P19634 (SL9A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Sodium/hydrogen exchanger 1

Alternative name(s):
APNH
Na(+)/H(+) antiporter, amiloride-sensitive
Na(+)/H(+) exchanger 1
Short name=NHE-1
Solute carrier family 9 member 1

Gene names

Name:	SLC9A1
Synonyms:	APNH1, NHE1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	815 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subunit structure	Interacts with CALMODULIN, CHP, CHP2 and TESC. Ref.12 Ref.13 Ref.14 Ref.15
Subcellular location	Membrane; Multi-pass membrane protein.
Tissue specificity	Kidney and intestine.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.17 Ref.18 Ref.19 Ref.20 O-glycosylated. Ref.9
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.
Sequence similarities	Belongs to the monovalent cation:proton antiporter 1 (CPA1) transporter (TC 2.A.36) family. [View classification]
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. Although Ref.15 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. Although Ref.15 report that CHP and TESC bind to SLC9A1 at different sites, studies with rat SLC9A1 show that they bind at the same C-terminal site.
Biophysicochemical properties	pH dependence: Fully active at acidic pHs, the antiporter is virtually turned off at neutral pH.

Ontologies

Keywords
Biological process	Antiport Ion transport Sodium transport Transport
Cellular component	Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Transmembrane Transmembrane helix
Ligand	Sodium
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of pH Traceable author statement Ref.4. Source: UniProtKB
Cellular component	integral to membrane Traceable author statement Ref.4. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P19634-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P19634-2)

The sequence of this isoform differs from the canonical sequence as follows:
     496-554: GMTIRPLVDL...HWKDKLNRFN → VLGQGRAGPC...FWASVSSIVK
     555-815: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 815

815

Sodium/hydrogen exchanger 1

PRO_0000052347

Regions

Topological domain

1 – 12

12

Cytoplasmic Potential

Transmembrane

13 – 33

21

Helical; Name=M1; Potential

Topological domain

34 – 105

72

Extracellular Potential

Transmembrane

106 – 127

22

Helical; Name=M2; Potential

Topological domain

128 – 129

2

Cytoplasmic Potential

Transmembrane

130 – 149

20

Helical; Name=M3; Potential

Topological domain

150 – 154

5

Extracellular Potential

Transmembrane

155 – 174

20

Helical; Name=M4; Potential

Topological domain

175 – 191

17

Cytoplasmic Potential

Transmembrane

192 – 211

20

Helical; Name=M5; Potential

Topological domain

212 – 227

16

Extracellular Potential

Transmembrane

228 – 247

20

Helical; Name=M6; Potential

Topological domain

248 – 256

9

Cytoplasmic Potential

Transmembrane

257 – 276

20

Helical; Name=M7; Potential

Topological domain

277 – 294

18

Extracellular Potential

Transmembrane

295 – 315

21

Helical; Name=M8; Potential

Topological domain

316 – 338

23

Cytoplasmic Potential

Transmembrane

339 – 358

20

Helical; Name=M9; Potential

Topological domain

359 – 381

23

Extracellular Potential

Intramembrane

382 – 402

21

Name=H10; By similarity

Topological domain

403 – 410

8

Extracellular Potential

Transmembrane

411 – 430

20

Helical; Name=M10; Potential

Topological domain

431 – 448

18

Cytoplasmic Potential

Transmembrane

449 – 470

22

Helical; Name=M11; Potential

Topological domain

471 – 479

9

Extracellular Potential

Transmembrane

480 – 499

20

Helical; Name=M12; Potential

Topological domain

500 – 815

316

Cytoplasmic Potential

Region

516 – 539

24

Interaction with CHP2

Sites

Site

161

1

Channel pore-lining Probable

Site

370

1

Not glycosylated

Amino acid modifications

Modified residue

599

1

Phosphoserine By similarity

Modified residue

602

1

Phosphoserine By similarity

Modified residue

605

1

Phosphoserine By similarity

Modified residue

693

1

Phosphoserine By similarity

Modified residue

695

1

Phosphothreonine Ref.18

Modified residue

697

1

Phosphoserine Ref.19

Modified residue

703

1

Phosphoserine Ref.18 Ref.19 Ref.20

Modified residue

723

1

Phosphoserine Ref.19

Modified residue

726

1

Phosphoserine Ref.19

Modified residue

729

1

Phosphoserine Ref.19

Modified residue

785

1

Phosphoserine Ref.18 Ref.19

Modified residue

787

1

Phosphoserine Ref.17

Modified residue

788

1

Phosphoserine Ref.17

Glycosylation

75

1

N-linked (GlcNAc...) Ref.9

Natural variations

Alternative sequence

496 – 554

59

GMTIR…LNRFN → VLGQGRAGPCLGDPHRLFPW KERKACDLKCDSSPSSTTNL LCDLGRATPPFWASVSSIVK in isoform 2.

VSP_022101

Alternative sequence

555 – 815

261

Missing in isoform 2.

VSP_022102

Natural variant

682

1

N → K.
Corresponds to variant rs35703140 [ dbSNP | Ensembl ].

VAR_050231

Experimental info

Mutagenesis

155

1

F → C: Almost complete loss of activity. Ref.21

Mutagenesis

156

1

L → C: Almost complete loss of activity. Ref.21

Mutagenesis

157

1

Q → C: Reduces activity. Ref.21

Mutagenesis

158

1

S → C: Almost complete loss of activity. Ref.21

Mutagenesis

159

1

D → C: Almost complete loss of activity. Ref.21

Mutagenesis

160

1

V → C: Reduces activity. Ref.21

Mutagenesis

161

1

F → C: Reduces activity. Ref.21

Mutagenesis

162

1

F → C: Almost complete loss of activity. Ref.21

Mutagenesis

163

1

L → C: Reduces activity. Ref.21

Mutagenesis

164

1

F → C: Almost complete loss of activity. Ref.21

Mutagenesis

165

1

L → C: Reduces activity. Ref.21

Mutagenesis

166

1

L → C: Reduces activity. Ref.21

Mutagenesis

167

1

P → A: Reduces activity. Ref.16 Ref.21

Mutagenesis

167

1

P → C or G: Almost complete loss of activity. Reduces membrane localization. Ref.16 Ref.21

Mutagenesis

168

1

P → A or C: Almost complete loss of activity. Ref.16 Ref.21

Mutagenesis

168

1

P → G: Reduces activity. Ref.16 Ref.21

Mutagenesis

169

1

I → C: Reduces activity. Ref.21

Mutagenesis

170

1

I → C: Reduces activity. Ref.21

Mutagenesis

171

1

L → C: Reduces activity. Ref.21

Mutagenesis

172

1

D → C: Almost complete loss of activity. Ref.21

Mutagenesis

173

1

A → C: Reduces activity. Ref.21

Mutagenesis

174

1

G → C: Reduces activity. Ref.21

Mutagenesis

175

1

Y → C: Almost complete loss of activity. Ref.21

Mutagenesis

176

1

F → C: Almost complete loss of activity. Ref.21

Mutagenesis

177

1

L → C: Reduces activity. Ref.21

Mutagenesis

178

1

P → A: No effect.

Mutagenesis

180

1

R → C: Reduces activity. Ref.11

Mutagenesis

181

1

Q → C: Reduces activity. Ref.11

Mutagenesis

534

1

I → D or K: Strongly reduced interaction with CHP2. Ref.22

Mutagenesis

537

1

I → K: Strongly reduced interaction with CHP2. Ref.22

Secondary structure

1

.

.

.

815

Helix Strand Turn

Details...

Helix

518 – 538

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1991. Version 2. Checksum: 02EC748C79DF6526	FASTA	815	90,763
	10 20 30 40 50 60 MVLRSGICGL SPHRIFPSLL VVVALVGLLP VLRSHGLQLS PTASTIRSSE PPRERSIGDV 70 80 90 100 110 120 TTAPPEVTPE SRPVNHSVTD HGMKPRKAFP VLGIDYTHVR TPFEISLWIL LACLMKIGFH 130 140 150 160 170 180 VIPTISSIVP ESCLLIVVGL LVGGLIKGVG ETPPFLQSDV FFLFLLPPII LDAGYFLPLR 190 200 210 220 230 240 QFTENLGTIL IFAVVGTLWN AFFLGGLMYA VCLVGGEQIN NIGLLDNLLF GSIISAVDPV 250 260 270 280 290 300 AVLAVFEEIH INELLHILVF GESLLNDAVT VVLYHLFEEF ANYEHVGIVD IFLGFLSFFV 310 320 330 340 350 360 VALGGVLVGV VYGVIAAFTS RFTSHIRVIE PLFVFLYSYM AYLSAELFHL SGIMALIASG 370 380 390 400 410 420 VVMRPYVEAN ISHKSHTTIK YFLKMWSSVS ETLIFIFLGV STVAGSHHWN WTFVISTLLF 430 440 450 460 470 480 CLIARVLGVL GLTWFINKFR IVKLTPKDQF IIAYGGLRGA IAFSLGYLLD KKHFPMCDLF 490 500 510 520 530 540 LTAIITVIFF TVFVQGMTIR PLVDLLAVKK KQETKRSINE EIHTQFLDHL LTGIEDICGH 550 560 570 580 590 600 YGHHHWKDKL NRFNKKYVKK CLIAGERSKE PQLIAFYHKM EMKQAIELVE SGGMGKIPSA 610 620 630 640 650 660 VSTVSMQNIH PKSLPSERIL PALSKDKEEE IRKILRNNLQ KTRQRLRSYN RHTLVADPYE 670 680 690 700 710 720 EAWNQMLLRR QKARQLEQKI NNYLTVPAHK LDSPTMSRAR IGSDPLAYEP KEDLPVITID 730 740 750 760 770 780 PASPQSPESV DLVNEELKGK VLGLSRDPAK VAEEDEDDDG GIMMRSKETS SPGTDDVFTP 790 800 810 APSDSPSSQR IQRCLSDPGP HPEPGEGEPF FPKGQ
	Isoform 2 [UniParc]. Checksum: 961A4B1AEDEA68A5	FASTA	555	61,013
	10 20 30 40 50 60 MVLRSGICGL SPHRIFPSLL VVVALVGLLP VLRSHGLQLS PTASTIRSSE PPRERSIGDV 70 80 90 100 110 120 TTAPPEVTPE SRPVNHSVTD HGMKPRKAFP VLGIDYTHVR TPFEISLWIL LACLMKIGFH 130 140 150 160 170 180 VIPTISSIVP ESCLLIVVGL LVGGLIKGVG ETPPFLQSDV FFLFLLPPII LDAGYFLPLR 190 200 210 220 230 240 QFTENLGTIL IFAVVGTLWN AFFLGGLMYA VCLVGGEQIN NIGLLDNLLF GSIISAVDPV 250 260 270 280 290 300 AVLAVFEEIH INELLHILVF GESLLNDAVT VVLYHLFEEF ANYEHVGIVD IFLGFLSFFV 310 320 330 340 350 360 VALGGVLVGV VYGVIAAFTS RFTSHIRVIE PLFVFLYSYM AYLSAELFHL SGIMALIASG 370 380 390 400 410 420 VVMRPYVEAN ISHKSHTTIK YFLKMWSSVS ETLIFIFLGV STVAGSHHWN WTFVISTLLF 430 440 450 460 470 480 CLIARVLGVL GLTWFINKFR IVKLTPKDQF IIAYGGLRGA IAFSLGYLLD KKHFPMCDLF 490 500 510 520 530 540 LTAIITVIFF TVFVQVLGQG RAGPCLGDPH RLFPWKERKA CDLKCDSSPS STTNLLCDLG 550 RATPPFWASV SSIVK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning, primary structure, and expression of the human growth factor-activatable Na+/H+ antiporter." Sardet C., Franchi A., Pouyssegur J. Cell 56:271-280(1989) [PubMed: 2536298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[2]	"Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD." Sardet C., Counillon L., Franchi A., Pouyssegur J. Science 247:723-726(1990) [PubMed: 2154036] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Kidney.
[3]	"Molecular cloning and expression of a cDNA encoding the rabbit ileal villus cell basolateral membrane Na+/H+ exchanger." 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. EMBO J. 10:1957-1967(1991) [PubMed: 1712287] [Abstract] Cited for: SEQUENCE REVISION.
[4]	"Cloning and analysis of the human myocardial Na+/H+ exchanger." Fliegel L., Dyck J.R., Wang H., Fong C., Haworth R.S. Mol. Cell. Biochem. 125:137-143(1993) [PubMed: 8283968] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Heart.
[5]	"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." Garden O.A., Musk P., Worthington-White D.A., Dewey M.J., Rich I.N. Cancer Genet. Cytogenet. 120:37-43(2000) [PubMed: 10913675] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"The DNA sequence and biological annotation of human chromosome 1." 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. Nature 441:315-321(2006) [PubMed: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Placenta.
[9]	"The Na+/H+ exchanger NHE-1 possesses N- and O-linked glycosylation restricted to the first N-terminal extracellular domain." Counillon L., Pouyssegur J., Reithmeier R.A. Biochemistry 33:10463-10469(1994) [PubMed: 8068684] [Abstract] Cited for: GLYCOSYLATION AT ASN-75, O-LINKED GLYCOSYLATION.
[10]	"Topological analysis of NHE1, the ubiquitous Na+/H+ exchanger using chymotryptic cleavage." Shrode L.D., Gan B.S., D'Souza S.J., Orlowski J., Grinstein S. Am. J. Physiol. 275:C431-C439(1998) [PubMed: 9688597] [Abstract] Cited for: TOPOLOGY.
[11]	"A novel topology model of the human Na(+)/H(+) exchanger isoform 1." Wakabayashi S., Pang T., Su X., Shigekawa M. J. Biol. Chem. 275:7942-7949(2000) [PubMed: 10713111] [Abstract] Cited for: TOPOLOGY, MUTAGENESIS OF ARG-180 AND GLN-181.
[12]	"Human homolog of mouse tescalcin associates with Na(+)/H(+) exchanger type-1." Mailaender J., Mueller-Esterl W., Dedio J. FEBS Lett. 507:331-335(2001) [PubMed: 11696366] [Abstract] Cited for: INTERACTION WITH TESC.
[13]	"Calcineurin homologous protein as an essential cofactor for Na+/H+ exchangers." Pang T., Su X., Wakabayashi S., Shigekawa M. J. Biol. Chem. 276:17367-17372(2001) [PubMed: 11350981] [Abstract] Cited for: INTERACTION WITH CHP.
[14]	"Expression of calcineurin B homologous protein 2 protects serum deprivation-induced cell death by serum-independent activation of Na+/H+ exchanger." Pang T., Wakabayashi S., Shigekawa M. J. Biol. Chem. 277:43771-43777(2002) [PubMed: 12226101] [Abstract] Cited for: INTERACTION WITH CHP2.
[15]	"The Na+/H+ exchanger cytoplasmic tail: structure, function, and interactions with tescalcin." Li X., Liu Y., Kay C.M., Muller-Esterl W., Fliegel L. Biochemistry 42:7448-7456(2003) [PubMed: 12809501] [Abstract] Cited for: INTERACTION WITH TESC AND CALMODULIN.
[16]	"Proline residues in transmembrane segment IV are critical for activity, expression and targeting of the Na+/H+ exchanger isoform 1." Slepkov E.R., Chow S., Lemieux M.J., Fliegel L. Biochem. J. 379:31-38(2004) [PubMed: 14680478] [Abstract] Cited for: MUTAGENESIS OF PRO-167 AND PRO-168.
[17]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." 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. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-787 AND SER-788, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[18]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-695; SER-703 AND SER-785, MASS SPECTROMETRY. Tissue: Platelet.
[19]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697; SER-703; SER-723; SER-726; SER-729 AND SER-785, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[21]	"Structural and functional characterization of transmembrane segment IV of the NHE1 isoform of the Na+/H+ exchanger." Slepkov E.R., Rainey J.K., Li X., Liu Y., Cheng F.J., Lindhout D.A., Sykes B.D., Fliegel L. J. Biol. Chem. 280:17863-17872(2005) [PubMed: 15677483] [Abstract] Cited for: STRUCTURE BY NMR OF 155-180, 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.
[22]	"Crystal structure of CHP2 complexed with NHE1-cytosolic region and an implication for pH regulation." Ammar Y.B., Takeda S., Hisamitsu T., Mori H., Wakabayashi S. EMBO J. 25:2315-2325(2006) [PubMed: 16710297] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 503-545 IN COMPLEX WITH CHP2, MUTAGENESIS OF ILE-534 AND ILE-537.
[23]	"Solution structure of the cytoplasmic region of Na+/H+ exchanger 1 complexed with essential cofactor calcineurin B homologous protein 1." Mishima M., Wakabayashi S., Kojima C. J. Biol. Chem. 282:2741-2751(2007) [PubMed: 17050540] [Abstract] Cited for: STRUCTURE BY NMR OF 503-545 IN COMPLEX WITH CHP.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M81768 mRNA. Translation: AAB59460.1. Sequence problems.
S68616 mRNA. Translation: AAC60606.1.
AF141350 mRNA. Translation: AAF21350.1.
AF141351 mRNA. Translation: AAF21351.1.
AF141352 mRNA. Translation: AAF21352.1.
AF141353 mRNA. Translation: AAF21353.1.
AF141354 mRNA. Translation: AAF21354.1.
AF141355 mRNA. Translation: AAF21355.1.
AF141356 mRNA. Translation: AAF21356.1.
AF141357 mRNA. Translation: AAF21357.1.
AF141358 mRNA. Translation: AAF21358.1.
AF141359 mRNA. Translation: AAF21359.1.
AF146430 mRNA. Translation: AAF25592.1.
AF146431 mRNA. Translation: AAF25593.1.
AF146432 mRNA. Translation: AAF25594.1.
AF146433 mRNA. Translation: AAF25595.1.
AF146434 mRNA. Translation: AAF25596.1.
AF146435 mRNA. Translation: AAF25597.1.
AF146436 mRNA. Translation: AAF25598.1.
AF146437 mRNA. Translation: AAF25599.1.
AF146438 mRNA. Translation: AAF25600.1.
AF146439 mRNA. Translation: AAF25601.1.
AL590640, AL137860 Genomic DNA. Translation: CAH73555.1.
AL590640, AL137860 Genomic DNA. Translation: CAH73556.1.
AL137860, AL590640 Genomic DNA. Translation: CAI22089.1.
AL137860, AL590640 Genomic DNA. Translation: CAI22090.1.
CH471059 Genomic DNA. Translation: EAX07773.1.
CH471059 Genomic DNA. Translation: EAX07774.1.
BC012121 mRNA. Translation: AAH12121.1.

IPI

IPI00020060.
IPI00644335.

PIR

I57487.

RefSeq

NP_003038.2. NM_003047.3.

UniGene

Hs.469116.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1Y4E	NMR	-	A	155-180	[»]
2BEC	X-ray	2.70	B	503-545	[»]
2E30	NMR	-	B	503-545	[»]
2HTG	NMR	-	A	250-274	[»]
2KBV	NMR	-	A	447-472	[»]
2L0E	NMR	-	A	226-250	[»]
2YGG	X-ray	2.23	A	622-689	[»]

ProteinModelPortal

P19634.

SMR

P19634. Positions 155-180, 250-275, 338-365, 447-472, 503-545, 622-685.

ModBase

Search...

Protein-protein interaction databases

IntAct

P19634. 4 interactions.

MINT

MINT-194742.

STRING

P19634.

PTM databases

PhosphoSite

P19634.

Polymorphism databases

DMDM

127809.

Proteomic databases

PRIDE

P19634.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263980; ENSP00000263980; ENSG00000090020.

GeneID

6548.

KEGG

hsa:6548.

UCSC

uc001bnm.1. human.
uc001bnn.1. human.

Organism-specific databases

CTD

6548.

GeneCards

GC01M027425.

H-InvDB

HIX0000320.

HGNC

HGNC:11071. SLC9A1.

HPA

CAB022371.

MIM

107310. gene.

neXtProt

NX_P19634.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG14086.

HOGENOM

HBG444842.

HOVERGEN

HBG052615.

InParanoid

P19634.

OMA

IMISTTL.

OrthoDB

EOG4FR0R9.

PhylomeDB

P19634.

Enzyme and pathway databases

Pathway_Interaction_DB

endothelinpathway. Endothelins.
p38alphabetadownstreampathway. Signaling mediated by p38-alpha and p38-beta.

Reactome

REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpress

P19634.

Bgee

P19634.

CleanEx

HS_SLC9A1.

Genevestigator

P19634.

GermOnline

ENSG00000090020. Homo sapiens.

Family and domain databases

InterPro

IPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR001970. Na/H_exchanger_1.
IPR004709. NaH_exchanger.
[Graphical view]

KO

K05742.

PANTHER

PTHR10110. Cation/H_exchanger_cons-reg. 1 hit.

Pfam

PF00999. Na_H_Exchanger. 1 hit.
[Graphical view]

PRINTS

PR01084. NAHEXCHNGR.
PR01085. NAHEXCHNGR1.

TIGRFAMs

TIGR00840. B_cpa1. 1 hit.

ProtoNet

Search...

Other

DrugBank

DB00594. Amiloride.

NextBio

25485.

SOURCE

Search...

Entry information

Entry name

SL9A1_HUMAN

Accession

Primary (citable) accession number: P19634
Secondary accession number(s): B1ALD6, D3DPL4, Q96EM2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	November 1, 1991
Last modified:	January 25, 2012
This is version 134 of the entry and version 2 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.