Reviewed, UniProtKB/Swiss-Prot Q9UI12 (VATH_HUMAN)

Names and origin

Protein names

Recommended name:
    V-type proton ATPase subunit H
      Short name=V-ATPase subunit H
Alternative name(s):
    Vacuolar proton pump subunit H
    V-ATPase 50/57 kDa subunits
    Vacuolar proton pump subunit SFD
    VMA13
    Nef-binding protein 1
      Short name=NBP1

Gene names

Name:	ATP6V1H
ORF Names:	CGI-11

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	483 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subunit structure	V-ATPase is an heteromultimeric enzyme composed of a peripheral catalytic V1 complex (components A to H) attached to an integral membrane V0 proton pore complex (components: a, c, c', c'' and d). Interacts with HIV-1 Nef protein and AP2M1. Ref.2 Ref.8
Tissue specificity	Widely expressed. Ref.2
Sequence similarities	Belongs to the V-ATPase H subunit family.

Ontologies

Keywords
Biological process	Host-virus interaction Hydrogen ion transport Ion transport Transport
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	ATP hydrolysis coupled proton transport Non-traceable author statement. Source: UniProtKB ATP synthesis coupled proton transport Inferred from electronic annotation. Source: InterPro endocytosis Ref.8 Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of defense response to virus by virus Inferred from Experiment. Source: Reactome vacuolar acidification Non-traceable author statement. Source: UniProtKB
Cellular component	cytosol Inferred from Experiment. Source: Reactome plasma membrane Inferred from Experiment. Source: Reactome vacuolar proton-transporting V-type ATPase, V1 domain Non-traceable author statement. Source: UniProtKB
Molecular function	enzyme regulator activity Non-traceable author statement. Source: UniProtKB protein binding Ref.2 Ref.8 Inferred from physical interaction. Source: UniProtKB proton-transporting ATPase activity, rotational mechanism Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UI12-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q9UI12-2)

The sequence of this isoform differs from the canonical sequence as follows:
     176-193: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 483	483	V-type proton ATPase subunit H		PRO_0000124193
Amino acid modifications
	Modified residue	483	1	Phosphoserine Ref.9
Natural variations
	Alternative sequence	176 – 193	18	Missing in isoform 2.		VSP_012274
Experimental info
	Sequence conflict	129	1	M → I in AAD27720. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: EAE0457C538AC906	FASTA	483	55,883
	10 20 30 40 50 60 MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI QRFEMKRSPE 70 80 90 100 110 120 EKQEMLQTEG SQCAKTFINL MTHICKEQTV QYILTMVDDM LQENHQRVSI FFDYARCSKN 130 140 150 160 170 180 TAWPYFLPML NRQDPFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLSSQKLRGS 190 200 210 220 230 240 GVAVETGTVS SSDSSQYVQC VAGCLQLMLR VNEYRFAWVE ADGVNCIMGV LSNKCGFQLQ 250 260 270 280 290 300 YQMIFSIWLL AFSPQMCEHL RRYNIIPVLS DILQESVKEK VTRIILAAFR NFLEKSTERE 310 320 330 340 350 360 TRQEYALAMI QCKVLKQLEN LEQQKYDDED ISEDIKFLLE KLGESVQDLS SFDEYSSELK 370 380 390 400 410 420 SGRLEWSPVH KSEKFWRENA VRLNEKNYEL LKILTKLLEV SDDPQVLAVA AHDVGEYVRH 430 440 450 460 470 480 YPRGKRVIEQ LGGKQLVMNH MHHEDQQVRY NALLAVQKLM VHNWEYLGKQ LQSEQPQTAA ARS
	Isoform 2. Checksum: 710D9FAE82982B7A	FASTA	465	54,151
	10 20 30 40 50 60 MTKMDIRGAV DAAVPTNIIA AKAAEVRANK VNWQSYLQGQ MISAEDCEFI QRFEMKRSPE 70 80 90 100 110 120 EKQEMLQTEG SQCAKTFINL MTHICKEQTV QYILTMVDDM LQENHQRVSI FFDYARCSKN 130 140 150 160 170 180 TAWPYFLPML NRQDPFTVHM AARIIAKLAA WGKELMEGSD LNYYFNWIKT QLSSQSSQYV 190 200 210 220 230 240 QCVAGCLQLM LRVNEYRFAW VEADGVNCIM GVLSNKCGFQ LQYQMIFSIW LLAFSPQMCE 250 260 270 280 290 300 HLRRYNIIPV LSDILQESVK EKVTRIILAA FRNFLEKSTE RETRQEYALA MIQCKVLKQL 310 320 330 340 350 360 ENLEQQKYDD EDISEDIKFL LEKLGESVQD LSSFDEYSSE LKSGRLEWSP VHKSEKFWRE 370 380 390 400 410 420 NAVRLNEKNY ELLKILTKLL EVSDDPQVLA VAAHDVGEYV RHYPRGKRVI EQLGGKQLVM 430 440 450 460 NHMHHEDQQV RYNALLAVQK LMVHNWEYLG KQLQSEQPQT AAARS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y., Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y., Liu L.S., Ding J.F. , Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C., Zhao M.S., Hui R.T. Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Heart.
[2]	"Interactions between HIV1 Nef and vacuolar ATPase facilitate the internalization of CD4." Lu X., Yu H., Liu S.-H., Brodsky F.M., Peterlin B.M. Immunity 8:647-656(1998) [PubMed: 9620685] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH HIV-1 NEF. Tissue: B-cell.
[3]	"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning." Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L. Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed: 10931946] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Hypothalamus.
[4]	"Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics." Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C. Genome Res. 10:703-713(2000) [PubMed: 10810093] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Mammary gland.
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Eye and Lymphoma.
[8]	"Subunit H of the V-ATPase binds to the medium chain of adaptor protein complex 2 and connects Nef to the endocytic machinery." Geyer M., Yu H., Mandic R., Linnemann T., Zheng Y.-H., Fackler O.T., Peterlin B.M. J. Biol. Chem. 277:28521-28529(2002) [PubMed: 12032142] [Abstract] Cited for: INTERACTION WITH HIV-1 NEF AND AP2M1.
[9]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-483, MASS SPECTROMETRY.
[10]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF113222 mRNA. Translation: AAG39293.1. AF298777 mRNA. Translation: AAG22809.1. AF112204 mRNA. Translation: AAF17192.1. AF132945 mRNA. Translation: AAD27720.1. AK022345 mRNA. Translation: BAG51072.1. CH471068 Genomic DNA. Translation: EAW86727.1. BC025275 mRNA. Translation: AAH25275.1.
IPI	IPI00296191. IPI00414079.
RefSeq	NP_057025.2. NP_998784.1. NP_998785.1.
UniGene	Hs.491737
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UI12. 4 interactions.
STRING	Q9UI12.
Protein family/group databases
TCDB	3.A.2.2.4. H+- or Na+-translocating F-type, V-type and A-type ATPase (F-ATPase) superfamily.
PTM databases
PhosphoSite	Q9UI12.
Proteomic databases
PRIDE	Q9UI12.
Genome annotation databases
Ensembl	ENST00000359530; ENSP00000352522; ENSG00000047249; Homo sapiens. [Genome view] ENST00000396774; ENSP00000379995; ENSG00000047249; Homo sapiens. [Genome view]
GeneID	51606.
KEGG	hsa:51606.
UCSC	uc003xrk.1. human. uc003xrn.1. human.
Organism-specific databases
CTD	51606.
GeneCards	GC08M054790.
H-InvDB	HIX0020582.
HGNC	HGNC:18303. ATP6V1H.
HPA	CAB009532. HPA023421.
MIM	608861. gene.
PharmGKB	PA38521.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	HBG387727.
HOVERGEN	Q9UI12.
InParanoid	Q9UI12.
OMA	QGQMISG.
OrthoDB	EOG9J6VB7.
Enzyme and pathway databases
BRENDA	3.6.3.14. 247.
Reactome	REACT_6185. HIV Infection.
Gene expression databases
ArrayExpress	Q9UI12.
Bgee	Q9UI12.
CleanEx	HS_ATP6V1H.
Genevestigator	Q9UI12.
GermOnline	ENSG00000047249. Homo sapiens.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR004908. ATPase_V1-cplx_hsu. IPR011987. ATPase_V1-cplx_hsu_C. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 1 hit. G3DSA:1.25.40.150. ATPase_V1_H_C. 1 hit.
PANTHER	PTHR10698. ATPase_V1_H. 1 hit.
Pfam	PF03224. V-ATPase_H. 1 hit. [Graphical view]
PIRSF	PIRSF032184. ATPase_V1_H. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	55498.
SOURCE	Search...

Entry information

Entry name

VATH_HUMAN

Accession

Primary (citable) accession number: Q9UI12
Secondary accession number(s): B3KMR0 , Q6PK44, Q9H3E3, Q9Y300

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 2000
Last modified:	December 15, 2009
This is version 89 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.