ATPB_MOUSE - dbPTM
ATPB_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATPB_MOUSE
UniProt AC P56480
Protein Name ATP synthase subunit beta, mitochondrial {ECO:0000305}
Gene Name Atp5f1b {ECO:0000250|UniProtKB:P06576}
Organism Mus musculus (Mouse).
Sequence Length 529
Subcellular Localization Mitochondrion inner membrane
Peripheral membrane protein
Matrix side .
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..
Protein Sequence MLSLVGRVASASASGALRGLSPSAALPQAQLLLRAAPAGVHPARDYAAQASAAPKAGTATGRIVAVIGAVVDVQFDEGLPPILNALEVQGRDSRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGNEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGEYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS
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
21PhosphorylationSGALRGLSPSAALPQ
HHHHCCCCHHHHCHH		21.4524759943
23PhosphorylationALRGLSPSAALPQAQ
HHCCCCHHHHCHHHH		23.8526643407
106PhosphorylationVAQHLGESTVRTIAM
HHHHHCCCCEEEEEE		30.3323140645
106O-linked_GlycosylationVAQHLGESTVRTIAM
HHHHHCCCCEEEEEE		30.33-
107PhosphorylationAQHLGESTVRTIAMD
HHHHCCCCEEEEEEC		15.0923140645
110PhosphorylationLGESTVRTIAMDGTE
HCCCCEEEEEECCCC		14.5722817900
116PhosphorylationRTIAMDGTEGLVRGQ
EEEEECCCCCEECCE		23.7122817900
124AcetylationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.8123576753
124UbiquitinationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.8127667366
124SuccinylationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.8123806337
124SuccinylationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.81-
124MalonylationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.8126073543
124GlutarylationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.8124703693
128O-linked_GlycosylationRGQKVLDSGAPIKIP
CCEEEECCCCCCEEC		32.4736014013
128PhosphorylationRGQKVLDSGAPIKIP
CCEEEECCCCCCEEC		32.4720495213
133SuccinylationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.6423806337
133GlutarylationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.6424703693
133AcetylationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.6423576753
133MalonylationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.6426073543
133UbiquitinationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.6427667366
133SuccinylationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.64-
140PhosphorylationKIPVGPETLGRIMNV
EECCCHHHHHHHHHH		37.3322817900
159AcetylationIDERGPIKTKQFAPI
CCCCCCCCCCCCCCC		53.4523864654
159UbiquitinationIDERGPIKTKQFAPI
CCCCCCCCCCCCCCC		53.45-
159SuccinylationIDERGPIKTKQFAPI
CCCCCCCCCCCCCCC		53.4524315375
161AcetylationERGPIKTKQFAPIHA
CCCCCCCCCCCCCCC		38.1223576753
161SuccinylationERGPIKTKQFAPIHA
CCCCCCCCCCCCCCC		38.1223806337
161SuccinylationERGPIKTKQFAPIHA
CCCCCCCCCCCCCCC		38.12-
198AcetylationDLLAPYAKGGKIGLF
HHHHCCCCCCEEEEE		63.4523576753
198UbiquitinationDLLAPYAKGGKIGLF
HHHHCCCCCCEEEEE		63.4527667366
198SuccinylationDLLAPYAKGGKIGLF
HHHHCCCCCCEEEEE		63.45-
198GlutarylationDLLAPYAKGGKIGLF
HHHHCCCCCCEEEEE		63.4524703693
201UbiquitinationAPYAKGGKIGLFGGA
HCCCCCCEEEEECCC		42.1227667366
230PhosphorylationVAKAHGGYSVFAGVG
HHHHCCCEEEEECCC		13.2725195567
231PhosphorylationAKAHGGYSVFAGVGE
HHHCCCEEEEECCCC		17.6524899341
241DimethylationAGVGERTREGNDLYH
ECCCCCCCCCCHHHH		56.92-
247PhosphorylationTREGNDLYHEMIESG
CCCCCHHHHHHHHHC		9.90-
259AcetylationESGVINLKDATSKVA
HHCCCCHHHCCCCEE		40.6123576753
259UbiquitinationESGVINLKDATSKVA
HHCCCCHHHCCCCEE		40.61-
259SuccinylationESGVINLKDATSKVA
HHCCCCHHHCCCCEE		40.61-
259SuccinylationESGVINLKDATSKVA
HHCCCCHHHCCCCEE		40.6123806337
264AcetylationNLKDATSKVALVYGQ
CHHHCCCCEEEEEEE		27.4623576753
264SuccinylationNLKDATSKVALVYGQ
CHHHCCCCEEEEEEE		27.46-
264UbiquitinationNLKDATSKVALVYGQ
CHHHCCCCEEEEEEE		27.4627667366
264SuccinylationNLKDATSKVALVYGQ
CHHHCCCCEEEEEEE		27.4623806337
269NitrationTSKVALVYGQMNEPP
CCCEEEEEEECCCCC		11.51-
312PhosphorylationIDNIFRFTQAGSEVS
EECHHHHHCCCHHHH		17.1622817900
316PhosphorylationFRFTQAGSEVSALLG
HHHHCCCHHHHHHHC		37.5322817900
319PhosphorylationTQAGSEVSALLGRIP
HCCCHHHHHHHCCCC		14.7821183079
327PhosphorylationALLGRIPSAVGYQPT
HHHCCCCCCCCCCCE		32.9619854140
337PhosphorylationGYQPTLATDMGTMQE
CCCCEEECCCCCCHH		29.6319854140
341PhosphorylationTLATDMGTMQERITT
EEECCCCCCHHCEEC		14.7219854140
350AcetylationQERITTTKKGSITSV
HHCEECCCCCCEEEE		53.7123864654
353PhosphorylationITTTKKGSITSVQAI
EECCCCCCEEEEEEE		31.4121082442
356PhosphorylationTKKGSITSVQAIYVP
CCCCCEEEEEEEEEE		15.5721183079
403PhosphorylationPAVDPLDSTSRIMDP
CCCCCCCCCCCCCCC		35.6519060867
404PhosphorylationAVDPLDSTSRIMDPN
CCCCCCCCCCCCCCC		22.9923984901
405PhosphorylationVDPLDSTSRIMDPNI
CCCCCCCCCCCCCCC		24.6223984901
426AcetylationDVARGVQKILQDYKS
HHHHHHHHHHHHHHH		42.8723576753
426UbiquitinationDVARGVQKILQDYKS
HHHHHHHHHHHHHHH		42.87-
426SuccinylationDVARGVQKILQDYKS
HHHHHHHHHHHHHHH		42.8724315375
432AcetylationQKILQDYKSLQDIIA
HHHHHHHHHHHHHHH		53.6423864654
432SuccinylationQKILQDYKSLQDIIA
HHHHHHHHHHHHHHH		53.6426388266
433PhosphorylationKILQDYKSLQDIIAI
HHHHHHHHHHHHHHH		25.6523737553
447PhosphorylationILGMDELSEEDKLTV
HHCCHHCCHHHCHHH		36.5723984901
451AcetylationDELSEEDKLTVSRAR
HHCCHHHCHHHHHHH		49.7023954790
465PhosphorylationRKIQRFLSQPFQVAE
HHHHHHHCCCCEEEH		32.8523984901
475PhosphorylationFQVAEVFTGHMGKLV
CEEEHHHHCCCCCEE		31.2120495213
480AcetylationVFTGHMGKLVPLKET
HHHCCCCCEEEHHHH		38.4423576753
480SuccinylationVFTGHMGKLVPLKET
HHHCCCCCEEEHHHH		38.4426388266
485SuccinylationMGKLVPLKETIKGFQ
CCCEEEHHHHHHHHH		46.90-
485MalonylationMGKLVPLKETIKGFQ
CCCEEEHHHHHHHHH		46.9026320211
485AcetylationMGKLVPLKETIKGFQ
CCCEEEHHHHHHHHH		46.9023576753
485UbiquitinationMGKLVPLKETIKGFQ
CCCEEEHHHHHHHHH		46.9027667366
508NitrationHLPEQAFYMVGPIEE
CCCCCCEEEECCHHH		8.23-
519AcetylationPIEEAVAKADKLAEE
CHHHHHHHHHHHHHH		50.9823954790
522MalonylationEAVAKADKLAEEHGS
HHHHHHHHHHHHHCC		55.2326073543
522SuccinylationEAVAKADKLAEEHGS
HHHHHHHHHHHHHCC		55.2323806337
522SuccinylationEAVAKADKLAEEHGS
HHHHHHHHHHHHHCC		55.23-
522AcetylationEAVAKADKLAEEHGS
HHHHHHHHHHHHHCC		55.2323806337
529PhosphorylationKLAEEHGS-------
HHHHHHCC-------		38.6722324799
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 ATPB_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
133KAcetylation

23806337
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 ATPB_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ATPB_MOUSE !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATPB_MOUSE

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey.";
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
Mol. Cell 23:607-618(2006).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-133; LYS-259 AND LYS-522,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Mitochondrial phosphoproteome revealed by an improved IMAC method andMS/MS/MS.";
Lee J., Xu Y., Chen Y., Sprung R., Kim S.C., Xie S., Zhao Y.;
Mol. Cell. Proteomics 6:669-676(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-529, AND MASSSPECTROMETRY.

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