SYFB_YEAST - dbPTM
SYFB_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SYFB_YEAST
UniProt AC P15624
Protein Name Phenylalanine--tRNA ligase beta subunit
Gene Name FRS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 595
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MPTVSVNKQQLFDLLGKNYTSQEFDELCFEFGMEMDEDTTEEALKTGEEPELKLDISANRYDLLCIEGISQSLNEYLERKERPDYKLSKPTTKLIIDKSTEQIRPFATAAVLRNIKLNEKSYASFIALQDKLHANLCRNRSLVAMGTHDLDSIEGPFHYRALPPKDIKFVPLNQTQEFTGDKLIEFYKSPEQKNNIGRYVHIIEDSPVFPVIMDSKDRVCSLPPLINSEHSKISVNTRNILIDITATDKTKAEIVLNILTTMFSRYCDEPFTVEPVEIVSEHNGQSRLAPNFNDRIMDVSIKYINSCLGLDQSADEIAHCLKKMSLHAVQSKEDKDILHVDIPVTRPDILHACDIMEDAAVGYGFNNLPKGEKLSNANFIAKPLPINKVSDIFRVASSQATWVEVLPLTLCSHDENFKFLRQSDNGDLAVKLANPKTLEYQVVRTTLLPGILKTVKENRKHSLPIKVFETGDVVFKDDKLERKAYNERHWAAIYVGKNSGFEIIQGLLGKIMQTFRTEWIADYGAAASGRGYWIEEDDSVKTYFPGRGAKVMFRSKEGAEPKQIGHLGVLHPEVMMNFDVPFAASFVEVNAEVFL
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
5Phosphorylation---MPTVSVNKQQLF
---CCCEECCHHHHH
23.5830377154
8UbiquitinationMPTVSVNKQQLFDLL
CCCEECCHHHHHHHH
36.9524961812
21PhosphorylationLLGKNYTSQEFDELC
HHCCCCCHHHHHHHH
19.8328889911
93AcetylationKLSKPTTKLIIDKST
CCCCCCCEEEEECCC
39.9224489116
98AcetylationTTKLIIDKSTEQIRP
CCEEEEECCCHHHHH
49.2024489116
120AcetylationRNIKLNEKSYASFIA
HCCCCCCCCHHHHHH
47.9324489116
124PhosphorylationLNEKSYASFIALQDK
CCCCCHHHHHHHHHH
14.6728889911
131AcetylationSFIALQDKLHANLCR
HHHHHHHHHHHHHCC
29.2524489116
152PhosphorylationMGTHDLDSIEGPFHY
EECCCHHHCCCCCEE
29.8130377154
168AcetylationALPPKDIKFVPLNQT
CCCCCCCEEEECCCC
50.9022865919
182AcetylationTQEFTGDKLIEFYKS
CCCCCCCHHHHHHCC
53.3524489116
188AcetylationDKLIEFYKSPEQKNN
CHHHHHHCCHHHHCC
65.9324489116
189PhosphorylationKLIEFYKSPEQKNNI
HHHHHHCCHHHHCCC
23.4521440633
193AcetylationFYKSPEQKNNIGRYV
HHCCHHHHCCCCCEE
50.7525381059
193UbiquitinationFYKSPEQKNNIGRYV
HHCCHHHHCCCCCEE
50.7523749301
206PhosphorylationYVHIIEDSPVFPVIM
EEEEECCCCCCEEEE
15.3522369663
216AcetylationFPVIMDSKDRVCSLP
CEEEECCCCCEECCC
45.3424489116
216UbiquitinationFPVIMDSKDRVCSLP
CEEEECCCCCEECCC
45.3423749301
221PhosphorylationDSKDRVCSLPPLINS
CCCCCEECCCCCCCC
40.8421440633
249AcetylationIDITATDKTKAEIVL
EEEECCCCCHHHHHH
47.7924489116
306PhosphorylationVSIKYINSCLGLDQS
HHHHHHHHHCCCCCC
10.9321440633
331PhosphorylationMSLHAVQSKEDKDIL
CCHHEECCCCCCCCE
31.2627017623
373UbiquitinationNNLPKGEKLSNANFI
CCCCCCCCCCCCCEE
66.9223749301
373AcetylationNNLPKGEKLSNANFI
CCCCCCCCCCCCCEE
66.9224489116
375PhosphorylationLPKGEKLSNANFIAK
CCCCCCCCCCCEECC
44.9928889911
382AcetylationSNANFIAKPLPINKV
CCCCEECCCCCCCHH
42.1224489116
382UbiquitinationSNANFIAKPLPINKV
CCCCEECCCCCCCHH
42.1223749301
388UbiquitinationAKPLPINKVSDIFRV
CCCCCCCHHHHHHHH
43.7823749301
423PhosphorylationNFKFLRQSDNGDLAV
CCCEEEECCCCCEEE
26.9822369663
431UbiquitinationDNGDLAVKLANPKTL
CCCCEEEEECCCCCE
35.9523749301
431AcetylationDNGDLAVKLANPKTL
CCCCEEEEECCCCCE
35.9524489116
436UbiquitinationAVKLANPKTLEYQVV
EEEECCCCCEEEEEE
66.6023749301
436AcetylationAVKLANPKTLEYQVV
EEEECCCCCEEEEEE
66.6024489116
437PhosphorylationVKLANPKTLEYQVVR
EEECCCCCEEEEEEH
26.5317563356
453AcetylationTLLPGILKTVKENRK
HHCCCHHHHHHHHCC
49.7222865919
453UbiquitinationTLLPGILKTVKENRK
HHCCCHHHHHHHHCC
49.7223749301
476AcetylationETGDVVFKDDKLERK
ECCCEEECCCHHHHH
54.1024489116
476SuccinylationETGDVVFKDDKLERK
ECCCEEECCCHHHHH
54.1023954790
479AcetylationDVVFKDDKLERKAYN
CEEECCCHHHHHHHH
63.4824489116
541AcetylationIEEDDSVKTYFPGRG
ECCCCCCCEECCCCC
41.2724489116
550UbiquitinationYFPGRGAKVMFRSKE
ECCCCCCEEEEECCC
36.7423749301

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 SYFB_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SYFB_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 SYFB_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SYFA_YEASTFRS2physical
11805826
SYIC_YEASTILS1physical
16554755
SYFA_YEASTFRS2physical
16554755
GDS1_YEASTGDS1physical
16554755
SYFA_YEASTFRS2physical
16429126
MOB2_YEASTMOB2genetic
27708008
SEA4_YEASTSEA4genetic
27708008
ECM8_YEASTECM8genetic
27708008
UBC4_YEASTUBC4genetic
27708008
UBP6_YEASTUBP6genetic
27708008
DOA1_YEASTDOA1genetic
27708008
UTH1_YEASTUTH1genetic
27708008
GTR1_YEASTGTR1genetic
27708008
VPS27_YEASTVPS27genetic
27708008
ALG14_YEASTALG14genetic
27708008
DBF4_YEASTDBF4genetic
27708008
TRS23_YEASTTRS23genetic
27708008
GPI11_YEASTGPI11genetic
27708008
SP110_YEASTSPC110genetic
27708008
GPI17_YEASTGPI17genetic
27708008
GPI19_YEASTGPI19genetic
27708008
TAF6_YEASTTAF6genetic
27708008
XPO1_YEASTCRM1genetic
27708008
NU192_YEASTNUP192genetic
27708008
EXO70_YEASTEXO70genetic
27708008
GWT1_YEASTGWT1genetic
27708008
IF2A_YEASTSUI2genetic
27708008
ABF1_YEASTABF1genetic
27708008
NTR2_YEASTNTR2genetic
27708008
GPI13_YEASTGPI13genetic
27708008
GSP1_YEASTGSP1genetic
27708008
CDC91_YEASTGAB1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
OST2_YEASTOST2genetic
27708008
GPI2_YEASTGPI2genetic
27708008
YBF9_YEASTYBL059Wgenetic
27708008
ODPB_YEASTPDB1genetic
27708008
THRC_YEASTTHR4genetic
27708008
PDP2_YEASTPTC6genetic
27708008
MTU1_YEASTSLM3genetic
27708008
GET3_YEASTGET3genetic
27708008
RM01_YEASTMRPL1genetic
27708008
TRM1_YEASTTRM1genetic
27708008
ARO1_YEASTARO1genetic
27708008
UME6_YEASTUME6genetic
27708008
H2A1_YEASTHTA1genetic
27708008
MNN10_YEASTMNN10genetic
27708008
ODPA_YEASTPDA1genetic
27708008
MSH4_YEASTMSH4genetic
27708008
SA155_YEASTSAP155genetic
27708008
SGF73_YEASTSGF73genetic
27708008
GCN1_YEASTGCN1genetic
27708008
YGY5_YEASTYGL235Wgenetic
27708008
MTO1_YEASTMTO1genetic
27708008
ACBP_YEASTACB1genetic
27708008
ENV11_YEASTENV11genetic
27708008
UPF3_YEASTUPF3genetic
27708008
PFD3_YEASTPAC10genetic
27708008
PHB2_YEASTPHB2genetic
27708008
NPR3_YEASTNPR3genetic
27708008
NMD2_YEASTNMD2genetic
27708008
YIA6_YEASTYIA6genetic
27708008
PTK2_YEASTPTK2genetic
27708008
MPCP_YEASTMIR1genetic
27708008
YKC3_YEASTYKL023Wgenetic
27708008
RM49_YEASTMRP49genetic
27708008
SAC1_YEASTSAC1genetic
27708008
DBP7_YEASTDBP7genetic
27708008
IMH1_YEASTIMH1genetic
27708008
VID22_YEASTVID22genetic
27708008
ATP10_YEASTATP10genetic
27708008
SST2_YEASTSST2genetic
27708008
NU188_YEASTNUP188genetic
27708008
MAC1_YEASTMAC1genetic
27708008
MUB1_YEASTMUB1genetic
27708008
CIN4_YEASTCIN4genetic
27708008
HSC82_YEASTHSC82genetic
27708008
SKY1_YEASTSKY1genetic
27708008
UBP8_YEASTUBP8genetic
27708008
ZRC1_YEASTZRC1genetic
27708008
SCS7_YEASTSCS7genetic
27708008
MAS5_YEASTYDJ1genetic
27708008
ODP2_YEASTLAT1genetic
27708008
EOS1_YEASTEOS1genetic
27708008
LSM7_YEASTLSM7genetic
27708008
ATP23_YEASTATP23genetic
27708008
PT494_YEASTPET494genetic
27708008
BRE5_YEASTBRE5genetic
27708008
SIN3_YEASTSIN3genetic
27708008
IRA2_YEASTIRA2genetic
27708008
ZEO1_YEASTZEO1genetic
27708008
TRM11_YEASTTRM11genetic
27708008
TYW4_YEASTPPM2genetic
27708008
STI1_YEASTSTI1genetic
27708008
LIS1_YEASTPAC1genetic
27708008
MBF1_YEASTMBF1genetic
27708008
MSC6_YEASTMSC6genetic
27708008
PMA2_YEASTPMA2genetic
27708008
NIP80_YEASTNIP100genetic
27708008
WDR6_YEASTRTT10genetic
27708008
NAA30_YEASTMAK3genetic
27708008
CHMU_YEASTARO7genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SYFB_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-124 AND SER-375, ANDMASS 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 THR-437, AND MASSSPECTROMETRY.

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