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ARHGB_HUMAN
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   03-AUG-2022, entry version 198.
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=9; 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; 62.
DR   DIP; DIP-31622N; -.
DR   IntAct; O15085; 55.
DR   MINT; O15085; -.
DR   STRING; 9606.ENSP00000357177; -.
DR   ChEMBL; CHEMBL4523642; -.
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; O15085; -.
DR   PeptideAtlas; O15085; -.
DR   PRIDE; O15085; -.
DR   ProteomicsDB; 48441; -. [O15085-1]
DR   ProteomicsDB; 48442; -. [O15085-2]
DR   Antibodypedia; 1659; 279 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   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; WCEAMKR; -.
DR   OrthoDB; 319635at2759; -.
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; 18 hits in 1080 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 93 other 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 transcription, DNA-templated; 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; cd13391; PH_PRG; 1.
DR   CDD; cd08753; RGS_PDZRhoGEF; 1.
DR   CDD; cd00160; RhoGEF; 1.
DR   Gene3D; 1.10.167.10; -; 1.
DR   Gene3D; 1.20.900.10; -; 1.
DR   Gene3D; 2.30.29.30; -; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR035899; DBL_dom_sf.
DR   InterPro; IPR000219; DH-domain.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR032919; PDZ-RhoGEF.
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; PTHR45872:SF1; 2.
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; 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; 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
 
 
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