVSDASYAYARLTRRDDSDSSSSSASSTKNSKSAECTGSKQQCQLPTDSSHSTSVTVGVAVAVPVGVIIIVLAVILCIVYRRSKKEAEEDNDPDFEGDSEFLPTMKDYSPGINHLYSSDSQQDFMEKTLQQPPSDPFVGSMHSSKYNVRSATPPAIGRSWYVDPFQLPQESNDSNSLRDFAMRVQEDGLGGYKVAAESRNASQTSLHPDNFSNCTPIRASSRFQESESFRSHGSPIHNNQLSRGSATEGANKQFTFPNEDNDSSSVSEEAEVLNESNESASNDAFEFELDNSSEKTHERNLRFGKDDDNYELQDIREAEHMNDRSSSKSQDDDYYVSLLSPNEEEDIKRMKSIYQVYLDRAKTMKKEEDKADNANDISQEENRVDNIVQNPLPSIKINNNDNIDNNEVPEAKHLVKEALPLNNTNLAEYGPEMAQSQKQYPVQDTLTVNDTEAAPSNRIASSIYSEAIQPLNYQDQYQQQEQSPVYNGHTQYPGNGYSGNPQQQGYTAQFVQNPQWYGVPTPQQQQHNHPQTLETIGELPTPAYLAQSASSHSLTSFKRPNKQQLLQLQTARLNGTALNPVDHPEMFYSPTNDAYYAPQQQGQYMKFNENGAVPSPYQLRQSVVMTNPSDLTAKPSYKPAGSFRSVSATNSRNNSLTTQNNIYLQQQQQQLYNSRVSGILEETDVVQPPSVGGILPHSGSQDDLRKQLGSSHNYTVN
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
4Phosphorylation----MYHTHMHESLI
----CCCCCCCCHHE		11.9230377154
23PhosphorylationTVSVSDASYAYARLT
EEEHHHHHHHEEEEC		18.4530377154
116PhosphorylationDPDFEGDSEFLPTMK
CCCCCCCCCCCCCCC		40.9024909858
125PhosphorylationFLPTMKDYSPGINHL
CCCCCCCCCCCCCCC		15.9620377248
126PhosphorylationLPTMKDYSPGINHLY
CCCCCCCCCCCCCCC		27.1222369663
133PhosphorylationSPGINHLYSSDSQQD
CCCCCCCCCCCHHHH		9.8922369663
134PhosphorylationPGINHLYSSDSQQDF
CCCCCCCCCCHHHHH		33.7522369663
135PhosphorylationGINHLYSSDSQQDFM
CCCCCCCCCHHHHHH		27.9422369663
137PhosphorylationNHLYSSDSQQDFMEK
CCCCCCCHHHHHHHH		31.5222369663
144UbiquitinationSQQDFMEKTLQQPPS
HHHHHHHHHHCCCCC		42.6323749301
145PhosphorylationQQDFMEKTLQQPPSD
HHHHHHHHHCCCCCC		19.2519795423
151PhosphorylationKTLQQPPSDPFVGSM
HHHCCCCCCCCCCCC		65.6821440633
157PhosphorylationPSDPFVGSMHSSKYN
CCCCCCCCCCCCCCC		14.1822369663
160PhosphorylationPFVGSMHSSKYNVRS
CCCCCCCCCCCCCCC		21.6322369663
161PhosphorylationFVGSMHSSKYNVRSA
CCCCCCCCCCCCCCC		25.2022369663
162AcetylationVGSMHSSKYNVRSAT
CCCCCCCCCCCCCCC		43.8124489116
162UbiquitinationVGSMHSSKYNVRSAT
CCCCCCCCCCCCCCC		43.8123749301
163PhosphorylationGSMHSSKYNVRSATP
CCCCCCCCCCCCCCC		22.3421440633
167PhosphorylationSSKYNVRSATPPAIG
CCCCCCCCCCCCCCC		32.0122369663
169PhosphorylationKYNVRSATPPAIGRS
CCCCCCCCCCCCCCC		30.9322369663
188PhosphorylationPFQLPQESNDSNSLR
HHCCCCCCCCCCCHH		40.4622369663
191PhosphorylationLPQESNDSNSLRDFA
CCCCCCCCCCHHHHH		32.3522369663
193PhosphorylationQESNDSNSLRDFAMR
CCCCCCCCHHHHHHH		28.8222369663
210UbiquitinationEDGLGGYKVAAESRN
HCCCCCEEEEEECCC		28.7723749301
215PhosphorylationGYKVAAESRNASQTS
CEEEEEECCCCCCCC		26.5528152593
219PhosphorylationAAESRNASQTSLHPD
EEECCCCCCCCCCCC		37.2221082442
221PhosphorylationESRNASQTSLHPDNF
ECCCCCCCCCCCCCC		30.6617330950
222PhosphorylationSRNASQTSLHPDNFS
CCCCCCCCCCCCCCC		19.6217330950
229PhosphorylationSLHPDNFSNCTPIRA
CCCCCCCCCCCEECC		36.9321440633
232PhosphorylationPDNFSNCTPIRASSR
CCCCCCCCEECCCHH		26.4625704821
243PhosphorylationASSRFQESESFRSHG
CCHHCCCCHHHHHCC		27.9722369663
245PhosphorylationSRFQESESFRSHGSP
HHCCCCHHHHHCCCC		34.9322369663
248PhosphorylationQESESFRSHGSPIHN
CCCHHHHHCCCCCCC		30.1424930733
251PhosphorylationESFRSHGSPIHNNQL
HHHHHCCCCCCCCCC		18.4322369663
259PhosphorylationPIHNNQLSRGSATEG
CCCCCCCCCCCCCCC		25.4922369663
342PhosphorylationAEHMNDRSSSKSQDD
HHHHCCCCCCCCCCC		41.6519779198
343PhosphorylationEHMNDRSSSKSQDDD
HHHCCCCCCCCCCCC		42.5519779198
344PhosphorylationHMNDRSSSKSQDDDY
HHCCCCCCCCCCCCC		37.2630377154
346PhosphorylationNDRSSSKSQDDDYYV
CCCCCCCCCCCCCEE		40.5722369663
351PhosphorylationSKSQDDDYYVSLLSP
CCCCCCCCEEECCCC		16.8622369663
352PhosphorylationKSQDDDYYVSLLSPN
CCCCCCCEEECCCCC		7.2022369663
357PhosphorylationDYYVSLLSPNEEEDI
CCEEECCCCCCHHHH		30.8521551504
369PhosphorylationEDIKRMKSIYQVYLD
HHHHHHHHHHHHHHH		19.7217330950
371PhosphorylationIKRMKSIYQVYLDRA
HHHHHHHHHHHHHHH		10.0622890988
395PhosphorylationADNANDISQEENRVD
CCCHHHCCHHHHHHH		34.1120377248
411PhosphorylationIVQNPLPSIKINNND
HHCCCCCCCCCCCCC		44.1724961812
429AcetylationNNEVPEAKHLVKEAL
CCCCHHHHHHHHHHC		35.4924489116
606PhosphorylationDHPEMFYSPTNDAYY
CCCHHCCCCCCCCCC		17.6221440633
639PhosphorylationSPYQLRQSVVMTNPS
CHHHHCCEEEECCHH		15.3928132839
662PhosphorylationKPAGSFRSVSATNSR
CCCCCCEEEECCCCC		20.5823749301
664PhosphorylationAGSFRSVSATNSRNN
CCCCEEEECCCCCCC		30.5319779198
672PhosphorylationATNSRNNSLTTQNNI
CCCCCCCCCHHHCCH		30.5528152593
674PhosphorylationNSRNNSLTTQNNIYL
CCCCCCCHHHCCHHH		26.5923749301
680PhosphorylationLTTQNNIYLQQQQQQ
CHHHCCHHHHHHHHH		10.6919779198
694PhosphorylationQLYNSRVSGILEETD
HHHHHHHCHHHCCCC		21.0022369663
700PhosphorylationVSGILEETDVVQPPS
HCHHHCCCCCCCCCC		25.3922369663
707PhosphorylationTDVVQPPSVGGILPH
CCCCCCCCCCCCCCC		39.8322369663
715PhosphorylationVGGILPHSGSQDDLR
CCCCCCCCCCHHHHH		37.8922369663
717PhosphorylationGILPHSGSQDDLRKQ
CCCCCCCCHHHHHHH		33.1922369663
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 SKG6_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SKG6_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 SKG6_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZDS1_YEASTZDS1physical
11489916
ZDS2_YEASTZDS2physical
11489916
BCH1_YEASTBCH1physical
24656818
BCH2_YEASTBCH2physical
24656818
BUD7_YEASTBUD7physical
24656818
CHS5_YEASTCHS5physical
24656818
CDC24_YEASTCDC24genetic
27708008
PRP6_YEASTPRP6genetic
27708008
G6PI_YEASTPGI1genetic
27708008
NOP14_YEASTNOP14genetic
27708008
GLE1_YEASTGLE1genetic
27708008
RSP5_YEASTRSP5genetic
27708008
PRP18_YEASTPRP18genetic
27708008
DPOD2_YEASTPOL31genetic
27708008
PRP19_YEASTPRP19genetic
27708008
TAD3_YEASTTAD3genetic
27708008
POB3_YEASTPOB3genetic
27708008
DCP2_YEASTDCP2genetic
27708008
PRP2_YEASTPRP2genetic
27708008
UFE1_YEASTUFE1genetic
27708008
NAB3_YEASTNAB3genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SKG6_YEAST

loading...

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-126; SER-137; THR-169;SER-219; SER-222; SER-243; SER-245 AND SER-251, 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-126; SER-137; SER-251AND SER-715, AND MASS SPECTROMETRY.
"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-137; SER-222 ANDSER-369, AND MASS SPECTROMETRY.
"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 THR-169, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory