EF1A_YEAST - dbPTM
EF1A_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EF1A_YEAST
UniProt AC P02994
Protein Name Elongation factor 1-alpha
Gene Name TEF1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 458
Subcellular Localization Cytoplasm . Cytoplasm, cytoskeleton .
Protein Description GTP-binding component of the eukaryotic elongation factor 1 complex (eEF1). In its active GTP-bound form, binds to and delivers aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. In the presence of a correct codon-anticodon match between the aminoacyl-tRNA and the A-site codon of the ribosome-bound mRNA, the ribosome acts as a GTPase activator and the GTP is hydrolyzed. The inactive GDP-bound form leaves the ribosome and must be recycled by its guanine nucleotide exchange factor (GEF) (eEF1B subcomplex) before binding another molecule of aminoacyl-tRNA. Required for nuclear export of aminoacyl-tRNAs. May also be involved in translational quality control by targeting cotranslationally damaged proteins to the proteasome. Also exhibits actin filament-binding and -bundling activities and is involved in cytoskeleton organization. Plays a role as a negative regulator of GCN2 kinase activity by inhibiting GCN2-mediated eIF-2-alpha phosphorylation in amino acid-repleted cells. [PubMed: 21849502]
Protein Sequence MGKEKSHINVVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAELGKGSFKYAWVLDKLKAERERGITIDIALWKFETPKYQVTVIDAPGHRDFIKNMITGTSQADCAILIIAGGVGEFEAGISKDGQTREHALLAFTLGVRQLIVAVNKMDSVKWDESRFQEIVKETSNFIKKVGYNPKTVPFVPISGWNGDNMIEATTNAPWYKGWEKETKAGVVKGKTLLEAIDAIEQPSRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVIKPGMVVTFAPAGVTTEVKSVEMHHEQLEQGVPGDNVGFNVKNVSVKEIRRGNVCGDAKNDPPKGCASFNATVIVLNHPGQISAGYSPVLDCHTAHIACRFDELLEKNDRRSGKKLEDHPKFLKSGDAALVKFVPSKPMCVEAFSEYPPLGRFAVRDMRQTVAVGVIKSVDKTEKAAKVTKAAQKAAKK
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
1Blocked amino end (Met)-------MGKEKSHI
-------CCCCCCCE		18.26-
2Methylation------MGKEKSHIN
------CCCCCCCEE		46.9926545399
3Methylation-----MGKEKSHINV
-----CCCCCCCEEE		61.7526545399
5Ubiquitination---MGKEKSHINVVV
---CCCCCCCEEEEE		51.3117644757
6Phosphorylation--MGKEKSHINVVVI
--CCCCCCCEEEEEE		30.5917287358
18PhosphorylationVVIGHVDSGKSTTTG
EEEEEECCCCCCCCC		47.2117287358
20UbiquitinationIGHVDSGKSTTTGHL
EEEECCCCCCCCCEE		48.8917644757
22PhosphorylationHVDSGKSTTTGHLIY
EECCCCCCCCCEEEE		31.6820377248
23PhosphorylationVDSGKSTTTGHLIYK
ECCCCCCCCCEEEEE		37.5621440633
30AcetylationTTGHLIYKCGGIDKR
CCCEEEEECCCCCHH		21.2924489116
30MethylationTTGHLIYKCGGIDKR
CCCEEEEECCCCCHH		21.2922522802
36AcetylationYKCGGIDKRTIEKFE
EECCCCCHHHHHHHH		49.9025381059
36SuccinylationYKCGGIDKRTIEKFE
EECCCCCHHHHHHHH		49.9023954790
36UbiquitinationYKCGGIDKRTIEKFE
EECCCCCHHHHHHHH		49.9022817900
38PhosphorylationCGGIDKRTIEKFEKE
CCCCCHHHHHHHHHH		38.9523749301
412-HydroxyisobutyrylationIDKRTIEKFEKEAAE
CCHHHHHHHHHHHHH		55.78-
41AcetylationIDKRTIEKFEKEAAE
CCHHHHHHHHHHHHH		55.7824489116
41SuccinylationIDKRTIEKFEKEAAE
CCHHHHHHHHHHHHH		55.7823954790
41UbiquitinationIDKRTIEKFEKEAAE
CCHHHHHHHHHHHHH		55.7823749301
44AcetylationRTIEKFEKEAAELGK
HHHHHHHHHHHHHCC		56.6424489116
44UbiquitinationRTIEKFEKEAAELGK
HHHHHHHHHHHHHCC		56.6423749301
51UbiquitinationKEAAELGKGSFKYAW
HHHHHHCCCCEEEHH		65.1023749301
53PhosphorylationAAELGKGSFKYAWVL
HHHHCCCCEEEHHHH		23.2728889911
552-HydroxyisobutyrylationELGKGSFKYAWVLDK
HHCCCCEEEHHHHHH		35.44-
55AcetylationELGKGSFKYAWVLDK
HHCCCCEEEHHHHHH		35.4424489116
55SuccinylationELGKGSFKYAWVLDK
HHCCCCEEEHHHHHH		35.4423954790
55UbiquitinationELGKGSFKYAWVLDK
HHCCCCEEEHHHHHH		35.4423749301
56PhosphorylationLGKGSFKYAWVLDKL
HCCCCEEEHHHHHHH		12.0421440633
622-HydroxyisobutyrylationKYAWVLDKLKAERER
EEHHHHHHHHHHHHH		47.96-
62AcetylationKYAWVLDKLKAERER
EEHHHHHHHHHHHHH		47.9624489116
62SuccinylationKYAWVLDKLKAERER
EEHHHHHHHHHHHHH		47.9623954790
62UbiquitinationKYAWVLDKLKAERER
EEHHHHHHHHHHHHH		47.9623749301
64AcetylationAWVLDKLKAERERGI
HHHHHHHHHHHHHCC		54.6724489116
64UbiquitinationAWVLDKLKAERERGI
HHHHHHHHHHHHHCC		54.6722817900
72PhosphorylationAERERGITIDIALWK
HHHHHCCEEEEEEEE		18.5417287358
79"N6,N6,N6-trimethyllysine"TIDIALWKFETPKYQ
EEEEEEEEECCCCEE		33.89-
79MethylationTIDIALWKFETPKYQ
EEEEEEEEECCCCEE		33.8925446118
79UbiquitinationTIDIALWKFETPKYQ
EEEEEEEEECCCCEE		33.8922817900
82PhosphorylationIALWKFETPKYQVTV
EEEEEECCCCEEEEE		28.3717287358
84AcetylationLWKFETPKYQVTVID
EEEECCCCEEEEEEE		56.5924489116
84UbiquitinationLWKFETPKYQVTVID
EEEECCCCEEEEEEE		56.5923749301
85PhosphorylationWKFETPKYQVTVIDA
EEECCCCEEEEEEEC		14.9321440633
100UbiquitinationPGHRDFIKNMITGTS
CCCHHHHHHHCCCCC		40.2217644757
129UbiquitinationEFEAGISKDGQTREH
ECCCCCCCCCCCHHH		65.0523749301
1542-HydroxyisobutyrylationQLIVAVNKMDSVKWD
HHHHHHHCCCCCCCC		37.17-
154AcetylationQLIVAVNKMDSVKWD
HHHHHHHCCCCCCCC		37.1724489116
154SuccinylationQLIVAVNKMDSVKWD
HHHHHHHCCCCCCCC		37.1723954790
154UbiquitinationQLIVAVNKMDSVKWD
HHHHHHHCCCCCCCC		37.1723749301
157PhosphorylationVAVNKMDSVKWDESR
HHHHCCCCCCCCHHH		23.3020377248
1592-HydroxyisobutyrylationVNKMDSVKWDESRFQ
HHCCCCCCCCHHHHH		53.53-
159AcetylationVNKMDSVKWDESRFQ
HHCCCCCCCCHHHHH		53.5324489116
159SuccinylationVNKMDSVKWDESRFQ
HHCCCCCCCCHHHHH		53.5323954790
159UbiquitinationVNKMDSVKWDESRFQ
HHCCCCCCCCHHHHH		53.5323749301
163PhosphorylationDSVKWDESRFQEIVK
CCCCCCHHHHHHHHH		35.6022369663
1702-HydroxyisobutyrylationSRFQEIVKETSNFIK
HHHHHHHHHHHHHHH		62.02-
170AcetylationSRFQEIVKETSNFIK
HHHHHHHHHHHHHHH		62.0224489116
170SuccinylationSRFQEIVKETSNFIK
HHHHHHHHHHHHHHH		62.0223954790
170UbiquitinationSRFQEIVKETSNFIK
HHHHHHHHHHHHHHH		62.0223749301
173PhosphorylationQEIVKETSNFIKKVG
HHHHHHHHHHHHHHC		30.7319779198
1772-HydroxyisobutyrylationKETSNFIKKVGYNPK
HHHHHHHHHHCCCCC		36.95-
177AcetylationKETSNFIKKVGYNPK
HHHHHHHHHHCCCCC		36.9524489116
177SuccinylationKETSNFIKKVGYNPK
HHHHHHHHHHCCCCC		36.9523954790
177UbiquitinationKETSNFIKKVGYNPK
HHHHHHHHHHCCCCC		36.9523749301
1782-HydroxyisobutyrylationETSNFIKKVGYNPKT
HHHHHHHHHCCCCCC		35.76-
178AcetylationETSNFIKKVGYNPKT
HHHHHHHHHCCCCCC		35.7624489116
178UbiquitinationETSNFIKKVGYNPKT
HHHHHHHHHCCCCCC		35.7623749301
184AcetylationKKVGYNPKTVPFVPI
HHHCCCCCCCCEEEC		59.5224489116
184UbiquitinationKKVGYNPKTVPFVPI
HHHCCCCCCCCEEEC		59.5223749301
185PhosphorylationKVGYNPKTVPFVPIS
HHCCCCCCCCEEECC		34.3722369663
192PhosphorylationTVPFVPISGWNGDNM
CCCEEECCCCCCCCC		31.5221440633
203PhosphorylationGDNMIEATTNAPWYK
CCCCEEECCCCCCCC		14.0622369663
204PhosphorylationDNMIEATTNAPWYKG
CCCEEECCCCCCCCC		36.1122369663
209PhosphorylationATTNAPWYKGWEKET
ECCCCCCCCCCCHHC		9.8822369663
210AcetylationTTNAPWYKGWEKETK
CCCCCCCCCCCHHCC		54.3925381059
210SuccinylationTTNAPWYKGWEKETK
CCCCCCCCCCCHHCC		54.3923954790
210UbiquitinationTTNAPWYKGWEKETK
CCCCCCCCCCCHHCC		54.3923749301
2142-HydroxyisobutyrylationPWYKGWEKETKAGVV
CCCCCCCHHCCCCEE		65.26-
214AcetylationPWYKGWEKETKAGVV
CCCCCCCHHCCCCEE		65.2624489116
214SuccinylationPWYKGWEKETKAGVV
CCCCCCCHHCCCCEE		65.2623954790
214UbiquitinationPWYKGWEKETKAGVV
CCCCCCCHHCCCCEE		65.2622817900
2172-HydroxyisobutyrylationKGWEKETKAGVVKGK
CCCCHHCCCCEECCH		44.21-
217AcetylationKGWEKETKAGVVKGK
CCCCHHCCCCEECCH		44.2124489116
217SuccinylationKGWEKETKAGVVKGK
CCCCHHCCCCEECCH		44.2123954790
217UbiquitinationKGWEKETKAGVVKGK
CCCCHHCCCCEECCH		44.2123749301
2222-HydroxyisobutyrylationETKAGVVKGKTLLEA
HCCCCEECCHHHHHH		52.89-
222SuccinylationETKAGVVKGKTLLEA
HCCCCEECCHHHHHH		52.8923954790
222UbiquitinationETKAGVVKGKTLLEA
HCCCCEECCHHHHHH		52.8922817900
2242-HydroxyisobutyrylationKAGVVKGKTLLEAID
CCCEECCHHHHHHHH		30.22-
224AcetylationKAGVVKGKTLLEAID
CCCEECCHHHHHHHH		30.2224489116
224UbiquitinationKAGVVKGKTLLEAID
CCCEECCHHHHHHHH		30.2224961812
225PhosphorylationAGVVKGKTLLEAIDA
CCEECCHHHHHHHHH		45.2921440633
237PhosphorylationIDAIEQPSRPTDKPL
HHHHCCCCCCCCCCC		51.0621440633
240PhosphorylationIEQPSRPTDKPLRLP
HCCCCCCCCCCCCCC		56.3921440633
242AcetylationQPSRPTDKPLRLPLQ
CCCCCCCCCCCCCHH		48.7224489116
242SuccinylationQPSRPTDKPLRLPLQ
CCCCCCCCCCCCCHH		48.7223954790
242UbiquitinationQPSRPTDKPLRLPLQ
CCCCCCCCCCCCCHH		48.7223749301
2532-HydroxyisobutyrylationLPLQDVYKIGGIGTV
CCHHHEEEECCCEEE		34.42-
253AcetylationLPLQDVYKIGGIGTV
CCHHHEEEECCCEEE		34.4224489116
253SuccinylationLPLQDVYKIGGIGTV
CCHHHEEEECCCEEE		34.4223954790
253UbiquitinationLPLQDVYKIGGIGTV
CCHHHEEEECCCEEE		34.4223749301
259PhosphorylationYKIGGIGTVPVGRVE
EEECCCEEEECCEEE		21.5122369663
267PhosphorylationVPVGRVETGVIKPGM
EECCEEECCCCCCCE		33.6120377248
271AcetylationRVETGVIKPGMVVTF
EEECCCCCCCEEEEE		32.8624489116
271SuccinylationRVETGVIKPGMVVTF
EEECCCCCCCEEEEE		32.8623954790
271UbiquitinationRVETGVIKPGMVVTF
EEECCCCCCCEEEEE		32.8623749301
277PhosphorylationIKPGMVVTFAPAGVT
CCCCEEEEEECCCCC		11.5821440633
284PhosphorylationTFAPAGVTTEVKSVE
EEECCCCCEEEEEEE		19.1320377248
285PhosphorylationFAPAGVTTEVKSVEM
EECCCCCEEEEEEEH		36.0525752575
288UbiquitinationAGVTTEVKSVEMHHE
CCCCEEEEEEEHHHH		42.4222106047
289PhosphorylationGVTTEVKSVEMHHEQ
CCCEEEEEEEHHHHH		28.6125521595
311AcetylationDNVGFNVKNVSVKEI
CCCCEEEEECCCEEE		53.3824489116
311UbiquitinationDNVGFNVKNVSVKEI
CCCCEEEEECCCEEE		53.3823749301
314PhosphorylationGFNVKNVSVKEIRRG
CEEEEECCCEEEECC		36.5423749301
316"N6,N6-dimethyllysine"NVKNVSVKEIRRGNV
EEEECCCEEEECCCC		39.66-
316AcetylationNVKNVSVKEIRRGNV
EEEECCCEEEECCCC		39.6624489116
316MethylationNVKNVSVKEIRRGNV
EEEECCCEEEECCCC		39.6622522802
316UbiquitinationNVKNVSVKEIRRGNV
EEEECCCEEEECCCC		39.6623749301
328AcetylationGNVCGDAKNDPPKGC
CCCCCCCCCCCCCCC		67.6324489116
328SuccinylationGNVCGDAKNDPPKGC
CCCCCCCCCCCCCCC		67.6323954790
328UbiquitinationGNVCGDAKNDPPKGC
CCCCCCCCCCCCCCC		67.6323749301
333UbiquitinationDAKNDPPKGCASFNA
CCCCCCCCCCCEEEE		72.5123749301
355PhosphorylationPGQISAGYSPVLDCH
CCCCCCCCCCCCCCH		14.9828889911
356PhosphorylationGQISAGYSPVLDCHT
CCCCCCCCCCCCCHH		13.9628889911
3762-HydroxyisobutyrylationRFDELLEKNDRRSGK
HHHHHHHHCCCCCCC		65.21-
376AcetylationRFDELLEKNDRRSGK
HHHHHHHHCCCCCCC		65.2124489116
376SuccinylationRFDELLEKNDRRSGK
HHHHHHHHCCCCCCC		65.2123954790
376UbiquitinationRFDELLEKNDRRSGK
HHHHHHHHCCCCCCC		65.2123749301
383AcetylationKNDRRSGKKLEDHPK
HCCCCCCCCHHCCHH		56.2724489116
383UbiquitinationKNDRRSGKKLEDHPK
HCCCCCCCCHHCCHH		56.2717644757
384AcetylationNDRRSGKKLEDHPKF
CCCCCCCCHHCCHHH		61.7125381059
384UbiquitinationNDRRSGKKLEDHPKF
CCCCCCCCHHCCHHH		61.7117644757
3902-HydroxyisobutyrylationKKLEDHPKFLKSGDA
CCHHCCHHHHHCCCE		60.97-
390AcetylationKKLEDHPKFLKSGDA
CCHHCCHHHHHCCCE		60.9724489116
390MethylationKKLEDHPKFLKSGDA
CCHHCCHHHHHCCCE		60.9724517342
390UbiquitinationKKLEDHPKFLKSGDA
CCHHCCHHHHHCCCE		60.9722817900
3932-HydroxyisobutyrylationEDHPKFLKSGDAALV
HCCHHHHHCCCEEEE		56.37-
393AcetylationEDHPKFLKSGDAALV
HCCHHHHHCCCEEEE		56.3724489116
393SuccinylationEDHPKFLKSGDAALV
HCCHHHHHCCCEEEE		56.3723954790
393UbiquitinationEDHPKFLKSGDAALV
HCCHHHHHCCCEEEE		56.3723749301
394PhosphorylationDHPKFLKSGDAALVK
CCHHHHHCCCEEEEE		44.0121082442
401AcetylationSGDAALVKFVPSKPM
CCCEEEEEECCCCCC		41.3024489116
401SuccinylationSGDAALVKFVPSKPM
CCCEEEEEECCCCCC		41.3023954790
401UbiquitinationSGDAALVKFVPSKPM
CCCEEEEEECCCCCC		41.3023749301
405PhosphorylationALVKFVPSKPMCVEA
EEEEECCCCCCEEHH		44.0521440633
406AcetylationLVKFVPSKPMCVEAF
EEEECCCCCCEEHHH		30.6024489116
406UbiquitinationLVKFVPSKPMCVEAF
EEEECCCCCCEEHHH		30.6023749301
414PhosphorylationPMCVEAFSEYPPLGR
CCEEHHHHHCCCCCC		43.1817287358
416PhosphorylationCVEAFSEYPPLGRFA
EEHHHHHCCCCCCCH		14.6728889911
430PhosphorylationAVRDMRQTVAVGVIK
HHHCHHHHHEEEEEE		10.4817287358
4372-HydroxyisobutyrylationTVAVGVIKSVDKTEK
HHEEEEEEECCCHHH		41.86-
437AcetylationTVAVGVIKSVDKTEK
HHEEEEEEECCCHHH		41.8624489116
437SuccinylationTVAVGVIKSVDKTEK
HHEEEEEEECCCHHH		41.8623954790
437UbiquitinationTVAVGVIKSVDKTEK
HHEEEEEEECCCHHH		41.8623749301
438PhosphorylationVAVGVIKSVDKTEKA
HEEEEEEECCCHHHH		25.1528889911
4412-HydroxyisobutyrylationGVIKSVDKTEKAAKV
EEEEECCCHHHHHHH		57.33-
441AcetylationGVIKSVDKTEKAAKV
EEEEECCCHHHHHHH		57.3324489116
441SuccinylationGVIKSVDKTEKAAKV
EEEEECCCHHHHHHH		57.3323954790
4442-HydroxyisobutyrylationKSVDKTEKAAKVTKA
EECCCHHHHHHHHHH		59.90-
444AcetylationKSVDKTEKAAKVTKA
EECCCHHHHHHHHHH		59.9024489116
444SuccinylationKSVDKTEKAAKVTKA
EECCCHHHHHHHHHH		59.9023954790
4472-HydroxyisobutyrylationDKTEKAAKVTKAAQK
CCHHHHHHHHHHHHH		56.12-
447UbiquitinationDKTEKAAKVTKAAQK
CCHHHHHHHHHHHHH		56.1222817900
4502-HydroxyisobutyrylationEKAAKVTKAAQKAAK
HHHHHHHHHHHHHHH		44.72-
450AcetylationEKAAKVTKAAQKAAK
HHHHHHHHHHHHHHH		44.7225381059
450UbiquitinationEKAAKVTKAAQKAAK
HHHHHHHHHHHHHHH		44.7222817900
454AcetylationKVTKAAQKAAKK---
HHHHHHHHHHHC---		45.6523572591
454UbiquitinationKVTKAAQKAAKK---
HHHHHHHHHHHC---		45.6522817900
457AcetylationKAAQKAAKK------
HHHHHHHHC------		64.9723572591
458MethylationAAQKAAKK-------
HHHHHHHC-------		61.9310973948
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
267TPhosphorylationKinaseCCAMK-GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EF1A_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 EF1A_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EF1G1_YEASTCAM1physical
11805826
EF1B_YEASTEFB1physical
11805826
SSBP1_YEASTSBP1physical
11805826
EF1G2_YEASTTEF4physical
11805826
EF3A_YEASTYEF3physical
9705146
EF3A_YEASTYEF3physical
9990316
CEX1_YEASTCEX1physical
17203074
CSF1_YEASTCSF1genetic
19061648
ELP1_YEASTIKI3genetic
19061648
TRM7_YEASTTRM7genetic
19061648
MED31_YEASTSOH1genetic
19061648
ELP2_YEASTELP2genetic
19061648
XPOT_YEASTLOS1genetic
19061648
LTV1_YEASTLTV1genetic
19061648
CTK1_YEASTCTK1genetic
19061648
URM1_YEASTURM1genetic
19061648
PFD5_YEASTGIM5genetic
19061648
ELP6_YEASTELP6genetic
19061648
SYDM_YEASTMSD1genetic
19061648
ELP4_YEASTELP4genetic
19061648
ELP3_YEASTELP3genetic
19061648
NUP2_YEASTNUP2genetic
19061648
SKI2_YEASTSKI2genetic
19061648
NUP59_YEASTASM4genetic
19061648
NUP42_YEASTNUP42genetic
19061648
LRS4_YEASTLRS4genetic
19061648
EIF2A_YEASTYGR054Wgenetic
19061648
IF4F1_YEASTTIF4631genetic
19061648
MRT4_YEASTMRT4genetic
19061648
SRP40_YEASTSRP40genetic
19061648
SIN3_YEASTSIN3genetic
19061648
MLP2_YEASTMLP2genetic
19061648
ELP3_YEASTELP3genetic
19547744
GCN2_YEASTGCN2physical
21849502
RS22A_YEASTRPS22Aphysical
21849502
RS22B_YEASTRPS22Bphysical
21849502
ACTA_RABITACTA2physical
21964468
MSN5_YEASTMSN5genetic
27708008
YSP3_YEASTYSP3genetic
27708008
SNU66_YEASTSNU66genetic
27708008
MKK2_YEASTMKK2genetic
27708008
SWD1_YEASTSWD1genetic
27708008
THRC_YEASTTHR4genetic
27708008
RLA1_YEASTRPP1Agenetic
27708008
MAF1_YEASTMAF1genetic
27708008
DOS2_YEASTDOS2genetic
27708008
RPA14_YEASTRPA14genetic
27708008
TRM82_YEASTTRM82genetic
27708008
DHSD_YEASTSDH4genetic
27708008
UME6_YEASTUME6genetic
27708008
MNN10_YEASTMNN10genetic
27708008
HEL2_YEASTHEL2genetic
27708008
LSM6_YEASTLSM6genetic
27708008
PSP1_YEASTPSP1genetic
27708008
SPO73_YEASTSPO73genetic
27708008
RTR1_YEASTRTR1genetic
27708008
UBP3_YEASTUBP3genetic
27708008
IES1_YEASTIES1genetic
27708008
CGR1_YEASTCGR1genetic
27708008
CTU1_YEASTNCS6genetic
27708008
SKI8_YEASTSKI8genetic
27708008
EFM5_YEASTAML1genetic
27708008
RS25A_YEASTRPS25Agenetic
27708008
FYV8_YEASTFYV8genetic
27708008
SNG1_YEASTSNG1genetic
27708008
ELP2_YEASTELP2genetic
27708008
MED20_YEASTSRB2genetic
27708008
UBA4_YEASTUBA4genetic
27708008
STB5_YEASTSTB5genetic
27708008
URM1_YEASTURM1genetic
27708008
VPS53_YEASTVPS53genetic
27708008
ASF1_YEASTASF1genetic
27708008
DENR_YEASTTMA22genetic
27708008
KTI12_YEASTKTI12genetic
27708008
DGR2_YEASTDGR2genetic
27708008
XPOT_YEASTLOS1genetic
27708008
TM184_YEASTYKR051Wgenetic
27708008
RS21A_YEASTRPS21Agenetic
27708008
MTD1_YEASTMTD1genetic
27708008
METW_YEASTYLL058Wgenetic
27708008
YL030_YEASTYLR030Wgenetic
27708008
YL040_YEASTAFB1genetic
27708008
ICT1_YEASTICT1genetic
27708008
UPS1_YEASTUPS1genetic
27708008
LIPB_YEASTLIP2genetic
27708008
SEC22_YEASTSEC22genetic
27708008
COQ11_YEASTYLR290Cgenetic
27708008
ELP1_YEASTIKI3genetic
27708008
SST2_YEASTSST2genetic
27708008
SUB1_YEASTSUB1genetic
27708008
SAM37_YEASTSAM37genetic
27708008
VBA1_YEASTVBA1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
ELP6_YEASTELP6genetic
27708008
SWS2_YEASTSWS2genetic
27708008
CTU2_YEASTNCS2genetic
27708008
ATP23_YEASTATP23genetic
27708008
RRP6_YEASTRRP6genetic
27708008
EXO1_YEASTEXO1genetic
27708008
NRT1_YEASTNRT1genetic
27708008
AZF1_YEASTAZF1genetic
27708008
ELP3_YEASTELP3genetic
27708008
ELP4_YEASTELP4genetic
27708008
BEM4_YEASTBEM4genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
MRN1_YEASTMRN1genetic
27708008
PUS1_YEASTPUS1genetic
27708008
MDL2_YEASTMDL2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EF1A_YEAST

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"A novel post-translational modification of yeast elongation factor1A. Methylesterification at the C-terminus.";
Zobel-Thropp P., Yang M.C., Machado L., Clarke S.;
J. Biol. Chem. 275:37150-37158(2000).
Cited for: METHYLATION AT LYS-458.
"Characterization of yeast EF-1 alpha: non-conservation of post-translational modifications.";
Cavallius J., Zoll W., Chakraburtty K., Merrick W.C.;
Biochim. Biophys. Acta 1163:75-80(1993).
Cited for: PARTIAL PROTEIN SEQUENCE, AND METHYLATION AT LYS-30; LYS-79; LYS-316AND LYS-390.
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-53; THR-259; TYR-355;SER-356; SER-394 AND SER-414, 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-6; SER-18; THR-72;SER-163; SER-414 AND THR-430, AND MASS SPECTROMETRY.
"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-394, AND MASSSPECTROMETRY.

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