AT1B2_HUMAN
ID AT1B2_HUMAN Reviewed; 290 AA.
AC P14415; A0AV17; A8K278; D3DTQ2; O60444;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Sodium/potassium-transporting ATPase subunit beta-2;
DE AltName: Full=Adhesion molecule in glia;
DE Short=AMOG;
DE AltName: Full=Sodium/potassium-dependent ATPase subunit beta-2;
GN Name=ATP1B2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8305453; DOI=10.1016/0005-2736(94)90287-9;
RA Hernando N., Martin-Vasallo P., Ghosh S., Ghosh P.K., Swaroop A.,
RA Coca-Prados M.;
RT "Nucleotide sequence of a cDNA for the beta 2 subunit isoform of Na+,K(+)-
RT ATPase from human retina.";
RL Biochim. Biophys. Acta 1189:109-111(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retinal pigment epithelium;
RX PubMed=8918259; DOI=10.1016/0378-1119(96)00258-2;
RA Ruiz A.C., Bhat S.P., Bok D.;
RT "Expression and synthesis of the Na,K-ATPase beta 2 subunit in human
RT retinal pigment epithelium.";
RL Gene 176:237-242(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9524271; DOI=10.1016/s0378-1119(97)00661-6;
RA Avila J., Alvarez de la Rosa D., Gonzalez-Martinez L.M., Lecuona E.,
RA Martin-Vasallo P.;
RT "Structure and expression of the human Na,K-ATPase beta 2-subunit gene.";
RL Gene 208:221-227(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-290.
RX PubMed=2538450; DOI=10.1016/s0021-9258(18)83787-5;
RA Martin-Vasallo P., Dackowski W., Emanuel J.R., Levenson R.;
RT "Identification of a putative isoform of the Na,K-ATPase beta subunit.
RT Primary structure and tissue-specific expression.";
RL J. Biol. Chem. 264:4613-4618(1989).
RN [8]
RP DOMAIN IMMUNOGLOBULIN-LIKE.
RX PubMed=19694409; DOI=10.1021/bi900868e;
RA Bab-Dinitz E., Albeck S., Peleg Y., Brumfeld V., Gottschalk K.E.,
RA Karlish S.J.;
RT "A C-terminal lobe of the beta subunit of Na,K-ATPase and H,K-ATPase
RT resembles cell adhesion molecules.";
RL Biochemistry 48:8684-8691(2009).
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-238.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
CC -!- FUNCTION: This is the non-catalytic component of the active enzyme,
CC which catalyzes the hydrolysis of ATP coupled with the exchange of
CC Na(+) and K(+) ions across the plasma membrane. The exact function of
CC the beta-2 subunit is not known.
CC -!- FUNCTION: Mediates cell adhesion of neurons and astrocytes, and
CC promotes neurite outgrowth. {ECO:0000250}.
CC -!- SUBUNIT: The sodium/potassium-transporting ATPase is composed of a
CC catalytic alpha subunit, an auxiliary non-catalytic beta subunit and an
CC additional regulatory subunit. Interacts with isoform 2 of BSG (By
CC similarity). {ECO:0000250|UniProtKB:P14231, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type II membrane
CC protein.
CC -!- DOMAIN: The C-terminal lobe folds into an immunoglobulin-like domain
CC and mediates cell adhesion properties. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the X(+)/potassium ATPases subunit beta family.
CC {ECO:0000305}.
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DR EMBL; M81181; AAA51805.1; -; mRNA.
DR EMBL; U45945; AAC50873.1; -; mRNA.
DR EMBL; AF007876; AAC39686.1; -; Genomic_DNA.
DR EMBL; AK290143; BAF82832.1; -; mRNA.
DR EMBL; CH471108; EAW90148.1; -; Genomic_DNA.
DR EMBL; BC126175; AAI26176.1; -; mRNA.
DR CCDS; CCDS32550.1; -.
DR PIR; B32459; B32459.
DR PIR; JC5107; JC5107.
DR RefSeq; NP_001290192.1; NM_001303263.1.
DR RefSeq; NP_001669.3; NM_001678.4.
DR AlphaFoldDB; P14415; -.
DR SMR; P14415; -.
DR BioGRID; 106972; 14.
DR IntAct; P14415; 3.
DR STRING; 9606.ENSP00000250111; -.
DR BindingDB; P14415; -.
DR ChEMBL; CHEMBL2095186; -.
DR DrugBank; DB09020; Bisacodyl.
DR DrugBank; DB09479; Rubidium Rb-82.
DR DrugBank; DB16690; Tegoprazan.
DR DrugCentral; P14415; -.
DR GlyConnect; 1758; 1 N-Linked glycan (1 site).
DR GlyGen; P14415; 7 sites, 1 N-linked glycan (1 site).
DR iPTMnet; P14415; -.
DR PhosphoSitePlus; P14415; -.
DR BioMuta; ATP1B2; -.
DR DMDM; 125987795; -.
DR EPD; P14415; -.
DR jPOST; P14415; -.
DR MassIVE; P14415; -.
DR MaxQB; P14415; -.
DR PaxDb; P14415; -.
DR PeptideAtlas; P14415; -.
DR PRIDE; P14415; -.
DR ProteomicsDB; 53052; -.
DR Antibodypedia; 2415; 253 antibodies from 31 providers.
DR DNASU; 482; -.
DR Ensembl; ENST00000250111.9; ENSP00000250111.4; ENSG00000129244.9.
DR GeneID; 482; -.
DR KEGG; hsa:482; -.
DR MANE-Select; ENST00000250111.9; ENSP00000250111.4; NM_001678.5; NP_001669.3.
DR UCSC; uc002gif.2; human.
DR CTD; 482; -.
DR DisGeNET; 482; -.
DR GeneCards; ATP1B2; -.
DR HGNC; HGNC:805; ATP1B2.
DR HPA; ENSG00000129244; Group enriched (brain, retina).
DR MIM; 182331; gene.
DR neXtProt; NX_P14415; -.
DR OpenTargets; ENSG00000129244; -.
DR PharmGKB; PA67; -.
DR VEuPathDB; HostDB:ENSG00000129244; -.
DR eggNOG; KOG3927; Eukaryota.
DR GeneTree; ENSGT01030000234579; -.
DR HOGENOM; CLU_057702_1_1_1; -.
DR InParanoid; P14415; -.
DR OMA; VCRPGHY; -.
DR OrthoDB; 998086at2759; -.
DR PhylomeDB; P14415; -.
DR TreeFam; TF314618; -.
DR PathwayCommons; P14415; -.
DR Reactome; R-HSA-210991; Basigin interactions.
DR Reactome; R-HSA-5578775; Ion homeostasis.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR Reactome; R-HSA-9679191; Potential therapeutics for SARS.
DR SignaLink; P14415; -.
DR BioGRID-ORCS; 482; 6 hits in 1071 CRISPR screens.
DR ChiTaRS; ATP1B2; human.
DR GenomeRNAi; 482; -.
DR Pharos; P14415; Tclin.
DR PRO; PR:P14415; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P14415; protein.
DR Bgee; ENSG00000129244; Expressed in right hemisphere of cerebellum and 146 other tissues.
DR ExpressionAtlas; P14415; baseline and differential.
DR Genevisible; P14415; HS.
DR GO; GO:0016324; C:apical plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0097450; C:astrocyte end-foot; ISS:ARUK-UCL.
DR GO; GO:0097449; C:astrocyte projection; IDA:ARUK-UCL.
DR GO; GO:0044298; C:cell body membrane; ISS:ARUK-UCL.
DR GO; GO:0071944; C:cell periphery; ISS:ARUK-UCL.
DR GO; GO:0031253; C:cell projection membrane; ISS:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0016328; C:lateral plasma membrane; IDA:ARUK-UCL.
DR GO; GO:0016020; C:membrane; ISS:ARUK-UCL.
DR GO; GO:0098984; C:neuron to neuron synapse; ISS:ARUK-UCL.
DR GO; GO:0001917; C:photoreceptor inner segment; ISS:ARUK-UCL.
DR GO; GO:0005886; C:plasma membrane; ISS:ARUK-UCL.
DR GO; GO:0005890; C:sodium:potassium-exchanging ATPase complex; IDA:BHF-UCL.
DR GO; GO:0001671; F:ATPase activator activity; IDA:BHF-UCL.
DR GO; GO:0051117; F:ATPase binding; IPI:BHF-UCL.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:ARUK-UCL.
DR GO; GO:0030674; F:protein-macromolecule adaptor activity; IDA:BHF-UCL.
DR GO; GO:0086064; P:cell communication by electrical coupling involved in cardiac conduction; TAS:BHF-UCL.
DR GO; GO:0031589; P:cell-substrate adhesion; ISS:ARUK-UCL.
DR GO; GO:0030007; P:cellular potassium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
DR GO; GO:0021670; P:lateral ventricle development; ISS:ARUK-UCL.
DR GO; GO:0086009; P:membrane repolarization; IDA:BHF-UCL.
DR GO; GO:0061744; P:motor behavior; ISS:ARUK-UCL.
DR GO; GO:1903976; P:negative regulation of glial cell migration; ISS:ARUK-UCL.
DR GO; GO:0021944; P:neuronal-glial interaction involved in hindbrain glial-mediated radial cell migration; ISS:ARUK-UCL.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:ARUK-UCL.
DR GO; GO:0120036; P:plasma membrane bounded cell projection organization; ISS:ARUK-UCL.
DR GO; GO:0032781; P:positive regulation of ATP-dependent activity; IDA:BHF-UCL.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISS:ARUK-UCL.
DR GO; GO:1903288; P:positive regulation of potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1901018; P:positive regulation of potassium ion transmembrane transporter activity; IDA:BHF-UCL.
DR GO; GO:1903278; P:positive regulation of sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:1990573; P:potassium ion import across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0050821; P:protein stabilization; IDA:BHF-UCL.
DR GO; GO:0001895; P:retina homeostasis; ISS:ARUK-UCL.
DR GO; GO:0036376; P:sodium ion export across plasma membrane; IDA:BHF-UCL.
DR GO; GO:0021678; P:third ventricle development; ISS:ARUK-UCL.
DR GO; GO:0150104; P:transport across blood-brain barrier; NAS:ARUK-UCL.
DR Gene3D; 2.60.40.1660; -; 1.
DR InterPro; IPR000402; Na/K_ATPase_sub_beta.
DR InterPro; IPR038702; Na/K_ATPase_sub_beta_sf.
DR PANTHER; PTHR11523; PTHR11523; 1.
DR Pfam; PF00287; Na_K-ATPase; 1.
DR TIGRFAMs; TIGR01107; Na_K_ATPase_bet; 1.
DR PROSITE; PS00390; ATPASE_NA_K_BETA_1; 1.
DR PROSITE; PS00391; ATPASE_NA_K_BETA_2; 1.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell membrane; Disulfide bond; Glycoprotein; Ion transport;
KW Membrane; Potassium; Potassium transport; Reference proteome;
KW Signal-anchor; Sodium; Sodium transport; Sodium/potassium transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..290
FT /note="Sodium/potassium-transporting ATPase subunit beta-2"
FT /id="PRO_0000219104"
FT TOPO_DOM 1..39
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 40..67
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 68..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT REGION 193..290
FT /note="immunoglobulin-like"
FT CARBOHYD 96
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 159
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 197
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 238
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:19159218"
FT DISULFID 129..150
FT /evidence="ECO:0000250"
FT DISULFID 160..177
FT /evidence="ECO:0000250"
FT DISULFID 200..261
FT /evidence="ECO:0000250"
FT VARIANT 124
FT /note="Q -> L (in dbSNP:rs34745087)"
FT /id="VAR_061031"
FT VARIANT 199
FT /note="T -> A (in dbSNP:rs2227866)"
FT /id="VAR_030339"
FT CONFLICT 51
FT /note="L -> P (in Ref. 1; AAA51805 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 121
FT /note="I -> M (in Ref. 1; AAA51805 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="R -> L (in Ref. 1; AAA51805 and 6; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 248
FT /note="F -> L (in Ref. 2; AAC50873)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 290 AA; 33367 MW; CC5BFBB6D01347F1 CRC64;
MVIQKEKKSC GQVVEEWKEF VWNPRTHQFM GRTGTSWAFI LLFYLVFYGF LTAMFTLTMW
VMLQTVSDHT PKYQDRLATP GLMIRPKTEN LDVIVNVSDT ESWDQHVQKL NKFLEPYNDS
IQAQKNDVCR PGRYYEQPDN GVLNYPKRAC QFNRTQLGNC SGIGDSTHYG YSTGQPCVFI
KMNRVINFYA GANQSMNVTC AGKRDEDAEN LGNFVMFPAN GNIDLMYFPY YGKKFHVNYT
QPLVAVKFLN VTPNVEVNVE CRINAANIAT DDERDKFAGR VAFKLRINKT
