A0A5F9ZHW5 · A0A5F9ZHW5_HUMAN

  • Protein
    Ataxin 2
  • Gene
    ATXN2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    1/5

Function

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentcytosol
Molecular FunctionRNA binding

Subcellular Location

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 1,032 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)47PRIDEPhosphoserine
Modified residue (large scale data)53PRIDEPhosphoserine
Modified residue (large scale data)130PRIDEPhosphotyrosine
Modified residue (large scale data)196PRIDEPhosphoserine
Modified residue (large scale data)271PRIDEPhosphoserine
Modified residue (large scale data)306PRIDEPhosphoserine
Modified residue (large scale data)311PRIDEPhosphotyrosine
Modified residue (large scale data)318PRIDEPhosphoserine
Modified residue (large scale data)319PRIDEPhosphoserine
Modified residue (large scale data)353PRIDEPhosphoserine
Modified residue (large scale data)361PRIDEPhosphoserine
Modified residue (large scale data)369PRIDEPhosphothreonine
Modified residue (large scale data)370PRIDEPhosphoserine
Modified residue (large scale data)394PRIDEPhosphoserine
Modified residue (large scale data)398PRIDEPhosphoserine
Modified residue (large scale data)437PRIDEPhosphoserine
Modified residue (large scale data)456PRIDEPhosphoserine
Modified residue (large scale data)457PRIDEPhosphoserine
Modified residue (large scale data)464PRIDEPhosphoserine
Modified residue (large scale data)482PRIDEPhosphoserine
Modified residue (large scale data)500PRIDEPhosphothreonine
Modified residue (large scale data)506PRIDEPhosphothreonine
Modified residue (large scale data)507PRIDEPhosphoserine
Modified residue (large scale data)509PRIDEPhosphoserine
Modified residue (large scale data)512PRIDEPhosphothreonine
Modified residue (large scale data)524PRIDEPhosphoserine
Modified residue (large scale data)549PRIDEPhosphoserine
Modified residue (large scale data)557PRIDEPhosphothreonine
Modified residue (large scale data)568PRIDEPhosphoserine
Modified residue (large scale data)570PRIDEPhosphothreonine
Modified residue (large scale data)573PRIDEPhosphoserine
Modified residue (large scale data)581PRIDEPhosphothreonine
Modified residue (large scale data)583PRIDEPhosphoserine
Modified residue (large scale data)584PRIDEPhosphoserine
Modified residue (large scale data)598PRIDEPhosphoserine
Modified residue (large scale data)611PRIDEPhosphothreonine
Modified residue (large scale data)612PRIDEPhosphoserine
Modified residue (large scale data)614PRIDEPhosphoserine
Modified residue (large scale data)624PRIDEPhosphoserine
Modified residue (large scale data)628PRIDEPhosphoserine
Modified residue (large scale data)694PRIDEPhosphoserine
Modified residue (large scale data)696PRIDEPhosphoserine
Modified residue (large scale data)697PRIDEPhosphoserine
Modified residue (large scale data)701PRIDEPhosphoserine
Modified residue (large scale data)703PRIDEPhosphoserine
Modified residue (large scale data)705PRIDEPhosphoserine
Modified residue (large scale data)728PRIDEPhosphoserine
Modified residue (large scale data)729PRIDEPhosphoserine
Modified residue (large scale data)774PRIDEPhosphothreonine
Modified residue (large scale data)777PRIDEPhosphoserine
Modified residue (large scale data)1053PRIDEPhosphoserine

Proteomic databases

Expression

Gene expression databases

Family & Domains

Features

Showing features for compositional bias, region, domain.

TypeIDPosition(s)Description
Compositional bias1-32Polar residues
Region1-95Disordered
Compositional bias49-72Polar residues
Domain107-184Sm
Compositional bias299-328Basic and acidic residues
Region299-794Disordered
Compositional bias344-385Polar residues
Compositional bias417-442Pro residues
Compositional bias500-521Polar residues
Compositional bias530-547Polar residues
Compositional bias571-621Polar residues
Compositional bias624-643Basic and acidic residues
Compositional bias644-658Polar residues
Compositional bias659-681Basic and acidic residues
Compositional bias682-731Polar residues
Compositional bias732-749Basic and acidic residues
Compositional bias750-772Polar residues
Region977-1059Disordered
Compositional bias990-1035Polar residues
Compositional bias1043-1059Polar residues

Sequence similarities

Belongs to the ataxin-2 family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,178
  • Mass (Da)
    127,220
  • Last updated
    2019-12-11 v1
  • Checksum
    C3B0F3DB3C2216AE
MSLKPQQQQQQQQQQQQQQQQQQQQQQQPPPAAANVRKPGGSGLLASPAAAPSPSSSSVSSSSATAPSSVVAATSGGGRPGLGRGRNSNKGLPQSTISFDGIYANMRMVHILTSVVGSKCEVQVKNGGIYEGVFKTYSPKCDLVLDAAHEKSTESSSGPKREEIMESILFKCSDFVVVQFKDMDSSYAKRDAFTDSAISAKVNGEHKEKDLEPWDAGELTANEELEALENDVSNGWDPNDMFRYNEENYGVVSTYDSSLSSYTVPLERDNSEEFLKREARANQLAEEIESSAQYKARVALENDDRSEEEKYTAVQRNSSEREGHSINTRENKYIPPGQRNREVISWGSGRQNSPRMGQPGSGSMPSRSTSHTSDFNPNSGSDQRVVNGGVPWPSPCPSPSSRPPSRYQSGPNSLPPRAATPTRPPSRPPSRPSRPPSHPSAHGSPAPVSTMPKRMSSEGPPRMSPKAQRHPRNHRVSAGRGSISSGLEFVSHNPPSEAATPPVARTSPSGGTWSSVVSGVPRLSPKTHRPRSPRQNSIGNTPSGPVLASPQAGIIPTEAVAMPIPAASPTPASPASNRAVTPSSEAKDSRLQDQRQNSPAGNKENIKPNETSPSFSKAENKGISPVVSEHRKQIDDLKKFKNDFRLQPSSTSESMDQLLNKNREGEKSRDLIKDKIEPSAKDSFIENSSSNCTSGSSKPNSPSISPSILSNTEHKRGPEVTSQGVQTSSPACKQEKDDKEEKKDAAEQVRKSTLNPNAKEFNPRSFSQPKPSTTPTSPRPQAQPSPSMVGHQQPTPVYTQPVCFAPNMMYPVPVSPGVQPLYPIPMTPMPVNQAKTYRAVPNMPQQRQDQHHQSAMMHPASAAGPPIAATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPTHAQPGLVSSSATQYGAHEQTHAMYACPKLPYNKETSPSFYFAISTGSLAQQYAHPNATLHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQNSFPAAQQTVFTIHPSHVQPAYTNPPHMAHVPQCASEALARCGLEMRLSWIYLSEGYLAHVQSGMVPSHPTAHAPMMLMTTQPPGGPQAALAQSALQPIPVSTTAHFPYMTHPSVQAHHQQQL

Computationally mapped potential isoform sequences

There are 23 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
Q99700ATX2_HUMANATXN21313
A0A2R8Y7P6A0A2R8Y7P6_HUMANATXN2957
A0A2R8Y7E6A0A2R8Y7E6_HUMANATXN21158
A0A2R8Y6W7A0A2R8Y6W7_HUMANATXN2149
A0A2R8Y5A6A0A2R8Y5A6_HUMANATXN21166
A0A2R8YGV1A0A2R8YGV1_HUMANATXN2255
A0A2R8YDM9A0A2R8YDM9_HUMANATXN2968
F8WB05F8WB05_HUMANATXN2424
F8WB06F8WB06_HUMANATXN21087
A0A2R8YCG6A0A2R8YCG6_HUMANATXN2298
H0YH87H0YH87_HUMANATXN2835
F8VZC1F8VZC1_HUMANATXN2196
F8VQP2F8VQP2_HUMANATXN21073
F8VRK6F8VRK6_HUMANATXN2235
F8W0B5F8W0B5_HUMANATXN2908
A0A5F9ZI57A0A5F9ZI57_HUMANATXN21155
A0A5F9ZHX3A0A5F9ZHX3_HUMANATXN21167
A0A5F9ZH85A0A5F9ZH85_HUMANATXN2347
V9GY86V9GY86_HUMANATXN21153
A0A5F9ZHG6A0A5F9ZHG6_HUMANATXN2317
A0A5F9ZHH4A0A5F9ZHH4_HUMANATXN21065
S4R3J6S4R3J6_HUMANATXN2107
S4R3R6S4R3R6_HUMANATXN2119

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias1-32Polar residues
Compositional bias49-72Polar residues
Compositional bias299-328Basic and acidic residues
Compositional bias344-385Polar residues
Compositional bias417-442Pro residues
Compositional bias500-521Polar residues
Compositional bias530-547Polar residues
Compositional bias571-621Polar residues
Compositional bias624-643Basic and acidic residues
Compositional bias644-658Polar residues
Compositional bias659-681Basic and acidic residues
Compositional bias682-731Polar residues
Compositional bias732-749Basic and acidic residues
Compositional bias750-772Polar residues
Compositional bias990-1035Polar residues
Compositional bias1043-1059Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AC002395
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC137055
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF455720
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

Disclaimer

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