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P78348 (ASIC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 130. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ASIC1
Synonyms:ACCN2, BNAC2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length528 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.12

Isoform 1 does not display proton-gated cation channel activity. Ref.2 Ref.12

Enzyme regulation

Inhibited by the diuretic amiloride. Inhibited by Cs1+ ions. Inhibited by spider venom psalmotoxin 1; this locks the channel into its desensitized conformation. Ref.12

Subunit structure

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. Ref.8 Ref.10 Ref.12

Subcellular location

Cell membrane; Multi-pass membrane protein. Note: Localizes in synaptosomes at dendritic synapses of neurons. Colocalizes with DLG4 By similarity. Ref.2 Ref.10 Ref.12

Tissue specificity

Expressed in most or all neurons.

Domain

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.

Post-translational modification

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

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.

Sequence similarities

Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC1 subfamily. [View classification]

Ontologies

Keywords
   Biological processCalcium transport
Ion transport
Sodium transport
Transport
   Cellular componentCell membrane
Membrane
   Coding sequence diversityAlternative splicing
   DomainTransmembrane
Transmembrane helix
   LigandCalcium
Sodium
   Molecular functionIon channel
Sodium channel
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processassociative learning

Inferred from electronic annotation. Source: Ensembl

calcium ion transmembrane transport

Inferred from electronic annotation. Source: Ensembl

cellular response to pH

Inferred from direct assay Ref.12. Source: UniProtKB

ion transmembrane transport

Traceable author statement. Source: Reactome

memory

Inferred from electronic annotation. Source: Ensembl

negative regulation of neurotransmitter secretion

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of membrane potential

Inferred from electronic annotation. Source: Ensembl

response to acid

Inferred from electronic annotation. Source: Ensembl

response to pH

Traceable author statement PubMed 9062189. Source: ProtInc

sensory perception of sour taste

Inferred from mutant phenotype PubMed 19812697. Source: UniProt

signal transduction

Traceable author statement Ref.1. Source: ProtInc

sodium ion transmembrane transport

Inferred from direct assay Ref.12. Source: UniProtKB

sodium ion transport

Non-traceable author statement Ref.1. Source: UniProtKB

transmembrane transport

Traceable author statement. Source: Reactome

transport

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

integral component of plasma membrane

Inferred from mutant phenotype Ref.12. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

synapse

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionacid-sensing ion channel activity

Inferred from direct assay Ref.12. Source: UniProtKB

ion gated channel activity

Inferred from electronic annotation. Source: Ensembl

ligand-gated sodium channel activity

Traceable author statement PubMed 9062189. Source: ProtInc

protein binding

Inferred from physical interaction Ref.8. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PICK1Q9NRD53EBI-79189,EBI-79165

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Isoform 1 (identifier: P78348-1)

The sequence of this isoform differs from the canonical sequence as follows:
     433-433: G → GELLMTPVPFSCHGHGVAPYHPKAGCSLLSHEGPPPQRPFPKPCCLG
Isoform 3 (identifier: P78348-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 528528Acid-sensing ion channel 1
PRO_0000181294

Regions

Topological domain1 – 4545Cytoplasmic By similarity
Transmembrane46 – 6924Helical; By similarity
Topological domain70 – 427358Extracellular By similarity
Transmembrane428 – 45427Discontinuously helical; By similarity
Topological domain455 – 52874Cytoplasmic By similarity
Motif444 – 4463Selectivity filter Probable

Sites

Site711Important for channel gating By similarity
Site791Important for channel desensitizing By similarity
Site2871Important for channel gating By similarity

Amino acid modifications

Modified residue4791Phosphoserine; by PKA Ref.10
Glycosylation3681N-linked (GlcNAc...) Potential
Glycosylation3951N-linked (GlcNAc...) Potential
Disulfide bond93 ↔ 194 By similarity
Disulfide bond172 ↔ 179 By similarity
Disulfide bond290 ↔ 367 By similarity
Disulfide bond310 ↔ 363 By similarity
Disulfide bond314 ↔ 361 By similarity
Disulfide bond323 ↔ 345 By similarity
Disulfide bond325 ↔ 337 By similarity

Natural variations

Alternative sequence1 – 185185MELKA…AEDFK → MPIQIFCSMSFSSGEEAPGP LGDIWGPHHHQQQQDISESE EEEEEKEKEAVRKEASEGHS PMDLVAFANSCTLHGTNHIF VEGGPGPRQVLWAVAFVLAL GAFLCQVGDRVAYYLSYPHV TLLNEVATTELAFPAVTLCN TNAVRLSQLSYPDLLYLAPM LGLDESDDPGVPLAPPGPEA FSGEPFNLHRFYNRSCHRLE DMLLYCSYQGGPCGPHNFS in isoform 3.
VSP_045298
Alternative sequence4331G → GELLMTPVPFSCHGHGVAPY HPKAGCSLLSHEGPPPQRPF PKPCCLG in isoform 1.
VSP_015596

Experimental info

Mutagenesis4781S → A: No effect on phosphorylation. Ref.10
Mutagenesis4791S → A: Loss of phosphorylation. Ref.10
Sequence conflict2121G → D in AAB48980. Ref.1
Sequence conflict2121G → D in AAB48981. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 2 (Asic1a) [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: 9E998F711C208450

FASTA52859,909
        10         20         30         40         50         60 
MELKAEEEEV GGVQPVSIQA FASSSTLHGL AHIFSYERLS LKRALWALCF LGSLAVLLCV 

        70         80         90        100        110        120 
CTERVQYYFH YHHVTKLDEV AASQLTFPAV TLCNLNEFRF SQVSKNDLYH AGELLALLNN 

       130        140        150        160        170        180 
RYEIPDTQMA DEKQLEILQD KANFRSFKPK PFNMREFYDR AGHDIRDMLL SCHFRGEVCS 

       190        200        210        220        230        240 
AEDFKVVFTR YGKCYTFNSG RDGRPRLKTM KGGTGNGLEI MLDIQQDEYL PVWGETDETS 

       250        260        270        280        290        300 
FEAGIKVQIH SQDEPPFIDQ LGFGVAPGFQ TFVACQEQRL IYLPPPWGTC KAVTMDSDLD 

       310        320        330        340        350        360 
FFDSYSITAC RIDCETRYLV ENCNCRMVHM PGDAPYCTPE QYKECADPAL DFLVEKDQEY 

       370        380        390        400        410        420 
CVCEMPCNLT RYGKELSMVK IPSKASAKYL AKKFNKSEQY IGENILVLDI FFEVLNYETI 

       430        440        450        460        470        480 
EQKKAYEIAG LLGDIGGQMG LFIGASILTV LELFDYAYEV IKHKLCRRGK CQKEAKRSSA 

       490        500        510        520 
DKGVALSLDD VKRHNPCESL RGHPAGMTYA ANILPHHPAR GTFEDFTC 

« Hide

Isoform 1 [UniParc].

Checksum: 04B7E51DF15F90BF
Show »

FASTA57464,783
Isoform 3 [UniParc].

Checksum: 0EC8183120C02EC4
Show »

FASTA56262,700

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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]"Protein kinase C isoform antagonism controls BNaC2 (ASIC1) function."
Berdiev B.K., Xia J., Jovov B., Markert J.M., Mapstone T.B., Gillespie G.Y., Fuller C.M., Bubien J.K., Benos D.J.
J. Biol. Chem. 277:45734-45740(2002) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS44876.1. [P78348-2]
CCDS58228.1. [P78348-3]
CCDS8796.1. [P78348-1]
RefSeqNP_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]
UniGeneHs.274361.

3D structure databases

ProteinModelPortalP78348.
SMRP78348. Positions 40-462.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106559. 4 interactions.
IntActP78348. 1 interaction.
STRING9606.ENSP00000228468.

Chemistry

BindingDBP78348.
ChEMBLCHEMBL1628477.
DrugBankDB00594. Amiloride.
GuidetoPHARMACOLOGY684.

Polymorphism databases

DMDM296439456.

Proteomic databases

PaxDbP78348.
PRIDEP78348.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000228468; ENSP00000228468; ENSG00000110881. [P78348-1]
ENST00000447966; ENSP00000400228; ENSG00000110881. [P78348-2]
ENST00000552438; ENSP00000450247; ENSG00000110881. [P78348-3]
GeneID41.
KEGGhsa:41.
UCSCuc001rvv.4. human. [P78348-1]
uc001rvw.4. human. [P78348-2]
uc021qxr.2. human.

Organism-specific databases

CTD41.
GeneCardsGC12P050452.
HGNCHGNC:100. ASIC1.
MIM602866. gene.
neXtProtNX_P78348.
PharmGKBPA24434.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG262945.
HOGENOMHOG000247010.
HOVERGENHBG004150.
KOK04829.
OMAIQYYFLY.
OrthoDBEOG72VH5P.
PhylomeDBP78348.
TreeFamTF330663.

Enzyme and pathway databases

ReactomeREACT_15518. Transmembrane transport of small molecules.
SignaLinkP78348.

Gene expression databases

ArrayExpressP78348.
BgeeP78348.
CleanExHS_ACCN2.
GenevestigatorP78348.

Family and domain databases

InterProIPR004724. EnaC.
IPR001873. Na+channel_ASC.
IPR020903. Na+channel_ASC_CS.
[Graphical view]
PANTHERPTHR11690. PTHR11690. 1 hit.
PfamPF00858. ASC. 1 hit.
[Graphical view]
PRINTSPR01078. AMINACHANNEL.
TIGRFAMsTIGR00859. ENaC. 1 hit.
PROSITEPS01206. ASC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiACCN2.
GenomeRNAi41.
NextBio167.
PROP78348.
SOURCESearch...

Entry information

Entry nameASIC1_HUMAN
AccessionPrimary (citable) accession number: P78348
Secondary accession number(s): A3KN86 expand/collapse secondary AC list , E5KBL7, P78349, Q96CV2
Entry history
Integrated into UniProtKB/Swiss-Prot: December 5, 2001
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM