GYL1_YEAST - dbPTM
GYL1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GYL1_YEAST
UniProt AC Q04322
Protein Name Probable GTPase-activating protein GYL1
Gene Name GYL1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 720
Subcellular Localization Cytoplasm . Bud . Bud neck .
Protein Description Probable GTPase-activating protein which stimulates the GTP hydrolysis rate by GYP5 of YPT1 and SEC4. Involved in ER to Golgi trafficking and polarized exocytosis..
Protein Sequence MNSNEDIHEERIEVPRTPHQTQPEKDSDRIALRDEISVPEGDEKAYSDEKVEMATTNASSNFGSNESAKDGESIGAFSNPHEALMQSKLREESQSKTILPSDDLSQQLETEESKVEEALKRITSPPLPPRADCIEESASALKSSLPPVLAGNKNDQAPLDRPQLPPRQVVNAETLHLKAPHGNATPSKSPTSAVGNSSSSTPPTLPPRRIEDPLDLAAQKHFLASTFKRNMLFYKSEDNSIKCDLDKNILNLKEDSKKINNNEIPEEVSSFWLKVIGDYQNILINDIETLHFQLSRGIPAAYRLVVWQLVSYAKSKSFDPIYETYLTEMAPFDVQEFENQLKMMDEVPSEYVKRISNVLKAYLLFDPECEFSTDIAYIINMILDVCEEEANAFGLLVRLMKVYGLRLLFLPSASEIDILCYKFDRLVEEFYPEIHNHMVEKGVRSSMFLPGFFTTLFQKKLPTEIQPRIGDMVFLEGIDSIMRILATLLSNSRDHLLKMGFDDMLELLKSGLLDAYIKQNDGTRGDTLLSNECMDKLLQDSMMKVAITPKTMKKYSSEYEEIHRLDNEKEVQYKSITEKNLHLQKHVRKLENDYTSLNREHVTIANELVKNRLNIESVLNENNGYKLQILDLKKKLDSEKKKQVLGVYVPNDLKKDLEETMKKNTQVMDENLKLQDRISELERLIEEIKTANKNGTLFEYSNSKNNPLGAGWSGFKKVFK
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
1Acetylation-------MNSNEDIH
-------CCCCHHCH		12.8422814378
3Phosphorylation-----MNSNEDIHEE
-----CCCCHHCHHH		40.0522369663
17PhosphorylationERIEVPRTPHQTQPE
HHCCCCCCCCCCCCC		21.0317330950
21PhosphorylationVPRTPHQTQPEKDSD
CCCCCCCCCCCCCCC		42.9519779198
27PhosphorylationQTQPEKDSDRIALRD
CCCCCCCCCCEEECC		39.6021440633
37PhosphorylationIALRDEISVPEGDEK
EEECCCCCCCCCCCC		29.5822369663
47PhosphorylationEGDEKAYSDEKVEMA
CCCCCCCCCHHHHHE		44.1228889911
56PhosphorylationEKVEMATTNASSNFG
HHHHHEECCCCCCCC		21.1724961812
59PhosphorylationEMATTNASSNFGSNE
HHEECCCCCCCCCCC		28.0828889911
60PhosphorylationMATTNASSNFGSNES
HEECCCCCCCCCCCC		33.4921551504
64PhosphorylationNASSNFGSNESAKDG
CCCCCCCCCCCCCCC		33.0324961812
67PhosphorylationSNFGSNESAKDGESI
CCCCCCCCCCCCCCC		44.8928889911
73PhosphorylationESAKDGESIGAFSNP
CCCCCCCCCCCCCCH		31.6722369663
78PhosphorylationGESIGAFSNPHEALM
CCCCCCCCCHHHHHH		49.2521551504
105PhosphorylationILPSDDLSQQLETEE
CCCCHHHHHHHHCHH		23.9124961812
110PhosphorylationDLSQQLETEESKVEE
HHHHHHHCHHHHHHH		54.3624961812
113PhosphorylationQQLETEESKVEEALK
HHHHCHHHHHHHHHH		35.4521440633
123PhosphorylationEEALKRITSPPLPPR
HHHHHHCCCCCCCCC		38.9323749301
124PhosphorylationEALKRITSPPLPPRA
HHHHHCCCCCCCCCC		23.3425704821
137PhosphorylationRADCIEESASALKSS
CCHHHHHHHHHHHHC		18.0921551504
139PhosphorylationDCIEESASALKSSLP
HHHHHHHHHHHHCCC		43.3328889911
185PhosphorylationKAPHGNATPSKSPTS
ECCCCCCCCCCCCCC		31.9023749301
187PhosphorylationPHGNATPSKSPTSAV
CCCCCCCCCCCCCCC		41.2223749301
197PhosphorylationPTSAVGNSSSSTPPT
CCCCCCCCCCCCCCC		26.1823749301
198PhosphorylationTSAVGNSSSSTPPTL
CCCCCCCCCCCCCCC		32.1023749301
199PhosphorylationSAVGNSSSSTPPTLP
CCCCCCCCCCCCCCC		37.7423749301
200PhosphorylationAVGNSSSSTPPTLPP
CCCCCCCCCCCCCCC		47.0523749301
201PhosphorylationVGNSSSSTPPTLPPR
CCCCCCCCCCCCCCC		34.9229734811
204PhosphorylationSSSSTPPTLPPRRIE
CCCCCCCCCCCCCCC		53.7723749301
236PhosphorylationRNMLFYKSEDNSIKC
HCCEEEECCCCCEEC		38.5127017623
349PhosphorylationKMMDEVPSEYVKRIS
HHHHHCCHHHHHHHH		46.8919684113
498SumoylationNSRDHLLKMGFDDML
CCHHHHHHCCHHHHH		43.25-
498SumoylationNSRDHLLKMGFDDML
CCHHHHHHCCHHHHH		43.2515542864
498UbiquitinationNSRDHLLKMGFDDML
CCHHHHHHCCHHHHH		43.2515542864
541PhosphorylationMDKLLQDSMMKVAIT
HHHHHHHHHHHHHCC		14.0727017623
551PhosphorylationKVAITPKTMKKYSSE
HHHCCHHHHHHHCCC		35.1127017623
679PhosphorylationLKLQDRISELERLIE
HHHHHHHHHHHHHHH		36.7021440633
713PhosphorylationNPLGAGWSGFKKVFK
CCCCCCCCCCCHHCC		33.1724930733
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 GYL1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GYL1_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 GYL1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RV167_YEASTRVS167physical
15802519
GYP5_YEASTGYP5physical
15802519
GYP5_YEASTGYP5physical
16554755
RL36B_YEASTRPL36Bphysical
16429126
SSB2_YEASTSSB2physical
16429126
MCM5_YEASTMCM5physical
16429126
YN94_YEASTYNR065Cphysical
18467557
GYP5_YEASTGYP5physical
19591838
RUD3_YEASTRUD3genetic
15802519
SEC22_YEASTSEC22genetic
15802519
RV167_YEASTRVS167genetic
15802519
GYP5_YEASTGYP5physical
20826334
SLT2_YEASTSLT2genetic
20526336
GYP5_YEASTGYP5physical
21554509
RV167_YEASTRVS167physical
21554509
TBP6_YEASTYTA6physical
22875988
GYP5_YEASTGYP5physical
22875988
ARE1_YEASTARE1physical
22875988
SPR3_YEASTSPR3physical
22875988
ETP1_YEASTETP1physical
22875988
SGM1_YEASTSGM1physical
22875988
IFH1_YEASTIFH1physical
22875988
RNA1_YEASTRNA1physical
22875988
GPI17_YEASTGPI17genetic
23891562
RIC1_YEASTRIC1genetic
23891562
TPM1_YEASTTPM1genetic
23891562
SEC7_YEASTSEC7genetic
27708008
EXO70_YEASTEXO70genetic
27708008
CDK1_YEASTCDC28genetic
27708008
CDC10_YEASTCDC10genetic
27708008
RPB1_YEASTRPO21genetic
27708008
LCB2_YEASTLCB2genetic
27708008
CDC1_YEASTCDC1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
SDA1_YEASTSDA1genetic
27708008
NUP85_YEASTNUP85genetic
27708008
POB3_YEASTPOB3genetic
27708008
MCM1_YEASTMCM1genetic
27708008
CLP1_YEASTCLP1genetic
27708008
CET1_YEASTCET1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GYL1_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 THR-17; SER-37; SER-47;SER-73; SER-78; SER-124 AND SER-139, 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-37, 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 THR-17 AND SER-37, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"A proteomic strategy for gaining insights into protein sumoylation inyeast.";
Denison C., Rudner A.D., Gerber S.A., Bakalarski C.E., Moazed D.,Gygi S.P.;
Mol. Cell. Proteomics 4:246-254(2005).
Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND MASS SPECTROMETRY.

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