ATP5I_HUMAN - dbPTM
ATP5I_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATP5I_HUMAN
UniProt AC P56385
Protein Name ATP synthase subunit e, mitochondrial
Gene Name ATP5I
Organism Homo sapiens (Human).
Sequence Length 69
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. Minor subunit located with subunit a in the membrane..
Protein Sequence MVPPVQVSPLIKLGRYSALFLGVAYGATRYNYLKPRAEEERRIAAEEKKKQDELKRIARELAEDDSILK
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
8PhosphorylationMVPPVQVSPLIKLGR
CCCCCCCCHHHHHCH
9.2626074081
12UbiquitinationVQVSPLIKLGRYSAL
CCCCHHHHHCHHHHH
53.2024816145
17O-linked_GlycosylationLIKLGRYSALFLGVA
HHHHCHHHHHHHHHH
19.6930379171
25PhosphorylationALFLGVAYGATRYNY
HHHHHHHHCHHHHHC
12.60-
28PhosphorylationLGVAYGATRYNYLKP
HHHHHCHHHHHCCCH
29.35-
30PhosphorylationVAYGATRYNYLKPRA
HHHCHHHHHCCCHHH
12.1022817900
32PhosphorylationYGATRYNYLKPRAEE
HCHHHHHCCCHHHHH
13.7322817900
34SuccinylationATRYNYLKPRAEEER
HHHHHCCCHHHHHHH
23.3023954790
34UbiquitinationATRYNYLKPRAEEER
HHHHHCCCHHHHHHH
23.30-
34AcetylationATRYNYLKPRAEEER
HHHHHCCCHHHHHHH
23.3025825284
482-HydroxyisobutyrylationRRIAAEEKKKQDELK
HHHHHHHHHHHHHHH
57.69-
49UbiquitinationRIAAEEKKKQDELKR
HHHHHHHHHHHHHHH
59.9724816145
50UbiquitinationIAAEEKKKQDELKRI
HHHHHHHHHHHHHHH
74.2324816145
55UbiquitinationKKKQDELKRIARELA
HHHHHHHHHHHHHHH
39.4525015289
552-HydroxyisobutyrylationKKKQDELKRIARELA
HHHHHHHHHHHHHHH
39.45-
66PhosphorylationRELAEDDSILK----
HHHHHHCCCCC----
41.9925850435
69AcetylationAEDDSILK-------
HHHCCCCC-------
57.5368909
69UbiquitinationAEDDSILK-------
HHHCCCCC-------
57.5324816145

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 ATP5I_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATP5I_HUMAN !!

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 ATP5I_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RS16_HUMANRPS16physical
22939629
RS21_HUMANRPS21physical
22939629
RER1_HUMANRER1physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATP5I_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP