ERF1_YEAST - dbPTM
ERF1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERF1_YEAST
UniProt AC P12385
Protein Name Eukaryotic peptide chain release factor subunit 1
Gene Name SUP45
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 437
Subcellular Localization Cytoplasm .
Protein Description Directs the termination of nascent peptide synthesis (translation) in response to the termination codons UAA, UAG and UGA..
Protein Sequence MDNEVEKNIEIWKVKKLVQSLEKARGNGTSMISLVIPPKGQIPLYQKMLTDEYGTASNIKSRVNRLSVLSAITSTQQKLKLYNTLPKNGLVLYCGDIITEDGKEKKVTFDIEPYKPINTSLYLCDNKFHTEVLSELLQADDKFGFIVMDGQGTLFGSVSGNTRTVLHKFTVDLPKKHGRGGQSALRFARLREEKRHNYVRKVAEVAVQNFITNDKVNVKGLILAGSADFKTDLAKSELFDPRLACKVISIVDVSYGGENGFNQAIELSAEALANVKYVQEKKLLEAYFDEISQDTGKFCYGIDDTLKALDLGAVEKLIVFENLETIRYTFKDAEDNEVIKFAEPEAKDKSFAIDKATGQEMDVVSEEPLIEWLAANYKNFGATLEFITDKSSEGAQFVTGFGGIGAMLRYKVNFEQLVDESEDEYYDEDEGSDYDFI
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
13AcetylationEKNIEIWKVKKLVQS
HHHHHHHHHHHHHHH		50.2524489116
15UbiquitinationNIEIWKVKKLVQSLE
HHHHHHHHHHHHHHH		36.3417644757
16UbiquitinationIEIWKVKKLVQSLEK
HHHHHHHHHHHHHHH		57.8017644757
23AcetylationKLVQSLEKARGNGTS
HHHHHHHHHCCCCCE		48.9922865919
23UbiquitinationKLVQSLEKARGNGTS
HHHHHHHHHCCCCCE		48.9917644757
30PhosphorylationKARGNGTSMISLVIP
HHCCCCCEEEEEECC		18.6021440633
33PhosphorylationGNGTSMISLVIPPKG
CCCCEEEEEECCCCC		14.1430377154
47UbiquitinationGQIPLYQKMLTDEYG
CCCCHHHHHHCCCCC		23.4823749301
47AcetylationGQIPLYQKMLTDEYG
CCCCHHHHHHCCCCC		23.4824489116
50PhosphorylationPLYQKMLTDEYGTAS
CHHHHHHCCCCCCHH		24.2421126336
60UbiquitinationYGTASNIKSRVNRLS
CCCHHHHHHHHHHHH		36.1423749301
60AcetylationYGTASNIKSRVNRLS
CCCHHHHHHHHHHHH		36.1424489116
60SuccinylationYGTASNIKSRVNRLS
CCCHHHHHHHHHHHH		36.1423954790
602-HydroxyisobutyrylationYGTASNIKSRVNRLS
CCCHHHHHHHHHHHH		36.14-
67PhosphorylationKSRVNRLSVLSAITS
HHHHHHHHHHHHHHC		20.1330377154
78UbiquitinationAITSTQQKLKLYNTL
HHHCHHHHHHHHHCC		37.4617644757
78AcetylationAITSTQQKLKLYNTL
HHHCHHHHHHHHHCC		37.4624489116
80AcetylationTSTQQKLKLYNTLPK
HCHHHHHHHHHCCCC		56.8324489116
84PhosphorylationQKLKLYNTLPKNGLV
HHHHHHHCCCCCCEE		30.7727017623
103AcetylationDIITEDGKEKKVTFD
CEECCCCCCCEEEEE		77.8824489116
168AcetylationNTRTVLHKFTVDLPK
CCCEEEEEEEEECCH		38.2724489116
175AcetylationKFTVDLPKKHGRGGQ
EEEEECCHHHCCCHH		65.7825381059
182MethylationKKHGRGGQSALRFAR
HHHCCCHHHHHHHHH		28.4916321977
201UbiquitinationKRHNYVRKVAEVAVQ
HHCHHHHHHHHHHHH		35.4317644757
215AcetylationQNFITNDKVNVKGLI
HHCCCCCCCCEEEEE		37.4724489116
215UbiquitinationQNFITNDKVNVKGLI
HHCCCCCCCCEEEEE		37.4717644757
235UbiquitinationDFKTDLAKSELFDPR
CCCHHHHHCCCCCHH		52.3324961812
235AcetylationDFKTDLAKSELFDPR
CCCHHHHHCCCCCHH		52.3324489116
282AcetylationVKYVQEKKLLEAYFD
CCHHHHHHHHHHHHH		58.5124489116
331AcetylationETIRYTFKDAEDNEV
EEEEEEECCCCCCCE		48.5024489116
331UbiquitinationETIRYTFKDAEDNEV
EEEEEEECCCCCCCE		48.5023749301
331SuccinylationETIRYTFKDAEDNEV
EEEEEEECCCCCCCE		48.5023954790
340AcetylationAEDNEVIKFAEPEAK
CCCCCEEEECCCCCC		43.6324489116
347AcetylationKFAEPEAKDKSFAID
EECCCCCCCCCEEEE		65.1224489116
347UbiquitinationKFAEPEAKDKSFAID
EECCCCCCCCCEEEE		65.1223749301
349UbiquitinationAEPEAKDKSFAIDKA
CCCCCCCCCEEEECC		46.9323749301
350PhosphorylationEPEAKDKSFAIDKAT
CCCCCCCCEEEECCC		30.0021440633
377PhosphorylationIEWLAANYKNFGATL
HHHHHHHCCCCCEEE		11.5527017623
390UbiquitinationTLEFITDKSSEGAQF
EEEEEECCCCCCCEE		47.4317644757
392PhosphorylationEFITDKSSEGAQFVT
EEEECCCCCCCEEEE		45.8728889911
399PhosphorylationSEGAQFVTGFGGIGA
CCCCEEEECCCCHHH		28.2528889911
421PhosphorylationFEQLVDESEDEYYDE
HHHHCCCCCCCCCCC		45.9828152593
425PhosphorylationVDESEDEYYDEDEGS
CCCCCCCCCCCCCCC		28.6519823750
426PhosphorylationDESEDEYYDEDEGSD
CCCCCCCCCCCCCCC		15.7119823750
432PhosphorylationYYDEDEGSDYDFI--
CCCCCCCCCCCCC--		30.8328152593
434PhosphorylationDEDEGSDYDFI----
CCCCCCCCCCC----		17.9119823750
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 ERF1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
182QMethylation

15509572
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 ERF1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERF3_YEASTSUP35physical
11805826
CLU_YEASTCLU1physical
11805826
CORO_YEASTCRN1physical
11805826
ECM29_YEASTECM29physical
11805826
IMB4_YEASTKAP123physical
11805826
ATR_YEASTMEC1physical
11805826
C1TM_YEASTMIS1physical
11805826
ROM2_YEASTROM2physical
11805826
RPA2_YEASTRPA135physical
11805826
SEN54_YEASTSEN54physical
11805826
TAO3_YEASTTAO3physical
11805826
USO1_YEASTUSO1physical
11805826
UTP20_YEASTUTP20physical
11805826
YJB6_YEASTYJL016Wphysical
11805826
VAC14_YEASTVAC14physical
11805826
ERF3_YEASTSUP35physical
7556078
ERF3_YEASTSUP35physical
9111351
MLC1_YEASTMLC1physical
15228544
ERF3_YEASTSUP35physical
15337765
NAM7_YEASTNAM7physical
9620853
ITT1_YEASTITT1genetic
11570975
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RS7A_YEASTRPS7Aphysical
16429126
CORO_YEASTCRN1physical
16429126
ATR_YEASTMEC1physical
16429126
ROM2_YEASTROM2physical
16429126
RL36B_YEASTRPL36Bphysical
16429126
SEN54_YEASTSEN54physical
16429126
ERF3_YEASTSUP35physical
16429126
TAO3_YEASTTAO3physical
16429126
USO1_YEASTUSO1physical
16429126
VAC14_YEASTVAC14physical
16429126
UPF3_YEASTUPF3genetic
17705828
ERF3_YEASTSUP35physical
18463713
GLE1_YEASTGLE1physical
18724935
EF3A_YEASTYEF3genetic
19545407
EF1G2_YEASTTEF4genetic
19545407
EF1B_YEASTEFB1genetic
19545407
RLI1_YEASTRLI1physical
20062004
HEMH_YEASTHEM15physical
20062004
NAM7_YEASTNAM7genetic
17705828
MLC1_YEASTMLC1genetic
15228544
DBP5_YEASTDBP5genetic
17272721
ERF3_YEASTSUP35genetic
20444877
NAM7_YEASTNAM7genetic
22670525
NMD2_YEASTNMD2genetic
22670525
UPF3_YEASTUPF3genetic
22670525
NAM7_YEASTNAM7physical
22670525
RL21B_YEASTRPL21Bgenetic
27708008
RPB1_YEASTRPO21genetic
27708008
UBC3_YEASTCDC34genetic
27708008
RLI1_YEASTRLI1genetic
27708008
ERF3_YEASTSUP35genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RPN11_YEASTRPN11genetic
27708008
STT3_YEASTSTT3genetic
27708008
PRS8_YEASTRPT6genetic
27708008
HSF_YEASTHSF1genetic
27708008
TAF6_YEASTTAF6genetic
27708008
CDC12_YEASTCDC12genetic
27708008
DNA2_YEASTDNA2genetic
27708008
ARP3_YEASTARP3genetic
27708008
CDC11_YEASTCDC11genetic
27708008
PRS7_YEASTRPT1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
PRS10_YEASTRPT4genetic
27708008
PSA7_YEASTPRE10genetic
27708008
RPN4_YEASTRPN4genetic
27708008
OST4_YEASTOST4genetic
27708008
H2A1_YEASTHTA1genetic
27708008
RL2A_YEASTRPL2Agenetic
27708008
RL2B_YEASTRPL2Agenetic
27708008
RPN10_YEASTRPN10genetic
27708008
SDS3_YEASTSDS3genetic
27708008
FYV10_YEASTFYV10genetic
27708008
CYP7_YEASTCPR7genetic
27708008
MOG1_YEASTMOG1genetic
27708008
IRS4_YEASTIRS4genetic
27708008
MLP1_YEASTMLP1genetic
27708008
RT109_YEASTRTT109genetic
27708008
BPT1_YEASTBPT1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
TPM1_YEASTTPM1genetic
27708008
TEP1_YEASTTEP1genetic
27708008
EAF7_YEASTEAF7genetic
27708008
GPD2_YEASTGPD2genetic
27708008
STI1_YEASTSTI1genetic
27708008
YPK9_YEASTYPK9genetic
27708008
RU2A_YEASTLEA1genetic
27708008
AXL1_YEASTAXL1genetic
27708008
CTF4_YEASTCTF4genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERF1_YEAST

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Related Literatures of Post-Translational Modification
Methylation
ReferencePubMed
"The yeast translation release factors Mrf1p and Sup45p (eRF1) aremethylated, respectively, by the methyltransferases Mtq1p and Mtq2p.";
Polevoda B., Span L., Sherman F.;
J. Biol. Chem. 281:2562-2571(2006).
Cited for: METHYLATION AT GLN-182, AND MASS SPECTROMETRY.
"The glutamine residue of the conserved GGQ motif in Saccharomycescerevisiae release factor eRF1 is methylated by the product of theYDR140w gene.";
Heurgue-Hamard V., Champ S., Mora L., Merkulova-Rainon T.,Kisselev L.L., Buckingham R.H.;
J. Biol. Chem. 280:2439-2445(2005).
Cited for: METHYLATION AT GLN-182, AND MASS SPECTROMETRY.

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