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Identification
HMDB Protein ID HMDBP01785
Secondary Accession Numbers
  • 7138
Name Rab GDP dissociation inhibitor beta
Synonyms
  1. GDI-2
  2. Guanosine diphosphate dissociation inhibitor 2
  3. Rab GDI beta
Gene Name GDI2
Protein Type Unknown
Biological Properties
General Function Involved in regulation of GTPase activity
Specific Function 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
Pathways Not Available
Reactions Not Available
GO Classification
Function
small gtpase regulator activity
enzyme regulator activity
gdp-dissociation inhibitor activity
rab gdp-dissociation inhibitor activity
nucleoside-triphosphatase regulator activity
gtpase regulator activity
Process
establishment of localization
transport
protein transport
biological regulation
regulation of biological process
regulation of metabolic process
regulation of cellular metabolic process
regulation of nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
regulation of nucleotide metabolic process
regulation of nucleotide catabolic process
regulation of purine nucleotide catabolic process
regulation of gtp catabolic process
regulation of gtpase activity
Cellular Location
  1. Cytoplasm
  2. Peripheral membrane protein
  3. Membrane
Gene Properties
Chromosome Location Chromosome:1
Locus 10p15
SNPs GDI2
Gene Sequence
>1338 bp
ATGAATGAGGAGTACGACGTGATCGTGCTGGGCACCGGCCTGACGGAATGTATCCTGTCA
GGTATAATGTCAGTGAATGGCAAGAAAGTTCTTCATATGGATCGAAACCCTTACTACGGA
GGAGAGAGTGCATCTATAACACCATTGGAAGATTTATACAAAAGATTTAAAATACCAGGA
TCACCACCCGAGTCAATGGGGAGAGGAAGAGACTGGAATGTTGACTTGATTCCCAAGTTC
CTTATGGCTAATGGTCAGCTGGTTAAGATGCTGCTTTATACAGAGGTAACTCGCTATCTG
GATTTTAAAGTGACTGAAGGGAGCTTTGTCTATAAGGGTGGAAAAATCTACAAGGTTCCT
TCCACTGAAGCAGAAGCCCTGGCATCTAGCCTAATGGGATTGTTTGAAAAACGTCGCTTC
AGGAAATTCCTAGTGTATGTTGCCAACTTCGATGAAAAAGATCCAAGAACTTTTGAAGGC
ATTGATCCTAAGAAGACCACAATGCGAGATGTGTATAAGAAATTTGATTTGGGTCAAGAC
GTTATAGATTTTACTGGTCATGCTCTTGCACTTTACAGAACTGATGATTACTTAGATCAA
CCGTGTTATGAAACCATTAATAGAATTAAACTTTACAGTGAATCTTTGGCAAGATATGGC
AAAAGCCCATACCTTTATCCACTCTATGGCCTTGGAGAACTGCCCCAAGGATTTGCAAGG
CTAAGTGCTATTTATGGAGGTACCTATATGCTGAATAAACCCATTGAAGAAATCATTGTA
CAGAATGGAAAAGTAATTGGTGTAAAATCTGAAGGAGAAATTGCTCGCTGTAAGCAGCTC
ATCTGTGACCCCAGCTACGTAAAAGATCGGGTAGAAAAAGTGGGCCAGGTGATCAGAGTT
ATTTGCATCCTCAGCCACCCCATCAAGAACACCAATGATGCCAACTCCTGCCAGATCATT
ATTCCACAGAACCAAGTCAATCGAAAGTCAGATATCTACGTCTGCATGATCTCCTTTGCG
CACAATGTAGCAGCACAAGGGAAGTACATTGCTATAGTTAGTACAACTGTGGAAACCAAG
GAGCCTGAGAAGGAAATCAGACCAGCTTTGGAGCTCTTGGAACCAATTGAACAGAAATTT
GTTAGCATCAGTGACCTCCTGGTACCAAAAGACTTGGGAACAGAAAGCCAGATCTTTATT
TCCCGCACATATGATGCCACCACTCATTTTGAGACAACGTGTGATGACATTAAAAACATC
TATAAGAGGATGACAGGATCAGAGTTTGACTTTGAGGAAATGAAGCGCAAGAAGAATGAC
ATCTATGGGGAAGACTAA
Protein Properties
Number of Residues 445
Molecular Weight 50662.8
Theoretical pI 6.39
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Rab GDP dissociation inhibitor beta
MNEEYDVIVLGTGLTECILSGIMSVNGKKVLHMDRNPYYGGESASITPLEDLYKRFKIPG
SPPESMGRGRDWNVDLIPKFLMANGQLVKMLLYTEVTRYLDFKVTEGSFVYKGGKIYKVP
STEAEALASSLMGLFEKRRFRKFLVYVANFDEKDPRTFEGIDPKKTTMRDVYKKFDLGQD
VIDFTGHALALYRTDDYLDQPCYETINRIKLYSESLARYGKSPYLYPLYGLGELPQGFAR
LSAIYGGTYMLNKPIEEIIVQNGKVIGVKSEGEIARCKQLICDPSYVKDRVEKVGQVIRV
ICILSHPIKNTNDANSCQIIIPQNQVNRKSDIYVCMISFAHNVAAQGKYIAIVSTTVETK
EPEKEIRPALELLEPIEQKFVSISDLLVPKDLGTESQIFISRTYDATTHFETTCDDIKNI
YKRMTGSEFDFEEMKRKKNDIYGED
GenBank ID Protein 6598323
UniProtKB/Swiss-Prot ID P50395
UniProtKB/Swiss-Prot Entry Name GDIB_HUMAN
PDB IDs Not Available
GenBank Gene ID NM_001494.3
GeneCard ID GDI2
GenAtlas ID GDI2
HGNC ID HGNC:4227
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  3. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [PubMed:18669648 ]
  4. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. [PubMed:19413330 ]
  5. 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 JM, Yuan J, Bakalarski CE, Villen J, Kornhauser JM, Smith B, Li D, Zhou X, Gygi SP, Gu TL, Polakiewicz RD, Rush J, Comb MJ: Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell. 2007 Dec 14;131(6):1190-203. [PubMed:18083107 ]
  6. 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. 1995 Apr;4(4):701-8. [PubMed:7543319 ]
  7. Li X, Bu X, Lu B, Avraham H, Flavell RA, Lim B: The hematopoiesis-specific GTP-binding protein RhoH is GTPase deficient and modulates activities of other Rho GTPases by an inhibitory function. Mol Cell Biol. 2002 Feb;22(4):1158-71. [PubMed:11809807 ]
  8. 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. Mamm Genome. 1998 Jan;9(1):78-80. [PubMed:9434952 ]
  9. 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. 2000 Sep 14;79(4):628-47. [PubMed:10996854 ]