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Rho guanine nucleotide exchange factor 6 (Alpha-Pix) (COOL-2) (PAK-interacting exchange factor alpha) (Rac/Cdc42 guanine nucleotide exchange factor 6)

 ARHG6_HUMAN             Reviewed;         776 AA.
Q15052; A6NMW9; A8K6S7; B1AL37; Q15396; Q5JQ66; Q7Z3W1; Q86XH0;
26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
26-SEP-2001, sequence version 2.
22-NOV-2017, entry version 193.
RecName: Full=Rho guanine nucleotide exchange factor 6;
AltName: Full=Alpha-Pix;
AltName: Full=COOL-2;
AltName: Full=PAK-interacting exchange factor alpha;
AltName: Full=Rac/Cdc42 guanine nucleotide exchange factor 6;
Name=ARHGEF6; Synonyms=COOL2, KIAA0006, PIXA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Placenta;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Adipose tissue;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Testis;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-3 (ISOFORM 1), AND INVOLVEMENT IN
MRX46.
PubMed=11017088; DOI=10.1038/80002;
Kutsche K., Yntema H., Brandt A., Jantke I., Nothwang H.G., Orth U.,
Boavida M.G., David D., Chelly J., Fryns J.-P., Moraine C.,
Ropers H.-H., Hamel B.C.J., van Bokhoven H., Gal A.;
"Mutations in ARHGEF6, encoding a guanine nucleotide exchange factor
for Rho GTPases, in patients with X-linked mental retardation.";
Nat. Genet. 26:247-250(2000).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-776 (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[8]
CHARACTERIZATION.
PubMed=11337747; DOI=10.1002/ajmg.1189;
Lower K.M., Gecz J.;
"Characterization of ARHGEF6, a guanine nucleotide exchange factor for
Rho GTPases and a candidate gene for X-linked mental retardation:
mutation screening in Borjeson-Forssman-Lehmann syndrome and MRX27.";
Am. J. Med. Genet. 100:43-48(2001).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[10]
INTERACTION WITH PARVB.
PubMed=15005707; DOI=10.1111/j.1356-9597.2004.00717.x;
Mishima W., Suzuki A., Yamaji S., Yoshimi R., Ueda A., Kaneko T.,
Tanaka J., Miwa Y., Ohno S., Ishigatsubo Y.;
"The first CH domain of affixin activates Cdc42 and Rac1 through
alphaPIX, a Cdc42/Rac1-specific guanine nucleotide exchanging
factor.";
Genes Cells 9:193-204(2004).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-126; SER-144; SER-150;
SER-640 AND SER-684, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
INTERACTION WITH BIN2, AND IDENTIFICATION IN A COMPLEX WITH BIN2 AND
GIT2.
PubMed=23285027; DOI=10.1371/journal.pone.0052401;
Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
Veprintsev D.B., Evans P.R., McMahon H.T.;
"Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
podosomes, motility and phagocytosis.";
PLoS ONE 7:E52401-E52401(2012).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-684, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133; SER-225 AND
SER-684, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[15]
STRUCTURE BY NMR OF 4-222.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the CH domain and the SH3 domain in RAC/CDC42
guanine nucleotide exchange factor (GEF) 6.";
Submitted (FEB-2004) to the PDB data bank.
-!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF).
-!- SUBUNIT: Interacts with PAK kinases through the SH3 domain.
Interacts with GIT1. Component of cytoplasmic complexes, which
also contain PXN, GIT1 and PAK1 (By similarity). Interacts with
PARVB. Interacts with BIN2. Identified in a complex with BIN2 and
GIT2. {ECO:0000250, ECO:0000269|PubMed:15005707,
ECO:0000269|PubMed:23285027}.
-!- INTERACTION:
Q14161-11:GIT2; NbExp=4; IntAct=EBI-1642523, EBI-12028686;
Q7Z3Y8:KRT27; NbExp=4; IntAct=EBI-1642523, EBI-3044087;
P41227:NAA10; NbExp=3; IntAct=EBI-1642523, EBI-747693;
Q13177:PAK2; NbExp=4; IntAct=EBI-1642523, EBI-1045887;
O60880-1:SH2D1A; NbExp=3; IntAct=EBI-1642523, EBI-15552052;
-!- SUBCELLULAR LOCATION: Cell projection, lamellipodium
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q15052-1; Sequence=Displayed;
Name=2;
IsoId=Q15052-2; Sequence=VSP_015782;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- DISEASE: Mental retardation, X-linked 46 (MRX46) [MIM:300436]: A
disorder characterized by significantly below average general
intellectual functioning associated with impairments in adaptive
behavior and manifested during the developmental period.
Intellectual deficiency is the only primary symptom of non-
syndromic X-linked mental retardation, while syndromic mental
retardation presents with associated physical, neurological and/or
psychiatric manifestations. {ECO:0000269|PubMed:11017088}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA02796.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AK291742; BAF84431.1; -; mRNA.
EMBL; AK294929; BAH11929.1; -; mRNA.
EMBL; BX537390; CAD97632.1; -; mRNA.
EMBL; AL683813; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL135783; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471150; EAW88460.1; -; Genomic_DNA.
EMBL; CH471150; EAW88461.1; -; Genomic_DNA.
EMBL; BC039856; AAH39856.1; -; mRNA.
EMBL; BC043505; AAH43505.1; ALT_TERM; mRNA.
EMBL; AF207831; AAG27169.1; -; mRNA.
EMBL; D13631; BAA02796.1; ALT_INIT; mRNA.
EMBL; D25304; BAA04985.1; -; mRNA.
CCDS; CCDS14660.1; -. [Q15052-1]
CCDS; CCDS78509.1; -. [Q15052-2]
RefSeq; NP_001293106.1; NM_001306177.1. [Q15052-2]
RefSeq; NP_004831.1; NM_004840.2. [Q15052-1]
UniGene; Hs.522795; -.
PDB; 1UJY; NMR; -; A=160-222.
PDB; 1WYR; NMR; -; A=4-111.
PDBsum; 1UJY; -.
PDBsum; 1WYR; -.
ProteinModelPortal; Q15052; -.
SMR; Q15052; -.
BioGrid; 114847; 34.
CORUM; Q15052; -.
DIP; DIP-42694N; -.
IntAct; Q15052; 28.
MINT; MINT-2791937; -.
STRING; 9606.ENSP00000250617; -.
iPTMnet; Q15052; -.
PhosphoSitePlus; Q15052; -.
BioMuta; ARHGEF6; -.
DMDM; 17371603; -.
EPD; Q15052; -.
MaxQB; Q15052; -.
PaxDb; Q15052; -.
PeptideAtlas; Q15052; -.
PRIDE; Q15052; -.
Ensembl; ENST00000250617; ENSP00000250617; ENSG00000129675. [Q15052-1]
Ensembl; ENST00000370620; ENSP00000359654; ENSG00000129675. [Q15052-2]
Ensembl; ENST00000370622; ENSP00000359656; ENSG00000129675. [Q15052-2]
GeneID; 9459; -.
KEGG; hsa:9459; -.
UCSC; uc004fab.5; human. [Q15052-1]
CTD; 9459; -.
DisGeNET; 9459; -.
EuPathDB; HostDB:ENSG00000129675.15; -.
GeneCards; ARHGEF6; -.
HGNC; HGNC:685; ARHGEF6.
HPA; HPA003578; -.
MalaCards; ARHGEF6; -.
MIM; 300267; gene.
MIM; 300436; phenotype.
neXtProt; NX_Q15052; -.
OpenTargets; ENSG00000129675; -.
Orphanet; 777; X-linked non-syndromic intellectual disability.
PharmGKB; PA24976; -.
eggNOG; KOG2070; Eukaryota.
eggNOG; ENOG410XNNP; LUCA.
GeneTree; ENSGT00900000140891; -.
HOGENOM; HOG000231381; -.
HOVERGEN; HBG050569; -.
InParanoid; Q15052; -.
KO; K05729; -.
OMA; FQEWLEQ; -.
OrthoDB; EOG091G04XA; -.
PhylomeDB; Q15052; -.
TreeFam; TF316105; -.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
Reactome; R-HSA-446388; Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
ChiTaRS; ARHGEF6; human.
EvolutionaryTrace; Q15052; -.
GeneWiki; ARHGEF6; -.
GenomeRNAi; 9459; -.
PRO; PR:Q15052; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000129675; -.
CleanEx; HS_ARHGEF6; -.
Genevisible; Q15052; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005622; C:intracellular; IC:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0005096; F:GTPase activator activity; NAS:UniProtKB.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0006915; P:apoptotic process; NAS:UniProtKB.
GO; GO:0007254; P:JNK cascade; NAS:UniProtKB.
GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro.
GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
CDD; cd00014; CH; 1.
CDD; cd00160; RhoGEF; 1.
CDD; cd12060; SH3_alphaPIX; 1.
Gene3D; 1.10.418.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR035788; AlphaPIX_SH3.
InterPro; IPR036872; Calponin-like_dom_sf.
InterPro; IPR001715; CH-domain.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR032409; GEF_CC.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR003096; SM22_calponin.
Pfam; PF16523; betaPIX_CC; 1.
Pfam; PF00307; CH; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00621; RhoGEF; 1.
Pfam; PF14604; SH3_9; 1.
PRINTS; PR00452; SH3DOMAIN.
PRINTS; PR00888; SM22CALPONIN.
SMART; SM00033; CH; 1.
SMART; SM00233; PH; 1.
SMART; SM00325; RhoGEF; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF47576; SSF47576; 1.
SUPFAM; SSF48065; SSF48065; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF50729; SSF50729; 1.
PROSITE; PS50021; CH; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection;
Complete proteome; Guanine-nucleotide releasing factor;
Mental retardation; Phosphoprotein; Polymorphism; Reference proteome;
SH3 domain.
CHAIN 1 776 Rho guanine nucleotide exchange factor 6.
/FTId=PRO_0000080917.
DOMAIN 1 111 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 160 219 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 241 421 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 443 548 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOD_RES 126 126 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 133 133 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 144 144 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 150 150 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332}.
MOD_RES 225 225 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 488 488 Phosphoserine.
{ECO:0000250|UniProtKB:Q8K4I3}.
MOD_RES 640 640 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 154 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_015782.
VARIANT 297 297 Q -> H (in dbSNP:rs5974620).
/FTId=VAR_051981.
CONFLICT 199 199 E -> G (in Ref. 2; CAD97632).
{ECO:0000305}.
HELIX 4 14 {ECO:0000244|PDB:1WYR}.
HELIX 27 37 {ECO:0000244|PDB:1WYR}.
HELIX 39 48 {ECO:0000244|PDB:1WYR}.
HELIX 63 80 {ECO:0000244|PDB:1WYR}.
HELIX 87 91 {ECO:0000244|PDB:1WYR}.
HELIX 96 110 {ECO:0000244|PDB:1WYR}.
STRAND 163 166 {ECO:0000244|PDB:1UJY}.
STRAND 187 191 {ECO:0000244|PDB:1UJY}.
STRAND 194 196 {ECO:0000244|PDB:1UJY}.
STRAND 198 202 {ECO:0000244|PDB:1UJY}.
STRAND 205 209 {ECO:0000244|PDB:1UJY}.
TURN 211 213 {ECO:0000244|PDB:1UJY}.
STRAND 214 216 {ECO:0000244|PDB:1UJY}.
HELIX 219 222 {ECO:0000244|PDB:1UJY}.
SEQUENCE 776 AA; 87499 MW; 5D2622314E46341B CRC64;
MNPEEQIVTW LISLGVLESP KKTICDPEEF LKSSLKNGVV LCKLINRLMP GSVEKFCLDP
QTEADCINNI NDFLKGCATL QVEIFDPDDL YSGVNFSKVL STLLAVNKAT EDQLSERPCG
RSSSLSAANT SQTNPQGAVS STVSGLQRQS KTVEMTENGS HQLIVKARFN FKQTNEDELS
VCKGDIIYVT RVEEGGWWEG TLNGRTGWFP SNYVREIKSS ERPLSPKAVK GFETAPLTKN
YYTVVLQNIL DTEKEYAKEL QSLLVTYLRP LQSNNNLSTV EVTSLLGNFE EVCTFQQTLC
QALEECSKFP ENQHKVGGCL LSLMPHFKSM YLAYCANHPS AVNVLTQHSD ELEQFMENQG
ASSPGILILT TNLSKPFMRL EKYVTLLQEL ERHMEDTHPD HQDILKAIVA FKTLMGQCQD
LRKRKQLELQ ILSEPIQAWE GEDIKNLGNV IFMSQVMVQY GACEEKEERY LMLFSNVLIM
LSASPRMSGF IYQGKIPIAG TVVTRLDEIE GNDCTFEITG NTVERIVVHC NNNQDFQEWL
EQLNRLIRGP ASCSSLSKTS SSSCSAHSSF SSTGQPRGPL EPPQIIKPWS LSCLRPAPPL
RPSAALGYKE RMSYILKESS KSPKTMKKFL HKRKTERKPS EEEYVIRKST AALEEDAQIL
KVIEAYCTSA NFQQGHGSST RKDSIPQVLL PEEEKLIIEE TRSNGQTIME EKSLVDTVYA
LKDEVRELKQ ENKRMKQCLE EELKSRRDLE KLVRRLLKQT DECIRGESSS KTSILP


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