Q9Y2Y0 · AR2BP_HUMAN
- ProteinADP-ribosylation factor-like protein 2-binding protein
- GeneARL2BP
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids163 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Together with ARL2, plays a role in the nuclear translocation, retention and transcriptional activity of STAT3. May play a role as an effector of ARL2.
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 | centrosome | |
Cellular Component | cilium | |
Cellular Component | cytosol | |
Cellular Component | midbody | |
Cellular Component | mitochondrial intermembrane space | |
Cellular Component | mitochondrial matrix | |
Cellular Component | nucleoplasm | |
Cellular Component | spindle | |
Molecular Function | GTPase regulator activity | |
Molecular Function | transcription coactivator activity | |
Biological Process | maintenance of protein location in nucleus | |
Biological Process | positive regulation of tyrosine phosphorylation of STAT protein | |
Biological Process | signal transduction |
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameADP-ribosylation factor-like protein 2-binding protein
- Short namesARF-like 2-binding protein; ARL2-binding protein
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y2Y0
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: The complex formed with ARL2BP, ARL2 and SLC25A4 is expressed in mitochondria (By similarity).
Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization
Detected in the midbody matrix. Not detected in the Golgi, nucleus and on the mitotic spindle. Centrosome-associated throughout the cell cycle. Not detected to interphase microtubules. In retina photoreceptor cells, localized in the distal connecting cilia, basal body, ciliary-associated centriole, and ciliary rootlet. Interaction with ARL2 may be required for cilia basal body localization
Keywords
- Cellular component
Disease & Variants
Involvement in disease
Retinitis pigmentosa 82 with or without situs inversus (RP82)
- Note
- DescriptionAn autosomal recessive disorder characterized by variable association of retinitis pigmentosa with situs inversus. Retinitis pigmentosa is characterized by retinal pigment deposits visible on fundus examination and primary loss of rod photoreceptor cells followed by secondary loss of cone photoreceptors. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well. Situs inversus is a congenital abnormality in which organs in the thorax and the abdomen are opposite to their normal positions due to lateral transposition.
- See alsoMIM:615434
Natural variants in RP82
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_070227 | 45 | M>R | in RP82; drastic decrease ARL2-binding, diffuse cytoplasmic localization, no enrichement at cilia basal body; dbSNP:rs398123053 |
Features
Showing features for natural variant, mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_070227 | 45 | in RP82; drastic decrease ARL2-binding, diffuse cytoplasmic localization, no enrichement at cilia basal body; dbSNP:rs398123053 | |||
Sequence: M → R | ||||||
Mutagenesis | 56 | Decreases interaction with ARL2. | ||||
Sequence: E → A | ||||||
Mutagenesis | 57 | Decreases interaction with ARL2. | ||||
Sequence: E → A | ||||||
Mutagenesis | 60 | Decreases interaction with ARL2. | ||||
Sequence: L → A | ||||||
Mutagenesis | 74 | Decreases interaction with ARL2. | ||||
Sequence: E → A | ||||||
Mutagenesis | 76 | Decreases interaction with ARL2. | ||||
Sequence: Y → A | ||||||
Natural variant | VAR_053904 | 87 | in dbSNP:rs7198865 | |||
Sequence: E → K | ||||||
Mutagenesis | 109 | Decreases interaction with ARL2. | ||||
Sequence: F → A | ||||||
Mutagenesis | 110 | Decreases interaction with ARL2. | ||||
Sequence: D → A | ||||||
Mutagenesis | 111 | Does not decrease interaction with ARL2. | ||||
Sequence: M → A | ||||||
Mutagenesis | 112 | Decreases interaction with ARL2. | ||||
Sequence: L → A | ||||||
Mutagenesis | 115 | Decreases interaction with ARL2. | ||||
Sequence: F → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 167 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000287113 | 1-163 | UniProt | ADP-ribosylation factor-like protein 2-binding protein | |||
Sequence: MDALEGESFALSFSSASDAEFDAVVGYLEDIIMDDEFQLLQRNFMDKYYLEFEDTEENKLIYTPIFNEYISLVEKYIEEQLLQRIPEFNMAAFTTTLQHHKDEVAGDIFDMLLTFTDFLAFKEMFLDYRAEKEGRGLDLSSGLVVTSLCKSSSLPASQNNLRH | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 153 | PRIDE | Phosphoserine | ||||
Sequence: S |
Proteomic databases
PTM databases
Expression
Tissue specificity
Expressed in retina pigment epithelial cells (at protein level). Widely expressed.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Found in a complex with ARL2BP, ARL2 and SLC25A6. Found in a complex with ARL2, ARL2BP and SLC25A4. Interacts with STAT2, STAT3 and STAT4. Interacts with GTP-bound ARL2 and ARL3; the complex ARL2-ARL2BP as well as ARL2BP alone, binds to SLC25A4. Interaction with ARL2 may be required for targeting to cilia basal body. Interacts with STAT3; interaction is enhanced with ARL2.
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y2Y0 | ARL2 P36404 | 27 | EBI-3449344, EBI-752365 | |
BINARY | Q9Y2Y0 | ARL3 P36405 | 7 | EBI-3449344, EBI-712710 | |
BINARY | Q9Y2Y0 | BAG6 P46379-2 | 3 | EBI-3449344, EBI-10988864 | |
BINARY | Q9Y2Y0 | CFAP20 Q9Y6A4 | 7 | EBI-3449344, EBI-1046872 | |
BINARY | Q9Y2Y0 | FGFR3 P22607 | 3 | EBI-3449344, EBI-348399 | |
BINARY | Q9Y2Y0 | GSN P06396 | 3 | EBI-3449344, EBI-351506 | |
BINARY | Q9Y2Y0 | KLF11 O14901 | 3 | EBI-3449344, EBI-948266 | |
BINARY | Q9Y2Y0 | Q9Y649 | 3 | EBI-3449344, EBI-25900580 | |
BINARY | Q9Y2Y0 | TCP1 P17987 | 3 | EBI-3449344, EBI-356553 |
Protein-protein interaction databases
Miscellaneous
Structure
Sequence & Isoform
- Sequence statusComplete
This entry describes 2 isoforms produced by Alternative splicing.
Q9Y2Y0-1
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.
- Name1
- Length163
- Mass (Da)18,822
- Last updated1999-11-01 v1
- ChecksumE35EB5AC73FC1FEC
Q9Y2Y0-2
- Name2
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_025317 | 1-11 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_025318 | 12-13 | in isoform 2 | |||
Sequence: SF → MR | ||||||
Sequence conflict | 27 | in Ref. 4; AAH94878 | ||||
Sequence: Y → C | ||||||
Sequence conflict | 50 | in Ref. 4; AAH94878 | ||||
Sequence: L → Q | ||||||
Sequence conflict | 61 | in Ref. 4; AAH94878 | ||||
Sequence: I → T | ||||||
Sequence conflict | 83 | in Ref. 4; AAH94878 | ||||
Sequence: Q → E | ||||||
Sequence conflict | 87 | in Ref. 4; AAH94878 | ||||
Sequence: E → G | ||||||
Sequence conflict | 154 | in Ref. 4; AAH94878 | ||||
Sequence: L → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF126062 EMBL· GenBank· DDBJ | AAD20633.1 EMBL· GenBank· DDBJ | mRNA | ||
AK075050 EMBL· GenBank· DDBJ | BAG52057.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471092 EMBL· GenBank· DDBJ | EAW82913.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC003087 EMBL· GenBank· DDBJ | AAH03087.1 EMBL· GenBank· DDBJ | mRNA | ||
BC094878 EMBL· GenBank· DDBJ | AAH94878.1 EMBL· GenBank· DDBJ | mRNA |