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P78348

- ASIC1_HUMAN

UniProt

P78348 - ASIC1_HUMAN

Protein

Acid-sensing ion channel 1

Gene

ASIC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 3 (18 May 2010)
      Previous versions | rss
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    Functioni

    Isoform 2 and isoform 3 function as proton-gated sodium channels; they are activated by a drop of the extracellular pH and then become rapidly desensitized. The channel generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Isoform 2 can also transport potassium, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions. Isoform 3 can also transport calcium ions. Mediates glutamate-independent Ca2+ entry into neurons upon acidosis. This Ca2+ overloading is toxic for cortical neurons and may be in part responsible for ischemic brain injury. Heteromeric channel assembly seems to modulate channel properties. Functions as a postsynaptic proton receptor that influences intracellular Ca2+ concentration and calmodulin-dependent protein kinase II phosphorylation and thereby the density of dendritic spines. Modulates activity in the circuits underlying innate fear.1 Publication
    Isoform 1 does not display proton-gated cation channel activity.1 Publication

    Enzyme regulationi

    Inhibited by the diuretic amiloride. Inhibited by Cs1+ ions. Inhibited by spider venom psalmotoxin 1; this locks the channel into its desensitized conformation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei71 – 711Important for channel gatingBy similarity
    Sitei79 – 791Important for channel desensitizingBy similarity
    Sitei287 – 2871Important for channel gatingBy similarity

    GO - Molecular functioni

    1. acid-sensing ion channel activity Source: UniProtKB
    2. ion gated channel activity Source: Ensembl
    3. ligand-gated sodium channel activity Source: ProtInc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. associative learning Source: Ensembl
    2. calcium ion transmembrane transport Source: Ensembl
    3. cellular response to pH Source: UniProtKB
    4. ion transmembrane transport Source: Reactome
    5. memory Source: Ensembl
    6. negative regulation of neurotransmitter secretion Source: Ensembl
    7. protein homotrimerization Source: UniProtKB
    8. regulation of membrane potential Source: Ensembl
    9. response to acid chemical Source: Ensembl
    10. response to pH Source: ProtInc
    11. sensory perception of sour taste Source: UniProt
    12. signal transduction Source: ProtInc
    13. sodium ion transmembrane transport Source: UniProtKB
    14. sodium ion transport Source: UniProtKB
    15. transmembrane transport Source: Reactome
    16. transport Source: ProtInc

    Keywords - Molecular functioni

    Ion channel, Sodium channel

    Keywords - Biological processi

    Calcium transport, Ion transport, Sodium transport, Transport

    Keywords - Ligandi

    Calcium, Sodium

    Enzyme and pathway databases

    ReactomeiREACT_160189. Stimuli-sensing channels.
    SignaLinkiP78348.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acid-sensing ion channel 1
    Short name:
    ASIC1
    Alternative name(s):
    Amiloride-sensitive cation channel 2, neuronal
    Brain sodium channel 2
    Short name:
    BNaC2
    Gene namesi
    Name:ASIC1
    Synonyms:ACCN2, BNAC2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:100. ASIC1.

    Subcellular locationi

    Cell membrane 3 Publications; Multi-pass membrane protein 3 Publications
    Note: Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4 By similarity.By similarity

    GO - Cellular componenti

    1. cell surface Source: Ensembl
    2. integral component of plasma membrane Source: UniProtKB
    3. plasma membrane Source: Reactome
    4. synapse Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi478 – 4781S → A: No effect on phosphorylation. 1 Publication
    Mutagenesisi479 – 4791S → A: Loss of phosphorylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA24434.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 528528Acid-sensing ion channel 1PRO_0000181294Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi93 ↔ 194By similarity
    Disulfide bondi172 ↔ 179By similarity
    Disulfide bondi290 ↔ 367By similarity
    Disulfide bondi310 ↔ 363By similarity
    Disulfide bondi314 ↔ 361By similarity
    Disulfide bondi323 ↔ 345By similarity
    Disulfide bondi325 ↔ 337By similarity
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi395 – 3951N-linked (GlcNAc...)Sequence Analysis
    Modified residuei479 – 4791Phosphoserine; by PKA1 Publication

    Post-translational modificationi

    Phosphorylation by PKA regulates interaction with PRKCABP and subcellular location. Phosphorylation by PKC may regulate the channel.2 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP78348.
    PRIDEiP78348.

    Expressioni

    Tissue specificityi

    Expressed in most or all neurons.

    Gene expression databases

    ArrayExpressiP78348.
    BgeeiP78348.
    CleanExiHS_ACCN2.
    GenevestigatoriP78348.

    Interactioni

    Subunit structurei

    Homotrimer or heterotrimer with other ASIC proteins By similarity. Interacts with STOM and ASIC2 By similarity. Interacts with PRKCABP. Interacts with spider venom psalmotoxin 1.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PICK1Q9NRD53EBI-79189,EBI-79165

    Protein-protein interaction databases

    BioGridi106559. 4 interactions.
    IntActiP78348. 1 interaction.
    STRINGi9606.ENSP00000228468.

    Structurei

    3D structure databases

    ProteinModelPortaliP78348.
    SMRiP78348. Positions 40-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4545CytoplasmicBy similarityAdd
    BLAST
    Topological domaini70 – 427358ExtracellularBy similarityAdd
    BLAST
    Topological domaini455 – 52874CytoplasmicBy similarityAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei46 – 6924HelicalBy similarityAdd
    BLAST
    Transmembranei428 – 45427Discontinuously helicalBy similarityAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi444 – 4463Selectivity filterCurated

    Domaini

    Channel opening involves a conformation change that affects primarily the extracellular domain and the second transmembrane helix and its orientation in the membrane. In the open state, the second transmembrane helix is nearly perpendicular to the plane of the membrane; in the desensitized state it is strongly tilted. Besides, the second transmembrane domain is discontinuously helical in the open state. The GAS motif of the selectivity filter is in an extended conformation, giving rise to a distinct kink in the polypeptide chain. A domain swap between subunits gives rise to a full-length transmembrane helix By similarity.By similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG262945.
    HOGENOMiHOG000247010.
    HOVERGENiHBG004150.
    KOiK04829.
    OMAiIQYYFLY.
    OrthoDBiEOG72VH5P.
    PhylomeDBiP78348.
    TreeFamiTF330663.

    Family and domain databases

    InterProiIPR004724. EnaC.
    IPR001873. Na+channel_ASC.
    IPR020903. Na+channel_ASC_CS.
    [Graphical view]
    PANTHERiPTHR11690. PTHR11690. 1 hit.
    PfamiPF00858. ASC. 1 hit.
    [Graphical view]
    PRINTSiPR01078. AMINACHANNEL.
    TIGRFAMsiTIGR00859. ENaC. 1 hit.
    PROSITEiPS01206. ASC. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Note: The splice variant from ASIC1a described in mouse and rat, which gives rise to an isoform with different N-termini (Asic1b), does not seem to exist in human.

    Isoform 2 (identifier: P78348-2) [UniParc]FASTAAdd to Basket

    Also known as: Asic1a

    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

    MELKAEEEEV GGVQPVSIQA FASSSTLHGL AHIFSYERLS LKRALWALCF    50
    LGSLAVLLCV CTERVQYYFH YHHVTKLDEV AASQLTFPAV TLCNLNEFRF 100
    SQVSKNDLYH AGELLALLNN RYEIPDTQMA DEKQLEILQD KANFRSFKPK 150
    PFNMREFYDR AGHDIRDMLL SCHFRGEVCS AEDFKVVFTR YGKCYTFNSG 200
    RDGRPRLKTM KGGTGNGLEI MLDIQQDEYL PVWGETDETS FEAGIKVQIH 250
    SQDEPPFIDQ LGFGVAPGFQ TFVACQEQRL IYLPPPWGTC KAVTMDSDLD 300
    FFDSYSITAC RIDCETRYLV ENCNCRMVHM PGDAPYCTPE QYKECADPAL 350
    DFLVEKDQEY CVCEMPCNLT RYGKELSMVK IPSKASAKYL AKKFNKSEQY 400
    IGENILVLDI FFEVLNYETI EQKKAYEIAG LLGDIGGQMG LFIGASILTV 450
    LELFDYAYEV IKHKLCRRGK CQKEAKRSSA DKGVALSLDD VKRHNPCESL 500
    RGHPAGMTYA ANILPHHPAR GTFEDFTC 528
    Length:528
    Mass (Da):59,909
    Last modified:May 18, 2010 - v3
    Checksum:i9E998F711C208450
    GO
    Isoform 1 (identifier: P78348-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         433-433: G → GELLMTPVPFSCHGHGVAPYHPKAGCSLLSHEGPPPQRPFPKPCCLG

    Show »
    Length:574
    Mass (Da):64,783
    Checksum:i04B7E51DF15F90BF
    GO
    Isoform 3 (identifier: P78348-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-185: MELKAEEEEV...GEVCSAEDFK → MPIQIFCSMS...GGPCGPHNFS

    Show »
    Length:562
    Mass (Da):62,700
    Checksum:i0EC8183120C02EC4
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti212 – 2121G → D in AAB48980. (PubMed:9037075)Curated
    Sequence conflicti212 – 2121G → D in AAB48981. (PubMed:9037075)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 185185MELKA…AEDFK → MPIQIFCSMSFSSGEEAPGP LGDIWGPHHHQQQQDISESE EEEEEKEKEAVRKEASEGHS PMDLVAFANSCTLHGTNHIF VEGGPGPRQVLWAVAFVLAL GAFLCQVGDRVAYYLSYPHV TLLNEVATTELAFPAVTLCN TNAVRLSQLSYPDLLYLAPM LGLDESDDPGVPLAPPGPEA FSGEPFNLHRFYNRSCHRLE DMLLYCSYQGGPCGPHNFS in isoform 3. 1 PublicationVSP_045298Add
    BLAST
    Alternative sequencei433 – 4331G → GELLMTPVPFSCHGHGVAPY HPKAGCSLLSHEGPPPQRPF PKPCCLG in isoform 1. 3 PublicationsVSP_015596

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78180 mRNA. Translation: AAB48980.1.
    U78181 mRNA. Translation: AAB48981.1.
    HM991481 mRNA. Translation: ADP44689.1.
    EU078959 mRNA. Translation: ABU48925.1.
    AC025154 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW58118.1.
    BC013891 mRNA. Translation: AAH13891.2.
    BC133707 mRNA. Translation: AAI33708.1.
    CCDSiCCDS44876.1. [P78348-2]
    CCDS58228.1. [P78348-3]
    CCDS8796.1. [P78348-1]
    RefSeqiNP_001086.2. NM_001095.3. [P78348-2]
    NP_001243759.1. NM_001256830.1. [P78348-3]
    NP_064423.2. NM_020039.3. [P78348-1]
    XP_006719460.1. XM_006719397.1. [P78348-2]
    UniGeneiHs.274361.

    Genome annotation databases

    GeneIDi41.
    KEGGihsa:41.
    UCSCiuc001rvv.4. human. [P78348-1]
    uc001rvw.4. human. [P78348-2]
    uc021qxr.2. human.

    Polymorphism databases

    DMDMi296439456.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U78180 mRNA. Translation: AAB48980.1 .
    U78181 mRNA. Translation: AAB48981.1 .
    HM991481 mRNA. Translation: ADP44689.1 .
    EU078959 mRNA. Translation: ABU48925.1 .
    AC025154 Genomic DNA. No translation available.
    CH471111 Genomic DNA. Translation: EAW58118.1 .
    BC013891 mRNA. Translation: AAH13891.2 .
    BC133707 mRNA. Translation: AAI33708.1 .
    CCDSi CCDS44876.1. [P78348-2 ]
    CCDS58228.1. [P78348-3 ]
    CCDS8796.1. [P78348-1 ]
    RefSeqi NP_001086.2. NM_001095.3. [P78348-2 ]
    NP_001243759.1. NM_001256830.1. [P78348-3 ]
    NP_064423.2. NM_020039.3. [P78348-1 ]
    XP_006719460.1. XM_006719397.1. [P78348-2 ]
    UniGenei Hs.274361.

    3D structure databases

    ProteinModelPortali P78348.
    SMRi P78348. Positions 40-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106559. 4 interactions.
    IntActi P78348. 1 interaction.
    STRINGi 9606.ENSP00000228468.

    Chemistry

    BindingDBi P78348.
    ChEMBLi CHEMBL1628477.
    DrugBanki DB00594. Amiloride.
    GuidetoPHARMACOLOGYi 684.

    Polymorphism databases

    DMDMi 296439456.

    Proteomic databases

    PaxDbi P78348.
    PRIDEi P78348.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 41.
    KEGGi hsa:41.
    UCSCi uc001rvv.4. human. [P78348-1 ]
    uc001rvw.4. human. [P78348-2 ]
    uc021qxr.2. human.

    Organism-specific databases

    CTDi 41.
    GeneCardsi GC12P050452.
    HGNCi HGNC:100. ASIC1.
    MIMi 602866. gene.
    neXtProti NX_P78348.
    PharmGKBi PA24434.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262945.
    HOGENOMi HOG000247010.
    HOVERGENi HBG004150.
    KOi K04829.
    OMAi IQYYFLY.
    OrthoDBi EOG72VH5P.
    PhylomeDBi P78348.
    TreeFami TF330663.

    Enzyme and pathway databases

    Reactomei REACT_160189. Stimuli-sensing channels.
    SignaLinki P78348.

    Miscellaneous databases

    GeneWikii ACCN2.
    GenomeRNAii 41.
    NextBioi 167.
    PROi P78348.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P78348.
    Bgeei P78348.
    CleanExi HS_ACCN2.
    Genevestigatori P78348.

    Family and domain databases

    InterProi IPR004724. EnaC.
    IPR001873. Na+channel_ASC.
    IPR020903. Na+channel_ASC_CS.
    [Graphical view ]
    PANTHERi PTHR11690. PTHR11690. 1 hit.
    Pfami PF00858. ASC. 1 hit.
    [Graphical view ]
    PRINTSi PR01078. AMINACHANNEL.
    TIGRFAMsi TIGR00859. ENaC. 1 hit.
    PROSITEi PS01206. ASC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "BNaC1 and BNaC2 constitute a new family of human neuronal sodium channels related to degenerins and epithelial sodium channels."
      Garcia-Anoveros J., Derfler B.H., Neville-Golden J., Hyman B.T., Corey D.P.
      Proc. Natl. Acad. Sci. U.S.A. 94:1459-1464(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Brain.
    2. "Identification of a calcium permeable human acid-sensing ion channel 1 transcript variant."
      Hoagland E.N., Sherwood T.W., Lee K.G., Walker C.J., Askwith C.C.
      J. Biol. Chem. 285:41852-41862(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION (ISOFORMS 1; 2 AND 3), SUBCELLULAR LOCATION.
      Tissue: Spinal ganglion.
    3. "Acid sensing ion channels in human taste tissue."
      Huque T., Cao J., Lischka F.W., Spielman A.I., Feldman R.S., Cowart B.J., Wise P.M., Pribitkin E.A., Mackler S.A., Brand J.G.
      Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    4. "The finished DNA sequence of human chromosome 12."
      Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
      , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
      Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] OF 231-528 (ISOFORM 1).
      Tissue: Ovary.
    7. "Neuropeptide FF and FMRFamide potentiate acid-evoked currents from sensory neurons and proton-gated DEG/ENaC channels."
      Askwith C.C., Cheng C., Ikuma M., Benson C., Price M.P., Welsh M.J.
      Neuron 26:133-141(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGULATION BY FMRFAMIDE-RELATED PEPTIDES.
    8. "Interaction of the synaptic protein PICK1 (protein interacting with C kinase 1) with the non-voltage gated sodium channels BNC1 (brain Na+ channel 1) and ASIC (acid-sensing ion channel)."
      Hruska-Hageman A.M., Wemmie J.A., Price M.P., Welsh M.J.
      Biochem. J. 361:443-450(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRKCABP.
    9. Cited for: PHOSPHORYLATION BY PKC.
    10. "cAMP-dependent protein kinase phosphorylation of the acid-sensing ion channel-1 regulates its binding to the protein interacting with C-kinase-1."
      Leonard A.S., Yermolaieva O., Hruska-Hageman A., Askwith C.C., Price M.P., Wemmie J.A., Welsh M.J.
      Proc. Natl. Acad. Sci. U.S.A. 100:2029-2034(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY PKA, MUTAGENESIS OF SER-478 AND SER-479, PHOSPHORYLATION AT SER-479, INTERACTION WITH PRKCABP, SUBCELLULAR LOCATION.
    11. "Selective regulation of acid-sensing ion channel 1 by serine proteases."
      Poirot O., Vukicevic M., Boesch A., Kellenberger S.
      J. Biol. Chem. 279:38448-38457(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGULATION BY SERINE PROTEASES.
    12. "Structure of the acid-sensing ion channel 1 in complex with the gating modifier Psalmotoxin 1."
      Dawson R.J., Benz J., Stohler P., Tetaz T., Joseph C., Huber S., Schmid G., Hugin D., Pflimlin P., Trube G., Rudolph M.G., Hennig M., Ruf A.
      Nat. Commun. 3:936-936(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SPIDER VENOM PSALMOTOXIN, ENZYME REGULATION.

    Entry informationi

    Entry nameiASIC1_HUMAN
    AccessioniPrimary (citable) accession number: P78348
    Secondary accession number(s): A3KN86
    , E5KBL7, P78349, Q96CV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 5, 2001
    Last sequence update: May 18, 2010
    Last modified: October 1, 2014
    This is version 132 of the entry and version 3 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

    Potentiated by Ca2+, Mg2+, Ba2+ and multivalent cations. Inhibited by anti-inflammatory drugs like salicylic acid By similarity. Potentiated by FMRFamide-related neuropeptides. PH dependence may be regulated by serine proteases.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

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