CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-008279
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Rab GDP dissociation inhibitor alpha 
Protein Synonyms/Alias
 Rab GDI alpha; Guanosine diphosphate dissociation inhibitor 1; GDI-1 
Gene Name
 Gdi1 
Gene Synonyms/Alias
 Rabgdia 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
54TPLEELYKRFQLLEGacetylation[1]
54TPLEELYKRFQLLEGubiquitination[2]
112VEGSFVYKGGKIYKVacetylation[1]
174SMRDVYRKFDLGQDVacetylation[1]
210LETINRIKLYSESLAmethylation[3]
221ESLARYGKSPYLYPLacetylation[1]
253GGTYMLNKPVDDIIMacetylation[1]
264DIIMENGKVVGVKSEmethylation[3]
269NGKVVGVKSEGEVARacetylation[1]
269NGKVVGVKSEGEVARmethylation[3]
435AFDFENMKRKQNDVFacetylation[1]
437DFENMKRKQNDVFGEubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [2] Synaptic protein ubiquitination in rat brain revealed by antibody-based ubiquitome analysis.
 Na CH, Jones DR, Yang Y, Wang X, Xu Y, Peng J.
 J Proteome Res. 2012 Sep 7;11(9):4722-32. [PMID: 22871113]
 [3] A method for the comprehensive proteomic analysis of membrane proteins.
 Wu CC, MacCoss MJ, Howell KE, Yates JR 3rd.
 Nat Biotechnol. 2003 May;21(5):532-8. [PMID: 12692561
Functional Description
 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. 
Sequence Annotation
 MOD_RES 339 339 Phosphotyrosine (By similarity).  
Keyword
 Complete proteome; Cytoplasm; Direct protein sequencing; GTPase activation; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 447 AA 
Protein Sequence
MDEEYDVIVL GTGLTECILS GIMSVNGKKV LHMDRNPYYG GESSSITPLE ELYKRFQLLE 60
GPPESMGRGR DWNVDLIPKF LMANGQLVKM LLYTEVTRYL DFKVVEGSFV YKGGKIYKVP 120
STETEALASN LMGMFEKRRF RKFLVFVANF DENDPKTFEG VDPQTTSMRD VYRKFDLGQD 180
VIDFTGHALA LYRTDDYLDQ PCLETINRIK LYSESLARYG KSPYLYPLYG LGELPQGFAR 240
LSAIYGGTYM LNKPVDDIIM ENGKVVGVKS EGEVARCKQL ICDPSYIPDR VRKAGQVIRI 300
ICILSHPIKN TNDANSCQII IPQNQVNRKS DIYVCMISYA HNVAAQGKYI AIASTTVETA 360
EPEKEVEPAL ELLEPIDQKF VAISDLYEPI DDGSESQVFC SCSYDATTHF ETTCNDIKDI 420
YKRMAGSAFD FENMKRKQND VFGEADQ 447 
Gene Ontology
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0030496; C:midbody; IEA:Compara.
 GO:0043005; C:neuron projection; IDA:RGD.
 GO:0043234; C:protein complex; IDA:RGD.
 GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
 GO:0005093; F:Rab GDP-dissociation inhibitor activity; IDA:RGD.
 GO:0050771; P:negative regulation of axonogenesis; IDA:UniProtKB.
 GO:0043547; P:positive regulation of GTPase activity; IEA:GOC.
 GO:0015031; P:protein transport; IEA:InterPro.
 GO:0051592; P:response to calcium ion; IDA:RGD. 
Interpro
 IPR018203; GDP_dissociation_inhibitor.
 IPR016040; NAD(P)-bd_dom.
 IPR000806; RabGDI. 
Pfam
 PF00996; GDI 
SMART
  
PROSITE
  
PRINTS
 PR00892; RABGDI.
 PR00891; RABGDIREP.