ATPF_YEAST - dbPTM
ATPF_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATPF_YEAST
UniProt AC P05626
Protein Name ATP synthase subunit 4, mitochondrial
Gene Name ATP4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 244
Subcellular Localization Mitochondrion. Mitochondrion inner membrane.
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. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements..
Protein Sequence MSMSMGVRGLALRSVSKTLFSQGVRCPSMVIGARYMSSTPEKQTDPKAKANSIINAIPGNNILTKTGVLGTSAAAVIYAISNELYVINDESILLLTFLGFTGLVAKYLAPAYKDFADARMKKVSDVLNASRNKHVEAVKDRIDSVSQLQNVAETTKVLFDVSKETVELESEAFELKQKVELAHEAKAVLDSWVRYEASLRQLEQRQLAKSVISRVQSELGNPKFQEKVLQQSISEIEQLLSKLK
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
18PhosphorylationALRSVSKTLFSQGVR
HHHHHHHHHHHCCCC		26.0619779198
28PhosphorylationSQGVRCPSMVIGARY
HCCCCCCHHHCCHHH		29.3419779198
113SuccinylationKYLAPAYKDFADARM
HHHHHHHHHHHHHHH		48.7723954790
113AcetylationKYLAPAYKDFADARM
HHHHHHHHHHHHHHH		48.7724489116
1222-HydroxyisobutyrylationFADARMKKVSDVLNA
HHHHHHHHHHHHHHH		37.31-
124PhosphorylationDARMKKVSDVLNASR
HHHHHHHHHHHHHHC		30.7728889911
139AcetylationNKHVEAVKDRIDSVS
CHHHHHHHHHHCHHH		48.6224489116
144PhosphorylationAVKDRIDSVSQLQNV
HHHHHHCHHHHHHHH		22.6928889911
146PhosphorylationKDRIDSVSQLQNVAE
HHHHCHHHHHHHHHH		29.1724961812
176AcetylationESEAFELKQKVELAH
CHHHHHHHHHHHHHH		40.6624489116
209SuccinylationLEQRQLAKSVISRVQ
HHHHHHHHHHHHHHH		54.5723954790
217PhosphorylationSVISRVQSELGNPKF
HHHHHHHHHHCCHHH		31.7529734811
223AcetylationQSELGNPKFQEKVLQ
HHHHCCHHHHHHHHH		64.7724489116
223UbiquitinationQSELGNPKFQEKVLQ
HHHHCCHHHHHHHHH		64.7723749301
227UbiquitinationGNPKFQEKVLQQSIS
CCHHHHHHHHHHHHH		37.1523749301
232PhosphorylationQEKVLQQSISEIEQL
HHHHHHHHHHHHHHH		18.3430377154
234PhosphorylationKVLQQSISEIEQLLS
HHHHHHHHHHHHHHH		37.4630377154
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 ATPF_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATPF_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 ATPF_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATP6_YEASTATP6physical
14998992
ATP8_YEASTATP8physical
14998992
ATP9_YEASTOLI1physical
14998992
ATP6_YEASTATP6physical
9425084
ATP6_YEASTATP6physical
9893937
ATPK_YEASTATP17physical
9425084
ATPK_YEASTATP17physical
9893937
ATPO_YEASTATP5physical
9893937
ATPA_YEASTATP1physical
9867807
ATPB_YEASTATP2physical
9867807
ATPJ_YEASTTIM11physical
9867807
ATP14_YEASTATP14physical
9867807
ATP5E_YEASTATP15physical
9867807
ATPD_YEASTATP16physical
9867807
ATPK_YEASTATP17physical
9867807
ATP18_YEASTATP18physical
9867807
ATPN_YEASTATP20physical
9867807
ATPG_YEASTATP3physical
9867807
ATPO_YEASTATP5physical
9867807
ATP7_YEASTATP7physical
9867807
ATP8_YEASTATP8physical
9867807
ATP9_YEASTOLI1physical
9867807
ATIF_YEASTINH1physical
9867807
SHO1_YEASTSHO1genetic
20093466
PHB2_YEASTPHB2genetic
20093466
COX7_YEASTCOX7genetic
20093466
INO4_YEASTINO4genetic
20093466
MDL2_YEASTMDL2genetic
20093466
ATP6_YEASTATP6physical
21266956
ATP8_YEASTATP8physical
21266956
ATP9_YEASTOLI1physical
21266956
ATPF_YEASTATP4physical
11823415
DPOA2_YEASTPOL12genetic
27708008
CDC27_YEASTCDC27genetic
27708008
SCC1_YEASTMCD1genetic
27708008
ACT_YEASTACT1genetic
27708008
MTR4_YEASTMTR4genetic
27708008
HACD_YEASTPHS1genetic
27708008
ORC1_YEASTORC1genetic
27708008
CBF3B_YEASTCEP3genetic
27708008
LIP1_YEASTLIP1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
SYA_YEASTALA1genetic
27708008
DIB1_YEASTDIB1genetic
27708008
PSB5_YEASTPRE2genetic
27708008
ALG1_YEASTALG1genetic
27708008
MAK5_YEASTMAK5genetic
27708008
CDC10_YEASTCDC10genetic
27708008
NOP14_YEASTNOP14genetic
27708008
UPPS_YEASTNUS1genetic
27708008
DAD1_YEASTDAD1genetic
27708008
SRPR_YEASTSRP101genetic
27708008
TFC6_YEASTTFC6genetic
27708008
PSB3_YEASTPUP3genetic
27708008
RSP5_YEASTRSP5genetic
27708008
CCA1_YEASTCCA1genetic
27708008
MOB2_YEASTMOB2genetic
27708008
STT3_YEASTSTT3genetic
27708008
HSF_YEASTHSF1genetic
27708008
MCE1_YEASTCEG1genetic
27708008
CBF3A_YEASTCBF2genetic
27708008
YIP1_YEASTYIP1genetic
27708008
SYNC_YEASTDED81genetic
27708008
SLN1_YEASTSLN1genetic
27708008
CYAA_YEASTCYR1genetic
27708008
TAD2_YEASTTAD2genetic
27708008
NU192_YEASTNUP192genetic
27708008
TIM16_YEASTPAM16genetic
27708008
RSC58_YEASTRSC58genetic
27708008
MED14_YEASTRGR1genetic
27708008
BOS1_YEASTBOS1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
CDC3_YEASTCDC3genetic
27708008
TAF13_YEASTTAF13genetic
27708008
RNA1_YEASTRNA1genetic
27708008
CAP_YEASTSRV2genetic
27708008
DBP6_YEASTDBP6genetic
27708008
MED7_YEASTMED7genetic
27708008
PROF_YEASTPFY1genetic
27708008
PSB2_YEASTPUP1genetic
27708008
RRS1_YEASTRRS1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATPF_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-144, AND MASSSPECTROMETRY.

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