P21281 (VATB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
V-type proton ATPase subunit B, brain isoform
Short name=V-ATPase subunit B 2

Alternative name(s):
Endomembrane proton pump 58 kDa subunit
HO57
Vacuolar proton pump subunit B 2

Gene names

Name:	ATP6V1B2
Synonyms:	ATP6B2, VPP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
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.
Subunit structure	V-ATPase is a 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	Endomembrane system; Peripheral membrane protein. Melanosome. Note: Endomembrane. Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.8 Ref.9
Sequence similarities	Belongs to the ATPase alpha/beta chains family.

Ontologies

Keywords
Biological process	Hydrogen ion transport Ion transport Transport
Cellular component	Membrane
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	ATP hydrolysis coupled proton transport Inferred from electronic annotation. Source: InterPro cellular iron ion homeostasis Traceable author statement. Source: Reactome insulin receptor signaling pathway Traceable author statement. Source: Reactome interaction with host Traceable author statement. Source: Reactome phagosome maturation Traceable author statement. Source: Reactome transferrin transport Traceable author statement. Source: Reactome
Cellular_component	Golgi apparatus Inferred from direct assay. Source: HPA cytosol Inferred from sequence or structural similarity. Source: UniProtKB endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: Compara melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell microvillus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from sequence or structural similarity. Source: UniProtKB proton-transporting V-type ATPase, V1 domain Inferred from electronic annotation. Source: InterPro
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro proton-transporting ATPase activity, rotational mechanism Traceable author statement Ref.7. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 511	511	V-type proton ATPase subunit B, brain isoform		PRO_0000144626
Amino acid modifications
	Modified residue	404	1	Phosphoserine By similarity
	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.5
	Sequence conflict	171	1	Q → R in AAH30640. Ref.5
	Sequence conflict	342	1	E → G in AAH30640. Ref.5
	Sequence conflict	376	1	Q → L in AAA58661. Ref.2
	Sequence conflict	424 – 425	2	AC → RA in AAA35610. Ref.7
	Sequence conflict	435	1	M → V in AAA35610. Ref.7
	Sequence conflict	510 – 511	2	KH → ND in AAA35610. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P21281 [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Amygdala.
[4]	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 (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain and Eye.
[6]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
[7]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 106-511. Tissue: Brain.
[8]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[9]	"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] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. Tissue: Melanoma.
[10]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M60346 mRNA. Translation: AAA35610.1. L35249 mRNA. Translation: AAA58661.1. AK312372 mRNA. Translation: BAG35290.1. CH471080 Genomic DNA. Translation: EAW63758.1. CH471080 Genomic DNA. Translation: EAW63759.1. 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.
IPI	IPI00007812.
PIR	B44138. I39208.
RefSeq	NP_001684.2. NM_001693.3.
UniGene	Hs.295917.
3D structure databases
ProteinModelPortal	P21281.
ModBase	Search...
Protein-protein interaction databases
IntAct	P21281. 3 interactions.
MINT	MINT-5004128.
STRING	9606.ENSP00000276390.
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	P21281.
Polymorphism databases
DMDM	12643271.
2D gel databases
REPRODUCTION-2DPAGE	IPI00007812.
Proteomic databases
PaxDb	P21281.
PeptideAtlas	P21281.
PRIDE	P21281.
Protocols and materials databases
DNASU	526.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000276390; ENSP00000276390; ENSG00000147416.
GeneID	526.
KEGG	hsa:526.
UCSC	uc003wzp.3. human.
Organism-specific databases
CTD	526.
GeneCards	GC08P020054.
HGNC	HGNC:854. ATP6V1B2.
HPA	HPA008147.
MIM	606939. gene.
neXtProt	NX_P21281.
PharmGKB	PA25155.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1156.
HOGENOM	HOG000165320.
HOVERGEN	HBG002176.
InParanoid	P21281.
KO	K02147.
OMA	LMKEGIG.
OrthoDB	EOG4HMJ93.
PhylomeDB	P21281.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
ArrayExpress	P21281.
Bgee	P21281.
CleanEx	HS_ATP6V1B2.
Genevestigator	P21281.
GermOnline	ENSG00000147416. Homo sapiens.
Family and domain databases
InterPro	IPR020003. ATPase_a/bsu_AS. IPR004100. ATPase_a/bsu_N. IPR000793. ATPase_F1/V1/A1-cplx_a/bsu_C. IPR000194. ATPase_F1/V1/A1_a/bsu_nucl-bd. IPR005723. ATPase_V1-cplx_bsu. IPR022879. V-ATPase_su_B/beta. [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]
ProtoNet	Search...
Other
BindingDB	P21281.
ChEMBL	CHEMBL5641.
GenomeRNAi	526.
NextBio	2183.
SOURCE	Search...

Entry information

Entry name

VATB2_HUMAN

Accession

Primary (citable) accession number: P21281
Secondary accession number(s): B2R5Z3 , D3DSQ5, Q14544, Q15859, Q96IR0

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	December 1, 2000
Last modified:	May 1, 2013
This is version 140 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.