RPH3AL

Protein-coding gene in the species Homo sapiens
RPH3AL
Identifiers
AliasesRPH3AL, NOC2, rabphilin 3A-like (without C2 domains), rabphilin 3A like (without C2 domains)
External IDsOMIM: 604881; MGI: 1923492; HomoloGene: 5078; GeneCards: RPH3AL; OMA:RPH3AL - orthologs
Gene location (Human)
Chromosome 17 (human)
Chr.Chromosome 17 (human)[1]
Chromosome 17 (human)
Genomic location for RPH3AL
Genomic location for RPH3AL
Band17p13.3Start212,389 bp[1]
End386,254 bp[1]
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[2]
Chromosome 11 (mouse)
Genomic location for RPH3AL
Genomic location for RPH3AL
Band11|11 B5Start75,721,825 bp[2]
End75,829,255 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • anterior pituitary

  • islet of Langerhans

  • right adrenal gland

  • left adrenal cortex

  • sural nerve

  • right adrenal cortex

  • right lobe of liver

  • gonad

  • right lobe of thyroid gland
Top expressed in
  • primary oocyte

  • islet of Langerhans

  • zygote

  • epithelium of stomach

  • secondary oocyte

  • otolith organ

  • utricle

  • pituitary gland

  • Paneth cell

  • external carotid artery
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • calcium ion binding
  • metal ion binding
  • cytoskeletal protein binding
  • protein binding
  • calcium-dependent phospholipid binding
  • LIM domain binding
Cellular component
  • cytoplasm
  • secretory granule membrane
  • membrane
  • transport vesicle membrane
  • secretory granule
  • cytoplasmic vesicle
  • plasma membrane
  • intracellular anatomical structure
Biological process
  • glucose homeostasis
  • regulation of exocytosis
  • positive regulation of protein secretion
  • intracellular protein transport
  • negative regulation of G protein-coupled receptor signaling pathway
  • exocytosis
  • regulation of calcium ion-dependent exocytosis
  • positive regulation of insulin secretion
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

9501

380714

Ensembl

ENSG00000181031
ENSG00000262334
ENSG00000282013

ENSMUSG00000020847

UniProt

Q9UNE2

Q768S4

RefSeq (mRNA)

NM_001190411
NM_001190412
NM_001190413
NM_006987

NM_001291159
NM_029548

RefSeq (protein)

NP_001177340
NP_001177341
NP_001177342
NP_008918

NP_001278088
NP_083824

Location (UCSC)Chr 17: 0.21 – 0.39 MbChr 11: 75.72 – 75.83 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Rab effector Noc2 is a protein that in humans is encoded by the RPH3AL gene.[5][6]

Interactions

RPH3AL has been shown to interact with RAB27A.[7][8]

References

  1. ^ a b c ENSG00000262334, ENSG00000282013 GRCh38: Ensembl release 89: ENSG00000181031, ENSG00000262334, ENSG00000282013 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000020847 – 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. ^ Smith JS, Tachibana I, Allen C, Chiappa SA, Lee HK, McIver B, Jenkins RB, Raffel C (July 1999). "Cloning of a human ortholog (RPH3AL) of (RNO)Rph3al from a candidate 17p13.3 medulloblastoma tumor suppressor locus". Genomics. 59 (1): 97–101. doi:10.1006/geno.1999.5864. PMID 10395805.
  6. ^ "Entrez Gene: RPH3AL rabphilin 3A-like (without C2 domains)".
  7. ^ Cheviet S, Coppola T, Haynes LP, Burgoyne RD, Regazzi R (January 2004). "The Rab-binding protein Noc2 is associated with insulin-containing secretory granules and is essential for pancreatic beta-cell exocytosis". Molecular Endocrinology. 18 (1): 117–26. doi:10.1210/me.2003-0300. PMID 14593078.
  8. ^ Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". The Journal of Biological Chemistry. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.

Further reading

  • Kotake K, Ozaki N, Mizuta M, Sekiya S, Inagaki N, Seino S (November 1997). "Noc2, a putative zinc finger protein involved in exocytosis in endocrine cells". The Journal of Biological Chemistry. 272 (47): 29407–10. doi:10.1074/jbc.272.47.29407. PMID 9367993.
  • Fenster SD, Chung WJ, Zhai R, Cases-Langhoff C, Voss B, Garner AM, Kaempf U, Kindler S, Gundelfinger ED, Garner CC (January 2000). "Piccolo, a presynaptic zinc finger protein structurally related to bassoon". Neuron. 25 (1): 203–14. doi:10.1016/S0896-6273(00)80883-1. PMID 10707984. S2CID 10177138.
  • Haynes LP, Evans GJ, Morgan A, Burgoyne RD (March 2001). "A direct inhibitory role for the Rab3-specific effector, Noc2, in Ca2+-regulated exocytosis in neuroendocrine cells". The Journal of Biological Chemistry. 276 (13): 9726–32. doi:10.1074/jbc.M006959200. PMID 11134008.
  • Goi T, Takeuchi K, Katayama K, Hirose K, Yamaguchi A (2003). "Mutations of rabphillin-3A-like gene in colorectal cancers". Oncology Reports. 9 (6): 1189–92. doi:10.3892/or.9.6.1189. PMID 12375017.
  • Milkereit P, Strauss D, Bassler J, Gadal O, Kühn H, Schütz S, Gas N, Lechner J, Hurt E, Tschochner H (February 2003). "A Noc complex specifically involved in the formation and nuclear export of ribosomal 40 S subunits". The Journal of Biological Chemistry. 278 (6): 4072–81. doi:10.1074/jbc.M208898200. PMID 12446671.
  • Fukuda M (April 2003). "Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2". The Journal of Biological Chemistry. 278 (17): 15373–80. doi:10.1074/jbc.M212341200. PMID 12578829.
  • Cardoso C, Leventer RJ, Ward HL, Toyo-Oka K, Chung J, Gross A, Martin CL, Allanson J, Pilz DT, Olney AH, Mutchinick OM, Hirotsune S, Wynshaw-Boris A, Dobyns WB, Ledbetter DH (April 2003). "Refinement of a 400-kb critical region allows genotypic differentiation between isolated lissencephaly, Miller-Dieker syndrome, and other phenotypes secondary to deletions of 17p13.3". American Journal of Human Genetics. 72 (4): 918–30. doi:10.1086/374320. PMC 1180354. PMID 12621583.
  • Cheviet S, Coppola T, Haynes LP, Burgoyne RD, Regazzi R (January 2004). "The Rab-binding protein Noc2 is associated with insulin-containing secretory granules and is essential for pancreatic beta-cell exocytosis". Molecular Endocrinology. 18 (1): 117–26. doi:10.1210/me.2003-0300. PMID 14593078.
  • Manabe S, Nishimura N, Yamamoto Y, Kitamura H, Morimoto S, Imai M, Nagahiro S, Seino S, Sasaki T (March 2004). "Identification and characterization of Noc2 as a potential Rab3B effector protein in epithelial cells". Biochemical and Biophysical Research Communications. 316 (1): 218–25. doi:10.1016/j.bbrc.2004.02.026. PMID 15003533.
  • Matsumoto M, Miki T, Shibasaki T, Kawaguchi M, Shinozaki H, Nio J, Saraya A, Koseki H, Miyazaki M, Iwanaga T, Seino S (June 2004). "Noc2 is essential in normal regulation of exocytosis in endocrine and exocrine cells". Proceedings of the National Academy of Sciences of the United States of America. 101 (22): 8313–8. Bibcode:2004PNAS..101.8313M. doi:10.1073/pnas.0306709101. PMC 420391. PMID 15159548.
  • Katkoori VR, Jia X, Chatla C, Kumar S, Ponnazhagan S, Callens T, Messiaen L, Grizzle WE, Manne U (January 2008). "Clinical significance of a novel single nucleotide polymorphism in the 5' untranslated region of the Rabphillin-3A-Like gene in colorectal adenocarcinoma". Frontiers in Bioscience. 13 (1): 1050–61. doi:10.2741/2742. PMC 2667692. PMID 17981610.


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