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Q9ULJ8 · NEB1_HUMAN

  • Protein
    Neurabin-1
  • Gene
    PPP1R9A
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Binds to actin filaments (F-actin) and shows cross-linking activity. Binds along the sides of the F-actin. May be involved in neurite formation. Inhibits protein phosphatase 1-alpha activity (By similarity).

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 Componentactin cytoskeleton
Cellular Componentcortical actin cytoskeleton
Cellular Componentcytoplasm
Cellular Componentdendrite
Cellular Componentdendritic spine
Cellular Componentfilopodium
Cellular Componentpostsynaptic density
Molecular Functionactin filament binding
Biological Processactin filament organization
Biological Processcalcium-mediated signaling
Biological Processmodulation of chemical synaptic transmission
Biological Processneuron projection development

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Neurabin-1
  • Alternative names
    • Neurabin-I
    • Neural tissue-specific F-actin-binding protein I
    • Protein phosphatase 1 regulatory subunit 9A

Gene names

    • Name
      PPP1R9A
    • Synonyms
      KIAA1222

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q9ULJ8
  • Secondary accessions
    • A1L494
    • B2RWQ1
    • E9PCA0
    • E9PCK6
    • E9PDX1

Proteomes

Organism-specific databases

Disease & Variants

Features

Showing features for natural variant.

TypeIDPosition(s)Description
Natural variantVAR_051746331in dbSNP:rs10230714

Variants

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

The viewer provides 1,389 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

Type
IDPosition(s)Source
Description
ChainPRO_00000715071-1098UniProtNeurabin-1
Modified residue (large scale data)131PRIDEPhosphotyrosine
Modified residue (large scale data)160PRIDEPhosphoserine
Modified residue (large scale data)180PRIDEPhosphoserine
Modified residue (large scale data)184PRIDEPhosphoserine
Modified residue (large scale data)185PRIDEPhosphothreonine
Modified residue (large scale data)187PRIDEPhosphoserine
Modified residue (large scale data)190PRIDEPhosphoserine
Modified residue192UniProtPhosphoserine
Modified residue (large scale data)199PRIDEPhosphoserine
Modified residue (large scale data)214PRIDEPhosphoserine
Modified residue (large scale data)228PRIDEPhosphotyrosine
Modified residue (large scale data)288PRIDEPhosphoserine
Modified residue (large scale data)291PRIDEPhosphoserine
Modified residue312UniProtPhosphothreonine
Modified residue (large scale data)334PRIDEPhosphoserine
Modified residue338UniProtPhosphoserine
Modified residue (large scale data)338PRIDEPhosphoserine
Modified residue (large scale data)341PRIDEPhosphoserine
Modified residue371UniProtPhosphoserine
Modified residue (large scale data)371PRIDEPhosphoserine
Modified residue (large scale data)378PRIDEPhosphoserine
Modified residue460UniProtPhosphoserine; by PKA
Modified residue (large scale data)839PRIDEPhosphothreonine
Modified residue840UniProtPhosphoserine
Modified residue (large scale data)840PRIDEPhosphoserine
Modified residue (large scale data)909PRIDEPhosphoserine
Modified residue915UniProtPhosphoserine
Modified residue (large scale data)915PRIDEPhosphoserine
Modified residue928UniProtPhosphoserine
Modified residue956UniProtPhosphoserine
Modified residue957UniProtPhosphoserine
Modified residue960UniProtPhosphoserine
Modified residue974UniProtPhosphoserine

Keywords

Proteomic databases

PTM databases

Expression

Gene expression databases

Organism-specific databases

Interaction

Subunit

Possibly exists as a homodimer, homotrimer or a homotetramer. Interacts with F-actin, protein phosphatase 1 (PP1), neurabin-2 and p70-S6K (By similarity).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY Q9ULJ8RGS2 P412203EBI-2515561, EBI-712388

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for compositional bias, region, domain, coiled coil.

Type
IDPosition(s)Description
Compositional bias1-28Polar residues
Region1-66Disordered
Region1-144Actin-binding
Compositional bias31-53Basic and acidic residues
Region87-117Disordered
Compositional bias97-111Basic and acidic residues
Compositional bias147-170Basic and acidic residues
Region147-213Disordered
Compositional bias174-213Polar residues
Region251-395Disordered
Compositional bias279-295Polar residues
Region425-502Interaction with protein phosphatase 1
Domain504-592PDZ
Coiled coil597-627
Region597-1090Interaction with TGN38
Region627-647Disordered
Compositional bias628-645Acidic residues
Coiled coil670-824
Region839-865Disordered
Compositional bias851-865Polar residues
Region888-952Disordered
Compositional bias922-939Polar residues
Domain988-1051SAM
Coiled coil1033-1090
Compositional bias1051-1087Basic and acidic residues
Region1051-1098Disordered

Domain

Interacts with p70-S6K via its PDZ domain.
The PP1 binding region is natively unstructured, upon PP1 binding, it acquires structure, blocks a substrate-binding site, and restricts PP1 phosphatase specificity to a subset of substrates.

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (5)
  • Sequence status
    Complete

This entry describes 5 isoforms produced by Alternative splicing.

Q9ULJ8-1

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.

  • Name
    1
  • Synonyms
    Long
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Length
    1,098
  • Mass (Da)
    123,342
  • Last updated
    2004-07-19 v2
  • MD5 Checksum
    0F89A3CA86591B2DEE5ABC332AF043E5
MLKTESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKSDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPNENAAVIAKTRGKGGHSSPQRRMKPKEFLEKTDGSVVKLESSVSERISRFDTMYDGPSYSKFTETRKMFERSVHESGQNNRYSPKKEKAGGSEPQDEWGGSKSNRGSTDSLDSLSSRTEAVSPTVSQLSAVFENTDSPSAIISEKAENNEYSVTGHYPLNLPSVTVTNLDTFGHLKDSNSWPPSNKRGVDTEDAHKSNATPVPEVASKSTSLASIPGEEIQQSKEPEDSTSNQQTPDSIDKDGPEEPCAESKAMPKSEIPSPQSQLLEDAEANLVGREAAKQQRKELAGGDFTSPDASASSCGKEVPEDSNNFDGSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEEEDSDENSYYQPDMEYSEIVGLPEEEEIPANRKIKFSSAPIKVFNTYSNEDYDRRNDEVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLEQHYAQYDADDDETGEYATDEEEDEVGPVLPGSDMAIEVFELPENEDMFSPSELDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKTQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIKRQEAERKKIEDLEKAHLVEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRTSLGEVSKGDTMENLDGKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPSRTRLYDSVSSTDGEDSLERKNFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDESLDMIDDEILDDGQSPKHSQCQNRAVQEWSVQQVSHWLMSLNLEQYVSEFSAQNITGEQLLQLDGNKLKALGMTASQDRAVVKKKLKEMKMSLEKARKAQEKMEKQREKLRRKEQEQMQRKSKKTEKMTSTTAEGAGEQ

Q9ULJ8-2

  • Name
    2
  • Synonyms
    Short
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 1-918: MLKTESSGERTTLRSASPHRNAYRTEFQALKSTFDKPKSDGEQKTKEGEGSQQSRGRKYGSNVNRIKNLFMQMGMEPNENAAVIAKTRGKGGHSSPQRRMKPKEFLEKTDGSVVKLESSVSERISRFDTMYDGPSYSKFTETRKMFERSVHESGQNNRYSPKKEKAGGSEPQDEWGGSKSNRGSTDSLDSLSSRTEAVSPTVSQLSAVFENTDSPSAIISEKAENNEYSVTGHYPLNLPSVTVTNLDTFGHLKDSNSWPPSNKRGVDTEDAHKSNATPVPEVASKSTSLASIPGEEIQQSKEPEDSTSNQQTPDSIDKDGPEEPCAESKAMPKSEIPSPQSQLLEDAEANLVGREAAKQQRKELAGGDFTSPDASASSCGKEVPEDSNNFDGSHVYMHSDYNVYRVRSRYNSDWGETGTEQDEEEDSDENSYYQPDMEYSEIVGLPEEEEIPANRKIKFSSAPIKVFNTYSNEDYDRRNDEVDPVAASAEYELEKRVEKLELFPVELEKDEDGLGISIIGMGVGADAGLEKLGIFVKTVTEGGAAQRDGRIQVNDQIVEVDGISLVGVTQNFAATVLRNTKGNVRFVIGREKPGQVSEVAQLISQTLEQERRQRELLEQHYAQYDADDDETGEYATDEEEDEVGPVLPGSDMAIEVFELPENEDMFSPSELDTSKLSHKFKELQIKHAVTEAEIQKLKTKLQAAENEKVRWELEKTQLQQNIEENKERMLKLESYWIEAQTLCHTVNEHLKETQSQYQALEKKYNKAKKLIKDFQQKELDFIKRQEAERKKIEDLEKAHLVEVQGLQVRIRDLEAEVFRLLKQNGTQVNNNNNIFERRTSLGEVSKGDTMENLDGKQTSCQDGLSQDLNEAVPETERLDSKALKTRAQLSVKNRRQRPSRTRLYDSVSSTDGEDSLER → MHITKLLPPKGLRTSSPESDSGVPPLTPVDSNVPFSSDHIAEFQEEPLDPEMGPLSSMWGDTSLFSTSKSDHDVEESPCHHQTTNKKILREKDDAKDPKSLRASSSLAVQGGKIKRKFVDLGAPLRRNSSKGKKWKEKEKEASRFSAGSRIFRGRLENWTPKPCSTAQTSTRSPCMPFSWFNDSRKGSYSFRNLPAPTSSLQPSPETLISDKKGS
    • 960-967: Missing

Q9ULJ8-3

  • Name
    3
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 630-630: E → ENTVAELQGMSGNCNNNNNYFLK
    • 919-919: K → KPSNSFYNHMHITKLLPPKGLRTSSPESDSGVPPLTPVDSNVPFSSDHIAEFQEEPLDPEMGPLSSMWGDTSLFSTSKSDHDVEESPCHHQTTNKKILREKDDAKDPKSLRASSSLAVQGGKIKRKFVDLGAPLRRNSSKGKKWKEKEKEASRFSAGSRIFRGRLENWTPKPCSTAQTSTRSPCMPFSWFNDSRKGSYSFRNLPAPTSSLQPSPETLISDKKGSKVENTWITKANKRNPNPSSSSIFGRHSQLMSVVWIQETN
    • 960-967: Missing

Q9ULJ8-4

  • Name
    4
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 920-1028: NFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDESLDMIDDEILDDGQSPKHSQCQNRAVQEWSVQQVSHWLMSLNLEQYVSEFSAQNITGEQLLQLDGNKLK → PSNSFYNHMHITKLLPPKGLRTSSPESDSGVPPLTPVDSNVPFSSDHIAEFQEEPLDPEMGPLSSMWGDTSLFSTSKSDHDVEESPCHHQTTNKKILREKDDAKDPKSLRASSSLAVQGGKIKRKFVDLGAPLRRNSSKGKKWKEKEKEASRFSAGSRIFRGRLENWTPKPCSTAQTSTRSPCMPFSWFNDSRKGSYSFRNLPAPTSSLQPSPETLISDKKGSKNFTFNDDFSPSSTSSADLSGLGAEPKTPGLSQSLALSSDE

Q9ULJ8-5

  • Name
    5
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical
    • 919-919: K → KGLRTSSPESDSGVPPLTPVDSNVPFSSDHIAEFQEEPLDPEMGPLSSMWGDTSLFSTSKSDHDVEESPCHHQTTNKKILREKDDAKDPKSLRASSSLAVQGGKIKRKFVDLGAPLRRNSSKGKKWKEKEKEASRFSAGSRIFRGRLENWTPKPCSTAQTSTRSPCMPFSWFNDSRKGSYSFRNLPAPTSSLQPSPETLISDKKGSK
    • 960-967: Missing

Computationally mapped potential isoform sequences

There are 2 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C9J730C9J730_HUMANPPP1R9A73
C9J3G5C9J3G5_HUMANPPP1R9A41

Features

Showing features for compositional bias, alternative sequence, sequence conflict.

Type
IDPosition(s)Description
Compositional bias1-28Polar residues
Alternative sequenceVSP_0111391-918in isoform 2
Compositional bias31-53Basic and acidic residues
Compositional bias97-111Basic and acidic residues
Compositional bias147-170Basic and acidic residues
Compositional bias174-213Polar residues
Compositional bias279-295Polar residues
Sequence conflict379in Ref. 3; AAI50637
Compositional bias628-645Acidic residues
Alternative sequenceVSP_044469630in isoform 3
Compositional bias851-865Polar residues
Alternative sequenceVSP_044470919in isoform 3
Alternative sequenceVSP_053808919in isoform 5
Alternative sequenceVSP_044471920-1028in isoform 4
Compositional bias922-939Polar residues
Sequence conflict952in Ref. 1; BAA90928
Alternative sequenceVSP_005121960-967in isoform 2, isoform 3 and isoform 5
Sequence conflict1017In isoform Q9ULJ8-4; in Ref. 3; AAI30450
Sequence conflict1039In isoform Q9ULJ8-3; in Ref. 3; AAI50637
Compositional bias1051-1087Basic and acidic residues
Sequence conflict1057In isoform Q9ULJ8-4; in Ref. 3; AAI30450

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AK000075
EMBL· GenBank· DDBJ
BAA90928.1
EMBL· GenBank· DDBJ
mRNA
AC002429
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC004022
EMBL· GenBank· DDBJ
AAC35294.2
EMBL· GenBank· DDBJ
Genomic DNA
AC073886
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
AC073890
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC130449
EMBL· GenBank· DDBJ
AAI30450.1
EMBL· GenBank· DDBJ
mRNA
BC150636
EMBL· GenBank· DDBJ
AAI50637.1
EMBL· GenBank· DDBJ
mRNA
AB033048
EMBL· GenBank· DDBJ
BAA86536.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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