ATPD_HUMAN - dbPTM
ATPD_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATPD_HUMAN
UniProt AC P30049
Protein Name ATP synthase subunit delta, mitochondrial {ECO:0000305}
Gene Name ATP5F1D {ECO:0000312|HGNC:HGNC:837}
Organism Homo sapiens (Human).
Sequence Length 168
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 turnover 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(1) domain and of the central stalk which is part of the complex rotary element. 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 MLPAALLRRPGLGRLVRHARAYAEAAAAPAAASGPNQMSFTFASPTQVFFNGANVRQVDVPTLTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSIAVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQAELVGTADEATRAEIQIRIEANEALVKALE
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
39PhosphorylationASGPNQMSFTFASPT
HCCCCEEEEEECCCC
16.03-
44PhosphorylationQMSFTFASPTQVFFN
EEEEEECCCCEEEEC
25.04-
131UbiquitinationMLDLGAAKANLEKAQ
HHHHHHHHHHHHHHH
36.9523503661
136AcetylationAAKANLEKAQAELVG
HHHHHHHHHHHHHHC
49.3023954790
136SuccinylationAAKANLEKAQAELVG
HHHHHHHHHHHHHHC
49.30-
136UbiquitinationAAKANLEKAQAELVG
HHHHHHHHHHHHHHC
49.3023503661
1362-HydroxyisobutyrylationAAKANLEKAQAELVG
HHHHHHHHHHHHHHC
49.30-
136MalonylationAAKANLEKAQAELVG
HHHHHHHHHHHHHHC
49.3026320211
136SuccinylationAAKANLEKAQAELVG
HHHHHHHHHHHHHHC
49.3027452117
144PhosphorylationAQAELVGTADEATRA
HHHHHHCCCCHHHHH
24.37-
165AcetylationEANEALVKALE----
HHHHHHHHHHC----
48.3725038526
165SuccinylationEANEALVKALE----
HHHHHHHHHHC----
48.37-
165UbiquitinationEANEALVKALE----
HHHHHHHHHHC----
48.3724816145
165SuccinylationEANEALVKALE----
HHHHHHHHHHC----
48.3727452117

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 ATPD_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATPD_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 ATPD_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ATPA_HUMANATP5A1physical
26344197
ATPG_HUMANATP5C1physical
26344197
ATP5I_HUMANATP5Iphysical
26344197
ATP5J_HUMANATP5Jphysical
26344197
ATPK_HUMANATP5J2physical
26344197
VA0D1_HUMANATP6V0D1physical
26344197
COX41_HUMANCOX4I1physical
26344197
COX5A_HUMANCOX5Aphysical
26344197
OST48_HUMANDDOSTphysical
26344197
RT4I1_HUMANRTN4IP1physical
28514442
ATP5E_HUMANATP5Ephysical
28514442
F172A_HUMANFAM172Aphysical
28514442
AUHM_HUMANAUHphysical
28514442
ATPB_HUMANATP5Bphysical
28514442
MTG2_HUMANMTG2physical
28514442
ATP8_HUMANATP8physical
28514442
ATPA_HUMANATP5A1physical
28514442
AT5F1_HUMANATP5F1physical
28514442
CPT2_HUMANCPT2physical
28514442
ATP5H_HUMANATP5Hphysical
28514442
TOP3A_HUMANTOP3Aphysical
28514442
TRUA_HUMANPUS1physical
28514442
NDUB5_HUMANNDUFB5physical
28514442
ATPO_HUMANATP5Ophysical
28514442
DHRS4_HUMANDHRS4physical
28514442
IF2M_HUMANMTIF2physical
28514442
SYYM_HUMANYARS2physical
28514442
NPS3A_HUMANNIPSNAP3Aphysical
28514442
ATP5L_HUMANATP5Lphysical
28514442
ATPG_HUMANATP5C1physical
28514442
PNPT1_HUMANPNPT1physical
28514442
ACTBL_HUMANACTBL2physical
28514442
SYLM_HUMANLARS2physical
28514442
COPB2_HUMANCOPB2physical
28514442
SIR3_HUMANSIRT3physical
28514442
ATP5I_HUMANATP5Iphysical
28514442
EFTS_HUMANTSFMphysical
28514442
CQ080_HUMANC17orf80physical
28514442

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

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Related Literatures of Post-Translational Modification

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