ATPB_RAT - dbPTM
ATPB_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATPB_RAT
UniProt AC P10719
Protein Name ATP synthase subunit beta, mitochondrial {ECO:0000305}
Gene Name Atp5f1b {ECO:0000312|RGD:621368}
Organism Rattus norvegicus (Rat).
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 MLSLVGRVASASASGALRGLNPLAALPQAHLLLRTAPAGVHPARDYAAQSSAAPKAGTATGQIVAVIGAVVDVQFDEGLPPILNALEVQGRESRLVLEVAQHLGESTVRTIAMDGTEGLVRGQKVLDSGAPIKIPVGPETLGRIMNVIGEPIDERGPIKTKQFAPIHAEAPEFIEMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYHEMIESGVINLKDATSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGTMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIVGSEHYDVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVSRARKIQRFLSQPFQVAEVFTGHMGKLVPLKETIKGFQQILAGDYDHLPEQAFYMVGPIEEAVAKADKLAEEHGS
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
106PhosphorylationVAQHLGESTVRTIAM
HHHHHCCCCEEEEEE		30.3323991683
106O-linked_GlycosylationVAQHLGESTVRTIAM
HHHHHCCCCEEEEEE		30.3318683930
107PhosphorylationAQHLGESTVRTIAMD
HHHHCCCCEEEEEEC		15.0923991683
116O-linked_GlycosylationRTIAMDGTEGLVRGQ
EEEEECCCCCEECCE		23.7118683930
124SuccinylationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.81-
124SuccinylationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.8126843850
124AcetylationEGLVRGQKVLDSGAP
CCEECCEEEECCCCC		47.8122902405
128O-linked_GlycosylationRGQKVLDSGAPIKIP
CCEEEECCCCCCEEC		32.4718683930
133SuccinylationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.64-
133AcetylationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.6425786129
133SuccinylationLDSGAPIKIPVGPET
ECCCCCCEECCCHHH		39.6426843850
159AcetylationIDERGPIKTKQFAPI
CCCCCCCCCCCCCCC		53.4522902405
161AcetylationERGPIKTKQFAPIHA
CCCCCCCCCCCCCCC		38.1226302492
161SuccinylationERGPIKTKQFAPIHA
CCCCCCCCCCCCCCC		38.12-
161SuccinylationERGPIKTKQFAPIHA
CCCCCCCCCCCCCCC		38.12-
198SuccinylationDLLAPYAKGGKIGLF
HHHHCCCCCCEEEEE		63.4526843850
198AcetylationDLLAPYAKGGKIGLF
HHHHCCCCCCEEEEE		63.4522902405
230PhosphorylationVAKAHGGYSVFAGVG
HHHHCCCEEEEECCC		13.2723991683
231PhosphorylationAKAHGGYSVFAGVGE
HHHCCCEEEEECCCC		17.6523991683
231O-linked_GlycosylationAKAHGGYSVFAGVGE
HHHCCCEEEEECCCC		17.6518683930
259SuccinylationESGVINLKDATSKVA
HHCCCCHHHCCCCEE		40.61-
259SuccinylationESGVINLKDATSKVA
HHCCCCHHHCCCCEE		40.61-
259AcetylationESGVINLKDATSKVA
HHCCCCHHHCCCCEE		40.6125786129
264SuccinylationNLKDATSKVALVYGQ
CHHHCCCCEEEEEEE		27.46-
264SuccinylationNLKDATSKVALVYGQ
CHHHCCCCEEEEEEE		27.46-
264AcetylationNLKDATSKVALVYGQ
CHHHCCCCEEEEEEE		27.4622902405
312PhosphorylationIDNIFRFTQAGSEVS
EECHHHHHCCCHHHH		17.16-
316O-linked_GlycosylationFRFTQAGSEVSALLG
HHHHCCCHHHHHHHC		37.5318683930
316PhosphorylationFRFTQAGSEVSALLG
HHHHCCCHHHHHHHC		37.5323984901
319PhosphorylationTQAGSEVSALLGRIP
HCCCHHHHHHHCCCC		14.7823984901
327O-linked_GlycosylationALLGRIPSAVGYQPT
HHHCCCCCCCCCCCE		32.9618683930
331PhosphorylationRIPSAVGYQPTLATD
CCCCCCCCCCEEECC		12.53-
351AcetylationERITTTKKGSITSVQ
HCEECCCCCCEEEEE		56.6655699601
395PhosphorylationAIAELGIYPAVDPLD
HHHHHCCCCCCCCCC		5.37-
403PhosphorylationPAVDPLDSTSRIMDP
CCCCCCCCCCCCCCC		35.6522673903
404PhosphorylationAVDPLDSTSRIMDPN
CCCCCCCCCCCCCCC		22.9922673903
405PhosphorylationVDPLDSTSRIMDPNI
CCCCCCCCCCCCCCC		24.6222673903
415O-linked_GlycosylationMDPNIVGSEHYDVAR
CCCCCCCCHHHHHHH		15.4218683930
415PhosphorylationMDPNIVGSEHYDVAR
CCCCCCCCHHHHHHH		15.4223991683
418PhosphorylationNIVGSEHYDVARGVQ
CCCCCHHHHHHHHHH		14.2028689409
426AcetylationDVARGVQKILQDYKS
HHHHHHHHHHHHHHH		42.8722902405
432AcetylationQKILQDYKSLQDIIA
HHHHHHHHHHHHHHH		53.6426302492
433PhosphorylationKILQDYKSLQDIIAI
HHHHHHHHHHHHHHH		25.6522673903
455O-linked_GlycosylationEEDKLTVSRARKIQR
HHHCHHHHHHHHHHH		18.2618683930
465PhosphorylationRKIQRFLSQPFQVAE
HHHHHHHCCCCEEEH		32.8523984901
465O-linked_GlycosylationRKIQRFLSQPFQVAE
HHHHHHHCCCCEEEH		32.8518683930
480AcetylationVFTGHMGKLVPLKET
HHHCCCCCEEEHHHH		38.4422902405
485AcetylationMGKLVPLKETIKGFQ
CCCEEEHHHHHHHHH		46.9022902405
485SuccinylationMGKLVPLKETIKGFQ
CCCEEEHHHHHHHHH		46.9026843850
487O-linked_GlycosylationKLVPLKETIKGFQQI
CEEEHHHHHHHHHHH		26.8018683930
489AcetylationVPLKETIKGFQQILA
EEHHHHHHHHHHHHC		62.1826302492
519AcetylationPIEEAVAKADKLAEE
CHHHHHHHHHHHHHH		50.9825786129
522SuccinylationEAVAKADKLAEEHGS
HHHHHHHHHHHHHCC		55.23-
522SuccinylationEAVAKADKLAEEHGS
HHHHHHHHHHHHHCC		55.23-
522AcetylationEAVAKADKLAEEHGS
HHHHHHHHHHHHHCC		55.2325786129
529PhosphorylationKLAEEHGS-------
HHHHHHCC-------		38.6729779826
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_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATPB_RAT !!
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_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

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

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Related Literatures of Post-Translational Modification

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