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Rho guanine nucleotide exchange factor 7 (Beta-Pix) (COOL-1) (PAK-interacting exchange factor beta) (p85)

 ARHG7_HUMAN             Reviewed;         803 AA.
Q14155; B1ALK6; B1ALK8; Q3LIA4; Q5W9H0; Q6P9G3; Q6PII2; Q86W63;
Q8N3M1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
22-NOV-2017, entry version 195.
RecName: Full=Rho guanine nucleotide exchange factor 7;
AltName: Full=Beta-Pix;
AltName: Full=COOL-1;
AltName: Full=PAK-interacting exchange factor beta;
AltName: Full=p85;
Name=ARHGEF7; Synonyms=COOL1, KIAA0142, P85SPR, PAK3BP, PIXB;
ORFNames=Nbla10314;
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] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. IV.
The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:167-174(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9726964; DOI=10.1074/jbc.273.37.23633;
Bagrodia S., Taylor S.J., Jordon K.A., Van Aelst L., Cerione R.A.;
"A novel regulator of p21-activated kinases.";
J. Biol. Chem. 273:23633-23636(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
TISSUE=Amygdala;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
TISSUE=Brain, and 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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 52-803 (ISOFORM 5).
PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
"Alternative splice variants encoding unstable protein domains exist
in the human brain.";
J. Mol. Biol. 343:1207-1220(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-803.
TISSUE=Neuroblastoma;
PubMed=12880961; DOI=10.1016/S0304-3835(03)00085-5;
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
Hirato J., Nakagawara A.;
"Neuroblastoma oligo-capping cDNA project: toward the understanding of
the genesis and biology of neuroblastoma.";
Cancer Lett. 197:63-68(2003).
[9]
INTERACTION WITH SCRIB.
PubMed=15182672; DOI=10.1016/j.cub.2004.05.051;
Audebert S., Navarro C., Nourry C., Chasserot-Golaz S., Lecine P.,
Bellaiche Y., Dupont J.-L., Premont R.T., Sempere C., Strub J.-M.,
Van Dorsselaer A., Vitale N., Borg J.-P.;
"Mammalian Scribble forms a tight complex with the betaPIX exchange
factor.";
Curr. Biol. 14:987-995(2004).
[10]
FUNCTION, AND INTERACTION WITH SCRIB.
PubMed=19041750; DOI=10.1016/j.cell.2008.09.045;
Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B.,
Allred C., Muthuswamy S.K.;
"Deregulation of scribble promotes mammary tumorigenesis and reveals a
role for cell polarity in carcinoma.";
Cell 135:865-878(2008).
[11]
FUNCTION IN CELL MIGRATION.
PubMed=18716323; DOI=10.1093/hmg/ddn248;
Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
Navarro C., Rachel R., Montcouquiol M., Sans N.,
Etienne-Manneville S., Borg J.-P., Santoni M.-J.;
"Scrib regulates PAK activity during the cell migration process.";
Hum. Mol. Genet. 17:3552-3565(2008).
[12]
INTERACTION WITH FRMPD4.
PubMed=19118189; DOI=10.1523/JNEUROSCI.3112-08.2008;
Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y.,
Kang G.B., Eom S.H., Kim H., Kim E.;
"Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
regulates dendritic spine morphogenesis.";
J. Neurosci. 28:14546-14556(2008).
[13]
FUNCTION, PHOSPHORYLATION AT SER-694, AND INTERACTION WITH CAMK1.
PubMed=18184567; DOI=10.1016/j.neuron.2007.11.016;
Saneyoshi T., Wayman G., Fortin D., Davare M., Hoshi N., Nozaki N.,
Natsume T., Soderling T.R.;
"Activity-dependent synaptogenesis: regulation by a CaM-kinase
kinase/CaM-kinase I/betaPIX signaling complex.";
Neuron 57:94-107(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, 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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
INTERACTION WITH SNX27.
PubMed=21926430; DOI=10.1074/jbc.M111.260802;
Valdes J.L., Tang J., McDermott M.I., Kuo J.C., Zimmerman S.P.,
Wincovitch S.M., Waterman C.M., Milgram S.L., Playford M.P.;
"Sorting nexin 27 protein regulates trafficking of a p21-activated
kinase (PAK) interacting exchange factor (beta-Pix)-G protein-coupled
receptor kinase interacting protein (GIT) complex via a PDZ domain
interaction.";
J. Biol. Chem. 286:39403-39416(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-694,
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-579 (ISOFORM
1), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-664
(ISOFORM 5), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[19]
ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORMS 1 AND 6),
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 1),
CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 6),
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[20]
INTERACTION WITH BIN2.
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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 1 AND 6), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-518 AND
SER-694, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 (ISOFORM 1),
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 (ISOFORM 5), 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).
[24]
STRUCTURE BY NMR OF 260-467.
PubMed=9846881; DOI=10.1038/4209;
Aghazadeh B., Zhu K., Kubiseski T.J., Liu G.A., Pawson T., Zheng Y.,
Rosen M.K.;
"Structure and mutagenesis of the Dbl homology domain.";
Nat. Struct. Biol. 5:1098-1107(1998).
[25]
STRUCTURE BY NMR OF 179-243 OF COMPLEX WITH UNPHOSPHORYLATED PAK1.
PubMed=16101281; DOI=10.1021/bi050374a;
Mott H.R., Nietlispach D., Evetts K.A., Owen D.;
"Structural analysis of the SH3 domain of beta-PIX and its interaction
with alpha-p21 activated kinase (PAK).";
Biochemistry 44:10977-10983(2005).
[26]
STRUCTURE BY NMR OF 1-137.
Northeast structural genomics consortium (NESG);
"Northeast structural genomics consortium target HR4495E.";
Submitted (DEC-2010) to the PDB data bank.
[27]
VARIANT ALA-790.
PubMed=21248752; DOI=10.1038/nature09639;
Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P.,
Davies H., Jones D., Lin M.L., Teague J., Bignell G., Butler A.,
Cho J., Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C.,
Jia M., Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A.,
Mudie L., Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S.,
Kahnoski R.J., Anema J., Tuveson D.A., Perez-Mancera P.A.,
Mustonen V., Fischer A., Adams D.J., Rust A., Chan-On W., Subimerb C.,
Dykema K., Furge K., Campbell P.J., Teh B.T., Stratton M.R.,
Futreal P.A.;
"Exome sequencing identifies frequent mutation of the SWI/SNF complex
gene PBRM1 in renal carcinoma.";
Nature 469:539-542(2011).
-!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF)
and can induce membrane ruffling. Functions in cell migration,
attachment and cell spreading. Promotes targeting of RAC1 to focal
adhesions (By similarity). May function as a positive regulator of
apoptosis. Downstream of NMDA receptors and CaMKK-CaMK1 signaling
cascade, promotes the formation of spines and synapses in
hippocampal neurons. {ECO:0000250, ECO:0000269|PubMed:18184567,
ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750}.
-!- SUBUNIT: Interacts with PAK kinases through the SH3 domain.
Interacts with GIT1 and TGFB1I1. Interacts with PTK2/FAK1 and
RAC1. Interacts with ITCH and PARVB (By similarity). Interacts
with unphosphorylated PAK1. Interacts with SCRIB; interaction is
direct and may play a role in regulation of apoptosis. Interacts
with FRMPD4 (via N-terminus). Interacts with CaMK1. Interacts with
BIN2. Isoform 1 and isoform 5 interact with SNX27. {ECO:0000250,
ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:18184567,
ECO:0000269|PubMed:19041750, ECO:0000269|PubMed:19118189,
ECO:0000269|PubMed:21926430, ECO:0000269|PubMed:23285027}.
-!- INTERACTION:
P22681:CBL; NbExp=9; IntAct=EBI-717515, EBI-518228;
P60953-2:CDC42; NbExp=3; IntAct=EBI-717515, EBI-287394;
Q9Y2X7:GIT1; NbExp=4; IntAct=EBI-717515, EBI-466061;
Q5S007:LRRK2; NbExp=7; IntAct=EBI-717515, EBI-5323863;
P50222:MEOX2; NbExp=3; IntAct=EBI-717515, EBI-748397;
P41227:NAA10; NbExp=3; IntAct=EBI-717515, EBI-747693;
Q13153:PAK1; NbExp=7; IntAct=EBI-717515, EBI-1307;
Q13177:PAK2; NbExp=4; IntAct=EBI-717515, EBI-1045887;
P30153:PPP2R1A; NbExp=3; IntAct=EBI-717515, EBI-302388;
P63000:RAC1; NbExp=8; IntAct=EBI-717515, EBI-413628;
Q14160:SCRIB; NbExp=9; IntAct=EBI-717515, EBI-357345;
O60880-1:SH2D1A; NbExp=5; IntAct=EBI-717515, EBI-15552052;
Q7Z6B7:SRGAP1; NbExp=4; IntAct=EBI-717515, EBI-2481729;
-!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}.
Cell projection, ruffle {ECO:0000250}. Cytoplasm, cell cortex
{ECO:0000250}. Cell projection, lamellipodium {ECO:0000250}.
Note=Detected at cell adhesions. A small proportion is detected at
focal adhesions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=4;
IsoId=Q14155-4; Sequence=Displayed;
Name=1;
IsoId=Q14155-1; Sequence=VSP_011032, VSP_011035;
Note=Contains a N-acetylmethionine at position 1. Initiator
Met-1 is removed. Contains a N-acetylthreonine at position 2.
Contains a phosphoserine at position 560. Contains a
phosphoserine at position 579. {ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:24275569};
Name=2;
IsoId=Q14155-2; Sequence=VSP_011033;
Name=3;
IsoId=Q14155-3; Sequence=VSP_011034;
Name=5;
IsoId=Q14155-5; Sequence=VSP_034639, VSP_011035;
Note=Contains a phosphoserine at position 645. Contains a
phosphoserine at position 664. {ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569};
Name=6;
IsoId=Q14155-6; Sequence=VSP_011032;
Note=Contains a N-acetylmethionine at position 1. Initiator
Met-1 is removed. Contains a N-acetylthreonine at position 2.
{ECO:0000244|PubMed:22223895, ECO:0000244|PubMed:22814378};
-!- PTM: Phosphorylated by PTK2/FAK1; this promotes interaction with
RAC1 (By similarity). Phosphorylated on Ser-694 by CaMK1;
enhancement of GEF activity and downstream activation of RAC1.
{ECO:0000250, ECO:0000269|PubMed:18184567}.
-!- SEQUENCE CAUTION:
Sequence=AAH50521.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA09763.2; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAD38906.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; D63476; BAA09763.2; ALT_INIT; mRNA.
EMBL; AL834228; CAD38906.1; ALT_INIT; mRNA.
EMBL; AL390754; CAI12461.1; -; Genomic_DNA.
EMBL; AL139086; CAI12461.1; JOINED; Genomic_DNA.
EMBL; AL139086; CAI14671.1; -; Genomic_DNA.
EMBL; AL390754; CAI14671.1; JOINED; Genomic_DNA.
EMBL; AL390754; CAM13628.1; -; Genomic_DNA.
EMBL; AL139086; CAM13628.1; JOINED; Genomic_DNA.
EMBL; AL139086; CAM20788.1; -; Genomic_DNA.
EMBL; AL390754; CAM20788.1; JOINED; Genomic_DNA.
EMBL; CH471085; EAX09143.1; -; Genomic_DNA.
EMBL; BC033905; AAH33905.1; -; mRNA.
EMBL; BC050521; AAH50521.1; ALT_INIT; mRNA.
EMBL; BC060776; AAH60776.1; -; mRNA.
EMBL; AB177849; BAD66827.1; -; mRNA.
EMBL; AB075521; BAE45764.1; -; mRNA.
CCDS; CCDS32009.1; -. [Q14155-3]
CCDS; CCDS45068.1; -. [Q14155-4]
CCDS; CCDS45069.1; -. [Q14155-2]
CCDS; CCDS9521.1; -. [Q14155-1]
RefSeq; NP_001106983.1; NM_001113511.2. [Q14155-4]
RefSeq; NP_001106984.1; NM_001113512.2. [Q14155-2]
RefSeq; NP_001106985.1; NM_001113513.1. [Q14155-1]
RefSeq; NP_001307780.1; NM_001320851.1. [Q14155-1]
RefSeq; NP_001307782.1; NM_001320853.1.
RefSeq; NP_001307783.1; NM_001320854.1.
RefSeq; NP_001317526.1; NM_001330597.1. [Q14155-6]
RefSeq; NP_001317527.1; NM_001330598.1. [Q14155-6]
RefSeq; NP_003890.1; NM_003899.3. [Q14155-1]
RefSeq; NP_663788.1; NM_145735.3. [Q14155-3]
RefSeq; XP_016876313.1; XM_017020824.1. [Q14155-1]
RefSeq; XP_016876314.1; XM_017020825.1. [Q14155-1]
UniGene; Hs.508738; -.
PDB; 1BY1; NMR; -; A=260-467.
PDB; 1ZSG; NMR; -; A=179-243.
PDB; 2L3G; NMR; -; A=1-137.
PDB; 5SXP; X-ray; 1.65 A; A/B/C/D=183-243.
PDBsum; 1BY1; -.
PDBsum; 1ZSG; -.
PDBsum; 2L3G; -.
PDBsum; 5SXP; -.
ProteinModelPortal; Q14155; -.
SMR; Q14155; -.
BioGrid; 114393; 50.
CORUM; Q14155; -.
DIP; DIP-40794N; -.
IntAct; Q14155; 27.
MINT; MINT-92779; -.
STRING; 9606.ENSP00000364893; -.
iPTMnet; Q14155; -.
PhosphoSitePlus; Q14155; -.
BioMuta; ARHGEF7; -.
DMDM; 50403776; -.
EPD; Q14155; -.
PaxDb; Q14155; -.
PeptideAtlas; Q14155; -.
PRIDE; Q14155; -.
DNASU; 8874; -.
Ensembl; ENST00000317133; ENSP00000325994; ENSG00000102606. [Q14155-3]
Ensembl; ENST00000375723; ENSP00000364875; ENSG00000102606. [Q14155-6]
Ensembl; ENST00000375736; ENSP00000364888; ENSG00000102606. [Q14155-1]
Ensembl; ENST00000375739; ENSP00000364891; ENSG00000102606. [Q14155-2]
Ensembl; ENST00000375741; ENSP00000364893; ENSG00000102606. [Q14155-4]
Ensembl; ENST00000426073; ENSP00000397068; ENSG00000102606. [Q14155-1]
GeneID; 8874; -.
KEGG; hsa:8874; -.
UCSC; uc001vrr.3; human. [Q14155-4]
CTD; 8874; -.
DisGeNET; 8874; -.
EuPathDB; HostDB:ENSG00000102606.17; -.
GeneCards; ARHGEF7; -.
H-InvDB; HIX0037536; -.
HGNC; HGNC:15607; ARHGEF7.
HPA; HPA004744; -.
MIM; 605477; gene.
neXtProt; NX_Q14155; -.
OpenTargets; ENSG00000102606; -.
PharmGKB; PA24977; -.
eggNOG; KOG2070; Eukaryota.
eggNOG; ENOG410XNNP; LUCA.
GeneTree; ENSGT00900000140891; -.
HOVERGEN; HBG050569; -.
InParanoid; Q14155; -.
KO; K13710; -.
OrthoDB; EOG091G04XA; -.
PhylomeDB; Q14155; -.
TreeFam; TF316105; -.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-193648; NRAGE signals death through JNK.
Reactome; R-HSA-194840; Rho GTPase cycle.
Reactome; R-HSA-3928664; Ephrin signaling.
Reactome; R-HSA-416482; G alpha (12/13) signalling events.
SignaLink; Q14155; -.
SIGNOR; Q14155; -.
ChiTaRS; ARHGEF7; human.
EvolutionaryTrace; Q14155; -.
GeneWiki; ARHGEF7; -.
GenomeRNAi; 8874; -.
PRO; PR:Q14155; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000102606; -.
ExpressionAtlas; Q14155; baseline and differential.
Genevisible; Q14155; HS.
GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
GO; GO:0000322; C:storage vacuole; IEA:Ensembl.
GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
GO; GO:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
GO; GO:0048041; P:focal adhesion assembly; IDA:UniProtKB.
GO; GO:0007030; P:Golgi organization; IMP:ParkinsonsUK-UCL.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IEA:Ensembl.
GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010763; P:positive regulation of fibroblast migration; IDA:UniProtKB.
GO; GO:0060124; P:positive regulation of growth hormone secretion; IEA:Ensembl.
GO; GO:0043547; P:positive regulation of GTPase activity; IDA:BHF-UCL.
GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; IMP:UniProtKB.
GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; IMP:UniProtKB.
GO; GO:1904424; P:regulation of GTP binding; IMP:ParkinsonsUK-UCL.
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.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
CDD; cd00160; RhoGEF; 1.
CDD; cd12061; SH3_betaPIX; 1.
Gene3D; 1.10.418.10; -; 1.
Gene3D; 1.20.900.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
InterPro; IPR035789; BetaPIX_SH3.
InterPro; IPR036872; Calponin-like_dom_sf.
InterPro; IPR001715; CH-domain.
InterPro; IPR035899; DBL_dom_sf.
InterPro; IPR000219; DH-domain.
InterPro; IPR001331; GDS_CDC24_CS.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR001849; PH_domain.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
Pfam; PF00307; CH; 1.
Pfam; PF00169; PH; 1.
Pfam; PF00621; RhoGEF; 1.
Pfam; PF07653; SH3_2; 1.
PRINTS; PR00452; SH3DOMAIN.
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; PS00741; DH_1; 1.
PROSITE; PS50010; DH_2; 1.
PROSITE; PS50003; PH_DOMAIN; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Cell junction;
Cell projection; Complete proteome; Cytoplasm;
Guanine-nucleotide releasing factor; Neurogenesis; Phosphoprotein;
Polymorphism; Reference proteome; SH3 domain.
CHAIN 1 803 Rho guanine nucleotide exchange factor 7.
/FTId=PRO_0000080921.
DOMAIN 1 133 Calponin-homology (CH).
{ECO:0000255|PROSITE-ProRule:PRU00044}.
DOMAIN 184 243 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 271 451 DH. {ECO:0000255|PROSITE-
ProRule:PRU00062}.
DOMAIN 473 578 PH. {ECO:0000255|PROSITE-
ProRule:PRU00145}.
MOD_RES 153 153 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES28}.
MOD_RES 176 176 Phosphoserine.
{ECO:0000250|UniProtKB:Q9ES28}.
MOD_RES 249 249 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 257 257 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 518 518 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 694 694 Phosphoserine; by CaMK1.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:18184567}.
VAR_SEQ 1 178 Missing (in isoform 1 and isoform 6).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8590280,
ECO:0000303|PubMed:9726964}.
/FTId=VSP_011032.
VAR_SEQ 56 105 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_011033.
VAR_SEQ 85 177 Missing (in isoform 5).
{ECO:0000303|PubMed:15491607}.
/FTId=VSP_034639.
VAR_SEQ 85 105 Missing (in isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_011034.
VAR_SEQ 733 803 TWQGTDLMHNHVLADDDQPSLDSLGRRSSLSRLEPSDLSED
SDYDSIWTAHSYRMGSTSRKSCCSYISHQN -> SSRKESA
PQVLLPEEEKIIVEETKSNGQTVIEEKSLVDTVYALKDEVQ
ELRQDNKKMKKSLEEEQRARKDLEKLVRKVLKNMNDPAWDE
TNL (in isoform 1 and isoform 5).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:15491607,
ECO:0000303|PubMed:8590280,
ECO:0000303|PubMed:9726964}.
/FTId=VSP_011035.
VARIANT 790 790 T -> A (found in a clear cell renal
carcinoma case; somatic mutation).
{ECO:0000269|PubMed:21248752}.
/FTId=VAR_064694.
CONFLICT 52 55 TIEK -> EEKR (in Ref. 7; BAD66827).
{ECO:0000305}.
CONFLICT 343 343 Q -> K (in Ref. 6; AAH33905).
{ECO:0000305}.
CONFLICT 552 552 M -> V (in Ref. 6; AAH33905).
{ECO:0000305}.
CONFLICT 595 595 H -> D (in Ref. 7; BAD66827).
{ECO:0000305}.
CONFLICT 636 636 I -> T (in Ref. 6; AAH50521).
{ECO:0000305}.
CONFLICT 740 740 M -> L (in Ref. 6; AAH33905).
{ECO:0000305}.
HELIX 3 13 {ECO:0000244|PDB:2L3G}.
HELIX 27 35 {ECO:0000244|PDB:2L3G}.
HELIX 39 48 {ECO:0000244|PDB:2L3G}.
HELIX 63 79 {ECO:0000244|PDB:2L3G}.
HELIX 109 113 {ECO:0000244|PDB:2L3G}.
HELIX 118 135 {ECO:0000244|PDB:2L3G}.
STRAND 188 193 {ECO:0000244|PDB:5SXP}.
STRAND 210 216 {ECO:0000244|PDB:5SXP}.
STRAND 218 226 {ECO:0000244|PDB:5SXP}.
STRAND 229 234 {ECO:0000244|PDB:5SXP}.
HELIX 235 237 {ECO:0000244|PDB:5SXP}.
STRAND 238 240 {ECO:0000244|PDB:5SXP}.
HELIX 271 301 {ECO:0000244|PDB:1BY1}.
TURN 302 304 {ECO:0000244|PDB:1BY1}.
STRAND 305 310 {ECO:0000244|PDB:1BY1}.
HELIX 311 313 {ECO:0000244|PDB:1BY1}.
HELIX 316 338 {ECO:0000244|PDB:1BY1}.
HELIX 346 378 {ECO:0000244|PDB:1BY1}.
TURN 379 381 {ECO:0000244|PDB:1BY1}.
HELIX 382 385 {ECO:0000244|PDB:1BY1}.
TURN 386 389 {ECO:0000244|PDB:1BY1}.
TURN 395 397 {ECO:0000244|PDB:1BY1}.
HELIX 398 402 {ECO:0000244|PDB:1BY1}.
TURN 406 408 {ECO:0000244|PDB:1BY1}.
HELIX 409 411 {ECO:0000244|PDB:1BY1}.
HELIX 413 422 {ECO:0000244|PDB:1BY1}.
STRAND 428 430 {ECO:0000244|PDB:1BY1}.
HELIX 432 453 {ECO:0000244|PDB:1BY1}.
TURN 454 456 {ECO:0000244|PDB:1BY1}.
SEQUENCE 803 AA; 90012 MW; 613EBA839E6FDBFD CRC64;
MNSAEQTVTW LITLGVLESP KKTISDPEGF LQASLKDGVV LCRLLERLLP GTIEKVYPEP
RSESECLSNI REFLRGCGAS LRLELLFPPS QPPQHLVTTI LLSASTFDAN DLYQGQNFNK
VLSSLVTLNK VTADIGLGSD SVCARPSSHR IKSFDSLGSQ SLHTRTSKLF QGQYRSLDMT
DNSNNQLVVR AKFNFQQTNE DELSFSKGDV IHVTRVEEGG WWEGTLNGRT GWFPSNYVRE
VKASEKPVSP KSGTLKSPPK GFDTTAINKS YYNVVLQNIL ETENEYSKEL QTVLSTYLRP
LQTSEKLSSA NISYLMGNLE EICSFQQMLV QSLEECTKLP EAQQRVGGCF LNLMPQMKTL
YLTYCANHPS AVNVLTEHSE ELGEFMETKG ASSPGILVLT TGLSKPFMRL DKYPTLLKEL
ERHMEDYHTD RQDIQKSMAA FKNLSAQCQE VRKRKELELQ ILTEAIRNWE GDDIKTLGNV
TYMSQVLIQC AGSEEKNERY LLLFPNVLLM LSASPRMSGF IYQGKLPTTG MTITKLEDSE
NHRNAFEISG SMIERILVSC NNQQDLQEWV EHLQKQTKVT SVGNPTIKPH SVPSHTLPSH
PVTPSSKHAD SKPAPLTPAY HTLPHPSHHG TPHTTINWGP LEPPKTPKPW SLSCLRPAPP
LRPSAALCYK EDLSKSPKTM KKLLPKRKPE RKPSDEEFAS RKSTAALEED AQILKVIEAY
CTSAKTRQTL NSTWQGTDLM HNHVLADDDQ PSLDSLGRRS SLSRLEPSDL SEDSDYDSIW
TAHSYRMGST SRKSCCSYIS HQN


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