VPP2_HUMAN - dbPTM
VPP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VPP2_HUMAN
UniProt AC Q9Y487
Protein Name V-type proton ATPase 116 kDa subunit a isoform 2
Gene Name ATP6V0A2
Organism Homo sapiens (Human).
Sequence Length 856
Subcellular Localization Cell membrane
Multi-pass membrane protein. Endosome membrane. In kidney proximal tubules, also detected in subapical vesicles..
Protein Description Part of the proton channel of V-ATPases. Essential component of the endosomal pH-sensing machinery. May play a role in maintaining the Golgi functions, such as glycosylation maturation, by controlling the Golgi pH. 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 MGSLFRSETMCLAQLFLQSGTAYECLSALGEKGLVQFRDLNQNVSSFQRKFVGEVKRCEELERILVYLVQEINRADIPLPEGEASPPAPPLKQVLEMQEQLQKLEVELREVTKNKEKLRKNLLELIEYTHMLRVTKTFVKRNVEFEPTYEEFPSLESDSLLDYSCMQRLGAKLGFVSGLINQGKVEAFEKMLWRVCKGYTIVSYAELDESLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHVYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVYSRVIQVKKMKAIYHMLNMCSFDVTNKCLIAEVWCPEADLQDLRRALEEGSRESGATIPSFMNIIPTKETPPTRIRTNKFTEGFQNIVDAYGVGSYREVNPALFTIITFPFLFAVMFGDFGHGFVMFLFALLLVLNENHPRLNQSQEIMRMFFNGRYILLLMGLFSVYTGLIYNDCFSKSVNLFGSGWNVSAMYSSSHPPAEHKKMVLWNDSVVRHNSILQLDPSIPGVFRGPYPLGIDPIWNLATNRLTFLNSFKMKMSVILGIIHMTFGVILGIFNHLHFRKKFNIYLVSIPELLFMLCIFGYLIFMIFYKWLVFSAETSRVAPSILIEFINMFLFPASKTSGLYTGQEYVQRVLLVVTALSVPVLFLGKPLFLLWLHNGRSCFGVNRSGYTLIRKDSEEEVSLLGSQDIEEGNHQVEDGCREMACEEFNFGEILMTQVIHSIEYCLGCISNTASYLRLWALSLAHAQLSDVLWAMLMRVGLRVDTTYGVLLLLPVIALFAVLTIFILLIMEGLSAFLHAIRLHWVEFQNKFYVGAGTKFVPFSFSLLSSKFNNDDSVA
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
92UbiquitinationSPPAPPLKQVLEMQE
CCCCCCHHHHHHHHH		44.1021963094
103UbiquitinationEMQEQLQKLEVELRE
HHHHHHHHHHHHHHH		56.0332015554
115AcetylationLREVTKNKEKLRKNL
HHHHHCCHHHHHHHH		58.757708601
115UbiquitinationLREVTKNKEKLRKNL
HHHHHCCHHHHHHHH		58.7524816145
128PhosphorylationNLLELIEYTHMLRVT
HHHHHHHHHHHHHHH		8.5821406692
129PhosphorylationLLELIEYTHMLRVTK
HHHHHHHHHHHHHHH		6.5021406692
135PhosphorylationYTHMLRVTKTFVKRN
HHHHHHHHHHHHHCC		20.2421406692
136UbiquitinationTHMLRVTKTFVKRNV
HHHHHHHHHHHHCCC		36.7933845483
148PhosphorylationRNVEFEPTYEEFPSL
CCCCCCCCHHHCCCC		36.0525841592
149PhosphorylationNVEFEPTYEEFPSLE
CCCCCCCHHHCCCCC		24.9522817900
154PhosphorylationPTYEEFPSLESDSLL
CCHHHCCCCCCCCHH		50.5222199227
157PhosphorylationEEFPSLESDSLLDYS
HHCCCCCCCCHHCHH		37.4822199227
159PhosphorylationFPSLESDSLLDYSCM
CCCCCCCCHHCHHHH		39.8622199227
163PhosphorylationESDSLLDYSCMQRLG
CCCCHHCHHHHHHHH		12.0722817900
172UbiquitinationCMQRLGAKLGFVSGL
HHHHHHCHHHHHHHH		47.5523000965
177PhosphorylationGAKLGFVSGLINQGK
HCHHHHHHHHCCCCH		26.1422817900
223PhosphorylationTGEVIKWYVFLISFW
CHHHHHHHHHHHHHH		4.02-
279UbiquitinationDLYTVLHKTEDYLRQ
HHHHHHHHCHHHHHH		49.8221963094
279AcetylationDLYTVLHKTEDYLRQ
HHHHHHHHCHHHHHH		49.8219608861
290UbiquitinationYLRQVLCKAAESVYS
HHHHHHHHHHHHHHH		46.6133845483
320PhosphorylationNMCSFDVTNKCLIAE
HHCCCCCCCCEEEEE		30.7029759185
349PhosphorylationLEEGSRESGATIPSF
HHHCCCCCCCCCCCH		32.3918452278
352PhosphorylationGSRESGATIPSFMNI
CCCCCCCCCCCHHHC		36.6318452278
355PhosphorylationESGATIPSFMNIIPT
CCCCCCCCHHHCCCC		33.0218452278
363UbiquitinationFMNIIPTKETPPTRI
HHHCCCCCCCCCCCC		54.9922817900
374UbiquitinationPTRIRTNKFTEGFQN
CCCCCCCCCCHHHHH		53.7221890473
484N-linked_GlycosylationNLFGSGWNVSAMYSS
EECCCCCCHHHHHCC		22.76UniProtKB CARBOHYD
490PhosphorylationWNVSAMYSSSHPPAE
CCHHHHHCCCCCCHH		16.57-
491PhosphorylationNVSAMYSSSHPPAEH
CHHHHHCCCCCCHHH		18.38-
492PhosphorylationVSAMYSSSHPPAEHK
HHHHHCCCCCCHHHC		33.79-
505N-linked_GlycosylationHKKMVLWNDSVVRHN
HCCEEEECCHHHCCC		27.76UniProtKB CARBOHYD
507PhosphorylationKMVLWNDSVVRHNSI
CEEEECCHHHCCCHH		21.21-
529PhosphorylationPGVFRGPYPLGIDPI
CCCCCCCCCCCCCCH		17.5722210691
541PhosphorylationDPIWNLATNRLTFLN
CCHHHHHCCCHHHHH		24.8422210691
549PhosphorylationNRLTFLNSFKMKMSV
CCHHHHHHHHHHHHH		28.5222210691
680S-palmitoylationWLHNGRSCFGVNRSG
EECCCCCCCCCCCCC		3.1129575903
686PhosphorylationSCFGVNRSGYTLIRK
CCCCCCCCCCEEEEC		30.8328152594
688PhosphorylationFGVNRSGYTLIRKDS
CCCCCCCCEEEECCC		10.3028152594
689PhosphorylationGVNRSGYTLIRKDSE
CCCCCCCEEEECCCH		21.1628152594
693UbiquitinationSGYTLIRKDSEEEVS
CCCEEEECCCHHHHH		59.62-
695PhosphorylationYTLIRKDSEEEVSLL
CEEEECCCHHHHHHH		50.3629255136
700PhosphorylationKDSEEEVSLLGSQDI
CCCHHHHHHHCCCCC		22.5830266825
704PhosphorylationEEVSLLGSQDIEEGN
HHHHHHCCCCCCCCC		25.3417525332
841PhosphorylationGTKFVPFSFSLLSSK
CCCCEEEEHHHHHHH		14.0930622161
843PhosphorylationKFVPFSFSLLSSKFN
CCEEEEHHHHHHHCC		27.4830622161
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 VPP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VPP2_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 VPP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LAMP2_HUMANLAMP2physical
27244671
VA0D2_HUMANATP6V0D2physical
28514442
K2013_HUMANKIAA2013physical
28514442
TMCC3_HUMANTMCC3physical
28514442
CLCN6_HUMANCLCN6physical
28514442
SPRY7_HUMANSPRYD7physical
28514442
CC115_HUMANCCDC115physical
28514442
VATC1_HUMANATP6V1C1physical
28514442
VATD_HUMANATP6V1Dphysical
28514442
VMA21_HUMANVMA21physical
28514442
VPP1_HUMANATP6V0A1physical
28514442
VATE1_HUMANATP6V1E1physical
28514442
VAS1_HUMANATP6AP1physical
28514442
ANKL2_HUMANANKLE2physical
28514442
VATB2_HUMANATP6V1B2physical
28514442
CSCL2_HUMANTMEM63Bphysical
28514442
PMGT1_HUMANPOMGNT1physical
28514442
VATF_HUMANATP6V1Fphysical
28514442
ANXA6_HUMANANXA6physical
28514442
AT11C_HUMANATP11Cphysical
28514442
B4GT3_HUMANB4GALT3physical
28514442
PPAL_HUMANACP2physical
28514442
AT5F1_HUMANATP5F1physical
28514442
TYW1_HUMANTYW1physical
28514442
Drug and Disease Associations
Kegg Disease
H00557 Cutis laxa, including: Autosomal dominant cutis laxa (ADCL); Autosomal recessive cutis laxa I (ARCL1
OMIM Disease
219200Cutis laxa, autosomal recessive, 2A (ARCL2A)
278250Wrinkly skin syndrome (WSS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VPP2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-279, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-700 ANDSER-704, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695 AND SER-704, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-177 AND SER-695, ANDMASS SPECTROMETRY.

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