Reviewed, UniProtKB/Swiss-Prot P21281 (VATB2_HUMAN)

Names and origin

Protein names

Recommended name:
    Vacuolar ATP synthase subunit B, brain isoform
    EC=3.6.3.14
Alternative name(s):
    V-ATPase subunit B 2
    Vacuolar proton pump subunit B 2
    Endomembrane proton pump 58 kDa subunit
    HO57

Gene names

Name:	ATP6V1B2
Synonyms:	ATP6B2, VPP3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Non-catalytic subunit of the peripheral V1 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Catalytic activity	ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
Subunit structure	V-ATPase is an heteromultimeric enzyme composed of a peripheral catalytic V1 complex (main components: subunits A, B, C, D, E, and F) attached to an integral membrane V0 proton pore complex (main component: the proteolipid protein).
Subcellular location	Intracytoplasmic membrane; Peripheral membrane protein. Melanosome. Note= Endomembrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV.
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	ATP synthesis Hydrogen ion transport Ion transport Transport
Cellular component	Membrane
Molecular function	Hydrolase
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	proton transport Ref.5 Traceable author statement. Source: ProtInc
Molecular function	hydrogen ion transporting ATPase activity, rotational mechanism Ref.5 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view
Molecule processing
	Chain	1 – 511	511	Vacuolar ATP synthase subunit B, brain isoform
Amino acid modifications
	Modified residue	498	1	Phosphoserine By similarity
Experimental info
	Sequence conflict	28	1	A → S in CAA44721. Ref.1
	Sequence conflict	29	1	R → Q in AAH30640. Ref.3
	Sequence conflict	171	1	Q → R in AAH30640. Ref.3
	Sequence conflict	342	1	E → G in AAH30640. Ref.3
	Sequence conflict	376	1	Q → L in AAA58661. Ref.2
	Sequence conflict	424 – 425	2	AC → RA in AAA35610. Ref.5
	Sequence conflict	435	1	M → V in AAA35610. Ref.5
	Sequence conflict	510 – 511	2	KH → ND in AAA35610. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	P21281-1 [UniParc]. Last modified December 1, 2000. Version 3. Checksum: E01E85BBA36E5DED	FASTA	511	56,501
	10 20 30 40 50 60 MALRAMRGIV NGAAPELPVP TGGPAVGARE QALAVSRNYL SQPRLTYKTV SGVNGPLVIL 70 80 90 100 110 120 DHVKFPRYAE IVHLTLPDGT KRSGQVLEVS GSKAVVQVFE GTSGIDAKKT SCEFTGDILR 130 140 150 160 170 180 TPVSEDMLGR VFNGSGKPID RGPVVLAEDF LDIMGQPINP QCRIYPEEMI QTGISAIDGM 190 200 210 220 230 240 NSIARGQKIP IFSAAGLPHN EIAAQICRQA GLVKKSKDVV DYSEENFAIV FAAMGVNMET 250 260 270 280 290 300 ARFFKSDFEE NGSMDNVCLF LNLANDPTIE RIITPRLALT TAEFLAYQCE KHVLVILTDM 310 320 330 340 350 360 SSYAEALREV SAAREEVPGR RGFPGYMYTD LATIYERAGR VEGRNGSITQ IPILTMPNDD 370 380 390 400 410 420 ITHPIPDLTG YITEGQIYVD RQLHNRQIYP PINVLPSLSR LMKSAIGEGM TRKDHADVSN 430 440 450 460 470 480 QLYACYAIGK DVQAMKAVVG EEALTSDDLL YLEFLQKFER NFIAQGPYEN RTVFETLDIG 490 500 510 WQLLRIFPKE MLKRIPQSTL SEFYPRDSAK H

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells." Nelson R.D., Guo X.-L., Masood K., Brown D., Kalkbrenner M., Gluck S. Proc. Natl. Acad. Sci. U.S.A. 89:3541-3545(1992) [PubMed: 1373501] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Heterogeneity of vacuolar H(+)-ATPase: differential expression of two human subunit B isoforms." van Hille B., Richener H., Schmid P., Puettner I., Green J.R., Bilbe G. Biochem. J. 303:191-198(1994) [PubMed: 7945239] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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]. Tissue: Brain and Eye.
[4]	"Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit gene in differentiating THP-1 cells." Lee B.S., Underhill D.M., Crane M.K., Gluck S.L. J. Biol. Chem. 270:7320-7329(1995) [PubMed: 7706273] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
[5]	"An mRNA from human brain encodes an isoform of the B subunit of the vacuolar H(+)-ATPase." Bernasconi P., Rausch T., Struve I., Morgan L., Taiz L. J. Biol. Chem. 265:17428-17431(1990) [PubMed: 2145275] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-511. Tissue: Brain.
[6]	"Proteomic analysis of early melanosomes: identification of novel melanosomal proteins." Basrur V., Yang F., Kushimoto T., Higashimoto Y., Yasumoto K., Valencia J., Muller J., Vieira W.D., Watabe H., Shabanowitz J., Hearing V.J., Hunt D.F., Appella E. J. Proteome Res. 2:69-79(2003) [PubMed: 12643545] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60346 mRNA. Translation: AAA35610.1. L35249 mRNA. Translation: AAA58661.1. BC003100 mRNA. Translation: AAH03100.1. BC007309 mRNA. Translation: AAH07309.1. BC030640 mRNA. Translation: AAH30640.1. Z37165 Genomic DNA. Translation: CAA85522.1. X62949 mRNA. Translation: CAA44721.1.
PIR	B44138. I39208.
RefSeq	NP_001684.2.
UniGene	Hs.295917
3D structure databases
ModBase	Search...
PTM databases
PhosphoSite	P21281.
2-D gel databases
REPRODUCTION-2DPAGE	IPI00007812.
Proteomic databases
PeptideAtlas	P21281.
Genome annotation databases
Ensembl	ENSG00000147416. Homo sapiens. [Contig view]
GeneID	526.
KEGG	hsa:526.
Organism-specific databases
H-InvDB	HIX0007352. HIX0068099.
HGNC	HGNC:854. ATP6V1B2.
MIM	606939. gene.
PharmGKB	PA25155.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	P21281.
HOVERGEN	P21281.
Gene expression databases
ArrayExpress	P21281.
CleanEx	HS_ATP6V1B2.
GermOnline	ENSG00000147416. Homo sapiens.
Family and domain databases
InterPro	IPR000793. ATPase_a_b_C. IPR004100. ATPase_a_b_N. IPR000194. ATPase_a_b_nl_bd. IPR005723. ATPase_V1_B. [Graphical view]
Pfam	PF00006. ATP-synt_ab. 1 hit. PF00306. ATP-synt_ab_C. 1 hit. PF02874. ATP-synt_ab_N. 1 hit. [Graphical view]
TIGRFAMs	TIGR01040. V-ATPase_V1_B. 1 hit.
PROSITE	PS00152. ATPASE_ALPHA_BETA. 1 hit. [Graphical view]
ProDom	P21281. [Graphical view] [Entries sharing at least one domain]
BLOCKS	Search...
Other Resources
LinkHub	P21281.
SOURCE	Search...
ProtoNet	Search...

Entry information

Entry name

VATB2_HUMAN

Accession

Primary (citable) accession number: P21281
Secondary accession number(s): Q14544, Q15859, Q96IR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	December 1, 2000
Last modified:	July 22, 2008
This is version 86 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)