ATP5H_RAT - dbPTM
ATP5H_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATP5H_RAT
UniProt AC P31399
Protein Name ATP synthase subunit d, mitochondrial
Gene Name Atp5h
Organism Rattus norvegicus (Rat).
Sequence Length 161
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 MAGRKLALKTIDWVSFVEIMPQNQKAIGNALKSWNETFHTRLASLSEKPPAIDWAYYRANVDKPGLVDDFKNKYNALKIPVPEDKYTALVDAEEKEDVKNCAQFVTGSQARVREYEKQLEKIKNMIPFDQMTIDDLNEVFPETKLDKRKYPYWPHQPIENL
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
2Acetylation------MAGRKLALK
------CCCCHHHHH
26.88-
10PhosphorylationGRKLALKTIDWVSFV
CCHHHHHHCCEEEEE
25.6423991683
15PhosphorylationLKTIDWVSFVEIMPQ
HHHCCEEEEEEECCC
21.2223991683
32AcetylationKAIGNALKSWNETFH
HHHHHHHHHHHHHHH
51.5222902405
33PhosphorylationAIGNALKSWNETFHT
HHHHHHHHHHHHHHH
35.6623991683
44PhosphorylationTFHTRLASLSEKPPA
HHHHHHHHHCCCCCC
36.7023991683
44O-linked_GlycosylationTFHTRLASLSEKPPA
HHHHHHHHHCCCCCC
36.7026446791
46PhosphorylationHTRLASLSEKPPAID
HHHHHHHCCCCCCCC
40.8723991683
48AcetylationRLASLSEKPPAIDWA
HHHHHCCCCCCCCEE
53.5822902405
63SuccinylationYYRANVDKPGLVDDF
EHHCCCCCCCCHHHH
36.3826843850
63AcetylationYYRANVDKPGLVDDF
EHHCCCCCCCCHHHH
36.3822902405
71SuccinylationPGLVDDFKNKYNALK
CCCHHHHHHHCCCCC
60.5726843850
71AcetylationPGLVDDFKNKYNALK
CCCHHHHHHHCCCCC
60.5722902405
73SuccinylationLVDDFKNKYNALKIP
CHHHHHHHCCCCCCC
40.2426843850
73AcetylationLVDDFKNKYNALKIP
CHHHHHHHCCCCCCC
40.2422902405
78SuccinylationKNKYNALKIPVPEDK
HHHCCCCCCCCCCCC
42.42-
78AcetylationKNKYNALKIPVPEDK
HHHCCCCCCCCCCCC
42.4222902405
85SuccinylationKIPVPEDKYTALVDA
CCCCCCCCCEEEECH
42.72-
85AcetylationKIPVPEDKYTALVDA
CCCCCCCCCEEEECH
42.7222902405
95AcetylationALVDAEEKEDVKNCA
EEECHHHHHHHHHHH
51.2022902405
95SuccinylationALVDAEEKEDVKNCA
EEECHHHHHHHHHHH
51.2026843850
99AcetylationAEEKEDVKNCAQFVT
HHHHHHHHHHHHHHH
59.6422902405
106PhosphorylationKNCAQFVTGSQARVR
HHHHHHHHHHHHHHH
32.1927097102
108PhosphorylationCAQFVTGSQARVREY
HHHHHHHHHHHHHHH
15.9927097102
117AcetylationARVREYEKQLEKIKN
HHHHHHHHHHHHHHH
60.3225786129
117SuccinylationARVREYEKQLEKIKN
HHHHHHHHHHHHHHH
60.3226843850
121AcetylationEYEKQLEKIKNMIPF
HHHHHHHHHHHCCCC
68.5226302492
123AcetylationEKQLEKIKNMIPFDQ
HHHHHHHHHCCCCCC
52.0822902405
144SuccinylationNEVFPETKLDKRKYP
HHHCCCCCCCCCCCC
53.69-
144AcetylationNEVFPETKLDKRKYP
HHHCCCCCCCCCCCC
53.6922902405
147AcetylationFPETKLDKRKYPYWP
CCCCCCCCCCCCCCC
62.3126302492
149AcetylationETKLDKRKYPYWPHQ
CCCCCCCCCCCCCCC
57.2122902405
149SuccinylationETKLDKRKYPYWPHQ
CCCCCCCCCCCCCCC
57.2126843850
152PhosphorylationLDKRKYPYWPHQPIE
CCCCCCCCCCCCCCC
28.60-

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 ATP5H_RAT !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATP5H_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 ATP5H_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ATP5H_RAT !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATP5H_RAT

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Related Literatures of Post-Translational Modification

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