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Protein

Rab GDP dissociation inhibitor beta

Gene

Gdi2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulates the GDP/GTP exchange reaction of most Rab proteins by inhibiting the dissociation of GDP from them, and the subsequent binding of GTP to them.

GO - Molecular functioni

  • GTPase activator activity Source: UniProtKB-KW
  • oxidoreductase activity Source: InterPro
  • poly(A) RNA binding Source: Ensembl
  • Rab GDP-dissociation inhibitor activity Source: RGD
  • small GTPase binding Source: RGD

GO - Biological processi

  • protein transport Source: RGD
  • small GTPase mediated signal transduction Source: Ensembl
  • vesicle-mediated transport Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

GTPase activation

Enzyme and pathway databases

ReactomeiR-RNO-194840. Rho GTPase cycle.

Names & Taxonomyi

Protein namesi
Recommended name:
Rab GDP dissociation inhibitor beta
Short name:
Rab GDI beta
Alternative name(s):
GDI-3
Guanosine diphosphate dissociation inhibitor 2
Short name:
GDI-2
Gene namesi
Name:Gdi2
Synonyms:Gdi3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 17

Organism-specific databases

RGDi61802. Gdi2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
  • extracellular exosome Source: Ensembl
  • focal adhesion Source: Ensembl
  • Golgi apparatus Source: Ensembl
  • membrane Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 445445Rab GDP dissociation inhibitor betaPRO_0000056683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei112 – 1121N6-acetyllysineBy similarity
Modified residuei130 – 1301PhosphoserineCombined sources
Modified residuei269 – 2691N6-acetyllysineBy similarity
Modified residuei382 – 3821PhosphoserineBy similarity
Modified residuei427 – 4271PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP50399.
PRIDEiP50399.

PTM databases

iPTMnetiP50399.
PhosphoSiteiP50399.

Expressioni

Tissue specificityi

Ubiquitously expressed.

Gene expression databases

GenevisibleiP50399. RN.

Interactioni

Subunit structurei

Interacts with RHOH.By similarity

GO - Molecular functioni

  • small GTPase binding Source: RGD

Protein-protein interaction databases

BioGridi248284. 2 interactions.
IntActiP50399. 1 interaction.
MINTiMINT-4575868.
STRINGi10116.ENSRNOP00000024952.

Structurei

3D structure databases

ProteinModelPortaliP50399.
SMRiP50399. Positions 1-430.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the Rab GDI family.Curated

Phylogenomic databases

eggNOGiKOG1439. Eukaryota.
COG5044. LUCA.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000163825.
HOVERGENiHBG000839.
InParanoidiP50399.
KOiK17255.
OMAiMAVETIH.
OrthoDBiEOG7PP56D.
PhylomeDBiP50399.
TreeFamiTF300449.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR018203. GDP_dissociation_inhibitor.
IPR000806. RabGDI.
[Graphical view]
PfamiPF00996. GDI. 1 hit.
[Graphical view]
PRINTSiPR00892. RABGDI.
PR00891. RABGDIREP.
SUPFAMiSSF51905. SSF51905. 2 hits.

Sequencei

Sequence statusi: Complete.

P50399-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDQNPYYG GESASITPLE
60 70 80 90 100
DLYKRFKLPG QPPASMGRGR DWNVDLIPKF LMANGQLVKM LLFTEVTRYM
110 120 130 140 150
DFKVIEGSFV YKGGKIYKVP STEAEALASS LMGLFEKRRF RKFLVYVANF
160 170 180 190 200
DEKDPRTFEG VDPKKTSMRD VYKKFDLGQD VIDFTGHSLA LYRTDDYLDQ
210 220 230 240 250
PCCETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR LSAIYGGTYM
260 270 280 290 300
LNKPIEEIIV QNGKVVGVKS EGEIARCKQL ICDPSYVKDR VEKVGQVIRV
310 320 330 340 350
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISFA HNVAAQGKYI
360 370 380 390 400
AIVSTTVETK EPEKEIRPAL ELLEPIEQKF VSISDLFVPK DLGTDSQIFI
410 420 430 440
SRAYDATTHF ETTCDDIKDI YKRMTGSEFD FEEMKRKKND IYGED
Length:445
Mass (Da):50,537
Last modified:January 23, 2007 - v2
Checksum:i483B7C7456B30525
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti205 – 2117TINRIKL → RLTELNF in CAA52412 (PubMed:8188702).Curated
Sequence conflicti231 – 2322LG → PW in CAA52412 (PubMed:8188702).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74401 mRNA. Translation: CAA52412.1.
BC061767 mRNA. Translation: AAH61767.1.
PIRiB54091.
RefSeqiNP_058972.2. NM_017276.2.
UniGeneiRn.1441.

Genome annotation databases

EnsembliENSRNOT00000024952; ENSRNOP00000024952; ENSRNOG00000018091.
GeneIDi29662.
KEGGirno:29662.
UCSCiRGD:61802. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X74401 mRNA. Translation: CAA52412.1.
BC061767 mRNA. Translation: AAH61767.1.
PIRiB54091.
RefSeqiNP_058972.2. NM_017276.2.
UniGeneiRn.1441.

3D structure databases

ProteinModelPortaliP50399.
SMRiP50399. Positions 1-430.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248284. 2 interactions.
IntActiP50399. 1 interaction.
MINTiMINT-4575868.
STRINGi10116.ENSRNOP00000024952.

PTM databases

iPTMnetiP50399.
PhosphoSiteiP50399.

Proteomic databases

PaxDbiP50399.
PRIDEiP50399.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000024952; ENSRNOP00000024952; ENSRNOG00000018091.
GeneIDi29662.
KEGGirno:29662.
UCSCiRGD:61802. rat.

Organism-specific databases

CTDi2665.
RGDi61802. Gdi2.

Phylogenomic databases

eggNOGiKOG1439. Eukaryota.
COG5044. LUCA.
GeneTreeiENSGT00530000063044.
HOGENOMiHOG000163825.
HOVERGENiHBG000839.
InParanoidiP50399.
KOiK17255.
OMAiMAVETIH.
OrthoDBiEOG7PP56D.
PhylomeDBiP50399.
TreeFamiTF300449.

Enzyme and pathway databases

ReactomeiR-RNO-194840. Rho GTPase cycle.

Miscellaneous databases

PROiP50399.

Gene expression databases

GenevisibleiP50399. RN.

Family and domain databases

Gene3Di3.50.50.60. 3 hits.
InterProiIPR023753. FAD/NAD-binding_dom.
IPR018203. GDP_dissociation_inhibitor.
IPR000806. RabGDI.
[Graphical view]
PfamiPF00996. GDI. 1 hit.
[Graphical view]
PRINTSiPR00892. RABGDI.
PR00891. RABGDIREP.
SUPFAMiSSF51905. SSF51905. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of two rab GDI species from rat brain: brain-specific and ubiquitous types."
    Nishimura N., Nakamura H., Takai Y., Sano K.
    J. Biol. Chem. 269:14191-14198(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Prostate.
  3. "Purification and characterization of Rab GDI beta from rat brain."
    Araki K., Nakanishi H., Hirano H., Kato M., Sasaki T., Takai Y.
    Biochem. Biophys. Res. Commun. 211:296-305(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-54 AND 58-74, CHARACTERIZATION.
  4. Lubec G., Afjehi-Sadat L., Kang S.U.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 80-98; 104-112; 119-137; 143-156; 175-193; 211-218; 349-360 AND 365-402, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain and Spinal cord.
  5. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiGDIB_RAT
AccessioniPrimary (citable) accession number: P50399
Secondary accession number(s): Q6P797
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 114 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.