Asic2

Functionⁱ

Cation channel with high affinity for sodium, which is gated by extracellular protons and inhibited by the diuretic amiloride. Also permeable for Li⁺ and K⁺. Activation by an extracellular pH drop is followed by a rapid pH-independent inactivation. Heteromeric channel assembly seems to modulate channel properties.3 Publications

Miscellaneous

Regulated by Zn²⁺. Inhibited by anti-inflammatory drugs like salicylic acid.

GO - Molecular functionⁱ

ion channel activity
Source: RGD
Inferred from direct assayⁱ
- 14976185
ligand-gated sodium channel activity Source: InterPro
voltage-gated sodium channel activity
Source: RGD
Inferred from direct assayⁱ
- 9368048

Complete GO annotation...

GO - Biological processⁱ

Complete GO annotation...

Keywordsⁱ

Molecular function	Ion channel, Sodium channel
Biological process	Ion transport, Sodium transport, Transport
Ligand	Sodium

Protein family/group databases

TCDBⁱ	1.A.6.1.2. the epithelial na(+) channel (enac) family.

TCDBⁱ

1.A.6.1.2. the epithelial na(+) channel (enac) family.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Acid-sensing ion channel 2 Short name: ASIC2 Alternative name(s): Amiloride-sensitive brain sodium channel Amiloride-sensitive brain sodium channel 2 Amiloride-sensitive cation channel 1, neuronal Amiloride-sensitive cation channel neuronal 1 Brain sodium channel 1 Short name: BNC1 Short name: BNaC1 Mammalian degenerin homolog1 Publication Short name: MDEG1 Publication
Gene namesⁱ	Name:Asic2 Synonyms:Accn1, Bnac1, Mdeg
Organismⁱ	Rattus norvegicus (Rat)
Taxonomic identifierⁱ	10116 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus
Proteomesⁱ	UP000002494 Componentⁱ: Unplaced

Organism-specific databases

Rat genome database More...RGDⁱ	2017. Asic2.

RGDⁱ

2017. Asic2.

Subcellular locationⁱ

Cell membrane
2 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "Functional implications of the localization and activity of acid-sensitive channels in rat peripheral nervous system."
  Alvarez de la Rosa D., Zhang P., Shao D., White F., Canessa C.M.
  Proc. Natl. Acad. Sci. U.S.A. 99:2326-2331(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
- Ref.9
  "A stomatin dimer modulates the activity of acid-sensing ion channels."
  Brand J., Smith E.S., Schwefel D., Lapatsina L., Poole K., Omerbasic D., Kozlenkov A., Behlke J., Lewin G.R., Daumke O.
  EMBO J. 31:3635-3646(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH STOM, SUBCELLULAR LOCATION.
; Multi-pass membrane protein
2 Publications
Manual assertion based on experiment inⁱ
- Ref.6
  "Functional implications of the localization and activity of acid-sensitive channels in rat peripheral nervous system."
  Alvarez de la Rosa D., Zhang P., Shao D., White F., Canessa C.M.
  Proc. Natl. Acad. Sci. U.S.A. 99:2326-2331(2002) [PubMed] [Europe PMC] [Abstract]
  Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
- Ref.9
  "A stomatin dimer modulates the activity of acid-sensing ion channels."
  Brand J., Smith E.S., Schwefel D., Lapatsina L., Poole K., Omerbasic D., Kozlenkov A., Behlke J., Lewin G.R., Daumke O.
  EMBO J. 31:3635-3646(2012) [PubMed] [Europe PMC] [Abstract]
  Cited for: FUNCTION, INTERACTION WITH STOM, SUBCELLULAR LOCATION.

Note:

Localized at the plasma membrane of neurons, in the soma and punctated peripheral processes.

Topology

Feature key	Position(s)	DescriptionActions	Length
Topological domainⁱ	1 – 37	Cytoplasmic1 PublicationAdd BLAST	37
Transmembraneⁱ	38 – 58	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	59 – 427	Extracellular1 PublicationAdd BLAST	369
Transmembraneⁱ	428 – 448	HelicalSequence analysisAdd BLAST	21
Topological domainⁱ	449 – 512	Cytoplasmic1 PublicationAdd BLAST	64

GO - Cellular componentⁱ

integral component of membrane Source: UniProtKB-KW
plasma membrane Source: UniProtKB-SubCell

Complete GO annotation...

Keywords - Cellular componentⁱ

Cell membrane, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	4	K → N: No effect on N-glycosylation. 1 Publication	1
Mutagenesisⁱ	22	N → S: No effect on N-glycosylation. 1 Publication	1
Mutagenesisⁱ	37	P → N: No effect on N-glycosylation. 1 Publication	1
Mutagenesisⁱ	63	R → N: No effect on N-glycosylation. 1 Publication	1
Mutagenesisⁱ	67	Y → N: No effect on N-glycosylation. 1 Publication	1
Mutagenesisⁱ	72	H → A: Inactive. Active at lower pH; when associated with V-430. 2 Publications	1
Mutagenesisⁱ	72	H → N: Increases N-glycosylation. 2 Publications	1
Mutagenesisⁱ	81	A → N: Increases N-glycosylation. 1 Publication	1
Mutagenesisⁱ	109	H → A: No effect on pH dependence and function. 1 Publication	1
Mutagenesisⁱ	127	H → A: No effect on pH dependence and function. 1 Publication	1
Mutagenesisⁱ	145	H → A: No effect on pH dependence and function. 1 Publication	1
Mutagenesisⁱ	158	H → A: No effect on pH dependence and function. 1 Publication	1
Mutagenesisⁱ	162	H → A: Loss of potentiation by Zn(2+). 1 Publication	1
Mutagenesisⁱ	180	H → A: No effect on pH dependence and function. 1 Publication	1
Mutagenesisⁱ	249	H → A: No effect on pH dependence and function. 1 Publication	1
Mutagenesisⁱ	326	H → A: No effect on pH dependence and function. 1 Publication	1
Mutagenesisⁱ	339	H → A: Loss of potentiation by Zn(2+). 1 Publication	1
Mutagenesisⁱ	365	N → S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-392. 1 Publication	1
Mutagenesisⁱ	392	N → S: Reduces N-glycosylation. Abolishes N-glycosylation; when associated with S-365. 1 Publication	1
Mutagenesisⁱ	414	Y → N: Increases N-glycosylation. 1 Publication	1
Mutagenesisⁱ	423 – 425	YEV → NES: Increases N-glycosylation. 1 Publication	3
Mutagenesisⁱ	430	G → C: Partial activation. 2 Publications	1
Mutagenesisⁱ	430	G → F: Constitutive activation causing cell death. Inactive; when associated with F-443. 2 Publications	1
Mutagenesisⁱ	430	G → K or T: Constitutive activation causing cell death. 2 Publications	1
Mutagenesisⁱ	430	G → S: No constitutive activation. 2 Publications	1
Mutagenesisⁱ	430	G → V: Constitutive activation causing cell death. Activated at lower pH; when associated with A-72. 2 Publications	1
Mutagenesisⁱ	443	S → F: Loss of function. Inactive; when associated with F-430. 1 Publication	1
Mutagenesisⁱ	453 – 455	YIY → NIS: No effect on N-glycosylation. 1 Publication	3
Mutagenesisⁱ	478	N → S: No effect on N-glycosylation. 1 Publication	1
Mutagenesisⁱ	487	N → S: No effect on N-glycosylation. 1 Publication	1

Chemistry databases

ChEMBLⁱ	CHEMBL3562171.

ChEMBLⁱ

CHEMBL3562171.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000181292	1 – 512	Acid-sensing ion channel 2Add BLAST		512

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	8	PhosphoserineCombined sources	1
Modified residueⁱ	11	PhosphoserineCombined sources	1
Disulfide bondⁱ	92 ↔ 193	By similarity
Disulfide bondⁱ	171 ↔ 178	By similarity
Disulfide bondⁱ	289 ↔ 364	By similarity
Disulfide bondⁱ	307 ↔ 360	By similarity
Disulfide bondⁱ	311 ↔ 358	By similarity
Disulfide bondⁱ	320 ↔ 342	By similarity
Disulfide bondⁱ	322 ↔ 334	By similarity
Glycosylationⁱ	365	N-linked (GlcNAc...) asparagine1 Publication	1
Glycosylationⁱ	392	N-linked (GlcNAc...) asparagine1 Publication	1

Sites

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Siteⁱ	478	Not glycosylated		1
Siteⁱ	487	Not glycosylated		1

Keywords - PTMⁱ

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PRIDEⁱ	Q62962.

PRIDEⁱ

Q62962.

PTM databases

iPTMnetⁱ	Q62962.
PhosphoSitePlusⁱ	Q62962.

Expressionⁱ

Tissue specificityⁱ

Expressed in sciatic nerve and dorsal root ganglion (DRG) (at protein level). Both isoforms display the same expression pattern except in DRG where isoform 2 is more abundantly expressed. Widely distributed throughout the brain. Highly expressed in the main olfactory bulb, neo- and allo-cortical regions, hippocampal formation, habenula, basolateral amygdaloid nuclei, and cerebellum. In the olfactory system, expressed in the glomerular cell layer, the internal granular layer, and the mitral and internal plexiform cell layers. Within the glomerular layer, restricted to the periglomerular cells. In the neocortex, strongly expressed in the large pyramidal neurons in all cortical layers as well as in the oligo-, astro-, or micro-glia cells. In the hippocampal formation, expressed in dentate granule cells and hilar neurons, as well as in pyramidal cells of CA1-CA3 subfields. Expressed in stratum oriens and radiatum of all subfields. Within the thalamus, expressed moderately in the medial and lateral habenula. In the cerebellar cortex expressed in Purkinje cells and granule cells. Expressed at low levels in choroid plexus.4 Publications

Developmental stageⁱ

Appears just before birth, reaches maximum levels after birth, then declines slightly until adulthood.

Inductionⁱ

Up-regulation upon tissues inflammation is abolished by anti-inflammatory drugs.1 Publication

Gene expression databases

Bgeeⁱ	ENSRNOG00000007019.

Bgeeⁱ

ENSRNOG00000007019.

Interactionⁱ

Subunit structureⁱ

Homotrimer or heterotrimer with other ASIC proteins (By similarity). Interacts with PRKCABP (By similarity). Interacts with STOM; this regulates channel activity. Interacts with ASIC1. Isoform 2 interacts with ASIC3. Heterotrimer of Asic1a-Asic2a interacts with the snake venom mambalgin-1, mambalgin-2 and mambalgin-3 (PubMed:23034652, PubMed:23624383). Heterotrimer of Asic1a-Asic2b interacts with the snake venom mambalgin-1 and mambalgin-2 (PubMed:23034652).By similarity4 Publications

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-41193N.
Molecular INTeraction database More...MINTⁱ	MINT-223656.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q62962.
SMRⁱ	Q62962.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the amiloride-sensitive sodium channel (TC 1.A.6) family. ASIC2 subfamily. [View classification]Curated

Keywords - Domainⁱ

Transmembrane, Transmembrane helix

Phylogenomic databases

HOGENOMⁱ	HOG000247010.
HOVERGENⁱ	HBG004150.
InParanoidⁱ	Q62962.
KEGG Orthology (KO) More...KOⁱ	K04828.
PhylomeDBⁱ	Q62962.
TreeFamⁱ	TF330663.

Family and domain databases

InterProⁱ	View protein in InterPro IPR001873. ENaC. IPR004724. ENaC_chordates. IPR020903. ENaC_CS.
PANTHERⁱ	PTHR11690. PTHR11690. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00858. ASC. 1 hit.
PRINTSⁱ	PR01078. AMINACHANNEL.
TIGRFAMsⁱ	TIGR00859. ENaC. 1 hit.
PROSITEⁱ	View protein in PROSITE PS01206. ASC. 1 hit.

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q62962-1) [UniParc]FASTA Add to basket

Also known as: Mdeg11 Publication, Asic2a

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

        10         20         30         40         50
MDLKESPSEG SLQPSSIQIF ANTSTLHGIR HIFVYGPLTI RRVLWAVAFV 
        60         70         80         90        100
GSLGLLLVES SERVSYYFSY QHVTKVDEVV AQSLVFPAVT LCNLNGFRFS 
       110        120        130        140        150
RLTTNDLYHA GELLALLDVN LQIPDPHLAD PTVLEALRQK ANFKHYKPKQ 
       160        170        180        190        200
FSMLEFLHRV GHDLKDMMLY CKFKGQECGH QDFTTVFTKY GKCYMFNSGE 
       210        220        230        240        250
DGKPLLTTVK GGTGNGLEIM LDIQQDEYLP IWGETEETTF EAGVKVQIHS 
       260        270        280        290        300
QSEPPFIQEL GFGVAPGFQT FVATQEQRLT YLPPPWGECR SSEMGLDFFP 
       310        320        330        340        350
VYSITACRID CETRYIVENC NCRMVHMPGD APFCTPEQHK ECAEPALGLL 
       360        370        380        390        400
AEKDSNYCLC RTPCNLTRYN KELSMVKIPS KTSAKYLEKK FNKSEKYISE 
       410        420        430        440        450
NILVLDIFFE ALNYETIEQK KAYEVAALLG DIGGQMGLFI GASLLTILEL 
       460        470        480        490        500
FDYIYELIKE KLLDLLGKEE EEGSHDENMS TCDTMPNHSE TISHTVNVPL 
       510 
QTALGTLEEI AC

Length:512

Mass (Da):57,739

Last modified:November 1, 1997 - v1

Checksum:ⁱ38D0A77C3C430B03

GO

Isoform 2 (identifier: Q62962-2) [UniParc]FASTA Add to basket

Also known as: Mdeg21 Publication, Asic2b

The sequence of this isoform differs from the canonical sequence as follows:
1-184: Missing.
185-185: T → MSRSGGARLP...ELCGPHNFSS

« Hide

        10         20         30         40         50
MSRSGGARLP ATALSGPGRF RMAREQPAPV AVAAARQPGG DRSGDPALQG 
        60         70         80         90        100
PGVARRGRPS LSRTKLHGLR HMCAGRTAAG GSFQRRALWV LAFCTSLGLL 
       110        120        130        140        150
LSWSSNRLLY WLSFPSHTRV HREWSRQLPF PAVTVCNNNP LRFPRLSKGD 
       160        170        180        190        200
LYYAGHWLGL LLPNRTARPL VSELLRGDEP RRQWFRKLAD FRLFLPPRHF 
       210        220        230        240        250
EGISAAFMDR LGHQLEDMLL SCKYRGELCG PHNFSSVFTK YGKCYMFNSG 
       260        270        280        290        300
EDGKPLLTTV KGGTGNGLEI MLDIQQDEYL PIWGETEETT FEAGVKVQIH 
       310        320        330        340        350
SQSEPPFIQE LGFGVAPGFQ TFVATQEQRL TYLPPPWGEC RSSEMGLDFF 
       360        370        380        390        400
PVYSITACRI DCETRYIVEN CNCRMVHMPG DAPFCTPEQH KECAEPALGL 
       410        420        430        440        450
LAEKDSNYCL CRTPCNLTRY NKELSMVKIP SKTSAKYLEK KFNKSEKYIS 
       460        470        480        490        500
ENILVLDIFF EALNYETIEQ KKAYEVAALL GDIGGQMGLF IGASLLTILE 
       510        520        530        540        550
LFDYIYELIK EKLLDLLGKE EEEGSHDENM STCDTMPNHS ETISHTVNVP 
       560 
LQTALGTLEE IAC

Note: Seems to be inactive as monomer or in a monomeric assembly and is not activated by mutagenesis of Gly-430. Mutagenesis of Ser-60 into Gly reduces activation by PKC through PRKCABP/PICK-1 of a ASIC3/ACCN3-ASIC2/ASIC2b channel.

Show »

Length:563

Mass (Da):63,115

Checksum:ⁱDCE1B4A0A45F21E2

GO

Alternative sequence

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Alternative sequenceⁱVSP_015594	1 – 184	Missing in isoform 2. 1 PublicationAdd BLAST		184
Alternative sequenceⁱVSP_015595	185	T → MSRSGGARLPATALSGPGRF RMAREQPAPVAVAAARQPGG DRSGDPALQGPGVARRGRPS LSRTKLHGLRHMCAGRTAAG GSFQRRALWVLAFCTSLGLL LSWSSNRLLYWLSFPSHTRV HREWSRQLPFPAVTVCNNNP LRFPRLSKGDLYYAGHWLGL LLPNRTARPLVSELLRGDEP RRQWFRKLADFRLFLPPRHF EGISAAFMDRLGHQLEDMLL SCKYRGELCGPHNFSS in isoform 2. 1 Publication		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U53211 mRNA. Translation: AAC52588.1. Y14635 mRNA. Translation: CAA74979.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001029186.1. NM_001034014.1. [Q62962-1] NP_037024.2. NM_012892.2. [Q62962-2]
UniGeneⁱ	Rn.37523.

Genome annotation databases

GeneIDⁱ	25364.
KEGGⁱ	rno:25364.

Keywords - Coding sequence diversityⁱ

Alternative splicing

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	U53211 mRNA. Translation: AAC52588.1. Y14635 mRNA. Translation: CAA74979.1.
NCBI Reference Sequences More...RefSeqⁱ	NP_001029186.1. NM_001034014.1. [Q62962-1] NP_037024.2. NM_012892.2. [Q62962-2]
UniGeneⁱ	Rn.37523.

3D structure databases

ProteinModelPortalⁱ	Q62962.
SMRⁱ	Q62962.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

Database of interacting proteins More...DIPⁱ	DIP-41193N.
Molecular INTeraction database More...MINTⁱ	MINT-223656.

Chemistry databases

ChEMBLⁱ	CHEMBL3562171.

ChEMBLⁱ

CHEMBL3562171.

Protein family/group databases

TCDBⁱ	1.A.6.1.2. the epithelial na(+) channel (enac) family.

TCDBⁱ

1.A.6.1.2. the epithelial na(+) channel (enac) family.

PTM databases

iPTMnetⁱ	Q62962.
PhosphoSitePlusⁱ	Q62962.

Proteomic databases

PRIDEⁱ	Q62962.

PRIDEⁱ

Q62962.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	25364.
KEGGⁱ	rno:25364.

Organism-specific databases

CTDⁱ	40.
Rat genome database More...RGDⁱ	2017. Asic2.

Phylogenomic databases

HOGENOMⁱ	HOG000247010.
HOVERGENⁱ	HBG004150.
InParanoidⁱ	Q62962.
KEGG Orthology (KO) More...KOⁱ	K04828.
PhylomeDBⁱ	Q62962.
TreeFamⁱ	TF330663.

Miscellaneous databases

Protein Ontology More...PROⁱ	PR:Q62962.

PROⁱ

PR:Q62962.

Gene expression databases

Bgeeⁱ	ENSRNOG00000007019.

Bgeeⁱ

ENSRNOG00000007019.

Family and domain databases

InterProⁱ	View protein in InterPro IPR001873. ENaC. IPR004724. ENaC_chordates. IPR020903. ENaC_CS.
PANTHERⁱ	PTHR11690. PTHR11690. 1 hit.
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00858. ASC. 1 hit.
PRINTSⁱ	PR01078. AMINACHANNEL.
TIGRFAMsⁱ	TIGR00859. ENaC. 1 hit.
PROSITEⁱ	View protein in PROSITE PS01206. ASC. 1 hit.
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ASIC2_RAT
Accessionⁱ	Q62962Primary (citable) accession number: Q62962 Secondary accession number(s): O55163
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
	Last sequence update:	November 1, 1997
	Last modified:	July 5, 2017
	This is version 133 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q62962 (ASIC2_RAT)

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Acid-sensing ion channel 2

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Protein family/group databases

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Topology

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Chemistry databases

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Sites

Proteomic databases

PTM databases

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

Alternative sequence

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry databases

Protein family/group databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (2)ⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ