Q9R0C8

SS
Gene name
Vav3
Protein name
Guanine nucleotide exchange factor VAV3
Names
VAV-3
Species
Mus musculus (Mouse)
KEGG Pathway
mmu:57257
EC number
Protein Class

Descriptions

The Vav family is a group of tyrosine phosphorylation-dependent guanine nucleotide exchange factors (GEFs) that activate members of the Rac and Rho families of guanosine triphosphatases (GTPases) downstream of protein tyrosine kinases. When the tyrosine residues within the acidic (Ac) region are non-phosphorylated, the CH domain and Ac region occlude the GTPase-binding site within DH domain. The interaction is stabilized by the interaction between the hydroxyl group of Tyr174 within Ac region and GTPase binding site as well as the interaction between CH domain and DH-PH domains. The Y174F mutant displays constitutive and phosphorylation-independent catalytic activity. In addition to the N-terminal autoinhibitory regions, the truncation of C-terminal SH3 domain also relives the autoinhibition. C-terminal SH3 domain interacts with DH-PH domains and the intramolecular interaction occludes the GTPase-binding site of DH domain.

Autoinhibitory domains (AIDs)

1-134 (CH domain) SS

Target domain

192-371 (DH domain)

Relief mechanism

PTM

Assay

166-177 (a helix in N-terminal acidic region) SS

Target domain

192-371 (DH domain)

Relief mechanism

PTM

Assay

788-847 (C-terminal SH3 domain) SS

Target domain

192-371 (DH domain)

Relief mechanism

Partner binding, PTM

Assay

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q9R0C8

Entry ID Method Resolution Chain Position Source
AF-Q9R0C8-F1 Predicted AlphaFoldDB

27 variants for Q9R0C8

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3393440195 19 P>S No EVA
rs3541755117 26 D>E No EVA
rs3388648761 83 C>* No EVA
rs3388658043 91 S>N No EVA
rs3393503388 104 D>Y No EVA
rs3388662280 134 S>I No EVA
rs3388651859 158 D>V No EVA
rs3388658072 166 E>D No EVA
rs3393503397 178 K>E No EVA
rs3388656710 224 R>G No EVA
rs3541714048 315 N>Y No EVA
rs3388664093 336 L>I No EVA
rs3388651881 362 K>E No EVA
rs3388648241 364 L>F No EVA
rs3388661135 432 C>Y No EVA
rs3388651845 535 R>G No EVA
rs3388660317 559 V>I No EVA
rs3388651865 570 Q>* No EVA
rs3393052392 572 P>A No EVA
rs3388640588 663 K>N No EVA
rs3388659803 703 S>Y No EVA
rs3388640613 727 F>L No EVA
rs3388656703 728 F>L No EVA
rs3388654393 738 S>G No EVA
rs3541705035 770 E>D No EVA
rs3388648764 790 L>V No EVA
rs3388651899 791 G>S No EVA

No associated diseases with Q9R0C8

13 regional properties for Q9R0C8

Type Name Position InterPro Accession
domain Dbl homology (DH) domain 192 - 371 IPR000219
domain SH2 domain 670 - 766 IPR000980
conserved_site Guanine-nucleotide dissociation stimulator, CDC24, conserved site 320 - 345 IPR001331
domain SH3 domain 592 - 660 IPR001452-1
domain SH3 domain 788 - 847 IPR001452-2
domain Calponin homology domain 1 - 119 IPR001715
domain Pleckstrin homology domain 400 - 504 IPR001849
domain Protein kinase C-like, phorbol ester/diacylglycerol-binding domain 513 - 563 IPR002219
domain Calmodulin-regulated spectrin-associated protein-like, Calponin-homology domain 19 - 103 IPR022613
domain VAV3 protein, second SH3 domain 791 - 846 IPR035734
domain VAV3, SH2 domain 666 - 768 IPR035881
domain Vav, PH domain 383 - 506 IPR037832
domain VAV3 protein, first SH3 domain 596 - 657 IPR047015

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
cytoplasm The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures.
immunological synapse An area of close contact between a lymphocyte (T-, B-, or natural killer cell) and a target cell formed through the clustering of particular signaling and adhesion molecules and their associated membrane rafts on both the lymphocyte and the target cell and facilitating activation of the lymphocyte, transfer of membrane from the target cell to the lymphocyte, and in some situations killing of the target cell through release of secretory granules and/or death-pathway ligand-receptor interaction.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.

3 GO annotations of molecular function

Name Definition
epidermal growth factor receptor binding Binding to an epidermal growth factor receptor.
guanyl-nucleotide exchange factor activity Stimulates the exchange of GDP to GTP on a signaling GTPase, changing its conformation to its active form. Guanine nucleotide exchange factors (GEFs) act by stimulating the release of guanosine diphosphate (GDP) to allow binding of guanosine triphosphate (GTP), which is more abundant in the cell under normal cellular physiological conditions.
metal ion binding Binding to a metal ion.

15 GO annotations of biological process

Name Definition
angiogenesis Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels.
B cell receptor signaling pathway The series of molecular signals initiated by the cross-linking of an antigen receptor on a B cell.
cell migration The controlled self-propelled movement of a cell from one site to a destination guided by molecular cues.
cell projection assembly Formation of a prolongation or process extending from a cell, e.g. a flagellum or axon.
DNA damage response Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism.
integrin-mediated signaling pathway The series of molecular signals initiated by an extracellular ligand binding to an integrin on the surface of a target cell, and ending with the regulation of a downstream cellular process, e.g. transcription.
lamellipodium assembly Formation of a lamellipodium, a thin sheetlike extension of the surface of a migrating cell.
neutrophil chemotaxis The directed movement of a neutrophil cell, the most numerous polymorphonuclear leukocyte found in the blood, in response to an external stimulus, usually an infection or wounding.
positive regulation of B cell proliferation Any process that activates or increases the rate or extent of B cell proliferation.
positive regulation of cell adhesion Any process that activates or increases the frequency, rate or extent of cell adhesion.
positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction Any process that activates or increases the frequency, rate or extent of protein kinase B signaling, a series of reactions mediated by the intracellular serine/threonine kinase protein kinase B.
regulation of cell size Any process that modulates the size of a cell.
response to xenobiotic stimulus Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical.
small GTPase-mediated signal transduction The series of molecular signals in which a small monomeric GTPase relays a signal.
vesicle fusion Fusion of the membrane of a transport vesicle with its target membrane.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q9NHV9 Vav Protein vav Drosophila melanogaster (Fruit fly) SS
P15498 VAV1 Proto-oncogene vav Homo sapiens (Human) EV SS
P52735 VAV2 Guanine nucleotide exchange factor VAV2 Homo sapiens (Human) SS
Q9UKW4 VAV3 Guanine nucleotide exchange factor VAV3 Homo sapiens (Human) SS
P27870 Vav1 Proto-oncogene vav Mus musculus (Mouse) EV
Q60992 Vav2 Guanine nucleotide exchange factor VAV2 Mus musculus (Mouse) SS
P54100 Vav1 Proto-oncogene vav Rattus norvegicus (Rat) SS
Q45FX5 vav-1 Protein vav-1 Caenorhabditis elegans SS
10 20 30 40 50 60
MEPWKQCAQW LIHSKVLPPN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL RPHSINLKEI
70 80 90 100 110 120
NLRPQMSQFL CLKNIRTFLA ACCDTFGMRK SELFEAFDLF DVRDFGKVIE TLSRLSRTPI
130 140 150 160 170 180
ALATGIRPFP TEESINDEDI YKGLPDLIDE TRVEDEEDLY DCVYGEDEGG EVYEDLMKAE
190 200 210 220 230 240
EAQQPKSQEN DIRSCCLAEI RQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPD
250 260 270 280 290 300
LVKVHRSLMQ EIHDSIVNKD DQNLYQVFIN YKERLVIYGQ YCSGVESAIS NLDYISKTKE
310 320 330 340 350 360
DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTHDPME KANLKLALDA
370 380 390 400 410 420
MKDLAQYVNE VKRDNETLRE IKQFQLSIEN LNQPVLLFGR PQGDGEIRIT TLDKHTKQER
430 440 450 460 470 480
HIFLFDLAVI VCKRKGDNYE MKEIIDLQQY KIANNPTTDK ENKKWSYGFY LIHTQGQNGL
490 500 510 520 530 540
EFYCKTKDLK KKWLEQFEMA LSNIRPDYAD SNFHDFKMHT FTRVTSCRVC QMLLRGTFYQ
550 560 570 580 590 600
GYLCFKCGAK AHKECLGRVD NCGRVNSVEQ GPFKPPEKRT NGLRRASRQV DPGLPKMQVI
610 620 630 640 650 660
RNYTGTPAPG LHEGPPLHIQ AGDTVELLRG DAHSVFWQGR NLASGEVGFF PSDAVKPSPC
670 680 690 700 710 720
VPKPVDYSCQ PWYAGPMERL QAETELINRV NSTYLVRHRT KESGEYAISI KYNNEAKHIK
730 740 750 760 770 780
ILTRDGFFHI AENRKFKSLM ELVEYYKHHS LKEGFRTLDT TLQFPYKEPE QPAGQRGNRT
790 800 810 820 830 840
GNSLLSPKVL GIAIARYDFC ARDMRELSLL KGDMVKIYTK MSANGWWRGE VNGRVGWFPS
TYVEEDE