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Rho guanine nucleotide exchange factor 2 (Guanine nucleotide exchange factor H1) (GEF-H1) (LBC'S first cousin) (Lymphoid blast crisis-like 1) (Oncogene LFC) (Rhobin)

 ARHG2_MOUSE             Reviewed;         985 AA.
Q60875; E9QNW9; O09115; Q3TBI4; Q3TJ16; Q8CHE1; Q923E0; Q9ESG7;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 4.
31-JAN-2018, entry version 159.
RecName: Full=Rho guanine nucleotide exchange factor 2;
AltName: Full=Guanine nucleotide exchange factor H1;
Short=GEF-H1;
AltName: Full=LBC'S first cousin;
AltName: Full=Lymphoid blast crisis-like 1;
AltName: Full=Oncogene LFC;
AltName: Full=Rhobin;
Name=Arhgef2; Synonyms=Kiaa0651, Lbcl1, Lfc;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Myeloid;
PubMed=7629163; DOI=10.1074/jbc.270.31.18388;
Whitehead I., Kirk H., Tognon C., Trigo-Gonzalez G., Kay R.;
"Expression cloning of lfc, a novel oncogene with structural
similarities to guanine nucleotide exchange factors and to the
regulatory region of protein kinase C.";
J. Biol. Chem. 270:18388-18395(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=BALB/cJ;
Olofsson B.;
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
De Sepulveda P., Rottapel R.;
Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=12465718; DOI=10.1093/dnares/9.5.179;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T.,
Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
I. The complete nucleotide sequences of 100 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 9:179-188(2002).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, and Liver;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
SUBCELLULAR LOCATION.
PubMed=12604587; DOI=10.1083/jcb.200211047;
Benais-Pont G., Punn A., Flores-Maldonado C., Eckert J., Raposo G.,
Fleming T.P., Cereijido M., Balda M.S., Matter K.;
"Identification of a tight junction-associated guanine nucleotide
exchange factor that activates Rho and regulates paracellular
permeability.";
J. Cell Biol. 160:729-740(2003).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain cortex;
PubMed=17114649; DOI=10.1074/mcp.M600046-MCP200;
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,
Gerrits B., Panse C., Schlapbach R., Mansuy I.M.;
"Qualitative and quantitative analyses of protein phosphorylation in
naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-931 AND SER-959, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
REVIEW ON FUNCTION.
PubMed=18394899; DOI=10.1016/j.tcb.2008.02.006;
Birkenfeld J., Nalbant P., Yoon S.-H., Bokoch G.M.;
"Cellular functions of GEF-H1, a microtubule-regulated Rho-GEF: is
altered GEF-H1 activity a crucial determinant of disease
pathogenesis?";
Trends Cell Biol. 18:210-219(2008).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-163; SER-174; SER-646;
SER-781; THR-795; SER-885; SER-931; SER-939; SER-940; SER-955 AND
SER-959, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-646, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-151; SER-163; SER-174;
SER-885; SER-939; SER-940; THR-944; SER-946; SER-951; SER-952; SER-955
AND SER-959, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[15]
INTERACTION WITH CAPN6.
PubMed=21406564; DOI=10.1242/jcs.072561;
Tonami K., Kurihara Y., Arima S., Nishiyama K., Uchijima Y., Asano T.,
Sorimachi H., Kurihara H.;
"Calpain-6, a microtubule-stabilizing protein, regulates Rac1 activity
and cell motility through interaction with GEF-H1.";
J. Cell Sci. 124:1214-1223(2011).
[16]
FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND DISRUPTION
PHENOTYPE.
PubMed=28453519; DOI=10.1371/journal.pgen.1006746;
Ravindran E., Hu H., Yuzwa S.A., Hernandez-Miranda L.R., Kraemer N.,
Ninnemann O., Musante L., Boltshauser E., Schindler D., Huebner A.,
Reinecker H.C., Ropers H.H., Birchmeier C., Miller F.D., Wienker T.F.,
Huebner C., Kaindl A.M.;
"Homozygous ARHGEF2 mutation causes intellectual disability and
midbrain-hindbrain malformation.";
PLoS Genet. 13:E1006746-E1006746(2017).
-!- FUNCTION: Activates Rho-GTPases by promoting the exchange of GDP
for GTP. May be involved in epithelial barrier permeability, cell
motility and polarization, dendritic spine morphology, antigen
presentation, leukemic cell differentiation, cell cycle
regulation, innate immune response, and cancer. Binds Rac-GTPases,
but does not seem to promote nucleotide exchange activity toward
Rac-GTPases. May stimulate instead the cortical activity of Rac.
Inactive toward CDC42, TC10, or Ras-GTPases. Forms an
intracellular sensing system along with NOD1 for the detection of
microbial effectors during cell invasion by pathogens. Involved in
innate immune signaling transduction pathway promoting cytokine
IL6/interleukin-6 and TNF-alpha secretion in macrophage upon
stimulation by bacterial peptidoglycans; acts as a signaling
intermediate between NOD2 receptor and RIPK2 kinase. Contributes
to the tyrosine phosphorylation of RIPK2 through Src tyrosine
kinase leading to NF-kappaB activation by NOD2. Overexpression
activates Rho-, but not Rac-GTPases, and increases paracellular
permeability (By similarity). Involved in neuronal progenitor cell
division and differentiation (PubMed:28453519). Involved in the
migration of precerebellar neurons (PubMed:28453519).
{ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974,
ECO:0000269|PubMed:28453519}.
-!- SUBUNIT: Found in a complex composed at least of ARHGEF2, NOD2 and
RIPK2. Interacts with RIPK2; the interaction mediates tyrosine
phosphorylation of RIPK2 by Src kinase CSK. Interacts with RIPK1
and RIPK3. Interacts with YWHAZ/14-3-3 zeta; when phosphorylated
at Ser-885. Interacts with the kinases PAK4, AURKA and MAPK1.
Interacts with RHOA and RAC1. Interacts with NOD1 (By similarity).
Interacts (via the N- terminal zinc finger) with CAPN6 (via domain
II). Interacts with DYNLT1. {ECO:0000250,
ECO:0000250|UniProtKB:Q865S3, ECO:0000269|PubMed:21406564}.
-!- INTERACTION:
Q61097:Ksr1; NbExp=5; IntAct=EBI-772191, EBI-1536336;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}.
Cytoplasm {ECO:0000250|UniProtKB:Q865S3,
ECO:0000250|UniProtKB:Q92974}. Cell junction, tight junction
{ECO:0000269|PubMed:12604587}. Golgi apparatus
{ECO:0000250|UniProtKB:Q92974}. Cytoplasm, cytoskeleton, spindle
{ECO:0000250|UniProtKB:Q865S3, ECO:0000250|UniProtKB:Q92974}.
Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q92974}. Note=Localizes
to the tips of cortical microtubules of the mitotic spindle during
cell division, and is further released upon microtubule
depolymerization (By similarity). Colocalized with NOD2 and RIPK2
in vesicles and with the cytoskeleton (By similarity). Associated
with apical intercellular junctions in the trophectoderm of the
blastocyst (PubMed:12604587). {ECO:0000250|UniProtKB:Q92974,
ECO:0000269|PubMed:12604587}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=Q60875-1; Sequence=Displayed;
Name=2;
IsoId=Q60875-2; Sequence=VSP_022641;
Name=3;
IsoId=Q60875-3; Sequence=VSP_022640, VSP_022642, VSP_022643;
Name=4;
IsoId=Q60875-4; Sequence=VSP_034962;
Name=5;
IsoId=Q60875-5; Sequence=VSP_034962, VSP_034963;
-!- TISSUE SPECIFICITY: Ubiquitous, with the exception of liver
tissue. Levels are high in hemopoietic tissues (thymus, spleen,
bone marrow) as well as in kidney and lung. Expressed in the
germinal zones of both the neocortex and the cerebellum and in the
pontine gray nuclei (PubMed:28453519).
{ECO:0000269|PubMed:28453519}.
-!- DEVELOPMENTAL STAGE: Expressed in the neuroepithelium of
telencephalon, diencephalon and rhombencephalon at 11 dpc
(PubMed:28453519). {ECO:0000269|PubMed:28453519}.
-!- DOMAIN: The DH (DBL-homology) domain promotes tyrosine
phosphorylation of RIPK2 (By similarity). The DH (DBL-homology)
domain interacts with and promotes loading of GTP on RhoA.
{ECO:0000250}.
-!- DOMAIN: The PH domain has no affinity for phosphoinositides
suggesting that it does not interact directly with membranes.
{ECO:0000250|UniProtKB:Q92974}.
-!- DOMAIN: The phorbol-ester/DAG-type zinc-finger and the C-terminal
coiled-coil domains (606-986) are both important for association
with microtubules. {ECO:0000250|UniProtKB:Q92974}.
-!- PTM: Phosphorylation of Ser-885 by PAK1 induces binding to protein
YWHAZ, promoting its relocation to microtubules and the inhibition
of its activity. Phosphorylated by AURKA and CDK1 during mitosis,
which negatively regulates its activity. Phosphorylation by MAPK1
or MAPK3 increases nucleotide exchange activity. Phosphorylation
by PAK4 releases GEF-H1 from the microtubules. Phosphorylated on
serine, threonine and tyrosine residues in a RIPK2-dependent
manner (By similarity). {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show reduced volume of the total brain,
the cerebellum and the brainstem. Show complete lack of
precerebellar pontin gray and reticulotegmental nuclei. Show
impaired precerebellar neuron migration.
{ECO:0000269|PubMed:28453519}.
-!- SEQUENCE CAUTION:
Sequence=BAC41438.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U28495; AAC52234.1; -; mRNA.
EMBL; X95761; CAA65067.1; -; mRNA.
EMBL; AF177032; AAG09271.1; -; mRNA.
EMBL; AB093254; BAC41438.1; ALT_INIT; mRNA.
EMBL; AK167628; BAE39679.1; -; mRNA.
EMBL; AK171223; BAE42325.1; -; mRNA.
EMBL; AC145168; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC006589; AAH06589.1; -; mRNA.
CCDS; CCDS17481.1; -. [Q60875-1]
CCDS; CCDS57221.1; -. [Q60875-5]
CCDS; CCDS57222.1; -. [Q60875-4]
PIR; I49342; I49342.
RefSeq; NP_001185840.1; NM_001198911.1.
RefSeq; NP_001185841.1; NM_001198912.1. [Q60875-4]
RefSeq; NP_001185842.1; NM_001198913.1. [Q60875-5]
RefSeq; NP_032513.3; NM_008487.3. [Q60875-1]
RefSeq; XP_006501130.1; XM_006501067.3. [Q60875-4]
UniGene; Mm.239329; -.
UniGene; Mm.482396; -.
PDB; 5WI4; X-ray; 2.00 A; A/B/C=139-164.
PDBsum; 5WI4; -.
ProteinModelPortal; Q60875; -.
SMR; Q60875; -.
BioGrid; 201114; 13.
IntAct; Q60875; 8.
MINT; MINT-2982807; -.
STRING; 10090.ENSMUSP00000029694; -.
iPTMnet; Q60875; -.
PhosphoSitePlus; Q60875; -.
SwissPalm; Q60875; -.
PaxDb; Q60875; -.
PeptideAtlas; Q60875; -.
PRIDE; Q60875; -.
Ensembl; ENSMUST00000029694; ENSMUSP00000029694; ENSMUSG00000028059. [Q60875-1]
Ensembl; ENSMUST00000107510; ENSMUSP00000103134; ENSMUSG00000028059. [Q60875-4]
Ensembl; ENSMUST00000170653; ENSMUSP00000127843; ENSMUSG00000028059. [Q60875-5]
Ensembl; ENSMUST00000175911; ENSMUSP00000135428; ENSMUSG00000028059. [Q60875-3]
GeneID; 16800; -.
KEGG; mmu:16800; -.
UCSC; uc008pvw.2; mouse. [Q60875-1]
UCSC; uc008pvy.2; mouse. [Q60875-5]
UCSC; uc008pwa.1; mouse. [Q60875-3]
CTD; 9181; -.
MGI; MGI:103264; Arhgef2.
eggNOG; ENOG410IR0Y; Eukaryota.
eggNOG; ENOG410XT68; LUCA.
GeneTree; ENSGT00760000119193; -.
HOVERGEN; HBG050566; -.
InParanoid; Q60875; -.
KO; K12791; -.
OMA; QSVRICP; -.
OrthoDB; EOG091G00G7; -.
TreeFam; TF325887; -.
Reactome; R-MMU-193648; NRAGE signals death through JNK.
Reactome; R-MMU-194840; Rho GTPase cycle.
Reactome; R-MMU-416482; G alpha (12/13) signalling events.
ChiTaRS; Arhgef2; mouse.
PRO; PR:Q60875; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000028059; -.
ExpressionAtlas; Q60875; baseline and differential.
Genevisible; Q60875; MM.
GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005856; C:cytoskeleton; ISS:UniProtKB.
GO; GO:0043198; C:dendritic shaft; IDA:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
GO; GO:0005874; C:microtubule; ISS:UniProtKB.
GO; GO:0043025; C:neuronal cell body; IDA:MGI.
GO; GO:0002102; C:podosome; IDA:MGI.
GO; GO:0014069; C:postsynaptic density; IDA:MGI.
GO; GO:0043234; C:protein complex; ISS:UniProtKB.
GO; GO:0032587; C:ruffle membrane; ISS:UniProtKB.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0031982; C:vesicle; ISS:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IDA:MGI.
GO; GO:0048365; F:Rac GTPase binding; ISS:UniProtKB.
GO; GO:0030676; F:Rac guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
GO; GO:0017048; F:Rho GTPase binding; ISS:UniProtKB.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; IDA:MGI.
GO; GO:0007015; P:actin filament organization; IPI:MGI.
GO; GO:0055059; P:asymmetric neuroblast division; IMP:UniProtKB.
GO; GO:0000902; P:cell morphogenesis; IDA:MGI.
GO; GO:0071225; P:cellular response to muramyl dipeptide; ISS:UniProtKB.
GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0007026; P:negative regulation of microtubule depolymerization; ISS:UniProtKB.
GO; GO:0050768; P:negative regulation of neurogenesis; IMP:UniProtKB.
GO; GO:0071802; P:negative regulation of podosome assembly; IMP:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB.
GO; GO:2001224; P:positive regulation of neuron migration; IMP:UniProtKB.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:UniProtKB.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0032760; P:positive regulation of tumor necrosis factor production; ISS:UniProtKB.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IDA:MGI.
CDD; cd00029; C1; 1.
CDD; cd00160; RhoGEF; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR002219; PE/DAG-bd.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
Pfam; PF00169; PH; 1.
Pfam; PF00621; RhoGEF; 1.
SMART; SM00109; C1; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS00479; ZF_DAG_PE_1; 1.
PROSITE; PS50081; ZF_DAG_PE_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell cycle;
Cell division; Cell junction; Coiled coil; Complete proteome;
Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Developmental protein;
Differentiation; Golgi apparatus; Guanine-nucleotide releasing factor;
Immunity; Innate immunity; Metal-binding; Microtubule; Mitosis;
Neurogenesis; Phosphoprotein; Proto-oncogene; Reference proteome;
Tight junction; Zinc; Zinc-finger.
CHAIN 1 985 Rho guanine nucleotide exchange factor 2.
/FTId=PRO_0000080910.
DOMAIN 236 433 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 473 572 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
ZN_FING 39 86 Phorbol-ester/DAG-type.
{ECO:0000255|PROSITE-ProRule:PRU00226}.
REGION 131 161 Interaction with DYNLT1.
{ECO:0000250|UniProtKB:Q865S3}.
COILED 591 619 {ECO:0000255}.
COILED 797 866 {ECO:0000255}.
COMPBIAS 493 496 Poly-Leu.
MOD_RES 109 109 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 122 122 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 129 129 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 133 133 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 143 143 Phosphoserine; by PAK4.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 151 151 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 163 163 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 172 172 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 174 174 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 177 177 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 354 354 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 646 646 Phosphoserine.
{ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:19144319}.
MOD_RES 649 649 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 680 680 Phosphothreonine; by MAPK1 or MAPK3.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 692 692 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 710 710 Phosphoserine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 781 781 Phosphoserine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 795 795 Phosphothreonine.
{ECO:0000244|PubMed:19144319}.
MOD_RES 885 885 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 893 893 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 895 895 Phosphoserine; by PAK4.
{ECO:0000250|UniProtKB:Q92974}.
MOD_RES 931 931 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319}.
MOD_RES 939 939 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 940 940 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 944 944 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 946 946 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 951 951 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 952 952 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 955 955 Phosphoserine.
{ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 959 959 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 27 Missing (in isoform 4 and isoform 5).
{ECO:0000303|PubMed:12465718,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_034962.
VAR_SEQ 1 21 MSRIESLTRARIDRSKEQATK -> MSGNRRQPSRRGQ
(in isoform 3). {ECO:0000303|Ref.2}.
/FTId=VSP_022640.
VAR_SEQ 112 113 Missing (in isoform 5).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_034963.
VAR_SEQ 574 985 Missing (in isoform 2).
{ECO:0000303|PubMed:7629163}.
/FTId=VSP_022641.
VAR_SEQ 596 596 T -> S (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_022642.
VAR_SEQ 597 985 Missing (in isoform 3).
{ECO:0000303|Ref.2}.
/FTId=VSP_022643.
CONFLICT 156 156 A -> V (in Ref. 2; CAA65067).
{ECO:0000305}.
CONFLICT 539 539 M -> V (in Ref. 3; AAG09271).
{ECO:0000305}.
CONFLICT 679 679 M -> T (in Ref. 3; AAG09271, 4; BAC41438
and 7; AAH06589). {ECO:0000305}.
CONFLICT 810 810 H -> Y (in Ref. 5; BAE42325).
{ECO:0000305}.
CONFLICT 941 941 D -> G (in Ref. 3; AAG09271).
{ECO:0000305}.
SEQUENCE 985 AA; 111974 MW; 1A5EAB73F95005D1 CRC64;
MSRIESLTRA RIDRSKEQAT KTREKEKMKE AKDARYTNGH LFTTISVSGM TMCYACNKSI
TAKEALICPT CNVTIHNRCK DTLANCTKVK QKQQKAALLR NNTALQSVSL RSKTTTRERP
TSAIYPSDSF RQSLLGSRRG LSSLSLAKSV STTNIAGHFN DESPLGLRQI LSQSTDSLNM
RNRTLSVESL IDEGVEVFYN ELMSDFEMDE KDFEADSWSL AVDSSFLQQH KKEVMKKQDV
IYELIQTELH HVRTLKIMTR LFRTGMLEEL QMEPEVVQGL FPCVDELSDI HTRFLNQLLE
RRRQALCPGS TRNFVIHRLG DLLISQFSGS NAEQMRKTYS EFCSRHTKAL KLYKELYARD
KRFQQFIRKM TRSAVLKRHG VQECILLVTQ RITKYPVLIN RILQNSHGVE EEYQDLASAL
GLVKELLSNV DQDVHELEKE ARLQEIYNRM DPRAQTPVPG KGPFGRDELL RRKLIHEGCL
LWKTATGRFK DVLLLLMTDV LVFLQEKDQK YIFTSLDKPS VVSLQNLIVR DIANQAKGMF
LISSGPPEMY EVHAASRDDR TTWIRVIQQS VRLCPSREDF PLIETEDKAY LRRIKTKLQQ
KNQALVELLQ KNVELFAEMV HFQALKAGFV GMPPPALPRG LFRLESFESL RGERLLKDAL
REVEGLKDLL LGPCVDLPMT SREPALPLDS DSGSCPGVTA NGEARTFNGS IELCRADSDS
SQKDRNGNQL RSPQEEVLQP LINLYGLLHG LQAVVVQQER LMEALFPEGP ERWEKLSRAN
SRDGEAGRAA VASVTPEKQA TELALLQRQH TLLQEELRRC QRLGEERATE AGSLEARLRE
SEQARALLER EAEEIRRQLA ALGQNEPLPA EAPWARRPLD PRRRSLPAGD ALYLSFNPPQ
PSRGHDRLDL PVTVRSLHRP FDDREAQELG SPEDRLQDSS DPDTGSEEEV SSRLSPPHSP
RDFTRMQDIP EETESRDGEP TASES


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