VPP1_HUMAN - dbPTM
VPP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPP1_HUMAN
UniProt AC Q93050
Protein Name V-type proton ATPase 116 kDa subunit a isoform 1
Gene Name ATP6V0A1
Organism Homo sapiens (Human).
Sequence Length 837
Subcellular Localization Cytoplasmic vesicle membrane
Multi-pass membrane protein. Melanosome. Coated vesicle. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Protein Description Required for assembly and activity of the vacuolar ATPase. Potential role in differential targeting and regulation of the enzyme for a specific organelle (By similarity)..
Protein Sequence MGELFRSEEMTLAQLFLQSEAAYCCVSELGELGKVQFRDLNPDVNVFQRKFVNEVRRCEEMDRKLRFVEKEIRKANIPIMDTGENPEVPFPRDMIDLEANFEKIENELKEINTNQEALKRNFLELTELKFILRKTQQFFDEMADPDLLEESSSLLEPSEMGRGTPLRLGFVAGVINRERIPTFERMLWRVCRGNVFLRQAEIENPLEDPVTGDYVHKSVFIIFFQGDQLKNRVKKICEGFRASLYPCPETPQERKEMASGVNTRIDDLQMVLNQTEDHRQRVLQAAAKNIRVWFIKVRKMKAIYHTLNLCNIDVTQKCLIAEVWCPVTDLDSIQFALRRGTEHSGSTVPSILNRMQTNQTPPTYNKTNKFTYGFQNIVDAYGIGTYREINPAPYTIITFPFLFAVMFGDFGHGILMTLFAVWMVLRESRILSQKNENEMFSTVFSGRYIILLMGVFSMYTGLIYNDCFSKSLNIFGSSWSVRPMFTYNWTEETLRGNPVLQLNPALPGVFGGPYPFGIDPIWNIATNKLTFLNSFKMKMSVILGIIHMLFGVSLSLFNHIYFKKPLNIYFGFIPEIIFMTSLFGYLVILIFYKWTAYDAHTSENAPSLLIHFINMFLFSYPESGYSMLYSGQKGIQCFLVVVALLCVPWMLLFKPLVLRRQYLRRKHLGTLNFGGIRVGNGPTEEDAEIIQHDQLSTHSEDADEPSEDEVFDFGDTMVHQAIHTIEYCLGCISNTASYLRLWALSLAHAQLSEVLWTMVIHIGLSVKSLAGGLVLFFFFTAFATLTVAILLIMEGLSAFLHALRLHWVEFQNKFYSGTGFKFLPFSFEHIREGKFEE
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
25S-palmitoylationQSEAAYCCVSELGEL
HCHHHHHHHHHHHHH		2.1628266544
50UbiquitinationDVNVFQRKFVNEVRR
CCCHHHHHHHHHHHH		42.77-
70AcetylationRKLRFVEKEIRKANI
HHHHHHHHHHHHCCC		53.8126051181
70 (in isoform 3)Ubiquitination-53.81-
74UbiquitinationFVEKEIRKANIPIMD
HHHHHHHHCCCCCCC		51.9921906983
74 (in isoform 2)Ubiquitination-51.9921890473
74 (in isoform 1)Ubiquitination-51.9921890473
74 (in isoform 3)Ubiquitination-51.99-
103 (in isoform 1)Ubiquitination-51.7021890473
103UbiquitinationDLEANFEKIENELKE
CHHHHHHHHHHHHHH		51.7021906983
103 (in isoform 2)Ubiquitination-51.7021890473
109UbiquitinationEKIENELKEINTNQE
HHHHHHHHHCCCCHH		50.82-
119UbiquitinationNTNQEALKRNFLELT
CCCHHHHHHHHHHHH		52.95-
1192-HydroxyisobutyrylationNTNQEALKRNFLELT
CCCHHHHHHHHHHHH		52.95-
134UbiquitinationELKFILRKTQQFFDE
HHHHHHHHHHHHHHH		47.44-
151PhosphorylationDPDLLEESSSLLEPS
CHHHHHHHHHCCCHH		18.8224275569
153PhosphorylationDLLEESSSLLEPSEM
HHHHHHHHCCCHHHC		46.3728857561
214PhosphorylationEDPVTGDYVHKSVFI
CCCCCCCCCCCEEEE		13.0524927040
235UbiquitinationQLKNRVKKICEGFRA
HHHHHHHHHHHHHHH		50.13-
242 (in isoform 3)Ubiquitination-11.13-
250PhosphorylationSLYPCPETPQERKEM
HHCCCCCCHHHHHHH		18.5321082442
270SulfoxidationTRIDDLQMVLNQTED
CHHHHHHHHHHCCHH		4.8721406390
288 (in isoform 1)Ubiquitination-48.4521890473
288 (in isoform 2)Ubiquitination-48.4521890473
288UbiquitinationRVLQAAAKNIRVWFI
HHHHHHHHHCCEEEE		48.4521890473
295UbiquitinationKNIRVWFIKVRKMKA
HHCCEEEEEHHHHHH		2.0621890473
332PhosphorylationCPVTDLDSIQFALRR
CCCCCHHHHHHHHHC		26.1127067055
357PhosphorylationSILNRMQTNQTPPTY
HHHHHHHCCCCCCCC		21.6823186163
360PhosphorylationNRMQTNQTPPTYNKT
HHHHCCCCCCCCCCC		33.0527732954
363PhosphorylationQTNQTPPTYNKTNKF
HCCCCCCCCCCCCCC		40.7127732954
364PhosphorylationTNQTPPTYNKTNKFT
CCCCCCCCCCCCCCC		22.0425884760
366 (in isoform 1)Ubiquitination-42.9621890473
366UbiquitinationQTPPTYNKTNKFTYG
CCCCCCCCCCCCCCC		42.9621906983
366 (in isoform 2)Ubiquitination-42.9621890473
369UbiquitinationPTYNKTNKFTYGFQN
CCCCCCCCCCCCCCC		44.2921890473
369 (in isoform 1)Ubiquitination-44.2921890473
369 (in isoform 2)Ubiquitination-44.2921890473
373 (in isoform 3)Ubiquitination-18.01-
376UbiquitinationKFTYGFQNIVDAYGI
CCCCCCCCHHHHHCC		33.7121890473
428PhosphorylationVWMVLRESRILSQKN
HHHHHHHHHHHCCCC		20.4220068231
434UbiquitinationESRILSQKNENEMFS
HHHHHCCCCCCCHHH		63.95-
441PhosphorylationKNENEMFSTVFSGRY
CCCCCHHHHHHCHHH		23.5022210691
445PhosphorylationEMFSTVFSGRYIILL
CHHHHHHCHHHHHHH		20.3022210691
666 (in isoform 2)Ubiquitination-36.4321890473
666 (in isoform 1)Ubiquitination-36.4321890473
666UbiquitinationRRQYLRRKHLGTLNF
HHHHHHHCCCCCEEC		36.4321890473
670PhosphorylationLRRKHLGTLNFGGIR
HHHCCCCCEECCCEE		25.5320860994
673UbiquitinationKHLGTLNFGGIRVGN
CCCCCEECCCEECCC		12.1821890473
673 (in isoform 3)Ubiquitination-12.18-
815PhosphorylationVEFQNKFYSGTGFKF
HHCCCCCCCCCCCCC		14.06-
816PhosphorylationEFQNKFYSGTGFKFL
HCCCCCCCCCCCCCC		32.77-
818PhosphorylationQNKFYSGTGFKFLPF
CCCCCCCCCCCCCCC		33.24-
821UbiquitinationFYSGTGFKFLPFSFE
CCCCCCCCCCCCCHH		47.54-
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 VPP1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPP1_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 VPP1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZNT5_HUMANSLC30A5physical
22939629
CLIC1_HUMANCLIC1physical
21988832
SNX4_HUMANSNX4physical
21988832
ZN267_HUMANZNF267physical
21988832
SEH1_HUMANSEH1Lphysical
21988832
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 VPP1_HUMAN

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Related Literatures of Post-Translational Modification

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