GDIB_HUMAN
ID GDIB_HUMAN Reviewed; 445 AA.
AC P50395; O43928; Q5SX88; Q9UQM6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 27-APR-2001, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Rab GDP dissociation inhibitor beta;
DE Short=Rab GDI beta;
DE AltName: Full=Guanosine diphosphate dissociation inhibitor 2;
DE Short=GDI-2;
GN Name=GDI2; Synonyms=RABGDIB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Asada M., Kaibuchi K., Takai Y.;
RL Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
RX PubMed=9434952; DOI=10.1007/s003359900685;
RA Sedlacek Z., Munstermann E., Mincheva A., Lichter P., Poutska A.;
RT "The human rab GDI beta gene with long retroposon-rich introns maps to
RT 10p15 and its pseudogene to 7p11-p13.";
RL Mamm. Genome 9:78-80(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 81-439 (ISOFORM 1).
RC TISSUE=Pancreas;
RX PubMed=10996854;
RX DOI=10.1002/1097-4644(20001215)79:4<628::aid-jcb120>3.0.co;2-t;
RA Caillol N., Pasqualini E., Lloubes R., Lombardo D.;
RT "Impairment of bile salt-dependent lipase secretion in human pancreatic
RT tumoral SOJ-6 cells.";
RL J. Cell. Biochem. 79:628-647(2000).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=7543319; DOI=10.1093/hmg/4.4.701;
RA Bachner D., Sedlacek Z., Korn B., Hameister H., Poustka A.;
RT "Expression patterns of two human genes coding for different rab GDP-
RT dissociation inhibitors (GDIs), extremely conserved proteins involved in
RT cellular transport.";
RL Hum. Mol. Genet. 4:701-708(1995).
RN [9]
RP INTERACTION WITH RHOH.
RX PubMed=11809807; DOI=10.1128/mcb.22.4.1158-1171.2002;
RA Li X., Bu X., Lu B., Avraham H., Flavell R.A., Lim B.;
RT "The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient
RT and modulates activities of other Rho GTPases by an inhibitory function.";
RL Mol. Cell. Biol. 22:1158-1171(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-269, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, 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 [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., Buerckstuemmer T.,
RA 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND IDENTIFICATION BY
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-382, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP FUNCTION, AND INTERACTION WITH DZIP1 AND RAB8A.
RX PubMed=25860027; DOI=10.1371/journal.pbio.1002129;
RA Zhang B., Zhang T., Wang G., Wang G., Chi W., Jiang Q., Zhang C.;
RT "GSK3beta-Dzip1-Rab8 cascade regulates ciliogenesis after mitosis.";
RL PLoS Biol. 13:e1002129-e1002129(2015).
RN [18]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [19]
RP INTERACTION WITH RAB8A; RAB10 AND RAB12.
RX PubMed=26824392; DOI=10.7554/elife.12813;
RA Steger M., Tonelli F., Ito G., Davies P., Trost M., Vetter M., Wachter S.,
RA Lorentzen E., Duddy G., Wilson S., Baptista M.A., Fiske B.K., Fell M.J.,
RA Morrow J.A., Reith A.D., Alessi D.R., Mann M.;
RT "Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates
RT a subset of Rab GTPases.";
RL Elife 5:0-0(2016).
RN [20]
RP INTERACTION WITH RAB3A; RAB3B; RAB3C; RAB3D; RAB5A; RAB5B; RAB5C; RAB8A;
RP RAB8B; RAB10; RAB12; RAB35 AND RAB43.
RX PubMed=29125462; DOI=10.7554/elife.31012;
RA Steger M., Diez F., Dhekne H.S., Lis P., Nirujogi R.S., Karayel O.,
RA Tonelli F., Martinez T.N., Lorentzen E., Pfeffer S.R., Alessi D.R.,
RA Mann M.;
RT "Systematic proteomic analysis of LRRK2-mediated Rab GTPase phosphorylation
RT establishes a connection to ciliogenesis.";
RL Elife 6:0-0(2017).
CC -!- FUNCTION: GDP-dissociation inhibitor preventing the GDP to GTP exchange
CC of most Rab proteins. By keeping these small GTPases in their inactive
CC GDP-bound form regulates intracellular membrane trafficking
CC (PubMed:25860027). Negatively regulates protein transport to the cilium
CC and ciliogenesis through the inhibition of RAB8A (PubMed:25860027).
CC {ECO:0000269|PubMed:25860027}.
CC -!- SUBUNIT: Interacts with RHOH (PubMed:11809807). Interacts with the GDP-
CC bound forms of RAB3A, RAB3B, RAB3C, RAB5A, RAB5B, RAB5C, RAB8B, RAB10,
CC RAB12, RAB35, and RAB43; binds RAB3D to a lesser extent
CC (PubMed:26824392, PubMed:29125462). Interacts with RAB8A (GDP-bound
CC inactive form); prevents RAB8A activation (PubMed:25860027,
CC PubMed:26824392, PubMed:29125462). Interacts with DZIP1; negatively
CC regulates the interaction of GDI2 with GDP-bound RAB8A
CC (PubMed:25860027). {ECO:0000269|PubMed:11809807,
CC ECO:0000269|PubMed:25860027, ECO:0000269|PubMed:26824392,
CC ECO:0000269|PubMed:29125462}.
CC -!- INTERACTION:
CC P50395; P62820-1: RAB1A; NbExp=2; IntAct=EBI-1049143, EBI-15666813;
CC P50395; Q8BMD2: Dzip1; Xeno; NbExp=2; IntAct=EBI-1049143, EBI-7089968;
CC P50395; Q8BMD2-1: Dzip1; Xeno; NbExp=3; IntAct=EBI-1049143, EBI-16153101;
CC P50395; P61027: Rab10; Xeno; NbExp=3; IntAct=EBI-1049143, EBI-911581;
CC P50395; P55258: Rab8a; Xeno; NbExp=3; IntAct=EBI-1049143, EBI-398411;
CC P50395; P61007: RAB8A; Xeno; NbExp=2; IntAct=EBI-1049143, EBI-7473289;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250};
CC Peripheral membrane protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50395-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50395-2; Sequence=VSP_043469;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:7543319}.
CC -!- SIMILARITY: Belongs to the Rab GDI family. {ECO:0000305}.
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DR EMBL; D13988; BAA03095.1; -; mRNA.
DR EMBL; Y13286; CAA73734.1; -; mRNA.
DR EMBL; Y13287; CAA73735.1; -; Genomic_DNA.
DR EMBL; Y13288; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13289; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13290; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13291; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13292; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13293; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13294; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13295; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13296; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; Y13297; CAA73735.1; JOINED; Genomic_DNA.
DR EMBL; BT006868; AAP35514.1; -; mRNA.
DR EMBL; AK297554; BAG59947.1; -; mRNA.
DR EMBL; AL596094; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005145; AAH05145.1; -; mRNA.
DR EMBL; AF144713; AAD34588.1; -; mRNA.
DR CCDS; CCDS44352.1; -. [P50395-2]
DR CCDS; CCDS7071.1; -. [P50395-1]
DR RefSeq; NP_001108628.1; NM_001115156.1. [P50395-2]
DR RefSeq; NP_001485.2; NM_001494.3. [P50395-1]
DR AlphaFoldDB; P50395; -.
DR SMR; P50395; -.
DR BioGRID; 108933; 115.
DR DIP; DIP-50593N; -.
DR IntAct; P50395; 56.
DR MINT; P50395; -.
DR STRING; 9606.ENSP00000369538; -.
DR GlyGen; P50395; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P50395; -.
DR MetOSite; P50395; -.
DR PhosphoSitePlus; P50395; -.
DR SwissPalm; P50395; -.
DR BioMuta; GDI2; -.
DR DMDM; 13638228; -.
DR OGP; P50395; -.
DR REPRODUCTION-2DPAGE; IPI00031461; -.
DR REPRODUCTION-2DPAGE; P50395; -.
DR CPTAC; CPTAC-512; -.
DR CPTAC; CPTAC-513; -.
DR EPD; P50395; -.
DR jPOST; P50395; -.
DR MassIVE; P50395; -.
DR PaxDb; P50395; -.
DR PeptideAtlas; P50395; -.
DR PRIDE; P50395; -.
DR ProteomicsDB; 56216; -. [P50395-1]
DR ProteomicsDB; 56217; -. [P50395-2]
DR Antibodypedia; 10649; 263 antibodies from 28 providers.
DR DNASU; 2665; -.
DR Ensembl; ENST00000380181.7; ENSP00000369528.3; ENSG00000057608.17. [P50395-2]
DR Ensembl; ENST00000380191.9; ENSP00000369538.4; ENSG00000057608.17. [P50395-1]
DR GeneID; 2665; -.
DR KEGG; hsa:2665; -.
DR MANE-Select; ENST00000380191.9; ENSP00000369538.4; NM_001494.4; NP_001485.2.
DR UCSC; uc001iim.5; human. [P50395-1]
DR CTD; 2665; -.
DR DisGeNET; 2665; -.
DR GeneCards; GDI2; -.
DR HGNC; HGNC:4227; GDI2.
DR HPA; ENSG00000057608; Low tissue specificity.
DR MIM; 600767; gene.
DR neXtProt; NX_P50395; -.
DR OpenTargets; ENSG00000057608; -.
DR PharmGKB; PA28642; -.
DR VEuPathDB; HostDB:ENSG00000057608; -.
DR eggNOG; KOG1439; Eukaryota.
DR GeneTree; ENSGT00950000182994; -.
DR HOGENOM; CLU_021695_0_0_1; -.
DR InParanoid; P50395; -.
DR OMA; YIPTDLG; -.
DR PhylomeDB; P50395; -.
DR TreeFam; TF300449; -.
DR PathwayCommons; P50395; -.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR Reactome; R-HSA-8876198; RAB GEFs exchange GTP for GDP on RABs.
DR SignaLink; P50395; -.
DR BioGRID-ORCS; 2665; 62 hits in 1080 CRISPR screens.
DR ChiTaRS; GDI2; human.
DR GeneWiki; GDI2; -.
DR GenomeRNAi; 2665; -.
DR Pharos; P50395; Tbio.
DR PRO; PR:P50395; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P50395; protein.
DR Bgee; ENSG00000057608; Expressed in jejunal mucosa and 208 other tissues.
DR ExpressionAtlas; P50395; baseline and differential.
DR Genevisible; P50395; HS.
DR GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:Ensembl.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:1902018; P:negative regulation of cilium assembly; IMP:UniProtKB.
DR GO; GO:1903565; P:negative regulation of protein localization to cilium; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:Ensembl.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR000806; RabGDI.
DR PANTHER; PTHR11787; PTHR11787; 1.
DR Pfam; PF00996; GDI; 1.
DR PRINTS; PR00892; RABGDI.
DR PRINTS; PR00891; RABGDIREP.
DR SUPFAM; SSF51905; SSF51905; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; GTPase activation; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..445
FT /note="Rab GDP dissociation inhibitor beta"
FT /id="PRO_0000056679"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 57
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q61598"
FT MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 112
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P50399"
FT MOD_RES 269
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 86..130
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043469"
FT CONFLICT 2
FT /note="N -> D (in Ref. 1; BAA03095)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 445 AA; 50663 MW; CE186A2E3A47FCC9 CRC64;
MNEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESASITPLE DLYKRFKIPG
SPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVTEGSFV YKGGKIYKVP
STEAEALASS LMGLFEKRRF RKFLVYVANF DEKDPRTFEG IDPKKTTMRD VYKKFDLGQD
VIDFTGHALA LYRTDDYLDQ PCYETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR
LSAIYGGTYM LNKPIEEIIV QNGKVIGVKS EGEIARCKQL ICDPSYVKDR VEKVGQVIRV
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISFA HNVAAQGKYI AIVSTTVETK
EPEKEIRPAL ELLEPIEQKF VSISDLLVPK DLGTESQIFI SRTYDATTHF ETTCDDIKNI
YKRMTGSEFD FEEMKRKKND IYGED
