GEA2_YEAST - dbPTM
GEA2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GEA2_YEAST
UniProt AC P39993
Protein Name ARF guanine-nucleotide exchange factor 2
Gene Name GEA2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1459
Subcellular Localization Cytoplasm, cytosol . Membrane
Peripheral membrane protein . Soluble and partially membrane-bound.
Protein Description Activates the ARF proteins by exchanging bound GDP for free GTP..
Protein Sequence MSDREFVTVDPVTIIIKECINLSTAMRKYSKFTSQSGVAALLGGGSEIFSNQDDYLAHTFNNLNTNKHNDPFLSGFIQLRLMLNKLKNLDNIDSLTILQPFLLIVSTSSISGYITSLALDSLQKFFTLNIINESSQNYIGAHRATVNALTHCRFEGSQQLSDDSVLLKVVFLLRSIVDSPYGDLLSNSIIYDVLQTILSLACNNRRSEVLRNAAQSTMIAVTVKIFSKLKTIEPVNVNQIYINDESYTNDVLKADTIGTNVESKEEGSQEDPIGMKVNNEEAISEDDGIEEEHIHSEKSTNGAEQLDIVQKTTRSNSRIQAYADDNYGLPVVRQYLNLLLSLIAPENELKHSYSTRIFGLELIQTALEISGDRLQLYPRLFTLISDPIFKSILFIIQNTTKLSLLQATLQLFTTLVVILGNNLQLQIELTLTRIFSILLDDGTANNSSSENKNKPSIIKELLIEQISILWTRSPSFFTSTFINFDCNLDRADVSINFLKALTKLALPESALTTTESVPPICLEGLVSLVDDMFDHMKDIDREEFGRQKNEMEILKKRDRKTEFIECTNAFNEKPKKGIPMLIEKGFIASDSDKDIAEFLFNNNNRMNKKTIGLLLCHPDKVSLLNEYIRLFDFSGLRVDEAIRILLTKFRLPGESQQIERIIEAFSSAYCENQDYDPSKISDNAEDDISTVQPDADSVFILSYSIIMLNTDLHNPQVKEHMSFEDYSGNLKGCCNHKDFPFWYLDRIYCSIRDKEIVMPEEHHGNEKWFEDAWNNLISSTTVITEIKKDTQSVMDKLTPLELLNFDRAIFKQVGPSIVSTLFNIYVVASDDHISTRMITSLDKCSYISAFFDFKDLFNDILNSIAKGTTLINSSHDDELSTLAFEYGPMPLVQIKFEDTNTEIPVSTDAVRFGRSFKGQLNTVVFFRIIRRNKDPKIFSKELWLNIVNIILTLYEDLILSPDIFPDLQKRLKLSNLPKPSPEISINKSKESKGLLSTFASYLKGDEEPTEEEIKSSKKAMECIKSSNIAASVFGNESNITADLIKTLLDSAKTEKNADNSRYFEAELLFIIELTIALFLFCKEEKELGKFILQKVFQLSHTKGLTKRTVRRMLTYKILLISLCADQTEYLSKLINDELLKKGDIFTQKFFATNQGKEFLKRLFSLTESEFYRGFLLGNENFWKFLRKVTAMKEQSESIFEYLNESIKTDSNILTNENFMWVLGLLDEISSMGAVGNHWEIEYKKLTESGHKIDKENPYKKSIELSLKSIQLTSHLLEDNNDLRKNEIFAIIQALAHQCINPCKQISEFAVVTLEQTLINKIEIPTNEMESVEELIEGGLLPLLNSSETQEDQKILISSILTIISNVYLHYLKLGKTSNETFLKILSIFNKFVEDSDIEKKLQQLILDKKSIEKGNGSSSHGSAHEQTPESNDVEIEATAPIDDNTDDDNKPKLSDVEKD
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
33PhosphorylationMRKYSKFTSQSGVAA
HHHHHHCCCHHHHCH
29.5922369663
34PhosphorylationRKYSKFTSQSGVAAL
HHHHHCCCHHHHCHH
26.0222369663
36PhosphorylationYSKFTSQSGVAALLG
HHHCCCHHHHCHHHC
34.6922369663
46PhosphorylationAALLGGGSEIFSNQD
CHHHCCCCHHCCCCH
30.6922369663
50PhosphorylationGGGSEIFSNQDDYLA
CCCCHHCCCCHHHHH
38.9622369663
55PhosphorylationIFSNQDDYLAHTFNN
HCCCCHHHHHHHHCC
17.6822369663
59PhosphorylationQDDYLAHTFNNLNTN
CHHHHHHHHCCCCCC
23.5827214570
65PhosphorylationHTFNNLNTNKHNDPF
HHHCCCCCCCCCCCC
49.1322369663
217PhosphorylationLRNAAQSTMIAVTVK
HHHHHHHHHHHHHHH
10.6619779198
222PhosphorylationQSTMIAVTVKIFSKL
HHHHHHHHHHHHHCC
13.6819779198
264UbiquitinationIGTNVESKEEGSQED
CCCCCCCCCCCCCCC
46.4023749301
268PhosphorylationVESKEEGSQEDPIGM
CCCCCCCCCCCCCCC
33.4123749301
284PhosphorylationVNNEEAISEDDGIEE
ECCHHHCCCCCCCCH
41.8622369663
296PhosphorylationIEEEHIHSEKSTNGA
CCHHHCCCCCCCCHH
46.2322369663
298UbiquitinationEEHIHSEKSTNGAEQ
HHHCCCCCCCCHHHH
66.6423749301
299PhosphorylationEHIHSEKSTNGAEQL
HHCCCCCCCCHHHHH
24.0522369663
300PhosphorylationHIHSEKSTNGAEQLD
HCCCCCCCCHHHHHH
49.0622369663
311UbiquitinationEQLDIVQKTTRSNSR
HHHHHHHHHCCCCCC
40.7523749301
312PhosphorylationQLDIVQKTTRSNSRI
HHHHHHHHCCCCCCH
15.4522369663
313PhosphorylationLDIVQKTTRSNSRIQ
HHHHHHHCCCCCCHH
38.8522369663
315PhosphorylationIVQKTTRSNSRIQAY
HHHHHCCCCCCHHHE
36.7422369663
317PhosphorylationQKTTRSNSRIQAYAD
HHHCCCCCCHHHEEC
31.8222369663
322PhosphorylationSNSRIQAYADDNYGL
CCCCHHHEECCCCCH
8.3222369663
436PhosphorylationLTLTRIFSILLDDGT
EHHHHHHHHHHCCCC
15.2324909858
573AcetylationCTNAFNEKPKKGIPM
CCCCCCCCCCCCCCC
64.3424489116
648AcetylationAIRILLTKFRLPGES
HHHHHHHHCCCCCCH
28.5824489116
974PhosphorylationLQKRLKLSNLPKPSP
HHHHHCCCCCCCCCC
34.4321440633
980PhosphorylationLSNLPKPSPEISINK
CCCCCCCCCCCCCCC
41.0921440633
984PhosphorylationPKPSPEISINKSKES
CCCCCCCCCCCCHHH
20.6021440633
992UbiquitinationINKSKESKGLLSTFA
CCCCHHHCCHHHHHH
55.4524961812
1417PhosphorylationSIEKGNGSSSHGSAH
HHHCCCCCCCCCCCC
32.4429136822
1418PhosphorylationIEKGNGSSSHGSAHE
HHCCCCCCCCCCCCC
27.9629136822
1419PhosphorylationEKGNGSSSHGSAHEQ
HCCCCCCCCCCCCCC
33.3029136822
1422PhosphorylationNGSSSHGSAHEQTPE
CCCCCCCCCCCCCCC
22.4924961812
1427PhosphorylationHGSAHEQTPESNDVE
CCCCCCCCCCCCCCE
26.4924961812
1430PhosphorylationAHEQTPESNDVEIEA
CCCCCCCCCCCEEEE
39.2624961812
1445PhosphorylationTAPIDDNTDDDNKPK
ECCCCCCCCCCCCCC
48.0429136822
1450UbiquitinationDNTDDDNKPKLSDVE
CCCCCCCCCCHHHCC
50.9924961812
1452UbiquitinationTDDDNKPKLSDVEKD
CCCCCCCCHHHCCCC
63.3324961812

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 GEA2_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GEA2_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 GEA2_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATC3_YEASTDRS2physical
14734650
ARF1_YEASTARF1genetic
11294905
GEA1_YEASTGEA1genetic
16269340
ARF1_YEASTARF1genetic
16269340
ERD2_YEASTERD2genetic
16269340
ATC3_YEASTDRS2genetic
16269340
SC6B2_YEASTSBH2genetic
16269340
SCS7_YEASTSCS7genetic
16269340
PGA3_YEASTPGA3genetic
16269340
RIC1_YEASTRIC1genetic
16269340
COPG_YEASTSEC21physical
19039328
COG4_YEASTCOG4physical
21813735
TRS65_YEASTTRS65physical
21813735
COG2_YEASTCOG2physical
21813735
TRS33_YEASTTRS33physical
21813735
TR130_YEASTTRS130physical
21813735
TRS31_YEASTTRS31physical
21813735
TRS65_YEASTTRS65genetic
21813735
MNN11_YEASTMNN11genetic
23891562
HOC1_YEASTHOC1genetic
23891562
PSD1_YEASTPSD1genetic
23891562
GYP1_YEASTGYP1genetic
23891562
SEC14_YEASTSEC14genetic
23891562
MSMO_YEASTERG25genetic
23891562
ERG3_YEASTERG3genetic
23891562
PACC_YEASTRIM101genetic
23891562
PALH_YEASTRIM21genetic
23891562
CSG2_YEASTCSG2genetic
23891562
SUR1_YEASTSUR1genetic
23891562
RAD51_YEASTRAD51genetic
23891562
ATC3_YEASTDRS2physical
23345439
ARL1_YEASTARL1physical
23345439
GEA1_YEASTGEA1genetic
23345439

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GEA2_YEAST

loading...

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-46; SER-284; THR-313 ANDSER-317, 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-284 AND THR-313, ANDMASS SPECTROMETRY.
"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-284, 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 SER-284 AND SER-317, ANDMASS SPECTROMETRY.

TOP