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Protein

Potassium-transporting ATPase subunit beta

Gene

ATP4B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Required for stabilization and maturation of the catalytic proton pump alpha subunit and may also involved in cell adhesion and establishing epithelial cell polarity.1 Publication

GO - Molecular functioni

  • hydrogen:potassium-exchanging ATPase activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion, Hydrogen ion transport, Ion transport, Potassium transport, Transport

Keywords - Ligandi

Potassium

Enzyme and pathway databases

BioCyciMetaCyc:G66-33511-MONOMER.
ReactomeiREACT_25149. Ion transport by P-type ATPases.

Protein family/group databases

TCDBi3.A.3.1.2. the p-type atpase (p-atpase) superfamily.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium-transporting ATPase subunit beta
Alternative name(s):
Gastric H(+)/K(+) ATPase subunit beta
Proton pump beta chain
Gene namesi
Name:ATP4B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:820. ATP4B.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3636CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei37 – 5721Helical; Signal-anchor for type II membrane proteinSequence AnalysisAdd
BLAST
Topological domaini58 – 291234ExtracellularSequence AnalysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA25114.

Polymorphism and mutation databases

BioMutaiATP4B.
DMDMi1703461.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 291291Potassium-transporting ATPase subunit betaPRO_0000219091Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi99 – 991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi103 – 1031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi131 ↔ 152By similarity
Glycosylationi146 – 1461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi161 – 1611N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi162 ↔ 178By similarity
Glycosylationi193 – 1931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi201 ↔ 263By similarity
Glycosylationi222 – 2221N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP51164.
PRIDEiP51164.

PTM databases

PhosphoSiteiP51164.

Expressioni

Gene expression databases

BgeeiP51164.
CleanExiHS_ATP4B.
GenevisibleiP51164. HS.

Organism-specific databases

HPAiCAB005598.
HPA045400.
HPA052649.

Interactioni

Subunit structurei

Composed of two subunits: alpha (catalytic) and beta.

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNDBP1O952733EBI-3904463,EBI-748961

Protein-protein interaction databases

BioGridi106986. 5 interactions.
IntActiP51164. 3 interactions.
STRINGi9606.ENSP00000334216.

Structurei

3D structure databases

ProteinModelPortaliP51164.
SMRiP51164. Positions 32-291.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni194 – 29198immunoglobulin-likeAdd
BLAST

Domaini

The C-terminal lobe folds into an immunoglobulin-like domain and mediates cell adhesion properties.1 Publication

Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG289316.
GeneTreeiENSGT00550000074530.
HOGENOMiHOG000039248.
HOVERGENiHBG050603.
InParanoidiP51164.
KOiK01543.
OMAiKAQPHYS.
OrthoDBiEOG7M6D85.
PhylomeDBiP51164.
TreeFamiTF314618.

Family and domain databases

InterProiIPR000402. Na/K_ATPase_sub_beta.
[Graphical view]
PANTHERiPTHR11523. PTHR11523. 1 hit.
PfamiPF00287. Na_K-ATPase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITEiPS00390. ATPASE_NA_K_BETA_1. 1 hit.
PS00391. ATPASE_NA_K_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P51164-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAALQEKKTC GQRMEEFQRY CWNPDTGQML GRTLSRWVWI SLYYVAFYVV
60 70 80 90 100
MTGLFALCLY VLMQTVDPYT PDYQDQLRSP GVTLRPDVYG EKGLEIVYNV
110 120 130 140 150
SDNRTWADLT QTLHAFLAGY SPAAQEDSIN CTSEQYFFQE SFRAPNHTKF
160 170 180 190 200
SCKFTADMLQ NCSGLADPNF GFEEGKPCFI IKMNRIVKFL PSNGSAPRVD
210 220 230 240 250
CAFLDQPREL GQPLQVKYYP PNGTFSLHYF PYYGKKAQPH YSNPLVAAKL
260 270 280 290
LNIPRNAEVA IVCKVMAEHV TFNNPHDPYE GKVEFKLKIE K
Length:291
Mass (Da):33,367
Last modified:October 1, 1996 - v1
Checksum:i573F6D729CED1C3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9539.1.
PIRiJH0480.
RefSeqiNP_000696.1. NM_000705.3.
UniGeneiHs.434202.

Genome annotation databases

EnsembliENST00000335288; ENSP00000334216; ENSG00000186009.
GeneIDi496.
KEGGihsa:496.
UCSCiuc001vtz.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS9539.1.
PIRiJH0480.
RefSeqiNP_000696.1. NM_000705.3.
UniGeneiHs.434202.

3D structure databases

ProteinModelPortaliP51164.
SMRiP51164. Positions 32-291.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106986. 5 interactions.
IntActiP51164. 3 interactions.
STRINGi9606.ENSP00000334216.

Chemistry

BindingDBiP51164.
ChEMBLiCHEMBL2095173.

Protein family/group databases

TCDBi3.A.3.1.2. the p-type atpase (p-atpase) superfamily.

PTM databases

PhosphoSiteiP51164.

Polymorphism and mutation databases

BioMutaiATP4B.
DMDMi1703461.

Proteomic databases

PaxDbiP51164.
PRIDEiP51164.

Protocols and materials databases

DNASUi496.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000335288; ENSP00000334216; ENSG00000186009.
GeneIDi496.
KEGGihsa:496.
UCSCiuc001vtz.3. human.

Organism-specific databases

CTDi496.
GeneCardsiGC13M114303.
HGNCiHGNC:820. ATP4B.
HPAiCAB005598.
HPA045400.
HPA052649.
MIMi137217. gene.
neXtProtiNX_P51164.
PharmGKBiPA25114.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG289316.
GeneTreeiENSGT00550000074530.
HOGENOMiHOG000039248.
HOVERGENiHBG050603.
InParanoidiP51164.
KOiK01543.
OMAiKAQPHYS.
OrthoDBiEOG7M6D85.
PhylomeDBiP51164.
TreeFamiTF314618.

Enzyme and pathway databases

BioCyciMetaCyc:G66-33511-MONOMER.
ReactomeiREACT_25149. Ion transport by P-type ATPases.

Miscellaneous databases

GenomeRNAii496.
NextBioi2083.
PROiP51164.
SOURCEiSearch...

Gene expression databases

BgeeiP51164.
CleanExiHS_ATP4B.
GenevisibleiP51164. HS.

Family and domain databases

InterProiIPR000402. Na/K_ATPase_sub_beta.
[Graphical view]
PANTHERiPTHR11523. PTHR11523. 1 hit.
PfamiPF00287. Na_K-ATPase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01107. Na_K_ATPase_bet. 1 hit.
PROSITEiPS00390. ATPASE_NA_K_BETA_1. 1 hit.
PS00391. ATPASE_NA_K_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiATP4B_HUMAN
AccessioniPrimary (citable) accession number: P51164
Secondary accession number(s): B1B0N8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 24, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.