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Protein

Sodium/hydrogen exchanger 1

Gene

SLC9A1

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

Functioni

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.3 Publications

pH dependencei

Fully active at acidic pHs, the antiporter is virtually turned off at neutral pH.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei161Channel pore-liningCurated1

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate binding Source: BHF-UCL
  • potassium:proton antiporter activity Source: GO_Central
  • protein binding, bridging Source: BHF-UCL
  • protein complex scaffold Source: BHF-UCL
  • protein phosphatase 2B binding Source: BHF-UCL
  • sodium:proton antiporter activity Source: UniProtKB
  • sodium:proton antiporter activity involved in regulation of cardiac muscle cell membrane potential Source: BHF-UCL
  • solute:proton antiporter activity Source: UniProtKB

GO - Biological processi

  • cardiac muscle cell contraction Source: Ensembl
  • cardiac muscle cell differentiation Source: Ensembl
  • cell growth Source: Ensembl
  • cell migration Source: BHF-UCL
  • cellular response to acidic pH Source: UniProtKB
  • cellular response to antibiotic Source: Ensembl
  • cellular response to electrical stimulus Source: Ensembl
  • cellular response to epinephrine stimulus Source: BHF-UCL
  • cellular response to hypoxia Source: Ensembl
  • cellular response to insulin stimulus Source: Ensembl
  • cellular response to mechanical stimulus Source: BHF-UCL
  • cellular sodium ion homeostasis Source: BHF-UCL
  • hyaluronan catabolic process Source: Reactome
  • hydrogen ion transmembrane transport Source: BHF-UCL
  • ion transport Source: Reactome
  • maintenance of cell polarity Source: BHF-UCL
  • negative regulation of apoptotic process Source: Ensembl
  • neuron death Source: Ensembl
  • positive regulation of action potential Source: Ensembl
  • positive regulation of apoptotic process Source: Ensembl
  • positive regulation of calcineurin-NFAT signaling cascade Source: BHF-UCL
  • positive regulation of calcium:sodium antiporter activity Source: BHF-UCL
  • positive regulation of cardiac muscle hypertrophy Source: BHF-UCL
  • positive regulation of cell growth Source: Ensembl
  • positive regulation of mitochondrial membrane permeability Source: Ensembl
  • positive regulation of NFAT protein import into nucleus Source: BHF-UCL
  • positive regulation of the force of heart contraction Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • potassium ion transmembrane transport Source: GO_Central
  • protein oligomerization Source: UniProtKB
  • regulation of cardiac muscle cell membrane potential Source: BHF-UCL
  • regulation of cardiac muscle contraction by calcium ion signaling Source: BHF-UCL
  • regulation of focal adhesion assembly Source: BHF-UCL
  • regulation of intracellular pH Source: UniProtKB
  • regulation of pH Source: UniProtKB
  • regulation of sensory perception of pain Source: Ensembl
  • regulation of stress fiber assembly Source: BHF-UCL
  • regulation of the force of heart contraction by cardiac conduction Source: BHF-UCL
  • response to acidic pH Source: UniProtKB
  • response to drug Source: Ensembl
  • response to muscle stretch Source: BHF-UCL
  • sodium ion export Source: UniProtKB
  • sodium ion import across plasma membrane Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Antiport, Ion transport, Sodium transport, Transport

Keywords - Ligandi

Calmodulin-binding, Sodium

Enzyme and pathway databases

BioCyciZFISH:ENSG00000090020-MONOMER.
ReactomeiR-HSA-2160916. Hyaluronan uptake and degradation.
R-HSA-425986. Sodium/Proton exchangers.
SignaLinkiP19634.
SIGNORiP19634.

Protein family/group databases

TCDBi2.A.36.1.13. the monovalent cation:proton antiporter-1 (cpa1) family.

Names & Taxonomyi

Protein namesi
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 namesi
Name:SLC9A1
Synonyms:APNH1, NHE1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:11071. SLC9A1.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
Transmembranei13 – 33Helical; Name=M1Sequence analysisAdd BLAST21
Topological domaini34 – 105ExtracellularSequence analysisAdd BLAST72
Transmembranei106 – 127Helical; Name=M2Sequence analysisAdd BLAST22
Topological domaini128 – 129CytoplasmicSequence analysis2
Transmembranei130 – 149Helical; Name=M3Sequence analysisAdd BLAST20
Topological domaini150 – 154ExtracellularSequence analysis5
Transmembranei155 – 174Helical; Name=M4Sequence analysisAdd BLAST20
Topological domaini175 – 191CytoplasmicSequence analysisAdd BLAST17
Transmembranei192 – 211Helical; Name=M5Sequence analysisAdd BLAST20
Topological domaini212 – 227ExtracellularSequence analysisAdd BLAST16
Transmembranei228 – 247Helical; Name=M6Sequence analysisAdd BLAST20
Topological domaini248 – 256CytoplasmicSequence analysis9
Transmembranei257 – 276Helical; Name=M7Sequence analysisAdd BLAST20
Topological domaini277 – 294ExtracellularSequence analysisAdd BLAST18
Transmembranei295 – 315Helical; Name=M8Sequence analysisAdd BLAST21
Topological domaini316 – 338CytoplasmicSequence analysisAdd BLAST23
Transmembranei339 – 358Helical; Name=M9Sequence analysisAdd BLAST20
Topological domaini359 – 381ExtracellularSequence analysisAdd BLAST23
Intramembranei382 – 402Name=H10By similarityAdd BLAST21
Topological domaini403 – 410ExtracellularSequence analysis8
Transmembranei411 – 430Helical; Name=M10Sequence analysisAdd BLAST20
Topological domaini431 – 448CytoplasmicSequence analysisAdd BLAST18
Transmembranei449 – 470Helical; Name=M11Sequence analysisAdd BLAST22
Topological domaini471 – 479ExtracellularSequence analysis9
Transmembranei480 – 499Helical; Name=M12Sequence analysisAdd BLAST20
Topological domaini500 – 815CytoplasmicSequence analysisAdd BLAST316

GO - Cellular componenti

  • apical plasma membrane Source: Ensembl
  • basolateral plasma membrane Source: Ensembl
  • cation-transporting ATPase complex Source: BHF-UCL
  • cell surface Source: Ensembl
  • cytoplasm Source: UniProtKB
  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • integral component of membrane Source: UniProtKB
  • integral component of plasma membrane Source: BHF-UCL
  • intercalated disc Source: Ensembl
  • lamellipodium Source: BHF-UCL
  • membrane raft Source: BHF-UCL
  • mitochondrion Source: Ensembl
  • nucleoplasm Source: HPA
  • perinuclear region of cytoplasm Source: Ensembl
  • plasma membrane Source: UniProtKB
  • T-tubule Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Involvement in diseasei

Lichtenstein-Knorr syndrome (LIKNS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive neurologic disorder characterized by progressive cerebellar ataxia and severe progressive sensorineural hearing loss.
See also OMIM:616291
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073439305G → R in LIKNS; causes reduced expression of the mutant protein; hypoglycosylated; does not localize properly at the plasma membrane; small residual activity. 1 PublicationCorresponds to variant rs786204831dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi155F → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi156L → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi157Q → C: Reduces activity. 1 Publication1
Mutagenesisi158S → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi159D → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi160V → C: Reduces activity. 1 Publication1
Mutagenesisi161F → C: Reduces activity. 1 Publication1
Mutagenesisi162F → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi163L → C: Reduces activity. 1 Publication1
Mutagenesisi164F → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi165L → C: Reduces activity. 1 Publication1
Mutagenesisi166L → C: Reduces activity. 1 Publication1
Mutagenesisi167P → A: Reduces activity. 2 Publications1
Mutagenesisi167P → C or G: Almost complete loss of activity. Reduces membrane localization. 2 Publications1
Mutagenesisi168P → A or C: Almost complete loss of activity. 2 Publications1
Mutagenesisi168P → G: Reduces activity. 2 Publications1
Mutagenesisi169I → C: Reduces activity. 1 Publication1
Mutagenesisi170I → C: Reduces activity. 1 Publication1
Mutagenesisi171L → C: Reduces activity. 1 Publication1
Mutagenesisi172D → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi173A → C: Reduces activity. 1 Publication1
Mutagenesisi174G → C: Reduces activity. 1 Publication1
Mutagenesisi175Y → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi176F → C: Almost complete loss of activity. 1 Publication1
Mutagenesisi177L → C: Reduces activity. 1 Publication1
Mutagenesisi178P → A: No effect. 1
Mutagenesisi180R → C: Reduces activity. 1 Publication1
Mutagenesisi181Q → C: Reduces activity. 1 Publication1
Mutagenesisi518I → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-522. 1 Publication1
Mutagenesisi522I → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-518. 1 Publication1
Mutagenesisi526 – 531FLDHLL → QQDHQQ: Inhibits interaction with CHP1 and the exchange activity. CHPI does not localize at the cell membrane. 1 Publication6
Mutagenesisi526 – 531FLDHLL → RRDHRR: Inhibits interaction with CHP1 and the exchange activity. CHPI does not localize at the cell membrane. 1 Publication6
Mutagenesisi526F → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-527. 1 Publication1
Mutagenesisi527L → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-526. 1 Publication1
Mutagenesisi530L → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-531. 1 Publication1
Mutagenesisi531L → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-530. 1 Publication1
Mutagenesisi534I → D or K: Strongly reduced interaction with CHP2. 1 Publication1
Mutagenesisi537I → K: Strongly reduced interaction with CHP2. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation, Neurodegeneration

Organism-specific databases

DisGeNETi6548.
MIMi616291. phenotype.
OpenTargetsiENSG00000090020.
PharmGKBiPA35928.

Chemistry databases

ChEMBLiCHEMBL2781.
DrugBankiDB00594. Amiloride.

Polymorphism and mutation databases

BioMutaiSLC9A1.
DMDMi127809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000523471 – 815Sodium/hydrogen exchanger 1Add BLAST815

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi75N-linked (GlcNAc...)1 Publication1
Modified residuei599PhosphoserineCombined sources1
Modified residuei602PhosphoserineCombined sources1
Modified residuei603PhosphothreonineBy similarity1
Modified residuei605PhosphoserineCombined sources1
Modified residuei693PhosphoserineCombined sources1
Modified residuei697PhosphoserineCombined sources1
Modified residuei703PhosphoserineCombined sources1
Modified residuei723PhosphoserineCombined sources1
Modified residuei726PhosphoserineCombined sources1
Modified residuei729PhosphoserineCombined sources1
Modified residuei785PhosphoserineCombined sources1
Modified residuei787PhosphoserineBy similarity1
Modified residuei796PhosphoserineBy similarity1

Post-translational modificationi

O-glycosylated.1 Publication
Ubiquitinated, leading to its degradation by the proteasome. Ubiquitination is reduced by CHP1 (By similarity).By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei370Not glycosylated1

Keywords - PTMi

Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP19634.
MaxQBiP19634.
PaxDbiP19634.
PeptideAtlasiP19634.
PRIDEiP19634.

PTM databases

iPTMnetiP19634.
PhosphoSitePlusiP19634.

Expressioni

Tissue specificityi

Kidney and intestine.

Gene expression databases

BgeeiENSG00000090020.
CleanExiHS_SLC9A1.
ExpressionAtlasiP19634. baseline and differential.
GenevisibleiP19634. HS.

Organism-specific databases

HPAiCAB022371.
HPA048532.
HPA052891.

Interactioni

Subunit structurei

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.By similarity10 Publications

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • protein binding, bridging Source: BHF-UCL
  • protein complex scaffold Source: BHF-UCL
  • protein phosphatase 2B binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi112438. 37 interactors.
IntActiP19634. 13 interactors.
MINTiMINT-194742.
STRINGi9606.ENSP00000263980.

Chemistry databases

BindingDBiP19634.

Structurei

Secondary structure

1815
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi162 – 165Combined sources4
Helixi171 – 174Combined sources4
Helixi177 – 180Combined sources4
Helixi231 – 234Combined sources4
Helixi239 – 249Combined sources11
Turni252 – 254Combined sources3
Turni256 – 258Combined sources3
Helixi259 – 269Combined sources11
Turni271 – 273Combined sources3
Helixi448 – 451Combined sources4
Turni452 – 455Combined sources4
Helixi459 – 471Combined sources13
Helixi518 – 538Combined sources21
Helixi625 – 651Combined sources27
Helixi658 – 681Combined sources24
Turni682 – 684Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y4ENMR-A155-180[»]
2BECX-ray2.70B503-545[»]
2E30NMR-B503-545[»]
2HTGNMR-A250-274[»]
2KBVNMR-A447-472[»]
2L0ENMR-A226-250[»]
2MDFNMR-A226-274[»]
2YGGX-ray2.23A622-689[»]
ProteinModelPortaliP19634.
SMRiP19634.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19634.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni516 – 539Interaction with CHP2Add BLAST24

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1966. Eukaryota.
COG0025. LUCA.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000247044.
HOVERGENiHBG052615.
InParanoidiP19634.
KOiK05742.
OMAiKPIMIST.
OrthoDBiEOG091G02Q0.
PhylomeDBiP19634.
TreeFamiTF317212.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR001970. Na/H_exchanger_1.
IPR004709. NaH_exchanger.
IPR032103. NHE_CaM-bd.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 1 hit.
PTHR10110:SF59. PTHR10110:SF59. 1 hit.
PfamiPF00999. Na_H_Exchanger. 1 hit.
PF16644. NEXCaM_BD. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01085. NAHEXCHNGR1.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P19634-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MVLRSGICGL SPHRIFPSLL VVVALVGLLP VLRSHGLQLS PTASTIRSSE
60 70 80 90 100
PPRERSIGDV TTAPPEVTPE SRPVNHSVTD HGMKPRKAFP VLGIDYTHVR
110 120 130 140 150
TPFEISLWIL LACLMKIGFH VIPTISSIVP ESCLLIVVGL LVGGLIKGVG
160 170 180 190 200
ETPPFLQSDV FFLFLLPPII LDAGYFLPLR QFTENLGTIL IFAVVGTLWN
210 220 230 240 250
AFFLGGLMYA VCLVGGEQIN NIGLLDNLLF GSIISAVDPV AVLAVFEEIH
260 270 280 290 300
INELLHILVF GESLLNDAVT VVLYHLFEEF ANYEHVGIVD IFLGFLSFFV
310 320 330 340 350
VALGGVLVGV VYGVIAAFTS RFTSHIRVIE PLFVFLYSYM AYLSAELFHL
360 370 380 390 400
SGIMALIASG VVMRPYVEAN ISHKSHTTIK YFLKMWSSVS ETLIFIFLGV
410 420 430 440 450
STVAGSHHWN WTFVISTLLF CLIARVLGVL GLTWFINKFR IVKLTPKDQF
460 470 480 490 500
IIAYGGLRGA IAFSLGYLLD KKHFPMCDLF LTAIITVIFF TVFVQGMTIR
510 520 530 540 550
PLVDLLAVKK KQETKRSINE EIHTQFLDHL LTGIEDICGH YGHHHWKDKL
560 570 580 590 600
NRFNKKYVKK CLIAGERSKE PQLIAFYHKM EMKQAIELVE SGGMGKIPSA
610 620 630 640 650
VSTVSMQNIH PKSLPSERIL PALSKDKEEE IRKILRNNLQ KTRQRLRSYN
660 670 680 690 700
RHTLVADPYE EAWNQMLLRR QKARQLEQKI NNYLTVPAHK LDSPTMSRAR
710 720 730 740 750
IGSDPLAYEP KEDLPVITID PASPQSPESV DLVNEELKGK VLGLSRDPAK
760 770 780 790 800
VAEEDEDDDG GIMMRSKETS SPGTDDVFTP APSDSPSSQR IQRCLSDPGP
810
HPEPGEGEPF FPKGQ
Length:815
Mass (Da):90,763
Last modified:November 1, 1991 - v2
Checksum:i02EC748C79DF6526
GO
Isoform 2 (identifier: P19634-2) [UniParc]FASTAAdd to basket

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.
Show »
Length:555
Mass (Da):61,013
Checksum:i961A4B1AEDEA68A5
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073439305G → R in LIKNS; causes reduced expression of the mutant protein; hypoglycosylated; does not localize properly at the plasma membrane; small residual activity. 1 PublicationCorresponds to variant rs786204831dbSNPEnsembl.1
Natural variantiVAR_050231682N → K.Corresponds to variant rs35703140dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_022101496 – 554GMTIR…LNRFN → VLGQGRAGPCLGDPHRLFPW KERKACDLKCDSSPSSTTNL LCDLGRATPPFWASVSSIVK in isoform 2. 1 PublicationAdd BLAST59
Alternative sequenceiVSP_022102555 – 815Missing in isoform 2. 1 PublicationAdd BLAST261

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS295.1. [P19634-1]
PIRiI57487.
RefSeqiNP_003038.2. NM_003047.4. [P19634-1]
UniGeneiHs.469116.

Genome annotation databases

EnsembliENST00000263980; ENSP00000263980; ENSG00000090020. [P19634-1]
ENST00000374086; ENSP00000363199; ENSG00000090020. [P19634-2]
GeneIDi6548.
KEGGihsa:6548.
UCSCiuc001bnm.5. human. [P19634-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS295.1. [P19634-1]
PIRiI57487.
RefSeqiNP_003038.2. NM_003047.4. [P19634-1]
UniGeneiHs.469116.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1Y4ENMR-A155-180[»]
2BECX-ray2.70B503-545[»]
2E30NMR-B503-545[»]
2HTGNMR-A250-274[»]
2KBVNMR-A447-472[»]
2L0ENMR-A226-250[»]
2MDFNMR-A226-274[»]
2YGGX-ray2.23A622-689[»]
ProteinModelPortaliP19634.
SMRiP19634.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi112438. 37 interactors.
IntActiP19634. 13 interactors.
MINTiMINT-194742.
STRINGi9606.ENSP00000263980.

Chemistry databases

BindingDBiP19634.
ChEMBLiCHEMBL2781.
DrugBankiDB00594. Amiloride.

Protein family/group databases

TCDBi2.A.36.1.13. the monovalent cation:proton antiporter-1 (cpa1) family.

PTM databases

iPTMnetiP19634.
PhosphoSitePlusiP19634.

Polymorphism and mutation databases

BioMutaiSLC9A1.
DMDMi127809.

Proteomic databases

EPDiP19634.
MaxQBiP19634.
PaxDbiP19634.
PeptideAtlasiP19634.
PRIDEiP19634.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000263980; ENSP00000263980; ENSG00000090020. [P19634-1]
ENST00000374086; ENSP00000363199; ENSG00000090020. [P19634-2]
GeneIDi6548.
KEGGihsa:6548.
UCSCiuc001bnm.5. human. [P19634-1]

Organism-specific databases

CTDi6548.
DisGeNETi6548.
GeneCardsiSLC9A1.
HGNCiHGNC:11071. SLC9A1.
HPAiCAB022371.
HPA048532.
HPA052891.
MIMi107310. gene.
616291. phenotype.
neXtProtiNX_P19634.
OpenTargetsiENSG00000090020.
PharmGKBiPA35928.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1966. Eukaryota.
COG0025. LUCA.
GeneTreeiENSGT00760000119074.
HOGENOMiHOG000247044.
HOVERGENiHBG052615.
InParanoidiP19634.
KOiK05742.
OMAiKPIMIST.
OrthoDBiEOG091G02Q0.
PhylomeDBiP19634.
TreeFamiTF317212.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000090020-MONOMER.
ReactomeiR-HSA-2160916. Hyaluronan uptake and degradation.
R-HSA-425986. Sodium/Proton exchangers.
SignaLinkiP19634.
SIGNORiP19634.

Miscellaneous databases

ChiTaRSiSLC9A1. human.
EvolutionaryTraceiP19634.
GeneWikiiSodium%E2%80%93hydrogen_antiporter_1.
GenomeRNAii6548.
PROiP19634.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000090020.
CleanExiHS_SLC9A1.
ExpressionAtlasiP19634. baseline and differential.
GenevisibleiP19634. HS.

Family and domain databases

InterProiIPR006153. Cation/H_exchanger.
IPR018422. Cation/H_exchanger_CPA1.
IPR001970. Na/H_exchanger_1.
IPR004709. NaH_exchanger.
IPR032103. NHE_CaM-bd.
[Graphical view]
PANTHERiPTHR10110. PTHR10110. 1 hit.
PTHR10110:SF59. PTHR10110:SF59. 1 hit.
PfamiPF00999. Na_H_Exchanger. 1 hit.
PF16644. NEXCaM_BD. 1 hit.
[Graphical view]
PRINTSiPR01084. NAHEXCHNGR.
PR01085. NAHEXCHNGR1.
TIGRFAMsiTIGR00840. b_cpa1. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiSL9A1_HUMAN
AccessioniPrimary (citable) accession number: P19634
Secondary accession number(s): B1ALD6, D3DPL4, Q96EM2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: November 1, 1991
Last modified: November 2, 2016
This is version 185 of the entry and version 2 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

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.

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.Curated
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.Curated
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.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.