Full text data of ARHGDIB
ARHGDIB
(GDIA2, GDID4, RAP1GN1)
[Confidence: low (only semi-automatic identification from reviews)]
Rho GDP-dissociation inhibitor 2; Rho GDI 2 (Ly-GDI; Rho-GDI beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Rho GDP-dissociation inhibitor 2; Rho GDI 2 (Ly-GDI; Rho-GDI beta)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P52566
ID GDIR2_HUMAN Reviewed; 201 AA.
AC P52566; B5BU79;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Rho GDP-dissociation inhibitor 2;
DE Short=Rho GDI 2;
DE AltName: Full=Ly-GDI;
DE AltName: Full=Rho-GDI beta;
GN Name=ARHGDIB; Synonyms=GDIA2, GDID4, RAP1GN1;
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 [MRNA].
RX PubMed=8356058; DOI=10.1073/pnas.90.16.7568;
RA Scherle P., Behrens T., Staudt L.M.;
RT "Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein,
RT is expressed preferentially in lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7568-7572(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8262133; DOI=10.1006/excr.1993.1298;
RA Leffers H., Nielsen M.S., Andersen A.H., Honore B., Madsen P.,
RA Vandekerckhove J., Celis J.E.;
RT "Identification of two human Rho GDP dissociation inhibitor proteins
RT whose overexpression leads to disruption of the actin cytoskeleton.";
RL Exp. Cell Res. 209:165-174(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8434008; DOI=10.1073/pnas.90.4.1479;
RA Lelias J.M., Adra C.N., Wulf G.M., Guillemot J.-C., Caput D., Lim B.;
RT "cDNA cloning of a human mRNA preferentially expressed in
RT hematopoietic cells and with homology to a GDP-dissociation inhibitor
RT for the rho GTP-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1479-1483(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [8]
RP PROTEIN SEQUENCE OF 2-20; 33-46 AND 50-62, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 10-19; 21-25; 51-58; 142-148 AND 150-156.
RX PubMed=2226408; DOI=10.1002/elps.1150110702;
RA Aebersold R., Leavitt J.;
RT "Sequence analysis of proteins separated by polyacrylamide gel
RT electrophoresis: towards an integrated protein database.";
RL Electrophoresis 11:517-527(1990).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND MASS
RP SPECTROMETRY.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-25; LYS-40; LYS-47;
RP LYS-102; LYS-124 AND LYS-175, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP INTERACTION WITH RHOA.
RX PubMed=20400958; DOI=10.1038/ncb2049;
RA Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G.,
RA Brennwald P.J., Burridge K.;
RT "Regulation of Rho GTPase crosstalk, degradation and activity by
RT RhoGDI1.";
RL Nat. Cell Biol. 12:477-483(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH RAC2.
RX PubMed=10655614; DOI=10.1038/72392;
RA Scheffzek K., Stephan I., Jensen O.N., Illenberger D., Gierschik P.;
RT "The Rac-RhoGDI complex and the structural basis for the regulation of
RT Rho proteins by RhoGDI.";
RL Nat. Struct. Biol. 7:122-126(2000).
CC -!- FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho
CC proteins by inhibiting the dissociation of GDP from them, and the
CC subsequent binding of GTP to them.
CC -!- SUBUNIT: Interacts with RHOA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the Rho GDI family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L20688; AAA59539.1; -; mRNA.
DR EMBL; X69549; CAA49280.1; -; mRNA.
DR EMBL; L07916; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF498927; AAM21075.1; -; mRNA.
DR EMBL; AB451315; BAG70129.1; -; mRNA.
DR EMBL; AB451445; BAG70259.1; -; mRNA.
DR EMBL; CH471094; EAW96336.1; -; Genomic_DNA.
DR EMBL; BC009200; AAH09200.1; -; mRNA.
DR PIR; A47742; A47742.
DR RefSeq; NP_001166.3; NM_001175.4.
DR RefSeq; XP_005253424.1; XM_005253367.1.
DR RefSeq; XP_005253425.1; XM_005253368.1.
DR UniGene; Hs.504877; -.
DR PDB; 1DS6; X-ray; 2.35 A; B=23-199.
DR PDBsum; 1DS6; -.
DR ProteinModelPortal; P52566; -.
DR SMR; P52566; 23-199.
DR DIP; DIP-40959N; -.
DR IntAct; P52566; 8.
DR MINT; MINT-1616342; -.
DR STRING; 9606.ENSP00000228945; -.
DR PhosphoSite; P52566; -.
DR DMDM; 1707893; -.
DR OGP; P52566; -.
DR SWISS-2DPAGE; P52566; -.
DR PaxDb; P52566; -.
DR PRIDE; P52566; -.
DR DNASU; 397; -.
DR Ensembl; ENST00000228945; ENSP00000228945; ENSG00000111348.
DR Ensembl; ENST00000541546; ENSP00000440560; ENSG00000111348.
DR Ensembl; ENST00000541644; ENSP00000444860; ENSG00000111348.
DR GeneID; 397; -.
DR KEGG; hsa:397; -.
DR UCSC; uc001rcq.1; human.
DR CTD; 397; -.
DR GeneCards; GC12M015094; -.
DR H-InvDB; HIX0036989; -.
DR HGNC; HGNC:679; ARHGDIB.
DR HPA; CAB018584; -.
DR MIM; 602843; gene.
DR neXtProt; NX_P52566; -.
DR PharmGKB; PA24964; -.
DR eggNOG; NOG253438; -.
DR HOGENOM; HOG000175765; -.
DR HOVERGEN; HBG000206; -.
DR InParanoid; P52566; -.
DR KO; K12462; -.
DR OMA; EPHLEED; -.
DR OrthoDB; EOG72JWH9; -.
DR PhylomeDB; P52566; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; P52566; -.
DR GeneWiki; ARHGDIB; -.
DR GenomeRNAi; 397; -.
DR NextBio; 1665; -.
DR PMAP-CutDB; P52566; -.
DR PRO; PR:P52566; -.
DR ArrayExpress; P52566; -.
DR Bgee; P52566; -.
DR CleanEx; HS_ARHGDIB; -.
DR Genevestigator; P52566; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; TAS:ProtInc.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR GO; GO:0007162; P:negative regulation of cell adhesion; TAS:ProtInc.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR Gene3D; 2.70.50.30; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000406; Rho_GDI.
DR InterPro; IPR024792; RhoGDI_domain.
DR PANTHER; PTHR10980; PTHR10980; 1.
DR Pfam; PF02115; Rho_GDI; 1.
DR PRINTS; PR00492; RHOGDI.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 201 Rho GDP-dissociation inhibitor 2.
FT /FTId=PRO_0000219016.
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 21 21 N6-acetyllysine.
FT MOD_RES 24 24 Phosphotyrosine.
FT MOD_RES 25 25 N6-acetyllysine.
FT MOD_RES 40 40 N6-acetyllysine.
FT MOD_RES 47 47 N6-acetyllysine.
FT MOD_RES 102 102 N6-acetyllysine.
FT MOD_RES 124 124 N6-acetyllysine.
FT MOD_RES 145 145 Phosphoserine.
FT MOD_RES 175 175 N6-acetyllysine.
FT CONFLICT 153 153 Y -> V (in Ref. 9; AA sequence).
FT CONFLICT 169 170 RG -> QD (in Ref. 3; L07916).
FT HELIX 32 37
FT TURN 38 41
FT HELIX 43 52
FT STRAND 62 64
FT STRAND 69 75
FT STRAND 84 86
FT HELIX 91 96
FT STRAND 98 102
FT STRAND 106 113
FT STRAND 120 131
FT STRAND 134 146
FT STRAND 153 156
FT TURN 166 168
FT STRAND 170 179
FT STRAND 187 198
SQ SEQUENCE 201 AA; 22988 MW; F1E840134F643E5F CRC64;
MTEKAPEPHV EEDDDDELDS KLNYKPPPQK SLKELQEMDK DDESLIKYKK TLLGDGPVVT
DPKAPNVVVT RLTLVCESAP GPITMDLTGD LEALKKETIV LKEGSEYRVK IHFKVNRDIV
SGLKYVQHTY RTGVKVDKAT FMVGSYGPRP EEYEFLTPVE EAPKGMLARG TYHNKSFFTD
DDKQDHLSWE WNLSIKKEWT E
//
ID GDIR2_HUMAN Reviewed; 201 AA.
AC P52566; B5BU79;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 132.
DE RecName: Full=Rho GDP-dissociation inhibitor 2;
DE Short=Rho GDI 2;
DE AltName: Full=Ly-GDI;
DE AltName: Full=Rho-GDI beta;
GN Name=ARHGDIB; Synonyms=GDIA2, GDID4, RAP1GN1;
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 [MRNA].
RX PubMed=8356058; DOI=10.1073/pnas.90.16.7568;
RA Scherle P., Behrens T., Staudt L.M.;
RT "Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein,
RT is expressed preferentially in lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:7568-7572(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8262133; DOI=10.1006/excr.1993.1298;
RA Leffers H., Nielsen M.S., Andersen A.H., Honore B., Madsen P.,
RA Vandekerckhove J., Celis J.E.;
RT "Identification of two human Rho GDP dissociation inhibitor proteins
RT whose overexpression leads to disruption of the actin cytoskeleton.";
RL Exp. Cell Res. 209:165-174(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8434008; DOI=10.1073/pnas.90.4.1479;
RA Lelias J.M., Adra C.N., Wulf G.M., Guillemot J.-C., Caput D., Lim B.;
RT "cDNA cloning of a human mRNA preferentially expressed in
RT hematopoietic cells and with homology to a GDP-dissociation inhibitor
RT for the rho GTP-binding proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:1479-1483(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RA Puhl H.L. III, Ikeda S.R., Aronstam R.S.;
RT "cDNA clones of human proteins involved in signal transduction
RT sequenced by the Guthrie cDNA resource center (www.cdna.org).";
RL Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lymph;
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 [8]
RP PROTEIN SEQUENCE OF 2-20; 33-46 AND 50-62, CLEAVAGE OF INITIATOR
RP METHIONINE, ACETYLATION AT THR-2, AND MASS SPECTROMETRY.
RC TISSUE=T-cell;
RA Bienvenut W.V., Kanor S., Tissot J.-D., Quadroni M.;
RL Submitted (MAY-2006) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 10-19; 21-25; 51-58; 142-148 AND 150-156.
RX PubMed=2226408; DOI=10.1002/elps.1150110702;
RA Aebersold R., Leavitt J.;
RT "Sequence analysis of proteins separated by polyacrylamide gel
RT electrophoresis: towards an integrated protein database.";
RL Electrophoresis 11:517-527(1990).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, AND MASS
RP SPECTROMETRY.
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-145, AND MASS
RP SPECTROMETRY.
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 [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-21; LYS-25; LYS-40; LYS-47;
RP LYS-102; LYS-124 AND LYS-175, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP INTERACTION WITH RHOA.
RX PubMed=20400958; DOI=10.1038/ncb2049;
RA Boulter E., Garcia-Mata R., Guilluy C., Dubash A., Rossi G.,
RA Brennwald P.J., Burridge K.;
RT "Regulation of Rho GTPase crosstalk, degradation and activity by
RT RhoGDI1.";
RL Nat. Cell Biol. 12:477-483(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF COMPLEX WITH RAC2.
RX PubMed=10655614; DOI=10.1038/72392;
RA Scheffzek K., Stephan I., Jensen O.N., Illenberger D., Gierschik P.;
RT "The Rac-RhoGDI complex and the structural basis for the regulation of
RT Rho proteins by RhoGDI.";
RL Nat. Struct. Biol. 7:122-126(2000).
CC -!- FUNCTION: Regulates the GDP/GTP exchange reaction of the Rho
CC proteins by inhibiting the dissociation of GDP from them, and the
CC subsequent binding of GTP to them.
CC -!- SUBUNIT: Interacts with RHOA.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the Rho GDI family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; L20688; AAA59539.1; -; mRNA.
DR EMBL; X69549; CAA49280.1; -; mRNA.
DR EMBL; L07916; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF498927; AAM21075.1; -; mRNA.
DR EMBL; AB451315; BAG70129.1; -; mRNA.
DR EMBL; AB451445; BAG70259.1; -; mRNA.
DR EMBL; CH471094; EAW96336.1; -; Genomic_DNA.
DR EMBL; BC009200; AAH09200.1; -; mRNA.
DR PIR; A47742; A47742.
DR RefSeq; NP_001166.3; NM_001175.4.
DR RefSeq; XP_005253424.1; XM_005253367.1.
DR RefSeq; XP_005253425.1; XM_005253368.1.
DR UniGene; Hs.504877; -.
DR PDB; 1DS6; X-ray; 2.35 A; B=23-199.
DR PDBsum; 1DS6; -.
DR ProteinModelPortal; P52566; -.
DR SMR; P52566; 23-199.
DR DIP; DIP-40959N; -.
DR IntAct; P52566; 8.
DR MINT; MINT-1616342; -.
DR STRING; 9606.ENSP00000228945; -.
DR PhosphoSite; P52566; -.
DR DMDM; 1707893; -.
DR OGP; P52566; -.
DR SWISS-2DPAGE; P52566; -.
DR PaxDb; P52566; -.
DR PRIDE; P52566; -.
DR DNASU; 397; -.
DR Ensembl; ENST00000228945; ENSP00000228945; ENSG00000111348.
DR Ensembl; ENST00000541546; ENSP00000440560; ENSG00000111348.
DR Ensembl; ENST00000541644; ENSP00000444860; ENSG00000111348.
DR GeneID; 397; -.
DR KEGG; hsa:397; -.
DR UCSC; uc001rcq.1; human.
DR CTD; 397; -.
DR GeneCards; GC12M015094; -.
DR H-InvDB; HIX0036989; -.
DR HGNC; HGNC:679; ARHGDIB.
DR HPA; CAB018584; -.
DR MIM; 602843; gene.
DR neXtProt; NX_P52566; -.
DR PharmGKB; PA24964; -.
DR eggNOG; NOG253438; -.
DR HOGENOM; HOG000175765; -.
DR HOVERGEN; HBG000206; -.
DR InParanoid; P52566; -.
DR KO; K12462; -.
DR OMA; EPHLEED; -.
DR OrthoDB; EOG72JWH9; -.
DR PhylomeDB; P52566; -.
DR Reactome; REACT_111102; Signal Transduction.
DR EvolutionaryTrace; P52566; -.
DR GeneWiki; ARHGDIB; -.
DR GenomeRNAi; 397; -.
DR NextBio; 1665; -.
DR PMAP-CutDB; P52566; -.
DR PRO; PR:P52566; -.
DR ArrayExpress; P52566; -.
DR Bgee; P52566; -.
DR CleanEx; HS_ARHGDIB; -.
DR Genevestigator; P52566; -.
DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; TAS:ProtInc.
DR GO; GO:0005856; C:cytoskeleton; TAS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; TAS:ProtInc.
DR GO; GO:0030036; P:actin cytoskeleton organization; TAS:ProtInc.
DR GO; GO:0006928; P:cellular component movement; TAS:UniProtKB.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0007275; P:multicellular organismal development; TAS:ProtInc.
DR GO; GO:0007162; P:negative regulation of cell adhesion; TAS:ProtInc.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007266; P:Rho protein signal transduction; TAS:ProtInc.
DR Gene3D; 2.70.50.30; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000406; Rho_GDI.
DR InterPro; IPR024792; RhoGDI_domain.
DR PANTHER; PTHR10980; PTHR10980; 1.
DR Pfam; PF02115; Rho_GDI; 1.
DR PRINTS; PR00492; RHOGDI.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Complete proteome; Cytoplasm;
KW Direct protein sequencing; GTPase activation; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 201 Rho GDP-dissociation inhibitor 2.
FT /FTId=PRO_0000219016.
FT MOD_RES 2 2 N-acetylthreonine.
FT MOD_RES 21 21 N6-acetyllysine.
FT MOD_RES 24 24 Phosphotyrosine.
FT MOD_RES 25 25 N6-acetyllysine.
FT MOD_RES 40 40 N6-acetyllysine.
FT MOD_RES 47 47 N6-acetyllysine.
FT MOD_RES 102 102 N6-acetyllysine.
FT MOD_RES 124 124 N6-acetyllysine.
FT MOD_RES 145 145 Phosphoserine.
FT MOD_RES 175 175 N6-acetyllysine.
FT CONFLICT 153 153 Y -> V (in Ref. 9; AA sequence).
FT CONFLICT 169 170 RG -> QD (in Ref. 3; L07916).
FT HELIX 32 37
FT TURN 38 41
FT HELIX 43 52
FT STRAND 62 64
FT STRAND 69 75
FT STRAND 84 86
FT HELIX 91 96
FT STRAND 98 102
FT STRAND 106 113
FT STRAND 120 131
FT STRAND 134 146
FT STRAND 153 156
FT TURN 166 168
FT STRAND 170 179
FT STRAND 187 198
SQ SEQUENCE 201 AA; 22988 MW; F1E840134F643E5F CRC64;
MTEKAPEPHV EEDDDDELDS KLNYKPPPQK SLKELQEMDK DDESLIKYKK TLLGDGPVVT
DPKAPNVVVT RLTLVCESAP GPITMDLTGD LEALKKETIV LKEGSEYRVK IHFKVNRDIV
SGLKYVQHTY RTGVKVDKAT FMVGSYGPRP EEYEFLTPVE EAPKGMLARG TYHNKSFFTD
DDKQDHLSWE WNLSIKKEWT E
//
MIM
602843
*RECORD*
*FIELD* NO
602843
*FIELD* TI
*602843 RHO GDP-DISSOCIATION INHIBITOR BETA; ARHGDIB
;;GDP-DISSOCIATION INHIBITOR D4; GDID4; D4;;
read moreLYGDI
*FIELD* TX
DESCRIPTION
Members of the Rho (or ARH) protein family (see 165390) and other
Ras-related small GTP-binding proteins (see 179520) are involved in
diverse cellular events, including cell signaling, proliferation,
cytoskeletal organization, and secretion. The GTP-binding proteins are
active only in the GTP-bound state. At least 3 classes of proteins
tightly regulate cycling between the GTP-bound and GDP-bound states:
GTPase-activating proteins (GAPs), guanine nucleotide-releasing factors
(GRFs), and GDP-dissociation inhibitors (GDIs). The GDIs, including
ARHGDIB, decrease the rate of GDP dissociation from Ras-like GTPases
(summary by Scherle et al., 1993).
CLONING
By using a subtractive hybridization approach, Scherle et al. (1993)
identified a B-cell cDNA encoding ARHGDIB, which shares homology to
RhoGDI (ARHGDIA; 601925). They designated the gene LyGDI for
'lymphoid-specific GDI.' Northern blot analysis revealed that LyGDI is
expressed as a 1.4-kb transcript only in hematopoietic tissues.
Antibodies against LyGDI recognized a 27-kD protein on Western blots of
B- and T-cell line lysates. Scherle et al. (1993) found that LyGDI bound
RhoA and, in vitro, inhibited GDP dissociation from RhoA. Stimulation of
T lymphocytes with phorbol ester led to phosphorylation of LyGDI.
Independently, Lelias et al. (1993) cloned the LyGDI gene from human and
from mouse, and designated it GDP-dissociation inhibitor D4. The
sequence of the predicted 201-amino acid human protein was 67% identical
to that of bovine RhoGDI. Mouse and human D4 shared 89% amino acid
sequence identity.
Leffers et al. (1993) identified 3 human proteins related to bovine
RhoGDI and found that they corresponded to 3 proteins in the
keratinocyte 2-dimensional-gel protein database, called IEF (for
'isoelectric focusing') 8120, IEF8118, and IEF1120. By screening an
embryonic lung fibroblast library with an oligonucleotide based on the
protein sequence of IEF8120, Leffers et al. (1993) isolated cDNAs
encoding ARHGDIB. They reported that ARHGDIB had a pI of 4.79. Northern
blot analysis revealed that ARHGDIB was expressed abundantly in lung,
and at lower levels in several other tissues. Overexpression of ARHGDIB
in mammalian cells caused them to 'round up' and disrupted the actin
cytoskeleton, mimicking the phenotypic changes associated with
inactivation of Rho proteins.
MAPPING
By fluorescence in situ hybridization, Adra et al. (1994) mapped the
ARHGDIB gene to chromosome 12p12.3.
*FIELD* RF
1. Adra, C. N.; Kobayashi, H.; Rowley, J. D.; Lim, B.: Assignment
of the human GDID4 gene, a GDP/GTP-exchange regulator, to chromosome
12p12.3. Genomics 24: 188-190, 1994.
2. Leffers, H.; Nielsen, M. S.; Andersen, A. H.; Honore, B.; Madsen,
P.; Vandekerckhove, J.; Celis, J. E.: Identification of two human
Rho GDP dissociation inhibitor proteins whose overexpression leads
to disruption of the actin cytoskeleton. Exp. Cell Res. 209: 165-174,
1993.
3. Lelias, J.-M.; Adra, C. N.; Wulf, G. M.; Guillemot, J.-C.; Khagad,
M.; Caput, D.; Lim, B.: cDNA cloning of a human mRNA preferentially
expressed in hematopoietic cells and with homology to a GDP-dissociation
inhibitor for the rho GTP-binding proteins. Proc. Nat. Acad. Sci. 90:
1479-1483, 1993.
4. Scherle, P.; Behrens, T.; Staudt, L. M.: Ly-GDI, a GDP-dissociation
inhibitor of the RhoA GTP-binding protein, is expressed preferentially
in lymphocytes. Proc. Nat. Acad. Sci. 90: 7568-7572, 1993.
*FIELD* CD
Rebekah S. Rasooly: 7/13/1998
*FIELD* ED
joanna: 11/30/2010
wwang: 11/23/2010
tkritzer: 7/13/2004
alopez: 7/14/1998
*RECORD*
*FIELD* NO
602843
*FIELD* TI
*602843 RHO GDP-DISSOCIATION INHIBITOR BETA; ARHGDIB
;;GDP-DISSOCIATION INHIBITOR D4; GDID4; D4;;
read moreLYGDI
*FIELD* TX
DESCRIPTION
Members of the Rho (or ARH) protein family (see 165390) and other
Ras-related small GTP-binding proteins (see 179520) are involved in
diverse cellular events, including cell signaling, proliferation,
cytoskeletal organization, and secretion. The GTP-binding proteins are
active only in the GTP-bound state. At least 3 classes of proteins
tightly regulate cycling between the GTP-bound and GDP-bound states:
GTPase-activating proteins (GAPs), guanine nucleotide-releasing factors
(GRFs), and GDP-dissociation inhibitors (GDIs). The GDIs, including
ARHGDIB, decrease the rate of GDP dissociation from Ras-like GTPases
(summary by Scherle et al., 1993).
CLONING
By using a subtractive hybridization approach, Scherle et al. (1993)
identified a B-cell cDNA encoding ARHGDIB, which shares homology to
RhoGDI (ARHGDIA; 601925). They designated the gene LyGDI for
'lymphoid-specific GDI.' Northern blot analysis revealed that LyGDI is
expressed as a 1.4-kb transcript only in hematopoietic tissues.
Antibodies against LyGDI recognized a 27-kD protein on Western blots of
B- and T-cell line lysates. Scherle et al. (1993) found that LyGDI bound
RhoA and, in vitro, inhibited GDP dissociation from RhoA. Stimulation of
T lymphocytes with phorbol ester led to phosphorylation of LyGDI.
Independently, Lelias et al. (1993) cloned the LyGDI gene from human and
from mouse, and designated it GDP-dissociation inhibitor D4. The
sequence of the predicted 201-amino acid human protein was 67% identical
to that of bovine RhoGDI. Mouse and human D4 shared 89% amino acid
sequence identity.
Leffers et al. (1993) identified 3 human proteins related to bovine
RhoGDI and found that they corresponded to 3 proteins in the
keratinocyte 2-dimensional-gel protein database, called IEF (for
'isoelectric focusing') 8120, IEF8118, and IEF1120. By screening an
embryonic lung fibroblast library with an oligonucleotide based on the
protein sequence of IEF8120, Leffers et al. (1993) isolated cDNAs
encoding ARHGDIB. They reported that ARHGDIB had a pI of 4.79. Northern
blot analysis revealed that ARHGDIB was expressed abundantly in lung,
and at lower levels in several other tissues. Overexpression of ARHGDIB
in mammalian cells caused them to 'round up' and disrupted the actin
cytoskeleton, mimicking the phenotypic changes associated with
inactivation of Rho proteins.
MAPPING
By fluorescence in situ hybridization, Adra et al. (1994) mapped the
ARHGDIB gene to chromosome 12p12.3.
*FIELD* RF
1. Adra, C. N.; Kobayashi, H.; Rowley, J. D.; Lim, B.: Assignment
of the human GDID4 gene, a GDP/GTP-exchange regulator, to chromosome
12p12.3. Genomics 24: 188-190, 1994.
2. Leffers, H.; Nielsen, M. S.; Andersen, A. H.; Honore, B.; Madsen,
P.; Vandekerckhove, J.; Celis, J. E.: Identification of two human
Rho GDP dissociation inhibitor proteins whose overexpression leads
to disruption of the actin cytoskeleton. Exp. Cell Res. 209: 165-174,
1993.
3. Lelias, J.-M.; Adra, C. N.; Wulf, G. M.; Guillemot, J.-C.; Khagad,
M.; Caput, D.; Lim, B.: cDNA cloning of a human mRNA preferentially
expressed in hematopoietic cells and with homology to a GDP-dissociation
inhibitor for the rho GTP-binding proteins. Proc. Nat. Acad. Sci. 90:
1479-1483, 1993.
4. Scherle, P.; Behrens, T.; Staudt, L. M.: Ly-GDI, a GDP-dissociation
inhibitor of the RhoA GTP-binding protein, is expressed preferentially
in lymphocytes. Proc. Nat. Acad. Sci. 90: 7568-7572, 1993.
*FIELD* CD
Rebekah S. Rasooly: 7/13/1998
*FIELD* ED
joanna: 11/30/2010
wwang: 11/23/2010
tkritzer: 7/13/2004
alopez: 7/14/1998