Q9UKW4 (VAV3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Guanine nucleotide exchange factor VAV3
Short name=VAV-3

Gene names

Name:

VAV3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	847 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Exchange factor for GTP-binding proteins RhoA, RhoG and, to a lesser extent, Rac1. Binds physically to the nucleotide-free states of those 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. May be important for integrin-mediated signaling, at least in some cell types. In osteoclasts, along with SYK tyrosine kinase, required for signaling through integrin alpha-v/beta-1 (ITAGV-ITGB1), a crucial event for osteoclast proper cytoskeleton organization and function. This signaling pathway involves RAC1, but not RHO, activation. Necessary for proper wound healing. In the course of wound healing, required for the phagocytotic cup formation preceding macrophage phagocytosis of apoptotic neutrophils. Responsible for integrin beta-2 (ITGB2)-mediated macrophage adhesion and, to a lesser extent, contributes to beta-3 (ITGB3)-mediated adhesion. Does not affect integrin beta-1 (ITGB1)-mediated adhesion By similarity.
Subunit structure	Interacts with the PH domain of APS. Interacts (via SH2 domains) with the phosphorylated form of EPHA2. Interacts with ROS1; constitutive interaction that mediates VAV3 phosphorylation. Ref.7 Ref.8 Ref.9
Tissue specificity	Isoform 1 and isoform 3 are widely expressed; both are expressed at very low levels in skeletal muscle. In keratinocytes, isoform 1 is less abundant than isoform 3. Isoform 3 is detected at very low levels, if any, in adrenal gland, bone marrow, spleen, fetal brain and spinal chord; in these tissues, isoform 1 is readily detectable. Ref.1 Ref.7
Induction	Down-regulated by EGF and TGF-beta. Ref.1
Post-translational modification	Phosphorylated. Phosphorylation can be mediated by ROS1. In osteoclasts, undergoes tyrosine phosphorylation in response to CSF1 By similarity. Ref.7
Sequence similarities	Contains 1 CH (calponin-homology) domain. Contains 1 DH (DBL-homology) domain. Contains 1 PH domain. Contains 1 phorbol-ester/DAG-type zinc finger. Contains 1 SH2 domain. Contains 2 SH3 domains.
Sequence caution	The sequence AAD03799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Angiogenesis
Coding sequence diversity	Alternative promoter usage Alternative splicing Polymorphism
Domain	Repeat SH2 domain SH3 domain Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B cell receptor signaling pathway Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB Fc-gamma receptor signaling pathway involved in phagocytosis Traceable author statement. Source: Reactome angiogenesis Inferred from electronic annotation. Source: UniProtKB-KW apoptotic signaling pathway Traceable author statement. Source: Reactome cell migration Inferred from electronic annotation. Source: Compara innate immune response Traceable author statement. Source: Reactome integrin-mediated signaling pathway Inferred from electronic annotation. Source: Compara lamellipodium assembly Inferred from electronic annotation. Source: Compara neurotrophin TRK receptor signaling pathway Traceable author statement. Source: Reactome platelet activation Traceable author statement. Source: Reactome positive regulation of B cell proliferation Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB positive regulation of cell adhesion Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Inferred from electronic annotation. Source: Compara regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome response to DNA damage stimulus Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB response to drug Inferred from mutant phenotype PubMed 17875758. Source: UniProtKB small GTPase mediated signal transduction Traceable author statement. Source: Reactome vesicle fusion Inferred from electronic annotation. Source: Compara
Cellular_component	cytosol Traceable author statement. Source: Reactome plasma membrane Inferred from electronic annotation. Source: Compara
Molecular_function	GTPase activator activity Traceable author statement Ref.2. Source: ProtInc Rac guanyl-nucleotide exchange factor activity Inferred from electronic annotation. Source: Compara SH3/SH2 adaptor activity Traceable author statement Ref.2. Source: ProtInc guanyl-nucleotide exchange factor activity Inferred from experiment. Source: Reactome metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GRB2	P62993	5	EBI-297568,EBI-401755

Alternative products

This entry describes 4 isoforms produced by alternative promoter usage and alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9UKW4-1)

Also known as: Alpha;

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.

Isoform 2 (identifier: Q9UKW4-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-107: MEPWKQCAQW...DLFDVRDFGK → MQLPDCPCRAHLP

Isoform 3 (identifier: Q9UKW4-3)

Also known as: VAV3.1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-560: Missing.
     561-568: NCGRVNSG → MPIFTFLS

Note: May be produced by alternative promoter usage.

Isoform 4 (identifier: Q9UKW4-4)

The sequence of this isoform differs from the canonical sequence as follows:
     783-784: SL → SSPSLFCGFSFVTPPDYSFVPPSSTPFWSV

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 847

847

Guanine nucleotide exchange factor VAV3

PRO_0000080986

Regions

Domain

1 – 119

119

CH

Domain

192 – 371

180

DH

Domain

400 – 502

103

PH

Domain

592 – 660

69

SH3 1

Domain

672 – 766

95

SH2

Domain

788 – 847

60

SH3 2

Zinc finger

513 – 562

50

Phorbol-ester/DAG-type

Region

560 – 847

288

Sufficient for interaction with ROS1

Amino acid modifications

Modified residue

141

1

Phosphotyrosine Ref.10

Natural variations

Alternative sequence

1 – 560

560

Missing in isoform 3.

VSP_041360

Alternative sequence

1 – 107

107

MEPWK…RDFGK → MQLPDCPCRAHLP in isoform 2.

VSP_001820

Alternative sequence

561 – 568

8

NCGRVNSG → MPIFTFLS in isoform 3.

VSP_041361

Alternative sequence

783 – 784

2

SL → SSPSLFCGFSFVTPPDYSFV PPSSTPFWSV in isoform 4.

VSP_042359

Natural variant

139

1

D → N.
Corresponds to variant rs34318889 [ dbSNP | Ensembl ].

VAR_061800

Natural variant

298

1

T → S. Ref.1 Ref.6
Corresponds to variant rs7528153 [ dbSNP | Ensembl ].

VAR_033522

Natural variant

616

1

P → S.
Corresponds to variant rs12410676 [ dbSNP | Ensembl ].

VAR_051998

Natural variant

618

1

Q → H.
Corresponds to variant rs12403266 [ dbSNP | Ensembl ].

VAR_033523

Experimental info

Sequence conflict

107

1

K → E in AAC79695. Ref.1

Sequence conflict

217

1

Y → H in AAD20348. Ref.2

Sequence conflict

429

1

V → A in AAD20348. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

847

Helix Strand Turn

Details...

Helix

3 – 13

11

Helix

30 – 38

9

Helix

41 – 50

10

Helix

57 – 59

3

Helix

68 – 84

17

Turn

90 – 92

3

Helix

96 – 100

5

Helix

106 – 115

10

Helix

121 – 124

4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified May 1, 2000. Version 1. Checksum: C1E29F0B094CB721	FASTA	847	97,776
	10 20 30 40 50 60 MEPWKQCAQW LIHCKVLPTN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL RAHSINLKEI 70 80 90 100 110 120 NLRPQMSQFL CLKNIRTFLT ACCETFGMRK SELFEAFDLF DVRDFGKVIE TLSRLSRTPI 130 140 150 160 170 180 ALATGIRPFP TEESINDEDI YKGLPDLIDE TLVEDEEDLY DCVYGEDEGG EVYEDLMKAE 190 200 210 220 230 240 EAHQPKCPEN DIRSCCLAEI KQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPE 250 260 270 280 290 300 LVKLHRNLMQ EIHDSIVNKN DQNLYQVFIN YKERLVIYGQ YCSGVESAIS SLDYISKTKE 310 320 330 340 350 360 DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTTDPTE 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 FTRVTSCKVC QMLLRGTFYQ 550 560 570 580 590 600 GYLCFKCGAR AHKECLGRVD NCGRVNSGEQ GTLKLPEKRT NGLRRTPKQV DPGLPKMQVI 610 620 630 640 650 660 RNYSGTPPPA LHEGPPLQLQ AGDTVELLKG DAHSLFWQGR NLASGEVGFF PSDAVKPCPC 670 680 690 700 710 720 VPKPVDYSCQ PWYAGAMERL QAETELINRV NSTYLVRHRT KESGEYAISI KYNNEAKHIK 730 740 750 760 770 780 ILTRDGFFHI AENRKFKSLM ELVEYYKHHS LKEGFRTLDT TLQFPYKEPE HSAGQRGNRA 790 800 810 820 830 840 GNSLLSPKVL GIAIARYDFC ARDMRELSLL KGDVVKIYTK MSANGWWRGE VNGRVGWFPS TYVEEDE
	Isoform 2 (Beta) [UniParc]. Checksum: A67868CBD2FFD9A7	FASTA	753	86,696
	10 20 30 40 50 60 MQLPDCPCRA HLPVIETLSR LSRTPIALAT GIRPFPTEES INDEDIYKGL PDLIDETLVE 70 80 90 100 110 120 DEEDLYDCVY GEDEGGEVYE DLMKAEEAHQ PKCPENDIRS CCLAEIKQTE EKYTETLESI 130 140 150 160 170 180 EKYFMAPLKR FLTAAEFDSV FINIPELVKL HRNLMQEIHD SIVNKNDQNL YQVFINYKER 190 200 210 220 230 240 LVIYGQYCSG VESAISSLDY ISKTKEDVKL KLEECSKRAN NGKFTLRDLL VVPMQRVLKY 250 260 270 280 290 300 HLLLQELVKH TTDPTEKANL KLALDAMKDL AQYVNEVKRD NETLREIKQF QLSIENLNQP 310 320 330 340 350 360 VLLFGRPQGD GEIRITTLDK HTKQERHIFL FDLAVIVCKR KGDNYEMKEI IDLQQYKIAN 370 380 390 400 410 420 NPTTDKENKK WSYGFYLIHT QGQNGLEFYC KTKDLKKKWL EQFEMALSNI RPDYADSNFH 430 440 450 460 470 480 DFKMHTFTRV TSCKVCQMLL RGTFYQGYLC FKCGARAHKE CLGRVDNCGR VNSGEQGTLK 490 500 510 520 530 540 LPEKRTNGLR RTPKQVDPGL PKMQVIRNYS GTPPPALHEG PPLQLQAGDT VELLKGDAHS 550 560 570 580 590 600 LFWQGRNLAS GEVGFFPSDA VKPCPCVPKP VDYSCQPWYA GAMERLQAET ELINRVNSTY 610 620 630 640 650 660 LVRHRTKESG EYAISIKYNN EAKHIKILTR DGFFHIAENR KFKSLMELVE YYKHHSLKEG 670 680 690 700 710 720 FRTLDTTLQF PYKEPEHSAG QRGNRAGNSL LSPKVLGIAI ARYDFCARDM RELSLLKGDV 730 740 750 VKIYTKMSAN GWWRGEVNGR VGWFPSTYVE EDE
	Isoform 3 (VAV3.1) [UniParc]. Checksum: D23C21EBEF7F48CF	FASTA	287	32,604
	10 20 30 40 50 60 MPIFTFLSEQ GTLKLPEKRT NGLRRTPKQV DPGLPKMQVI RNYSGTPPPA LHEGPPLQLQ 70 80 90 100 110 120 AGDTVELLKG DAHSLFWQGR NLASGEVGFF PSDAVKPCPC VPKPVDYSCQ PWYAGAMERL 130 140 150 160 170 180 QAETELINRV NSTYLVRHRT KESGEYAISI KYNNEAKHIK ILTRDGFFHI AENRKFKSLM 190 200 210 220 230 240 ELVEYYKHHS LKEGFRTLDT TLQFPYKEPE HSAGQRGNRA GNSLLSPKVL GIAIARYDFC 250 260 270 280 ARDMRELSLL KGDVVKIYTK MSANGWWRGE VNGRVGWFPS TYVEEDE
	Isoform 4 [UniParc]. Checksum: AD6B651338EEE812	FASTA	875	100,828
	10 20 30 40 50 60 MEPWKQCAQW LIHCKVLPTN HRVTWDSAQV FDLAQTLRDG VLLCQLLNNL RAHSINLKEI 70 80 90 100 110 120 NLRPQMSQFL CLKNIRTFLT ACCETFGMRK SELFEAFDLF DVRDFGKVIE TLSRLSRTPI 130 140 150 160 170 180 ALATGIRPFP TEESINDEDI YKGLPDLIDE TLVEDEEDLY DCVYGEDEGG EVYEDLMKAE 190 200 210 220 230 240 EAHQPKCPEN DIRSCCLAEI KQTEEKYTET LESIEKYFMA PLKRFLTAAE FDSVFINIPE 250 260 270 280 290 300 LVKLHRNLMQ EIHDSIVNKN DQNLYQVFIN YKERLVIYGQ YCSGVESAIS SLDYISKTKE 310 320 330 340 350 360 DVKLKLEECS KRANNGKFTL RDLLVVPMQR VLKYHLLLQE LVKHTTDPTE 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 FTRVTSCKVC QMLLRGTFYQ 550 560 570 580 590 600 GYLCFKCGAR AHKECLGRVD NCGRVNSGEQ GTLKLPEKRT NGLRRTPKQV DPGLPKMQVI 610 620 630 640 650 660 RNYSGTPPPA LHEGPPLQLQ AGDTVELLKG DAHSLFWQGR NLASGEVGFF PSDAVKPCPC 670 680 690 700 710 720 VPKPVDYSCQ PWYAGAMERL QAETELINRV NSTYLVRHRT KESGEYAISI KYNNEAKHIK 730 740 750 760 770 780 ILTRDGFFHI AENRKFKSLM ELVEYYKHHS LKEGFRTLDT TLQFPYKEPE HSAGQRGNRA 790 800 810 820 830 840 GNSSPSLFCG FSFVTPPDYS FVPPSSTPFW SVLSPKVLGI AIARYDFCAR DMRELSLLKG 850 860 870 DVVKIYTKMS ANGWWRGEVN GRVGWFPSTY VEEDE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Non-stoichiometric reduced complexity probes for cDNA arrays." Trenkle T., Welsh J., Jung B., Mathieu-Daude F., McClelland M. Nucleic Acids Res. 26:3883-3891(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 1-692 (ISOFORM 3), ALTERNATIVE PROMOTER USAGE, TISSUE SPECIFICITY, INDUCTION, VARIANT SER-298. Tissue: Keratinocyte.
[2]	"Biological and regulatory properties of Vav-3, a new member of the Vav family of oncoproteins." Movilla N., Bustelo X.R. Mol. Cell. Biol. 19:7870-7885(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), ALTERNATIVE SPLICING.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Trachea.
[4]	"The DNA sequence and biological annotation of human chromosome 1." Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R. Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT SER-298.
[7]	"Vav3 mediates receptor protein tyrosine kinase signaling, regulates GTPase activity, modulates cell morphology, and induces cell transformation." Zeng L., Sachdev P., Yan L., Chan J.L., Trenkle T., McClelland M., Welsh J., Wang L.H. Mol. Cell. Biol. 20:9212-9224(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ROS1, PHOSPHORYLATION, TISSUE SPECIFICITY.
[8]	"Adaptor protein APS binds the NH2-terminal autoinhibitory domain of guanine nucleotide exchange factor Vav3 and augments its activity." Yabana N., Shibuya M. Oncogene 21:7720-7729(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH APS.
[9]	"Essential role of Vav family guanine nucleotide exchange factors in EphA receptor-mediated angiogenesis." Hunter S.G., Zhuang G., Brantley-Sieders D.M., Swat W., Cowan C.W., Chen J. Mol. Cell. Biol. 26:4830-4842(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPHA2.
[10]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-141, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[11]	"Solution structure of the CH domain from human VAV-3 protein." RIKEN structural genomics initiative (RSGI) Submitted (DEC-2006) to the PDB data bank Cited for: STRUCTURE BY NMR OF 1-134.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF035442 mRNA. Translation: AAD03799.1. Different initiation.
AF067817 mRNA. Translation: AAC79695.1.
AF118887 mRNA. Translation: AAD20349.1.
AF118886 mRNA. Translation: AAD20348.1.
AK304088 mRNA. Translation: BAG64994.1.
AK316295 mRNA. Translation: BAH14666.1.
AL391235 , AC114491, AL353892, AL513206, AL591042 Genomic DNA. Translation: CAH72458.1.
AL513206 , AC114491, AL353892, AL391235, AL591042 Genomic DNA. Translation: CAH73195.1.
AL513206, AC114491, AL591042 Genomic DNA. Translation: CAH73196.1.
AL591042 , AC114491, AL353892, AL391235, AL513206 Genomic DNA. Translation: CAI14457.1.
AL591042, AC114491, AL513206 Genomic DNA. Translation: CAI14458.1.
AL353892 , AC114491, AL391235, AL513206, AL591042 Genomic DNA. Translation: CAI21786.1.
CH471156 Genomic DNA. Translation: EAW51252.1.
BC143969 mRNA. Translation: AAI43970.1.

IPI

IPI00219689.
IPI00299763.
IPI00976117.

RefSeq

NP_001073343.1. NM_001079874.1.
NP_006104.4. NM_006113.4.

UniGene

Hs.267659.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D86	NMR	-	A	1-130	[»]

ProteinModelPortal

Q9UKW4.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9UKW4. 3 interactions.

MINT

MINT-256977.

STRING

9606.ENSP00000359073.

PTM databases

PhosphoSite

Q9UKW4.

Polymorphism databases

DMDM

12643372.

Proteomic databases

PaxDb

Q9UKW4.

PRIDE

Q9UKW4.

Protocols and materials databases

DNASU

10451.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000370056; ENSP00000359073; ENSG00000134215.
ENST00000415432; ENSP00000394897; ENSG00000134215.
ENST00000527011; ENSP00000432540; ENSG00000134215.

GeneID

10451.

KEGG

hsa:10451.

UCSC

uc001dvj.1. human.
uc001dvk.1. human.
uc010ouw.1. human.

Organism-specific databases

CTD

10451.

GeneCards

GC01M108113.

HGNC

HGNC:12659. VAV3.

HPA

CAB002012.
HPA028138.

MIM

605541. gene.

neXtProt

NX_Q9UKW4.

PharmGKB

PA37282.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG326494.

HOGENOM

HOG000049191.

HOVERGEN

HBG018066.

InParanoid

Q9UKW4.

KO

K05730.

OMA

EAKHIKI.

OrthoDB

EOG4TB49P.

PhylomeDB

Q9UKW4.

Enzyme and pathway databases

Pathway_Interaction_DB

ar_pathway. Coregulation of Androgen receptor activity.
epha_fwdpathway. EPHA forward signaling.
epha2_fwdpathway. EPHA2 forward signaling.
avb3_integrin_pathway. Integrins in angiogenesis.
avb3_opn_pathway. Osteopontin-mediated events.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SignaLink

Q9UKW4.

Gene expression databases

ArrayExpress

Q9UKW4.

Bgee

Q9UKW4.

CleanEx

HS_VAV3.

Genevestigator

Q9UKW4.

GermOnline

ENSG00000134215. Homo sapiens.

Family and domain databases

Gene3D

1.10.418.10. 1 hit.
1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
3.30.505.10. 1 hit.

InterPro

IPR001715. CH-domain.
IPR000219. DH-domain.
IPR001331. GDS_CDC24_CS.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR000980. SH2.
IPR011511. SH3_2.
IPR001452. SH3_domain.
IPR003096. SM22_calponin.
[Graphical view]

Pfam

PF00130. C1_1. 1 hit.
PF00307. CH. 1 hit.
PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF00017. SH2. 1 hit.
PF07653. SH3_2. 2 hits.
[Graphical view]

PRINTS

PR00401. SH2DOMAIN.
PR00452. SH3DOMAIN.
PR00888. SM22CALPONIN.

SMART

SM00109. C1. 1 hit.
SM00033. CH. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
SM00252. SH2. 1 hit.
SM00326. SH3. 2 hits.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.
SSF48065. DH-domain. 1 hit.
SSF50044. SH3. 2 hits.

PROSITE

PS50021. CH. 1 hit.
PS00741. DH_1. 1 hit.
PS50010. DH_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
PS50001. SH2. 1 hit.
PS50002. SH3. 2 hits.
PS00479. ZF_DAG_PE_1. 1 hit.
PS50081. ZF_DAG_PE_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

VAV3. human.

EvolutionaryTrace

Q9UKW4.

GenomeRNAi

10451.

NextBio

39617.

SOURCE

Search...

Entry information

Entry name

VAV3_HUMAN

Accession

Primary (citable) accession number: Q9UKW4
Secondary accession number(s): B1AMM0 , B1APV5, B4E232, B7ZLR1, E9PQ97, O60498, O95230, Q9Y5X8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 24, 2001
Last sequence update:	May 1, 2000
Last modified:	May 29, 2013
This is version 136 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.