Q5SSL4 · ABR_MOUSE
- ProteinActive breakpoint cluster region-related protein
- GeneAbr
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids859 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form. The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (By similarity).
Functions as an important negative regulator of neuronal RAC1 activity (PubMed:20962234).
Regulates macrophage functions such as CSF-1 directed motility and phagocytosis through the modulation of RAC1 activity (PubMed:17116687).
Functions as an important negative regulator of neuronal RAC1 activity (PubMed:20962234).
Regulates macrophage functions such as CSF-1 directed motility and phagocytosis through the modulation of RAC1 activity (PubMed:17116687).
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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Keywords
- Molecular function
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameActive breakpoint cluster region-related protein
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ5SSL4
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Phenotypes & Variants
Disruption phenotype
Mutant mice show impaired spatial and object recognition memory with reduced maintenance of long-term potentiation (LTP) in Schaffer collateral-CA1 pyramidal neuron synapses.
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 38 variants from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000355539 | 1-859 | Active breakpoint cluster region-related protein | |||
Sequence: MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGDSVSPTPPEGLAPGVEAGKGLEMRKLVLSGFLASEEIYINQLEALLLPMKPLKATATTSQPVLTIQQIETIFYKIQDIYEIHKEFYDNLCPKVQQWDSQVTMGHLFQKLASQLGVYKAFVDNYKVALETAEKCSQSNNQFQKISEELKVKGPKDSKDSHTSVTMEALLYKPIDRVTRSTLVLHDLLKHTPVDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEMSESSRKLRHVFLFTDVLLCAKLKKTSAGKHQQYDCKWYIPLADLVFPSPEESEASPQVHPFPDHELEDMKTKISALKSEIQKEKANKGQSRAIERLKKKMFENEFLLLLNSPTIPFRIHNRNGKSYLFLLSSDYERSEWREAIQKLQKKDLQAFVLSSVELQVLTGSCFKLRTVHNIPVTSNKDDDESPGLYGFLHVIVHSAKGFKQSANLYCTLEVDSFGYFVSKAKTRVFRDTTEPKWDEEFEIELEGSQSLRILCYEKCYDKTKVNKDNNEIVDKIMGKGQIQLDPQTVESKNWHTDVIEMNGIKVEFSMKFTSRDMSLKRTPSKKQTGVFGVKISVVTKRERSKVPYIVRQCIEEVEKRGIEEVGIYRISGVATDIQALKAVFDANNKDILLMLSDMDINAIAGTLKLYFRELPEPLLTDRLYPAFMEGIALSDPAAKENCMMHLLRSLPDPNLITFLFLLEHLKRVAEKEPINKMSLHNLATVFGPTLLRPSEVESKAHLTSAADIWSHDVMAQVQVLLYYLQHPPISFAELKRNTLYFSTDV | ||||||
Modified residue | 57 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
In hippocampal subregions, expressed at similarly high levels in the dentate gyrus and CA1 regions, but lower in the CA3 region.
Gene expression databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 29-84 | Disordered | ||||
Sequence: YDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGDSVSPTPPEGLAPGVE | ||||||
Compositional bias | 50-71 | Polar residues | ||||
Sequence: IDESPTMSPQLSARSQGGGDSV | ||||||
Domain | 91-284 | DH | ||||
Sequence: MRKLVLSGFLASEEIYINQLEALLLPMKPLKATATTSQPVLTIQQIETIFYKIQDIYEIHKEFYDNLCPKVQQWDSQVTMGHLFQKLASQLGVYKAFVDNYKVALETAEKCSQSNNQFQKISEELKVKGPKDSKDSHTSVTMEALLYKPIDRVTRSTLVLHDLLKHTPVDHPDYPLLQDALRISQNFLSSINED | ||||||
Domain | 301-459 | PH | ||||
Sequence: QLVKDGFLVEMSESSRKLRHVFLFTDVLLCAKLKKTSAGKHQQYDCKWYIPLADLVFPSPEESEASPQVHPFPDHELEDMKTKISALKSEIQKEKANKGQSRAIERLKKKMFENEFLLLLNSPTIPFRIHNRNGKSYLFLLSSDYERSEWREAIQKLQK | ||||||
Domain | 484-613 | C2 | ||||
Sequence: TVHNIPVTSNKDDDESPGLYGFLHVIVHSAKGFKQSANLYCTLEVDSFGYFVSKAKTRVFRDTTEPKWDEEFEIELEGSQSLRILCYEKCYDKTKVNKDNNEIVDKIMGKGQIQLDPQTVESKNWHTDVI | ||||||
Domain | 647-845 | Rho-GAP | ||||
Sequence: VKISVVTKRERSKVPYIVRQCIEEVEKRGIEEVGIYRISGVATDIQALKAVFDANNKDILLMLSDMDINAIAGTLKLYFRELPEPLLTDRLYPAFMEGIALSDPAAKENCMMHLLRSLPDPNLITFLFLLEHLKRVAEKEPINKMSLHNLATVFGPTLLRPSEVESKAHLTSAADIWSHDVMAQVQVLLYYLQHPPISF |
Domain
The central Dbl homology (DH) domain functions as a guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form. The C-terminus is a Rho-GAP domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. The protein has a unique structure having two opposing regulatory activities toward small GTP-binding proteins.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q5SSL4-1
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
- Length859
- Mass (Da)97,667
- Last updated2004-12-21 v1
- Checksum79ED2F432899A1F9
Q5SSL4-2
- Name2
- Differences from canonical
- 1-21: MEPLSHRGLPRLSWIDTLYSN → MAAGGRRRRPLRYQSLAALVEDSQWPFLFLVSD
Q5SSL4-3
- Name3
Q5SSL4-4
- Name4
- Differences from canonical
- 1-82: MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGDSVSPTPPEGLAPG → MEEEEEAIGFLDKVLEDEDVFLLEECELGTPTSPGSGSPFLVAVK
Computationally mapped potential isoform sequences
There are 6 potential isoforms mapped to this entry
Sequence caution
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_035905 | 1-21 | in isoform 2 | |||
Sequence: MEPLSHRGLPRLSWIDTLYSN → MAAGGRRRRPLRYQSLAALVEDSQWPFLFLVSD | ||||||
Alternative sequence | VSP_035904 | 1-82 | in isoform 4 | |||
Sequence: MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGDSVSPTPPEGLAPG → MEEEEEAIGFLDKVLEDEDVFLLEECELGTPTSPGSGSPFLVAVK | ||||||
Alternative sequence | VSP_035903 | 1-218 | in isoform 3 | |||
Sequence: Missing | ||||||
Compositional bias | 50-71 | Polar residues | ||||
Sequence: IDESPTMSPQLSARSQGGGDSV | ||||||
Sequence conflict | 164 | in Ref. 1; BAE32119 | ||||
Sequence: W → R | ||||||
Alternative sequence | VSP_035906 | 219-233 | in isoform 3 | |||
Sequence: GPKDSKDSHTSVTME → MEILLIIRFCCNCTY | ||||||
Sequence conflict | 630 | in Ref. 1; BAE22375 | ||||
Sequence: D → E |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK134993 EMBL· GenBank· DDBJ | BAE22375.1 EMBL· GenBank· DDBJ | mRNA | ||
AK142364 EMBL· GenBank· DDBJ | BAE25044.1 EMBL· GenBank· DDBJ | mRNA | ||
AK153615 EMBL· GenBank· DDBJ | BAE32119.1 EMBL· GenBank· DDBJ | mRNA | ||
AL591143 EMBL· GenBank· DDBJ | CAI24541.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL663050 EMBL· GenBank· DDBJ | CAI24541.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL591143 EMBL· GenBank· DDBJ | CAI24542.3 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL663050 EMBL· GenBank· DDBJ | CAI24542.3 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL591143 EMBL· GenBank· DDBJ | CAI24543.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL663050 EMBL· GenBank· DDBJ | CAI24543.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL591143 EMBL· GenBank· DDBJ | CAI24545.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL663050 EMBL· GenBank· DDBJ | CAI24545.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL591143 EMBL· GenBank· DDBJ | CAI24547.2 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL663050 EMBL· GenBank· DDBJ | CAI25860.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL591143 EMBL· GenBank· DDBJ | CAI25860.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL663050 EMBL· GenBank· DDBJ | CAQ11498.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL591143 EMBL· GenBank· DDBJ | CAQ11498.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL663050 EMBL· GenBank· DDBJ | CAQ11499.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL591143 EMBL· GenBank· DDBJ | CAQ11499.1 EMBL· GenBank· DDBJ | Genomic DNA | Sequence problems. | |
AL663050 EMBL· GenBank· DDBJ | CAQ11500.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AL591143 EMBL· GenBank· DDBJ | CAQ11500.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC056385 EMBL· GenBank· DDBJ | AAH56385.1 EMBL· GenBank· DDBJ | mRNA | ||
BC058708 EMBL· GenBank· DDBJ | AAH58708.1 EMBL· GenBank· DDBJ | mRNA | ||
BC059064 EMBL· GenBank· DDBJ | AAH59064.1 EMBL· GenBank· DDBJ | mRNA |