VATA_MOUSE - dbPTM
VATA_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VATA_MOUSE
UniProt AC P50516
Protein Name V-type proton ATPase catalytic subunit A
Gene Name Atp6v1a
Organism Mus musculus (Mouse).
Sequence Length 617
Subcellular Localization
Protein Description Catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase vacuolar ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells. 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 (By similarity)..
Protein Sequence MDFSKLPKIRDEDKESTFGYVHGVSGPVVTACDMAGAAMYELVRVGHSELVGEIIRLEGDMATIQVYEETSGVSVGDPVLRTGKPLSVELGPGIMGAIFDGIQRPLSDISSQTQSIYIPRGVNVSALSRDIKWEFIPSKNLRVGSHITGGDIYGIVNENSLIKHKIMLPPRNRGSVTYIAPPGNYDASDVVLELEFEGVKEKFSMVQVWPVRQVRPVTEKLPANHPLLTGQRVLDALFPCVQGGTTAIPGAFGCGKTVISQSLSKYSNSDVIIYVGCGERGNEMSEVLRDFPELTMEVDGKVESIMKRTALVANTSNMPVAAREASIYTGITLSEYFRDMGYHVSMMADSTSRWAEALREISGRLAEMPADSGYPAYLGARLASFYERAGRVKCLGNPEREGSVSIVGAVSPPGGDFSDPVTSATLGIVQVFWGLDKKLAQRKHFPSVNWLISYSKYMRALDEYYDKHFTEFVPLRTKAKEILQEEEDLAEIVQLVGKASLAETDKITLEVAKLIKDDFLQQNGYTPYDRFCPFYKTVGMLSNMISFYDMARRAVETTAQSDNKITWSIIREHMGEILYKLSSMKFKDPVKDGEAKIKADYAQLLEDMQNAFRSLED
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
40PhosphorylationDMAGAAMYELVRVGH
HHHCHHHHHHHHCCC		11.03-
84UbiquitinationDPVLRTGKPLSVELG
CCEECCCCCCEEEEC		42.0222790023
132UbiquitinationSALSRDIKWEFIPSK
HHHCCCCCCEECCCC		44.9822790023
139UbiquitinationKWEFIPSKNLRVGSH
CCEECCCCCCEEECE		55.4322790023
160PhosphorylationYGIVNENSLIKHKIM
EEEECCCCCCEEEEE		25.8729899451
163UbiquitinationVNENSLIKHKIMLPP
ECCCCCCEEEEECCC		44.1022790023
165UbiquitinationENSLIKHKIMLPPRN
CCCCCEEEEECCCCC		25.4722790023
175PhosphorylationLPPRNRGSVTYIAPP
CCCCCCCCEEEEECC		14.1922817900
202UbiquitinationEFEGVKEKFSMVQVW
EEECHHHCEEEEEEE		36.7022790023
220UbiquitinationQVRPVTEKLPANHPL
CCEECCCCCCCCCCC		50.8622790023
240S-palmitoylationVLDALFPCVQGGTTA
HHHHHHCCCCCCCCC		2.5328680068
307UbiquitinationGKVESIMKRTALVAN
CCHHHHHHHHEEEEC		44.9527667366
309PhosphorylationVESIMKRTALVANTS
HHHHHHHHEEEECCC		20.8720531401
316PhosphorylationTALVANTSNMPVAAR
HEEEECCCCCCCHHH		30.8220531401
326PhosphorylationPVAAREASIYTGITL
CCHHHHHHHHCCCCH		16.0420531401
328PhosphorylationAAREASIYTGITLSE
HHHHHHHHCCCCHHH		9.0920531401
329PhosphorylationAREASIYTGITLSEY
HHHHHHHCCCCHHHH		22.0420531401
332PhosphorylationASIYTGITLSEYFRD
HHHHCCCCHHHHHHH		26.1020531401
334PhosphorylationIYTGITLSEYFRDMG
HHCCCCHHHHHHHCC		22.9220531401
336PhosphorylationTGITLSEYFRDMGYH
CCCCHHHHHHHCCCC		10.6720531401
342PhosphorylationEYFRDMGYHVSMMAD
HHHHHCCCCHHEECC		7.7520531401
345PhosphorylationRDMGYHVSMMADSTS
HHCCCCHHEECCCHH		6.9120531401
350PhosphorylationHVSMMADSTSRWAEA
CHHEECCCHHHHHHH		20.8120531401
351PhosphorylationVSMMADSTSRWAEAL
HHEECCCHHHHHHHH		23.9020531401
352PhosphorylationSMMADSTSRWAEALR
HEECCCHHHHHHHHH		29.7620531401
372PhosphorylationLAEMPADSGYPAYLG
HCCCCCCCCCCCHHH		42.1920415495
374PhosphorylationEMPADSGYPAYLGAR
CCCCCCCCCCHHHHH		6.6622817900
384PhosphorylationYLGARLASFYERAGR
HHHHHHHHHHHHCCC		32.7122942356
465PhosphorylationMRALDEYYDKHFTEF
HHHHHHHHHHHCHHC		19.23-
467UbiquitinationALDEYYDKHFTEFVP
HHHHHHHHHCHHCCC		25.2122790023
467AcetylationALDEYYDKHFTEFVP
HHHHHHHHHCHHCCC		25.2123954790
480UbiquitinationVPLRTKAKEILQEEE
CCCHHHHHHHHHCHH		47.0122790023
513UbiquitinationKITLEVAKLIKDDFL
CHHHHHHHHHHHHHH		56.7922790023
516UbiquitinationLEVAKLIKDDFLQQN
HHHHHHHHHHHHHHC		62.7822790023
528PhosphorylationQQNGYTPYDRFCPFY
HHCCCCCHHHCCHHH		16.3825367039
532S-nitrosylationYTPYDRFCPFYKTVG
CCCHHHCCHHHHHHH		2.0724895380
561PhosphorylationAVETTAQSDNKITWS
HHHHHHCCCCCCCHH		40.4629899451
568PhosphorylationSDNKITWSIIREHMG
CCCCCCHHHHHHHHH		10.2522817900
579PhosphorylationEHMGEILYKLSSMKF
HHHHHHHHHHHCCCC		18.6225195567
580UbiquitinationHMGEILYKLSSMKFK
HHHHHHHHHHCCCCC		38.1522790023
587UbiquitinationKLSSMKFKDPVKDGE
HHHCCCCCCCCCCCC		56.4527667366
598UbiquitinationKDGEAKIKADYAQLL
CCCCHHHHHHHHHHH		34.2022790023
601NitrationEAKIKADYAQLLEDM
CHHHHHHHHHHHHHH		10.91-
614PhosphorylationDMQNAFRSLED----
HHHHHHHCCCC----		29.6529899451
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
175SPhosphorylationKinaseAURKAO14965
GPS
175SPhosphorylationKinasePRKACAP17612
GPS
175SPhosphorylationKinasePKA-FAMILY-GPS
384SPhosphorylationKinasePRKAA1Q13131
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VATA_MOUSE !!
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 VATA_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TRAF6_MOUSETraf6physical
16196101
ACTN4_MOUSEActn4physical
16196101
ACTN1_MOUSEActn1physical
16196101
ACTB_MOUSEActbphysical
16196101
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VATA_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations.";
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
Mol. Cell. Proteomics 6:283-293(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384, AND MASSSPECTROMETRY.
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain.";
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
J. Proteome Res. 7:311-318(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-374, AND MASSSPECTROMETRY.

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