OLA1_YEAST - dbPTM
OLA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID OLA1_YEAST
UniProt AC P38219
Protein Name Obg-like ATPase 1 {ECO:0000255|HAMAP-Rule:MF_03167}
Gene Name OLA1 {ECO:0000255|HAMAP-Rule:MF_03167}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 394
Subcellular Localization Cytoplasm .
Protein Description Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP..
Protein Sequence MPPKKQVEEKKVLLGRPGNNLKAGIVGLANVGKSTFFQAITRCPLGNPANYPFATIDPEEARVIVPSPRFDKLCEIYKKTASEVPAHLTVYDIAGLTKGASAGEGLGNAFLSHIRSVDSIYQVVRCFDDAEIIHVEGDVDPVRDLEIINQELRLKDIEFAQKALEGAEKIAKRGGQSLEVKQKKEEMDLITKIIKLLESGQRVANHSWTSKEVEIINSMFLLTAKPCIYLINLSERDYIRKKNKHLLRIKEWVDKYSPGDLIIPFSVSLEERLSHMSPEDAEEELKKLQTISALPKIITTMRQKLDLISFFTCGPDEVREWTIRRGTKAPQAAGVIHNDLMNTFILAQVMKCEDVFEYKDDSAIKAAGKLMQKGKDYVVEDGDIIYFRAGAGKN
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
22AcetylationGRPGNNLKAGIVGLA
CCCCCCCCEEEEEEC		46.8424489116
22UbiquitinationGRPGNNLKAGIVGLA
CCCCCCCCEEEEEEC		46.8423749301
33UbiquitinationVGLANVGKSTFFQAI
EEECCCCCCHHHHHH		41.8823749301
34PhosphorylationGLANVGKSTFFQAIT
EECCCCCCHHHHHHH		25.2321440633
35PhosphorylationLANVGKSTFFQAITR
ECCCCCCHHHHHHHC		31.7727214570
41PhosphorylationSTFFQAITRCPLGNP
CHHHHHHHCCCCCCC		29.2729688323
67PhosphorylationEARVIVPSPRFDKLC
HCEEEECCCCHHHHH		20.1521082442
72UbiquitinationVPSPRFDKLCEIYKK
ECCCCHHHHHHHHHH		52.9415699485
72AcetylationVPSPRFDKLCEIYKK
ECCCCHHHHHHHHHH		52.9424489116
78AcetylationDKLCEIYKKTASEVP
HHHHHHHHHCHHHCC		49.6724489116
78UbiquitinationDKLCEIYKKTASEVP
HHHHHHHHHCHHHCC		49.6722817900
79UbiquitinationKLCEIYKKTASEVPA
HHHHHHHHCHHHCCC		32.1423749301
89PhosphorylationSEVPAHLTVYDIAGL
HHCCCEEEEEEHHCC		13.7328889911
98UbiquitinationYDIAGLTKGASAGEG
EEHHCCCCCCCCCCC		58.4822106047
101PhosphorylationAGLTKGASAGEGLGN
HCCCCCCCCCCCCHH		45.5427214570
116PhosphorylationAFLSHIRSVDSIYQV
HHHHHHCCCCHHHHH		29.6724930733
119PhosphorylationSHIRSVDSIYQVVRC
HHHCCCCHHHHHHHC		22.5027214570
155AcetylationINQELRLKDIEFAQK
HCHHHHHHHHHHHHH		50.6724489116
155UbiquitinationINQELRLKDIEFAQK
HCHHHHHHHHHHHHH		50.6723749301
1552-HydroxyisobutyrylationINQELRLKDIEFAQK
HCHHHHHHHHHHHHH		50.67-
162SuccinylationKDIEFAQKALEGAEK
HHHHHHHHHHHHHHH		52.0523954790
162UbiquitinationKDIEFAQKALEGAEK
HHHHHHHHHHHHHHH		52.0524961812
162AcetylationKDIEFAQKALEGAEK
HHHHHHHHHHHHHHH		52.0524489116
169UbiquitinationKALEGAEKIAKRGGQ
HHHHHHHHHHHHCCC		47.6423749301
177PhosphorylationIAKRGGQSLEVKQKK
HHHHCCCCCCHHHHH		29.7623749301
192AcetylationEEMDLITKIIKLLES
HHHHHHHHHHHHHHH		35.1324489116
195UbiquitinationDLITKIIKLLESGQR
HHHHHHHHHHHHCCC		50.9523749301
195AcetylationDLITKIIKLLESGQR
HHHHHHHHHHHHCCC		50.9524489116
256PhosphorylationIKEWVDKYSPGDLII
HHHHHHHCCCCCEEE		18.6822369663
257PhosphorylationKEWVDKYSPGDLIIP
HHHHHHCCCCCEEEE		28.3122369663
266PhosphorylationGDLIIPFSVSLEERL
CCEEEEEEECHHHHH		12.8722369663
268PhosphorylationLIIPFSVSLEERLSH
EEEEEEECHHHHHHC		28.9422369663
286AcetylationEDAEEELKKLQTISA
HHHHHHHHHHHHHHH		55.5124489116
287AcetylationDAEEELKKLQTISAL
HHHHHHHHHHHHHHH		59.4524489116
290PhosphorylationEELKKLQTISALPKI
HHHHHHHHHHHHHHH		27.6019823750
292PhosphorylationLKKLQTISALPKIIT
HHHHHHHHHHHHHHH		27.4319823750
296AcetylationQTISALPKIITTMRQ
HHHHHHHHHHHHHHH		47.8124489116
296UbiquitinationQTISALPKIITTMRQ
HHHHHHHHHHHHHHH		47.8123749301
359AcetylationCEDVFEYKDDSAIKA
CHHHHCCCCHHHHHH		48.1124489116
362PhosphorylationVFEYKDDSAIKAAGK
HHCCCCHHHHHHHHH		41.8627717283
3732-HydroxyisobutyrylationAAGKLMQKGKDYVVE
HHHHHHHCCCCEEEE		54.70-
373AcetylationAAGKLMQKGKDYVVE
HHHHHHHCCCCEEEE		54.7024489116
375AcetylationGKLMQKGKDYVVEDG
HHHHHCCCCEEEECC		53.5824489116
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 OLA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of OLA1_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 OLA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
OLA1_YEASTOLA1physical
14759368
SWD3_YEASTSWD3physical
16429126
YGD9_YEASTYGL039Wphysical
16429126
CSN12_YEASTYJR084Wgenetic
27708008
YRA2_YEASTYRA2genetic
27708008
CDC7_YEASTCDC7genetic
27708008
DBF4_YEASTDBF4genetic
27708008
CDC37_YEASTCDC37genetic
27708008
CDC1_YEASTCDC1genetic
27708008
SNU56_YEASTSNU56genetic
27708008
RPN11_YEASTRPN11genetic
27708008
DPB11_YEASTDPB11genetic
27708008
PROF_YEASTPFY1genetic
27708008
RPN7_YEASTRPN7genetic
27708008
TPS2_YEASTTPS2genetic
27708008
APT2_YEASTAPT2genetic
27708008
TAPT1_YEASTEMP65genetic
27708008
GCN20_YEASTGCN20genetic
27708008
GCN1_YEASTGCN1genetic
27708008
YHK8_YEASTYHK8genetic
27708008
SIP4_YEASTSIP4genetic
27708008
RPA34_YEASTRPA34genetic
27708008
IME1_YEASTIME1genetic
27708008
MYO3_YEASTMYO3genetic
27708008
ALAM_YEASTALT1genetic
27708008
SHH4_YEASTSHH4genetic
27708008
SSO2_YEASTSSO2genetic
27708008
FAP1_YEASTFAP1genetic
27708008
YNE0_YEASTYNL040Wgenetic
27708008
PFD4_YEASTGIM3genetic
27708008
DCAM_YEASTSPE2genetic
27708008
MBF1_YEASTMBF1genetic
27708008
MRN1_YEASTMRN1genetic
27708008
YP089_YEASTYPR089Wgenetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of OLA1_YEAST

loading...

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-34; SER-67; THR-89 ANDSER-116, 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-67, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory