GYP2_YEAST - dbPTM
GYP2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GYP2_YEAST
UniProt AC P53258
Protein Name GTPase-activating protein GYP2
Gene Name MDR1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 950
Subcellular Localization Cytoplasm . Distributed throughout the cytoplasm and accumulates in punctate structures, which concentrate in an actin-dependent manner at sites of polarized growth.
Protein Description Stimulates specifically the GTPase activity of SEC4, YPT6 and YPT36. Inactivates YPT6 during recycling between the endosome and the Golgi compartments..
Protein Sequence MSFFDSLRQKAPFLDKLADSFTPTLTRDEKFRLKYKLPANENILEDTNAEVSFATSIKDGKGHSDRVNNKGRKTAYVYSGRLFLTPHFLVFRDAFDHSSCVLILNISTIKRVERSPSESYEFALLVTLYTGAKVLIQFIGIRYRSEQFCDKLKLNLKENIPNAKTLPAFLETSYSEFLIAKNILGKKDITVPRAGLGQHFKYPGNPTMVKEKAKLRLWFDYFRENGRNLAVVQTPMFRKLIRIGVPNRMRGEIWELCSGAMYMRYANSGEYERILNENAGKTSQAIDEIEKDLKRSLPEYSAYQTEEGIQRLRNVLTAYSWKNPDVGYCQAMNIVVAGFLIFMSEEQAFWCLCNLCDIYVPGYYSKTMYGTLLDQRVFESFVEDRMPVLWEYILQHDIQLSVVSLPWFLSLFFTSMPLEYAVRIMDIFFMNGSITLFQVALAVLKINADDILQADDDGMFIAIIKHYFQTLGQSAHPDSSDIKYRQITKFQELLVTAFKEFSVISEEMAMHARHKYEKGIFQNIETFMKRTQLRHMPKTFNLSSDDLSNIYDMFYQSIETYKISMGTGSSNMGFEVFIQFLSKFCDSCRPCEKDKDPAFRKQKRNFLQRLFDNWDSAHIGELTLNDVVTGLDKLVTVDLLQAINYFFSLYDTDGDGELHREEVLQLSEGLLLLTEPWKSGRYVDLLTKKRIEDDIAENIIKESGGEIATMNQIELPTGVTIDEEKYKVEQAERYLKAASNFLQRSFEYAKAVDLAEEVNLIDLSDDEGEEKRTVKQKQLESIKANAALDPTHPKVIDLPTFRMIILADETYELFFSNTLRSSVHVDEHVNIDNKNKVLRSMFDGILADGKRVAEQVRRRVDSVATRSSIASVESTPTAAASSITTKEEKYDDLDDFTSEHQPENEELLQSSWFEIDDANETSTKAIQERSFEPLSANSSEEKSNLIEFEA
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
2Acetylation------MSFFDSLRQ
------CCHHHHHHH		34.3222814378
2Phosphorylation------MSFFDSLRQ
------CCHHHHHHH		34.3228152593
22PhosphorylationDKLADSFTPTLTRDE
HHHHHHCCCCCCCCC		21.2230377154
107PhosphorylationCVLILNISTIKRVER
EEEEEEHHHCEEEEC		24.0119779198
115PhosphorylationTIKRVERSPSESYEF
HCEEEECCCCCCHHH		21.1927017623
119PhosphorylationVERSPSESYEFALLV
EECCCCCCHHHHHHH		34.0127017623
120PhosphorylationERSPSESYEFALLVT
ECCCCCCHHHHHHHH		15.8327017623
127PhosphorylationYEFALLVTLYTGAKV
HHHHHHHHHHHCHHH		17.6427017623
129PhosphorylationFALLVTLYTGAKVLI
HHHHHHHHHCHHHHH		8.1827017623
130PhosphorylationALLVTLYTGAKVLIQ
HHHHHHHHCHHHHHH		33.5027017623
186AcetylationIAKNILGKKDITVPR
HHHHCCCCCCCCCCC		43.7724489116
202PhosphorylationGLGQHFKYPGNPTMV
CCCCCCCCCCCCCCC		18.5428889911
210UbiquitinationPGNPTMVKEKAKLRL
CCCCCCCCCHHHHHH		42.5523749301
595AcetylationCRPCEKDKDPAFRKQ
CCCCCCCCCHHHHHH		76.3525381059
764PhosphorylationEVNLIDLSDDEGEEK
HCCCCCCCCCCCHHH		38.9917330950
862PhosphorylationQVRRRVDSVATRSSI
HHHHHHHHHHCHHHH		15.7017330950
865PhosphorylationRRVDSVATRSSIASV
HHHHHHHCHHHHHCC		29.0024961812
867PhosphorylationVDSVATRSSIASVES
HHHHHCHHHHHCCCC		23.0322369663
868PhosphorylationDSVATRSSIASVEST
HHHHCHHHHHCCCCC		20.9122369663
871PhosphorylationATRSSIASVESTPTA
HCHHHHHCCCCCCCC		25.4222369663
874PhosphorylationSSIASVESTPTAAAS
HHHHCCCCCCCCCCC		37.2222369663
875PhosphorylationSIASVESTPTAAASS
HHHCCCCCCCCCCCC		15.9122369663
877PhosphorylationASVESTPTAAASSIT
HCCCCCCCCCCCCCC		29.0822369663
881PhosphorylationSTPTAAASSITTKEE
CCCCCCCCCCCCCHH		19.9722369663
882PhosphorylationTPTAAASSITTKEEK
CCCCCCCCCCCCHHH		21.1622369663
884PhosphorylationTAAASSITTKEEKYD
CCCCCCCCCCHHHCC		33.4922369663
885PhosphorylationAAASSITTKEEKYDD
CCCCCCCCCHHHCCC		34.4922369663
930PhosphorylationTKAIQERSFEPLSAN
CHHHHHHCCCCCCCC		32.9619823750
935PhosphorylationERSFEPLSANSSEEK
HHCCCCCCCCCCHHH		35.8021440633
938PhosphorylationFEPLSANSSEEKSNL
CCCCCCCCCHHHHCC		38.5521440633
939PhosphorylationEPLSANSSEEKSNLI
CCCCCCCCHHHHCCC		49.9721440633
942UbiquitinationSANSSEEKSNLIEFE
CCCCCHHHHCCCCCC		40.3623749301
943PhosphorylationANSSEEKSNLIEFEA
CCCCHHHHCCCCCCC		39.9027017623
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 GYP2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GYP2_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 GYP2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YPT6_YEASTYPT6physical
10559187
SEC4_YEASTSEC4physical
10559187
SSB1_YEASTSSB1physical
19536198
GYP2_YEASTMDR1physical
22940862
ARO1_YEASTARO1genetic
27708008
AROC_YEASTARO2genetic
27708008
HXT5_YEASTHXT5genetic
27708008
SDS3_YEASTSDS3genetic
27708008
SAC1_YEASTSAC1genetic
27708008
ERG3_YEASTERG3genetic
27708008
YL446_YEASTYLR446Wgenetic
27708008
U5072_YEASTYML002Wgenetic
27708008
PYRE_YEASTURA5genetic
27708008
HFD1_YEASTHFD1genetic
27708008
MGR3_YEASTMGR3genetic
27708008
RGM1_YEASTRGM1genetic
27708008
OCA2_YEASTOCA2genetic
27708008
PPQ1_YEASTPPQ1genetic
27708008
MRN1_YEASTMRN1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GYP2_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-764; SER-862; SER-867;SER-871; SER-881 AND SER-882, 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-862, 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-764 AND SER-871, ANDMASS SPECTROMETRY.

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