EF3A_YEAST - dbPTM
EF3A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF3A_YEAST
UniProt AC P16521
Protein Name Elongation factor 3A
Gene Name YEF3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1044
Subcellular Localization Cytoplasm .
Protein Description Required for the ATP-dependent release of deacylated tRNA from the ribosomal E-site during protein biosynthesis. Stimulates the eEF1A-dependent binding of aminoacyl-tRNA to the ribosomal A-site, which has reduced affinity for tRNA as long as the E-site is occupied. Plays a role as a negative regulator of the GCN2 kinase activity; impairs GCN1-mediated GCN2 activation on ribosomes by reducing GCN1-ribosome affinity, and hence GCN2-mediated eIF-2-alpha phosphorylation in amino acid-starved or repleted cells. [PubMed: 22888004]
Protein Sequence MSDSQQSIKVLEELFQKLSVATADNRHEIASEVASFLNGNIIEHDVPEHFFGELAKGIKDKKTAANAMQAVAHIANQSNLSPSVEPYIVQLVPAICTNAGNKDKEIQSVASETLISIVNAVNPVAIKALLPHLTNAIVETNKWQEKIAILAAISAMVDAAKDQVALRMPELIPVLSETMWDTKKEVKAAATAAMTKATETVDNKDIERFIPSLIQCIADPTEVPETVHLLGATTFVAEVTPATLSIMVPLLSRGLNERETGIKRKSAVIIDNMCKLVEDPQVIAPFLGKLLPGLKSNFATIADPEAREVTLRALKTLRRVGNVGEDDAIPEVSHAGDVSTTLQVVNELLKDETVAPRFKIVVEYIAAIGADLIDERIIDQQAWFTHITPYMTIFLHEKKAKDILDEFRKRAVDNIPVGPNFDDEEDEGEDLCNCEFSLAYGAKILLNKTQLRLKRARRYGICGPNGCGKSTLMRAIANGQVDGFPTQEECRTVYVEHDIDGTHSDTSVLDFVFESGVGTKEAIKDKLIEFGFTDEMIAMPISALSGGWKMKLALARAVLRNADILLLDEPTNHLDTVNVAWLVNYLNTCGITSITISHDSVFLDNVCEYIINYEGLKLRKYKGNFTEFVKKCPAAKAYEELSNTDLEFKFPEPGYLEGVKTKQKAIVKVTNMEFQYPGTSKPQITDINFQCSLSSRIAVIGPNGAGKSTLINVLTGELLPTSGEVYTHENCRIAYIKQHAFAHIESHLDKTPSEYIQWRFQTGEDRETMDRANRQINENDAEAMNKIFKIEGTPRRIAGIHSRRKFKNTYEYECSFLLGENIGMKSERWVPMMSVDNAWIPRGELVESHSKMVAEVDMKEALASGQFRPLTRKEIEEHCSMLGLDPEIVSHSRIRGLSGGQKVKLVLAAGTWQRPHLIVLDEPTNYLDRDSLGALSKALKEFEGGVIIITHSAEFTKNLTEEVWAVKDGRMTPSGHNWVSGQGAGPRIEKKEDEEDKFDAMGNKIAGGKKKKKLSSAELRKKKKERMKKKKELGDAYVSSDEEF
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------MSDSQQSIK
------CCHHHHHHH
58.229298649
2Phosphorylation------MSDSQQSIK
------CCHHHHHHH
58.2230377154
4Phosphorylation----MSDSQQSIKVL
----CCHHHHHHHHH
39.1428152593
7Phosphorylation-MSDSQQSIKVLEEL
-CCHHHHHHHHHHHH
19.4228152593
9AcetylationSDSQQSIKVLEELFQ
CHHHHHHHHHHHHHH
46.1224489116
9SuccinylationSDSQQSIKVLEELFQ
CHHHHHHHHHHHHHH
46.1223954790
9UbiquitinationSDSQQSIKVLEELFQ
CHHHHHHHHHHHHHH
46.1224961812
17AcetylationVLEELFQKLSVATAD
HHHHHHHHHCHHCCC
35.0824489116
17UbiquitinationVLEELFQKLSVATAD
HHHHHHHHHCHHCCC
35.0817644757
19PhosphorylationEELFQKLSVATADNR
HHHHHHHCHHCCCCH
19.4228889911
31PhosphorylationDNRHEIASEVASFLN
CCHHHHHHHHHHHHC
37.9622369663
35PhosphorylationEIASEVASFLNGNII
HHHHHHHHHHCCCCC
35.1322369663
56UbiquitinationHFFGELAKGIKDKKT
HHHHHHHHCCCCHHH
74.0217644757
102UbiquitinationICTNAGNKDKEIQSV
HHCCCCCCCHHHHHH
70.0717644757
104UbiquitinationTNAGNKDKEIQSVAS
CCCCCCCHHHHHHHH
59.3217644757
127UbiquitinationAVNPVAIKALLPHLT
CCCHHHHHHHHHHHH
24.2017644757
134PhosphorylationKALLPHLTNAIVETN
HHHHHHHHHHHHHCC
21.4122369663
140PhosphorylationLTNAIVETNKWQEKI
HHHHHHHCCCHHHHH
31.0722369663
142AcetylationNAIVETNKWQEKIAI
HHHHHCCCHHHHHHH
58.6424489116
142UbiquitinationNAIVETNKWQEKIAI
HHHHHCCCHHHHHHH
58.6423749301
146UbiquitinationETNKWQEKIAILAAI
HCCCHHHHHHHHHHH
23.4922817900
161UbiquitinationSAMVDAAKDQVALRM
HHHHHHHHHHHHHHC
50.8723749301
176PhosphorylationPELIPVLSETMWDTK
HHHHHHHCHHCCCCH
31.1222369663
178PhosphorylationLIPVLSETMWDTKKE
HHHHHCHHCCCCHHH
21.8622369663
182PhosphorylationLSETMWDTKKEVKAA
HCHHCCCCHHHHHHH
28.6221440633
183AcetylationSETMWDTKKEVKAAA
CHHCCCCHHHHHHHH
44.4524489116
183SuccinylationSETMWDTKKEVKAAA
CHHCCCCHHHHHHHH
44.4523954790
183UbiquitinationSETMWDTKKEVKAAA
CHHCCCCHHHHHHHH
44.4522106047
184AcetylationETMWDTKKEVKAAAT
HHCCCCHHHHHHHHH
70.5924489116
184UbiquitinationETMWDTKKEVKAAAT
HHCCCCHHHHHHHHH
70.5917644757
187"N6,N6,N6-trimethyllysine"WDTKKEVKAAATAAM
CCCHHHHHHHHHHHH
33.14-
187MethylationWDTKKEVKAAATAAM
CCCHHHHHHHHHHHH
33.1422522802
187UbiquitinationWDTKKEVKAAATAAM
CCCHHHHHHHHHHHH
33.1423749301
191PhosphorylationKEVKAAATAAMTKAT
HHHHHHHHHHHHHHH
15.3822369663
195PhosphorylationAAATAAMTKATETVD
HHHHHHHHHHHHCCC
16.8922369663
196"N6,N6,N6-trimethyllysine"AATAAMTKATETVDN
HHHHHHHHHHHCCCH
39.98-
1962-HydroxyisobutyrylationAATAAMTKATETVDN
HHHHHHHHHHHCCCH
39.98-
196AcetylationAATAAMTKATETVDN
HHHHHHHHHHHCCCH
39.9824489116
196MethylationAATAAMTKATETVDN
HHHHHHHHHHHCCCH
39.9822522802
196SuccinylationAATAAMTKATETVDN
HHHHHHHHHHHCCCH
39.9823954790
196UbiquitinationAATAAMTKATETVDN
HHHHHHHHHHHCCCH
39.9823749301
198PhosphorylationTAAMTKATETVDNKD
HHHHHHHHHCCCHHH
33.4723749301
200PhosphorylationAMTKATETVDNKDIE
HHHHHHHCCCHHHHH
28.8923749301
2042-HydroxyisobutyrylationATETVDNKDIERFIP
HHHCCCHHHHHHHHH
56.47-
204AcetylationATETVDNKDIERFIP
HHHCCCHHHHHHHHH
56.4724489116
204SuccinylationATETVDNKDIERFIP
HHHCCCHHHHHHHHH
56.4723954790
204UbiquitinationATETVDNKDIERFIP
HHHCCCHHHHHHHHH
56.4723749301
2632-HydroxyisobutyrylationNERETGIKRKSAVII
CCCCCCCCHHHEEEE
55.93-
263UbiquitinationNERETGIKRKSAVII
CCCCCCCCHHHEEEE
55.9322817900
265UbiquitinationRETGIKRKSAVIIDN
CCCCCCHHHEEEECC
37.4523749301
266PhosphorylationETGIKRKSAVIIDNM
CCCCCHHHEEEECCH
31.6221440633
275AcetylationVIIDNMCKLVEDPQV
EEECCHHHHCCCHHH
44.8124489116
275UbiquitinationVIIDNMCKLVEDPQV
EEECCHHHHCCCHHH
44.8117644757
289AcetylationVIAPFLGKLLPGLKS
HHHHHHHHHCCCHHH
49.3424489116
289SuccinylationVIAPFLGKLLPGLKS
HHHHHHHHHCCCHHH
49.3423954790
289UbiquitinationVIAPFLGKLLPGLKS
HHHHHHHHHCCCHHH
49.3423749301
295AcetylationGKLLPGLKSNFATIA
HHHCCCHHHCCCCCC
49.6324489116
295SuccinylationGKLLPGLKSNFATIA
HHHCCCHHHCCCCCC
49.6323954790
295UbiquitinationGKLLPGLKSNFATIA
HHHCCCHHHCCCCCC
49.6323749301
296PhosphorylationKLLPGLKSNFATIAD
HHCCCHHHCCCCCCC
42.0721440633
3152-HydroxyisobutyrylationEVTLRALKTLRRVGN
HHHHHHHHHHHHHCC
44.52-
350AcetylationQVVNELLKDETVAPR
HHHHHHHCCCCCCHH
67.1724489116
350UbiquitinationQVVNELLKDETVAPR
HHHHHHHCCCCCCHH
67.1723749301
359UbiquitinationETVAPRFKIVVEYIA
CCCCHHHHHHHHHHH
35.5517644757
364PhosphorylationRFKIVVEYIAAIGAD
HHHHHHHHHHHHCCC
5.5729688323
385PhosphorylationIDQQAWFTHITPYMT
CCCHHHHHCCCCCHH
11.1529688323
388PhosphorylationQAWFTHITPYMTIFL
HHHHHCCCCCHHHHC
10.7729688323
390PhosphorylationWFTHITPYMTIFLHE
HHHCCCCCHHHHCCH
9.7629688323
392PhosphorylationTHITPYMTIFLHEKK
HCCCCCHHHHCCHHH
11.6129688323
398AcetylationMTIFLHEKKAKDILD
HHHHCCHHHHHHHHH
47.4824489116
398UbiquitinationMTIFLHEKKAKDILD
HHHHCCHHHHHHHHH
47.4817644757
399AcetylationTIFLHEKKAKDILDE
HHHCCHHHHHHHHHH
58.6524489116
399UbiquitinationTIFLHEKKAKDILDE
HHHCCHHHHHHHHHH
58.6517644757
4012-HydroxyisobutyrylationFLHEKKAKDILDEFR
HCCHHHHHHHHHHHH
54.93-
401AcetylationFLHEKKAKDILDEFR
HCCHHHHHHHHHHHH
54.9324489116
401UbiquitinationFLHEKKAKDILDEFR
HCCHHHHHHHHHHHH
54.9323749301
409UbiquitinationDILDEFRKRAVDNIP
HHHHHHHHHHHHCCC
50.4517644757
443UbiquitinationFSLAYGAKILLNKTQ
HHHHHHHHHHHCHHH
29.5322817900
4482-HydroxyisobutyrylationGAKILLNKTQLRLKR
HHHHHHCHHHHHHHH
37.30-
448AcetylationGAKILLNKTQLRLKR
HHHHHHCHHHHHHHH
37.3024489116
448SuccinylationGAKILLNKTQLRLKR
HHHHHHCHHHHHHHH
37.3023954790
448UbiquitinationGAKILLNKTQLRLKR
HHHHHHCHHHHHHHH
37.3023749301
449PhosphorylationAKILLNKTQLRLKRA
HHHHHCHHHHHHHHH
31.5921440633
469AcetylationCGPNGCGKSTLMRAI
CCCCCCCHHHHHHHH
44.3224489116
469UbiquitinationCGPNGCGKSTLMRAI
CCCCCCCHHHHHHHH
44.3223749301
470PhosphorylationGPNGCGKSTLMRAIA
CCCCCCHHHHHHHHH
16.4423749301
520UbiquitinationFESGVGTKEAIKDKL
HCCCCCCHHHHHHHH
38.9417644757
5242-HydroxyisobutyrylationVGTKEAIKDKLIEFG
CCCHHHHHHHHHHCC
56.72-
526UbiquitinationTKEAIKDKLIEFGFT
CHHHHHHHHHHCCCC
46.4915699485
549UbiquitinationSALSGGWKMKLALAR
HHHCCCHHHHHHHHH
29.4515699485
5512-HydroxyisobutyrylationLSGGWKMKLALARAV
HCCCHHHHHHHHHHH
27.21-
551UbiquitinationLSGGWKMKLALARAV
HCCCHHHHHHHHHHH
27.2123749301
620UbiquitinationYEGLKLRKYKGNFTE
CCCCCCEEECCCHHH
62.8517644757
6222-HydroxyisobutyrylationGLKLRKYKGNFTEFV
CCCCEEECCCHHHHH
50.87-
622AcetylationGLKLRKYKGNFTEFV
CCCCEEECCCHHHHH
50.8724489116
622SuccinylationGLKLRKYKGNFTEFV
CCCCEEECCCHHHHH
50.8723954790
622UbiquitinationGLKLRKYKGNFTEFV
CCCCEEECCCHHHHH
50.8723749301
626PhosphorylationRKYKGNFTEFVKKCP
EEECCCHHHHHHHCH
32.3021440633
6302-HydroxyisobutyrylationGNFTEFVKKCPAAKA
CCHHHHHHHCHHHHH
54.71-
630AcetylationGNFTEFVKKCPAAKA
CCHHHHHHHCHHHHH
54.7124489116
630SuccinylationGNFTEFVKKCPAAKA
CCHHHHHHHCHHHHH
54.7123954790
630UbiquitinationGNFTEFVKKCPAAKA
CCHHHHHHHCHHHHH
54.7123749301
631UbiquitinationNFTEFVKKCPAAKAY
CHHHHHHHCHHHHHH
39.9022817900
636UbiquitinationVKKCPAAKAYEELSN
HHHCHHHHHHHHHCC
54.3223749301
638PhosphorylationKCPAAKAYEELSNTD
HCHHHHHHHHHCCCC
14.8325521595
642PhosphorylationAKAYEELSNTDLEFK
HHHHHHHCCCCCEEC
40.7522369663
644PhosphorylationAYEELSNTDLEFKFP
HHHHHCCCCCEECCC
38.2925521595
649AcetylationSNTDLEFKFPEPGYL
CCCCCEECCCCCCCC
51.1124489116
649SuccinylationSNTDLEFKFPEPGYL
CCCCCEECCCCCCCC
51.1123954790
649UbiquitinationSNTDLEFKFPEPGYL
CCCCCEECCCCCCCC
51.1124961812
660AcetylationPGYLEGVKTKQKAIV
CCCCCCCCCCCEEEE
61.9424489116
660SuccinylationPGYLEGVKTKQKAIV
CCCCCCCCCCCEEEE
61.9423954790
660UbiquitinationPGYLEGVKTKQKAIV
CCCCCCCCCCCEEEE
61.9423749301
664UbiquitinationEGVKTKQKAIVKVTN
CCCCCCCEEEEEEEC
41.4522817900
668UbiquitinationTKQKAIVKVTNMEFQ
CCCEEEEEEECCEEE
36.9123749301
679PhosphorylationMEFQYPGTSKPQITD
CEEECCCCCCCCEEE
29.1328889911
680PhosphorylationEFQYPGTSKPQITDI
EEECCCCCCCCEEEE
48.5321440633
681AcetylationFQYPGTSKPQITDIN
EECCCCCCCCEEEEE
40.5624489116
681UbiquitinationFQYPGTSKPQITDIN
EECCCCCCCCEEEEE
40.5623749301
707UbiquitinationIGPNGAGKSTLINVL
ECCCCCCHHHHHHHH
39.4723749301
708PhosphorylationGPNGAGKSTLINVLT
CCCCCCHHHHHHHHC
27.7728889911
709PhosphorylationPNGAGKSTLINVLTG
CCCCCHHHHHHHHCC
34.8329136822
715PhosphorylationSTLINVLTGELLPTS
HHHHHHHCCCCCCCC
25.0730377154
721PhosphorylationLTGELLPTSGEVYTH
HCCCCCCCCCCEECC
49.7028889911
726PhosphorylationLPTSGEVYTHENCRI
CCCCCCEECCCCCEE
9.7028889911
727PhosphorylationPTSGEVYTHENCRIA
CCCCCEECCCCCEEE
28.0828889911
735PhosphorylationHENCRIAYIKQHAFA
CCCCEEEEEHHHHHH
13.2819779198
7372-HydroxyisobutyrylationNCRIAYIKQHAFAHI
CCEEEEEHHHHHHHH
24.29-
737AcetylationNCRIAYIKQHAFAHI
CCEEEEEHHHHHHHH
24.2922865919
737UbiquitinationNCRIAYIKQHAFAHI
CCEEEEEHHHHHHHH
24.2924961812
750AcetylationHIESHLDKTPSEYIQ
HHHHHHCCCHHHHHH
69.5624489116
750UbiquitinationHIESHLDKTPSEYIQ
HHHHHHCCCHHHHHH
69.5617644757
751PhosphorylationIESHLDKTPSEYIQW
HHHHHCCCHHHHHHH
31.5428889911
753PhosphorylationSHLDKTPSEYIQWRF
HHHCCCHHHHHHHHH
48.5428889911
755PhosphorylationLDKTPSEYIQWRFQT
HCCCHHHHHHHHHCC
11.6219779198
762PhosphorylationYIQWRFQTGEDRETM
HHHHHHCCCCCHHHH
39.5717287358
768PhosphorylationQTGEDRETMDRANRQ
CCCCCHHHHHHHHHH
25.8417287358
786AcetylationNDAEAMNKIFKIEGT
HHHHHHHHHHEEECC
36.1124489116
786SuccinylationNDAEAMNKIFKIEGT
HHHHHHHHHHEEECC
36.1123954790
786UbiquitinationNDAEAMNKIFKIEGT
HHHHHHHHHHEEECC
36.1123749301
789"N6,N6,N6-trimethyllysine"EAMNKIFKIEGTPRR
HHHHHHHEEECCCCE
43.23-
7892-HydroxyisobutyrylationEAMNKIFKIEGTPRR
HHHHHHHEEECCCCE
43.23-
789AcetylationEAMNKIFKIEGTPRR
HHHHHHHEEECCCCE
43.2324489116
789MethylationEAMNKIFKIEGTPRR
HHHHHHHEEECCCCE
43.2322522802
789SuccinylationEAMNKIFKIEGTPRR
HHHHHHHEEECCCCE
43.2323954790
789UbiquitinationEAMNKIFKIEGTPRR
HHHHHHHEEECCCCE
43.2323749301
793PhosphorylationKIFKIEGTPRRIAGI
HHHEEECCCCEECCC
10.7923749301
802PhosphorylationRRIAGIHSRRKFKNT
CEECCCCCCCCCCCC
31.6821440633
807UbiquitinationIHSRRKFKNTYEYEC
CCCCCCCCCCEEEEE
51.9523749301
825AcetylationLGENIGMKSERWVPM
HCCCCCCCCCCEEEE
43.9124489116
825UbiquitinationLGENIGMKSERWVPM
HCCCCCCCCCCEEEE
43.9123749301
826PhosphorylationGENIGMKSERWVPMM
CCCCCCCCCCEEEEE
24.4121440633
834PhosphorylationERWVPMMSVDNAWIP
CCEEEEEEECCCEEE
21.7724961812
848PhosphorylationPRGELVESHSKMVAE
ECCHHHHHHCCEEEE
26.1121440633
850PhosphorylationGELVESHSKMVAEVD
CHHHHHHCCEEEEEC
31.5528889911
851UbiquitinationELVESHSKMVAEVDM
HHHHHHCCEEEEECH
31.7824961812
859AcetylationMVAEVDMKEALASGQ
EEEEECHHHHHHCCC
35.0624489116
859UbiquitinationMVAEVDMKEALASGQ
EEEEECHHHHHHCCC
35.0623749301
864PhosphorylationDMKEALASGQFRPLT
CHHHHHHCCCCCCCC
33.7028889911
873AcetylationQFRPLTRKEIEEHCS
CCCCCCHHHHHHHHH
58.7824489116
873UbiquitinationQFRPLTRKEIEEHCS
CCCCCCHHHHHHHHH
58.7823749301
902UbiquitinationRGLSGGQKVKLVLAA
CCCCCCCEEEEEEEC
44.6123749301
904UbiquitinationLSGGQKVKLVLAAGT
CCCCCEEEEEEECCC
39.6617644757
931PhosphorylationTNYLDRDSLGALSKA
CCCCCHHHHHHHHHH
29.6021440633
936PhosphorylationRDSLGALSKALKEFE
HHHHHHHHHHHHHCC
18.4921440633
937AcetylationDSLGALSKALKEFEG
HHHHHHHHHHHHCCC
59.6024489116
937UbiquitinationDSLGALSKALKEFEG
HHHHHHHHHHHHCCC
59.6023749301
940UbiquitinationGALSKALKEFEGGVI
HHHHHHHHHCCCCEE
66.2822817900
957UbiquitinationTHSAEFTKNLTEEVW
ECCHHHHCCCCCEEE
56.1117644757
9672-HydroxyisobutyrylationTEEVWAVKDGRMTPS
CCEEEEEECCCCCCC
46.87-
967AcetylationTEEVWAVKDGRMTPS
CCEEEEEECCCCCCC
46.8724489116
967SuccinylationTEEVWAVKDGRMTPS
CCEEEEEECCCCCCC
46.8723954790
967UbiquitinationTEEVWAVKDGRMTPS
CCEEEEEECCCCCCC
46.8723749301
972PhosphorylationAVKDGRMTPSGHNWV
EEECCCCCCCCCCCC
16.9722369663
974PhosphorylationKDGRMTPSGHNWVSG
ECCCCCCCCCCCCCC
43.4422369663
980PhosphorylationPSGHNWVSGQGAGPR
CCCCCCCCCCCCCCC
19.6029136822
990UbiquitinationGAGPRIEKKEDEEDK
CCCCCCCCCCCCCCC
60.1217644757
991AcetylationAGPRIEKKEDEEDKF
CCCCCCCCCCCCCCC
58.5725381059
991UbiquitinationAGPRIEKKEDEEDKF
CCCCCCCCCCCCCCC
58.5717644757
997AcetylationKKEDEEDKFDAMGNK
CCCCCCCCCHHHCCC
48.7224489116
997UbiquitinationKKEDEEDKFDAMGNK
CCCCCCCCCHHHCCC
48.7217644757
1004AcetylationKFDAMGNKIAGGKKK
CCHHHCCCCCCCHHC
28.3622865919
1004UbiquitinationKFDAMGNKIAGGKKK
CCHHHCCCCCCCHHC
28.3617644757
1011UbiquitinationKIAGGKKKKKLSSAE
CCCCCHHCCCCCHHH
59.6417644757
1012UbiquitinationIAGGKKKKKLSSAEL
CCCCHHCCCCCHHHH
68.7517644757
1013AcetylationAGGKKKKKLSSAELR
CCCHHCCCCCHHHHH
63.5825381059
1013UbiquitinationAGGKKKKKLSSAELR
CCCHHCCCCCHHHHH
63.5817644757
1015PhosphorylationGKKKKKLSSAELRKK
CHHCCCCCHHHHHHH
36.0622369663
1016PhosphorylationKKKKKLSSAELRKKK
HHCCCCCHHHHHHHH
35.8822369663
1021UbiquitinationLSSAELRKKKKERMK
CCHHHHHHHHHHHHH
79.9617644757
1030UbiquitinationKKERMKKKKELGDAY
HHHHHHHHHHHHHCC
46.0623749301
1037PhosphorylationKKELGDAYVSSDEEF
HHHHHHCCCCCCCCC
12.9525521595
1039PhosphorylationELGDAYVSSDEEF--
HHHHCCCCCCCCC--
21.2822369663
1040PhosphorylationLGDAYVSSDEEF---
HHHCCCCCCCCC---
38.7122369663

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 EF3A_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF3A_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 EF3A_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
YEC3_YEASTYEL023Cphysical
16554755
HFM1_YEASTHFM1physical
16554755
NU159_YEASTNUP159physical
16554755
POB3_YEASTPOB3physical
16554755
SEC65_YEASTSEC65physical
16554755
NEW1_YEASTNEW1physical
16554755
EF1B_YEASTEFB1physical
17179749
EF1G2_YEASTTEF4genetic
17179749
EF1G2_YEASTTEF4genetic
22194687
RS22A_YEASTRPS22Aphysical
22888004
RS22B_YEASTRPS22Bphysical
22888004
DED1_YEASTDED1genetic
27708008
STU1_YEASTSTU1genetic
27708008
KPC1_YEASTPKC1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
DCP2_YEASTDCP2genetic
27708008
PMP1_YEASTPMP1physical
26404137

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF3A_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT SER-2.
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-642; THR-644; THR-972;TYR-1037; SER-1039 AND SER-1040, 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-642; SER-1016; SER-1039AND SER-1040, 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-1015 AND SER-1016, 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-1039 AND SER-1040, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae.";
Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.;
Nat. Biotechnol. 20:301-305(2002).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1039 AND SER-1040, ANDMASS SPECTROMETRY.

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