P51164 (ATP4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Potassium-transporting ATPase subunit beta

Alternative name(s):
Gastric H(+)/K(+) ATPase subunit beta
Proton pump beta chain

Gene names

Name:

ATP4B

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	291 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Required for stabilization and maturation of the catalytic proton pump alpha subunit and may also involved in cell adhesion and establishing epithelial cell polarity. Ref.6
Subunit structure	Composed of two subunits: alpha (catalytic) and beta.
Subcellular location	Cell membrane; Single-pass type II membrane protein.
Domain	The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties. Ref.6
Sequence similarities	Belongs to the X(+)/potassium ATPases subunit beta family.

Ontologies

Keywords
Biological process	Cell adhesion Hydrogen ion transport Ion transport Potassium transport Transport
Cellular component	Cell membrane Membrane
Domain	Signal-anchor Transmembrane Transmembrane helix
Ligand	Potassium
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW response to lipopolysaccharide Inferred from electronic annotation. Source: Compara response to organic nitrogen Inferred from electronic annotation. Source: Compara sodium ion transport Inferred from electronic annotation. Source: InterPro
Cellular_component	plasma membrane Traceable author statement. Source: Reactome sodium:potassium-exchanging ATPase complex Inferred from electronic annotation. Source: InterPro
Molecular_function	hydrogen:potassium-exchanging ATPase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 291	291	Potassium-transporting ATPase subunit beta		PRO_0000219091
Regions
	Topological domain	1 – 36	36	Cytoplasmic Potential
	Transmembrane	37 – 57	21	Helical; Signal-anchor for type II membrane protein; Potential
	Topological domain	58 – 291	234	Extracellular Potential
	Region	194 – 291	98	immunoglobulin-like
Amino acid modifications
	Glycosylation	99	1	N-linked (GlcNAc...) Potential
	Glycosylation	103	1	N-linked (GlcNAc...) Potential
	Glycosylation	130	1	N-linked (GlcNAc...) Potential
	Glycosylation	146	1	N-linked (GlcNAc...) Potential
	Glycosylation	161	1	N-linked (GlcNAc...) Potential
	Glycosylation	193	1	N-linked (GlcNAc...) Potential
	Glycosylation	222	1	N-linked (GlcNAc...) Potential
	Disulfide bond	131 ↔ 152		By similarity
	Disulfide bond	162 ↔ 178		By similarity
	Disulfide bond	201 ↔ 263		By similarity

Sequences

	Sequence		Length	Mass (Da)
	P51164 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 573F6D729CED1C3D	FASTA	291	33,367
	10 20 30 40 50 60 MAALQEKKTC GQRMEEFQRY CWNPDTGQML GRTLSRWVWI SLYYVAFYVV MTGLFALCLY 70 80 90 100 110 120 VLMQTVDPYT PDYQDQLRSP GVTLRPDVYG EKGLEIVYNV SDNRTWADLT QTLHAFLAGY 130 140 150 160 170 180 SPAAQEDSIN CTSEQYFFQE SFRAPNHTKF SCKFTADMLQ NCSGLADPNF GFEEGKPCFI 190 200 210 220 230 240 IKMNRIVKFL PSNGSAPRVD CAFLDQPREL GQPLQVKYYP PNGTFSLHYF PYYGKKAQPH 250 260 270 280 290 YSNPLVAAKL LNIPRNAEVA IVCKVMAEHV TFNNPHDPYE GKVEFKLKIE K

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning of the beta-subunit of the human gastric H,K-ATPase." Ma J.-Y., Song Y.-H., Sjoestrand S.E., Rask L., Maardh S. Biochem. Biophys. Res. Commun. 180:39-45(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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].
[4]	"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: Colon.
[5]	"GATA-6 DNA binding protein expressed in human gastric adenocarcinoma MKN45 cells." Yoshida T., Sato R., Mahmood S., Kawasaki S., Futai M., Maeda M. FEBS Lett. 414:333-337(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-14. Tissue: Liver.
[6]	"A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase resembles cell adhesion molecules." Bab-Dinitz E., Albeck S., Peleg Y., Brumfeld V., Gottschalk K.E., Karlish S.J. Biochemistry 48:8684-8691(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, IMMUNOGLOBULIN-LIKE DOMAIN.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M75110 mRNA. Translation: AAA35987.1. BX537316 Genomic DNA. Translation: CAM28358.1. CH471085 Genomic DNA. Translation: EAX09221.1. BC029059 mRNA. Translation: AAH29059.1. AB008783 Genomic DNA. Translation: BAA23425.1.
IPI	IPI00016421.
PIR	JH0480.
RefSeq	NP_000696.1. NM_000705.3.
UniGene	Hs.434202.
3D structure databases
ProteinModelPortal	P51164.
ModBase	Search...
Protein-protein interaction databases
IntAct	P51164. 2 interactions.
STRING	9606.ENSP00000334216.
Protein family/group databases
TCDB	3.A.3.1.2. P-type ATPase (P-ATPase) superfamily.
PTM databases
PhosphoSite	P51164.
Polymorphism databases
DMDM	1703461.
Proteomic databases
PaxDb	P51164.
PRIDE	P51164.
Protocols and materials databases
DNASU	496.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000335288; ENSP00000334216; ENSG00000186009.
GeneID	496.
KEGG	hsa:496.
UCSC	uc001vtz.3. human.
Organism-specific databases
CTD	496.
GeneCards	GC13M114303.
HGNC	HGNC:820. ATP4B.
HPA	CAB005598.
MIM	137217. gene.
neXtProt	NX_P51164.
PharmGKB	PA25114.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG289316.
HOGENOM	HOG000039248.
HOVERGEN	HBG050603.
InParanoid	P51164.
KO	K01543.
OMA	QPHYSNP.
OrthoDB	EOG4TXBS9.
PhylomeDB	P51164.
Enzyme and pathway databases
BioCyc	MetaCyc:G66-33511-MONOMER.
Reactome	REACT_15518. Transmembrane transport of small molecules.
Gene expression databases
Bgee	P51164.
CleanEx	HS_ATP4B.
Genevestigator	P51164.
GermOnline	ENSG00000186009. Homo sapiens.
Family and domain databases
InterPro	IPR000402. Na/K_ATPase_sub_beta. [Graphical view]
PANTHER	PTHR11523. PTHR11523. 1 hit.
Pfam	PF00287. Na_K-ATPase. 1 hit. [Graphical view]
TIGRFAMs	TIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITE	PS00390. ATPASE_NA_K_BETA_1. 1 hit. PS00391. ATPASE_NA_K_BETA_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P51164.
ChEMBL	CHEMBL5207.
DrugBank	DB01129. Rabeprazole.
GenomeRNAi	496.
NextBio	2083.
SOURCE	Search...

Entry information

Entry name

ATP4B_HUMAN

Accession

Primary (citable) accession number: P51164
Secondary accession number(s): B1B0N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 107 of the entry and version 1 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.