Q9Z131 · 3BP5_MOUSE
- ProteinSH3 domain-binding protein 5
- GeneSh3bp5
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids463 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Functions as a guanine nucleotide exchange factor (GEF) with specificity for RAB11A and RAB25 (By similarity).
Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death
Inhibits the auto- and transphosphorylation activity of BTK. Plays a negative regulatory role in BTK-related cytoplasmic signaling in B-cells. May be involved in BCR-induced apoptotic cell death
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 | cytoplasmic vesicle membrane | |
Cellular Component | mitochondrion | |
Cellular Component | nuclear body | |
Molecular Function | guanyl-nucleotide exchange factor activity | |
Molecular Function | protein kinase inhibitor activity | |
Molecular Function | SH3 domain binding | |
Biological Process | intracellular signal transduction | |
Biological Process | negative regulation of protein kinase activity |
Keywords
- Molecular function
Names & Taxonomy
Protein names
- Recommended nameSH3 domain-binding protein 5
- Short namesSH3BP-5
- Alternative names
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 accessionQ9Z131
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Cytoplasmic vesicle membrane ; Peripheral membrane protein
Note: Colocalizes with RAB11A on cytoplasmic vesicle membranes.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000064369 | 1-463 | SH3 domain-binding protein 5 | |||
Sequence: MDTALKRSRSDEPAELPPPAREVEEKEEEEERMEQGLEEEEEEVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNAMGPRGCGVGAEGSIASVENLPVSKPEPDAISVASEAFEDDNCSNLVSEDDSETQSVSSFSSGPTSPSEMPDQFPAVARPGSLDLPSPVSLSEFGMMFPILGPRSECSGASSPECEVERGDRAEGAENKMSDKANNNRVLGSTNGGSGRSRSQSSTSLESQALETRMKQLSLQCSKGRDGIIADIKMIFIFYTFLQ | ||||||
Modified residue | 354 | Phosphoserine; by MAPK12 and MAPK9 | ||||
Sequence: S | ||||||
Modified residue | 378 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 379 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 421 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 424 | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Structure
Family & Domains
Features
Showing features for compositional bias, region, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-26 | Basic and acidic residues | ||||
Sequence: MDTALKRSRSDEPAELPPPAREVEEK | ||||||
Region | 1-69 | Disordered | ||||
Sequence: MDTALKRSRSDEPAELPPPAREVEEKEEEEERMEQGLEEEEEEVDPRIQGELEKLNQSTDDINRRETEL | ||||||
Compositional bias | 27-46 | Acidic residues | ||||
Sequence: EEEEERMEQGLEEEEEEVDP | ||||||
Region | 33-268 | Sufficient for interaction with RAB11A and for guanine nucleotide exchange activity | ||||
Sequence: MEQGLEEEEEEVDPRIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKKIGKAVEDSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLEDDKRQFDSAWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKKLKRAINKSKPYFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISDEIHERRRSNA | ||||||
Coiled coil | 47-93 | |||||
Sequence: RIQGELEKLNQSTDDINRRETELEDARQKFRSVLVEATVKLDELAKK | ||||||
Coiled coil | 100-148 | |||||
Sequence: DSKPYWEARRVARQAQLEAQKATQDFQRATEVLRAAKETISLAEQRLLE | ||||||
Coiled coil | 157-203 | |||||
Sequence: AWQEMLNHATQRVMEAEQTKTRSELVHKETAARYNAAMGRMRQLEKK | ||||||
Coiled coil | 214-258 | |||||
Sequence: YFELKAKYYVQLEQLKKTVDDLQAKLALAKGEYKAALKSLERISD | ||||||
Compositional bias | 309-336 | Polar residues | ||||
Sequence: NCSNLVSEDDSETQSVSSFSSGPTSPSE | ||||||
Region | 309-348 | Disordered | ||||
Sequence: NCSNLVSEDDSETQSVSSFSSGPTSPSEMPDQFPAVARPG | ||||||
Region | 372-429 | Disordered | ||||
Sequence: SECSGASSPECEVERGDRAEGAENKMSDKANNNRVLGSTNGGSGRSRSQSSTSLESQA | ||||||
Compositional bias | 382-398 | Basic and acidic residues | ||||
Sequence: CEVERGDRAEGAENKMS | ||||||
Compositional bias | 399-429 | Polar residues | ||||
Sequence: DKANNNRVLGSTNGGSGRSRSQSSTSLESQA |
Domain
The N-terminal half of the protein mediates interaction with RAB11A and functions as a guanine nucleotide exchange factor. Four long alpha-helices (interrupted by a central kink) assemble into coiled coils, giving rise to a 'V' shape.
Sequence similarities
Belongs to the SH3BP5 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q9Z131-1
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
- Length463
- Mass (Da)51,807
- Last updated2007-01-23 v3
- ChecksumA4274A91DDD91670
Q9Z131-2
- Name2
- Differences from canonical
- 455-463: IFIFYTFLQ → VQIG
Q9Z131-3
- Name3
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-26 | Basic and acidic residues | ||||
Sequence: MDTALKRSRSDEPAELPPPAREVEEK | ||||||
Alternative sequence | VSP_022572 | 1-70 | in isoform 3 | |||
Sequence: MDTALKRSRSDEPAELPPPAREVEEKEEEEERMEQGLEEEEEEVDPRIQGELEKLNQSTDDINRRETELE → MDWARTVMASTGLAPASAAPHTGSRAQPCLFLAPVPPHFAWFIFLDPALPCSTLAQSVSFKPCCGVVK | ||||||
Compositional bias | 27-46 | Acidic residues | ||||
Sequence: EEEEERMEQGLEEEEEEVDP | ||||||
Sequence conflict | 299 | in Ref. 1; BAC31530 | ||||
Sequence: S → SS | ||||||
Compositional bias | 309-336 | Polar residues | ||||
Sequence: NCSNLVSEDDSETQSVSSFSSGPTSPSE | ||||||
Compositional bias | 382-398 | Basic and acidic residues | ||||
Sequence: CEVERGDRAEGAENKMS | ||||||
Compositional bias | 399-429 | Polar residues | ||||
Sequence: DKANNNRVLGSTNGGSGRSRSQSSTSLESQA | ||||||
Alternative sequence | VSP_010882 | 455-463 | in isoform 2 and isoform 3 | |||
Sequence: IFIFYTFLQ → VQIG |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK043375 EMBL· GenBank· DDBJ | BAC31530.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK161427 EMBL· GenBank· DDBJ | BAE36389.1 EMBL· GenBank· DDBJ | mRNA | ||
BC018237 EMBL· GenBank· DDBJ | AAH18237.2 EMBL· GenBank· DDBJ | mRNA | ||
BC053741 EMBL· GenBank· DDBJ | AAH53741.2 EMBL· GenBank· DDBJ | mRNA | ||
AB016835 EMBL· GenBank· DDBJ | BAA75641.1 EMBL· GenBank· DDBJ | mRNA |