Full text data of GDI2
GDI2
(RABGDIB)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Rab GDP dissociation inhibitor beta; Rab GDI beta (Guanosine diphosphate dissociation inhibitor 2; GDI-2)
Rab GDP dissociation inhibitor beta; Rab GDI beta (Guanosine diphosphate dissociation inhibitor 2; GDI-2)
hRBCD
IPI00031461
IPI00031461 Rab GDP dissociation inhibitor beta the alpha is in the membrane soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00031461 Rab GDP dissociation inhibitor beta the alpha is in the membrane soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
P50395
ID GDIB_HUMAN Reviewed; 445 AA.
AC P50395; O43928; Q5SX88; Q9UQM6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-APR-2001, sequence version 2.
DT 22-JAN-2014, entry version 124.
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] (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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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
RT project: 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
RT pancreatic 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
RT in 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
RT deficient and modulates activities of other Rho GTPases by an
RT inhibitory function.";
RL Mol. Cell. Biol. 22:1158-1171(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [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).
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 -!- INTERACTION:
CC P61027:Rab10 (xeno); NbExp=3; IntAct=EBI-1049143, EBI-911581;
CC P20338:RAB4A; NbExp=2; IntAct=EBI-1049143, EBI-722284;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC Peripheral membrane protein (By similarity).
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 Note=No experimental confirmation available;
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; AK297554; BAG59947.1; -; mRNA.
DR EMBL; AL596094; CAI13363.1; -; Genomic_DNA.
DR EMBL; BC005145; AAH05145.1; -; mRNA.
DR EMBL; AF144713; AAD34588.1; -; mRNA.
DR RefSeq; NP_001108628.1; NM_001115156.1.
DR RefSeq; NP_001485.2; NM_001494.3.
DR UniGene; Hs.299055; -.
DR ProteinModelPortal; P50395; -.
DR SMR; P50395; 1-430.
DR DIP; DIP-50593N; -.
DR IntAct; P50395; 14.
DR MINT; MINT-4999214; -.
DR STRING; 9606.ENSP00000369538; -.
DR PhosphoSite; P50395; -.
DR DMDM; 13638228; -.
DR OGP; P50395; -.
DR REPRODUCTION-2DPAGE; IPI00031461; -.
DR REPRODUCTION-2DPAGE; P50395; -.
DR PaxDb; P50395; -.
DR PRIDE; P50395; -.
DR DNASU; 2665; -.
DR Ensembl; ENST00000380181; ENSP00000369528; ENSG00000057608.
DR Ensembl; ENST00000380191; ENSP00000369538; ENSG00000057608.
DR GeneID; 2665; -.
DR KEGG; hsa:2665; -.
DR UCSC; uc001iil.4; human.
DR CTD; 2665; -.
DR GeneCards; GC10M005807; -.
DR HGNC; HGNC:4227; GDI2.
DR HPA; HPA049290; -.
DR MIM; 600767; gene.
DR neXtProt; NX_P50395; -.
DR PharmGKB; PA28642; -.
DR eggNOG; COG5044; -.
DR HOGENOM; HOG000163825; -.
DR HOVERGEN; HBG000839; -.
DR InParanoid; P50395; -.
DR KO; K17255; -.
DR OrthoDB; EOG7PP56D; -.
DR PhylomeDB; P50395; -.
DR Reactome; REACT_111102; Signal Transduction.
DR ChiTaRS; GDI2; human.
DR GeneWiki; GDI2; -.
DR GenomeRNAi; 2665; -.
DR NextBio; 10516; -.
DR PRO; PR:P50395; -.
DR ArrayExpress; P50395; -.
DR Bgee; P50395; -.
DR CleanEx; HS_GDI2; -.
DR Genevestigator; P50395; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; TAS:ProtInc.
DR GO; GO:0005097; F:Rab GTPase activator activity; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR000806; RabGDI.
DR Pfam; PF00996; GDI; 1.
DR PRINTS; PR00892; RABGDI.
DR PRINTS; PR00891; RABGDIREP.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW GTPase activation; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1 445 Rab GDP dissociation inhibitor beta.
FT /FTId=PRO_0000056679.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 61 61 Phosphoserine.
FT MOD_RES 112 112 N6-acetyllysine.
FT MOD_RES 269 269 N6-acetyllysine.
FT VAR_SEQ 86 130 Missing (in isoform 2).
FT /FTId=VSP_043469.
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
//
ID GDIB_HUMAN Reviewed; 445 AA.
AC P50395; O43928; Q5SX88; Q9UQM6;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
read moreDT 27-APR-2001, sequence version 2.
DT 22-JAN-2014, entry version 124.
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] (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
RT 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA 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
RT project: 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
RT pancreatic 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
RT in 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
RT deficient and modulates activities of other Rho GTPases by an
RT inhibitory function.";
RL Mol. Cell. Biol. 22:1158-1171(2002).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASS
RP SPECTROMETRY.
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 MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a 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 MASS
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [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).
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 -!- INTERACTION:
CC P61027:Rab10 (xeno); NbExp=3; IntAct=EBI-1049143, EBI-911581;
CC P20338:RAB4A; NbExp=2; IntAct=EBI-1049143, EBI-722284;
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Membrane;
CC Peripheral membrane protein (By similarity).
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 Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the Rab GDI family.
CC -----------------------------------------------------------------------
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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; CAI13363.1; -; Genomic_DNA.
DR EMBL; BC005145; AAH05145.1; -; mRNA.
DR EMBL; AF144713; AAD34588.1; -; mRNA.
DR RefSeq; NP_001108628.1; NM_001115156.1.
DR RefSeq; NP_001485.2; NM_001494.3.
DR UniGene; Hs.299055; -.
DR ProteinModelPortal; P50395; -.
DR SMR; P50395; 1-430.
DR DIP; DIP-50593N; -.
DR IntAct; P50395; 14.
DR MINT; MINT-4999214; -.
DR STRING; 9606.ENSP00000369538; -.
DR PhosphoSite; P50395; -.
DR DMDM; 13638228; -.
DR OGP; P50395; -.
DR REPRODUCTION-2DPAGE; IPI00031461; -.
DR REPRODUCTION-2DPAGE; P50395; -.
DR PaxDb; P50395; -.
DR PRIDE; P50395; -.
DR DNASU; 2665; -.
DR Ensembl; ENST00000380181; ENSP00000369528; ENSG00000057608.
DR Ensembl; ENST00000380191; ENSP00000369538; ENSG00000057608.
DR GeneID; 2665; -.
DR KEGG; hsa:2665; -.
DR UCSC; uc001iil.4; human.
DR CTD; 2665; -.
DR GeneCards; GC10M005807; -.
DR HGNC; HGNC:4227; GDI2.
DR HPA; HPA049290; -.
DR MIM; 600767; gene.
DR neXtProt; NX_P50395; -.
DR PharmGKB; PA28642; -.
DR eggNOG; COG5044; -.
DR HOGENOM; HOG000163825; -.
DR HOVERGEN; HBG000839; -.
DR InParanoid; P50395; -.
DR KO; K17255; -.
DR OrthoDB; EOG7PP56D; -.
DR PhylomeDB; P50395; -.
DR Reactome; REACT_111102; Signal Transduction.
DR ChiTaRS; GDI2; human.
DR GeneWiki; GDI2; -.
DR GenomeRNAi; 2665; -.
DR NextBio; 10516; -.
DR PRO; PR:P50395; -.
DR ArrayExpress; P50395; -.
DR Bgee; P50395; -.
DR CleanEx; HS_GDI2; -.
DR Genevestigator; P50395; -.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005794; C:Golgi apparatus; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005093; F:Rab GDP-dissociation inhibitor activity; TAS:ProtInc.
DR GO; GO:0005097; F:Rab GTPase activator activity; IEA:Ensembl.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR GO; GO:0051056; P:regulation of small GTPase mediated signal transduction; TAS:Reactome.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; TAS:Reactome.
DR InterPro; IPR018203; GDP_dissociation_inhibitor.
DR InterPro; IPR000806; RabGDI.
DR Pfam; PF00996; GDI; 1.
DR PRINTS; PR00892; RABGDI.
DR PRINTS; PR00891; RABGDIREP.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW GTPase activation; Membrane; Phosphoprotein; Reference proteome.
FT CHAIN 1 445 Rab GDP dissociation inhibitor beta.
FT /FTId=PRO_0000056679.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 61 61 Phosphoserine.
FT MOD_RES 112 112 N6-acetyllysine.
FT MOD_RES 269 269 N6-acetyllysine.
FT VAR_SEQ 86 130 Missing (in isoform 2).
FT /FTId=VSP_043469.
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
//
MIM
600767
*RECORD*
*FIELD* NO
600767
*FIELD* TI
*600767 GDP-DISSOCIATION INHIBITOR 2; GDI2
;;RAB GDP-DISSOCIATION INHIBITOR, BETA; RABGDIB;;
read moreRAB GDI-BETA
*FIELD* TX
DESCRIPTION
GDI-beta (GDI2) is a member of the GDP-dissociation inhibitor family,
which includes GDI-alpha (GDI1; 300104). The rab GDIs modulate the
activity of G proteins of the rab family and play a role in the
regulation of vesicle-mediated cellular transport (summary by Sedlacek
et al., 1998).
CLONING
Shisheva et al. (1994) cloned mouse RABGDIB (which they referred to as
'smg p25A GDI') and reported the sequence. Sedlacek et al. (1994) found
that the human RABGDIB sequence is 86.5% similar to RABGDIA, which they
referred to as 'XAP-4.' Bachner et al. (1995) studied expression
patterns of the 2 human genes. They showed that the 2.5-kb mRNA for
RABGDIB is ubiquitously expressed, in contrast to RABGDIA, which is
expressed primarily in neural and sensory tissues.
Rak et al. (2003) used a combination of chemical synthesis and protein
engineering to generate and crystallize the monoprenylated YPT1-RABGDI
complex. The structure of this complex was determined to 1.5-angstrom
resolution and provided a structural basis for the ability of RABGDI to
inhibit nucleotide release by RAB proteins. Isoprenoid binding requires
a conformational change that opens a cavity in the hydrophobic core of
its domain II. Analysis of the structure provided a molecular basis for
understanding a RABGDI mutant that causes mental retardation.
GENE STRUCTURE
The GDI-beta gene contains 11 exons (Sedlacek et al., 1998).
MAPPING
By in situ hybridization, Sedlacek et al. (1998) demonstrated that the
GDI2 gene maps to 10p15; a processed pseudogene maps to 7p13-p11.
*FIELD* RF
1. Bachner, D.; Sedlacek, Z.; Korn, B.; Hameister, H.; Poustka, A.
: Expression patterns of two human genes coding for different rab
GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved
in cellular transport. Hum. Molec. Genet. 4: 701-708, 1995.
2. Rak, A.; Pylypenko, O.; Durek, T.; Watzke, A.; Kushnir, S.; Brunsveld,
L.; Waldmann, H.; Goody, R. S.; Alexandrov, K.: Structure of Rab
GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science 302:
646-650, 2003.
3. Sedlacek, Z.; Konecki, D. S.; Korn, B.; Klauck, S. M.; Poustka,
A.: Evolutionary conservation and genomic organization of XAP-4,
an Xq28 located gene coding for a human rab GDP-dissociation inhibitor
(GDI). Mammalian Genome 5: 633-639, 1994.
4. Sedlacek, Z.; Munstermann, E.; Mincheva, A.; Lichter, P.; Poustka,
A.: The human rab GDI beta gene with long retroposon-rich introns
maps to 10p15 and its pseudogene to 7p11-p13. Mammalian Genome 9:
78-80, 1998.
5. Shisheva, A.; Sudhof, T. C.; Czech, M. P.: Cloning, characterization,
and expression of a novel GDP dissociation inhibitor isoform from
skeletal muscle. Molec. Cell. Biol. 14: 3459-3468, 1994.
*FIELD* CN
Ada Hamosh - updated: 11/11/2003
Victor A. McKusick - updated: 2/19/1998
*FIELD* CD
Alan F. Scott: 9/11/1995
*FIELD* ED
carol: 08/02/2011
carol: 8/1/2011
tkritzer: 11/12/2003
terry: 11/11/2003
alopez: 3/8/1999
terry: 2/19/1998
mark: 11/14/1997
mark: 10/27/1997
mark: 10/25/1997
joanna: 4/5/1996
mark: 9/11/1995
*RECORD*
*FIELD* NO
600767
*FIELD* TI
*600767 GDP-DISSOCIATION INHIBITOR 2; GDI2
;;RAB GDP-DISSOCIATION INHIBITOR, BETA; RABGDIB;;
read moreRAB GDI-BETA
*FIELD* TX
DESCRIPTION
GDI-beta (GDI2) is a member of the GDP-dissociation inhibitor family,
which includes GDI-alpha (GDI1; 300104). The rab GDIs modulate the
activity of G proteins of the rab family and play a role in the
regulation of vesicle-mediated cellular transport (summary by Sedlacek
et al., 1998).
CLONING
Shisheva et al. (1994) cloned mouse RABGDIB (which they referred to as
'smg p25A GDI') and reported the sequence. Sedlacek et al. (1994) found
that the human RABGDIB sequence is 86.5% similar to RABGDIA, which they
referred to as 'XAP-4.' Bachner et al. (1995) studied expression
patterns of the 2 human genes. They showed that the 2.5-kb mRNA for
RABGDIB is ubiquitously expressed, in contrast to RABGDIA, which is
expressed primarily in neural and sensory tissues.
Rak et al. (2003) used a combination of chemical synthesis and protein
engineering to generate and crystallize the monoprenylated YPT1-RABGDI
complex. The structure of this complex was determined to 1.5-angstrom
resolution and provided a structural basis for the ability of RABGDI to
inhibit nucleotide release by RAB proteins. Isoprenoid binding requires
a conformational change that opens a cavity in the hydrophobic core of
its domain II. Analysis of the structure provided a molecular basis for
understanding a RABGDI mutant that causes mental retardation.
GENE STRUCTURE
The GDI-beta gene contains 11 exons (Sedlacek et al., 1998).
MAPPING
By in situ hybridization, Sedlacek et al. (1998) demonstrated that the
GDI2 gene maps to 10p15; a processed pseudogene maps to 7p13-p11.
*FIELD* RF
1. Bachner, D.; Sedlacek, Z.; Korn, B.; Hameister, H.; Poustka, A.
: Expression patterns of two human genes coding for different rab
GDP-dissociation inhibitors (GDIs), extremely conserved proteins involved
in cellular transport. Hum. Molec. Genet. 4: 701-708, 1995.
2. Rak, A.; Pylypenko, O.; Durek, T.; Watzke, A.; Kushnir, S.; Brunsveld,
L.; Waldmann, H.; Goody, R. S.; Alexandrov, K.: Structure of Rab
GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science 302:
646-650, 2003.
3. Sedlacek, Z.; Konecki, D. S.; Korn, B.; Klauck, S. M.; Poustka,
A.: Evolutionary conservation and genomic organization of XAP-4,
an Xq28 located gene coding for a human rab GDP-dissociation inhibitor
(GDI). Mammalian Genome 5: 633-639, 1994.
4. Sedlacek, Z.; Munstermann, E.; Mincheva, A.; Lichter, P.; Poustka,
A.: The human rab GDI beta gene with long retroposon-rich introns
maps to 10p15 and its pseudogene to 7p11-p13. Mammalian Genome 9:
78-80, 1998.
5. Shisheva, A.; Sudhof, T. C.; Czech, M. P.: Cloning, characterization,
and expression of a novel GDP dissociation inhibitor isoform from
skeletal muscle. Molec. Cell. Biol. 14: 3459-3468, 1994.
*FIELD* CN
Ada Hamosh - updated: 11/11/2003
Victor A. McKusick - updated: 2/19/1998
*FIELD* CD
Alan F. Scott: 9/11/1995
*FIELD* ED
carol: 08/02/2011
carol: 8/1/2011
tkritzer: 11/12/2003
terry: 11/11/2003
alopez: 3/8/1999
terry: 2/19/1998
mark: 11/14/1997
mark: 10/27/1997
mark: 10/25/1997
joanna: 4/5/1996
mark: 9/11/1995