EF1G2_YEAST - dbPTM
EF1G2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1G2_YEAST
UniProt AC P36008
Protein Name Elongation factor 1-gamma 2
Gene Name TEF4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 412
Subcellular Localization Cytoplasm .
Protein Description Subunit of the eukaryotic elongation factor 1 complex (eEF1). Probably plays a role in anchoring the complex to other cellular components (By similarity)..
Protein Sequence MSQGTLYINRSPRNYASEALISYFKLDVKIVDLEQSSEFASLFPLKQAPAFLGPKGLKLTEALAIQFYLANQVADEKERARLLGSDVIEKSQILRWASLANSDVMSNIARPFLSFKGLIPYNKKDVDACFVKIDNLAAVFDARLRDYTFVATENISLGDLHAAGSWAFGLATILGPEWRAKHPHLMRWFNTVAASPIVKTPFAEVKLAEKALTYTPPKKQKAEKPKAEKSKAEKKKDEAKPADDAAPAKKPKHPLEALGKSTFVLDDWKRKYSNDDTRPVALPWFWEHYNPEEYSIWKVGYKYNDELTLTFMSNNLVGGFFNRLSASTKYMFGCLVVYGENNNNGIVGAVMVRGQDFAPAFDVAPDWESYEYTKLDPTKEEDKEFVNNMWAWDKPVVVNGEDKEIVDGKVLK
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------MSQGTLYIN
------CCCCCEEEC		37.0022814378
2Phosphorylation------MSQGTLYIN
------CCCCCEEEC		37.0024961812
5Phosphorylation---MSQGTLYINRSP
---CCCCCEEECCCC		14.5724961812
7Phosphorylation-MSQGTLYINRSPRN
-CCCCCEEECCCCCC		8.9330377154
11PhosphorylationGTLYINRSPRNYASE
CCEEECCCCCCHHHH		24.5928152593
25UbiquitinationEALISYFKLDVKIVD
HHHHHHHCCEEEEEE		35.2317644757
29UbiquitinationSYFKLDVKIVDLEQS
HHHCCEEEEEEHHHC		36.3617644757
36PhosphorylationKIVDLEQSSEFASLF
EEEEHHHCHHHHHHC		23.5924961812
37PhosphorylationIVDLEQSSEFASLFP
EEEHHHCHHHHHHCC		36.1121551504
41PhosphorylationEQSSEFASLFPLKQA
HHCHHHHHHCCHHHC		35.5424961812
46AcetylationFASLFPLKQAPAFLG
HHHHCCHHHCCCCCC		44.6524489116
46SuccinylationFASLFPLKQAPAFLG
HHHHCCHHHCCCCCC		44.6523954790
46UbiquitinationFASLFPLKQAPAFLG
HHHHCCHHHCCCCCC		44.6522106047
55SuccinylationAPAFLGPKGLKLTEA
CCCCCCCCCCHHHHH		75.0723954790
77UbiquitinationANQVADEKERARLLG
HHHCCCHHHHHHHHC		53.7123749301
85PhosphorylationERARLLGSDVIEKSQ
HHHHHHCCHHHCHHH		28.7722369663
90AcetylationLGSDVIEKSQILRWA
HCCHHHCHHHHHHHH		36.2124489116
90SuccinylationLGSDVIEKSQILRWA
HCCHHHCHHHHHHHH		36.2123954790
90UbiquitinationLGSDVIEKSQILRWA
HCCHHHCHHHHHHHH		36.2123749301
116AcetylationARPFLSFKGLIPYNK
CHHCCCCCCCCCCCC		49.8124489116
123SuccinylationKGLIPYNKKDVDACF
CCCCCCCCCCCCEEE		44.5023954790
123AcetylationKGLIPYNKKDVDACF
CCCCCCCCCCCCEEE		44.5024489116
124AcetylationGLIPYNKKDVDACFV
CCCCCCCCCCCEEEE		60.3824489116
199AcetylationVAASPIVKTPFAEVK
CCCCCCCCCCCCEEE		51.7224489116
199UbiquitinationVAASPIVKTPFAEVK
CCCCCCCCCCCCEEE		51.7223749301
200PhosphorylationAASPIVKTPFAEVKL
CCCCCCCCCCCEEEH		16.8522369663
206AcetylationKTPFAEVKLAEKALT
CCCCCEEEHHHHHHH		33.2224489116
210UbiquitinationAEVKLAEKALTYTPP
CEEEHHHHHHHCCCC		42.9923749301
210AcetylationAEVKLAEKALTYTPP
CEEEHHHHHHHCCCC		42.9924489116
213PhosphorylationKLAEKALTYTPPKKQ
EHHHHHHHCCCCCCH		30.1522369663
214PhosphorylationLAEKALTYTPPKKQK
HHHHHHHCCCCCCHH		20.3522369663
215PhosphorylationAEKALTYTPPKKQKA
HHHHHHCCCCCCHHC		28.0722369663
218SuccinylationALTYTPPKKQKAEKP
HHHCCCCCCHHCCCC		69.8723954790
240UbiquitinationEKKKDEAKPADDAAP
HHHHHCCCCCCCCCC		38.4022106047
252UbiquitinationAAPAKKPKHPLEALG
CCCCCCCCCCHHHCC		67.7317644757
260AcetylationHPLEALGKSTFVLDD
CCHHHCCCCEEEECC		47.3624489116
260UbiquitinationHPLEALGKSTFVLDD
CCHHHCCCCEEEECC		47.3624961812
261PhosphorylationPLEALGKSTFVLDDW
CHHHCCCCEEEECCH		25.8622369663
262PhosphorylationLEALGKSTFVLDDWK
HHHCCCCEEEECCHH		22.6522369663
269UbiquitinationTFVLDDWKRKYSNDD
EEEECCHHHHCCCCC		46.1117644757
271UbiquitinationVLDDWKRKYSNDDTR
EECCHHHHCCCCCCC		49.6717644757
272PhosphorylationLDDWKRKYSNDDTRP
ECCHHHHCCCCCCCC		19.4228889911
273PhosphorylationDDWKRKYSNDDTRPV
CCHHHHCCCCCCCCC		36.5028889911
277PhosphorylationRKYSNDDTRPVALPW
HHCCCCCCCCCCCCC		39.4724961812
298UbiquitinationPEEYSIWKVGYKYND
HHHHEEEEEEEEECC		24.9017644757
379AcetylationYTKLDPTKEEDKEFV
CCCCCCCHHHHHHHH		65.5822865919
394AcetylationNNMWAWDKPVVVNGE
HHHCCCCCCEEECCC		29.0724489116
409UbiquitinationDKEIVDGKVLK----
CCEEECCEECC----		39.6723749301
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 EF1G2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF1G2_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 EF1G2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1B_YEASTEFB1physical
11805826
FAP1_YEASTFAP1physical
11805826
GFA1_YEASTGFA1physical
11805826
THDH_YEASTILV1physical
11805826
IMB4_YEASTKAP123physical
11805826
MGA2_YEASTMGA2physical
11805826
NEW1_YEASTNEW1physical
11805826
COPB2_YEASTSEC27physical
11805826
OLA1_YEASTOLA1physical
11805826
SYEC_YEASTGUS1physical
11805826
LAM1_YEASTYSP1physical
16554755
EF1G1_YEASTCAM1physical
16554755
EF1B_YEASTEFB1physical
16429126
NEW1_YEASTNEW1physical
16429126
PFKA1_YEASTPFK1physical
16429126
RPN2_YEASTRPN2physical
16429126
OLA1_YEASTOLA1physical
16429126
THDH_YEASTILV1physical
16429126
COPB2_YEASTSEC27physical
16429126
MPG1_YEASTPSA1physical
16429126
EF1B_YEASTEFB1physical
17179749
KRR1_YEASTKRR1genetic
19061648
EIF3J_YEASTHCR1genetic
19061648
TAD3_YEASTTAD3genetic
19061648
NOT2_YEASTCDC36genetic
19061648
FBRL_YEASTNOP1genetic
19061648
RRP8_YEASTRRP8genetic
19061648
RLI1_YEASTRLI1genetic
19061648
LRS4_YEASTLRS4genetic
19061648
NMD5_YEASTNMD5genetic
19061648
LTV1_YEASTLTV1genetic
19061648
PAP2_YEASTPAP2genetic
19061648
BRX1_YEASTBRX1genetic
19061648
NU159_YEASTNUP159genetic
19061648
PFD5_YEASTGIM5genetic
19061648
ELP6_YEASTELP6genetic
19061648
LSM7_YEASTLSM7genetic
19061648
ELP4_YEASTELP4genetic
19061648
SYNC_YEASTDED81genetic
19061648
ELP5_YEASTIKI1genetic
19061648
XRN1_YEASTXRN1genetic
19061648
HIR2_YEASTHIR2genetic
19061648
RAD52_YEASTRAD52genetic
19061648
SAP30_YEASTSAP30genetic
19061648
HSC82_YEASTHSC82physical
19536198
ELP6_YEASTELP6genetic
19547744
PFD5_YEASTGIM5genetic
19547744
HIR2_YEASTHIR2genetic
19547744
PFD5_YEASTGIM5genetic
21987634
SAP30_YEASTSAP30genetic
21987634
NEW1_YEASTNEW1genetic
21987634
SSBP1_YEASTSBP1genetic
25887987
YCY0_YEASTYCR090Cgenetic
27708008
RV167_YEASTRVS167genetic
27708008
YBQ6_YEASTYBR056Wgenetic
27708008
EF1A_YEASTTEF2genetic
27708008
AIM4_YEASTAIM4genetic
27708008
SWC5_YEASTSWC5genetic
27708008
REI1_YEASTREI1genetic
27708008
RRP8_YEASTRRP8genetic
27708008
MKC7_YEASTMKC7genetic
27708008
YPS7_YEASTYPS7genetic
27708008
RGA2_YEASTRGA2genetic
27708008
TPA1_YEASTTPA1genetic
27708008
COM1_YEASTSAE2genetic
27708008
ASK10_YEASTASK10genetic
27708008
AP18B_YEASTYAP1802genetic
27708008
MET28_YEASTMET28genetic
27708008
ALN_YEASTDAL1genetic
27708008
SDHX_YEASTYJL045Wgenetic
27708008
YJY1_YEASTYJR011Cgenetic
27708008
IME1_YEASTIME1genetic
27708008
YL042_YEASTYLR042Cgenetic
27708008
SWI6_YEASTSWI6genetic
27708008
GBLP_YEASTASC1genetic
27708008
ALDH3_YEASTALD3genetic
27708008
RAD14_YEASTRAD14genetic
27708008
SIW14_YEASTSIW14genetic
27708008
NST1_YEASTNST1genetic
27708008
AIM41_YEASTAIM41genetic
27708008
RMI1_YEASTRMI1genetic
27708008
RL36A_YEASTRPL36Agenetic
29158977
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF1G2_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-85 AND THR-215, AND MASSSPECTROMETRY.

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