ID ARHGB_HUMAN Reviewed; 1522 AA.
AC O15085; D3DVD0; Q5VY40; Q6PFW2;
DT 29-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 206.
DE RecName: Full=Rho guanine nucleotide exchange factor 11;
DE AltName: Full=PDZ-RhoGEF;
GN Name=ARHGEF11; Synonyms=KIAA0380;
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=Brain;
RX PubMed=9205841; DOI=10.1093/dnares/4.2.141;
RA Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VII. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 4:141-150(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-1427.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [5]
RP INTERACTION WITH RHOA.
RX PubMed=10526156; DOI=10.1016/s0014-5793(99)01270-3;
RA Ruemenapp U., Blomquist A., Schwoerer G., Schablowski H., Psoma A.,
RA Jakobs K.H.;
RT "Rho-specific binding and guanine nucleotide exchange catalysis by
RT KIAA0380, a dbl family member.";
RL FEBS Lett. 459:313-318(1999).
RN [6]
RP INTERACTION WITH GNA12 AND GNA13, AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10026210; DOI=10.1074/jbc.274.9.5868;
RA Fukuhara S., Murga C., Zohar M., Igishi T., Gutkind J.S.;
RT "A novel PDZ domain containing guanine nucleotide exchange factor links
RT heterotrimeric G proteins to Rho.";
RL J. Biol. Chem. 274:5868-5879(1999).
RN [7]
RP INTERACTION WITH PLXNB1 AND PLXNB2.
RX PubMed=12372594; DOI=10.1016/s0014-5793(02)03323-9;
RA Driessens M.H.E., Olivo C., Nagata K., Inagaki M., Collard J.G.;
RT "B plexins activate Rho through PDZ-RhoGEF.";
RL FEBS Lett. 529:168-172(2002).
RN [8]
RP INTERACTION WITH PLXNB1 AND PLXNB2.
RX PubMed=12183458; DOI=10.1074/jbc.m206005200;
RA Perrot V., Vazquez-Prado J., Gutkind J.S.;
RT "Plexin B regulates Rho through the guanine nucleotide exchange factors
RT leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF.";
RL J. Biol. Chem. 277:43115-43120(2002).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=10900204; DOI=10.1074/jbc.m003726200;
RA Togashi H., Nagata K., Takagishi M., Saitoh N., Inagaki M.;
RT "Functions of a rho-specific guanine nucleotide exchange factor in neurite
RT retraction. Possible role of a proline-rich motif of KIAA0380 in
RT localization.";
RL J. Biol. Chem. 275:29570-29578(2000).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND THR-668, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245; SER-251; THR-254;
RP THR-668; THR-672; SER-1155; SER-1300; SER-1457; SER-1458; THR-1475 AND
RP SER-1480, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-668, 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 [13]
RP INTERACTION WITH GCSAM.
RX PubMed=20844236; DOI=10.1182/blood-2010-04-281568;
RA Jiang X., Lu X., McNamara G., Liu X., Cubedo E., Sarosiek K.A.,
RA Sanchez-Garcia I., Helfman D.M., Lossos I.S.;
RT "HGAL, a germinal center specific protein, decreases lymphoma cell motility
RT by modulation of the RhoA signaling pathway.";
RL Blood 116:5217-5227(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-245, AND IDENTIFICATION BY
RP 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 [15]
RP FUNCTION, UBIQUITINATION, AND PHOSPHORYLATION.
RX PubMed=21670212; DOI=10.1083/jcb.201103015;
RA Lin M.Y., Lin Y.M., Kao T.C., Chuang H.H., Chen R.H.;
RT "PDZ-RhoGEF ubiquitination by Cullin3-KLHL20 controls neurotrophin-induced
RT neurite outgrowth.";
RL J. Cell Biol. 193:985-994(2011).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION BY
RP 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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-16; SER-35; SER-556;
RP SER-635; THR-668; THR-672; SER-1295; SER-1458; THR-1462 AND SER-1480, 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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663 AND THR-668, 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 [19]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 281-490.
RX PubMed=11470431; DOI=10.1016/s0969-2126(01)00620-7;
RA Longenecker K.L., Lewis M.E., Chikumi H., Gutkind J.S., Derewenda Z.S.;
RT "Structure of the RGS-like domain from PDZ-RhoGEF: linking heterotrimeric g
RT protein-coupled signaling to Rho GTPases.";
RL Structure 9:559-569(2001).
RN [20]
RP STRUCTURE BY NMR OF 44-123.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the PDZ domain of human Rho guanine nucleotide
RT exchange factor 11.";
RL Submitted (OCT-2006) to the PDB data bank.
CC -!- FUNCTION: May play a role in the regulation of RhoA GTPase by guanine
CC nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). Acts as
CC guanine nucleotide exchange factor (GEF) for RhoA GTPase and may act as
CC GTPase-activating protein (GAP) for GNA12 and GNA13. Involved in
CC neurotrophin-induced neurite outgrowth. {ECO:0000269|PubMed:21670212}.
CC -!- SUBUNIT: Interacts with GNA12 and GNA13 through the RGS domain.
CC Interacts with RHOA, PLXNB1 and PLXNB2. Interacts with SLC1A6 (By
CC similarity). Interacts (via DH domain) with GCSAM (via C-terminus).
CC {ECO:0000250, ECO:0000269|PubMed:10026210, ECO:0000269|PubMed:10526156,
CC ECO:0000269|PubMed:12183458, ECO:0000269|PubMed:12372594,
CC ECO:0000269|PubMed:20844236}.
CC -!- INTERACTION:
CC O15085; P46108: CRK; NbExp=2; IntAct=EBI-311099, EBI-886;
CC O15085; P16333: NCK1; NbExp=3; IntAct=EBI-311099, EBI-389883;
CC O15085; P61586: RHOA; NbExp=11; IntAct=EBI-311099, EBI-446668;
CC O15085; Q7DB74: espH; Xeno; NbExp=4; IntAct=EBI-311099, EBI-7864788;
CC O15085-1; Q96PX9: PLEKHG4B; NbExp=3; IntAct=EBI-25399484, EBI-11741362;
CC O15085-2; Q8BPM0: Daam1; Xeno; NbExp=3; IntAct=EBI-6169263, EBI-772938;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10900204}. Membrane
CC {ECO:0000269|PubMed:10900204}. Note=Translocated to the membrane upon
CC stimulation.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15085-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15085-2; Sequence=VSP_042003;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10026210}.
CC -!- DOMAIN: The poly-Pro region is essential for plasma membrane
CC localization upon stimulation.
CC -!- PTM: Phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or
CC MAPK14).
CC -!- PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex when
CC previously phosphorylated by MAP kinase p38 (MAPK11, MAPK12, MAPK13
CC and/or MAPK14), leading to its degradation, thereby restricting RhoA
CC activity and facilitating growth cone spreading and neurite outgrowth.
CC {ECO:0000269|PubMed:21670212}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA20834.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB002378; BAA20834.2; ALT_INIT; mRNA.
DR EMBL; AL356104; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL157713; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471121; EAW52893.1; -; Genomic_DNA.
DR EMBL; CH471121; EAW52894.1; -; Genomic_DNA.
DR EMBL; BC057394; AAH57394.1; -; mRNA.
DR CCDS; CCDS1162.1; -. [O15085-1]
DR CCDS; CCDS1163.1; -. [O15085-2]
DR RefSeq; NP_055599.1; NM_014784.3. [O15085-1]
DR RefSeq; NP_937879.1; NM_198236.2. [O15085-2]
DR PDB; 1HTJ; X-ray; 2.20 A; F=281-490.
DR PDB; 1XCG; X-ray; 2.50 A; A/E=714-1081.
DR PDB; 2DLS; NMR; -; A=44-123.
DR PDB; 3KZ1; X-ray; 2.70 A; A/B=710-1085.
DR PDB; 3T06; X-ray; 2.84 A; A/E=672-1081.
DR PDB; 5E6P; X-ray; 3.21 A; B=42-125.
DR PDB; 5JHG; X-ray; 2.50 A; A/E=714-1081.
DR PDB; 5JHH; X-ray; 2.30 A; A/E=714-1081.
DR PDB; 5TYT; X-ray; 2.40 A; A/B/C/D=41-123.
DR PDBsum; 1HTJ; -.
DR PDBsum; 1XCG; -.
DR PDBsum; 2DLS; -.
DR PDBsum; 3KZ1; -.
DR PDBsum; 3T06; -.
DR PDBsum; 5E6P; -.
DR PDBsum; 5JHG; -.
DR PDBsum; 5JHH; -.
DR PDBsum; 5TYT; -.
DR AlphaFoldDB; O15085; -.
DR SMR; O15085; -.
DR BioGRID; 115164; 65.
DR DIP; DIP-31622N; -.
DR IntAct; O15085; 54.
DR MINT; O15085; -.
DR STRING; 9606.ENSP00000357177; -.
DR ChEMBL; CHEMBL4523642; -.
DR GlyCosmos; O15085; 1 site, 2 glycans.
DR GlyGen; O15085; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O15085; -.
DR PhosphoSitePlus; O15085; -.
DR BioMuta; ARHGEF11; -.
DR EPD; O15085; -.
DR jPOST; O15085; -.
DR MassIVE; O15085; -.
DR MaxQB; O15085; -.
DR PaxDb; 9606-ENSP00000357177; -.
DR PeptideAtlas; O15085; -.
DR ProteomicsDB; 48441; -. [O15085-1]
DR ProteomicsDB; 48442; -. [O15085-2]
DR Pumba; O15085; -.
DR Antibodypedia; 1659; 303 antibodies from 29 providers.
DR DNASU; 9826; -.
DR Ensembl; ENST00000361409.2; ENSP00000354644.2; ENSG00000132694.19. [O15085-1]
DR Ensembl; ENST00000368194.8; ENSP00000357177.3; ENSG00000132694.19. [O15085-2]
DR GeneID; 9826; -.
DR KEGG; hsa:9826; -.
DR MANE-Select; ENST00000368194.8; ENSP00000357177.3; NM_198236.3; NP_937879.1. [O15085-2]
DR UCSC; uc001fqn.3; human. [O15085-1]
DR AGR; HGNC:14580; -.
DR CTD; 9826; -.
DR DisGeNET; 9826; -.
DR GeneCards; ARHGEF11; -.
DR HGNC; HGNC:14580; ARHGEF11.
DR HPA; ENSG00000132694; Low tissue specificity.
DR MIM; 605708; gene.
DR neXtProt; NX_O15085; -.
DR OpenTargets; ENSG00000132694; -.
DR PharmGKB; PA24968; -.
DR VEuPathDB; HostDB:ENSG00000132694; -.
DR eggNOG; KOG3520; Eukaryota.
DR GeneTree; ENSGT00940000158350; -.
DR HOGENOM; CLU_003962_5_0_1; -.
DR InParanoid; O15085; -.
DR OMA; FICGERQ; -.
DR OrthoDB; 2875542at2759; -.
DR PhylomeDB; O15085; -.
DR TreeFam; TF106495; -.
DR PathwayCommons; O15085; -.
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-416572; Sema4D induced cell migration and growth-cone collapse.
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 SignaLink; O15085; -.
DR SIGNOR; O15085; -.
DR BioGRID-ORCS; 9826; 19 hits in 1161 CRISPR screens.
DR ChiTaRS; ARHGEF11; human.
DR EvolutionaryTrace; O15085; -.
DR GeneWiki; ARHGEF11; -.
DR GenomeRNAi; 9826; -.
DR Pharos; O15085; Tbio.
DR PRO; PR:O15085; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; O15085; Protein.
DR Bgee; ENSG00000132694; Expressed in right testis and 95 other cell types or tissues.
DR Genevisible; O15085; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0001664; F:G protein-coupled receptor binding; IDA:MGI.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB.
DR GO; GO:0030010; P:establishment of cell polarity; NAS:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IDA:MGI.
DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IDA:UniProtKB.
DR GO; GO:0001558; P:regulation of cell growth; NAS:UniProtKB.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; IDA:UniProtKB.
DR GO; GO:0006941; P:striated muscle contraction; NAS:UniProtKB.
DR CDD; cd00992; PDZ_signaling; 1.
DR CDD; cd13391; PH_PRG; 1.
DR CDD; cd08753; RGS_PDZRhoGEF; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 1.20.900.10; Dbl homology (DH) domain; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 1.10.167.10; Regulator of G-protein Signalling 4, domain 2; 1.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR037889; PDZRhoGEF_RGS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR041020; PH_16.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037803; PRG_PH.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR015212; RGS-like_dom.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR044926; RGS_subdomain_2.
DR PANTHER; PTHR45872:SF1; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 11; 1.
DR PANTHER; PTHR45872; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR 2, ISOFORM D; 1.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF17838; PH_16; 1.
DR Pfam; PF09128; RGS-like; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00315; RGS; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; DBL homology domain (DH-domain); 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50729; PH domain-like; 1.
DR SUPFAM; SSF48097; Regulator of G-protein signaling, RGS; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW GTPase activation; Guanine-nucleotide releasing factor; Membrane;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1522
FT /note="Rho guanine nucleotide exchange factor 11"
FT /id="PRO_0000080928"
FT DOMAIN 47..126
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 306..486
FT /note="RGSL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 734..923
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 965..1079
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..40
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..231
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 490..555
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 573..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1223..1320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1332..1423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1453..1522
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 444..470
FT /evidence="ECO:0000255"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..166
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 573..598
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..643
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..668
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1104
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1228..1249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1366..1381
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1406
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES67"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 254
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES67"
FT MOD_RES 271
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9ES67"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 668
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 672
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1155
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1300
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1458
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1462
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1475
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 194
FT /note="Q -> QRICEVYSRNPASLLEEQIEGARRRVTQLQLKIQQETGGSV (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042003"
FT VARIANT 1416
FT /note="S -> G (in dbSNP:rs868188)"
FT /id="VAR_061795"
FT VARIANT 1427
FT /note="H -> R (in dbSNP:rs945508)"
FT /evidence="ECO:0000269|Ref.3"
FT /id="VAR_024285"
FT STRAND 41..51
FT /evidence="ECO:0007829|PDB:5TYT"
FT STRAND 53..56
FT /evidence="ECO:0007829|PDB:2DLS"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5TYT"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:5TYT"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:5TYT"
FT STRAND 74..76
FT /evidence="ECO:0007829|PDB:2DLS"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:5TYT"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:5TYT"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:2DLS"
FT HELIX 102..110
FT /evidence="ECO:0007829|PDB:5TYT"
FT STRAND 112..126
FT /evidence="ECO:0007829|PDB:5TYT"
FT HELIX 307..312
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 314..319
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 321..334
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 338..349
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 356..368
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 381..392
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 398..424
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 428..431
FT /evidence="ECO:0007829|PDB:1HTJ"
FT TURN 432..434
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 443..462
FT /evidence="ECO:0007829|PDB:1HTJ"
FT HELIX 466..482
FT /evidence="ECO:0007829|PDB:1HTJ"
FT STRAND 716..725
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 730..759
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 761..766
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 772..778
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 779..781
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 782..801
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 810..817
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 819..833
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 836..849
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 851..862
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 864..866
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 871..874
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 877..894
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 901..939
FT /evidence="ECO:0007829|PDB:5JHH"
FT TURN 944..946
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 951..956
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 961..963
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 966..975
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 977..979
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 981..999
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 1002..1004
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 1024..1027
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 1028..1030
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 1031..1035
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 1042..1047
FT /evidence="ECO:0007829|PDB:5JHH"
FT STRAND 1050..1052
FT /evidence="ECO:0007829|PDB:1XCG"
FT STRAND 1057..1060
FT /evidence="ECO:0007829|PDB:5JHH"
FT HELIX 1064..1080
FT /evidence="ECO:0007829|PDB:5JHH"
SQ SEQUENCE 1522 AA; 167704 MW; CA16E125B9F8A4AA CRC64;
MSVRLPQSID RLSSLSSLGD SAPERKSPSH HRQPSDASET TGLVQRCVII QKDQHGFGFT
VSGDRIVLVQ SVRPGGAAMK AGVKEGDRII KVNGTMVTNS SHLEVVKLIK SGAYVALTLL
GSSPSSMGIS GLQQDPSPAG APRITSVIPS PPPPPPLPPP QRITGPKPLQ DPEVQKHATQ
ILRNMLRQEE KELQDILPLY GDTSQRPSEG RLSLDSQEGD SGLDSGTERF PSLSESLMNR
NSVLSDPGLD SPRTSPVIMA RVAQHHRRQG SDAAVPSTGD QGVDQSPKPL IIGPEEDYDP
GYFNNESDII FQDLEKLKSR PAHLGVFLRY IFSQADPSPL LFYLCAEVYQ QASPKDSRSL
GKDIWNIFLE KNAPLRVKIP EMLQAEIDSR LRNSEDARGV LCEAQEAAMP EIQEQIHDYR
TKRTLGLGSL YGENDLLDLD GDPLRERQVA EKQLAALGDI LSKYEEDRSA PMDFALNTYM
SHAGIRLREA RPSNTAEKAQ SAPDKDKWLP FFPKTKKSSN SKKEKDALED KKRNPILKYI
GKPKSSSQST FHIPLSPVEV KPGNVRNIIQ HFENNQQYDA PEPGTQRLST GSFPEDLLES
DSSRSEIRLG RSESLKGREE MKRSRKAENV PRSRSDVDMD AAAEATRLHQ SASSSTSSLS
TRSLENPTPP FTPKMGRRSI ESPSLGFCTD TLLPHLLEDD LGQLSDLEPE PDAQNWQHTV
GKDVVAGLTQ REIDRQEVIN ELFVTEASHL RTLRVLDLIF YQRMKKENLM PREELARLFP
NLPELIEIHN SWCEAMKKLR EEGPIIKEIS DLMLARFDGP AREELQQVAA QFCSYQSIAL
ELIKTKQRKE SRFQLFMQEA ESHPQCRRLQ LRDLIISEMQ RLTKYPLLLE SIIKHTEGGT
SEHEKLCRAR DQCREILKYV NEAVKQTENR HRLEGYQKRL DATALERASN PLAAEFKSLD
LTTRKMIHEG PLTWRISKDK TLDLHVLLLE DLLVLLQKQD EKLLLKCHSK TAVGSSDSKQ
TFSPVLKLNA VLIRSVATDK RAFFIICTSK LGPPQIYELV ALTSSDKNTW MELLEEAVRN
ATRHPGAAPM PVHPPPPGPR EPAQQGPTPS RVELDDSDVF HGEPEPEELP GGTGSQQRVQ
GKHQVLLEDP EQEGSAEEEE LGVLPCPSTS LDGENRGIRT RNPIHLAFPG PLFMEGLADS
ALEDVENLRH LILWSLLPGH TMETQAAQEP EDDLTPTPSV ISVTSHPWDP GSPGQAPPGG
EGDNTQLAGL EGERPEQEDM GLCSLEHLPP RTRNSGIWES PELDRNLAED ASSTEAAGGY
KVVRKAEVAG SKVVPALPES GQSEPGPPEV EGGTKATGNC FYVSMPSGPP DSSTDHSEAP
MSPPQPDSLP AGQTEPQPQL QGGNDDPRRP SRSPPSLALR DVGMIFHTIE QLTLKLNRLK
DMELAHRELL KSLGGESSGG TTPVGSFHTE AARWTDGSLS PPAKEPLASD SRNSHELGPC
PEDGSDAPLE DSTADAAASP GP
//
