Q9Y3L3 · 3BP1_HUMAN
- ProteinSH3 domain-binding protein 1
- GeneSH3BP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids701 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Also negatively regulates CDC42 in the process of actin remodeling and the formation of epithelial cell junctions (PubMed:22891260).
Through its GAP activity toward RAC1 and/or CDC42 plays a specific role in phagocytosis of large particles. Specifically recruited by a PI3 kinase/PI3K-dependent mechanism to sites of large particles engagement, inactivates RAC1 and/or CDC42 allowing the reorganization of the underlying actin cytoskeleton required for engulfment (PubMed:26465210).
It also plays a role in angiogenesis and the process of repulsive guidance as part of a semaphorin-plexin signaling pathway. Following the binding of PLXND1 to extracellular SEMA3E it dissociates from PLXND1 and inactivates RAC1, inducing the intracellular reorganization of the actin cytoskeleton and the collapse of cells (PubMed:24841563).
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
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameSH3 domain-binding protein 1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ9Y3L3
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Accumulation at forming phagocytic cups is PI3 kinase/PI3K-dependent and is specific for sites of large particles engagement and their phosphatidylinositol 3,4,5-triphosphate membrane content (PubMed:26465210).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 312 | Probable loss of the GTPase activator activity. Loss of function in cell migration. | ||||
Sequence: R → A | ||||||
Natural variant | VAR_033450 | 511 | in dbSNP:rs929038 | |||
Sequence: P → L | ||||||
Natural variant | VAR_033451 | 656 | in dbSNP:rs2269548 | |||
Sequence: S → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 758 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000056723 | 1-701 | UniProt | SH3 domain-binding protein 1 | |||
Sequence: MMKRQLHRMRQLAQTGSLGRTPETAEFLGEDLLQVEQRLEPAKRAAHNIHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQATKNSGSSQGLGGSPGSHSHTTMANKVETLKEEEEELKRKVEQCRDEYLADLYHFVTKEDSYANYFIRLLEIQADYHRRSLSSLDTALAELRENHGQADHSPSMTATHFPRVYGVSLATHLQELGREIALPIEACVMMLLSEGMKEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTFDLYDDWMRAASLKEPGARLQALQEVCSRLPPENLSNLRYLMKFLARLAEEQEVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVSSIQVVGVVEALIQSADTLFPGDINFNVSGLFSAVTLQDTVSDRLASEELPSTAVPTPATTPAPAPAPAPAPAPALASAATKERTESEVPPRPASPKVTRSPPETAAPVEDMARRTKRPAPARPTMPPPQVSGSRSSPPAPPLPPGSGSPGTPQALPRRLVGSSLRAPTVPPPLPPTPPQPARRQSRRSPASPSPASPGPASPSPVSLSNPAQVDLGAATAEGGAPEAISGVPTPPAIPPQPRPRSLASETN | |||||||
Modified residue (large scale data) | 15 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 17 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 169 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 175 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 241 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 262 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 262 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 264 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 534 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 536 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 544 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 544 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 548 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 550 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 550 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 554 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 585 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 586 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 596 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 598 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 601 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 601 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 626 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 626 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 653 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 695 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Interacts with the exocyst via EXOC4 and EXOC8; required for the localization of both SH3BP1 and the exocyst to the leading edge of migrating cells (PubMed:21658605).
Interacts with CD2AP and CGNL1; probably part of a complex at cell junctions (PubMed:22891260).
Interacts with CAPZA1; recruits CAPZA1 to forming cell junctions (PubMed:22891260).
May interact with AFDN (PubMed:22891260).
Interacts with PLXND1; they dissociate upon SEMA3E binding to PLXND1 allowing SH3BP1 to transduce downstream signal through RAC1 inactivation (PubMed:24841563).
Interacts with ABL1, GRB2 and SRC (via SH3 domain) (By similarity).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q9Y3L3 | ABI2 Q9NYB9-2 | 3 | EBI-346869, EBI-11096309 | |
BINARY | Q9Y3L3 | ABI3 Q9P2A4 | 3 | EBI-346869, EBI-742038 | |
BINARY | Q9Y3L3 | ARHGAP17 Q68EM7 | 4 | EBI-346869, EBI-1642807 | |
BINARY | Q9Y3L3 | CCDC146 Q8IYE0 | 3 | EBI-346869, EBI-10749669 | |
BINARY | Q9Y3L3 | FGA P02671-2 | 3 | EBI-346869, EBI-9640259 | |
BINARY | Q9Y3L3 | TERF1 P54274 | 2 | EBI-346869, EBI-710997 | |
BINARY | Q9Y3L3 | TRIP10 Q15642 | 3 | EBI-346869, EBI-739936 | |
BINARY | Q9Y3L3 | TRIP10 Q15642-2 | 3 | EBI-346869, EBI-6550597 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, domain, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-23 | Disordered | ||||
Sequence: MMKRQLHRMRQLAQTGSLGRTPE | ||||||
Region | 1-275 | Interaction with CGNL1 | ||||
Sequence: MMKRQLHRMRQLAQTGSLGRTPETAEFLGEDLLQVEQRLEPAKRAAHNIHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQATKNSGSSQGLGGSPGSHSHTTMANKVETLKEEEEELKRKVEQCRDEYLADLYHFVTKEDSYANYFIRLLEIQADYHRRSLSSLDTALAELRENHGQADHSPSMTATHFPRVYG | ||||||
Domain | 17-262 | BAR | ||||
Sequence: SLGRTPETAEFLGEDLLQVEQRLEPAKRAAHNIHKRLQACLQGQSGADMDKRVKKLPLMALSTTMAESFKELDPDSSMGKALEMSCAIQNQLARILAEFEMTLERDVLQPLSRLSEEELPAILKHKKSLQKLVSDWNTLKSRLSQATKNSGSSQGLGGSPGSHSHTTMANKVETLKEEEEELKRKVEQCRDEYLADLYHFVTKEDSYANYFIRLLEIQADYHRRSLSSLDTALAELRENHGQADHS | ||||||
Region | 160-182 | Disordered | ||||
Sequence: SQATKNSGSSQGLGGSPGSHSHT | ||||||
Domain | 276-469 | Rho-GAP | ||||
Sequence: VSLATHLQELGREIALPIEACVMMLLSEGMKEEGLFRLAAGASVLKRLKQTMASDPHSLEEFCSDPHAVAGALKSYLRELPEPLMTFDLYDDWMRAASLKEPGARLQALQEVCSRLPPENLSNLRYLMKFLARLAEEQEVNKMTPSNIAIVLGPNLLWPPEKEGDQAQLDAASVSSIQVVGVVEALIQSADTLF | ||||||
Region | 470-701 | Interaction with CD2AP | ||||
Sequence: PGDINFNVSGLFSAVTLQDTVSDRLASEELPSTAVPTPATTPAPAPAPAPAPAPALASAATKERTESEVPPRPASPKVTRSPPETAAPVEDMARRTKRPAPARPTMPPPQVSGSRSSPPAPPLPPGSGSPGTPQALPRRLVGSSLRAPTVPPPLPPTPPQPARRQSRRSPASPSPASPGPASPSPVSLSNPAQVDLGAATAEGGAPEAISGVPTPPAIPPQPRPRSLASETN | ||||||
Region | 496-701 | Disordered | ||||
Sequence: SEELPSTAVPTPATTPAPAPAPAPAPAPALASAATKERTESEVPPRPASPKVTRSPPETAAPVEDMARRTKRPAPARPTMPPPQVSGSRSSPPAPPLPPGSGSPGTPQALPRRLVGSSLRAPTVPPPLPPTPPQPARRQSRRSPASPSPASPGPASPSPVSLSNPAQVDLGAATAEGGAPEAISGVPTPPAIPPQPRPRSLASETN | ||||||
Compositional bias | 506-522 | Pro residues | ||||
Sequence: TPATTPAPAPAPAPAPA | ||||||
Compositional bias | 570-600 | Pro residues | ||||
Sequence: PARPTMPPPQVSGSRSSPPAPPLPPGSGSPG | ||||||
Motif | 616-625 | SH3-binding | ||||
Sequence: APTVPPPLPP | ||||||
Compositional bias | 617-632 | Pro residues | ||||
Sequence: PTVPPPLPPTPPQPAR |
Domain
It also mediates the interaction with PLXND1 (PubMed:24841563).
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing & Alternative initiation.
Q9Y3L3-1
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
- Length701
- Mass (Da)75,713
- Last updated2004-08-16 v3
- Checksum877D144E81F0F974
Q9Y3L3-2
- Name2
Q6ZT62-1
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameLong BGIN
Q6ZT62-2
The sequence of this isoform can be found in the external entry linked below. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly.
View isoform- NameShort BGIN
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2R8Y5V0 | A0A2R8Y5V0_HUMAN | SH3BP1 | 387 | ||
F8WEQ3 | F8WEQ3_HUMAN | SH3BP1 | 20 | ||
A0A3B3IU28 | A0A3B3IU28_HUMAN | SH3BP1 | 206 |
Sequence caution
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_011373 | 440-452 | in isoform 2 | |||
Sequence: DQAQLDAASVSSI → TEPARELGSQTLC | ||||||
Alternative sequence | VSP_011374 | 453-701 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 506-522 | Pro residues | ||||
Sequence: TPATTPAPAPAPAPAPA | ||||||
Compositional bias | 570-600 | Pro residues | ||||
Sequence: PARPTMPPPQVSGSRSSPPAPPLPPGSGSPG | ||||||
Compositional bias | 617-632 | Pro residues | ||||
Sequence: PTVPPPLPPTPPQPAR |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CR456576 EMBL· GenBank· DDBJ | CAG30462.1 EMBL· GenBank· DDBJ | mRNA | ||
AK124370 EMBL· GenBank· DDBJ | BAC85842.1 EMBL· GenBank· DDBJ | mRNA | Sequence problems. | |
Z83844 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC008282 EMBL· GenBank· DDBJ | AAH08282.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AL157480 EMBL· GenBank· DDBJ | CAB75671.2 EMBL· GenBank· DDBJ | mRNA |