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 09-DEC-2015, entry version 150. 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; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; 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. RT The complete sequences of 100 new cDNA clones from brain which can RT code for 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., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA 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., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA 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., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA 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., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA 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 RT project: 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 RT links 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 RT factors 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 RT neurite retraction. Possible role of a proline-rich motif of KIAA0380 RT in 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., RA Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in RT signaling 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 RP 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 RP BY 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 RT motility 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 RP 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., RA Mann M.; RT "Quantitative phosphoproteomics reveals widespread full RT phosphorylation 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- RT induced neurite outgrowth."; RL J. Cell Biol. 193:985-994(2011). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251, AND IDENTIFICATION RP 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., RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., RA Blagoev B.; RT "System-wide temporal characterization of the proteome and RT phosphoproteome of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [17] 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., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] 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., RA Derewenda Z.S.; RT "Structure of the RGS-like domain from PDZ-RhoGEF: linking RT heterotrimeric g protein-coupled signaling to Rho GTPases."; RL Structure 9:559-569(2001). RN [19] 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 CC guanine nucleotide-binding alpha-12 (GNA12) and alpha-13 (GNA13). CC Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase CC and may act as GTPase-activating protein (GAP) for GNA12 and CC GNA13. Involved in neurotrophin-induced neurite outgrowth. CC {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- CC terminus). {ECO:0000250, ECO:0000269|PubMed:10026210, CC ECO:0000269|PubMed:10526156, ECO:0000269|PubMed:12183458, CC ECO:0000269|PubMed:12372594, ECO:0000269|PubMed:20844236}. CC -!- INTERACTION: CC P46108:CRK; NbExp=2; IntAct=EBI-311099, EBI-886; CC Q8BPM0:Daam1 (xeno); NbExp=3; IntAct=EBI-6169263, EBI-772938; CC Q7DB74:ECs4564 (xeno); NbExp=4; IntAct=EBI-311099, EBI-7864788; CC P16333:NCK1; NbExp=3; IntAct=EBI-311099, EBI-389883; CC P61586:RHOA; NbExp=6; IntAct=EBI-311099, EBI-446668; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10900204}. CC Membrane {ECO:0000269|PubMed:10900204}. Note=Translocated to the CC membrane upon 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 Note=No experimental confirmation available.; 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 CC and/or MAPK14). CC -!- PTM: Ubiquitinated by the BCR(KLHL20) E3 ubiquitin ligase complex CC when previously phosphorylated by MAP kinase p38 (MAPK11, MAPK12, CC MAPK13 and/or MAPK14), leading to its degradation, thereby CC restricting RhoA activity and facilitating growth cone spreading CC and neurite outgrowth. {ECO:0000269|PubMed:21670212}. CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain. CC {ECO:0000255|PROSITE-ProRule:PRU00062}. CC -!- SIMILARITY: Contains 1 PDZ (DHR) domain. {ECO:0000255|PROSITE- CC ProRule:PRU00143}. CC -!- SIMILARITY: Contains 1 PH domain. {ECO:0000255|PROSITE- CC ProRule:PRU00145}. CC -!- SIMILARITY: Contains 1 RGSL (RGS-like) domain. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA20834.2; Type=Erroneous initiation; 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; AB002378; BAA20834.2; ALT_INIT; mRNA. DR EMBL; AL356104; CAH72940.1; -; Genomic_DNA. DR EMBL; AL157713; CAH72940.1; JOINED; Genomic_DNA. DR EMBL; AL157713; CAH70127.1; -; Genomic_DNA. DR EMBL; AL356104; CAH70127.1; JOINED; Genomic_DNA. DR EMBL; AL157713; CAH70128.1; -; Genomic_DNA. DR EMBL; AL356104; CAH70128.1; JOINED; Genomic_DNA. DR EMBL; AL356104; CAH72939.1; -; Genomic_DNA. DR EMBL; AL157713; CAH72939.1; JOINED; 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 UniGene; Hs.516954; -. 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 PDBsum; 1HTJ; -. DR PDBsum; 1XCG; -. DR PDBsum; 2DLS; -. DR PDBsum; 3KZ1; -. DR PDBsum; 3T06; -. DR ProteinModelPortal; O15085; -. DR SMR; O15085; 37-120, 306-487, 714-1081. DR BioGrid; 115164; 17. DR DIP; DIP-31622N; -. DR IntAct; O15085; 23. DR MINT; MINT-1897198; -. DR STRING; 9606.ENSP00000357177; -. DR PhosphoSite; O15085; -. DR BioMuta; ARHGEF11; -. DR MaxQB; O15085; -. DR PaxDb; O15085; -. DR PRIDE; O15085; -. DR Ensembl; ENST00000361409; ENSP00000354644; ENSG00000132694. [O15085-1] DR Ensembl; ENST00000368194; ENSP00000357177; ENSG00000132694. [O15085-2] DR GeneID; 9826; -. DR KEGG; hsa:9826; -. DR UCSC; uc001fqn.3; human. [O15085-2] DR UCSC; uc001fqo.3; human. [O15085-1] DR CTD; 9826; -. DR GeneCards; ARHGEF11; -. DR HGNC; HGNC:14580; ARHGEF11. DR HPA; HPA011026; -. DR HPA; HPA012037; -. DR HPA; HPA014658; -. DR MIM; 605708; gene. DR neXtProt; NX_O15085; -. DR PharmGKB; PA24968; -. DR eggNOG; KOG3520; Eukaryota. DR eggNOG; COG5422; LUCA. DR GeneTree; ENSGT00760000119193; -. DR HOGENOM; HOG000034045; -. DR HOVERGEN; HBG101340; -. DR InParanoid; O15085; -. DR KO; K12331; -. DR OMA; TGNCFYV; -. DR OrthoDB; EOG7GJ6CF; -. DR PhylomeDB; O15085; -. DR TreeFam; TF106495; -. DR Reactome; R-HSA-193648; NRAGE signals death through JNK. DR Reactome; R-HSA-194840; Rho GTPase cycle. 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 ChiTaRS; ARHGEF11; human. DR EvolutionaryTrace; O15085; -. DR GeneWiki; ARHGEF11; -. DR GenomeRNAi; 9826; -. DR NextBio; 37012; -. DR PRO; PR:O15085; -. DR Proteomes; UP000005640; Chromosome 1. DR Bgee; O15085; -. DR CleanEx; HS_ARHGEF11; -. DR Genevisible; O15085; HS. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005622; C:intracellular; IC:UniProtKB. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. 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:0005089; F:Rho guanyl-nucleotide exchange factor activity; TAS:UniProtKB. DR GO; GO:0030036; P:actin cytoskeleton organization; NAS:UniProtKB. DR GO; GO:0097190; P:apoptotic signaling pathway; TAS:Reactome. DR GO; GO:0007411; P:axon guidance; TAS:Reactome. DR GO; GO:0000910; P:cytokinesis; NAS:UniProtKB. DR GO; GO:0030010; P:establishment of cell polarity; NAS:UniProtKB. DR GO; GO:0007186; P:G-protein coupled receptor signaling pathway; TAS:UniProtKB. DR GO; GO:0006928; P:movement of cell or subcellular component; NAS:UniProtKB. DR GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome. DR GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome. DR GO; GO:0043547; P:positive regulation of GTPase activity; TAS:GOC. DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB. DR GO; GO:0001558; P:regulation of cell growth; NAS:UniProtKB. DR GO; GO:0035023; P:regulation of Rho protein signal transduction; IEA:InterPro. 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:0007264; P:small GTPase mediated signal transduction; TAS:Reactome. DR GO; GO:0006941; P:striated muscle contraction; NAS:UniProtKB. DR Gene3D; 1.20.900.10; -; 1. DR Gene3D; 2.30.29.30; -; 1. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR000219; DH-domain. DR InterPro; IPR001478; PDZ. DR InterPro; IPR011993; PH/PTB_dom. DR InterPro; IPR001849; PH_domain. DR InterPro; IPR016137; RGS. DR InterPro; IPR015212; RGS-like_dom. DR Pfam; PF00595; PDZ; 1. DR Pfam; PF16652; PH_13; 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; SSF48065; 1. DR SUPFAM; SSF48097; SSF48097; 1. DR SUPFAM; SSF50156; SSF50156; 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; Complete proteome; KW Cytoplasm; GTPase activation; Guanine-nucleotide releasing factor; KW Membrane; Phosphoprotein; Polymorphism; Reference proteome; KW Ubl conjugation. FT CHAIN 1 1522 Rho guanine nucleotide exchange factor FT 11. FT /FTId=PRO_0000080928. FT DOMAIN 47 126 PDZ. {ECO:0000255|PROSITE- FT ProRule:PRU00143}. FT DOMAIN 306 486 RGSL. {ECO:0000255|PROSITE- FT ProRule:PRU00171}. FT DOMAIN 734 923 DH. {ECO:0000255|PROSITE- FT ProRule:PRU00062}. FT DOMAIN 965 1079 PH. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT COILED 444 470 {ECO:0000255}. FT COMPBIAS 1094 1099 Poly-Pro. FT MOD_RES 14 14 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9ES67}. FT MOD_RES 35 35 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9ES67}. FT MOD_RES 245 245 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:20068231}. FT MOD_RES 251 251 Phosphoserine. FT {ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:21406692}. FT MOD_RES 254 254 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 255 255 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9ES67}. FT MOD_RES 271 271 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9ES67}. FT MOD_RES 663 663 Phosphoserine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 668 668 Phosphothreonine. FT {ECO:0000244|PubMed:17081983, FT ECO:0000244|PubMed:18669648, FT ECO:0000244|PubMed:19690332, FT ECO:0000244|PubMed:24275569}. FT MOD_RES 672 672 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1155 1155 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1300 1300 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1457 1457 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1458 1458 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1475 1475 Phosphothreonine. FT {ECO:0000244|PubMed:18669648}. FT MOD_RES 1480 1480 Phosphoserine. FT {ECO:0000244|PubMed:18669648}. FT VAR_SEQ 194 194 Q -> QRICEVYSRNPASLLEEQIEGARRRVTQLQLKIQQE FT TGGSV (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_042003. FT VARIANT 1416 1416 S -> G (in dbSNP:rs868188). FT /FTId=VAR_061795. FT VARIANT 1427 1427 H -> R (in dbSNP:rs945508). FT {ECO:0000269|Ref.3}. FT /FTId=VAR_024285. FT STRAND 45 51 {ECO:0000244|PDB:2DLS}. FT STRAND 53 56 {ECO:0000244|PDB:2DLS}. FT STRAND 59 62 {ECO:0000244|PDB:2DLS}. FT STRAND 64 66 {ECO:0000244|PDB:2DLS}. FT STRAND 68 72 {ECO:0000244|PDB:2DLS}. FT STRAND 74 76 {ECO:0000244|PDB:2DLS}. FT TURN 77 82 {ECO:0000244|PDB:2DLS}. FT STRAND 88 92 {ECO:0000244|PDB:2DLS}. FT STRAND 98 100 {ECO:0000244|PDB:2DLS}. FT HELIX 102 109 {ECO:0000244|PDB:2DLS}. FT STRAND 111 120 {ECO:0000244|PDB:2DLS}. FT HELIX 307 312 {ECO:0000244|PDB:1HTJ}. FT HELIX 314 319 {ECO:0000244|PDB:1HTJ}. FT HELIX 321 334 {ECO:0000244|PDB:1HTJ}. FT HELIX 338 349 {ECO:0000244|PDB:1HTJ}. FT HELIX 356 368 {ECO:0000244|PDB:1HTJ}. FT HELIX 381 392 {ECO:0000244|PDB:1HTJ}. FT HELIX 398 424 {ECO:0000244|PDB:1HTJ}. FT HELIX 428 431 {ECO:0000244|PDB:1HTJ}. FT TURN 432 434 {ECO:0000244|PDB:1HTJ}. FT HELIX 435 438 {ECO:0000244|PDB:1HTJ}. FT HELIX 443 462 {ECO:0000244|PDB:1HTJ}. FT HELIX 466 482 {ECO:0000244|PDB:1HTJ}. FT TURN 716 718 {ECO:0000244|PDB:1XCG}. FT STRAND 719 724 {ECO:0000244|PDB:1XCG}. FT HELIX 725 727 {ECO:0000244|PDB:1XCG}. FT HELIX 730 759 {ECO:0000244|PDB:1XCG}. FT HELIX 761 766 {ECO:0000244|PDB:1XCG}. FT HELIX 772 778 {ECO:0000244|PDB:1XCG}. FT STRAND 779 781 {ECO:0000244|PDB:1XCG}. FT HELIX 782 801 {ECO:0000244|PDB:1XCG}. FT HELIX 810 817 {ECO:0000244|PDB:1XCG}. FT HELIX 819 833 {ECO:0000244|PDB:1XCG}. FT HELIX 836 849 {ECO:0000244|PDB:1XCG}. FT HELIX 851 861 {ECO:0000244|PDB:1XCG}. FT HELIX 864 866 {ECO:0000244|PDB:1XCG}. FT HELIX 871 874 {ECO:0000244|PDB:1XCG}. FT HELIX 877 894 {ECO:0000244|PDB:1XCG}. FT HELIX 901 939 {ECO:0000244|PDB:1XCG}. FT TURN 943 945 {ECO:0000244|PDB:1XCG}. FT TURN 951 953 {ECO:0000244|PDB:1XCG}. FT HELIX 954 958 {ECO:0000244|PDB:1XCG}. FT HELIX 961 963 {ECO:0000244|PDB:1XCG}. FT STRAND 966 974 {ECO:0000244|PDB:1XCG}. FT STRAND 977 979 {ECO:0000244|PDB:1XCG}. FT STRAND 983 998 {ECO:0000244|PDB:1XCG}. FT STRAND 1024 1027 {ECO:0000244|PDB:1XCG}. FT HELIX 1028 1030 {ECO:0000244|PDB:1XCG}. FT STRAND 1031 1035 {ECO:0000244|PDB:1XCG}. FT STRAND 1040 1047 {ECO:0000244|PDB:1XCG}. FT STRAND 1050 1052 {ECO:0000244|PDB:1XCG}. FT STRAND 1056 1060 {ECO:0000244|PDB:1XCG}. FT HELIX 1064 1080 {ECO:0000244|PDB:1XCG}. 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 //