P52735 · VAV2_HUMAN
- ProteinGuanine nucleotide exchange factor VAV2
- GeneVAV2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids878 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Guanine nucleotide exchange factor for the Rho family of Ras-related GTPases. Plays an important role in angiogenesis. Its recruitment by phosphorylated EPHA2 is critical for EFNA1-induced RAC1 GTPase activation and vascular endothelial cell migration and assembly (By similarity).
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
- Ligand
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameGuanine nucleotide exchange factor VAV2
- Short namesVAV-2
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP52735
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_045690 | 594 | in dbSNP:rs602990 | |||
Sequence: M → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 915 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_0000080984 | 1-878 | UniProt | Guanine nucleotide exchange factor VAV2 | |||
Sequence: MEQWRQCGRWLIDCKVLPPNHRVVWPSAVVFDLAQALRDGVLLCQLLHNLSPGSIDLKDINFRPQMSQFLCLKNIRTFLKVCHDKFGLRNSELFDPFDLFDVRDFGKVISAVSRLSLHSIAQNKGIRPFPSEETTENDDDVYRSLEELADEHDLGEDIYDCVPCEDGGDDIYEDIIKVEVQQPMIRYMQKMGMTEDDKRNCCLLEIQETEAKYYRTLEDIEKNYMSPLRLVLSPADMAAVFINLEDLIKVHHSFLRAIDVSVMVGGSTLAKVFLDFKERLLIYGEYCSHMEHAQNTLNQLLASREDFRQKVEECTLKVQDGKFKLQDLLVVPMQRVLKYHLLLKELLSHSAERPERQQLKEALEAMQDLAMYINEVKRDKETLRKISEFQSSIENLQVKLEEFGRPKIDGELKVRSIVNHTKQDRYLFLFDKVVIVCKRKGYSYELKEIIELLFHKMTDDPMNNKDVKKSHGKMWSYGFYLIHLQGKQGFQFFCKTEDMKRKWMEQFEMAMSNIKPDKANANHHSFQMYTFDKTTNCKACKMFLRGTFYQGYMCTKCGVGAHKECLEVIPPCKFTSPADLDASGAGPGPKMVAMQNYHGNPAPPGKPVLTFQTGDVLELLRGDPESPWWEGRLVQTRKSGYFPSSSVKPCPVDGRPPISRPPSREIDYTAYPWFAGNMERQQTDNLLKSHASGTYLIRERPAEAERFAISIKFNDEVKHIKVVEKDNWIHITEAKKFDSLLELVEYYQCHSLKESFKQLDTTLKYPYKSRERSASRASSRSPASCASYNFSFLSPQGLSFASQGPSAPFWSVFTPRVIGTAVARYNFAARDMRELSLREGDVVRIYSRIGGDQGWWKGETNGRIGWFPSTYVEEEGIQ | |||||||
Modified residue (large scale data) | 91 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 142 | UniProt | Phosphotyrosine; by EGFR | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 142 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 159 | UniProt | Phosphotyrosine; by EGFR | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 159 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 172 | UniProt | Phosphotyrosine; by EGFR | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 172 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 442 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 576 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 576 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 583 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 583 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 626 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 639 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 663 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 769 | UniProt | In isoform P52735-3; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 771 | UniProt | In isoform P52735-3; Phosphoserine | ||||
Sequence: E | |||||||
Modified residue (large scale data) | 871 | PRIDE | Phosphotyrosine | ||||
Sequence: Y |
Post-translational modification
Phosphorylated on tyrosine residues in response to FGR activation.
Keywords
- PTM
Proteomic databases
PTM databases
Interaction
Subunit
Interacts (via SH2 domains) with the phosphorylated form of EPHA2. Interacts with SSX2IP (By similarity).
Interacts with NEK3 and PRLR and this interaction is prolactin-dependent
Interacts with NEK3 and PRLR and this interaction is prolactin-dependent
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | P52735 | ABI1 Q8IZP0 | 2 | EBI-297549, EBI-375446 | |
BINARY | P52735 | CAV1 Q03135 | 2 | EBI-297549, EBI-603614 | |
BINARY | P52735 | ERBB2 P04626 | 3 | EBI-297549, EBI-641062 | |
BINARY | P52735 | GAB1 Q13480 | 2 | EBI-297549, EBI-517684 | |
BINARY | P52735 | NEK3 P51956 | 3 | EBI-297549, EBI-476041 | |
BINARY | P52735 | SH3BP2 P78314 | 4 | EBI-297549, EBI-727062 | |
BINARY | P52735 | TOM1L1 O75674 | 2 | EBI-297549, EBI-712991 | |
BINARY | P52735 | TXNIP Q9H3M7 | 2 | EBI-297549, EBI-1369170 | |
BINARY | P52735-1 | CAV1 Q03135 | 3 | EBI-15875004, EBI-603614 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for domain, zinc finger.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-120 | Calponin-homology (CH) | ||||
Sequence: MEQWRQCGRWLIDCKVLPPNHRVVWPSAVVFDLAQALRDGVLLCQLLHNLSPGSIDLKDINFRPQMSQFLCLKNIRTFLKVCHDKFGLRNSELFDPFDLFDVRDFGKVISAVSRLSLHSI | ||||||
Domain | 198-376 | DH | ||||
Sequence: KRNCCLLEIQETEAKYYRTLEDIEKNYMSPLRLVLSPADMAAVFINLEDLIKVHHSFLRAIDVSVMVGGSTLAKVFLDFKERLLIYGEYCSHMEHAQNTLNQLLASREDFRQKVEECTLKVQDGKFKLQDLLVVPMQRVLKYHLLLKELLSHSAERPERQQLKEALEAMQDLAMYINEV | ||||||
Domain | 405-512 | PH | ||||
Sequence: RPKIDGELKVRSIVNHTKQDRYLFLFDKVVIVCKRKGYSYELKEIIELLFHKMTDDPMNNKDVKKSHGKMWSYGFYLIHLQGKQGFQFFCKTEDMKRKWMEQFEMAMS | ||||||
Zinc finger | 523-572 | Phorbol-ester/DAG-type | ||||
Sequence: HHSFQMYTFDKTTNCKACKMFLRGTFYQGYMCTKCGVGAHKECLEVIPPC | ||||||
Domain | 586-652 | SH3 1 | ||||
Sequence: GPGPKMVAMQNYHGNPAPPGKPVLTFQTGDVLELLRGDPESPWWEGRLVQTRKSGYFPSSSVKPCPV | ||||||
Domain | 673-767 | SH2 | ||||
Sequence: WFAGNMERQQTDNLLKSHASGTYLIRERPAEAERFAISIKFNDEVKHIKVVEKDNWIHITEAKKFDSLLELVEYYQCHSLKESFKQLDTTLKYPY | ||||||
Domain | 816-877 | SH3 2 | ||||
Sequence: RVIGTAVARYNFAARDMRELSLREGDVVRIYSRIGGDQGWWKGETNGRIGWFPSTYVEEEGI |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P52735-1
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
- Length878
- Mass (Da)101,289
- Last updated2008-07-22 v2
- ChecksumC186911605FD5B73
P52735-2
- Name2
P52735-3
- Name3
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_034900 | 185-189 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 241 | in Ref. 5; CAE45861 | ||||
Sequence: F → L | ||||||
Sequence conflict | 254 | in Ref. 5; CAE45861 | ||||
Sequence: F → L | ||||||
Alternative sequence | VSP_034901 | 470-474 | in isoform 2 and isoform 3 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_034902 | 783-811 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 877 | in Ref. 5; CAE45861 | ||||
Sequence: I → T |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
S76992 EMBL· GenBank· DDBJ | AAB34377.1 EMBL· GenBank· DDBJ | mRNA | ||
AL590710 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL445931 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AL357934 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471090 EMBL· GenBank· DDBJ | EAW88108.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC033187 EMBL· GenBank· DDBJ | AAH33187.1 EMBL· GenBank· DDBJ | mRNA | ||
BC132965 EMBL· GenBank· DDBJ | AAI32966.1 EMBL· GenBank· DDBJ | mRNA | ||
BC132967 EMBL· GenBank· DDBJ | AAI32968.1 EMBL· GenBank· DDBJ | mRNA | ||
BX640754 EMBL· GenBank· DDBJ | CAE45861.1 EMBL· GenBank· DDBJ | mRNA | ||
AY563001 EMBL· GenBank· DDBJ | AAS75591.1 EMBL· GenBank· DDBJ | mRNA |