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Q9UHC3

- ASIC3_HUMAN

UniProt

Q9UHC3 - ASIC3_HUMAN

Protein

Acid-sensing ion channel 3

Gene

ASIC3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (13 Sep 2005)
      Previous versions | rss
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    Functioni

    Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Generates a biphasic current with a fast inactivating and a slow sustained phase. In sensory neurons is proposed to mediate the pain induced by acidosis that occurs in ischemic, damaged or inflamed tissue. May be involved in hyperalgesia. May play a role in mechanoreception. Heteromeric channel assembly seems to modulate channel properties.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei26 – 261Potassium ion selectivity and permeabilityBy similarity

    GO - Molecular functioni

    1. cation channel activity Source: ProtInc
    2. enterobactin transporter activity Source: Ensembl
    3. ligand-gated sodium channel activity Source: Ensembl
    4. sodium channel activity Source: ProtInc

    GO - Biological processi

    1. detection of chemical stimulus involved in sensory perception of pain Source: Ensembl
    2. detection of mechanical stimulus involved in sensory perception of pain Source: Ensembl
    3. detection of temperature stimulus involved in sensory perception of pain Source: Ensembl
    4. ion transmembrane transport Source: Reactome
    5. response to acid chemical Source: Ensembl
    6. response to heat Source: Ensembl
    7. sensory perception Source: ProtInc
    8. sensory perception of sour taste Source: UniProt
    9. signal transduction Source: ProtInc
    10. sodium ion transmembrane transport Source: GOC
    11. transmembrane transport Source: Reactome
    12. transport Source: ProtInc

    Keywords - Molecular functioni

    Ion channel, Sodium channel

    Keywords - Biological processi

    Ion transport, Sodium transport, Transport

    Keywords - Ligandi

    Sodium

    Enzyme and pathway databases

    ReactomeiREACT_160189. Stimuli-sensing channels.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Acid-sensing ion channel 3
    Short name:
    ASIC3
    Short name:
    hASIC3
    Alternative name(s):
    Amiloride-sensitive cation channel 3
    Neuronal amiloride-sensitive cation channel 3
    Testis sodium channel 1
    Short name:
    hTNaC1
    Gene namesi
    Name:ASIC3
    Synonyms:ACCN3, SLNAC1, TNAC1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:101. ASIC3.

    Subcellular locationi

    Cell membrane By similarity; Multi-pass membrane protein By similarity. Cytoplasm By similarity
    Note: Cell surface expression may be stabilized by interaction with LIN7B and cytoplasmic retention by interaction with DLG4. In part cytoplasmic in cochlea cells By similarity.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. integral component of plasma membrane Source: ProtInc
    3. plasma membrane Source: Reactome

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi528 – 5281V → A: No effect on interaction with LIN7B, MAGI1 and GOPC. 1 Publication
    Mutagenesisi529 – 5291T → A: Loss of interaction with LIN7B, MAGI1. 1 Publication
    Mutagenesisi530 – 5301Q → A: Loss of interaction with GOPC. No effect on interaction LIN7B and MAGI1. 1 Publication
    Mutagenesisi531 – 5311L → A: Loss of interaction with LIN7B, MAGI1 and GOPC. 1 Publication

    Organism-specific databases

    PharmGKBiPA24435.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 531531Acid-sensing ion channel 3PRO_0000181301Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi92 ↔ 186By similarity
    Disulfide bondi164 ↔ 171By similarity
    Glycosylationi175 – 1751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi282 ↔ 370By similarity
    Disulfide bondi315 ↔ 366By similarity
    Disulfide bondi319 ↔ 364By similarity
    Disulfide bondi328 ↔ 350By similarity
    Disulfide bondi330 ↔ 342By similarity
    Glycosylationi398 – 3981N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Phosphorylated by PKA. Phosphorylated by PKC. In vitro, PRKCABP/PICK-1 is necessary for PKC phosphorylation and activation of a ASIC3/ACCN3-ASIC2/ASIC2b channel, but does not activate a homomeric ASIC3 channel By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiQ9UHC3.
    PRIDEiQ9UHC3.

    PTM databases

    PhosphoSiteiQ9UHC3.

    Expressioni

    Tissue specificityi

    Expressed by sensory neurons. Strongly expressed in brain, spinal chord, lung, lymph nodes, kidney, pituitary, heart and testis.2 Publications

    Developmental stagei

    Expressed in fetal tissues, expression increases in lung and kidney adult tissues.1 Publication

    Gene expression databases

    ArrayExpressiQ9UHC3.
    BgeeiQ9UHC3.
    CleanExiHS_ACCN3.
    GenevestigatoriQ9UHC3.

    Organism-specific databases

    HPAiHPA049155.

    Interactioni

    Subunit structurei

    Homotrimer or heterotrimer with other ASIC proteins By similarity. Interacts with STOM; this regulates channel activity. Interacts with DLG4 By similarity. Interacts with LIN7B, MAGI1/BAIAP1, GOPC and ASIC2.By similarity2 Publications

    Protein-protein interaction databases

    BioGridi114723. 7 interactions.
    STRINGi9606.ENSP00000297512.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UHC3.
    SMRiQ9UHC3. Positions 52-456.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 4343CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini62 – 441380ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini461 – 53171CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei44 – 6118HelicalSequence AnalysisAdd
    BLAST
    Transmembranei442 – 46019HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi528 – 5314PDZ-binding

    Domaini

    The PDZ domain-binding motif is involved in interaction with LIN7A, GOPC and MAGI1.

    Sequence similaritiesi

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG262945.
    HOVERGENiHBG004150.
    KOiK04830.
    OMAiKDACACP.
    OrthoDBiEOG72VH5P.
    PhylomeDBiQ9UHC3.
    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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UHC3-1) [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

    MKPTSGPEEA RRPASDIRVF ASNCSMHGLG HVFGPGSLSL RRGMWAAAVV    50
    LSVATFLYQV AERVRYYREF HHQTALDERE SHRLIFPAVT LCNINPLRRS 100
    RLTPNDLHWA GSALLGLDPA EHAAFLRALG RPPAPPGFMP SPTFDMAQLY 150
    ARAGHSLDDM LLDCRFRGQP CGPENFTTIF TRMGKCYTFN SGADGAELLT 200
    TTRGGMGNGL DIMLDVQQEE YLPVWRDNEE TPFEVGIRVQ IHSQEEPPII 250
    DQLGLGVSPG YQTFVSCQQQ QLSFLPPPWG DCSSASLNPN YEPEPSDPLG 300
    SPSPSPSPPY TLMGCRLACE TRYVARKCGC RMVYMPGDVP VCSPQQYKNC 350
    AHPAIDAMLR KDSCACPNPC ASTRYAKELS MVRIPSRAAA RFLARKLNRS 400
    EAYIAENVLA LDIFFEALNY ETVEQKKAYE MSELLGDIGG QMGLFIGASL 450
    LTILEILDYL CEVFRDKVLG YFWNRQHSQR HSSTNLLQEG LGSHRTQVPH 500
    LSLGPRPPTP PCAVTKTLSA SHRTCYLVTQ L 531
    Length:531
    Mass (Da):58,905
    Last modified:September 13, 2005 - v2
    Checksum:iA46DD64590EC4871
    GO
    Isoform 2 (identifier: Q9UHC3-2) [UniParc]FASTAAdd to Basket

    Also known as: ASIC3b

    The sequence of this isoform differs from the canonical sequence as follows:
         487-531: LQEGLGSHRT...HRTCYLVTQL → TSHPSLCRHQ...AFPSSPQIKS

    Show »
    Length:543
    Mass (Da):60,332
    Checksum:i9411BD1485BA93F1
    GO
    Isoform 3 (identifier: Q9UHC3-3) [UniParc]FASTAAdd to Basket

    Also known as: ASIC3c

    The sequence of this isoform differs from the canonical sequence as follows:
         506-531: RPPTPPCAVTKTLSASHRTCYLVTQL → STLLCSEDLPPLPVPSPRLSPPPTAPATLSHSSRPAVCVLGAPP

    Show »
    Length:549
    Mass (Da):60,491
    Checksum:iED2C4D628AF9E18F
    GO
    Isoform 4 (identifier: Q9UHC3-4) [UniParc]FASTAAdd to Basket

    Also known as: c

    The sequence of this isoform differs from the canonical sequence as follows:
         356-407: DAMLRKDSCA...NRSEAYIAEN → GRTCWPWTSS...GPACSPSSRS
         408-531: Missing.

    Show »
    Length:407
    Mass (Da):44,999
    Checksum:i0C6D7DCF3F525596
    GO

    Sequence cautioni

    The sequence BAA25897.1 differs from that shown. Reason: Frameshift at positions 303, 305 and 313.
    The sequence BAD92658.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131P → Q in BAA25897. (PubMed:9571199)Curated
    Sequence conflicti13 – 131P → Q in AAC62935. (PubMed:9886053)Curated
    Sequence conflicti14 – 141A → P in AAC62935. (PubMed:9886053)Curated
    Sequence conflicti85 – 851I → V in AAC62935. (PubMed:9886053)Curated
    Sequence conflicti243 – 2442SQ → GH in BAA25897. (PubMed:9571199)Curated
    Sequence conflicti358 – 3581M → I in AAC62935. (PubMed:9886053)Curated
    Sequence conflicti397 – 3971L → F in BAA25897. (PubMed:9571199)Curated
    Sequence conflicti400 – 4001S → R in BAA25897. (PubMed:9571199)Curated
    Sequence conflicti518 – 5181L → F in BAA25897. (PubMed:9571199)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti228 – 2281N → S.
    Corresponds to variant rs1864545 [ dbSNP | Ensembl ].
    VAR_052037

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei356 – 40752DAMLR…YIAEN → GRTCWPWTSSLRPSTMRPWS RRRPMRCQSCLVTLGARWGC SSGPACSPSSRS in isoform 4. 1 PublicationVSP_015600Add
    BLAST
    Alternative sequencei408 – 531124Missing in isoform 4. 1 PublicationVSP_015601Add
    BLAST
    Alternative sequencei487 – 53145LQEGL…LVTQL → TSHPSLCRHQDSLRLPPHLL PCHTALDLLSVSSEPRPDIL DMPSLHVAFPSSPQIKS in isoform 2. 2 PublicationsVSP_015602Add
    BLAST
    Alternative sequencei506 – 53126RPPTP…LVTQL → STLLCSEDLPPLPVPSPRLS PPPTAPATLSHSSRPAVCVL GAPP in isoform 3. 1 PublicationVSP_015603Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010575 mRNA. Translation: BAA25897.1. Frameshift.
    AF095897 mRNA. Translation: AAC64188.1.
    AF057711 mRNA. Translation: AAC62935.1.
    AF195024 mRNA. Translation: AAF19817.1.
    AF195025 mRNA. Translation: AAF19818.1.
    AK313926 mRNA. Translation: BAG36647.1.
    AB209421 mRNA. Translation: BAD92658.1. Different initiation.
    CH471173 Genomic DNA. Translation: EAW54052.1.
    CCDSiCCDS5914.1. [Q9UHC3-2]
    CCDS5915.1. [Q9UHC3-3]
    CCDS5916.1. [Q9UHC3-1]
    PIRiJE0091.
    RefSeqiNP_004760.1. NM_004769.3. [Q9UHC3-1]
    NP_064717.1. NM_020321.3. [Q9UHC3-3]
    NP_064718.1. NM_020322.3. [Q9UHC3-2]
    UniGeneiHs.647113.

    Genome annotation databases

    EnsembliENST00000297512; ENSP00000297512; ENSG00000213199. [Q9UHC3-3]
    ENST00000349064; ENSP00000344838; ENSG00000213199. [Q9UHC3-1]
    ENST00000357922; ENSP00000350600; ENSG00000213199. [Q9UHC3-2]
    ENST00000377904; ENSP00000367136; ENSG00000213199. [Q9UHC3-4]
    ENST00000468325; ENSP00000418605; ENSG00000213199. [Q9UHC3-4]
    GeneIDi9311.
    KEGGihsa:9311.
    UCSCiuc003win.3. human. [Q9UHC3-1]
    uc003wio.3. human. [Q9UHC3-3]
    uc003wip.3. human. [Q9UHC3-2]

    Polymorphism databases

    DMDMi82582992.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB010575 mRNA. Translation: BAA25897.1 . Frameshift.
    AF095897 mRNA. Translation: AAC64188.1 .
    AF057711 mRNA. Translation: AAC62935.1 .
    AF195024 mRNA. Translation: AAF19817.1 .
    AF195025 mRNA. Translation: AAF19818.1 .
    AK313926 mRNA. Translation: BAG36647.1 .
    AB209421 mRNA. Translation: BAD92658.1 . Different initiation.
    CH471173 Genomic DNA. Translation: EAW54052.1 .
    CCDSi CCDS5914.1. [Q9UHC3-2 ]
    CCDS5915.1. [Q9UHC3-3 ]
    CCDS5916.1. [Q9UHC3-1 ]
    PIRi JE0091.
    RefSeqi NP_004760.1. NM_004769.3. [Q9UHC3-1 ]
    NP_064717.1. NM_020321.3. [Q9UHC3-3 ]
    NP_064718.1. NM_020322.3. [Q9UHC3-2 ]
    UniGenei Hs.647113.

    3D structure databases

    ProteinModelPortali Q9UHC3.
    SMRi Q9UHC3. Positions 52-456.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114723. 7 interactions.
    STRINGi 9606.ENSP00000297512.

    Chemistry

    BindingDBi Q9UHC3.
    ChEMBLi CHEMBL5368.
    GuidetoPHARMACOLOGYi 686.

    PTM databases

    PhosphoSitei Q9UHC3.

    Polymorphism databases

    DMDMi 82582992.

    Proteomic databases

    PaxDbi Q9UHC3.
    PRIDEi Q9UHC3.

    Protocols and materials databases

    DNASUi 9311.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297512 ; ENSP00000297512 ; ENSG00000213199 . [Q9UHC3-3 ]
    ENST00000349064 ; ENSP00000344838 ; ENSG00000213199 . [Q9UHC3-1 ]
    ENST00000357922 ; ENSP00000350600 ; ENSG00000213199 . [Q9UHC3-2 ]
    ENST00000377904 ; ENSP00000367136 ; ENSG00000213199 . [Q9UHC3-4 ]
    ENST00000468325 ; ENSP00000418605 ; ENSG00000213199 . [Q9UHC3-4 ]
    GeneIDi 9311.
    KEGGi hsa:9311.
    UCSCi uc003win.3. human. [Q9UHC3-1 ]
    uc003wio.3. human. [Q9UHC3-3 ]
    uc003wip.3. human. [Q9UHC3-2 ]

    Organism-specific databases

    CTDi 9311.
    GeneCardsi GC07P150746.
    HGNCi HGNC:101. ASIC3.
    HPAi HPA049155.
    MIMi 611741. gene.
    neXtProti NX_Q9UHC3.
    PharmGKBi PA24435.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG262945.
    HOVERGENi HBG004150.
    KOi K04830.
    OMAi KDACACP.
    OrthoDBi EOG72VH5P.
    PhylomeDBi Q9UHC3.
    TreeFami TF330663.

    Enzyme and pathway databases

    Reactomei REACT_160189. Stimuli-sensing channels.

    Miscellaneous databases

    GeneWikii ACCN3.
    GenomeRNAii 9311.
    NextBioi 34875.
    PROi Q9UHC3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHC3.
    Bgeei Q9UHC3.
    CleanExi HS_ACCN3.
    Genevestigatori Q9UHC3.

    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. "Molecular cloning of a DEG/ENaC sodium channel cDNA from human testis."
      Ishibashi K., Marumo F.
      Biochem. Biophys. Res. Commun. 245:589-593(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
      Tissue: Testis.
    2. "Identification, functional expression and chromosomal localisation of a sustained human proton-gated cation channel."
      de Weille J.R., Bassilana F., Lazdunski M., Waldmann R.
      FEBS Lett. 433:257-260(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
      Tissue: Embryo.
    3. "Molecular cloning and regional distribution of a human proton receptor subunit with biphasic functional properties."
      Babinski K., Le K.-T., Seguela P.
      J. Neurochem. 72:51-57(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, FUNCTION.
      Tissue: Fetal brain.
    4. "ASIC3b and ASIC3c, new modulatory subunits of the acid sensing ion channel family."
      Renard S., Besnard F., Partiseti M., Graham D.
      Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
    5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    6. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Brain.
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "Mammalian ASIC2a and ASIC3 subunits co-assemble into heteromeric proton-gated channels sensitive to Gd3+."
      Babinski K., Catarsi S., Biagini G., Seguela P.
      J. Biol. Chem. 275:28519-28525(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ASIC1.
    9. "Selective modulation of heteromeric ASIC proton-gated channels by neuropeptide FF."
      Catarsi S., Babinski K., Seguela P.
      Neuropharmacology 41:592-600(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: REGULATION BY NPFF.
    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.
    11. "PSD-95 and Lin-7b interact with acid-sensing ion channel-3 and have opposite effects on H+- gated current."
      Hruska-Hageman A.M., Benson C.J., Leonard A.S., Price M.P., Welsh M.J.
      J. Biol. Chem. 279:46962-46968(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LIN7B; MAGI1 AND GOPC, MUTAGENESIS OF VAL-528; THR-529; GLN-530 AND LEU-531.

    Entry informationi

    Entry nameiASIC3_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHC3
    Secondary accession number(s): B2R9V0
    , O60263, O75906, Q59FN9, Q9UER8, Q9UHC4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 13, 2005
    Last sequence update: September 13, 2005
    Last modified: October 1, 2014
    This is version 115 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

    Potentiated by FMRFamide-related neuropeptides. Sensitized and potentiated by NPSF. Regulated by lactate and Ca2+. Inhibited by anti-inflammatory drugs, like salicylic acid By similarity. Sensitized and potentiated by NPFF.By similarity

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3