VAS1_HUMAN - dbPTM
VAS1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VAS1_HUMAN
UniProt AC Q15904
Protein Name V-type proton ATPase subunit S1
Gene Name ATP6AP1
Organism Homo sapiens (Human).
Sequence Length 470
Subcellular Localization Endoplasmic reticulum membrane
Single-pass membrane protein . Endoplasmic reticulum-Golgi intermediate compartment membrane . Not detected in trans-Golgi network.
Protein Description Accessory subunit of the proton-transporting vacuolar (V)-ATPase protein pump, which is required for luminal acidification of secretory vesicles. Guides the V-type ATPase into specialized subcellular compartments, such as neuroendocrine regulated secretory vesicles or the ruffled border of the osteoclast, thereby regulating its activity. Involved in membrane trafficking and Ca(2+)-dependent membrane fusion. May play a role in the assembly of the V-type ATPase complex. 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 MMAAMATARVRMGPRCAQALWRMPWLPVFLSLAAAAAAAAAEQQVPLVLWSSDRDLWAPAADTHEGHITSDLQLSTYLDPALELGPRNVLLFLQDKLSIEDFTAYGGVFGNKQDSAFSNLENALDLAPSSLVLPAVDWYAVSTLTTYLQEKLGASPLHVDLATLRELKLNASLPALLLIRLPYTASSGLMAPREVLTGNDEVIGQVLSTLKSEDVPYTAALTAVRPSRVARDVAVVAGGLGRQLLQKQPVSPVIHPPVSYNDTAPRILFWAQNFSVAYKDQWEDLTPLTFGVQELNLTGSFWNDSFARLSLTYERLFGTTVTFKFILANRLYPVSARHWFTMERLEVHSNGSVAYFNASQVTGPSIYSFHCEYVSSLSKKGSLLVARTQPSPWQMMLQDFQIQAFNVMGEQFSYASDCASFFSPGIWMGLLTSLFMLFIFTYGLHMILSLKTMDRFDDHKGPTISLTQIV
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
7Phosphorylation-MMAAMATARVRMGP
-CCCHHHCCHHHCCH		11.2522817900
75O-linked_GlycosylationITSDLQLSTYLDPAL
CCCCEEHHHCCCHHH		11.31OGP
76O-linked_GlycosylationTSDLQLSTYLDPALE
CCCEEHHHCCCHHHH		36.37OGP
103PhosphorylationKLSIEDFTAYGGVFG
CCCHHHHHHCCCCCC		31.1520068231
168UbiquitinationLATLRELKLNASLPA
HHHHHHHHCCCCCCE		34.64-
170N-linked_GlycosylationTLRELKLNASLPALL
HHHHHHCCCCCCEEE		26.37UniProtKB CARBOHYD
184O-linked_GlycosylationLLIRLPYTASSGLMA
EHHCCCCCCCCCCCC		20.3755834495
208PhosphorylationEVIGQVLSTLKSEDV
HHHHHHHHHCCCCCC		32.6023532336
209PhosphorylationVIGQVLSTLKSEDVP
HHHHHHHHCCCCCCC		33.7623532336
211UbiquitinationGQVLSTLKSEDVPYT
HHHHHHCCCCCCCCC		52.4621906983
218O-linked_GlycosylationKSEDVPYTAALTAVR
CCCCCCCCEEEEECC		10.21OGP
218PhosphorylationKSEDVPYTAALTAVR
CCCCCCCCEEEEECC		10.21-
227O-linked_GlycosylationALTAVRPSRVARDVA
EEEECCHHHHHHHHH		28.90OGP
261N-linked_GlycosylationIHPPVSYNDTAPRIL
CCCCCCCCCCCCCEE		32.4219159218
273N-linked_GlycosylationRILFWAQNFSVAYKD
CEEEEECCEEEEEHH		24.3419159218
296N-linked_GlycosylationTFGVQELNLTGSFWN
EEEEEEEEECCCCCC		34.50UniProtKB CARBOHYD
303N-linked_GlycosylationNLTGSFWNDSFARLS
EECCCCCCCCHHHHH		32.79UniProtKB CARBOHYD
312PhosphorylationSFARLSLTYERLFGT
CHHHHHEEHHHHHCC		21.6925690035
313PhosphorylationFARLSLTYERLFGTT
HHHHHEEHHHHHCCE		12.3525690035
319PhosphorylationTYERLFGTTVTFKFI
EHHHHHCCEEEEEHH		15.6820886841
320PhosphorylationYERLFGTTVTFKFIL
HHHHHCCEEEEEHHH		20.2320886841
322PhosphorylationRLFGTTVTFKFILAN
HHHCCEEEEEHHHHC		21.0020068231
330MethylationFKFILANRLYPVSAR
EEHHHHCCCCCCCHH		29.96-
332PhosphorylationFILANRLYPVSARHW
HHHHCCCCCCCHHHE		9.8025307156
335PhosphorylationANRLYPVSARHWFTM
HCCCCCCCHHHEEEE		18.3224719451
350N-linked_GlycosylationERLEVHSNGSVAYFN
EEEEEECCCCEEEEE		31.70UniProtKB CARBOHYD
357N-linked_GlycosylationNGSVAYFNASQVTGP
CCCEEEEEHHHCCCC		26.46UniProtKB CARBOHYD
380UbiquitinationYVSSLSKKGSLLVAR
HHHHHCCCCCEEEEE		50.812190698
382PhosphorylationSSLSKKGSLLVARTQ
HHHCCCCCEEEEECC		27.6624076635
449PhosphorylationYGLHMILSLKTMDRF
HHHHHHHHHHCCCCC		19.5224719451
4602-HydroxyisobutyrylationMDRFDDHKGPTISLT
CCCCCCCCCCEEEEE		73.84-
460UbiquitinationMDRFDDHKGPTISLT
CCCCCCCCCCEEEEE		73.84-
463PhosphorylationFDDHKGPTISLTQIV
CCCCCCCEEEEEECC		31.6930266825
465PhosphorylationDHKGPTISLTQIV--
CCCCCEEEEEECC--		28.0430266825
467PhosphorylationKGPTISLTQIV----
CCCEEEEEECC----		14.9530266825
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 VAS1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VAS1_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 VAS1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ANGI_HUMANANGphysical
16169070
HBA_HUMANHBA1physical
16169070
VATC1_HUMANATP6V1C1physical
22939629
NR1I2_HUMANNR1I2physical
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 VAS1_HUMAN

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-261 AND ASN-273, AND MASSSPECTROMETRY.

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