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P51164 (ATP4B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Potassium-transporting ATPase subunit beta
Alternative name(s):
Gastric H(+)/K(+) ATPase subunit beta
Proton pump beta chain
Gene names
Name:ATP4B
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length291 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 291291Potassium-transporting ATPase subunit beta
PRO_0000219091

Regions

Topological domain1 – 3636Cytoplasmic Potential
Transmembrane37 – 5721Helical; Signal-anchor for type II membrane protein; Potential
Topological domain58 – 291234Extracellular Potential
Region194 – 29198immunoglobulin-like

Amino acid modifications

Glycosylation991N-linked (GlcNAc...) Potential
Glycosylation1031N-linked (GlcNAc...) Potential
Glycosylation1301N-linked (GlcNAc...) Potential
Glycosylation1461N-linked (GlcNAc...) Potential
Glycosylation1611N-linked (GlcNAc...) Potential
Glycosylation1931N-linked (GlcNAc...) Potential
Glycosylation2221N-linked (GlcNAc...) Potential
Disulfide bond131 ↔ 152 By similarity
Disulfide bond162 ↔ 178 By similarity
Disulfide bond201 ↔ 263 By similarity

Sequences

Sequence LengthMass (Da)Tools
P51164 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 573F6D729CED1C3D

FASTA29133,367
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, DOMAIN IMMUNOGLOBULIN-LIKE.
+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.
PIRJH0480.
RefSeqNP_000696.1. NM_000705.3.
UniGeneHs.434202.

3D structure databases

ProteinModelPortalP51164.
SMRP51164. Positions 32-291.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106986. 4 interactions.
IntActP51164. 2 interactions.
STRING9606.ENSP00000334216.

Chemistry

BindingDBP51164.
ChEMBLCHEMBL2095173.
DrugBankDB01129. Rabeprazole.

Protein family/group databases

TCDB3.A.3.1.2. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteP51164.

Polymorphism databases

DMDM1703461.

Proteomic databases

PaxDbP51164.
PRIDEP51164.

Protocols and materials databases

DNASU496.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335288; ENSP00000334216; ENSG00000186009.
GeneID496.
KEGGhsa:496.
UCSCuc001vtz.3. human.

Organism-specific databases

CTD496.
GeneCardsGC13M114303.
HGNCHGNC:820. ATP4B.
HPACAB005598.
HPA045400.
MIM137217. gene.
neXtProtNX_P51164.
PharmGKBPA25114.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG289316.
HOGENOMHOG000039248.
HOVERGENHBG050603.
InParanoidP51164.
KOK01543.
OMAKAQPHYS.
OrthoDBEOG7M6D85.
PhylomeDBP51164.
TreeFamTF314618.

Enzyme and pathway databases

BioCycMetaCyc:G66-33511-MONOMER.
ReactomeREACT_15518. Transmembrane transport of small molecules.

Gene expression databases

BgeeP51164.
CleanExHS_ATP4B.
GenevestigatorP51164.

Family and domain databases

InterProIPR000402. Na/K_ATPase_sub_beta.
[Graphical view]
PANTHERPTHR11523. PTHR11523. 1 hit.
PfamPF00287. Na_K-ATPase. 1 hit.
[Graphical view]
TIGRFAMsTIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITEPS00390. ATPASE_NA_K_BETA_1. 1 hit.
PS00391. ATPASE_NA_K_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GenomeRNAi496.
NextBio2083.
PROP51164.
SOURCESearch...

Entry information

Entry nameATP4B_HUMAN
AccessionPrimary (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: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 13

Human chromosome 13: entries, gene names and cross-references to MIM