ARHG7_HUMAN
ID ARHG7_HUMAN Reviewed; 803 AA.
AC Q14155; B1ALK6; B1ALK8; Q3LIA4; Q5W9H0; Q6P9G3; Q6PII2; Q86W63; Q8N3M1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 227.
DE RecName: Full=Rho guanine nucleotide exchange factor 7;
DE AltName: Full=Beta-Pix;
DE AltName: Full=COOL-1;
DE AltName: Full=PAK-interacting exchange factor beta;
DE AltName: Full=p85;
GN Name=ARHGEF7; Synonyms=COOL1, KIAA0142, P85SPR, PAK3BP, PIXB;
GN ORFNames=Nbla10314;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV. The
RT coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9726964; DOI=10.1074/jbc.273.37.23633;
RA Bagrodia S., Taylor S.J., Jordon K.A., Van Aelst L., Cerione R.A.;
RT "A novel regulator of p21-activated kinases.";
RL J. Biol. Chem. 273:23633-23636(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4).
RC TISSUE=Brain, and Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 52-803 (ISOFORM 5).
RX PubMed=15491607; DOI=10.1016/j.jmb.2004.09.028;
RA Homma K., Kikuno R.F., Nagase T., Ohara O., Nishikawa K.;
RT "Alternative splice variants encoding unstable protein domains exist in the
RT human brain.";
RL J. Mol. Biol. 343:1207-1220(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 433-803.
RC TISSUE=Neuroblastoma;
RX PubMed=12880961; DOI=10.1016/s0304-3835(03)00085-5;
RA Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S.,
RA Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S.,
RA Hirato J., Nakagawara A.;
RT "Neuroblastoma oligo-capping cDNA project: toward the understanding of the
RT genesis and biology of neuroblastoma.";
RL Cancer Lett. 197:63-68(2003).
RN [9]
RP INTERACTION WITH SCRIB.
RX PubMed=15182672; DOI=10.1016/j.cub.2004.05.051;
RA Audebert S., Navarro C., Nourry C., Chasserot-Golaz S., Lecine P.,
RA Bellaiche Y., Dupont J.-L., Premont R.T., Sempere C., Strub J.-M.,
RA Van Dorsselaer A., Vitale N., Borg J.-P.;
RT "Mammalian Scribble forms a tight complex with the betaPIX exchange
RT factor.";
RL Curr. Biol. 14:987-995(2004).
RN [10]
RP FUNCTION, AND INTERACTION WITH SCRIB.
RX PubMed=19041750; DOI=10.1016/j.cell.2008.09.045;
RA Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C.,
RA Muthuswamy S.K.;
RT "Deregulation of scribble promotes mammary tumorigenesis and reveals a role
RT for cell polarity in carcinoma.";
RL Cell 135:865-878(2008).
RN [11]
RP FUNCTION IN CELL MIGRATION.
RX PubMed=18716323; DOI=10.1093/hmg/ddn248;
RA Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
RA Navarro C., Rachel R., Montcouquiol M., Sans N., Etienne-Manneville S.,
RA Borg J.-P., Santoni M.-J.;
RT "Scrib regulates PAK activity during the cell migration process.";
RL Hum. Mol. Genet. 17:3552-3565(2008).
RN [12]
RP INTERACTION WITH FRMPD4.
RX PubMed=19118189; DOI=10.1523/jneurosci.3112-08.2008;
RA Lee H.W., Choi J., Shin H., Kim K., Yang J., Na M., Choi S.Y., Kang G.B.,
RA Eom S.H., Kim H., Kim E.;
RT "Preso, a novel PSD-95-interacting FERM and PDZ domain protein that
RT regulates dendritic spine morphogenesis.";
RL J. Neurosci. 28:14546-14556(2008).
RN [13]
RP FUNCTION, PHOSPHORYLATION AT SER-694, AND INTERACTION WITH CAMK1.
RX PubMed=18184567; DOI=10.1016/j.neuron.2007.11.016;
RA Saneyoshi T., Wayman G., Fortin D., Davare M., Hoshi N., Nozaki N.,
RA Natsume T., Soderling T.R.;
RT "Activity-dependent synaptogenesis: regulation by a CaM-kinase kinase/CaM-
RT kinase I/betaPIX signaling complex.";
RL Neuron 57:94-107(2008).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-694, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-518, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP INTERACTION WITH SNX27.
RX PubMed=21926430; DOI=10.1074/jbc.m111.260802;
RA Valdes J.L., Tang J., McDermott M.I., Kuo J.C., Zimmerman S.P.,
RA Wincovitch S.M., Waterman C.M., Milgram S.L., Playford M.P.;
RT "Sorting nexin 27 protein regulates trafficking of a p21-activated kinase
RT (PAK) interacting exchange factor (beta-Pix)-G protein-coupled receptor
RT kinase interacting protein (GIT) complex via a PDZ domain interaction.";
RL J. Biol. Chem. 286:39403-39416(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-694,
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 AND SER-579 (ISOFORM 1),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 AND SER-664 (ISOFORM 5),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2 (ISOFORMS 1 AND 6), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 1), CLEAVAGE OF
RP INITIATOR METHIONINE [LARGE SCALE ANALYSIS] (ISOFORM 6), AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP INTERACTION WITH BIN2.
RX PubMed=23285027; DOI=10.1371/journal.pone.0052401;
RA Sanchez-Barrena M.J., Vallis Y., Clatworthy M.R., Doherty G.J.,
RA Veprintsev D.B., Evans P.R., McMahon H.T.;
RT "Bin2 is a membrane sculpting N-BAR protein that influences leucocyte
RT podosomes, motility and phagocytosis.";
RL PLoS ONE 7:E52401-E52401(2012).
RN [21]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORMS 1 AND 6), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257; SER-518 AND SER-694, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-560 (ISOFORM 1),
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-645 (ISOFORM 5), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [24]
RP STRUCTURE BY NMR OF 260-467.
RX PubMed=9846881; DOI=10.1038/4209;
RA Aghazadeh B., Zhu K., Kubiseski T.J., Liu G.A., Pawson T., Zheng Y.,
RA Rosen M.K.;
RT "Structure and mutagenesis of the Dbl homology domain.";
RL Nat. Struct. Biol. 5:1098-1107(1998).
RN [25]
RP STRUCTURE BY NMR OF 179-243 OF COMPLEX WITH UNPHOSPHORYLATED PAK1.
RX PubMed=16101281; DOI=10.1021/bi050374a;
RA Mott H.R., Nietlispach D., Evetts K.A., Owen D.;
RT "Structural analysis of the SH3 domain of beta-PIX and its interaction with
RT alpha-p21 activated kinase (PAK).";
RL Biochemistry 44:10977-10983(2005).
RN [26]
RP STRUCTURE BY NMR OF 1-137.
RG Northeast structural genomics consortium (NESG);
RT "Northeast structural genomics consortium target HR4495E.";
RL Submitted (DEC-2010) to the PDB data bank.
RN [27]
RP VARIANT ALA-790.
RX PubMed=21248752; DOI=10.1038/nature09639;
RA Varela I., Tarpey P., Raine K., Huang D., Ong C.K., Stephens P., Davies H.,
RA Jones D., Lin M.L., Teague J., Bignell G., Butler A., Cho J.,
RA Dalgliesh G.L., Galappaththige D., Greenman C., Hardy C., Jia M.,
RA Latimer C., Lau K.W., Marshall J., McLaren S., Menzies A., Mudie L.,
RA Stebbings L., Largaespada D.A., Wessels L.F.A., Richard S., Kahnoski R.J.,
RA Anema J., Tuveson D.A., Perez-Mancera P.A., Mustonen V., Fischer A.,
RA Adams D.J., Rust A., Chan-On W., Subimerb C., Dykema K., Furge K.,
RA Campbell P.J., Teh B.T., Stratton M.R., Futreal P.A.;
RT "Exome sequencing identifies frequent mutation of the SWI/SNF complex gene
RT PBRM1 in renal carcinoma.";
RL Nature 469:539-542(2011).
CC -!- FUNCTION: Acts as a RAC1 guanine nucleotide exchange factor (GEF) and
CC can induce membrane ruffling. Functions in cell migration, attachment
CC and cell spreading. Promotes targeting of RAC1 to focal adhesions (By
CC similarity). May function as a positive regulator of apoptosis.
CC Downstream of NMDA receptors and CaMKK-CaMK1 signaling cascade,
CC promotes the formation of spines and synapses in hippocampal neurons.
CC {ECO:0000250, ECO:0000269|PubMed:18184567, ECO:0000269|PubMed:18716323,
CC ECO:0000269|PubMed:19041750}.
CC -!- SUBUNIT: Interacts with PAK kinases through the SH3 domain. Interacts
CC with GIT1 and TGFB1I1. Interacts with PTK2/FAK1 and RAC1. Interacts
CC with ITCH and PARVB (By similarity). Interacts with unphosphorylated
CC PAK1. Interacts with SCRIB; interaction is direct and may play a role
CC in regulation of apoptosis. Interacts with FRMPD4 (via N-terminus).
CC Interacts with CaMK1. Interacts with BIN2. Isoform 1 and isoform 5
CC interact with SNX27. Interacts with YWHAZ (By similarity).
CC {ECO:0000250, ECO:0000250|UniProtKB:Q9ES28,
CC ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:18184567,
CC ECO:0000269|PubMed:19041750, ECO:0000269|PubMed:19118189,
CC ECO:0000269|PubMed:21926430, ECO:0000269|PubMed:23285027}.
CC -!- INTERACTION:
CC Q14155; P22681: CBL; NbExp=9; IntAct=EBI-717515, EBI-518228;
CC Q14155; P60953-2: CDC42; NbExp=3; IntAct=EBI-717515, EBI-287394;
CC Q14155; Q9Y2X7: GIT1; NbExp=4; IntAct=EBI-717515, EBI-466061;
CC Q14155; Q5S007: LRRK2; NbExp=7; IntAct=EBI-717515, EBI-5323863;
CC Q14155; P50222: MEOX2; NbExp=3; IntAct=EBI-717515, EBI-748397;
CC Q14155; P41227: NAA10; NbExp=3; IntAct=EBI-717515, EBI-747693;
CC Q14155; Q13153: PAK1; NbExp=12; IntAct=EBI-717515, EBI-1307;
CC Q14155; Q13177: PAK2; NbExp=4; IntAct=EBI-717515, EBI-1045887;
CC Q14155; P30153: PPP2R1A; NbExp=3; IntAct=EBI-717515, EBI-302388;
CC Q14155; P63000: RAC1; NbExp=8; IntAct=EBI-717515, EBI-413628;
CC Q14155; Q14160: SCRIB; NbExp=11; IntAct=EBI-717515, EBI-357345;
CC Q14155; O60880-1: SH2D1A; NbExp=5; IntAct=EBI-717515, EBI-15552052;
CC Q14155; Q9BYB0: SHANK3; NbExp=2; IntAct=EBI-717515, EBI-1752330;
CC Q14155; Q7Z6B7: SRGAP1; NbExp=4; IntAct=EBI-717515, EBI-2481729;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000250}. Cell
CC projection, ruffle {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}.
CC Cell projection, lamellipodium {ECO:0000250}. Note=Detected at cell
CC adhesions. A small proportion is detected at focal adhesions.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=4;
CC IsoId=Q14155-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q14155-1; Sequence=VSP_011032, VSP_011035;
CC Name=2;
CC IsoId=Q14155-2; Sequence=VSP_011033;
CC Name=3;
CC IsoId=Q14155-3; Sequence=VSP_011034;
CC Name=5;
CC IsoId=Q14155-5; Sequence=VSP_034639, VSP_011035;
CC Name=6;
CC IsoId=Q14155-6; Sequence=VSP_011032;
CC -!- PTM: Phosphorylated by PTK2/FAK1; this promotes interaction with RAC1
CC (By similarity). Phosphorylated on Ser-694 by CaMK1; enhancement of GEF
CC activity and downstream activation of RAC1. {ECO:0000250,
CC ECO:0000269|PubMed:18184567}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH50521.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA09763.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=CAD38906.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D63476; BAA09763.2; ALT_INIT; mRNA.
DR EMBL; AL834228; CAD38906.1; ALT_INIT; mRNA.
DR EMBL; AL139086; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL390754; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471085; EAX09143.1; -; Genomic_DNA.
DR EMBL; BC033905; AAH33905.1; -; mRNA.
DR EMBL; BC050521; AAH50521.1; ALT_INIT; mRNA.
DR EMBL; BC060776; AAH60776.1; -; mRNA.
DR EMBL; AB177849; BAD66827.1; -; mRNA.
DR EMBL; AB075521; BAE45764.1; -; mRNA.
DR CCDS; CCDS32009.1; -. [Q14155-3]
DR CCDS; CCDS45068.1; -. [Q14155-4]
DR CCDS; CCDS45069.1; -. [Q14155-2]
DR CCDS; CCDS86362.1; -. [Q14155-6]
DR CCDS; CCDS9521.1; -. [Q14155-1]
DR RefSeq; NP_001106983.1; NM_001113511.2. [Q14155-4]
DR RefSeq; NP_001106984.1; NM_001113512.2. [Q14155-2]
DR RefSeq; NP_001106985.1; NM_001113513.1. [Q14155-1]
DR RefSeq; NP_001307780.1; NM_001320851.1. [Q14155-1]
DR RefSeq; NP_001307782.1; NM_001320853.1.
DR RefSeq; NP_001307783.1; NM_001320854.1.
DR RefSeq; NP_001317526.1; NM_001330597.1. [Q14155-6]
DR RefSeq; NP_001317527.1; NM_001330598.1. [Q14155-6]
DR RefSeq; NP_003890.1; NM_003899.3. [Q14155-1]
DR RefSeq; NP_663788.1; NM_145735.3. [Q14155-3]
DR RefSeq; XP_016876313.1; XM_017020824.1.
DR RefSeq; XP_016876314.1; XM_017020825.1.
DR PDB; 1BY1; NMR; -; A=260-467.
DR PDB; 1ZSG; NMR; -; A=179-243.
DR PDB; 2L3G; NMR; -; A=1-137.
DR PDB; 5SXP; X-ray; 1.65 A; A/B/C/D=183-243.
DR PDBsum; 1BY1; -.
DR PDBsum; 1ZSG; -.
DR PDBsum; 2L3G; -.
DR PDBsum; 5SXP; -.
DR AlphaFoldDB; Q14155; -.
DR SMR; Q14155; -.
DR BioGRID; 114393; 111.
DR CORUM; Q14155; -.
DR DIP; DIP-40794N; -.
DR IntAct; Q14155; 54.
DR MINT; Q14155; -.
DR STRING; 9606.ENSP00000364893; -.
DR GlyGen; Q14155; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q14155; -.
DR MetOSite; Q14155; -.
DR PhosphoSitePlus; Q14155; -.
DR BioMuta; ARHGEF7; -.
DR DMDM; 50403776; -.
DR EPD; Q14155; -.
DR jPOST; Q14155; -.
DR MassIVE; Q14155; -.
DR MaxQB; Q14155; -.
DR PaxDb; Q14155; -.
DR PeptideAtlas; Q14155; -.
DR PRIDE; Q14155; -.
DR ProteomicsDB; 59858; -. [Q14155-4]
DR ProteomicsDB; 59859; -. [Q14155-1]
DR ProteomicsDB; 59860; -. [Q14155-2]
DR ProteomicsDB; 59861; -. [Q14155-3]
DR ProteomicsDB; 59862; -. [Q14155-5]
DR ProteomicsDB; 59863; -. [Q14155-6]
DR Antibodypedia; 1486; 301 antibodies from 33 providers.
DR DNASU; 8874; -.
DR Ensembl; ENST00000317133.9; ENSP00000325994.5; ENSG00000102606.19. [Q14155-3]
DR Ensembl; ENST00000375723.5; ENSP00000364875.1; ENSG00000102606.19. [Q14155-6]
DR Ensembl; ENST00000375736.8; ENSP00000364888.4; ENSG00000102606.19. [Q14155-1]
DR Ensembl; ENST00000375739.6; ENSP00000364891.2; ENSG00000102606.19. [Q14155-2]
DR Ensembl; ENST00000375741.6; ENSP00000364893.2; ENSG00000102606.19. [Q14155-4]
DR Ensembl; ENST00000426073.6; ENSP00000397068.2; ENSG00000102606.19. [Q14155-1]
DR GeneID; 8874; -.
DR KEGG; hsa:8874; -.
DR UCSC; uc001vrr.3; human. [Q14155-4]
DR CTD; 8874; -.
DR DisGeNET; 8874; -.
DR GeneCards; ARHGEF7; -.
DR HGNC; HGNC:15607; ARHGEF7.
DR HPA; ENSG00000102606; Low tissue specificity.
DR MIM; 605477; gene.
DR neXtProt; NX_Q14155; -.
DR OpenTargets; ENSG00000102606; -.
DR PharmGKB; PA24977; -.
DR VEuPathDB; HostDB:ENSG00000102606; -.
DR eggNOG; KOG2070; Eukaryota.
DR GeneTree; ENSGT00940000155360; -.
DR InParanoid; Q14155; -.
DR OrthoDB; 547556at2759; -.
DR PhylomeDB; Q14155; -.
DR TreeFam; TF316105; -.
DR PathwayCommons; Q14155; -.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-3928664; Ephrin signaling.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013406; RHOQ GTPase cycle.
DR Reactome; R-HSA-9013409; RHOJ GTPase cycle.
DR Reactome; R-HSA-9013420; RHOU GTPase cycle.
DR Reactome; R-HSA-9013424; RHOV GTPase cycle.
DR Reactome; R-HSA-9619229; Activation of RAC1 downstream of NMDARs. [Q14155-1]
DR SignaLink; Q14155; -.
DR SIGNOR; Q14155; -.
DR BioGRID-ORCS; 8874; 226 hits in 1073 CRISPR screens.
DR ChiTaRS; ARHGEF7; human.
DR EvolutionaryTrace; Q14155; -.
DR GeneWiki; ARHGEF7; -.
DR GenomeRNAi; 8874; -.
DR Pharos; Q14155; Tbio.
DR PRO; PR:Q14155; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q14155; protein.
DR Bgee; ENSG00000102606; Expressed in middle temporal gyrus and 192 other tissues.
DR ExpressionAtlas; Q14155; baseline and differential.
DR Genevisible; Q14155; HS.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0097431; C:mitotic spindle pole; IDA:UniProtKB.
DR GO; GO:0043005; C:neuron projection; IDA:BHF-UCL.
DR GO; GO:0043025; C:neuronal cell body; IDA:BHF-UCL.
DR GO; GO:0098794; C:postsynapse; ISS:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0043015; F:gamma-tubulin binding; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:BHF-UCL.
DR GO; GO:0019901; F:protein kinase binding; IPI:BHF-UCL.
DR GO; GO:0048013; P:ephrin receptor signaling pathway; TAS:Reactome.
DR GO; GO:0048041; P:focal adhesion assembly; HDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0030032; P:lamellipodium assembly; ISS:UniProtKB.
DR GO; GO:1905833; P:negative regulation of microtubule nucleation; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
DR GO; GO:0010763; P:positive regulation of fibroblast migration; HDA:UniProtKB.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:BHF-UCL.
DR GO; GO:2000394; P:positive regulation of lamellipodium morphogenesis; HMP:UniProtKB.
DR GO; GO:1900026; P:positive regulation of substrate adhesion-dependent cell spreading; HMP:UniProtKB.
DR GO; GO:1904424; P:regulation of GTP binding; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR CDD; cd01225; PH_Cool_Pix; 1.
DR CDD; cd00160; RhoGEF; 1.
DR CDD; cd12061; SH3_betaPIX; 1.
DR Gene3D; 1.10.418.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR IDEAL; IID00279; -.
DR InterPro; IPR035789; BetaPIX_SH3.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR046376; PH_Cool_Pix.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00307; CH; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF07653; SH3_2; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00033; CH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell junction;
KW Cell projection; Cytoplasm; Guanine-nucleotide releasing factor;
KW Neurogenesis; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..803
FT /note="Rho guanine nucleotide exchange factor 7"
FT /id="PRO_0000080921"
FT DOMAIN 1..133
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 184..243
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 271..451
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 473..578
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 580..655
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 678..704
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..773
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 580..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 688..704
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 153
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES28"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES28"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 694
FT /note="Phosphoserine; by CaMK1"
FT /evidence="ECO:0000269|PubMed:18184567,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..178
FT /note="Missing (in isoform 1 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8590280, ECO:0000303|PubMed:9726964"
FT /id="VSP_011032"
FT VAR_SEQ 56..105
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011033"
FT VAR_SEQ 85..177
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15491607"
FT /id="VSP_034639"
FT VAR_SEQ 85..105
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_011034"
FT VAR_SEQ 733..803
FT /note="TWQGTDLMHNHVLADDDQPSLDSLGRRSSLSRLEPSDLSEDSDYDSIWTAHS
FT YRMGSTSRKSCCSYISHQN -> SSRKESAPQVLLPEEEKIIVEETKSNGQTVIEEKSL
FT VDTVYALKDEVQELRQDNKKMKKSLEEEQRARKDLEKLVRKVLKNMNDPAWDETNL
FT (in isoform 1 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15491607, ECO:0000303|PubMed:8590280,
FT ECO:0000303|PubMed:9726964"
FT /id="VSP_011035"
FT VARIANT 790
FT /note="T -> A (found in a clear cell renal carcinoma case;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:21248752"
FT /id="VAR_064694"
FT CONFLICT 52..55
FT /note="TIEK -> EEKR (in Ref. 7; BAD66827)"
FT /evidence="ECO:0000305"
FT CONFLICT 343
FT /note="Q -> K (in Ref. 6; AAH33905)"
FT /evidence="ECO:0000305"
FT CONFLICT 552
FT /note="M -> V (in Ref. 6; AAH33905)"
FT /evidence="ECO:0000305"
FT CONFLICT 595
FT /note="H -> D (in Ref. 7; BAD66827)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="I -> T (in Ref. 6; AAH50521)"
FT /evidence="ECO:0000305"
FT CONFLICT 740
FT /note="M -> L (in Ref. 6; AAH33905)"
FT /evidence="ECO:0000305"
FT HELIX 3..13
FT /evidence="ECO:0007829|PDB:2L3G"
FT HELIX 27..35
FT /evidence="ECO:0007829|PDB:2L3G"
FT HELIX 39..48
FT /evidence="ECO:0007829|PDB:2L3G"
FT HELIX 63..79
FT /evidence="ECO:0007829|PDB:2L3G"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:2L3G"
FT HELIX 118..135
FT /evidence="ECO:0007829|PDB:2L3G"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:5SXP"
FT STRAND 210..216
FT /evidence="ECO:0007829|PDB:5SXP"
FT STRAND 218..226
FT /evidence="ECO:0007829|PDB:5SXP"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5SXP"
FT HELIX 235..237
FT /evidence="ECO:0007829|PDB:5SXP"
FT STRAND 238..240
FT /evidence="ECO:0007829|PDB:5SXP"
FT HELIX 271..301
FT /evidence="ECO:0007829|PDB:1BY1"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1BY1"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:1BY1"
FT HELIX 311..313
FT /evidence="ECO:0007829|PDB:1BY1"
FT HELIX 316..338
FT /evidence="ECO:0007829|PDB:1BY1"
FT HELIX 346..378
FT /evidence="ECO:0007829|PDB:1BY1"
FT TURN 379..381
FT /evidence="ECO:0007829|PDB:1BY1"
FT HELIX 382..385
FT /evidence="ECO:0007829|PDB:1BY1"
FT TURN 386..389
FT /evidence="ECO:0007829|PDB:1BY1"
FT TURN 395..397
FT /evidence="ECO:0007829|PDB:1BY1"
FT HELIX 398..402
FT /evidence="ECO:0007829|PDB:1BY1"
FT TURN 406..408
FT /evidence="ECO:0007829|PDB:1BY1"
FT HELIX 409..411
FT /evidence="ECO:0007829|PDB:1BY1"
FT HELIX 413..422
FT /evidence="ECO:0007829|PDB:1BY1"
FT STRAND 428..430
FT /evidence="ECO:0007829|PDB:1BY1"
FT HELIX 432..453
FT /evidence="ECO:0007829|PDB:1BY1"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:1BY1"
FT INIT_MET Q14155-1:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q14155-1:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q14155-1:2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q14155-1:560
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES Q14155-1:579
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES Q14155-5:645
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES Q14155-5:664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT INIT_MET Q14155-6:1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES Q14155-6:1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES Q14155-6:2
FT /note="N-acetylthreonine"
FT /evidence="ECO:0007744|PubMed:22223895"
SQ 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
