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Sodium/hydrogen exchanger 1 (APNH) (Na( )/H( ) antiporter, amiloride-sensitive) (Na( )/H( ) exchanger 1) (NHE-1) (Solute carrier family 9 member 1)

 SL9A1_HUMAN             Reviewed;         815 AA.
P19634; B1ALD6; D3DPL4; Q96EM2;
01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
01-NOV-1991, sequence version 2.
18-JUL-2018, entry version 201.
RecName: Full=Sodium/hydrogen exchanger 1;
AltName: Full=APNH;
AltName: Full=Na(+)/H(+) antiporter, amiloride-sensitive;
AltName: Full=Na(+)/H(+) exchanger 1;
Short=NHE-1;
AltName: Full=Solute carrier family 9 member 1;
Name=SLC9A1; Synonyms=APNH1, NHE1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=2536298; DOI=10.1016/0092-8674(89)90901-X;
Sardet C., Franchi A., Pouyssegur J.;
"Molecular cloning, primary structure, and expression of the human
growth factor-activatable Na+/H+ antiporter.";
Cell 56:271-280(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Kidney;
PubMed=2154036; DOI=10.1126/science.2154036;
Sardet C., Counillon L., Franchi A., Pouyssegur J.;
"Growth factors induce phosphorylation of the Na+/H+ antiporter,
glycoprotein of 110 kD.";
Science 247:723-726(1990).
[3]
SEQUENCE REVISION.
PubMed=1712287;
Tse C.-M., Ma A.I., Yang V.W., Watson A.J.M., Levine S.,
Montrose M.H., Potter J., Sardet C., Pouyssegur J., Donowitz M.;
"Molecular cloning and expression of a cDNA encoding the rabbit ileal
villus cell basolateral membrane Na+/H+ exchanger.";
EMBO J. 10:1957-1967(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Heart;
PubMed=8283968; DOI=10.1007/BF00936442;
Fliegel L., Dyck J.R., Wang H., Fong C., Haworth R.S.;
"Cloning and analysis of the human myocardial Na+/H+ exchanger.";
Mol. Cell. Biochem. 125:137-143(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=10913675; DOI=10.1016/S0165-4608(99)00246-0;
Garden O.A., Musk P., Worthington-White D.A., Dewey M.J., Rich I.N.;
"Silent polymorphisms within the coding region of human
sodium/hydrogen exchanger isoform-1 cDNA in peripheral blood
mononuclear cells of leukemia patients: a comparison with healthy
controls.";
Cancer Genet. Cytogenet. 120:37-43(2000).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
GLYCOSYLATION AT ASN-75, AND O-LINKED GLYCOSYLATION.
PubMed=8068684; DOI=10.1021/bi00200a030;
Counillon L., Pouyssegur J., Reithmeier R.A.;
"The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation
restricted to the first N-terminal extracellular domain.";
Biochemistry 33:10463-10469(1994).
[10]
INTERACTION WITH CHP1.
PubMed=8967452;
Goss G., Orlowski J., Grinstein S.;
"Coimmunoprecipitation of a 24-kDa protein with NHE1, the ubiquitous
isoform of the Na+/H+ exchanger.";
Am. J. Physiol. 270:C1493-C1502(1996).
[11]
FUNCTION IN PH REGULATION, AND INTERACTION WITH CHP1.
PubMed=8901634; DOI=10.1073/pnas.93.22.12631;
Lin X., Barber D.L.;
"A calcineurin homologous protein inhibits GTPase-stimulated Na-H
exchange.";
Proc. Natl. Acad. Sci. U.S.A. 93:12631-12636(1996).
[12]
TOPOLOGY.
PubMed=9688597;
Shrode L.D., Gan B.S., D'Souza S.J., Orlowski J., Grinstein S.;
"Topological analysis of NHE1, the ubiquitous Na+/H+ exchanger using
chymotryptic cleavage.";
Am. J. Physiol. 275:C431-C439(1998).
[13]
TOPOLOGY, AND MUTAGENESIS OF ARG-180 AND GLN-181.
PubMed=10713111; DOI=10.1074/jbc.275.11.7942;
Wakabayashi S., Pang T., Su X., Shigekawa M.;
"A novel topology model of the human Na(+)/H(+) exchanger isoform 1.";
J. Biol. Chem. 275:7942-7949(2000).
[14]
INTERACTION WITH TESC, AND SUBCELLULAR LOCATION.
PubMed=11696366; DOI=10.1016/S0014-5793(01)02986-6;
Mailaender J., Mueller-Esterl W., Dedio J.;
"Human homolog of mouse tescalcin associates with Na(+)/H(+) exchanger
type-1.";
FEBS Lett. 507:331-335(2001).
[15]
FUNCTION, INTERACTION WITH CHP1, AND MUTAGENESIS OF ILE-518; ILE-522;
PHE-526; LEU-527; LEU-530; LEU-531 AND 526-PHE--LEU-531.
PubMed=11350981; DOI=10.1074/jbc.M100296200;
Pang T., Su X., Wakabayashi S., Shigekawa M.;
"Calcineurin homologous protein as an essential cofactor for Na+/H+
exchangers.";
J. Biol. Chem. 276:17367-17372(2001).
[16]
INTERACTION WITH CHP2.
PubMed=12226101; DOI=10.1074/jbc.M208313200;
Pang T., Wakabayashi S., Shigekawa M.;
"Expression of calcineurin B homologous protein 2 protects serum
deprivation-induced cell death by serum-independent activation of
Na+/H+ exchanger.";
J. Biol. Chem. 277:43771-43777(2002).
[17]
INTERACTION WITH TESC AND CALMODULIN.
PubMed=12809501; DOI=10.1021/bi027143d;
Li X., Liu Y., Kay C.M., Muller-Esterl W., Fliegel L.;
"The Na+/H+ exchanger cytoplasmic tail: structure, function, and
interactions with tescalcin.";
Biochemistry 42:7448-7456(2003).
[18]
FUNCTION IN PH REGULATION, INTERACTION WITH CHP1, AND SUBCELLULAR
LOCATION.
PubMed=15035633; DOI=10.1021/bi0360004;
Pang T., Hisamitsu T., Mori H., Shigekawa M., Wakabayashi S.;
"Role of calcineurin B homologous protein in pH regulation by the
Na+/H+ exchanger 1: tightly bound Ca2+ ions as important structural
elements.";
Biochemistry 43:3628-3636(2004).
[19]
MUTAGENESIS OF PRO-167 AND PRO-168.
PubMed=14680478; DOI=10.1042/BJ20030884;
Slepkov E.R., Chow S., Lemieux M.J., Fliegel L.;
"Proline residues in transmembrane segment IV are critical for
activity, expression and targeting of the Na+/H+ exchanger isoform
1.";
Biochem. J. 379:31-38(2004).
[20]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Platelet;
PubMed=18088087; DOI=10.1021/pr0704130;
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697; SER-703; SER-723;
SER-726; SER-729 AND SER-785, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[25]
INTERACTION WITH CHP2, AND SUBCELLULAR LOCATION.
PubMed=21392185; DOI=10.1111/j.1365-2443.2011.01497.x;
Li Q.H., Wang L.H., Lin Y.N., Chang G.Q., Li H.W., Jin W.N., Hu R.H.,
Pang T.X.;
"Nuclear accumulation of calcineurin B homologous protein 2 (CHP2)
results in enhanced proliferation of tumor cells.";
Genes Cells 16:416-426(2011).
[26]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602; SER-605; SER-693;
SER-703 AND SER-785, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-599; SER-602 AND
SER-703, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[29]
INVOLVEMENT IN LIKNS, VARIANT LIKNS ARG-305, AND CHARACTERIZATION OF
VARIANT LIKNS ARG-305.
PubMed=25205112; DOI=10.1093/hmg/ddu461;
Guissart C., Li X., Leheup B., Drouot N., Montaut-Verient B.,
Raffo E., Jonveaux P., Roux A.F., Claustres M., Fliegel L., Koenig M.;
"Mutation of SLC9A1, encoding the major Na[?]/H[?] exchanger, causes
ataxia-deafness Lichtenstein-Knorr syndrome.";
Hum. Mol. Genet. 24:463-470(2015).
[30]
STRUCTURE BY NMR OF 155-180, AND MUTAGENESIS OF PHE-155; LEU-156;
GLN-157; SER-158; ASP-159; VAL-160; PHE-161; PHE-162; LEU-163;
PHE-164; LEU-165; LEU-166; PRO-167; PRO-168; ILE-169; ILE-170;
LEU-171; ASP-172; ALA-173; GLY-174; TYR-175; PHE-176 AND LEU-177.
PubMed=15677483; DOI=10.1074/jbc.M409608200;
Slepkov E.R., Rainey J.K., Li X., Liu Y., Cheng F.J., Lindhout D.A.,
Sykes B.D., Fliegel L.;
"Structural and functional characterization of transmembrane segment
IV of the NHE1 isoform of the Na+/H+ exchanger.";
J. Biol. Chem. 280:17863-17872(2005).
[31]
PRELIMINARY X-RAY CRYSTALLOGRAPHY OF 503-545 IN COMPLEX WITH CHP2.
PubMed=16511206; DOI=10.1107/S1744309105030836;
Ben Ammar Y., Takeda S., Sugawara M., Miyano M., Mori H.,
Wakabayashi S.;
"Crystallization and preliminary crystallographic analysis of the
human calcineurin homologous protein CHP2 bound to the cytoplasmic
region of the Na+/H+ exchanger NHE1.";
Acta Crystallogr. F 61:956-958(2005).
[32]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 503-545 IN COMPLEX WITH CHP2,
AND MUTAGENESIS OF ILE-534 AND ILE-537.
PubMed=16710297; DOI=10.1038/sj.emboj.7601145;
Ammar Y.B., Takeda S., Hisamitsu T., Mori H., Wakabayashi S.;
"Crystal structure of CHP2 complexed with NHE1-cytosolic region and an
implication for pH regulation.";
EMBO J. 25:2315-2325(2006).
[33]
STRUCTURE BY NMR OF 503-545 IN COMPLEX WITH CHP1.
PubMed=17050540; DOI=10.1074/jbc.M604092200;
Mishima M., Wakabayashi S., Kojima C.;
"Solution structure of the cytoplasmic region of Na+/H+ exchanger 1
complexed with essential cofactor calcineurin B homologous protein
1.";
J. Biol. Chem. 282:2741-2751(2007).
-!- FUNCTION: Involved in pH regulation to eliminate acids generated
by active metabolism or to counter adverse environmental
conditions. Major proton extruding system driven by the inward
sodium ion chemical gradient. Plays an important role in signal
transduction. {ECO:0000269|PubMed:11350981,
ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:8901634}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Fully active at acidic pHs, the antiporter is virtually turned
off at neutral pH.;
-!- SUBUNIT: Oligomer (By similarity). Interacts with calmodulin and
TESC. Interacts (via the juxtamembrane region of the cytoplasmic
C-terminal domain) with CHP1; the interaction occurs at the plasma
membrane in a calcium-dependent manner. Interacts with CHP2; the
interaction occurs in a calcium-dependent manner. {ECO:0000250,
ECO:0000269|PubMed:11350981, ECO:0000269|PubMed:11696366,
ECO:0000269|PubMed:12226101, ECO:0000269|PubMed:12809501,
ECO:0000269|PubMed:15035633, ECO:0000269|PubMed:16710297,
ECO:0000269|PubMed:17050540, ECO:0000269|PubMed:21392185,
ECO:0000269|PubMed:8901634, ECO:0000269|PubMed:8967452}.
-!- INTERACTION:
P31946:YWHAB; NbExp=4; IntAct=EBI-743635, EBI-359815;
-!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane
protein {ECO:0000250}. Cell membrane; Multi-pass membrane protein.
Note=Colocalizes with CHP1 at the reticulum endoplasmic (By
similarity). Colocalizes with CHP1 and CHP2 at the plasma
membrane. {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P19634-1; Sequence=Displayed;
Name=2;
IsoId=P19634-2; Sequence=VSP_022101, VSP_022102;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Kidney and intestine.
-!- PTM: O-glycosylated. {ECO:0000269|PubMed:8068684}.
-!- PTM: Ubiquitinated, leading to its degradation by the proteasome.
Ubiquitination is reduced by CHP1 (By similarity). {ECO:0000250}.
-!- DISEASE: Lichtenstein-Knorr syndrome (LIKNS) [MIM:616291]: An
autosomal recessive neurologic disorder characterized by
progressive cerebellar ataxia and severe progressive sensorineural
hearing loss. {ECO:0000269|PubMed:25205112}. Note=The disease is
caused by mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: Inhibited by amiloride and 5-amino-substituted
derivatives and activated in a cooperative fashion by
intracellular H(+). In quiescent cells upon growth factor
stimulation, the apparent affinity for internal H(+) is increased,
resulting in a persistent rise in cytoplasmic pH.
-!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1
(CPA1) transporter (TC 2.A.36) family. {ECO:0000305}.
-!- CAUTION: The region between transmembrane regions M4 and M5 and
between M6 and M7 (also termed intracellular loops IL2 and IL4,
respectively) seem to be localized at least in part in the
membrane. The hydrophobic region H10 is proposed to be located
within the membrane. {ECO:0000305}.
-!- CAUTION: Although PubMed:12809501 report that TESC-binding results
in a decrease in activity, studies with rat SLC9A1 show that TESC-
binding results in the maturation and accumulation of SLC9A1 at
the cell surface. {ECO:0000305}.
-!- CAUTION: Although PubMed:12809501 report that CHP1 and TESC bind
to SLC9A1 at different sites, studies with rat SLC9A1 show that
they bind at the same C-terminal site. {ECO:0000305}.
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EMBL; M81768; AAB59460.1; ALT_SEQ; mRNA.
EMBL; S68616; AAC60606.1; -; mRNA.
EMBL; AF141350; AAF21350.1; -; mRNA.
EMBL; AF141351; AAF21351.1; -; mRNA.
EMBL; AF141352; AAF21352.1; -; mRNA.
EMBL; AF141353; AAF21353.1; -; mRNA.
EMBL; AF141354; AAF21354.1; -; mRNA.
EMBL; AF141355; AAF21355.1; -; mRNA.
EMBL; AF141356; AAF21356.1; -; mRNA.
EMBL; AF141357; AAF21357.1; -; mRNA.
EMBL; AF141358; AAF21358.1; -; mRNA.
EMBL; AF141359; AAF21359.1; -; mRNA.
EMBL; AF146430; AAF25592.1; -; mRNA.
EMBL; AF146431; AAF25593.1; -; mRNA.
EMBL; AF146432; AAF25594.1; -; mRNA.
EMBL; AF146433; AAF25595.1; -; mRNA.
EMBL; AF146434; AAF25596.1; -; mRNA.
EMBL; AF146435; AAF25597.1; -; mRNA.
EMBL; AF146436; AAF25598.1; -; mRNA.
EMBL; AF146437; AAF25599.1; -; mRNA.
EMBL; AF146438; AAF25600.1; -; mRNA.
EMBL; AF146439; AAF25601.1; -; mRNA.
EMBL; AL590640; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL137860; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471059; EAX07773.1; -; Genomic_DNA.
EMBL; CH471059; EAX07774.1; -; Genomic_DNA.
EMBL; BC012121; AAH12121.1; -; mRNA.
CCDS; CCDS295.1; -. [P19634-1]
PIR; I57487; I57487.
RefSeq; NP_003038.2; NM_003047.4. [P19634-1]
UniGene; Hs.469116; -.
PDB; 1Y4E; NMR; -; A=155-180.
PDB; 2BEC; X-ray; 2.70 A; B=503-545.
PDB; 2E30; NMR; -; B=503-545.
PDB; 2HTG; NMR; -; A=250-274.
PDB; 2KBV; NMR; -; A=447-472.
PDB; 2L0E; NMR; -; A=226-250.
PDB; 2MDF; NMR; -; A=226-274.
PDB; 2YGG; X-ray; 2.23 A; A=622-689.
PDBsum; 1Y4E; -.
PDBsum; 2BEC; -.
PDBsum; 2E30; -.
PDBsum; 2HTG; -.
PDBsum; 2KBV; -.
PDBsum; 2L0E; -.
PDBsum; 2MDF; -.
PDBsum; 2YGG; -.
ProteinModelPortal; P19634; -.
SMR; P19634; -.
BioGrid; 112438; 48.
IntAct; P19634; 14.
MINT; P19634; -.
STRING; 9606.ENSP00000263980; -.
BindingDB; P19634; -.
ChEMBL; CHEMBL2781; -.
DrugBank; DB00594; Amiloride.
DrugBank; DB02624; Homoserine Lactone.
TCDB; 2.A.36.1.13; the monovalent cation:proton antiporter-1 (cpa1) family.
iPTMnet; P19634; -.
PhosphoSitePlus; P19634; -.
BioMuta; SLC9A1; -.
DMDM; 127809; -.
EPD; P19634; -.
MaxQB; P19634; -.
PaxDb; P19634; -.
PeptideAtlas; P19634; -.
PRIDE; P19634; -.
ProteomicsDB; 53683; -.
ProteomicsDB; 53684; -. [P19634-2]
Ensembl; ENST00000263980; ENSP00000263980; ENSG00000090020. [P19634-1]
Ensembl; ENST00000374086; ENSP00000363199; ENSG00000090020. [P19634-2]
GeneID; 6548; -.
KEGG; hsa:6548; -.
UCSC; uc001bnm.5; human. [P19634-1]
CTD; 6548; -.
DisGeNET; 6548; -.
EuPathDB; HostDB:ENSG00000090020.10; -.
GeneCards; SLC9A1; -.
HGNC; HGNC:11071; SLC9A1.
HPA; CAB022371; -.
HPA; HPA048532; -.
HPA; HPA052891; -.
MalaCards; SLC9A1; -.
MIM; 107310; gene.
MIM; 616291; phenotype.
neXtProt; NX_P19634; -.
OpenTargets; ENSG00000090020; -.
PharmGKB; PA35928; -.
eggNOG; KOG1966; Eukaryota.
eggNOG; COG0025; LUCA.
GeneTree; ENSGT00760000119074; -.
HOGENOM; HOG000247044; -.
HOVERGEN; HBG052615; -.
InParanoid; P19634; -.
KO; K05742; -.
OMA; ERSTHDL; -.
OrthoDB; EOG091G02Q0; -.
PhylomeDB; P19634; -.
TreeFam; TF317212; -.
Reactome; R-HSA-2160916; Hyaluronan uptake and degradation.
Reactome; R-HSA-425986; Sodium/Proton exchangers.
SignaLink; P19634; -.
SIGNOR; P19634; -.
ChiTaRS; SLC9A1; human.
EvolutionaryTrace; P19634; -.
GeneWiki; Sodium%E2%80%93hydrogen_antiporter_1; -.
GenomeRNAi; 6548; -.
PRO; PR:P19634; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000090020; -.
CleanEx; HS_SLC9A1; -.
ExpressionAtlas; P19634; baseline and differential.
Genevisible; P19634; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:Ensembl.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0090533; C:cation-transporting ATPase complex; IDA:BHF-UCL.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; TAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL.
GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
GO; GO:0030027; C:lamellipodium; TAS:BHF-UCL.
GO; GO:0045121; C:membrane raft; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030315; C:T-tubule; IEA:Ensembl.
GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; TAS:BHF-UCL.
GO; GO:0015386; F:potassium:proton antiporter activity; IBA:GO_Central.
GO; GO:0030674; F:protein binding, bridging; TAS:BHF-UCL.
GO; GO:0030346; F:protein phosphatase 2B binding; IDA:BHF-UCL.
GO; GO:0032947; F:protein-containing complex scaffold activity; TAS:BHF-UCL.
GO; GO:0015385; F:sodium:proton antiporter activity; IDA:UniProtKB.
GO; GO:0086040; F:sodium:proton antiporter activity involved in regulation of cardiac muscle cell membrane potential; TAS:BHF-UCL.
GO; GO:0015299; F:solute:proton antiporter activity; TAS:UniProtKB.
GO; GO:0086003; P:cardiac muscle cell contraction; IEA:Ensembl.
GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0016477; P:cell migration; TAS:BHF-UCL.
GO; GO:0071468; P:cellular response to acidic pH; IDA:BHF-UCL.
GO; GO:0071236; P:cellular response to antibiotic; IEA:Ensembl.
GO; GO:0070417; P:cellular response to cold; IEA:Ensembl.
GO; GO:0071257; P:cellular response to electrical stimulus; IEA:Ensembl.
GO; GO:0071872; P:cellular response to epinephrine stimulus; IMP:BHF-UCL.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:0032869; P:cellular response to insulin stimulus; IEA:Ensembl.
GO; GO:0071260; P:cellular response to mechanical stimulus; TAS:BHF-UCL.
GO; GO:0006883; P:cellular sodium ion homeostasis; IDA:BHF-UCL.
GO; GO:0030214; P:hyaluronan catabolic process; TAS:Reactome.
GO; GO:0006811; P:ion transport; TAS:Reactome.
GO; GO:0030011; P:maintenance of cell polarity; TAS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0070997; P:neuron death; IEA:Ensembl.
GO; GO:0045760; P:positive regulation of action potential; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IEA:Ensembl.
GO; GO:0070886; P:positive regulation of calcineurin-NFAT signaling cascade; IDA:BHF-UCL.
GO; GO:1903281; P:positive regulation of calcium:sodium antiporter activity; IMP:BHF-UCL.
GO; GO:0010613; P:positive regulation of cardiac muscle hypertrophy; IMP:BHF-UCL.
GO; GO:0030307; P:positive regulation of cell growth; IEA:Ensembl.
GO; GO:0035794; P:positive regulation of mitochondrial membrane permeability; IEA:Ensembl.
GO; GO:0098735; P:positive regulation of the force of heart contraction; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central.
GO; GO:0051259; P:protein complex oligomerization; ISS:UniProtKB.
GO; GO:1902600; P:proton transmembrane transport; IDA:BHF-UCL.
GO; GO:0086036; P:regulation of cardiac muscle cell membrane potential; TAS:BHF-UCL.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; IMP:BHF-UCL.
GO; GO:0051893; P:regulation of focal adhesion assembly; TAS:BHF-UCL.
GO; GO:0051453; P:regulation of intracellular pH; IDA:UniProtKB.
GO; GO:0006885; P:regulation of pH; IDA:UniProtKB.
GO; GO:0051930; P:regulation of sensory perception of pain; IEA:Ensembl.
GO; GO:0051492; P:regulation of stress fiber assembly; TAS:BHF-UCL.
GO; GO:0086092; P:regulation of the force of heart contraction by cardiac conduction; IMP:BHF-UCL.
GO; GO:0010447; P:response to acidic pH; IDA:UniProtKB.
GO; GO:0035994; P:response to muscle stretch; IMP:BHF-UCL.
GO; GO:0036376; P:sodium ion export across plasma membrane; ISS:UniProtKB.
GO; GO:0098719; P:sodium ion import across plasma membrane; IDA:BHF-UCL.
InterPro; IPR006153; Cation/H_exchanger.
InterPro; IPR018422; Cation/H_exchanger_CPA1.
InterPro; IPR001970; Na/H_exchanger_1.
InterPro; IPR004709; NaH_exchanger.
InterPro; IPR032103; NHE_CaM-bd.
PANTHER; PTHR10110; PTHR10110; 1.
PANTHER; PTHR10110:SF59; PTHR10110:SF59; 1.
Pfam; PF00999; Na_H_Exchanger; 1.
Pfam; PF16644; NEXCaM_BD; 1.
PRINTS; PR01084; NAHEXCHNGR.
PRINTS; PR01085; NAHEXCHNGR1.
TIGRFAMs; TIGR00840; b_cpa1; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Antiport; Calmodulin-binding;
Cell membrane; Complete proteome; Deafness; Disease mutation;
Endoplasmic reticulum; Glycoprotein; Ion transport; Membrane;
Neurodegeneration; Phosphoprotein; Polymorphism; Reference proteome;
Sodium; Sodium transport; Transmembrane; Transmembrane helix;
Transport; Ubl conjugation.
CHAIN 1 815 Sodium/hydrogen exchanger 1.
/FTId=PRO_0000052347.
TOPO_DOM 1 12 Cytoplasmic. {ECO:0000255}.
TRANSMEM 13 33 Helical; Name=M1. {ECO:0000255}.
TOPO_DOM 34 105 Extracellular. {ECO:0000255}.
TRANSMEM 106 127 Helical; Name=M2. {ECO:0000255}.
TOPO_DOM 128 129 Cytoplasmic. {ECO:0000255}.
TRANSMEM 130 149 Helical; Name=M3. {ECO:0000255}.
TOPO_DOM 150 154 Extracellular. {ECO:0000255}.
TRANSMEM 155 174 Helical; Name=M4. {ECO:0000255}.
TOPO_DOM 175 191 Cytoplasmic. {ECO:0000255}.
TRANSMEM 192 211 Helical; Name=M5. {ECO:0000255}.
TOPO_DOM 212 227 Extracellular. {ECO:0000255}.
TRANSMEM 228 247 Helical; Name=M6. {ECO:0000255}.
TOPO_DOM 248 256 Cytoplasmic. {ECO:0000255}.
TRANSMEM 257 276 Helical; Name=M7. {ECO:0000255}.
TOPO_DOM 277 294 Extracellular. {ECO:0000255}.
TRANSMEM 295 315 Helical; Name=M8. {ECO:0000255}.
TOPO_DOM 316 338 Cytoplasmic. {ECO:0000255}.
TRANSMEM 339 358 Helical; Name=M9. {ECO:0000255}.
TOPO_DOM 359 381 Extracellular. {ECO:0000255}.
INTRAMEM 382 402 Name=H10. {ECO:0000250}.
TOPO_DOM 403 410 Extracellular. {ECO:0000255}.
TRANSMEM 411 430 Helical; Name=M10. {ECO:0000255}.
TOPO_DOM 431 448 Cytoplasmic. {ECO:0000255}.
TRANSMEM 449 470 Helical; Name=M11. {ECO:0000255}.
TOPO_DOM 471 479 Extracellular. {ECO:0000255}.
TRANSMEM 480 499 Helical; Name=M12. {ECO:0000255}.
TOPO_DOM 500 815 Cytoplasmic. {ECO:0000255}.
REGION 516 539 Interaction with CHP2.
SITE 161 161 Channel pore-lining. {ECO:0000305}.
SITE 370 370 Not glycosylated.
MOD_RES 599 599 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 602 602 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 603 603 Phosphothreonine.
{ECO:0000250|UniProtKB:Q61165}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 693 693 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 697 697 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 703 703 Phosphoserine.
{ECO:0000244|PubMed:18088087,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 723 723 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 726 726 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 785 785 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 787 787 Phosphoserine.
{ECO:0000250|UniProtKB:Q61165}.
MOD_RES 796 796 Phosphoserine.
{ECO:0000250|UniProtKB:P26431}.
CARBOHYD 42 42 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 56 56 O-linked (GalNAc...) serine.
{ECO:0000255}.
CARBOHYD 61 61 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 62 62 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 68 68 O-linked (GalNAc...) threonine.
{ECO:0000255}.
CARBOHYD 75 75 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:8068684}.
VAR_SEQ 496 554 GMTIRPLVDLLAVKKKQETKRSINEEIHTQFLDHLLTGIED
ICGHYGHHHWKDKLNRFN -> VLGQGRAGPCLGDPHRLFP
WKERKACDLKCDSSPSSTTNLLCDLGRATPPFWASVSSIVK
(in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022101.
VAR_SEQ 555 815 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_022102.
VARIANT 305 305 G -> R (in LIKNS; causes reduced
expression of the mutant protein;
hypoglycosylated; does not localize
properly at the plasma membrane; small
residual activity; dbSNP:rs786204831).
{ECO:0000269|PubMed:25205112}.
/FTId=VAR_073439.
VARIANT 682 682 N -> K (in dbSNP:rs35703140).
/FTId=VAR_050231.
MUTAGEN 155 155 F->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 156 156 L->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 157 157 Q->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 158 158 S->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 159 159 D->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 160 160 V->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 161 161 F->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 162 162 F->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 163 163 L->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 164 164 F->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 165 165 L->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 166 166 L->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 167 167 P->A: Reduces activity.
{ECO:0000269|PubMed:14680478,
ECO:0000269|PubMed:15677483}.
MUTAGEN 167 167 P->C,G: Almost complete loss of activity.
Reduces membrane localization.
{ECO:0000269|PubMed:14680478,
ECO:0000269|PubMed:15677483}.
MUTAGEN 168 168 P->A,C: Almost complete loss of activity.
{ECO:0000269|PubMed:14680478,
ECO:0000269|PubMed:15677483}.
MUTAGEN 168 168 P->G: Reduces activity.
{ECO:0000269|PubMed:14680478,
ECO:0000269|PubMed:15677483}.
MUTAGEN 169 169 I->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 170 170 I->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 171 171 L->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 172 172 D->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 173 173 A->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 174 174 G->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 175 175 Y->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 176 176 F->C: Almost complete loss of activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 177 177 L->C: Reduces activity.
{ECO:0000269|PubMed:15677483}.
MUTAGEN 178 178 P->A: No effect.
MUTAGEN 180 180 R->C: Reduces activity.
{ECO:0000269|PubMed:10713111}.
MUTAGEN 181 181 Q->C: Reduces activity.
{ECO:0000269|PubMed:10713111}.
MUTAGEN 518 518 I->Q: Reduces interaction with CHP1 and
the exchange activity; when associated
with Q-522.
{ECO:0000269|PubMed:11350981}.
MUTAGEN 522 522 I->Q: Reduces interaction with CHP1 and
the exchange activity; when associated
with Q-518.
{ECO:0000269|PubMed:11350981}.
MUTAGEN 526 531 FLDHLL->QQDHQQ: Inhibits interaction with
CHP1 and the exchange activity. CHPI does
not localize at the cell membrane.
{ECO:0000269|PubMed:11350981}.
MUTAGEN 526 531 FLDHLL->RRDHRR: Inhibits interaction with
CHP1 and the exchange activity. CHPI does
not localize at the cell membrane.
{ECO:0000269|PubMed:11350981}.
MUTAGEN 526 526 F->Q: Reduces interaction with CHP1 and
the exchange activity; when associated
with Q-527.
{ECO:0000269|PubMed:11350981}.
MUTAGEN 527 527 L->Q: Reduces interaction with CHP1 and
the exchange activity; when associated
with Q-526.
{ECO:0000269|PubMed:11350981}.
MUTAGEN 530 530 L->Q: Reduces interaction with CHP1 and
the exchange activity; when associated
with Q-531.
{ECO:0000269|PubMed:11350981}.
MUTAGEN 531 531 L->Q: Reduces interaction with CHP1 and
the exchange activity; when associated
with Q-530.
{ECO:0000269|PubMed:11350981}.
MUTAGEN 534 534 I->D,K: Strongly reduced interaction with
CHP2. {ECO:0000269|PubMed:16710297}.
MUTAGEN 537 537 I->K: Strongly reduced interaction with
CHP2. {ECO:0000269|PubMed:16710297}.
HELIX 162 165 {ECO:0000244|PDB:1Y4E}.
HELIX 171 174 {ECO:0000244|PDB:1Y4E}.
HELIX 177 180 {ECO:0000244|PDB:1Y4E}.
HELIX 231 234 {ECO:0000244|PDB:2L0E}.
HELIX 239 249 {ECO:0000244|PDB:2L0E}.
TURN 252 254 {ECO:0000244|PDB:2MDF}.
TURN 256 258 {ECO:0000244|PDB:2MDF}.
HELIX 259 269 {ECO:0000244|PDB:2MDF}.
TURN 271 273 {ECO:0000244|PDB:2MDF}.
HELIX 448 451 {ECO:0000244|PDB:2KBV}.
TURN 452 455 {ECO:0000244|PDB:2KBV}.
HELIX 459 471 {ECO:0000244|PDB:2KBV}.
HELIX 518 538 {ECO:0000244|PDB:2BEC}.
HELIX 625 651 {ECO:0000244|PDB:2YGG}.
HELIX 658 681 {ECO:0000244|PDB:2YGG}.
TURN 682 684 {ECO:0000244|PDB:2YGG}.
SEQUENCE 815 AA; 90763 MW; 02EC748C79DF6526 CRC64;
MVLRSGICGL SPHRIFPSLL VVVALVGLLP VLRSHGLQLS PTASTIRSSE PPRERSIGDV
TTAPPEVTPE SRPVNHSVTD HGMKPRKAFP VLGIDYTHVR TPFEISLWIL LACLMKIGFH
VIPTISSIVP ESCLLIVVGL LVGGLIKGVG ETPPFLQSDV FFLFLLPPII LDAGYFLPLR
QFTENLGTIL IFAVVGTLWN AFFLGGLMYA VCLVGGEQIN NIGLLDNLLF GSIISAVDPV
AVLAVFEEIH INELLHILVF GESLLNDAVT VVLYHLFEEF ANYEHVGIVD IFLGFLSFFV
VALGGVLVGV VYGVIAAFTS RFTSHIRVIE PLFVFLYSYM AYLSAELFHL SGIMALIASG
VVMRPYVEAN ISHKSHTTIK YFLKMWSSVS ETLIFIFLGV STVAGSHHWN WTFVISTLLF
CLIARVLGVL GLTWFINKFR IVKLTPKDQF IIAYGGLRGA IAFSLGYLLD KKHFPMCDLF
LTAIITVIFF TVFVQGMTIR PLVDLLAVKK KQETKRSINE EIHTQFLDHL LTGIEDICGH
YGHHHWKDKL NRFNKKYVKK CLIAGERSKE PQLIAFYHKM EMKQAIELVE SGGMGKIPSA
VSTVSMQNIH PKSLPSERIL PALSKDKEEE IRKILRNNLQ KTRQRLRSYN RHTLVADPYE
EAWNQMLLRR QKARQLEQKI NNYLTVPAHK LDSPTMSRAR IGSDPLAYEP KEDLPVITID
PASPQSPESV DLVNEELKGK VLGLSRDPAK VAEEDEDDDG GIMMRSKETS SPGTDDVFTP
APSDSPSSQR IQRCLSDPGP HPEPGEGEPF FPKGQ


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EIAAB38596 Na(+)_H(+) exchanger 1,Nhe1,NHE-1,Rat,Rattus norvegicus,Slc9a1,Sodium_hydrogen exchanger 1,Solute carrier family 9 member 1
EIAAB38600 H7,Na(+)_H(+) exchanger 2,Nhe2,NHE-2,Rat,Rattus norvegicus,Slc9a2,Sodium_hydrogen exchanger 2,Solute carrier family 9 member 2
EIAAB38598 Na(+)_H(+) exchanger 2,NHE2,NHE-2,Oryctolagus cuniculus,Rabbit,SLC9A2,Sodium_hydrogen exchanger 2,Solute carrier family 9 member 2
EIAAB38604 Homo sapiens,Human,Na(+)_H(+) exchanger 4,NHE4,NHE-4,SLC9A4,Sodium_hydrogen exchanger 4,Solute carrier family 9 member 4
EIAAB38592 Na(+)_H(+) exchanger 1,NHE1,NHE-1,Oryctolagus cuniculus,Rabbit,SLC9A1,Sodium_hydrogen exchanger 1,Solute carrier family 9 member 1


 

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