AP1M2

Protein-coding gene in the species Homo sapiens
AP1M2
Identifiers
AliasesAP1M2, AP1-mu2, HSMU1B, MU-1B, MU1B, mu2, adaptor related protein complex 1 mu 2 subunit, adaptor related protein complex 1 subunit mu 2
External IDsOMIM: 607309 MGI: 1336974 HomoloGene: 55906 GeneCards: AP1M2
Gene location (Human)
Chromosome 19 (human)
Chr.Chromosome 19 (human)[1]
Chromosome 19 (human)
Genomic location for AP1M2
Genomic location for AP1M2
Band19p13.2Start10,572,671 bp[1]
End10,587,315 bp[1]
Gene location (Mouse)
Chromosome 9 (mouse)
Chr.Chromosome 9 (mouse)[2]
Chromosome 9 (mouse)
Genomic location for AP1M2
Genomic location for AP1M2
Band9 A3|9 7.76 cMStart21,205,571 bp[2]
End21,223,633 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • rectum

  • right lobe of thyroid gland

  • oocyte

  • right uterine tube

  • left lobe of thyroid gland

  • islet of Langerhans

  • body of pancreas

  • kidney

  • minor salivary glands

  • skin of abdomen
Top expressed in
  • pyloric antrum

  • ileum

  • epithelium of stomach

  • upper respiratory tract

  • olfactory epithelium

  • submandibular gland

  • lip

  • duodenum

  • parotid gland

  • colon
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein binding
Cellular component
  • cytosol
  • Golgi apparatus
  • trans-Golgi network membrane
  • intracellular membrane-bounded organelle
  • membrane
  • Golgi membrane
  • lysosomal membrane
  • clathrin-coated vesicle membrane
  • cytoplasmic vesicle membrane
  • cytoplasmic vesicle
  • clathrin adaptor complex
Biological process
  • protein targeting
  • vesicle targeting
  • antigen processing and presentation of exogenous peptide antigen via MHC class II
  • mitigation of host defenses by virus
  • protein transport
  • intracellular protein transport
  • vesicle-mediated transport
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

10053

11768

Ensembl

ENSG00000129354

ENSMUSG00000003309

UniProt

Q9Y6Q5

Q9WVP1

RefSeq (mRNA)

NM_001300887
NM_005498

NM_001110300
NM_009678

RefSeq (protein)

NP_001287816
NP_005489

NP_001103770
NP_033808

Location (UCSC)Chr 19: 10.57 – 10.59 MbChr 9: 21.21 – 21.22 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

AP-1 complex subunit mu-2 is a protein that in humans is encoded by the AP1M2 gene.[5][6]

Function

This gene encodes a subunit of the heterotetrameric adaptor-related protein complex 1 (AP-1), which belongs to the adaptor complexes medium subunits family. This protein is capable of interacting with tyrosine-based sorting signals.[6]

Interactions

AP1M2 has been shown to interact with AP2B1.[7]

References

  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000129354 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000003309 – 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. ^ Ohno H, Tomemori T, Nakatsu F, Okazaki Y, Aguilar RC, Foelsch H, Mellman I, Saito T, Shirasawa T, Bonifacino JS (Apr 1999). "Mu1B, a novel adaptor medium chain expressed in polarized epithelial cells". FEBS Letters. 449 (2–3): 215–20. doi:10.1016/S0014-5793(99)00432-9. PMID 10338135. S2CID 82686795.
  6. ^ a b "Entrez Gene: AP1M2 adaptor-related protein complex 1, mu 2 subunit".
  7. ^ 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 (Oct 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.

Further reading

  • Hirst J, Robinson MS (Aug 1998). "Clathrin and adaptors". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1404 (1–2): 173–93. doi:10.1016/S0167-4889(98)00056-1. PMID 9714795.
  • Ohno H, Stewart J, Fournier MC, Bosshart H, Rhee I, Miyatake S, Saito T, Gallusser A, Kirchhausen T, Bonifacino JS (Sep 1995). "Interaction of tyrosine-based sorting signals with clathrin-associated proteins". Science. 269 (5232): 1872–5. Bibcode:1995Sci...269.1872O. doi:10.1126/science.7569928. PMID 7569928.
  • Maruyama K, Sugano S (Jan 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.
  • Seaman MN, Sowerby PJ, Robinson MS (Oct 1996). "Cytosolic and membrane-associated proteins involved in the recruitment of AP-1 adaptors onto the trans-Golgi network". The Journal of Biological Chemistry. 271 (41): 25446–51. doi:10.1074/jbc.271.41.25446. PMID 8810314.
  • Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (Oct 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.
  • Stephens DJ, Banting G (Nov 1998). "Specificity of interaction between adaptor-complex medium chains and the tyrosine-based sorting motifs of TGN38 and lgp120". The Biochemical Journal. 335 (3): 567–72. doi:10.1042/bj3350567. PMC 1219817. PMID 9794796.
  • Berlioz-Torrent C, Shacklett BL, Erdtmann L, Delamarre L, Bouchaert I, Sonigo P, Dokhelar MC, Benarous R (Feb 1999). "Interactions of the cytoplasmic domains of human and simian retroviral transmembrane proteins with components of the clathrin adaptor complexes modulate intracellular and cell surface expression of envelope glycoproteins". Journal of Virology. 73 (2): 1350–61. doi:10.1128/JVI.73.2.1350-1361.1999. PMC 103959. PMID 9882340.
  • Fölsch H, Ohno H, Bonifacino JS, Mellman I (Oct 1999). "A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells". Cell. 99 (2): 189–98. doi:10.1016/S0092-8674(00)81650-5. PMID 10535737. S2CID 15288582.
  • Nakatsu F, Kadohira T, Gilbert DJ, Jenkins NA, Kakuta H, Copeland NG, Saito T, Ohno H (2000). "Genomic structure and chromosome mapping of the genes encoding clathrin-associated adaptor medium chains mu1A (Ap1m1) and mu1B (Ap1m2)". Cytogenetics and Cell Genetics. 87 (1–2): 53–8. doi:10.1159/000015391. PMID 10640811. S2CID 84417943.
  • Umeda A, Meyerholz A, Ungewickell E (May 2000). "Identification of the universal cofactor (auxilin 2) in clathrin coat dissociation". European Journal of Cell Biology. 79 (5): 336–42. doi:10.1078/S0171-9335(04)70037-0. PMID 10887964.
  • Fölsch H, Pypaert M, Schu P, Mellman I (Feb 2001). "Distribution and function of AP-1 clathrin adaptor complexes in polarized epithelial cells". The Journal of Cell Biology. 152 (3): 595–606. doi:10.1083/jcb.152.3.595. PMC 2195989. PMID 11157985.
  • Wyss S, Berlioz-Torrent C, Boge M, Blot G, Höning S, Benarous R, Thali M (Mar 2001). "The highly conserved C-terminal dileucine motif in the cytosolic domain of the human immunodeficiency virus type 1 envelope glycoprotein is critical for its association with the AP-1 clathrin adaptor [correction of adapter]". Journal of Virology. 75 (6): 2982–92. doi:10.1128/JVI.75.6.2982-2992.2001. PMC 115924. PMID 11222723.
  • Ohka S, Ohno H, Tohyama K, Nomoto A (Oct 2001). "Basolateral sorting of human poliovirus receptor alpha involves an interaction with the mu1B subunit of the clathrin adaptor complex in polarized epithelial cells". Biochemical and Biophysical Research Communications. 287 (4): 941–8. doi:10.1006/bbrc.2001.5660. PMID 11573956.
  • Korolchuk VI, Banting G (Jun 2002). "CK2 and GAK/auxilin2 are major protein kinases in clathrin-coated vesicles". Traffic. 3 (6): 428–39. doi:10.1034/j.1600-0854.2002.30606.x. PMID 12010461. S2CID 34467416.
  • Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ (May 2002). "Molecular architecture and functional model of the endocytic AP2 complex". Cell. 109 (4): 523–35. doi:10.1016/S0092-8674(02)00735-3. PMID 12086608. S2CID 483953.
  • Sugimoto H, Sugahara M, Fölsch H, Koide Y, Nakatsu F, Tanaka N, Nishimura T, Furukawa M, Mullins C, Nakamura N, Mellman I, Ohno H (Jul 2002). "Differential recognition of tyrosine-based basolateral signals by AP-1B subunit mu1B in polarized epithelial cells". Molecular Biology of the Cell. 13 (7): 2374–82. doi:10.1091/mbc.E01-10-0096. PMC 117320. PMID 12134076.

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