HRB1_YEAST - dbPTM
HRB1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HRB1_YEAST
UniProt AC P38922
Protein Name Protein HRB1
Gene Name HRB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 454
Subcellular Localization Nucleus .
Protein Description
Protein Sequence MSDQERGSENNNRSRSRSRSPVRRRMSDDHGYERDNHLSRRSGNYNGRRKFADTYRGSRDRGEYRGGRERSDYRERERFNNRDNPRSRDRYDDRRRGRDVTGRYGNRRDDYPRSFRSRHNTRDDSRRGGFGSSGARGDYGPLLARELDSTYEEKVNRNYSNSIFVGNLTYDSTPEDLTEFFSQIGKVVRADIITSRGHHRGMGTVEFTNSDDVDRAIRQYDGAFFMDRKIFVRQDNPPPSNNIKERKALDRGELRHNRKTHEVIVKNLPASVNWQALKDIFKECGNVAHADVELDGDGVSTGSGTVSFYDIKDLHRAIEKYNGYSIEGNVLDVKSKESVHNHSDGDDVDIPMDDSPVNEEARKFTENVVGGGERNRLIYCSNLPFSTAKSDLYDLFETIGKVNNAELRYDSKGAPTGIAVVEYDNVDDADVCIERLNNYNYGGCDLDISYAKRL
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
16PhosphorylationENNNRSRSRSRSPVR
CCCCCHHCCCCCCCH		35.5430377154
18PhosphorylationNNRSRSRSRSPVRRR
CCCHHCCCCCCCHHH		38.0519684113
20PhosphorylationRSRSRSRSPVRRRMS
CHHCCCCCCCHHHHH		29.0619684113
27PhosphorylationSPVRRRMSDDHGYER
CCCHHHHHCCCCCCC		37.77
32PhosphorylationRMSDDHGYERDNHLS
HHHCCCCCCCCCCCC		12.3628132839
50AcetylationGNYNGRRKFADTYRG
CCCCCCCCCCCCCCC		43.4725381059
149PhosphorylationLLARELDSTYEEKVN
HHHHHHCCCHHHHCC		45.5821440633
151PhosphorylationARELDSTYEEKVNRN
HHHHCCCHHHHCCCC		26.4921440633
195PhosphorylationVRADIITSRGHHRGM
HCEEEEECCCCCCCC		26.3427214570
240PhosphorylationRQDNPPPSNNIKERK
CCCCCCCCCCHHHHH		48.5625704821
335PhosphorylationGNVLDVKSKESVHNH
CCEEEECCCCCCCCC		41.3117330950
338PhosphorylationLDVKSKESVHNHSDG
EEECCCCCCCCCCCC		32.2022369663
343PhosphorylationKESVHNHSDGDDVDI
CCCCCCCCCCCCCCC		48.9122369663
355PhosphorylationVDIPMDDSPVNEEAR
CCCCCCCCCCCHHHH		26.8722369663
444GlutathionylationNNYNYGGCDLDISYA
HCCCCCCCCCCCHHH		4.0022833525
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 HRB1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HRB1_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 HRB1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HPR1_YEASTHPR1physical
14769921
SUB2_YEASTSUB2physical
14769921
GBP2_YEASTGBP2physical
14769921
TEX1_YEASTTEX1physical
14769921
THO2_YEASTTHO2physical
14769921
MFT1_YEASTMFT1physical
14769921
THP2_YEASTTHP2physical
14769921
YRA1_YEASTYRA1physical
14769921
GAL1_YEASTGAL1physical
14769921
PMA1_YEASTPMA1physical
14769921
IF5A1_YEASTHYP2physical
14769921
RS5_YEASTRPS5physical
14769921
DBP2_YEASTDBP2physical
14769921
ACT_YEASTACT1physical
14769921
CTK1_YEASTCTK1physical
14769921
THP2_YEASTTHP2physical
16554755
THO2_YEASTTHO2physical
16554755
TEX1_YEASTTEX1physical
16554755
H1_YEASTHHO1physical
16554755
HPR1_YEASTHPR1physical
16429126
THO2_YEASTTHO2physical
16429126
ATPB_YEASTATP2physical
16429126
RS4A_YEASTRPS4Aphysical
16429126
RS4B_YEASTRPS4Aphysical
16429126
RPN13_YEASTRPN13genetic
17314980
SUS1_YEASTSUS1genetic
17314980
FAB1_YEASTFAB1genetic
17314980
YPT6_YEASTYPT6genetic
17314980
SRP40_YEASTSRP40genetic
17314980
DOA1_YEASTDOA1genetic
17314980
POP8_YEASTPOP8genetic
19061648
SYNC_YEASTDED81genetic
19061648
YPT6_YEASTYPT6genetic
19061648
TAD3_YEASTTAD3genetic
19061648
RPB1_YEASTRPO21genetic
19061648
RLI1_YEASTRLI1genetic
19061648
HSP72_YEASTSSA2physical
19536198
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
CSN12_YEASTYJR084Wgenetic
27708008
INO4_YEASTINO4genetic
27708008
SWC3_YEASTSWC3genetic
27708008
CSG2_YEASTCSG2genetic
27708008
SWC5_YEASTSWC5genetic
27708008
GBP2_YEASTGBP2genetic
27708008
TMN2_YEASTTMN2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
SWR1_YEASTSWR1genetic
27708008
SDC1_YEASTSDC1genetic
27708008
HS150_YEASTHSP150genetic
27708008
DCOR_YEASTSPE1genetic
27708008
SAC1_YEASTSAC1genetic
27708008
BRE2_YEASTBRE2genetic
27708008
ARP6_YEASTARP6genetic
27708008
VPS71_YEASTVPS71genetic
27708008
KU80_YEASTYKU80genetic
27708008
PFKA2_YEASTPFK2genetic
27708008
RTC6_YEASTRTC6genetic
27708008
DSS4_YEASTDSS4genetic
27708008
MEX67_YEASTMEX67physical
27951587
MEX67_YEASTMEX67physical
24452287
PRP17_YEASTCDC40physical
24452287
RRP6_YEASTRRP6physical
24452287
PRP8_YEASTPRP8genetic
24452287
PRP17_YEASTCDC40genetic
24452287
PRP43_YEASTPRP43genetic
24452287
MLP1_YEASTMLP1genetic
24452287
RRP6_YEASTRRP6genetic
24452287
MTR4_YEASTMTR4genetic
24452287
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HRB1_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-338 AND SER-343, 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 SER-27, AND MASSSPECTROMETRY.
"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-343 AND SER-355, ANDMASS SPECTROMETRY.

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