CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022979
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 V-type proton ATPase subunit H 
Protein Synonyms/Alias
 V-ATPase subunit H; Nef-binding protein 1; NBP1; Protein VMA13 homolog; V-ATPase 50/57 kDa subunits; Vacuolar proton pump subunit H; Vacuolar proton pump subunit SFD 
Gene Name
 ATP6V1H 
Gene Synonyms/Alias
 CGI-11 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
22PTNIIAAKAAEVRANubiquitination[1, 2]
176KTQLSSQKLRGSGVAubiquitination[1]
325LENLEQQKYDDEDISubiquitination[1]
341DIKFLLEKLGESVQDubiquitination[1]
360DEYSSELKSGRLEWSubiquitination[1]
374SPVHKSEKFWRENAVubiquitination[2]
386NAVRLNEKNYELLKIubiquitination[2]
396ELLKILTKLLEVSDDubiquitination[1, 3, 4, 5, 6, 7]
469HNWEYLGKQLQSEQPubiquitination[4, 7]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [3] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [6] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 Subunit of the peripheral V1 complex of vacuolar ATPase. Subunit H activates the ATPase activity of the enzyme and couples ATPase activity to proton flow. 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 (By similarity). Involved in the endocytosis mediated by clathrin-coated pits, required for the formation of endosomes. 
Sequence Annotation
 MOD_RES 483 483 Phosphoserine.  
Keyword
 Alternative splicing; Complete proteome; Host-virus interaction; Hydrogen ion transport; Ion transport; Phosphoprotein; Reference proteome; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 483 AA 
Protein Sequence
MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI QRFEMKRSPE 60
EKQEMLQTEG SQCAKTFINL MTHICKEQTV QYILTMVDDM LQENHQRVSI FFDYARCSKN 120
TAWPYFLPML NRQDPFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLSSQKLRGS 180
GVAVETGTVS SSDSSQYVQC VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ 240
YQMIFSIWLL AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE 300
TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS SFDEYSSELK 360
SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV SDDPQVLAVA AHDVGEYVRH 420
YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA 480
ARS 483 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005886; C:plasma membrane; TAS:Reactome.
 GO:0000221; C:vacuolar proton-transporting V-type ATPase, V1 domain; NAS:UniProtKB.
 GO:0030234; F:enzyme regulator activity; NAS:UniProtKB.
 GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro.
 GO:0006200; P:ATP catabolic process; NAS:GOC.
 GO:0015991; P:ATP hydrolysis coupled proton transport; NAS:UniProtKB.
 GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
 GO:0006897; P:endocytosis; IDA:UniProtKB.
 GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
 GO:0051701; P:interaction with host; TAS:Reactome.
 GO:0090382; P:phagosome maturation; TAS:Reactome.
 GO:0050690; P:regulation of defense response to virus by virus; TAS:Reactome.
 GO:0033572; P:transferrin transport; TAS:Reactome.
 GO:0007035; P:vacuolar acidification; NAS:UniProtKB.
 GO:0016032; P:viral reproduction; TAS:Reactome.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR004908; ATPase_V1-cplx_hsu.
 IPR011987; ATPase_V1-cplx_hsu_C. 
Pfam
 PF11698; V-ATPase_H_C
 PF03224; V-ATPase_H_N 
SMART
  
PROSITE
  
PRINTS