SYT1_YEAST - dbPTM
SYT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYT1_YEAST
UniProt AC Q06836
Protein Name Arf guanine nucleotide exchange factor SYT1
Gene Name SYT1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1226
Subcellular Localization Cytoplasm .
Protein Description Guanine nucleotide exchange factor for Arf GTPases, stimulating the nucleotide exchange from the GDP-bound to the GTP-bound form. Catalyzes both the GDP release by and the GTP binding to ARF2. Has no exchange activity on Rab GTPases. Involved in vesicular transport..
Protein Sequence MNQSISSLIKLKFLQSHSNDKNGNKKGGSNVSTGIDKLRESESYRSPFLQLAEIQEHTNNDDDKLDVKECEPTKKHSKLSRIRRKMGRLDLNFRSANEKGSEDDEILVAQHLRNGQDPEEMPFKSENNIDSIEKVPKPDGERVTLTSSGSDNVKRNSKHAPFIPVKPALEKFPSSNRLSRDYRKSQEPTLFNGDRLVPTLPTVSRISTSSSVGSSTAASRYFNPSKRAVVASSSSSSSSIKFNSLHAIPLDATPQIELAKQQDEISKRRFGRRRSRTVDVFDYINKNNTAKNKPPLSPSSFIRTIDEKNTNSLMQDPMGSRGPLLPDDANIISNDTDGAEASHPDHQVLSRSRSQSTSFVQGKGGKRKSIEDEGYHNKLGLPHGSGPTSVYNNKSNANSTITGMSRRSSSIVNALSSFVNLRSSSLSSSRQQHLQQQQQLQQKLDVSLEDLPPVPAPEFSDSCKDFLIKLAPYGKFIGIILTEKDDEFKKNCLNYLLTNCFEFKNDPLDIALRKLLMFLELPKETQQIDRLIMAFSFAYYKAQKSYSKKKGIECPWSNADQVYFIAFSLLMLHTDYFNPNNKSKMTKHDFVDLVHNDKYSGGNEIPMAVLTYFYENVTAKESPKFNYFLMSPMALDDSILDKDAFDTNFAITLSSNSMYSPIDMIKRGSIIPKEASLSPIFYPLTNSISASGIAPSTAASCPPSTSGTINGANLGTANSNSNRPASNSISSYFSYNPSSSSSGNATLVQDDINVYSHIINDTLNEVNLFPEVSKYWNKNALKANLLRNEEHKYEKYYSIMNDTKGGYLRFHKSQLNKLNLPNFEILNDNSRSGCKNSDYKYCKILQMGAIMNLGMPSRKFSIVNSAKIHWKKEFAILTSLGLLICDKMDWINPQMMKDPKSGTTNYIIDFKSGFSFVPGSTIDVYNGLFADRERDSLGKSHFASLVLAYTEHHSTGSHTSNTTAASSSAKHNEGVFEPSSDEEDSITNSTDGTSSVSNGESDNDSVSSSDNQLSSNDSNEDYHSIKDEYPIFEDENADCLLYLHTCHRNFIWKCANKYERDNWIDSINLFSAYDGCYVEIGSIANTICNKRKLTILQRMERLRSIKSAKWEKLKKFESTLMLMGKCVPISTKTKTDMINRIRQLAVRMDWLIYEIKRSELFVSIIKEVTRKQAEKNILEHGKGEEEGQGNNDDSDGIDDIEESFLFNENSLQVCVSDSSYDEYSNE
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----MNQSISSLIKL
----CCHHHHHHHHH		35.7130377154
6Phosphorylation--MNQSISSLIKLKF
--CCHHHHHHHHHHH		25.0830377154
95PhosphorylationRLDLNFRSANEKGSE
CCCCCCCCCCCCCCC		31.1729688323
101PhosphorylationRSANEKGSEDDEILV
CCCCCCCCCCHHHHH		49.2521440633
144PhosphorylationKPDGERVTLTSSGSD
CCCCCCEEEECCCCC		30.4622890988
146PhosphorylationDGERVTLTSSGSDNV
CCCCEEEECCCCCCC		16.1022890988
147PhosphorylationGERVTLTSSGSDNVK
CCCEEEECCCCCCCC		35.5022890988
148PhosphorylationERVTLTSSGSDNVKR
CCEEEECCCCCCCCC		36.7622890988
150PhosphorylationVTLTSSGSDNVKRNS
EEEECCCCCCCCCCC		28.1422890988
157PhosphorylationSDNVKRNSKHAPFIP
CCCCCCCCCCCCCCC		29.8321551504
174PhosphorylationPALEKFPSSNRLSRD
HHHHHCCCCCCCCCC		43.2917287358
175PhosphorylationALEKFPSSNRLSRDY
HHHHCCCCCCCCCCH		26.6317287358
202PhosphorylationRLVPTLPTVSRISTS
CCCCCCCCEEEEECC		33.9421440633
207PhosphorylationLPTVSRISTSSSVGS
CCCEEEEECCCCCCC		22.5622369663
208PhosphorylationPTVSRISTSSSVGSS
CCEEEEECCCCCCCC		30.2022369663
209PhosphorylationTVSRISTSSSVGSST
CEEEEECCCCCCCCH		17.5222369663
210PhosphorylationVSRISTSSSVGSSTA
EEEEECCCCCCCCHH		29.1822369663
211PhosphorylationSRISTSSSVGSSTAA
EEEECCCCCCCCHHH		30.2022369663
214PhosphorylationSTSSSVGSSTAASRY
ECCCCCCCCHHHHHH		23.5122369663
215PhosphorylationTSSSVGSSTAASRYF
CCCCCCCCHHHHHHC		19.0122369663
216PhosphorylationSSSVGSSTAASRYFN
CCCCCCCHHHHHHCC		28.1322369663
219PhosphorylationVGSSTAASRYFNPSK
CCCCHHHHHHCCCCC		25.6722369663
225PhosphorylationASRYFNPSKRAVVAS
HHHHCCCCCCEEEEE		35.5621440633
232PhosphorylationSKRAVVASSSSSSSS
CCCEEEEECCCCCCC		21.1022369663
233PhosphorylationKRAVVASSSSSSSSI
CCEEEEECCCCCCCC		25.2222369663
234PhosphorylationRAVVASSSSSSSSIK
CEEEEECCCCCCCCE		31.5722369663
235PhosphorylationAVVASSSSSSSSIKF
EEEEECCCCCCCCEE		35.8722369663
236PhosphorylationVVASSSSSSSSIKFN
EEEECCCCCCCCEEC		35.8722369663
237PhosphorylationVASSSSSSSSIKFNS
EEECCCCCCCCEECE		30.0122369663
238PhosphorylationASSSSSSSSIKFNSL
EECCCCCCCCEECEE		37.7222369663
239PhosphorylationSSSSSSSSIKFNSLH
ECCCCCCCCEECEEE		31.5722369663
266PhosphorylationAKQQDEISKRRFGRR
HHCHHHHHHHHHCCC		20.3330377154
275PhosphorylationRRFGRRRSRTVDVFD
HHHCCCCCCEECHHH		30.4122369663
277PhosphorylationFGRRRSRTVDVFDYI
HCCCCCCEECHHHHH		23.4622369663
297PhosphorylationAKNKPPLSPSSFIRT
CCCCCCCCHHHHEEC		28.6325752575
299PhosphorylationNKPPLSPSSFIRTID
CCCCCCHHHHEECCC		34.2119684113
300PhosphorylationKPPLSPSSFIRTIDE
CCCCCHHHHEECCCC		28.2519684113
304PhosphorylationSPSSFIRTIDEKNTN
CHHHHEECCCCCCCC		28.1521440633
312PhosphorylationIDEKNTNSLMQDPMG
CCCCCCCCCCCCCCC		24.1527214570
352PhosphorylationDHQVLSRSRSQSTSF
CHHHHCCCCCCCCCC		32.6722369663
354PhosphorylationQVLSRSRSQSTSFVQ
HHHCCCCCCCCCCCC		29.7222369663
356PhosphorylationLSRSRSQSTSFVQGK
HCCCCCCCCCCCCCC		27.5422369663
357PhosphorylationSRSRSQSTSFVQGKG
CCCCCCCCCCCCCCC		20.6722369663
358PhosphorylationRSRSQSTSFVQGKGG
CCCCCCCCCCCCCCC		28.7722369663
369PhosphorylationGKGGKRKSIEDEGYH
CCCCCCCCCCCCCCC		34.9319823750
385PhosphorylationKLGLPHGSGPTSVYN
CCCCCCCCCCCCCCC		38.2719823750
388PhosphorylationLPHGSGPTSVYNNKS
CCCCCCCCCCCCCCC		34.0629136822
389PhosphorylationPHGSGPTSVYNNKSN
CCCCCCCCCCCCCCC		26.2429136822
391PhosphorylationGSGPTSVYNNKSNAN
CCCCCCCCCCCCCCC		16.8819823750
395PhosphorylationTSVYNNKSNANSTIT
CCCCCCCCCCCCCCC		43.2122369663
399PhosphorylationNNKSNANSTITGMSR
CCCCCCCCCCCCCCC		20.8328889911
405PhosphorylationNSTITGMSRRSSSIV
CCCCCCCCCCHHHHH		26.3628889911
408PhosphorylationITGMSRRSSSIVNAL
CCCCCCCHHHHHHHH		27.5921440633
409PhosphorylationTGMSRRSSSIVNALS
CCCCCCHHHHHHHHH		23.4422369663
410PhosphorylationGMSRRSSSIVNALSS
CCCCCHHHHHHHHHH		31.6321440633
416PhosphorylationSSIVNALSSFVNLRS
HHHHHHHHHHHHHHH		21.2222369663
417PhosphorylationSIVNALSSFVNLRSS
HHHHHHHHHHHHHHC		33.7822369663
425PhosphorylationFVNLRSSSLSSSRQQ
HHHHHHCCCCHHHHH		33.2523749301
428PhosphorylationLRSSSLSSSRQQHLQ
HHHCCCCHHHHHHHH		34.5323749301
473PhosphorylationFLIKLAPYGKFIGII
HHHHHCCCCCEEEEE		27.6021440633
622PhosphorylationENVTAKESPKFNYFL
HCCCCCCCCCCCEEE		32.4627017623
647PhosphorylationLDKDAFDTNFAITLS
CCCCCCCCCEEEEEC		26.2827017623
652PhosphorylationFDTNFAITLSSNSMY
CCCCEEEEECCCCCC		19.7027017623
654PhosphorylationTNFAITLSSNSMYSP
CCEEEEECCCCCCCC		20.8727017623
655PhosphorylationNFAITLSSNSMYSPI
CEEEEECCCCCCCCC		35.7227017623
657PhosphorylationAITLSSNSMYSPIDM
EEEECCCCCCCCCHH		22.5027017623
669PhosphorylationIDMIKRGSIIPKEAS
CHHHHCCCCCCCCCC		22.7525315811
1118PhosphorylationEKLKKFESTLMLMGK
HHHHHHHHHHHHCCC		29.9428889911
1130PhosphorylationMGKCVPISTKTKTDM
CCCEEECCCCCHHHH		20.1328889911
1131PhosphorylationGKCVPISTKTKTDMI
CCEEECCCCCHHHHH		43.3728889911
1133PhosphorylationCVPISTKTKTDMINR
EEECCCCCHHHHHHH		38.9928889911
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 SYT1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYT1_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 SYT1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARF2_YEASTARF2physical
10430582
SSB1_YEASTSSB1physical
19536198
RGP1_YEASTRGP1genetic
21987634
PEP7_YEASTPEP7genetic
21987634
RV167_YEASTRVS167genetic
21987634
VPS52_YEASTVPS52genetic
21987634
ISC1_YEASTISC1genetic
21987634
GET1_YEASTGET1genetic
21987634
ICE2_YEASTICE2genetic
21987634
RIC1_YEASTRIC1genetic
21987634
CDC42_YEASTCDC42genetic
21987634
ARV1_YEASTARV1genetic
21987634
YPT6_YEASTYPT6genetic
21987634
PFD5_YEASTGIM5genetic
21987634
CYK2_YEASTHOF1genetic
21987634
SCS7_YEASTSCS7genetic
21987634
RTG1_YEASTRTG1genetic
21987634
SSB1_YEASTSSB1physical
22940862
HSP72_YEASTSSA2physical
22940862
HSP71_YEASTSSA1physical
22940862
MAK16_YEASTMAK16genetic
27708008
KPC1_YEASTPKC1genetic
27708008
EXO84_YEASTEXO84genetic
27708008
GPI11_YEASTGPI11genetic
27708008
GPI19_YEASTGPI19genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
ARPC5_YEASTARC15genetic
27708008
RFC2_YEASTRFC2genetic
27708008
ABF1_YEASTABF1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
RPB2_YEASTRPB2genetic
27708008
GPI2_YEASTGPI2genetic
27708008
NIP7_YEASTNIP7genetic
27708008
OST4_YEASTOST4genetic
27708008
MNN10_YEASTMNN10genetic
27708008
THIK_YEASTPOT1genetic
27708008
PTM1_YEASTPTM1genetic
27708008
RS30A_YEASTRPS30Agenetic
27708008
RS30B_YEASTRPS30Agenetic
27708008
ROM2_YEASTROM2genetic
27708008
RAD14_YEASTRAD14genetic
27708008
PHO23_YEASTPHO23genetic
27708008
PMT3_YEASTPMT3genetic
27708008
MTHR1_YEASTMET12genetic
27708008
RU2A_YEASTLEA1genetic
27708008
ATC7_YEASTNEO1genetic
29674565
INO2_YEASTINO2genetic
29674565
NUM1_YEASTNUM1genetic
29674565
GPI19_YEASTGPI19genetic
29674565
SEC15_YEASTSEC15genetic
29674565
SLT2_YEASTSLT2genetic
29674565
ARP1_YEASTARP1genetic
29674565
ICE2_YEASTICE2genetic
29674565
EXO70_YEASTEXO70genetic
29674565
BET3_YEASTBET3genetic
29674565
LDB18_YEASTLDB18genetic
29674565
CSF1_YEASTCSF1genetic
29674565
SCS7_YEASTSCS7genetic
29674565
DYN3_YEASTDYN3genetic
29674565
LIS1_YEASTPAC1genetic
29674565
GGPPS_YEASTBTS1genetic
29674565
GPI2_YEASTGPI2genetic
29674565
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYT1_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-210; SER-211; SER-275;THR-277; SER-356; SER-369; SER-385 AND SER-409, AND MASS SPECTROMETRY.
"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-369, AND MASSSPECTROMETRY.
"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 THR-277, 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-277, AND MASSSPECTROMETRY.
"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-277, AND MASSSPECTROMETRY.

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