AHA1_YEAST - dbPTM
AHA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AHA1_YEAST
UniProt AC Q12449
Protein Name Hsp90 co-chaperone AHA1
Gene Name AHA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 350
Subcellular Localization Cytoplasm .
Protein Description Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic 'Arg-380' with ATP in the N-terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting..
Protein Sequence MVVNNPNNWHWVDKNCIGWAKEYFKQKLVGVEAGSVKDKKYAKIKSVSSIEGDCEVNQRKGKVISLFDLKITVLIEGHVDSKDGSALPFEGSINVPEVAFDSEASSYQFDISIFKETSELSEAKPLIRSELLPKLRQIFQQFGKDLLATHGNDIQVPESQVKSNYTRGNQKSSFTEIKDSASKPKKNALPSSTSTSAPVSSTNKVPQNGSGNSTSIYLEPTFNVPSSELYETFLDKQRILAWTRSAQFFNSGPKLETKEKFELFGGNVISELVSCEKDKKLVFHWKLKDWSAPFNSTIEMTFHESQEFHETKLQVKWTGIPVGEEDRVRANFEEYYVRSIKLTFGFGAVL
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
21AcetylationKNCIGWAKEYFKQKL
CCHHHHHHHHHHHHH		46.5724489116
35PhosphorylationLVGVEAGSVKDKKYA
HCCCCCCCCCCCCCE		32.8028889911
37AcetylationGVEAGSVKDKKYAKI
CCCCCCCCCCCCEEE		66.5825381059
49PhosphorylationAKIKSVSSIEGDCEV
EEEEECEEEECCCEE		23.6228889911
124AcetylationTSELSEAKPLIRSEL
CCCHHHCHHHHHHHH		35.9824489116
134AcetylationIRSELLPKLRQIFQQ
HHHHHHHHHHHHHHH		57.1624489116
144AcetylationQIFQQFGKDLLATHG
HHHHHHCHHHHHHCC		46.6324489116
159PhosphorylationNDIQVPESQVKSNYT
CCCCCCHHHHCCCCC		33.9223749301
162AcetylationQVPESQVKSNYTRGN
CCCHHHHCCCCCCCC		25.9125381059
172PhosphorylationYTRGNQKSSFTEIKD
CCCCCCCCCCEECHH		22.4122369663
173PhosphorylationTRGNQKSSFTEIKDS
CCCCCCCCCEECHHC		43.1322369663
175PhosphorylationGNQKSSFTEIKDSAS
CCCCCCCEECHHCCC		38.4519779198
180PhosphorylationSFTEIKDSASKPKKN
CCEECHHCCCCCCCC		29.4621551504
182PhosphorylationTEIKDSASKPKKNAL
EECHHCCCCCCCCCC		54.1419779198
186UbiquitinationDSASKPKKNALPSST
HCCCCCCCCCCCCCC		56.8523749301
191PhosphorylationPKKNALPSSTSTSAP
CCCCCCCCCCCCCCC		47.2828889911
194PhosphorylationNALPSSTSTSAPVSS
CCCCCCCCCCCCCCC		23.4719779198
195PhosphorylationALPSSTSTSAPVSST
CCCCCCCCCCCCCCC		29.0630377154
196PhosphorylationLPSSTSTSAPVSSTN
CCCCCCCCCCCCCCC		30.2823749301
200PhosphorylationTSTSAPVSSTNKVPQ
CCCCCCCCCCCCCCC		30.3121551504
201PhosphorylationSTSAPVSSTNKVPQN
CCCCCCCCCCCCCCC		35.9121551504
251PhosphorylationRSAQFFNSGPKLETK
HHHHHHHCCCCCCCH		51.8523749301
254AcetylationQFFNSGPKLETKEKF
HHHHCCCCCCCHHHE		63.5824489116
254UbiquitinationQFFNSGPKLETKEKF
HHHHCCCCCCCHHHE		63.5823749301
316AcetylationHETKLQVKWTGIPVG
ECCEEEEEECCCCCC		26.5224489116
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 AHA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AHA1_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 AHA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAD2_YEASTMAD2physical
10688190
HSP82_YEASTHSP82physical
12604615
HCH1_YEASTHCH1physical
14739935
HSP82_YEASTHSP82physical
15466438
HCH1_YEASTHCH1genetic
12604615
HSC82_YEASTHSC82physical
16554755
GCN1_YEASTGCN1physical
16429126
GFA1_YEASTGFA1physical
16429126
LYS12_YEASTLYS12physical
16429126
RPA2_YEASTRPA135physical
16429126
HSP82_YEASTHSP82physical
16429126
IMB4_YEASTKAP123physical
16429126
TBA1_YEASTTUB1physical
16429126
ARO1_YEASTARO1physical
16429126
HSC82_YEASTHSC82physical
16429126
RPN1_YEASTRPN1physical
16429126
TBB_YEASTTUB2physical
16429126
PFKA1_YEASTPFK1physical
16429126
TCPD_YEASTCCT4physical
16429126
ECM29_YEASTECM29physical
16429126
HSP82_YEASTHSP82physical
15633294
HCH1_YEASTHCH1physical
12604615
HSP82_YEASTHSP82physical
12667448
HSC82_YEASTHSC82physical
18719252
HSP82_YEASTHSP82physical
18719252
HSP71_YEASTSSA1physical
19536198
SSB1_YEASTSSB1physical
19536198
SIF2_YEASTSIF2genetic
20093466
SWD3_YEASTSWD3genetic
20093466
SWC5_YEASTSWC5genetic
20093466
HOSC_YEASTLYS20genetic
20093466
CRD1_YEASTCRD1genetic
20093466
CYK3_YEASTCYK3genetic
20093466
YD114_YEASTYDL114Wgenetic
20093466
PEX19_YEASTPEX19genetic
20093466
SLX5_YEASTSLX5genetic
20093466
BCS1_YEASTBCS1genetic
20093466
SPT3_YEASTSPT3genetic
20093466
EMI2_YEASTEMI2genetic
20093466
SLX8_YEASTSLX8genetic
20093466
SPT2_YEASTSPT2genetic
20093466
GTS1_YEASTGTS1genetic
20093466
PNC1_YEASTPNC1genetic
20093466
CGR1_YEASTCGR1genetic
20093466
ACBP_YEASTACB1genetic
20093466
HSV2_YEASTHSV2genetic
20093466
SPO13_YEASTSPO13genetic
20093466
YHI9_YEASTYHI9genetic
20093466
YHJ5_YEASTNEL1genetic
20093466
WSS1_YEASTWSS1genetic
20093466
YIQ5_YEASTYIL165Cgenetic
20093466
APQ12_YEASTAPQ12genetic
20093466
SAC1_YEASTSAC1genetic
20093466
RSF1_YEASTRSF1genetic
20093466
COQ7_YEASTCAT5genetic
20093466
PUR6_YEASTADE2genetic
20093466
NEW1_YEASTNEW1genetic
20093466
YME1_YEASTYME1genetic
20093466
HCH1_YEASTHCH1genetic
12504007
HSC82_YEASTHSC82physical
20159554
AHA1_YEASTAHA1physical
24614167
HSP82_YEASTHSP82physical
24614167
HSC82_YEASTHSC82physical
24614167
HSP82_YEASTHSP82physical
24462205
HSP82_YEASTHSP82physical
23396352
SLX5_YEASTSLX5genetic
27708008
SIF2_YEASTSIF2genetic
27708008
SHE3_YEASTSHE3genetic
27708008
ODPB_YEASTPDB1genetic
27708008
SWC5_YEASTSWC5genetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
MTU1_YEASTSLM3genetic
27708008
PEX19_YEASTPEX19genetic
27708008
CYK3_YEASTCYK3genetic
27708008
CRD1_YEASTCRD1genetic
27708008
BCS1_YEASTBCS1genetic
27708008
EMI2_YEASTEMI2genetic
27708008
SPT2_YEASTSPT2genetic
27708008
ODPA_YEASTPDA1genetic
27708008
CGR1_YEASTCGR1genetic
27708008
PNC1_YEASTPNC1genetic
27708008
MED5_YEASTNUT1genetic
27708008
ACBP_YEASTACB1genetic
27708008
ASK10_YEASTASK10genetic
27708008
UBCX_YEASTPEX4genetic
27708008
SPO11_YEASTSPO11genetic
27708008
YHI9_YEASTYHI9genetic
27708008
YHJ5_YEASTNEL1genetic
27708008
WSS1_YEASTWSS1genetic
27708008
YIQ5_YEASTYIL165Cgenetic
27708008
MOG1_YEASTMOG1genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
MCR1_YEASTMCR1genetic
27708008
RSF1_YEASTRSF1genetic
27708008
ASI3_YEASTASI3genetic
27708008
IDH1_YEASTIDH1genetic
27708008
IRA2_YEASTIRA2genetic
27708008
FABD_YEASTMCT1genetic
27708008
BEM4_YEASTBEM4genetic
27708008
NEW1_YEASTNEW1genetic
27708008
YME1_YEASTYME1genetic
27708008
KAR3_YEASTKAR3genetic
27708008
PMP1_YEASTPMP1physical
26404137
HSP82_YEASTHSP82physical
28851842
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AHA1_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-35; SER-49; SER-159 ANDSER-173, 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-172, AND MASSSPECTROMETRY.

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