GYP5_YEAST - dbPTM
GYP5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GYP5_YEAST
UniProt AC Q12344
Protein Name GTPase-activating protein GYP5
Gene Name GYP5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 894
Subcellular Localization Cytoplasm. Bud. Bud neck.
Protein Description GTPase-activating protein which accelerates the GTP hydrolysis rate of YPT1 and SEC4. Involved in ER to Golgi trafficking and polarized exocytosis..
Protein Sequence MSSDKSIEKNTDTIASEVHEGDNHSNNLGSMEEEIKSTPSDQYEEIAIIPTEPLHSDKELNDKQQSLGHEAPTNVSREEPIGISGDEDTQITEQNVNEQRQETREPSSEIDLNEPLDVEKDVTTDVQAPNGLNIEKEYDAVKENEKVYADTKEVVSSPENREVTGKNSGGEKSSSSKFLDDESGTTTAANANDISISSEVTPERSSENDNNQIHITNEVAAGINLNENKEQKAAIEDGPVTAENLSSETARKVPPIPTQIINEKGDNSSENEVSAIPTTSSPPLPPRQNVATSTSPKLPPRGKQREQPPKTKNAVPPPLEEEMKSEKFRKNFEETKRNSYHHVPLTGSKTAQLESTAEINLIASRYRKTSHHLNKEGEETRESLQEGQSFLKSTFTSFLENLSEYNEVENVNEEDREMFKIDWSFWTQVVNDYATVASNEPENLEAHVTNGIPPQIRGIIWQLMANSKSREMEDIYETLLDTECLHEATIRRDLRRTKFVAEDKMESLYKVIKVYSVYDPDVGYTQGMGFIAAPLLINCENEAESFGLLVGLMKNYGLRELFLPGMPGLMLMLYQFDRLLEEHSPSLYNRLIREGISSTMYATQWFLTFFAYKFPLEFVLRIFDIVFVEGIEVLLKFAVNLMLKNEETLVKLRFDELLDFLKDELFNYYLMGNQDDASVVQMGLSNGNSFKGNDDGTFSYNVDLFVHDAMTGVYITPLTLRRYRGEYVEIHEKEQKKEDHYESLRIQNHQLQREAQKLEHDYSILNKENISAANELIQNRLNMEMLLDEKNDLINTITDIKSQIEEEIRKQNLPNPDASLPKADLREDLERTISRNNEVMRENGQLEERITELQAEIDELININKEQVSTASLLERDSKAKGRKGWTGFKKVFK
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
2Phosphorylation------MSSDKSIEK
------CCCCHHCCC		47.4422369663
3Phosphorylation-----MSSDKSIEKN
-----CCCCHHCCCC		48.0022369663
6Phosphorylation--MSSDKSIEKNTDT
--CCCCHHCCCCCCC		40.7630377154
11PhosphorylationDKSIEKNTDTIASEV
CHHCCCCCCCHHHHH		45.6619823750
13PhosphorylationSIEKNTDTIASEVHE
HCCCCCCCHHHHHCC		19.1919795423
16PhosphorylationKNTDTIASEVHEGDN
CCCCCHHHHHCCCCC		35.9828889911
25PhosphorylationVHEGDNHSNNLGSME
HCCCCCCCCCCCCHH		33.4017330950
30PhosphorylationNHSNNLGSMEEEIKS
CCCCCCCCHHHHHHC		26.6219823750
37PhosphorylationSMEEEIKSTPSDQYE
CHHHHHHCCCCHHCE		51.7322369663
38PhosphorylationMEEEIKSTPSDQYEE
HHHHHHCCCCHHCEE		23.0822369663
40PhosphorylationEEIKSTPSDQYEEIA
HHHHCCCCHHCEEEE		37.1222369663
43PhosphorylationKSTPSDQYEEIAIIP
HCCCCHHCEEEEEEE		22.1122369663
51PhosphorylationEEIAIIPTEPLHSDK
EEEEEEECCCCCCCC		39.5720377248
56PhosphorylationIPTEPLHSDKELNDK
EECCCCCCCCHHCHH		59.0522369663
66PhosphorylationELNDKQQSLGHEAPT
HHCHHHHHHCCCCCC		33.5528889911
76PhosphorylationHEAPTNVSREEPIGI
CCCCCCCCCCCCCCC		35.7228889911
84PhosphorylationREEPIGISGDEDTQI
CCCCCCCCCCCCCCC		34.6723749301
89PhosphorylationGISGDEDTQITEQNV
CCCCCCCCCCCHHHH		21.5919795423
103PhosphorylationVNEQRQETREPSSEI
HHHHHHHHCCCCCCC		31.8122369663
107PhosphorylationRQETREPSSEIDLNE
HHHHCCCCCCCCCCC		35.5322369663
108PhosphorylationQETREPSSEIDLNEP
HHHCCCCCCCCCCCC		49.6522369663
123PhosphorylationLDVEKDVTTDVQAPN
CCCCCCCCCCCCCCC		27.6724961812
124PhosphorylationDVEKDVTTDVQAPNG
CCCCCCCCCCCCCCC		33.7428889911
136AcetylationPNGLNIEKEYDAVKE
CCCCCCCHHHHHHHC		58.7524489116
152UbiquitinationEKVYADTKEVVSSPE
CEEECCHHHHHCCCC		49.4023749301
156PhosphorylationADTKEVVSSPENREV
CCHHHHHCCCCCCCC		45.4022369663
157PhosphorylationDTKEVVSSPENREVT
CHHHHHCCCCCCCCC		25.3222369663
164PhosphorylationSPENREVTGKNSGGE
CCCCCCCCCCCCCCC		37.3722369663
246PhosphorylationPVTAENLSSETARKV
CCCHHHCCHHHHCCC		37.4028152593
247PhosphorylationVTAENLSSETARKVP
CCHHHCCHHHHCCCC		41.9825752575
249PhosphorylationAENLSSETARKVPPI
HHHCCHHHHCCCCCC		33.4423749301
268PhosphorylationINEKGDNSSENEVSA
CCCCCCCCCCCCCCC		43.7123749301
269PhosphorylationNEKGDNSSENEVSAI
CCCCCCCCCCCCCCC		51.1720377248
274PhosphorylationNSSENEVSAIPTTSS
CCCCCCCCCCCCCCC		17.8221551504
278PhosphorylationNEVSAIPTTSSPPLP
CCCCCCCCCCCCCCC		32.9520377248
279PhosphorylationEVSAIPTTSSPPLPP
CCCCCCCCCCCCCCC		23.1220377248
280PhosphorylationVSAIPTTSSPPLPPR
CCCCCCCCCCCCCCC		43.2420377248
281PhosphorylationSAIPTTSSPPLPPRQ
CCCCCCCCCCCCCCC		28.5721551504
292PhosphorylationPPRQNVATSTSPKLP
CCCCCCCCCCCCCCC		28.4020377248
293PhosphorylationPRQNVATSTSPKLPP
CCCCCCCCCCCCCCC		19.7029136822
294PhosphorylationRQNVATSTSPKLPPR
CCCCCCCCCCCCCCC		44.7020377248
295PhosphorylationQNVATSTSPKLPPRG
CCCCCCCCCCCCCCC		21.5821551504
335PhosphorylationFRKNFEETKRNSYHH
HHHHHHHHCCCCCCC		28.2728889911
339PhosphorylationFEETKRNSYHHVPLT
HHHHCCCCCCCCCCC		29.8517287358
340PhosphorylationEETKRNSYHHVPLTG
HHHCCCCCCCCCCCC		10.2519823750
346PhosphorylationSYHHVPLTGSKTAQL
CCCCCCCCCCCCEEC		33.0819823750
348PhosphorylationHHVPLTGSKTAQLES
CCCCCCCCCCEECCC		22.9219823750
350PhosphorylationVPLTGSKTAQLESTA
CCCCCCCCEECCCHH		22.7226447709
355PhosphorylationSKTAQLESTAEINLI
CCCEECCCHHHHHHH		41.3226447709
356PhosphorylationKTAQLESTAEINLIA
CCEECCCHHHHHHHH		20.9526447709
364PhosphorylationAEINLIASRYRKTSH
HHHHHHHHHHHHHHC		23.8926447709
389PhosphorylationESLQEGQSFLKSTFT
HHHHHHHHHHHHHHH		43.3225752575
597PhosphorylationRLIREGISSTMYATQ
HHHHHHHCHHHHHHH		30.5223607784
598PhosphorylationLIREGISSTMYATQW
HHHHHHCHHHHHHHH		18.4423607784
599PhosphorylationIREGISSTMYATQWF
HHHHHCHHHHHHHHH		13.8623607784
601PhosphorylationEGISSTMYATQWFLT
HHHCHHHHHHHHHHH		13.4423607784
603PhosphorylationISSTMYATQWFLTFF
HCHHHHHHHHHHHHH		14.6223607784
608PhosphorylationYATQWFLTFFAYKFP
HHHHHHHHHHHHCCC		13.7723607784
612PhosphorylationWFLTFFAYKFPLEFV
HHHHHHHHCCCHHHH		14.1723607784
802PhosphorylationNTITDIKSQIEEEIR
HHHHHHHHHHHHHHH		36.4028889911
819PhosphorylationNLPNPDASLPKADLR
CCCCCCCCCCHHHHH		53.2127017623
832PhosphorylationLREDLERTISRNNEV
HHHHHHHHHHHCHHH		17.5822369663
834PhosphorylationEDLERTISRNNEVMR
HHHHHHHHHCHHHHH		28.4822369663
869PhosphorylationNINKEQVSTASLLER
CCCHHHCCHHHHHHH		20.2524961812
870PhosphorylationINKEQVSTASLLERD
CCHHHCCHHHHHHHH		22.7821440633
872PhosphorylationKEQVSTASLLERDSK
HHHCCHHHHHHHHHH		33.3121440633
878PhosphorylationASLLERDSKAKGRKG
HHHHHHHHHHCCCCC		40.5124961812
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 GYP5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GYP5_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 GYP5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RV167_YEASTRVS167physical
15802519
GYL1_YEASTGYL1physical
15802519
RV167_YEASTRVS167physical
16554755
GYL1_YEASTGYL1physical
18182006
GYL1_YEASTGYL1genetic
15802519
RUD3_YEASTRUD3genetic
15802519
SEC22_YEASTSEC22genetic
15802519
RV167_YEASTRVS167genetic
15802519
VPS41_YEASTVPS41genetic
20526336
XRN1_YEASTXRN1genetic
20526336
SST2_YEASTSST2genetic
20526336
TGS1_YEASTTGS1genetic
20526336
GYL1_YEASTGYL1physical
21554509
RV167_YEASTRVS167physical
21554509
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
HSP7F_YEASTSSE1physical
22940862
RV161_YEASTRVS161physical
22940862
HDA2_YEASTHDA2physical
22875988
SPC25_YEASTSPC25physical
22875988
MED3_YEASTPGD1physical
22875988
PFD1_YEASTPFD1physical
22875988
GYL1_YEASTGYL1physical
22875988
NUF2_YEASTNUF2physical
22875988
PRS10_YEASTRPT4physical
22875988
TBP6_YEASTYTA6physical
22875988
GYP5_YEASTGYP5physical
22875988
KAR3_YEASTKAR3physical
22875988
KEL1_YEASTKEL1physical
22875988
SKN7_YEASTSKN7physical
22875988
END3_YEASTEND3physical
22875988
TUP1_YEASTTUP1physical
22875988
SNX41_YEASTSNX41physical
22875988
NNF2_YEASTNNF2physical
22875988
STB2_YEASTSTB2physical
22875988
YAP8_YEASTARR1physical
22875988
GET2_YEASTGET2genetic
23891562
SRO7_YEASTSRO7genetic
23891562
TPM1_YEASTTPM1genetic
23891562
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GYP5_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-25; SER-30; THR-51;SER-84; THR-103; SER-107; SER-108; SER-246; SER-247; THR-249; SER-268;SER-269; SER-274; THR-278; THR-279; SER-281; SER-295; SER-389; SER-834AND SER-872, 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-295, AND MASSSPECTROMETRY.
"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-339, AND MASSSPECTROMETRY.

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