P29373 · RABP2_HUMAN
- ProteinCellular retinoic acid-binding protein 2
- GeneCRABP2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids138 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 133-135 | all-trans-retinoate (UniProtKB | ChEBI) | |||
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | endoplasmic reticulum | |
Cellular Component | extracellular exosome | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | cyclin binding | |
Molecular Function | fatty acid binding | |
Molecular Function | retinal binding | |
Molecular Function | retinoic acid binding | |
Molecular Function | retinoid binding | |
Molecular Function | retinol binding | |
Biological Process | embryonic forelimb morphogenesis | |
Biological Process | epidermis development | |
Biological Process | fatty acid transport | |
Biological Process | positive regulation of collateral sprouting | |
Biological Process | regulation of DNA-templated transcription | |
Biological Process | retinoic acid metabolic process | |
Biological Process | signal transduction |
Keywords
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameCellular retinoic acid-binding protein 2
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP29373
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Mutagenesis | 21 | Loss of ligand-induced nuclear import; when associated with A-30 and A-31. | |||
Mutagenesis | 30 | Loss of ligand-induced nuclear import; when associated with A-21 and A-31. | |||
Mutagenesis | 31 | Loss of ligand-induced nuclear import; when associated with A-21 and A-30. | |||
Variants
![](/variants.8e7f84.jpg)
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.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | ||
---|---|---|---|---|---|---|
Chain | PRO_0000067415 | 1-138 | UniProt | Cellular retinoic acid-binding protein 2 | ||
Modified residue (large scale data) | 87 | PTMeXchange | Sumoylated lysine | |||
Modified residue (large scale data) | 99 | PTMeXchange | Sumoylated lysine | |||
Cross-link | 102 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | |||
Modified residue (large scale data) | 102 | PTMeXchange | Sumoylated lysine | |||
Post-translational modification
Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation.
Keywords
- PTM
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
Interacts with importin alpha
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | IntAct | |
---|---|---|---|---|---|
BINARY | P29373 | ACTN2 P35609 | 3 | EBI-10204806, EBI-77797 | |
BINARY | P29373 | CCND3 P30281 | 3 | EBI-10204806, EBI-375013 | |
BINARY | P29373 | FLAD1 Q8NFF5-2 | 3 | EBI-10204806, EBI-11526128 | |
BINARY | P29373 | KASH5 Q8N6L0 | 6 | EBI-10204806, EBI-749265 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for motif.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Motif | 21-31 | Nuclear localization signal | |||
Domain
Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Sequence similarities
Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length138
- Mass (Da)15,693
- Last updated2007-01-23 v2
- MD5 Checksum940C1E764AA7344633FEE214CEDE00DC
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
Q5SYZ4 | Q5SYZ4_HUMAN | CRABP2 | 82 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |