P29373 · RABP2_HUMAN

  • Protein
    Cellular retinoic acid-binding protein 2
  • Gene
    CRABP2
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.

Features

Showing features for binding site.

1138102030405060708090100110120130
TypeIDPosition(s)Description
Binding site133-135all-trans-retinoate (UniProtKB | ChEBI)

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 Componentcytoplasm
Cellular Componentcytosol
Cellular Componentendoplasmic reticulum
Cellular Componentextracellular exosome
Cellular Componentnucleoplasm
Cellular Componentnucleus
Molecular Functioncyclin binding
Molecular Functionfatty acid binding
Molecular Functionretinal binding
Molecular Functionretinoic acid binding
Molecular Functionretinoid binding
Molecular Functionretinol binding
Biological Processembryonic forelimb morphogenesis
Biological Processepidermis development
Biological Processfatty acid transport
Biological Processpositive regulation of collateral sprouting
Biological Processregulation of DNA-templated transcription
Biological Processretinoic acid metabolic process
Biological Processsignal transduction

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Cellular retinoic acid-binding protein 2
  • Alternative names
    • Cellular retinoic acid-binding protein II (CRABP-II)

Gene names

    • Name
      CRABP2

Organism names

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

Accessions

  • Primary accession
    P29373
  • Secondary accessions
    • B2R4Z8
    • D3DVC5
    • F1T098
    • Q6ICN6

Proteomes

Organism-specific databases

Subcellular Location

Note: Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus.

Keywords

Disease & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis21Loss of ligand-induced nuclear import; when associated with A-30 and A-31.
Mutagenesis30Loss of ligand-induced nuclear import; when associated with A-21 and A-31.
Mutagenesis31Loss of ligand-induced nuclear import; when associated with A-21 and A-30.

Variants

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

The viewer provides 184 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Organism-specific databases

Miscellaneous

Chemistry

Genetic variation databases

PTM/Processing

Features

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

Type
IDPosition(s)Source
Description
ChainPRO_00000674151-138UniProtCellular retinoic acid-binding protein 2
Modified residue (large scale data)87PTMeXchangeSumoylated lysine
Modified residue (large scale data)99PTMeXchangeSumoylated lysine
Cross-link102UniProtGlycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residue (large scale data)102PTMeXchangeSumoylated lysine

Post-translational modification

Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation.

Keywords

Proteomic databases

PTM databases

Expression

Induction

By retinoic acid.

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with RXR and RARA (By similarity).
Interacts with importin alpha

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntAct
BINARY P29373ACTN2 P356093EBI-10204806, EBI-77797
BINARY P29373CCND3 P302813EBI-10204806, EBI-375013
BINARY P29373FLAD1 Q8NFF5-23EBI-10204806, EBI-11526128
BINARY P29373KASH5 Q8N6L06EBI-10204806, EBI-749265

Protein-protein interaction databases

Chemistry

Miscellaneous

Family & Domains

Features

Showing features for motif.

TypeIDPosition(s)Description
Motif21-31Nuclear localization signal

Domain

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.

Sequence similarities

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    138
  • Mass (Da)
    15,693
  • Last updated
    2007-01-23 v2
  • MD5 Checksum
    940C1E764AA7344633FEE214CEDE00DC
MPNFSGNWKIIRSENFEELLKVLGVNVMLRKIAVAAASKPAVEIKQEGDTFYIKTSTTVRTTEINFKVGEEFEEQTVDGRPCKSLVKWESENKMVCEQKLLKGEGPKTSWTRELTNDGELILTMTADDVVCTRVYVRE

Computationally mapped potential isoform sequences

There is 1 potential isoform mapped to this entry

View all
EntryEntry nameGene nameLength
Q5SYZ4Q5SYZ4_HUMANCRABP282

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M68867
EMBL· GenBank· DDBJ
AAA52068.1
EMBL· GenBank· DDBJ
mRNA
M97815
EMBL· GenBank· DDBJ
AAA58430.1
EMBL· GenBank· DDBJ
Genomic DNA
M97814
EMBL· GenBank· DDBJ
AAA58430.1
EMBL· GenBank· DDBJ
Genomic DNA
CR450357
EMBL· GenBank· DDBJ
CAG29353.1
EMBL· GenBank· DDBJ
mRNA
BT019827
EMBL· GenBank· DDBJ
AAV38630.1
EMBL· GenBank· DDBJ
mRNA
AK312007
EMBL· GenBank· DDBJ
BAG34945.1
EMBL· GenBank· DDBJ
mRNA
AB593017
EMBL· GenBank· DDBJ
BAJ83972.1
EMBL· GenBank· DDBJ
mRNA
AL590666
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
CH471121
EMBL· GenBank· DDBJ
EAW52921.1
EMBL· GenBank· DDBJ
Genomic DNA
CH471121
EMBL· GenBank· DDBJ
EAW52922.1
EMBL· GenBank· DDBJ
Genomic DNA
BC001109
EMBL· GenBank· DDBJ
AAH01109.1
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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