GIS4_YEAST - dbPTM
GIS4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GIS4_YEAST
UniProt AC Q04233
Protein Name Protein GIS4
Gene Name GIS4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 774
Subcellular Localization Cytoplasm .
Protein Description May be involved in the Ras/cAMP signaling pathway..
Protein Sequence MQKSVRVGDYFDNDDNGLWSWYLTNLRLGDFEELIGNQLKYTLLKRFLNSHFYGDNNISARPNKKILLVSIPENVHEDISILEIFLKDYFHLEKLEHIQISKLTHSHCYNHENHYLLTDNLNNFQDPTFLEFASTSWQVQKNSKALNNNNRNSIPPPTISSSKASNGKLESNVSDDQWSNINTQTSTATRTNTNTRTLTSPDTVDINVTSVNSQSNNNDTPQDNENEVDEEDATSSIVLNFSHSRTVDSKPNRLPKIFPSYTNEDYTPSHSEIMSIDSFAGEDVSSTYPGQDLSLTTARREDESGQDEVEDHYSRVSHDLGDESIDQASYSMESSVSYTSYSSSSNSSSAHYSLSSSSRGNPKRENIDHTNATYVSELSSITSSIDNLTTSTTPEEEDNLIHHNYDAQGYGSGEDDGEEVYDDEDLSSSDYSVLSILPSISICDSLGYFRLVLQSILIQDPDTKEIFTAIRQSNNKPTMASVTDDWLLYDSNFSMNNLQILTLQDLLDIKRSFPKILFYTMVIVTNSGKQVEEEFKNPNYDNREGISKEQPLDSELSLTNDPQQYFPTAYNNGYNDYIDDEDDEDDGDDASLSEQSGPQMYIPTRMESNVTTAHRSIRTVNSIGEWAFNRHNSVTKIDKSNSNELDNSKTGESTVLSSEPHPMTQLSNSNTTSSNFSHSLKTKNSHKPNSKGNNESNSKNELKKIKSSINAMSAVERSKSLPLPTLLKSLSGIDNPTHATNKDRKRWKFQMNRFKNHKNSGSAGTDKSQRCAIM
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
40UbiquitinationELIGNQLKYTLLKRF
HHHHHHHHHHHHHHH		26.8224961812
153PhosphorylationLNNNNRNSIPPPTIS
HCCCCCCCCCCCCCC		32.9825752575
158PhosphorylationRNSIPPPTISSSKAS
CCCCCCCCCCCCCCC		38.9921440633
165PhosphorylationTISSSKASNGKLESN
CCCCCCCCCCCCCCC		50.2622369663
171PhosphorylationASNGKLESNVSDDQW
CCCCCCCCCCCHHHH		53.6322369663
174PhosphorylationGKLESNVSDDQWSNI
CCCCCCCCHHHHHCC		39.4622369663
179PhosphorylationNVSDDQWSNINTQTS
CCCHHHHHCCCCCCC		23.3822369663
183PhosphorylationDQWSNINTQTSTATR
HHHHCCCCCCCEEEE		29.4422369663
185PhosphorylationWSNINTQTSTATRTN
HHCCCCCCCEEEECC		26.4622369663
186PhosphorylationSNINTQTSTATRTNT
HCCCCCCCEEEECCC		13.2622369663
187PhosphorylationNINTQTSTATRTNTN
CCCCCCCEEEECCCC		35.1222369663
189PhosphorylationNTQTSTATRTNTNTR
CCCCCEEEECCCCCC		37.8122369663
304PhosphorylationTARREDESGQDEVED
EEECCCCCCCCHHHH		54.8222369663
478PhosphorylationRQSNNKPTMASVTDD
HHHCCCCCEEEECCC		27.2930377154
481PhosphorylationNNKPTMASVTDDWLL
CCCCCEEEECCCEEE		18.0930377154
483PhosphorylationKPTMASVTDDWLLYD
CCCEEEECCCEEEEC		26.2530377154
489PhosphorylationVTDDWLLYDSNFSMN
ECCCEEEECCCCCCC		18.3730377154
502PhosphorylationMNNLQILTLQDLLDI
CCCEEEEEHHHHHHH		24.8130377154
608PhosphorylationYIPTRMESNVTTAHR
CCCCCCCCCCCCCCC		27.5325752575
611PhosphorylationTRMESNVTTAHRSIR
CCCCCCCCCCCCCEE		23.6325005228
612PhosphorylationRMESNVTTAHRSIRT
CCCCCCCCCCCCEEE		19.0428889911
616PhosphorylationNVTTAHRSIRTVNSI
CCCCCCCCEEECHHH		13.4228889911
619PhosphorylationTAHRSIRTVNSIGEW
CCCCCEEECHHHHHH		23.5128889911
622PhosphorylationRSIRTVNSIGEWAFN
CCEEECHHHHHHHHH		27.8617330950
640PhosphorylationSVTKIDKSNSNELDN
CCEEECCCCCCCCCC		41.5719823750
642PhosphorylationTKIDKSNSNELDNSK
EEECCCCCCCCCCCC		38.4825521595
667PhosphorylationPHPMTQLSNSNTTSS
CCCCCCCCCCCCCCC		28.5221440633
677PhosphorylationNTTSSNFSHSLKTKN
CCCCCCCCCCCCCCC		19.2021440633
679PhosphorylationTSSNFSHSLKTKNSH
CCCCCCCCCCCCCCC		30.2921440633
685PhosphorylationHSLKTKNSHKPNSKG
CCCCCCCCCCCCCCC		34.1528889911
696PhosphorylationNSKGNNESNSKNELK
CCCCCCCCCCHHHHH		48.8330377154
698PhosphorylationKGNNESNSKNELKKI
CCCCCCCCHHHHHHH		46.2528889911
707PhosphorylationNELKKIKSSINAMSA
HHHHHHHHHHHHHHH		39.6717330950
708PhosphorylationELKKIKSSINAMSAV
HHHHHHHHHHHHHHH		18.1717330950
718PhosphorylationAMSAVERSKSLPLPT
HHHHHHHHHCCCHHH		17.0628889911
720PhosphorylationSAVERSKSLPLPTLL
HHHHHHHCCCHHHHH		36.1417330950
729PhosphorylationPLPTLLKSLSGIDNP
CHHHHHHHHCCCCCC		27.9522890988
731PhosphorylationPTLLKSLSGIDNPTH
HHHHHHHCCCCCCCC		40.5719823750
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
-KUbiquitinationE3 ubiquitin ligaseGRR1P24814
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GIS4_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 GIS4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUP2_YEASTCUP2physical
10688190
GRR1_YEASTGRR1physical
15890364
SNF1_YEASTSNF1physical
15890364
BMH2_YEASTBMH2physical
16554755
YFF4_YEASTYFL054Cphysical
16554755
STM1_YEASTSTM1physical
16554755
PP2B1_YEASTCNA1genetic
17030993
PP2B2_YEASTCMP2genetic
17030993
NRG1_YEASTNRG1genetic
18757815
HAL5_YEASTHAL5genetic
20206679
ATN1_YEASTENA1genetic
17030993
PDE2_YEASTPDE2genetic
10628841
GIS1_YEASTGIS1genetic
10628841
GIS2_YEASTGIS2genetic
10628841
GIS3_YEASTGIS3genetic
10628841
SGE1_YEASTSGE1genetic
10628841
TBA3_YEASTTUB3genetic
10628841
RAD4_YEASTRAD4genetic
27708008
YIA6_YEASTYIA6genetic
27708008
UBP13_YEASTUBP13genetic
27708008
AGP1_YEASTAGP1genetic
27708008
PP2C1_YEASTPTC1genetic
27708008
PEX19_YEASTPEX19genetic
27708008
ARO1_YEASTARO1genetic
27708008
SNF1_YEASTSNF1genetic
27708008
CHO2_YEASTCHO2genetic
27708008
DAL81_YEASTDAL81genetic
27708008
FPS1_YEASTFPS1genetic
27708008
MMR1_YEASTMMR1genetic
27708008
NKP2_YEASTNKP2genetic
27708008
NST1_YEASTNST1genetic
27708008
RTG1_YEASTRTG1genetic
27708008
SPEE_YEASTSPE3genetic
27708008
MED1_YEASTMED1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GIS4_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-304; SER-640 ANDSER-731, 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-642, 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-622; SER-707 ANDSER-720, AND MASS SPECTROMETRY.

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