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P19634

- SL9A1_HUMAN

UniProt

P19634 - SL9A1_HUMAN

Protein

Sodium/hydrogen exchanger 1

Gene

SLC9A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 163 (01 Oct 2014)
      Sequence version 2 (01 Nov 1991)
      Previous versions | rss
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    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)LengthDescriptionGraphical viewFeature identifierActions
    Sitei161 – 1611Channel pore-liningCurated
    Sitei370 – 3701Not glycosylated

    GO - Molecular functioni

    1. calcium-dependent protein binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. sodium:proton antiporter activity Source: UniProtKB
    4. solute:proton antiporter activity Source: UniProtKB

    GO - Biological processi

    1. carbohydrate metabolic process Source: Reactome
    2. cardiac muscle cell differentiation Source: Ensembl
    3. cell growth Source: Ensembl
    4. cellular response to acidic pH Source: UniProtKB
    5. glycosaminoglycan metabolic process Source: Reactome
    6. hyaluronan catabolic process Source: Reactome
    7. hyaluronan metabolic process Source: Reactome
    8. hydrogen ion transmembrane transport Source: GOC
    9. ion transport Source: Reactome
    10. negative regulation of apoptotic process Source: Ensembl
    11. neuron death Source: Ensembl
    12. positive regulation of action potential Source: Ensembl
    13. positive regulation of cell growth Source: Ensembl
    14. positive regulation of mitochondrial membrane permeability Source: Ensembl
    15. protein oligomerization Source: UniProtKB
    16. regulation of intracellular pH Source: UniProtKB
    17. regulation of pH Source: UniProtKB
    18. regulation of sensory perception of pain Source: Ensembl
    19. regulation of the force of heart contraction Source: Ensembl
    20. response to acid chemical Source: UniProtKB
    21. response to acidic pH Source: UniProtKB
    22. response to drug Source: Ensembl
    23. response to organic cyclic compound Source: Ensembl
    24. small molecule metabolic process Source: Reactome
    25. sodium ion export Source: UniProtKB
    26. transmembrane transport Source: Reactome

    Keywords - Biological processi

    Antiport, Ion transport, Sodium transport, Transport

    Keywords - Ligandi

    Calmodulin-binding, Sodium

    Enzyme and pathway databases

    ReactomeiREACT_120996. Hyaluronan uptake and degradation.
    REACT_19314. Sodium/Proton exchangers.
    SignaLinkiP19634.

    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
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:11071. SLC9A1.

    Subcellular locationi

    Membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane By similarity; Multi-pass membrane protein By similarity. 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.By similarity

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. endoplasmic reticulum Source: UniProtKB
    4. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    5. extracellular vesicular exosome Source: UniProt
    6. integral component of membrane Source: UniProtKB
    7. membrane raft Source: Ensembl
    8. mitochondrion Source: Ensembl
    9. nucleus Source: HPA
    10. plasma membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi155 – 1551F → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi156 – 1561L → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi157 – 1571Q → C: Reduces activity. 1 Publication
    Mutagenesisi158 – 1581S → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi159 – 1591D → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi160 – 1601V → C: Reduces activity. 1 Publication
    Mutagenesisi161 – 1611F → C: Reduces activity. 1 Publication
    Mutagenesisi162 – 1621F → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi163 – 1631L → C: Reduces activity. 1 Publication
    Mutagenesisi164 – 1641F → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi165 – 1651L → C: Reduces activity. 1 Publication
    Mutagenesisi166 – 1661L → C: Reduces activity. 1 Publication
    Mutagenesisi167 – 1671P → A: Reduces activity. 2 Publications
    Mutagenesisi167 – 1671P → C or G: Almost complete loss of activity. Reduces membrane localization. 2 Publications
    Mutagenesisi168 – 1681P → A or C: Almost complete loss of activity. 2 Publications
    Mutagenesisi168 – 1681P → G: Reduces activity. 2 Publications
    Mutagenesisi169 – 1691I → C: Reduces activity. 1 Publication
    Mutagenesisi170 – 1701I → C: Reduces activity. 1 Publication
    Mutagenesisi171 – 1711L → C: Reduces activity. 1 Publication
    Mutagenesisi172 – 1721D → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi173 – 1731A → C: Reduces activity. 1 Publication
    Mutagenesisi174 – 1741G → C: Reduces activity. 1 Publication
    Mutagenesisi175 – 1751Y → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi176 – 1761F → C: Almost complete loss of activity. 1 Publication
    Mutagenesisi177 – 1771L → C: Reduces activity. 1 Publication
    Mutagenesisi178 – 1781P → A: No effect.
    Mutagenesisi180 – 1801R → C: Reduces activity. 1 Publication
    Mutagenesisi181 – 1811Q → C: Reduces activity. 1 Publication
    Mutagenesisi518 – 5181I → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-522. 1 Publication
    Mutagenesisi522 – 5221I → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-518. 1 Publication
    Mutagenesisi526 – 5316FLDHLL → QQDHQQ: Inhibits interaction with CHP1 and the exchange activity. CHPI does not localize at the cell membrane. 1 Publication
    Mutagenesisi526 – 5316FLDHLL → RRDHRR: Inhibits interaction with CHP1 and the exchange activity. CHPI does not localize at the cell membrane. 1 Publication
    Mutagenesisi526 – 5261F → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-527. 1 Publication
    Mutagenesisi527 – 5271L → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-526. 1 Publication
    Mutagenesisi530 – 5301L → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-531. 1 Publication
    Mutagenesisi531 – 5311L → Q: Reduces interaction with CHP1 and the exchange activity; when associated with Q-530. 1 Publication
    Mutagenesisi534 – 5341I → D or K: Strongly reduced interaction with CHP2. 1 Publication
    Mutagenesisi537 – 5371I → K: Strongly reduced interaction with CHP2. 1 Publication

    Organism-specific databases

    PharmGKBiPA35928.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 815815Sodium/hydrogen exchanger 1PRO_0000052347Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi75 – 751N-linked (GlcNAc...)1 Publication
    Modified residuei599 – 5991PhosphoserineBy similarity
    Modified residuei605 – 6051PhosphoserineBy similarity
    Modified residuei693 – 6931PhosphoserineBy similarity
    Modified residuei697 – 6971Phosphoserine1 Publication
    Modified residuei703 – 7031Phosphoserine5 Publications
    Modified residuei723 – 7231Phosphoserine1 Publication
    Modified residuei726 – 7261Phosphoserine1 Publication
    Modified residuei729 – 7291Phosphoserine1 Publication
    Modified residuei785 – 7851Phosphoserine1 Publication

    Post-translational modificationi

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

    Keywords - PTMi

    Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP19634.
    PaxDbiP19634.
    PRIDEiP19634.

    PTM databases

    PhosphoSiteiP19634.

    Expressioni

    Tissue specificityi

    Kidney and intestine.

    Gene expression databases

    ArrayExpressiP19634.
    BgeeiP19634.
    CleanExiHS_SLC9A1.
    GenevestigatoriP19634.

    Organism-specific databases

    HPAiCAB022371.
    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

    Protein-protein interaction databases

    BioGridi112438. 14 interactions.
    IntActiP19634. 6 interactions.
    MINTiMINT-194742.
    STRINGi9606.ENSP00000263980.

    Structurei

    Secondary structure

    1
    815
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi162 – 1654
    Helixi171 – 1744
    Helixi177 – 1804
    Helixi231 – 2344
    Helixi239 – 24911
    Helixi448 – 4514
    Turni452 – 4554
    Helixi459 – 47113
    Helixi518 – 53821
    Helixi625 – 65127
    Helixi658 – 68124
    Turni682 – 6843

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1Y4ENMR-A155-180[»]
    2BECX-ray2.70B503-545[»]
    2E30NMR-B503-545[»]
    2HTGNMR-A250-274[»]
    2KBVNMR-A447-472[»]
    2L0ENMR-A226-250[»]
    2YGGX-ray2.23A622-689[»]
    ProteinModelPortaliP19634.
    SMRiP19634. Positions 155-180, 338-365, 447-472, 503-545, 622-685.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP19634.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1212CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini34 – 10572ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini128 – 1292CytoplasmicSequence Analysis
    Topological domaini150 – 1545ExtracellularSequence Analysis
    Topological domaini175 – 19117CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini212 – 22716ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini248 – 2569CytoplasmicSequence Analysis
    Topological domaini277 – 29418ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini316 – 33823CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini359 – 38123ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini403 – 4108ExtracellularSequence Analysis
    Topological domaini431 – 44818CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini471 – 4799ExtracellularSequence Analysis
    Topological domaini500 – 815316CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei382 – 40221Name=H10By similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei13 – 3321Helical; Name=M1Sequence AnalysisAdd
    BLAST
    Transmembranei106 – 12722Helical; Name=M2Sequence AnalysisAdd
    BLAST
    Transmembranei130 – 14920Helical; Name=M3Sequence AnalysisAdd
    BLAST
    Transmembranei155 – 17420Helical; Name=M4Sequence AnalysisAdd
    BLAST
    Transmembranei192 – 21120Helical; Name=M5Sequence AnalysisAdd
    BLAST
    Transmembranei228 – 24720Helical; Name=M6Sequence AnalysisAdd
    BLAST
    Transmembranei257 – 27620Helical; Name=M7Sequence AnalysisAdd
    BLAST
    Transmembranei295 – 31521Helical; Name=M8Sequence AnalysisAdd
    BLAST
    Transmembranei339 – 35820Helical; Name=M9Sequence AnalysisAdd
    BLAST
    Transmembranei411 – 43020Helical; Name=M10Sequence AnalysisAdd
    BLAST
    Transmembranei449 – 47022Helical; Name=M11Sequence AnalysisAdd
    BLAST
    Transmembranei480 – 49920Helical; Name=M12Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni516 – 53924Interaction with CHP2Add
    BLAST

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0025.
    HOGENOMiHOG000247044.
    HOVERGENiHBG052615.
    InParanoidiP19634.
    KOiK05742.
    OMAiQDWISAV.
    OrthoDBiEOG7XWPN4.
    PhylomeDBiP19634.
    TreeFamiTF317212.

    Family and domain databases

    InterProiIPR006153. Cation/H_exchanger.
    IPR018422. Cation/H_exchanger_CPA1.
    IPR001970. Na/H_exchanger_1.
    IPR004709. NaH_exchanger.
    [Graphical view]
    PANTHERiPTHR10110. PTHR10110. 1 hit.
    PfamiPF00999. Na_H_Exchanger. 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. Align

    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

    MVLRSGICGL SPHRIFPSLL VVVALVGLLP VLRSHGLQLS PTASTIRSSE    50
    PPRERSIGDV TTAPPEVTPE SRPVNHSVTD HGMKPRKAFP VLGIDYTHVR 100
    TPFEISLWIL LACLMKIGFH VIPTISSIVP ESCLLIVVGL LVGGLIKGVG 150
    ETPPFLQSDV FFLFLLPPII LDAGYFLPLR QFTENLGTIL IFAVVGTLWN 200
    AFFLGGLMYA VCLVGGEQIN NIGLLDNLLF GSIISAVDPV AVLAVFEEIH 250
    INELLHILVF GESLLNDAVT VVLYHLFEEF ANYEHVGIVD IFLGFLSFFV 300
    VALGGVLVGV VYGVIAAFTS RFTSHIRVIE PLFVFLYSYM AYLSAELFHL 350
    SGIMALIASG VVMRPYVEAN ISHKSHTTIK YFLKMWSSVS ETLIFIFLGV 400
    STVAGSHHWN WTFVISTLLF CLIARVLGVL GLTWFINKFR IVKLTPKDQF 450
    IIAYGGLRGA IAFSLGYLLD KKHFPMCDLF LTAIITVIFF TVFVQGMTIR 500
    PLVDLLAVKK KQETKRSINE EIHTQFLDHL LTGIEDICGH YGHHHWKDKL 550
    NRFNKKYVKK CLIAGERSKE PQLIAFYHKM EMKQAIELVE SGGMGKIPSA 600
    VSTVSMQNIH PKSLPSERIL PALSKDKEEE IRKILRNNLQ KTRQRLRSYN 650
    RHTLVADPYE EAWNQMLLRR QKARQLEQKI NNYLTVPAHK LDSPTMSRAR 700
    IGSDPLAYEP KEDLPVITID PASPQSPESV DLVNEELKGK VLGLSRDPAK 750
    VAEEDEDDDG GIMMRSKETS SPGTDDVFTP APSDSPSSQR IQRCLSDPGP 800
    HPEPGEGEPF FPKGQ 815
    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)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti682 – 6821N → K.
    Corresponds to variant rs35703140 [ dbSNP | Ensembl ].
    VAR_050231

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei496 – 55459GMTIR…LNRFN → VLGQGRAGPCLGDPHRLFPW KERKACDLKCDSSPSSTTNL LCDLGRATPPFWASVSSIVK in isoform 2. 1 PublicationVSP_022101Add
    BLAST
    Alternative sequencei555 – 815261Missing in isoform 2. 1 PublicationVSP_022102Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    Hs.91389.

    Genome annotation databases

    EnsembliENST00000263980; ENSP00000263980; ENSG00000090020. [P19634-1]
    ENST00000374086; ENSP00000363199; ENSG00000090020. [P19634-2]
    GeneIDi6548.
    KEGGihsa:6548.
    UCSCiuc001bnm.4. human. [P19634-1]
    uc001bnn.3. human. [P19634-2]

    Polymorphism databases

    DMDMi127809.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS295.1. [P19634-1 ]
    PIRi I57487.
    RefSeqi NP_003038.2. NM_003047.4. [P19634-1 ]
    UniGenei Hs.469116.
    Hs.91389.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    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 [» ]
    ProteinModelPortali P19634.
    SMRi P19634. Positions 155-180, 338-365, 447-472, 503-545, 622-685.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 112438. 14 interactions.
    IntActi P19634. 6 interactions.
    MINTi MINT-194742.
    STRINGi 9606.ENSP00000263980.

    Chemistry

    BindingDBi P19634.
    ChEMBLi CHEMBL2781.
    DrugBanki DB00594. Amiloride.

    Protein family/group databases

    TCDBi 2.A.36.1.13. the monovalent cation:proton antiporter-1 (cpa1) family.

    PTM databases

    PhosphoSitei P19634.

    Polymorphism databases

    DMDMi 127809.

    Proteomic databases

    MaxQBi P19634.
    PaxDbi P19634.
    PRIDEi P19634.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000263980 ; ENSP00000263980 ; ENSG00000090020 . [P19634-1 ]
    ENST00000374086 ; ENSP00000363199 ; ENSG00000090020 . [P19634-2 ]
    GeneIDi 6548.
    KEGGi hsa:6548.
    UCSCi uc001bnm.4. human. [P19634-1 ]
    uc001bnn.3. human. [P19634-2 ]

    Organism-specific databases

    CTDi 6548.
    GeneCardsi GC01M027425.
    HGNCi HGNC:11071. SLC9A1.
    HPAi CAB022371.
    HPA052891.
    MIMi 107310. gene.
    neXtProti NX_P19634.
    PharmGKBi PA35928.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0025.
    HOGENOMi HOG000247044.
    HOVERGENi HBG052615.
    InParanoidi P19634.
    KOi K05742.
    OMAi QDWISAV.
    OrthoDBi EOG7XWPN4.
    PhylomeDBi P19634.
    TreeFami TF317212.

    Enzyme and pathway databases

    Reactomei REACT_120996. Hyaluronan uptake and degradation.
    REACT_19314. Sodium/Proton exchangers.
    SignaLinki P19634.

    Miscellaneous databases

    ChiTaRSi SLC9A1. human.
    EvolutionaryTracei P19634.
    GeneWikii Sodium%E2%80%93hydrogen_antiporter_1.
    GenomeRNAii 6548.
    NextBioi 25485.
    PROi P19634.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P19634.
    Bgeei P19634.
    CleanExi HS_SLC9A1.
    Genevestigatori P19634.

    Family and domain databases

    InterProi IPR006153. Cation/H_exchanger.
    IPR018422. Cation/H_exchanger_CPA1.
    IPR001970. Na/H_exchanger_1.
    IPR004709. NaH_exchanger.
    [Graphical view ]
    PANTHERi PTHR10110. PTHR10110. 1 hit.
    Pfami PF00999. Na_H_Exchanger. 1 hit.
    [Graphical view ]
    PRINTSi PR01084. NAHEXCHNGR.
    PR01085. NAHEXCHNGR1.
    TIGRFAMsi TIGR00840. b_cpa1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. 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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT ASN-75, O-LINKED GLYCOSYLATION.
    10. "Coimmunoprecipitation of a 24-kDa protein with NHE1, the ubiquitous isoform of the Na+/H+ exchanger."
      Goss G., Orlowski J., Grinstein S.
      Am. J. Physiol. 270:C1493-C1502(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHP1.
    11. "A calcineurin homologous protein inhibits GTPase-stimulated Na-H exchange."
      Lin X., Barber D.L.
      Proc. Natl. Acad. Sci. U.S.A. 93:12631-12636(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PH REGULATION, INTERACTION WITH CHP1.
    12. "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] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY.
    13. "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] [Europe PMC] [Abstract]
      Cited for: TOPOLOGY, MUTAGENESIS OF ARG-180 AND GLN-181.
    14. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TESC, SUBCELLULAR LOCATION.
    15. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHP1, MUTAGENESIS OF ILE-518; ILE-522; PHE-526; LEU-527; LEU-530; LEU-531 AND 526-PHE--LEU-531.
    16. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHP2.
    17. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TESC AND CALMODULIN.
    18. "Role of calcineurin B homologous protein in pH regulation by the Na+/H+ exchanger 1: tightly bound Ca2+ ions as important structural elements."
      Pang T., Hisamitsu T., Mori H., Shigekawa M., Wakabayashi S.
      Biochemistry 43:3628-3636(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PH REGULATION, INTERACTION WITH CHP1, SUBCELLULAR LOCATION.
    19. "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] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF PRO-167 AND PRO-168.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    21. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Platelet.
    22. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-697; SER-703; SER-723; SER-726; SER-729 AND SER-785, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    23. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    24. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      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.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    25. "Nuclear accumulation of calcineurin B homologous protein 2 (CHP2) results in enhanced proliferation of tumor cells."
      Li Q.H., Wang L.H., Lin Y.N., Chang G.Q., Li H.W., Jin W.N., Hu R.H., Pang T.X.
      Genes Cells 16:416-426(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CHP2, SUBCELLULAR LOCATION.
    26. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-703, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    27. "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] [Europe PMC] [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.
    28. "Crystallization and preliminary crystallographic analysis of the human calcineurin homologous protein CHP2 bound to the cytoplasmic region of the Na+/H+ exchanger NHE1."
      Ben Ammar Y., Takeda S., Sugawara M., Miyano M., Mori H., Wakabayashi S.
      Acta Crystallogr. F 61:956-958(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PRELIMINARY X-RAY CRYSTALLOGRAPHY OF 503-545 IN COMPLEX WITH CHP2.
    29. "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] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 503-545 IN COMPLEX WITH CHP2, MUTAGENESIS OF ILE-534 AND ILE-537.
    30. "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] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 503-545 IN COMPLEX WITH CHP1.

    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: October 1, 2014
    This is version 163 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.

    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

    External Data

    Dasty 3