ARHG5_HUMAN
ID ARHG5_HUMAN Reviewed; 1597 AA.
AC Q12774; A6NNJ2; Q6ZML7;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 02-MAR-2010, sequence version 3.
DT 03-AUG-2022, entry version 190.
DE RecName: Full=Rho guanine nucleotide exchange factor 5;
DE AltName: Full=Ephexin-3;
DE AltName: Full=Guanine nucleotide regulatory protein TIM;
DE AltName: Full=Oncogene TIM;
DE AltName: Full=Transforming immortalized mammary oncogene;
DE AltName: Full=p60 TIM;
GN Name=ARHGEF5; Synonyms=TIM;
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 [MRNA] (ISOFORM 2).
RC TISSUE=Epithelium;
RX PubMed=8134109;
RA Chan A.M.-L., McGovern E.S., Catalano G., Fleming T.P., Miki T.;
RT "Expression cDNA cloning of a novel oncogene with sequence similarity to
RT regulators of small GTP-binding proteins.";
RL Oncogene 9:1057-1063(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta, and Skin;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING, AND TISSUE
RP SPECIFICITY.
RX PubMed=14662653; DOI=10.1093/hmg/ddh024;
RA Debily M.A., Camarca A., Ciullo M., Mayer C., El Marhomy S., Ba I.,
RA Jalil A., Anzisi A., Guardiola J., Piatier-Tonneau D.;
RT "Expression and molecular characterization of alternative transcripts of
RT the ARHGEF5/TIM oncogene specific for human breast cancer.";
RL Hum. Mol. Genet. 13:323-334(2004).
RN [7]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=15601624; DOI=10.1016/j.cellsig.2004.09.012;
RA Xie X., Chang S.W., Tatsumoto T., Chan A.M., Miki T.;
RT "TIM, a Dbl-related protein, regulates cell shape and cytoskeletal
RT organization in a Rho-dependent manner.";
RL Cell. Signal. 17:461-471(2005).
RN [8]
RP NOMENCLATURE.
RX PubMed=15848799; DOI=10.1016/j.neuron.2005.01.030;
RA Sahin M., Greer P.L., Lin M.Z., Poucher H., Eberhart J., Schmidt S.,
RA Wright T.M., Shamah S.M., O'connell S., Cowan C.W., Hu L., Goldberg J.L.,
RA Debant A., Corfas G., Krull C.E., Greenberg M.E.;
RT "Eph-dependent tyrosine phosphorylation of ephexin1 modulates growth cone
RT collapse.";
RL Neuron 46:191-204(2005).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445 AND SER-450, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184; SER-445; SER-450 AND
RP SER-1126, AND IDENTIFICATION BY 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-450 AND SER-1126,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-445; SER-450; SER-983;
RP SER-1011; SER-1044 AND SER-1126, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-450, AND IDENTIFICATION BY
RP 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 [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-866, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP INTERACTION WITH ODAM, AND SUBCELLULAR LOCATION.
RX PubMed=25911094; DOI=10.1074/jbc.m115.648022;
RA Lee H.K., Ji S., Park S.J., Choung H.W., Choi Y., Lee H.J., Park S.Y.,
RA Park J.C.;
RT "Odontogenic ameloblast-associated protein (ODAM) Mediates Junctional
RT Epithelium Attachment to Tooth via Integrin-ODAM-Rho guanine nucleotide
RT exchange factor 5 (ARHGEF5)-Ras homolog gene family member A (RhoA)
RT Signaling.";
RL J. Biol. Chem. 290:14740-14753(2015).
CC -!- FUNCTION: Guanine nucleotide exchange factor which activates Rho
CC GTPases (PubMed:15601624). Strongly activates RHOA (PubMed:15601624).
CC Also strongly activates RHOB, weakly activates RHOC and RHOG and shows
CC no effect on RHOD, RHOV, RHOQ or RAC1 (By similarity). Involved in
CC regulation of cell shape and actin cytoskeletal organization
CC (PubMed:15601624). Plays a role in actin organization by generating a
CC loss of actin stress fibers and the formation of membrane ruffles and
CC filopodia (PubMed:14662653). Required for SRC-induced podosome
CC formation (By similarity). Involved in positive regulation of immature
CC dendritic cell migration (By similarity).
CC {ECO:0000250|UniProtKB:E9Q7D5, ECO:0000269|PubMed:14662653,
CC ECO:0000269|PubMed:15601624}.
CC -!- SUBUNIT: Interacts with SRC (By similarity). Forms a ternary complex
CC with SRC and the PI3K 85 kDa subunit (By similarity). Interacts with
CC and is activated by the heterodimer formed by GNB1 and GNG2 (By
CC similarity). Interacts with ODAM (via C-terminus) (PubMed:25911094).
CC Interacts with RHOA (By similarity). {ECO:0000250|UniProtKB:E9Q7D5,
CC ECO:0000269|PubMed:25911094}.
CC -!- INTERACTION:
CC Q12774; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-602199, EBI-739580;
CC Q12774; Q9Y2V7: COG6; NbExp=5; IntAct=EBI-602199, EBI-3866319;
CC Q12774; Q5JST6: EFHC2; NbExp=6; IntAct=EBI-602199, EBI-2349927;
CC Q12774; Q7L775: EPM2AIP1; NbExp=3; IntAct=EBI-602199, EBI-6255981;
CC Q12774; P62993: GRB2; NbExp=7; IntAct=EBI-602199, EBI-401755;
CC Q12774; O75031: HSF2BP; NbExp=3; IntAct=EBI-602199, EBI-7116203;
CC Q12774; Q96EW2: HSPBAP1; NbExp=6; IntAct=EBI-602199, EBI-720457;
CC Q12774; P25791-3: LMO2; NbExp=3; IntAct=EBI-602199, EBI-11959475;
CC Q12774; Q96KN4: LRATD1; NbExp=5; IntAct=EBI-602199, EBI-11477916;
CC Q12774; Q8IYB1: MB21D2; NbExp=3; IntAct=EBI-602199, EBI-11323212;
CC Q12774; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-602199, EBI-10172526;
CC Q12774; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-602199, EBI-79165;
CC Q12774; Q58EX7: PLEKHG4; NbExp=3; IntAct=EBI-602199, EBI-949255;
CC Q12774; O15160: POLR1C; NbExp=5; IntAct=EBI-602199, EBI-1055079;
CC Q12774; Q8ND83: SLAIN1; NbExp=3; IntAct=EBI-602199, EBI-10269374;
CC Q12774; Q9NVG8: TBC1D13; NbExp=6; IntAct=EBI-602199, EBI-12264956;
CC Q12774; P15884-3: TCF4; NbExp=3; IntAct=EBI-602199, EBI-13636688;
CC Q12774; P14373: TRIM27; NbExp=6; IntAct=EBI-602199, EBI-719493;
CC Q12774; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-602199, EBI-2130429;
CC Q12774; P07947: YES1; NbExp=3; IntAct=EBI-602199, EBI-515331;
CC Q12774; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-602199, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14662653,
CC ECO:0000269|PubMed:25911094}. Nucleus {ECO:0000269|PubMed:14662653}.
CC Cell projection, podosome {ECO:0000250|UniProtKB:E9Q7D5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Comment=A number of additional isoforms are detected in primary
CC breast tumors but not in normal tissues.
CC {ECO:0000269|PubMed:14662653};
CC Name=1;
CC IsoId=Q12774-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12774-2; Sequence=VSP_035175;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed with highest levels in
CC placenta. High levels are also found in colon, kidney, trachea,
CC prostate, liver, pancreas, pituitary gland, thyroid gland and mammary
CC gland. In fetal tissues, expressed at high levels in kidney, lung and
CC liver (PubMed:15601624). Expressed at low levels in lung and heart
CC (PubMed:14662653). {ECO:0000269|PubMed:14662653,
CC ECO:0000269|PubMed:15601624}.
CC -!- DOMAIN: The PH domain binds to phosphoinositides and is essential for
CC podosome formation. {ECO:0000250|UniProtKB:E9Q7D5}.
CC -!- PTM: Activation of SRC induces tyrosine phosphorylation of ARHGEF5.
CC {ECO:0000250|UniProtKB:E9Q7D5}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD18708.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U02082; AAA18010.1; -; mRNA.
DR EMBL; AK160365; BAD18708.1; ALT_INIT; mRNA.
DR EMBL; AC004534; AAC12958.1; -; Genomic_DNA.
DR EMBL; CH471146; EAW80096.1; -; Genomic_DNA.
DR EMBL; BC010046; AAH10046.1; -; mRNA.
DR EMBL; BC011839; AAH11839.1; -; mRNA.
DR EMBL; BC014555; AAH14555.1; -; mRNA.
DR CCDS; CCDS34771.1; -. [Q12774-1]
DR PIR; I38402; I38402.
DR RefSeq; NP_005426.2; NM_005435.3. [Q12774-1]
DR AlphaFoldDB; Q12774; -.
DR SMR; Q12774; -.
DR BioGRID; 113696; 80.
DR IntAct; Q12774; 39.
DR MINT; Q12774; -.
DR STRING; 9606.ENSP00000056217; -.
DR iPTMnet; Q12774; -.
DR PhosphoSitePlus; Q12774; -.
DR BioMuta; ARHGEF5; -.
DR DMDM; 290457679; -.
DR EPD; Q12774; -.
DR jPOST; Q12774; -.
DR MassIVE; Q12774; -.
DR MaxQB; Q12774; -.
DR PaxDb; Q12774; -.
DR PeptideAtlas; Q12774; -.
DR PRIDE; Q12774; -.
DR ProteomicsDB; 58920; -. [Q12774-1]
DR ProteomicsDB; 58921; -. [Q12774-2]
DR Antibodypedia; 18513; 344 antibodies from 36 providers.
DR DNASU; 7984; -.
DR Ensembl; ENST00000056217.10; ENSP00000056217.5; ENSG00000050327.15. [Q12774-1]
DR Ensembl; ENST00000471847.2; ENSP00000418227.1; ENSG00000050327.15. [Q12774-2]
DR GeneID; 7984; -.
DR KEGG; hsa:7984; -.
DR MANE-Select; ENST00000056217.10; ENSP00000056217.5; NM_005435.4; NP_005426.2.
DR UCSC; uc003wel.4; human. [Q12774-1]
DR CTD; 7984; -.
DR DisGeNET; 7984; -.
DR GeneCards; ARHGEF5; -.
DR HGNC; HGNC:13209; ARHGEF5.
DR HPA; ENSG00000050327; Tissue enhanced (skin).
DR MIM; 600888; gene.
DR neXtProt; NX_Q12774; -.
DR OpenTargets; ENSG00000050327; -.
DR PharmGKB; PA24975; -.
DR VEuPathDB; HostDB:ENSG00000050327; -.
DR eggNOG; KOG3523; Eukaryota.
DR GeneTree; ENSGT01030000234571; -.
DR HOGENOM; CLU_003633_0_0_1; -.
DR InParanoid; Q12774; -.
DR OMA; QDDVMLG; -.
DR OrthoDB; 1176939at2759; -.
DR PhylomeDB; Q12774; -.
DR TreeFam; TF342609; -.
DR PathwayCommons; Q12774; -.
DR Reactome; R-HSA-193648; NRAGE signals death through JNK.
DR Reactome; R-HSA-416482; G alpha (12/13) signalling events.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013026; RHOB GTPase cycle.
DR Reactome; R-HSA-9013106; RHOC GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR SignaLink; Q12774; -.
DR SIGNOR; Q12774; -.
DR BioGRID-ORCS; 7984; 53 hits in 1063 CRISPR screens.
DR ChiTaRS; ARHGEF5; human.
DR GeneWiki; ARHGEF5; -.
DR GenomeRNAi; 7984; -.
DR Pharos; Q12774; Tbio.
DR PRO; PR:Q12774; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q12774; protein.
DR Bgee; ENSG00000050327; Expressed in lower esophagus mucosa and 92 other tissues.
DR ExpressionAtlas; Q12774; baseline and differential.
DR Genevisible; Q12774; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; TAS:ProtInc.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0030036; P:actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:0090630; P:activation of GTPase activity; IBA:GO_Central.
DR GO; GO:0061484; P:hematopoietic stem cell homeostasis; IEA:Ensembl.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0002408; P:myeloid dendritic cell chemotaxis; IEA:Ensembl.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
DR GO; GO:0043507; P:positive regulation of JUN kinase activity; IDA:UniProtKB.
DR GO; GO:0071803; P:positive regulation of podosome assembly; IEA:Ensembl.
DR GO; GO:1904591; P:positive regulation of protein import; IMP:UniProtKB.
DR GO; GO:0051496; P:positive regulation of stress fiber assembly; IMP:UniProtKB.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0043087; P:regulation of GTPase activity; IDA:MGI.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR029212; ARHGEF5/35_N.
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; IPR001849; PH_domain.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF15441; ARHGEF5_35; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF50044; SSF50044; 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 Alternative splicing; Cell junction; Cell projection; Cytoplasm;
KW Guanine-nucleotide releasing factor; Lipid-binding; Methylation; Nucleus;
KW Phosphoprotein; Proto-oncogene; Reference proteome; SH3 domain.
FT CHAIN 1..1597
FT /note="Rho guanine nucleotide exchange factor 5"
FT /id="PRO_0000080916"
FT DOMAIN 1174..1358
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 1390..1502
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 1510..1571
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 138..246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 258..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..1072
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..276
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 306..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 488..512
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 590..613
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..687
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 810..827
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..858
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 898..946
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 993..1014
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 184
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 445
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 450
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 866
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1011
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1044
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..1078
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:8134109"
FT /id="VSP_035175"
FT CONFLICT 487
FT /note="E -> G (in Ref. 2; BAD18708)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="P -> Q (in Ref. 2; BAD18708)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1597 AA; 176799 MW; 93EC1B1D7E1198C5 CRC64;
MEAEEAQRGA SPPISAIEEF SIIPEAPMRS SQVSALGLEA QEDEDPSYKW REEHRLSATQ
QSELRDVCDY AIETMPSFPK EGSADVEPNQ ESLVAEACDT PEHWEAVPQS LAGRQARTLA
PPELWACPIQ SEHLDMAPFS SDLGSEEEEV EFWPGLTSLT LGSGQAEEEE ETSSDNSGQT
RYYSPCEEHP AETNQNEGSE SGTIRQGEEL PPEELQESQG LLHPQEVQVL EEQGQQEAGF
RGEGTLREDV CADGLLGEEQ MIEQVNDEKG EQKQKQEQVQ DVMLGRQGER MGLTGEPEGL
NDGEWEQEDM ERKAQGQGGP EQGEERKREL QVPEENRADS QDEKSQTFLG KSEEVTGKQE
DHGIKEKGVP VSGQEAKEPE SWDGGRLGAV GRARSREEEN EHHGPSMPAL IAPEDSPHCD
LFPGASYLMT QIPGTQTESR AEELSPAALS PSLEPIRCSH QPISLLGSFL TEESPDKEID
QNSQQEESRL RKGTVSSQGT EVVFASASVT PPRTPDSAPP SPAEAYPITP ASVSARPPVA
FPRRETSCAA RAPETASAPL SMDDPSPCGT SEMCPAALYG FPSTGTSPPR PPANSTGTVQ
HLRSDSFPGS HRTEQTPDLV GMLLSYSHSE LPQRPPKPAI YSSVTPRRDR RSGRDYSTVS
ASPTALSTLK QDSQESISNL ERPSSPPSIQ PWVSPHNPAF ATESPAYGSS PSFVSMEDVR
IHEPLPPPPP QRRDTHPSVV ETDGHARVVV PTLKQHSHPP PLALGSGLHA PHKGPLPQAS
DPAVARQHRP LPSTPDSSHH AQATPRWRYN KPLPPTPDLP QPHLPPISAP GSSRIYRPLP
PLPIIDPPTE PPPLPPKSRG RSRSTRGGHM NSGGHAKTRP ACQDWTVPLP ASAGRTSWPP
ATARSTESFT STSRSKSEVS PGMAFSNMTN FLCPSSPTTP WTPELQGPTS KDEAGVSEHP
EAPAREPLRR TTPQQGASGP GRSPVGQARQ PEKPSHLHLE KASSWPHRRD SGRPPGDSSG
QAVAPSEGAN KHKGWSRQGL RRPSILPEGS SDSRGPAVEK HPGPSDTVVF REKKPKEVMG
GFSRRCSKLI NSSQLLYQEY SDVVLNKEIQ SQQRLESLSE TPGPSSPRQP RKALVSSESY
LQRLSMASSG SLWQEIPVVR NSTVLLSMTH EDQKLQEVKF ELIVSEASYL RSLNIAVDHF
QLSTSLRATL SNQEHQWLFS RLQDVRDVSA TFLSDLEENF ENNIFSFQVC DVVLNHAPDF
RRVYLPYVTN QTYQERTFQS LMNSNSNFRE VLEKLESDPV CQRLSLKSFL ILPFQRITRL
KLLLQNILKR TQPGSSEEAE ATKAHHALEQ LIRDCNNNVQ SMRRTEELIY LSQKIEFECK
IFPLISQSRW LVKSGELTAL EFSASPGLRR KLNTRPVHLH LFNDCLLLSR PREGSRFLVF
DHAPFSSIRG EKCEMKLHGP HKNLFRLFLR QNTQGAQAEF LFRTETQSEK LRWISALAMP
REELDLLECY NSPQVQCLRA YKPRENDELA LEKADVVMVT QQSSDGWLEG VRLSDGERGW
FPVQQVEFIS NPEVRAQNLK EAHRVKTAKL QLVEQQA
