VA0D1_HUMAN - dbPTM
VA0D1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VA0D1_HUMAN
UniProt AC P61421
Protein Name V-type proton ATPase subunit d 1
Gene Name ATP6V0D1
Organism Homo sapiens (Human).
Sequence Length 351
Subcellular Localization Membrane
Peripheral membrane protein
Cytoplasmic side . Localizes to centrosome and the base of the cilium.
Protein Description Subunit of the integral membrane V0 complex of vacuolar ATPase. Vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells, thus providing most of the energy required for transport processes in the vacuolar system. May play a role in coupling of proton transport and ATP hydrolysis (By similarity). May play a role in cilium biogenesis through regulation of the transport and the localization of proteins to the cilium (By similarity). In aerobic conditions, involved in intracellular iron homeostasis, thus triggering the activity of Fe(2+) prolyl hydroxylase (PHD) enzymes, and leading to HIF1A hydroxylation and subsequent proteasomal degradation. [PubMed: 28296633]
Protein Sequence MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLANEASPLTVSVIDDRLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNAILVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
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
24UbiquitinationEGLVRGLKAGVLSQA
HHHHHHHHHCCCCHH
46.01-
46UbiquitinationCETLEDLKLHLQSTD
CCCHHHHHHHHHCCC
46.30-
772-HydroxyisobutyrylationIDDRLKEKMVVEFRH
ECHHHHHHHHEEEHH
35.09-
77UbiquitinationIDDRLKEKMVVEFRH
ECHHHHHHHHEEEHH
35.09-
187AcetylationIIRNTLYKAYLESFY
HHHHHHHHHHHHHHH
33.4026051181
224PhosphorylationDRRAFIITINSFGTE
CCCEEEEEECCCCCC
14.86-
227PhosphorylationAFIITINSFGTELSK
EEEEEECCCCCCCCH
22.62-
230PhosphorylationITINSFGTELSKEDR
EEECCCCCCCCHHHH
31.57-
233PhosphorylationNSFGTELSKEDRAKL
CCCCCCCCHHHHHHH
27.97-
234UbiquitinationSFGTELSKEDRAKLF
CCCCCCCHHHHHHHC
76.02-
239UbiquitinationLSKEDRAKLFPHCGR
CCHHHHHHHCCCCCC
52.10-
248PhosphorylationFPHCGRLYPEGLAQL
CCCCCCCCHHHHHHH
9.6224927040
265UbiquitinationADDYEQVKNVADYYP
CCCHHHHHCHHHHCH
45.4521890473
270PhosphorylationQVKNVADYYPEYKLL
HHHCHHHHCHHHHHH
15.9319060867
271PhosphorylationVKNVADYYPEYKLLF
HHCHHHHCHHHHHHH
7.0822210691
274PhosphorylationVADYYPEYKLLFEGA
HHHHCHHHHHHHCCC
11.48-
275UbiquitinationADYYPEYKLLFEGAG
HHHCHHHHHHHCCCC
36.7321890473
283PhosphorylationLLFEGAGSNPGDKTL
HHHCCCCCCCCCCCH
39.0425850435
288UbiquitinationAGSNPGDKTLEDRFF
CCCCCCCCCHHHHHH
62.0121890473
289PhosphorylationGSNPGDKTLEDRFFE
CCCCCCCCHHHHHHH
39.8722210691
293MethylationGDKTLEDRFFEHEVK
CCCCHHHHHHHHHHH
28.86-
300UbiquitinationRFFEHEVKLNKLAFL
HHHHHHHHHHHHHHH
43.27-
343UbiquitinationIAQRHRAKIDNYIPI
HHHHHHHHHCCCCCC
51.022190698
347PhosphorylationHRAKIDNYIPIF---
HHHHHCCCCCCC---
12.3428796482

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 VA0D1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VA0D1_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 VA0D1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AT1A1_HUMANATP1A1physical
26344197
ATPA_HUMANATP5A1physical
26344197
ATPG_HUMANATP5C1physical
26344197
ATPO_HUMANATP5Ophysical
26344197
VPP1_HUMANATP6V0A1physical
26344197
EIF3A_HUMANEIF3Aphysical
26344197
NDUB8_HUMANNDUFB8physical
26344197
NDUS4_HUMANNDUFS4physical
26344197
NDUV1_HUMANNDUFV1physical
26344197
PSMD3_HUMANPSMD3physical
26344197
RAB2A_HUMANRAB2Aphysical
26344197
RPN1_HUMANRPN1physical
26344197
SSRA_HUMANSSR1physical
26344197
QCR6_HUMANUQCRHphysical
26344197
MVD1_HUMANMVDphysical
28514442
VPP2_HUMANATP6V0A2physical
28514442
VA0D2_HUMANATP6V0D2physical
28514442
LEPR_HUMANLEPRphysical
28514442
TBA3C_HUMANTUBA3Cphysical
28514442
VPP1_HUMANATP6V0A1physical
28514442
SNX25_HUMANSNX25physical
28514442
VMA21_HUMANVMA21physical
28514442
S22AN_HUMANSLC22A23physical
28514442
VPP3_HUMANTCIRG1physical
28514442
UBB_HUMANUBBphysical
28514442
S27A6_HUMANSLC27A6physical
28514442
CC115_HUMANCCDC115physical
28514442
UBP4_HUMANUSP4physical
28514442
SNX19_HUMANSNX19physical
28514442
F210B_HUMANFAM210Bphysical
28514442
M1IP1_HUMANMID1IP1physical
28514442
DHC24_HUMANDHCR24physical
28514442
PGES2_HUMANPTGES2physical
28514442
RENR_HUMANATP6AP2physical
28514442
SHIP2_HUMANINPPL1physical
28514442
B3GN2_HUMANB3GNT2physical
28514442
IKIP_HUMANIKBIPphysical
28514442
VAS1_HUMANATP6AP1physical
28514442
S27A2_HUMANSLC27A2physical
28514442
VATD_HUMANATP6V1Dphysical
28514442
CUL4A_HUMANCUL4Aphysical
28514442
MFS4B_HUMANKIAA1919physical
28514442
VATF_HUMANATP6V1Fphysical
28514442
K2013_HUMANKIAA2013physical
28514442
LETM1_HUMANLETM1physical
28514442
AGRL1_HUMANLPHN1physical
28514442
SCPDL_HUMANSCCPDHphysical
28514442
RDH13_HUMANRDH13physical
28514442
ENPP1_HUMANENPP1physical
28514442
ACSL4_HUMANACSL4physical
28514442

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 VA0D1_HUMAN

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Related Literatures of Post-Translational Modification

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