ERB1_YEAST - dbPTM
ERB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ERB1_YEAST
UniProt AC Q04660
Protein Name Ribosome biogenesis protein ERB1 {ECO:0000255|HAMAP-Rule:MF_03027}
Gene Name ERB1 {ECO:0000255|HAMAP-Rule:MF_03027, ECO:0000303|PubMed:11522832}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 807
Subcellular Localization Nucleus, nucleolus . Nucleus, nucleoplasm .
Protein Description Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome..
Protein Sequence MMAKNNKTTEAKMSKKRAASEESDVEEDEDKLLSVDGLIDAEASESDEDDDEYESAVEEKESSSDKEAQDDSDDDSDAELNKLLAEEEGDGEEDYDSSEFSDDTTSLTDRLSGVKLQTIVDPNIYSKYADGSDRIIKPEINPVYDSDDSDAETQNTIGNIPLSAYDEMPHIGYDINGKRIMRPAKGSALDQLLDSIELPEGWTGLLDKNSGSSLNLTKEELELISKIQRNEQTDDSINPYEPLIDWFTRHEEVMPLTAVPEPKRRFVPSKNEAKRVMKIVRAIREGRIIPPKKLKEMKEKEKIENYQYDLWGDSTETNDHVMHLRAPKLPPPTNEESYNPPEEYLLSPEEKEAWENTEYSERERNFIPQKYSALRKVPGYGESIRERFERSLDLYLAPRVRKNKLNIDPNSLIPELPSPKDLRPFPIRCSTIYAGHKGKVRTLSIDPSGLWLATGSDDGTVRVWEILTGREVYRTTLIDDEENPDYHIECIEWNPDANNGILAVAVGENIHLIVPPIFGYDIENNGKTKIEDGFGYDTFGTVKKSNLEVNENGDGDEDGENESAKNAVKKQVAQWNKPSQKQLEKDICITISCKKTVKKLSWHRKGDYFVTVQPDSGNTSVLIHQVSKHLTQSPFKKSKGIIMDAKFHPFKPQLFVCSQRYVRIYDLSQQILVKKLLPGARWLSKIDIHPRGDNLIASSFDKRVLWHDLDLASTPYKTLRYHEKAVRSVNFHKKLPLFSSAADDGTIHVFHATVYDDMMKNPMIVPLKKLTGHKVINSLGVLDAIWHPREAWLFSAGADNTARLWTT
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
8PhosphorylationMMAKNNKTTEAKMSK
CCCCCCCCHHHHHHH		31.8019823750
9PhosphorylationMAKNNKTTEAKMSKK
CCCCCCCHHHHHHHH		35.2419823750
20PhosphorylationMSKKRAASEESDVEE
HHHHHHHCCCCCCCC		40.6925521595
23PhosphorylationKRAASEESDVEEDED
HHHHCCCCCCCCCHH		42.7925521595
64PhosphorylationVEEKESSSDKEAQDD
HHHHHCCCCHHHCCC		63.0821551504
72PhosphorylationDKEAQDDSDDDSDAE
CHHHCCCCCCCCHHH		51.7522890988
76PhosphorylationQDDSDDDSDAELNKL
CCCCCCCCHHHHHHH		45.7922890988
95PhosphorylationEGDGEEDYDSSEFSD
HCCCCCCCCCCCCCC		22.4720377248
97PhosphorylationDGEEDYDSSEFSDDT
CCCCCCCCCCCCCCC		26.0720377248
98PhosphorylationGEEDYDSSEFSDDTT
CCCCCCCCCCCCCCC		39.5020377248
101PhosphorylationDYDSSEFSDDTTSLT
CCCCCCCCCCCCCHH		30.4420377248
104PhosphorylationSSEFSDDTTSLTDRL
CCCCCCCCCCHHHHH		24.2319795423
105PhosphorylationSEFSDDTTSLTDRLS
CCCCCCCCCHHHHHC		28.8220377248
106PhosphorylationEFSDDTTSLTDRLSG
CCCCCCCCHHHHHCC		31.2221551504
108PhosphorylationSDDTTSLTDRLSGVK
CCCCCCHHHHHCCCE		20.8819795423
112PhosphorylationTSLTDRLSGVKLQTI
CCHHHHHCCCEEEEE		42.2920377248
127AcetylationVDPNIYSKYADGSDR
ECCCHHHHCCCCCCC		27.7324489116
127UbiquitinationVDPNIYSKYADGSDR
ECCCHHHHCCCCCCC		27.7323749301
128PhosphorylationDPNIYSKYADGSDRI
CCCHHHHCCCCCCCC		12.1819823750
132PhosphorylationYSKYADGSDRIIKPE
HHHCCCCCCCCCCCC		25.0219823750
144PhosphorylationKPEINPVYDSDDSDA
CCCCCCCCCCCCCCC		15.8128889911
146PhosphorylationEINPVYDSDDSDAET
CCCCCCCCCCCCCCC		26.1524909858
149PhosphorylationPVYDSDDSDAETQNT
CCCCCCCCCCCCCCC		43.6524909858
153PhosphorylationSDDSDAETQNTIGNI
CCCCCCCCCCCCCCC		28.9219823750
156PhosphorylationSDAETQNTIGNIPLS
CCCCCCCCCCCCCCH		22.0519823750
163PhosphorylationTIGNIPLSAYDEMPH
CCCCCCCHHHCCCCC		21.3019823750
165PhosphorylationGNIPLSAYDEMPHIG
CCCCCHHHCCCCCCC		14.7319823750
173PhosphorylationDEMPHIGYDINGKRI
CCCCCCCEECCCCEE		17.0419795423
208UbiquitinationGWTGLLDKNSGSSLN
CCCCEECCCCCCCCC		53.6417644757
210PhosphorylationTGLLDKNSGSSLNLT
CCEECCCCCCCCCCC		45.8828889911
212PhosphorylationLLDKNSGSSLNLTKE
EECCCCCCCCCCCHH		31.3222369663
213PhosphorylationLDKNSGSSLNLTKEE
ECCCCCCCCCCCHHH		25.4621440633
218UbiquitinationGSSLNLTKEELELIS
CCCCCCCHHHHHHHH		52.9717644757
218AcetylationGSSLNLTKEELELIS
CCCCCCCHHHHHHHH		52.9724489116
226UbiquitinationEELELISKIQRNEQT
HHHHHHHHHHHCCCC		35.5517644757
347PhosphorylationPPEEYLLSPEEKEAW
CCHHHCCCHHHHHHH		27.8928152593
370AcetylationERNFIPQKYSALRKV
HHCCCCHHHHHHHCC		35.5024489116
402UbiquitinationYLAPRVRKNKLNIDP
HCCHHHHCCCCCCCC		56.4217644757
404UbiquitinationAPRVRKNKLNIDPNS
CHHHHCCCCCCCCCC		46.0417644757
411PhosphorylationKLNIDPNSLIPELPS
CCCCCCCCCCCCCCC		32.8221126336
418PhosphorylationSLIPELPSPKDLRPF
CCCCCCCCCCCCCCC		58.1517330950
420UbiquitinationIPELPSPKDLRPFPI
CCCCCCCCCCCCCCE		73.9717644757
442PhosphorylationGHKGKVRTLSIDPSG
CCCCEEEEEEECCCC		28.0422890988
444PhosphorylationKGKVRTLSIDPSGLW
CCEEEEEEECCCCCE		25.0822890988
448PhosphorylationRTLSIDPSGLWLATG
EEEEECCCCCEEEEC		42.6522890988
454PhosphorylationPSGLWLATGSDDGTV
CCCCEEEECCCCCCE		34.7422890988
456PhosphorylationGLWLATGSDDGTVRV
CCEEEECCCCCCEEE		28.3322890988
460PhosphorylationATGSDDGTVRVWEIL
EECCCCCCEEEEEEC		16.4822890988
544UbiquitinationDTFGTVKKSNLEVNE
CCCCEEEECCEEECC		39.9923749301
545PhosphorylationTFGTVKKSNLEVNEN
CCCEEEECCEEECCC		40.7130377154
563PhosphorylationDEDGENESAKNAVKK
CCCCCCHHHHHHHHH		57.0023749301
577MethylationKQVAQWNKPSQKQLE
HHHHHCCCCCHHHHH		42.9920137074
581MethylationQWNKPSQKQLEKDIC
HCCCCCHHHHHCCEE		62.2820137074
702AcetylationLIASSFDKRVLWHDL
EEEECCCHHHHHHHC		42.2524489116
713PhosphorylationWHDLDLASTPYKTLR
HHHCCCCCCCCHHHH		36.8924961812
714PhosphorylationHDLDLASTPYKTLRY
HHCCCCCCCCHHHHH		25.6524961812
717AcetylationDLASTPYKTLRYHEK
CCCCCCCHHHHHHHH		42.1424489116
771PhosphorylationIVPLKKLTGHKVINS
EEEHHHHCCCHHHCH		46.2328889911
774UbiquitinationLKKLTGHKVINSLGV
HHHHCCCHHHCHHCH		46.2717644757
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 ERB1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ERB1_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 ERB1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PESC_YEASTNOP7physical
14759368
YTM1_YEASTYTM1physical
14759368
ERB1_YEASTERB1physical
14759368
BRX1_YEASTBRX1physical
11805826
HAS1_YEASTHAS1physical
11805826
NOP2_YEASTNOP2physical
11805826
EIF3B_YEASTPRT1physical
11805826
RLP7_YEASTRLP7physical
11805826
NSA1_YEASTNSA1physical
11805826
PESC_YEASTNOP7physical
11805826
NOP15_YEASTNOP15physical
11805826
NOC2_YEASTNOC2physical
11805826
BRX1_YEASTBRX1physical
11805837
NOP16_YEASTNOP16physical
11805837
NOP2_YEASTNOP2physical
11805837
IF6_YEASTTIF6physical
11805837
PIB2_YEASTPIB2physical
11805837
FKBP4_YEASTFPR4physical
11805837
SCS2_YEASTSCS2physical
11805837
PESC_YEASTNOP7physical
11805837
EBP2_YEASTEBP2physical
11805837
NOG1_YEASTNOG1physical
11805837
THI21_YEASTTHI21physical
11805837
NOC3_YEASTNOC3physical
11805837
EXG1_YEASTEXG1physical
11805837
RLP7_YEASTRLP7physical
11805837
NOP15_YEASTNOP15physical
11805837
RRP17_YEASTRRP17physical
11805837
CIC1_YEASTCIC1physical
11805837
MRT4_YEASTMRT4physical
11805837
YTM1_YEASTYTM1physical
11805837
CDC14_YEASTCDC14physical
11805837
NSA1_YEASTNSA1physical
11805837
NOC2_YEASTNOC2physical
11805837
SYEC_YEASTGUS1physical
11805837
NACA_YEASTEGD2physical
11805837
HXT7_YEASTHXT7physical
11805837
TCPZ_YEASTCCT6physical
11805837
SPB4_YEASTSPB4physical
11805837
6PGD1_YEASTGND1physical
11805837
UBR2_YEASTUBR2physical
11805837
NUG1_YEASTNUG1physical
11805837
PRP43_YEASTPRP43physical
11805837
HSP7Q_YEASTSSQ1physical
11805837
ACON_YEASTACO1physical
11805837
HAS1_YEASTHAS1physical
11805837
METE_YEASTMET6physical
11805837
MUB1_YEASTMUB1physical
11805837
SAHH_YEASTSAH1physical
11805837
PMM_YEASTSEC53physical
11805837
UBP1_YEASTUBP1physical
16554755
DRS1_YEASTDRS1physical
16554755
YTM1_YEASTYTM1physical
16554755
FBRL_YEASTNOP1physical
16554755
SPT16_YEASTSPT16physical
16554755
RL4A_YEASTRPL4Aphysical
16429126
NOC2_YEASTNOC2physical
16429126
NOP15_YEASTNOP15physical
16429126
NOP2_YEASTNOP2physical
16429126
PESC_YEASTNOP7physical
16429126
RLP7_YEASTRLP7physical
16429126
RL3_YEASTRPL3physical
16429126
BRX1_YEASTBRX1physical
16429126
HAS1_YEASTHAS1physical
16429126
NSA1_YEASTNSA1physical
16429126
RRP5_YEASTRRP5physical
16429126
PESC_YEASTNOP7physical
15467761
PESC_YEASTNOP7physical
16287855
YTM1_YEASTYTM1physical
16287855
YTM1_YEASTYTM1physical
18448671
PESC_YEASTNOP7physical
18448671
SSB1_YEASTSSB1physical
19536198
YTM1_YEASTYTM1physical
25877921
DRS1_YEASTDRS1physical
25877921
URB1_YEASTURB1physical
25877921
NOG2_YEASTNOG2physical
25877921
PAT1_YEASTPAT1genetic
27708008
ARO1_YEASTARO1genetic
27708008
SWI5_YEASTSWI5genetic
27708008
SDS3_YEASTSDS3genetic
27708008
LSM1_YEASTLSM1genetic
27708008
XPOT_YEASTLOS1genetic
27708008
MAK5_YEASTMAK5genetic
27708008
DBF4_YEASTDBF4genetic
27708008
UBC3_YEASTCDC34genetic
27708008
CDC1_YEASTCDC1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
ACT_YEASTACT1genetic
27708008
PESC_YEASTNOP7genetic
27708008
RPF1_YEASTRPF1genetic
27708008
MET30_YEASTMET30genetic
27708008
ESS1_YEASTESS1genetic
27708008
MAK11_YEASTMAK11genetic
27708008
NOC3_YEASTNOC3genetic
27708008
NEP1_YEASTEMG1genetic
27708008
SEN1_YEASTSEN1genetic
27708008
HAS1_YEASTHAS1genetic
27708008
LIP1_YEASTLIP1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
HRP1_YEASTHRP1genetic
27708008
YTM1_YEASTYTM1genetic
27708008
NIP7_YEASTNIP7genetic
27708008
ATC3_YEASTDRS2genetic
27708008
BUD14_YEASTBUD14genetic
27708008
RL19A_YEASTRPL19Bgenetic
27708008
RL19B_YEASTRPL19Bgenetic
27708008
ETR1_YEASTETR1genetic
27708008
RFS1_YEASTRFS1genetic
27708008
PFF1_YEASTPFF1genetic
27708008
PYC2_YEASTPYC2genetic
27708008
NTM1_YEASTTAE1genetic
27708008
CHK1_YEASTCHK1genetic
27708008
FUB1_YEASTFUB1genetic
27708008
YCY9_YEASTYCR099Cgenetic
27708008
GPR1_YEASTGPR1genetic
27708008
VPS41_YEASTVPS41genetic
27708008
BMH2_YEASTBMH2genetic
27708008
SWM1_YEASTSWM1genetic
27708008
MSN5_YEASTMSN5genetic
27708008
PSP1_YEASTPSP1genetic
27708008
SPS2_YEASTSPS2genetic
27708008
BMH1_YEASTBMH1genetic
27708008
KCC1_YEASTCMK1genetic
27708008
RL26B_YEASTRPL26Bgenetic
27708008
PEF1_YEASTPEF1genetic
27708008
LRP1_YEASTLRP1genetic
27708008
KEL1_YEASTKEL1genetic
27708008
CRG1_YEASTCRG1genetic
27708008
AIR1_YEASTAIR1genetic
27708008
YIJ2_YEASTYIL092Wgenetic
27708008
VPS53_YEASTVPS53genetic
27708008
MNN11_YEASTMNN11genetic
27708008
YJ24_YEASTKCH1genetic
27708008
DBR1_YEASTDBR1genetic
27708008
YRA2_YEASTYRA2genetic
27708008
NU133_YEASTNUP133genetic
27708008
LOT6_YEASTLOT6genetic
27708008
CYSD_YEASTMET17genetic
27708008
RAD10_YEASTRAD10genetic
27708008
INO4_YEASTINO4genetic
27708008
RRP6_YEASTRRP6genetic
27708008
DIA2_YEASTDIA2genetic
27708008
HSP7F_YEASTSSE1genetic
27708008
YTM1_YEASTYTM1physical
28115637
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ERB1_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-23; SER-146; SER-149 ANDSER-418, 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-418, AND MASSSPECTROMETRY.
"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-20; SER-23; SER-72 ANDSER-76, AND MASS 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-23 AND SER-418, AND MASSSPECTROMETRY.

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