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P78348

- ASIC1_HUMAN

UniProt

P78348 - ASIC1_HUMAN

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Protein

Acid-sensing ion channel 1

Gene
ASIC1, ACCN2, BNAC2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.2 Publications
Isoform 1 does not display proton-gated cation channel activity.2 Publications

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 gating By similarity
Sitei79 – 791Important for channel desensitizing By similarity
Sitei287 – 2871Important for channel gating By 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 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4545Cytoplasmic By similarityAdd
BLAST
Transmembranei46 – 6924Helical; By similarityAdd
BLAST
Topological domaini70 – 427358Extracellular By similarityAdd
BLAST
Transmembranei428 – 45427Discontinuously helical; By similarityAdd
BLAST
Topological domaini455 – 52874Cytoplasmic By similarityAdd
BLAST

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
Complete GO annotation...

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 ↔ 194 By similarity
Disulfide bondi172 ↔ 179 By similarity
Disulfide bondi290 ↔ 367 By similarity
Disulfide bondi310 ↔ 363 By similarity
Disulfide bondi314 ↔ 361 By similarity
Disulfide bondi323 ↔ 345 By similarity
Disulfide bondi325 ↔ 337 By similarity
Glycosylationi368 – 3681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi395 – 3951N-linked (GlcNAc...) Reviewed prediction
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.

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 1.3 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.

Family & Domainsi

Motif

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

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.

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

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. VSP_045298Add
BLAST
Alternative sequencei433 – 4331G → GELLMTPVPFSCHGHGVAPY HPKAGCSLLSHEGPPPQRPF PKPCCLG in isoform 1. VSP_015596

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121G → D in AAB48980. 1 Publication
Sequence conflicti212 – 2121G → D in AAB48981. 1 Publication

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

EnsembliENST00000228468; ENSP00000228468; ENSG00000110881. [P78348-1]
ENST00000447966; ENSP00000400228; ENSG00000110881. [P78348-2]
ENST00000552438; ENSP00000450247; ENSG00000110881. [P78348-3]
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

Ensembli ENST00000228468 ; ENSP00000228468 ; ENSG00000110881 . [P78348-1 ]
ENST00000447966 ; ENSP00000400228 ; ENSG00000110881 . [P78348-2 ]
ENST00000552438 ; ENSP00000450247 ; ENSG00000110881 . [P78348-3 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 131 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.

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

Dasty 3

Similar proteinsi