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UniProtKB/Swiss-Prot entry P50395


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name GDIB_HUMAN
Primary accession number P50395
Secondary accession numbers O43928 Q9UQM6
Integrated into Swiss-Prot on October 1, 1996
Sequence was last modified on April 27, 2001 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 79)
Name and origin of the protein
Protein name Rab GDP dissociation inhibitor beta
Synonyms Rab GDI beta
Guanosine diphosphate dissociation inhibitor 2
GDI-2
Gene name
Name: GDI2
Synonyms: RABGDIB
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Asada M., Kaibuchi K., Takai Y.;
Submitted (APR-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
DOI=10.1007/s003359900685; PubMed=9434952 [NCBI, ExPASy, EBI, Israel, Japan]
Sedlacek Z., Munstermann E., Mincheva A., Lichter P., Poutska A.;
"The human rab GDI beta gene with long retroposon-rich introns maps to 10p15 and its pseudogene to 7p11-p13.";
Mamm. Genome 9:78-80(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 81-439.
TISSUE=Pancreas;
DOI=10.1002/1097-4644(20001215)79:4<628::AID-JCB120>3.0.CO;2-T; PubMed=10996854 [NCBI, ExPASy, EBI, Israel, Japan]
Caillol N., Pasqualini E., Lloubes R., Lombardo D.;
"Impairment of bile salt-dependent lipase secretion in human pancreatic tumoral SOJ-6 cells.";
J. Cell. Biochem. 79:628-647(2000).
[6]
TISSUE SPECIFICITY.
DOI=10.1093/hmg/4.4.701; PubMed=7543319 [NCBI, ExPASy, EBI, Israel, Japan]
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. Mol. Genet. 4:701-708(1995).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-203, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D13988; BAA03095.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13286; CAA73734.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13287; CAA73735.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13288; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13289; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13290; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13291; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13292; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13293; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13294; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13295; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13296; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13297; CAA73735.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT006868; AAP35514.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC005145; AAH05145.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF144713; AAD34588.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00031461; -.
RefSeq NP_001485.2; -.
UniGene Hs.299055
3D structure databases
HSSP P21856; 1D5T. [HSSP ENTRY / PDB]
SMR P50395; 1-431.
ModBase P50395.
Protein-protein interaction databases
IntAct P50395; 13.
PTM databases
PhosphoSite P50395; -.
Enzyme and pathway databases
Reactome REACT_11044; Signaling by Rho GTPases.
2D gel databases
OGP P50395; -.
REPRODUCTION-2DPAGE IPI00031461; -.
P50395; -.
Organism-specific databases
GeneCards GC01P072513; -.
GC10M005848; -.
H-InvDB HIX0008614; -.
HGNC HGNC:4227; GDI2.
GenAtlas GDI2.
MIM 600767; gene. [NCBI / EBI]
PharmGKB PA28642; -.
Gene expression databases
ArrayExpress P50395; -.
Bgee P50395; -.
CleanEx HS_GDI2; -.
GermOnline ENSG00000057608; Homo sapiens.
Ontologies
GO
GO:0009986; Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005737; Cellular component: cytoplasm (traceable author statement from UniProtKB).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005096; Molecular function: GTPase activator activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005093; Molecular function: Rab GDP-dissociation inhibitor activity (traceable author statement from ProtInc).
GO:0015031; Biological process: protein transport (inferred from electronic annotation from InterPro).
GO:0043087; Biological process: regulation of GTPase activity (inferred from electronic annotation from InterPro).
GO:0007165; Biological process: signal transduction (traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR018203; GDP_dissociation_inhibitor.
IPR002005; Rab_GDI_REP.
IPR000806; RabGDI.
Graphical view of domain structure.
PANTHER PTHR11787; Rab_GDI_REP; 1.
Pfam PF00996; GDI; 1.
Pfam graphical view of domain structure.
PRINTS PR00892; RABGDI.
PR00891; RABGDIREP.
Proteomic databases
PRIDE P50395; -.
Genome annotation databases
Ensembl ENSG00000057608; Homo sapiens. [Contig view]
GeneID 2665; -.
Phylogenomic databases
HOGENOM P50395; -.
HOVERGEN P50395; -.
OMA P50395; MREVYKK.
Other
NextBio 10516; -.
SOURCE GDI2; Homo sapiens.
ProtoNet P50395.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; GTPase activation; Membrane; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   445  445     Rab GDP dissociation inhibitor beta. PRO_0000056679
MOD_RES   61    61        Phosphoserine. 
MOD_RES   203   203        Phosphotyrosine. 
CONFLICT   2     2        N -> D (in Ref. 1; BAA03095). 
Sequence information
Length: 445 AA [This is the length of the unprocessed precursor] Molecular weight: 50663 Da [This is the MW of the unprocessed precursor] CRC64: CE186A2E3A47FCC9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESASITPLE DLYKRFKIPG 

        70         80         90        100        110        120 
SPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVTEGSFV YKGGKIYKVP 

       130        140        150        160        170        180 
STEAEALASS LMGLFEKRRF RKFLVYVANF DEKDPRTFEG IDPKKTTMRD VYKKFDLGQD 

       190        200        210        220        230        240 
VIDFTGHALA LYRTDDYLDQ PCYETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR 

       250        260        270        280        290        300 
LSAIYGGTYM LNKPIEEIIV QNGKVIGVKS EGEIARCKQL ICDPSYVKDR VEKVGQVIRV 

       310        320        330        340        350        360 
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISFA HNVAAQGKYI AIVSTTVETK 

       370        380        390        400        410        420 
EPEKEIRPAL ELLEPIEQKF VSISDLLVPK DLGTESQIFI SRTYDATTHF ETTCDDIKNI 

       430        440 
YKRMTGSEFD FEEMKRKKND IYGED 

P50395 in FASTA format

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