RABGEF1

Protein-coding gene in the species Homo sapiens

RABGEF1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1TXU, 2C7M, 2C7N, 2OT3, 4N3X, 4N3Y, 4N3Z, 4Q9U

Identifiers
AliasesRABGEF1, RABEX5, RAP1, rabex-5, RAB guanine nucleotide exchange factor 1
External IDsOMIM: 609700; MGI: 1929459; HomoloGene: 8720; GeneCards: RABGEF1; OMA:RABGEF1 - orthologs
Gene location (Human)
Chromosome 7 (human)
Chr.Chromosome 7 (human)[1]
Chromosome 7 (human)
Genomic location for RABGEF1
Genomic location for RABGEF1
Band7q11.21Start66,682,164 bp[1]
End66,811,464 bp[1]
Gene location (Mouse)
Chromosome 5 (mouse)
Chr.Chromosome 5 (mouse)[2]
Chromosome 5 (mouse)
Genomic location for RABGEF1
Genomic location for RABGEF1
Band5|5 G1.3Start130,200,639 bp[2]
End130,243,183 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • bone marrow

  • skin of leg

  • stromal cell of endometrium

  • skin of abdomen

  • gastric mucosa

  • tibial arteries

  • blood

  • vagina

  • superior frontal gyrus

  • bone marrow cells
Top expressed in
  • neural layer of retina

  • epithelium of lens

  • retinal pigment epithelium

  • sternocleidomastoid muscle

  • triceps brachii muscle

  • transitional epithelium of urinary bladder

  • temporal muscle

  • tibialis anterior muscle

  • muscle of thigh

  • digastric muscle
More reference expression data
BioGPS
n/a
Gene ontology
Molecular function
  • DNA binding
  • zinc ion binding
  • metal ion binding
  • protein binding
  • ubiquitin protein ligase activity
Cellular component
  • cytoplasm
  • recycling endosome
  • endosome
  • early endosome
  • nucleolus
  • cytosol
  • early endosome membrane
  • vesicle
Biological process
  • endocytosis
  • protein targeting to membrane
  • protein transport
  • negative regulation of protein phosphorylation
  • negative regulation of leukocyte migration
  • protein ubiquitination
  • negative regulation of mast cell activation
  • negative regulation of mast cell degranulation
  • negative regulation of Ras protein signal transduction
  • negative regulation of receptor-mediated endocytosis
  • negative regulation of inflammatory response
  • regulation of Fc receptor mediated stimulatory signaling pathway
  • negative regulation of Kit signaling pathway
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

27342

56715

Ensembl

ENSG00000154710

ENSMUSG00000025340

UniProt

Q9UJ41
Q3HKR1

Q9JM13

RefSeq (mRNA)

NM_001287060
NM_001287061
NM_001287062
NM_014504

NM_001199059
NM_019983
NM_001359233
NM_001378873

RefSeq (protein)
NP_001273989
NP_001273990
NP_001273991
NP_055319
NP_001354651

NP_001354652
NP_001354653
NP_001354654
NP_001354655
NP_001354656
NP_001354657
NP_001354658
NP_001354659
NP_001354660
NP_001354661
NP_001354662
NP_001354663
NP_001354664
NP_001354665
NP_001354666
NP_001354667
NP_001354668
NP_001354669
NP_001354670
NP_001354671
NP_001354672
NP_001354673
NP_001354674
NP_001354675
NP_001354676
NP_001354677
NP_001354678
NP_001354679
NP_001354680
NP_001354681
NP_001354682
NP_001354683
NP_001354684
NP_001354685

NP_001185988
NP_064367
NP_001346162
NP_001365802
NP_001390209

NP_001390210
NP_001390211
NP_001390212

Location (UCSC)Chr 7: 66.68 – 66.81 MbChr 5: 130.2 – 130.24 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Rab5 GDP/GTP exchange factor is a protein that in humans is encoded by the RABGEF1 gene.[5][6][7]

RABGEF1 forms a complex with rabaptin-5 (RABPT5; MIM 603616) that is required for endocytic membrane fusion, and it serves as a specific guanine nucleotide exchange factor for RAB5(RAB5A; MIM 179512) (Horiuchi et al., 1997) [supplied by OMIM].[7]


References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000154710 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000025340 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Mattera R, Arighi CN, Lodge R, Zerial M, Bonifacino JS (Dec 2002). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". EMBO J. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
  6. ^ Nimmrich I, Erdmann S, Melchers U, Finke U, Hentsch S, Moyer MP, Hoffmann I, Muller O (Dec 2000). "Seven genes that are differentially transcribed in colorectal tumor cell lines". Cancer Lett. 160 (1): 37–43. doi:10.1016/S0304-3835(00)00553-X. PMID 11098082.
  7. ^ a b "Entrez Gene: RABGEF1 RAB guanine nucleotide exchange factor (GEF) 1".

Further reading

  • Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
  • Horiuchi H, Lippé R, McBride HM, et al. (1997). "A novel Rab5 GDP/GTP exchange factor complexed to Rabaptin-5 links nucleotide exchange to effector recruitment and function". Cell. 90 (6): 1149–59. doi:10.1016/S0092-8674(00)80380-3. PMID 9323142. S2CID 13972726.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
  • Lippé R, Miaczynska M, Rybin V, et al. (2001). "Functional synergy between Rab5 effector Rabaptin-5 and exchange factor Rabex-5 when physically associated in a complex". Mol. Biol. Cell. 12 (7): 2219–28. doi:10.1091/mbc.12.7.2219. PMC 55678. PMID 11452015.
  • de Renzis S, Sönnichsen B, Zerial M (2002). "Divalent Rab effectors regulate the sub-compartmental organization and sorting of early endosomes". Nat. Cell Biol. 4 (2): 124–33. doi:10.1038/ncb744. PMID 11788822. S2CID 6596498.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7". Nature. 424 (6945): 157–64. Bibcode:2003Natur.424..157H. doi:10.1038/nature01782. PMID 12853948.
  • Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
  • Jin J, Smith FD, Stark C, et al. (2004). "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Curr. Biol. 14 (16): 1436–50. Bibcode:2004CBio...14.1436J. doi:10.1016/j.cub.2004.07.051. PMID 15324660. S2CID 2371325.
  • Delprato A, Merithew E, Lambright DG (2004). "Structure, exchange determinants, and family-wide rab specificity of the tandem helical bundle and Vps9 domains of Rabex-5". Cell. 118 (5): 607–17. doi:10.1016/j.cell.2004.08.009. PMID 15339665. S2CID 9638315.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Penengo L, Mapelli M, Murachelli AG, et al. (2006). "Crystal structure of the ubiquitin binding domains of rabex-5 reveals two modes of interaction with ubiquitin". Cell. 124 (6): 1183–95. doi:10.1016/j.cell.2006.02.020. PMID 16499958. S2CID 2639312.
  • Kalesnikoff J, Rios EJ, Chen CC, et al. (2007). "Roles of RabGEF1/Rabex-5 domains in regulating Fc epsilon RI surface expression and Fc epsilon RI-dependent responses in mast cells". Blood. 109 (12): 5308–17. doi:10.1182/blood-2007-01-067363. PMC 1890836. PMID 17341663.
  • Ewing RM, Chu P, Elisma F, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  • Delprato A, Lambright DG (2007). "Structural basis for Rab GTPase activation by VPS9 domain exchange factors". Nat. Struct. Mol. Biol. 14 (5): 406–12. doi:10.1038/nsmb1232. PMC 2254184. PMID 17450153.
  • v
  • t
  • e
  • 1txu: Crystal Structure of the Vps9 Domain of Rabex-5
    1txu: Crystal Structure of the Vps9 Domain of Rabex-5
  • 2c7m: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
    2c7m: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
  • 2c7n: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
    2c7n: HUMAN RABEX-5 RESIDUES 1-74 IN COMPLEX WITH UBIQUITIN
  • 2fid: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin
    2fid: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin
  • 2fif: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin
    2fif: Crystal Structure of a Bovine Rabex-5 fragment complexed with ubiquitin
  • 2ot3: Crystal structure of rabex-5 VPS9 domain in complex with nucleotide free RAB21
    2ot3: Crystal structure of rabex-5 VPS9 domain in complex with nucleotide free RAB21
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