ATPA_YEAST - dbPTM
ATPA_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATPA_YEAST
UniProt AC P07251
Protein Name ATP synthase subunit alpha, mitochondrial
Gene Name ATP1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 545
Subcellular Localization Mitochondrion inner membrane . Peripheral membrane protein.
Protein Description Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits. Subunit alpha does not bear the catalytic high-affinity ATP-binding sites (By similarity)..
Protein Sequence MLARTAAIRSLSRTLINSTKAARPAAAALASTRRLASTKAQPTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSLLLRRPPGREAYPGDVFYLHSRLLERAAKLSEKEGSGSLTALPVIETQGGDVSAYIPTNVISITDGQIFLEAELFYKGIRPAINVGLSVSRVGSAAQVKALKQVAGSLKLFLAQYREVAAFAQFGSDLDASTKQTLVRGERLTQLLKQNQYSPLATEEQVPLIYAGVNGHLDGIELSRIGEFESSFLSYLKSNHNELLTEIREKGELSKELLASLKSATESFVATF
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
31PhosphorylationPAAAALASTRRLAST
HHHHHHHHHHHHHCC		24.2430377154
43PhosphorylationASTKAQPTEVSSILE
HCCCCCCCHHHHHHH		36.6221126336
46PhosphorylationKAQPTEVSSILEERI
CCCCCHHHHHHHHHH		12.8727214570
47PhosphorylationAQPTEVSSILEERIK
CCCCHHHHHHHHHHC		36.0528152593
57PhosphorylationEERIKGVSDEANLNE
HHHHCCCCCCCCCCC		38.1027214570
126SuccinylationVKEGELVKRTGNIVD
EECCCEEEECCCEEE		57.7923954790
155UbiquitinationLGNPIDGKGPIDAAG
CCCCCCCCCCCCCCC		58.7423749301
155SuccinylationLGNPIDGKGPIDAAG
CCCCCCCCCCCCCCC		58.7423954790
155AcetylationLGNPIDGKGPIDAAG
CCCCCCCCCCCCCCC		58.7424489116
169SuccinylationGRSRAQVKAPGILPR
CCCCCCCCCCCCCCC		36.4623954790
178PhosphorylationPGILPRRSVHEPVQT
CCCCCCCCCCCCHHH		29.1622369663
188AcetylationEPVQTGLKAVDALVP
CCHHHCHHHHHEEEE		47.9424489116
188UbiquitinationEPVQTGLKAVDALVP
CCHHHCHHHHHEEEE		47.9415699485
1882-HydroxyisobutyrylationEPVQTGLKAVDALVP
CCHHHCHHHHHEEEE		47.94-
224AcetylationLDTILNQKRWNNGSD
HHHHHHCCCCCCCCH		59.3024489116
224SuccinylationLDTILNQKRWNNGSD
HHHHHHCCCCCCCCH		59.3023954790
224UbiquitinationLDTILNQKRWNNGSD
HHHHHHCCCCCCCCH		59.3024961812
230PhosphorylationQKRWNNGSDESKKLY
CCCCCCCCHHHCEEE		40.0928889911
234AcetylationNNGSDESKKLYCVYV
CCCCHHHCEEEEEEE		44.7625381059
246UbiquitinationVYVAVGQKRSTVAQL
EEEEECCCHHHHHHH		42.2417644757
264UbiquitinationLEQHDAMKYSIIVAA
HHHHCCHHHEEEEEE		37.2517644757
310AcetylationIVYDDLSKQAVAYRQ
EEEECHHHHHHHHHH		49.9624489116
3482-HydroxyisobutyrylationRLLERAAKLSEKEGS
HHHHHHHHHCCCCCC		52.11-
413PhosphorylationLSVSRVGSAAQVKAL
CCCHHCCCHHHHHHH		19.9928889911
418AcetylationVGSAAQVKALKQVAG
CCCHHHHHHHHHHHH		35.6024489116
4182-HydroxyisobutyrylationVGSAAQVKALKQVAG
CCCHHHHHHHHHHHH		35.60-
418UbiquitinationVGSAAQVKALKQVAG
CCCHHHHHHHHHHHH		35.6023749301
428AcetylationKQVAGSLKLFLAQYR
HHHHHHHHHHHHHHH		38.6024489116
445PhosphorylationAAFAQFGSDLDASTK
HHHHCCCCCCCCCCC		35.9727214570
452AcetylationSDLDASTKQTLVRGE
CCCCCCCCHHHHHHH		38.5025381059
510UbiquitinationSSFLSYLKSNHNELL
HHHHHHHHHCHHHHH		40.7624961812
511PhosphorylationSFLSYLKSNHNELLT
HHHHHHHHCHHHHHH		40.5028889911
5232-HydroxyisobutyrylationLLTEIREKGELSKEL
HHHHHHHHCCCCHHH		48.08-
523AcetylationLLTEIREKGELSKEL
HHHHHHHHCCCCHHH		48.0825381059
528AcetylationREKGELSKELLASLK
HHHCCCCHHHHHHHH		66.0724489116
528UbiquitinationREKGELSKELLASLK
HHHCCCCHHHHHHHH		66.0724961812
528SuccinylationREKGELSKELLASLK
HHHCCCCHHHHHHHH		66.0723954790
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 ATPA_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATPA_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 ATPA_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATP6_YEASTATP6physical
14998992
ATP8_YEASTATP8physical
14998992
ATP9_YEASTOLI1physical
14998992
ATPJ_YEASTTIM11physical
9271204
ATP12_YEASTATP12physical
10747017
ATPB_YEASTATP2physical
10449236
RAS2_YEASTRAS2genetic
10744740
ATP6_YEASTATP6physical
7962074
ATP9_YEASTOLI1physical
7962074
ODO1_YEASTKGD1genetic
16941010
SUCB_YEASTLSC2genetic
16941010
DIC1_YEASTDIC1genetic
16941010
FUMH_YEASTFUM1genetic
16941010
SDH3_YEASTSDH3genetic
16941010
PRS6B_YEASTRPT3genetic
21439406
COX17_YEASTCOX17genetic
21908598
PPOX_YEASTHEM14genetic
21908598
HSP71_YEASTSSA1physical
22940862
ATPG_YEASTATP3physical
22940862
PDC1_YEASTPDC1physical
22940862
HSP72_YEASTSSA2physical
22940862
ATPB_YEASTATP2physical
22940862
ATP7_YEASTATP7physical
22940862
ATPA_YEASTATP1physical
22940862
ATPO_YEASTATP5physical
22940862
ATPF_YEASTATP4physical
22940862
DOT6_YEASTDOT6genetic
26192197
TOD6_YEASTTOD6genetic
26192197
DCP2_YEASTDCP2genetic
26192197
EDC3_YEASTEDC3genetic
26192197
PBP1_YEASTPBP1genetic
26192197
PSP2_YEASTPSP2genetic
26192197
IF4B_YEASTTIF3genetic
26192197
IF4F2_YEASTTIF4632genetic
26192197
RL40A_YEASTRPL40Bgenetic
26192197
RL40B_YEASTRPL40Bgenetic
26192197
RLA0_YEASTRPP0genetic
26192197
TRM9_YEASTTRM9genetic
26192197
TRM11_YEASTTRM11genetic
26192197
MMS2_YEASTMMS2genetic
26192197
POC4_YEASTPOC4genetic
26192197
SSB1_YEASTSSB1genetic
26192197
SSB2_YEASTSSB2genetic
26192197
ZUO1_YEASTZUO1genetic
26192197
UBP3_YEASTUBP3genetic
26192197
YMW4_YEASTYMR074Cgenetic
26192197
YO098_YEASTYOL098Cgenetic
26192197
GIS2_YEASTGIS2genetic
26192197
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATPA_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Profiling phosphoproteins of yeast mitochondria reveals a role ofphosphorylation in assembly of the ATP synthase.";
Reinders J., Wagner K., Zahedi R.P., Stojanovski D., Eyrich B.,van der Laan M., Rehling P., Sickmann A., Pfanner N., Meisinger C.;
Mol. Cell. Proteomics 6:1896-1906(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57 AND SER-178, AND MASSSPECTROMETRY.

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