RHPN2

Protein-coding gene in the species Homo sapiens
RHPN2
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

2VSV

Identifiers
AliasesRHPN2, P76RBE, RHOBP, rhophilin, Rho GTPase binding protein 2, rhophilin Rho GTPase binding protein 2
External IDsOMIM: 617932; MGI: 1289234; HomoloGene: 12407; GeneCards: RHPN2; OMA:RHPN2 - orthologs
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for RHPN2
Genomic location for RHPN2
Band19q13.11Start32,978,592 bp[1]
End33,064,888 bp[1]
Gene location (Mouse)
Chromosome 7 (mouse)
Chr.Chromosome 7 (mouse)[2]
Chromosome 7 (mouse)
Genomic location for RHPN2
Genomic location for RHPN2
Band7 B2|7 21.36 cMStart35,033,595 bp[2]
End35,091,714 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pancreatic epithelial cell

  • pancreatic ductal cell

  • mucosa of ileum

  • oocyte

  • bronchial epithelial cell

  • mucosa of sigmoid colon

  • parotid gland

  • secondary oocyte

  • jejunal mucosa

  • germinal epithelium
Top expressed in
  • secondary oocyte

  • primary oocyte

  • zygote

  • parotid gland

  • submandibular gland

  • epithelium of stomach

  • lacrimal gland

  • left colon

  • migratory enteric neural crest cell

  • vestibular membrane of cochlear duct
More reference expression data
BioGPS
n/a
Orthologs
SpeciesHumanMouse
Entrez

85415

52428

Ensembl

ENSG00000131941

ENSMUSG00000030494

UniProt

Q8IUC4

Q8BWR8

RefSeq (mRNA)

NM_033103

NM_027897

RefSeq (protein)

NP_149094

NP_082173

Location (UCSC)Chr 19: 32.98 – 33.06 MbChr 7: 35.03 – 35.09 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Rhophilin-2 is a protein that in humans is encoded by the RHPN2 gene.[5][6]

Interactions

RHPN2 has been shown to interact with RHOB.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000131941 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000030494 – 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. ^ Peck JW, Oberst M, Bouker KB, Bowden E, Burbelo PD (November 2002). "The RhoA-binding protein, rhophilin-2, regulates actin cytoskeleton organization". J. Biol. Chem. 277 (46): 43924–32. doi:10.1074/jbc.M203569200. PMID 12221077.
  6. ^ "Entrez Gene: RHPN2 rhophilin, Rho GTPase binding protein 2".
  7. ^ Mircescu H, Steuve S, Savonet V, Degraef C, Mellor H, Dumont JE, Maenhaut C, Pirson I (December 2002). "Identification and characterization of a novel activated RhoB binding protein containing a PDZ domain whose expression is specifically modulated in thyroid cells by cAMP" (PDF). Eur. J. Biochem. 269 (24): 6241–9. doi:10.1046/j.1432-1033.2002.03343.x. PMID 12473120. S2CID 23901713.

Further reading

  • Mircescu H, Steuve S, Savonet V, Degraef C, Mellor H, Dumont JE, Maenhaut C, Pirson I (2002). "Identification and characterization of a novel activated RhoB binding protein containing a PDZ domain whose expression is specifically modulated in thyroid cells by cAMP" (PDF). Eur. J. Biochem. 269 (24): 6241–9. doi:10.1046/j.1432-1033.2002.03343.x. PMID 12473120. S2CID 23901713.
  • Jaffe AB, Aspenström P, Hall A (2004). "Human CNK1 acts as a scaffold protein, linking Rho and Ras signal transduction pathways". Mol. Cell. Biol. 24 (4): 1736–46. doi:10.1128/MCB.24.4.1736-1746.2004. PMC 344169. PMID 14749388.
  • Barrios-Rodiles M, Brown KR, Ozdamar B, Bose R, Liu Z, Donovan RS, Shinjo F, Liu Y, Dembowy J, Taylor IW, Luga V, Przulj N, Robinson M, Suzuki H, Hayashizaki Y, Jurisica I, Wrana JL (2005). "High-throughput mapping of a dynamic signaling network in mammalian cells". Science. 307 (5715): 1621–5. Bibcode:2005Sci...307.1621B. doi:10.1126/science.1105776. PMID 15761153. S2CID 39457788.
  • Benzinger A, Muster N, Koch HB, Yates JR, Hermeking H (2005). "Targeted proteomic analysis of 14-3-3 sigma, a p53 effector commonly silenced in cancer". Mol. Cell. Proteomics. 4 (6): 785–95. doi:10.1074/mcp.M500021-MCP200. PMID 15778465.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (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.
  • Zhan X, Desiderio DM (2006). "Nitroproteins from a human pituitary adenoma tissue discovered with a nitrotyrosine affinity column and tandem mass spectrometry". Anal. Biochem. 354 (2): 279–89. doi:10.1016/j.ab.2006.05.024. PMID 16777052.
  • Steuve S, Devosse T, Lauwers E, Vanderwinden JM, André B, Courtoy PJ, Pirson I (2006). "Rhophilin-2 is targeted to late-endosomal structures of the vesicular machinery in the presence of activated RhoB". Exp. Cell Res. 312 (20): 3981–9. doi:10.1016/j.yexcr.2006.08.028. PMID 17054945.
  • Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (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.


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