ID   GDIB_HUMAN              Reviewed;         445 AA.
AC   P50395; O43928; Q9UQM6;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   27-APR-2001, sequence version 2.
DT   03-NOV-2009, entry version 85.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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].
RX   MEDLINE=98096592; 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].
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
RT   vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 81-439.
RC   TISSUE=Pancreas;
RX   MEDLINE=20453283; 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
RT   pancreatic tumoral SOJ-6 cells.";
RL   J. Cell. Biochem. 79:628-647(2000).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   MEDLINE=95359978; 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
RT   in cellular transport.";
RL   Hum. Mol. Genet. 4:701-708(1995).
RN   [7]
RP   INTERACTION WITH RHOH.
RX   PubMed=11809807;
RA   Li X., Bu X., Lu B., Avraham H., Flavell R.A., Lim B.;
RT   "The hematopoiesis-specific GTP-binding protein RhoH is GTPase
RT   deficient and modulates activities of other Rho GTPases by an
RT   inhibitory function.";
RL   Mol. Cell. Biol. 22:1158-1171(2002).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, AND MASS
RP   SPECTROMETRY.
RX   PubMed=18083107; DOI=10.1016/j.cell.2007.11.025;
RA   Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,
RA   Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,
RA   Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,
RA   Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,
RA   Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
RT   "Global survey of phosphotyrosine signaling identifies oncogenic
RT   kinases in lung cancer.";
RL   Cell 131:1190-1203(2007).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASS
RP   SPECTROMETRY.
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   [10]
RP   IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
RA   Colinge J., Superti-Furga G., Bennett K.L.;
RL   Submitted (OCT-2008) to UniProtKB.
RN   [11]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-112 AND LYS-269, AND MASS
RP   SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
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).
CC   -!- FUNCTION: Regulates the GDP/GTP exchange reaction of most Rab
CC       proteins by inhibiting the dissociation of GDP from them, and the
CC       subsequent binding of GTP to them.
CC   -!- SUBUNIT: Interacts with RHOH.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC       Peripheral membrane protein (By similarity).
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- SIMILARITY: Belongs to the Rab GDI family.
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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; BC005145; AAH05145.1; -; mRNA.
DR   EMBL; AF144713; AAD34588.1; -; mRNA.
DR   IPI; IPI00940148; -.
DR   RefSeq; NP_001108628.1; -.
DR   RefSeq; NP_001485.2; -.
DR   UniGene; Hs.299055; -.
DR   HSSP; P21856; 1D5T.
DR   SMR; P50395; 1-431.
DR   IntAct; P50395; 13.
DR   STRING; P50395; -.
DR   PhosphoSite; P50395; -.
DR   OGP; P50395; -.
DR   REPRODUCTION-2DPAGE; IPI00031461; -.
DR   REPRODUCTION-2DPAGE; P50395; -.
DR   PRIDE; P50395; -.
DR   Ensembl; ENST00000380127; ENSP00000369470; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000380131; ENSP00000369474; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000380132; ENSP00000369475; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000380153; ENSP00000369498; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000380181; ENSP00000369528; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000380191; ENSP00000369538; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000418688; ENSP00000394177; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000435969; ENSP00000401924; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000447751; ENSP00000387565; ENSG00000057608; Homo sapiens.
DR   Ensembl; ENST00000456041; ENSP00000401733; ENSG00000057608; Homo sapiens.
DR   GeneID; 2665; -.
DR   KEGG; hsa:2665; -.
DR   UCSC; uc001iil.2; human.
DR   CTD; 2665; -.
DR   GeneCards; GC01P072513; -.
DR   GeneCards; GC10M005848; -.
DR   H-InvDB; HIX0008614; -.
DR   HGNC; HGNC:4227; GDI2.
DR   MIM; 600767; gene.
DR   PharmGKB; PA28642; -.
DR   HOGENOM; P50395; -.
DR   HOVERGEN; P50395; -.
DR   OMA; MREVYKK; -.
DR   Reactome; REACT_11044; Signaling by Rho GTPases.
DR   NextBio; 10516; -.
DR   ArrayExpress; P50395; -.
DR   Bgee; P50395; -.
DR   CleanEx; HS_GDI2; -.
DR   Genevestigator; P50395; -.
DR   GermOnline; ENSG00000057608; Homo sapiens.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
DR   GO; GO:0019898; C:extrinsic to membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:UniProtKB.
DR   GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; TAS:ProtInc.
DR   GO; GO:0015031; P:protein transport; IEA:InterPro.
DR   GO; GO:0043087; P:regulation of GTPase activity; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR   InterPro; IPR018203; GDP_dissociation_inhibitor.
DR   InterPro; IPR002005; Rab_GDI_REP.
DR   InterPro; IPR000806; RabGDI.
DR   PANTHER; PTHR11787; Rab_GDI_REP; 1.
DR   Pfam; PF00996; GDI; 1.
DR   PRINTS; PR00892; RABGDI.
DR   PRINTS; PR00891; RABGDIREP.
PE   1: Evidence at protein level;
KW   Acetylation; Complete proteome; Cytoplasm; GTPase activation;
KW   Membrane; Phosphoprotein.
FT   CHAIN         1    445       Rab GDP dissociation inhibitor beta.
FT                                /FTId=PRO_0000056679.
FT   MOD_RES      61     61       Phosphoserine.
FT   MOD_RES     112    112       N6-acetyllysine.
FT   MOD_RES     203    203       Phosphotyrosine.
FT   MOD_RES     269    269       N6-acetyllysine.
FT   CONFLICT      2      2       N -> D (in Ref. 1; BAA03095).
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
//