AP3M1

Protein-coding gene in the species Homo sapiens
AP3M1
Identifiers
AliasesAP3M1, adaptor related protein complex 3 mu 1 subunit, adaptor related protein complex 3 subunit mu 1
External IDsOMIM: 610366; MGI: 1929212; HomoloGene: 22693; GeneCards: AP3M1; OMA:AP3M1 - orthologs
Gene location (Human)
Chromosome 10 (human)
Chr.Chromosome 10 (human)[1]
Chromosome 10 (human)
Genomic location for AP3M1
Genomic location for AP3M1
Band10q22.2Start74,120,255 bp[1]
End74,150,842 bp[1]
Gene location (Mouse)
Chromosome 14 (mouse)
Chr.Chromosome 14 (mouse)[2]
Chromosome 14 (mouse)
Genomic location for AP3M1
Genomic location for AP3M1
Band14 A3|14 11.58 cMStart21,081,510 bp[2]
End21,102,576 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • pancreatic ductal cell

  • mucosa of ileum

  • ganglionic eminence

  • ventricular zone

  • islet of Langerhans

  • smooth muscle tissue

  • rectum

  • tibialis anterior muscle

  • monocyte

  • appendix
Top expressed in
  • ventricular zone

  • secondary oocyte

  • spermatocyte

  • genital tubercle

  • zygote

  • tail of embryo

  • spermatid

  • atrioventricular junction

  • granulocyte

  • lens
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein binding
Cellular component
  • lysosomal membrane
  • Golgi apparatus
  • lysosome
  • cytoplasmic vesicle membrane
  • membrane
  • cytoplasmic vesicle
  • clathrin adaptor complex
  • axon cytoplasm
Biological process
  • anterograde axonal transport
  • protein transport
  • anterograde synaptic vesicle transport
  • protein targeting to lysosome
  • intracellular protein transport
  • vesicle-mediated transport
  • transport
  • viral process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

26985

55946

Ensembl

ENSG00000185009

ENSMUSG00000021824

UniProt

Q9Y2T2

Q9JKC8

RefSeq (mRNA)

NM_012095
NM_207012
NM_001320263
NM_001320264
NM_001320265

NM_018829

RefSeq (protein)

NP_001307192
NP_001307193
NP_001307194
NP_036227
NP_996895

NP_061299

Location (UCSC)Chr 10: 74.12 – 74.15 MbChr 14: 21.08 – 21.1 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

AP-3 complex subunit mu-1 is a protein that in humans is encoded by the AP3M1 gene.[5][6]

The protein encoded by this gene is the medium subunit of AP-3, which is an adaptor-related protein complex associated with the Golgi region as well as more peripheral intracellular structures. AP-3 facilitates the budding of vesicles from the Golgi membrane and may be directly involved in protein sorting to the endosomal/lysosomal system. AP-3 is a heterotetrameric protein complex composed of two large subunits (delta and beta3), a medium subunit (mu3), and a small subunit (sigma 3). Mutations in one of the large subunits of AP-3 have been associated with the Hermansky-Pudlak syndrome, a genetic disorder characterized by defective lysosome-related organelles. Alternatively spliced transcript variants encoding the same protein have been observed.[6]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000185009 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000021824 – 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. ^ Dell'Angelica EC, Shotelersuk V, Aguilar RC, Gahl WA, Bonifacino JS (Mar 1999). "Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor". Mol Cell. 3 (1): 11–21. doi:10.1016/S1097-2765(00)80170-7. PMID 10024875.
  6. ^ a b "Entrez Gene: AP3M1 adaptor-related protein complex 3, mu 1 subunit".

External links

Further reading

  • Odorizzi G, Cowles CR, Emr SD (1998). "The AP-3 complex: a coat of many colours". Trends Cell Biol. 8 (7): 282–8. doi:10.1016/S0962-8924(98)01295-1. PMID 9714600.
  • Geyer M, Fackler OT, Peterlin BM (2001). "Structure--function relationships in HIV-1 Nef". EMBO Rep. 2 (7): 580–5. doi:10.1093/embo-reports/kve141. PMC 1083955. PMID 11463741.
  • Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. doi:10.1101/gr.6.9.791. PMID 8889548.
  • Höning S, Sandoval IV, von Figura K (1998). "A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3". EMBO J. 17 (5): 1304–14. doi:10.1093/emboj/17.5.1304. PMC 1170479. PMID 9482728.
  • Stephens DJ, Banting G (1998). "Specificity of interaction between adaptor-complex medium chains and the tyrosine-based sorting motifs of TGN38 and lgp120". Biochem. J. 335. ( Pt 3) (3): 567–72. doi:10.1042/bj3350567. PMC 1219817. PMID 9794796.
  • Dias Neto E, Correa RG, Verjovski-Almeida S, et al. (2000). "Shotgun sequencing of the human transcriptome with ORF expressed sequence tags". Proc. Natl. Acad. Sci. U.S.A. 97 (7): 3491–6. Bibcode:2000PNAS...97.3491D. doi:10.1073/pnas.97.7.3491. PMC 16267. PMID 10737800.
  • Craig HM, Reddy TR, Riggs NL, et al. (2000). "Interactions of HIV-1 nef with the mu subunits of adaptor protein complexes 1, 2, and 3: role of the dileucine-based sorting motif". Virology. 271 (1): 9–17. doi:10.1006/viro.2000.0277. PMID 10814565.
  • Drake MT, Zhu Y, Kornfeld S (2001). "The assembly of AP-3 adaptor complex-containing clathrin-coated vesicles on synthetic liposomes". Mol. Biol. Cell. 11 (11): 3723–36. doi:10.1091/mbc.11.11.3723. PMC 15032. PMID 11071902.
  • Madrid R, Le Maout S, Barrault MB, et al. (2002). "Polarized trafficking and surface expression of the AQP4 water channel are coordinated by serial and regulated interactions with different clathrin-adaptor complexes". EMBO J. 20 (24): 7008–21. doi:10.1093/emboj/20.24.7008. PMC 125333. PMID 11742978.
  • Jia L, Young MF, Powell J, et al. (2002). "Gene expression profile of human bone marrow stromal cells: high-throughput expressed sequence tag sequencing analysis". Genomics. 79 (1): 7–17. doi:10.1006/geno.2001.6683. PMID 11827452.
  • 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.
  • 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.
  • Suzuki Y, Yamashita R, Shirota M, et al. (2004). "Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions". Genome Res. 14 (9): 1711–8. doi:10.1101/gr.2435604. PMC 515316. PMID 15342556.
  • 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.
  • Coleman SH, Van Damme N, Day JR, et al. (2005). "Leucine-specific, functional interactions between human immunodeficiency virus type 1 Nef and adaptor protein complexes". J. Virol. 79 (4): 2066–78. doi:10.1128/JVI.79.4.2066-2078.2005. PMC 546596. PMID 15681409.


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