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AP1G1

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Protein-coding gene in the species Homo sapiens
AP1G1
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

1IU1

Identifiers
AliasesAP1G1, ADTG, CLAPG1, adaptor related protein complex 1 gamma 1 subunit, adaptor related protein complex 1 subunit gamma 1, USRISD
External IDsOMIM: 603533; MGI: 101919; HomoloGene: 47995; GeneCards: AP1G1; OMA:AP1G1 - orthologs
Gene location (Human)
Chromosome 16 (human)
Chr.Chromosome 16 (human)
Chromosome 16 (human)Genomic location for AP1G1Genomic location for AP1G1
Band16q22.2Start71,729,000 bp
End71,809,201 bp
Gene location (Mouse)
Chromosome 8 (mouse)
Chr.Chromosome 8 (mouse)
Chromosome 8 (mouse)Genomic location for AP1G1Genomic location for AP1G1
Band8 D3|8 57.26 cMStart110,505,186 bp
End110,590,836 bp
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • buccal mucosa cell

  • Achilles tendon

  • epithelium of colon

  • sperm

  • corpus epididymis

  • islet of Langerhans

  • sural nerve

  • left testis

  • middle temporal gyrus

  • right testis
Top expressed in
  • genital tubercle

  • tail of embryo

  • cumulus cell

  • granulocyte

  • neural layer of retina

  • dentate gyrus of hippocampal formation granule cell

  • Paneth cell

  • ventricular zone

  • spermatocyte

  • right kidney
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
Cellular component
Biological process
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

164

11765

Ensembl

ENSG00000166747

ENSMUSG00000031731

UniProt

O43747

P22892

RefSeq (mRNA)

NM_001128
NM_001030007

NM_001301211
NM_009677

RefSeq (protein)

NP_001025178
NP_001119

NP_001288140
NP_033807

Location (UCSC)Chr 16: 71.73 – 71.81 MbChr 8: 110.51 – 110.59 Mb
PubMed search
Wikidata
View/Edit HumanView/Edit Mouse

AP-1 complex subunit gamma-1 is a protein that in humans is encoded by the AP1G1 gene.

Function

Adaptins are important components of clathrin-coated vesicles transporting ligand-receptor complexes from the plasma membrane or from the trans-Golgi network to lysosomes. The adaptin family of proteins is composed of four classes of molecules named alpha, beta-, beta prime- and gamma- adaptins. Adaptins, together with medium and small subunits, form a heterotetrameric complex called an adaptor, whose role is to promote the formation of clathrin-coated pits and vesicles. The protein encoded by this gene is a gamma-adaptin protein and it belongs to the adaptor complexes large subunits family. Two transcript variants encoding different isoforms have been found for this gene.

Interactions

AP1G1 has been shown to interact with:

References

  1. ^ GRCh38: Ensembl release 89: ENSG00000166747Ensembl, May 2017
  2. ^ GRCm38: Ensembl release 89: ENSMUSG00000031731Ensembl, 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. Peyrard M, Parveneh S, Lagercrantz S, Ekman M, Fransson I, Sahlén S, Dumanski JP (Jun 1998). "Cloning, expression pattern, and chromosomal assignment to 16q23 of the human gamma-adaptin gene (ADTG)". Genomics. 50 (2): 275–80. doi:10.1006/geno.1998.5289. PMID 9653655.
  6. ^ Takatsu H, Sakurai M, Shin HW, Murakami K, Nakayama K (Sep 1998). "Identification and characterization of novel clathrin adaptor-related proteins". The Journal of Biological Chemistry. 273 (38): 24693–700. doi:10.1074/jbc.273.38.24693. PMID 9733768.
  7. "Entrez Gene: AP1G1 adaptor-related protein complex 1, gamma 1 subunit".
  8. ^ 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.
  9. ^ Page LJ, Robinson MS (Nov 1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". The Journal of Cell Biology. 131 (3): 619–30. doi:10.1083/jcb.131.3.619. PMC 2120623. PMID 7593184.
  10. ^ Nogi T, Shiba Y, Kawasaki M, Shiba T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Takatsu H, Nakayama K, Wakatsuki S (Jul 2002). "Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain". Nature Structural Biology. 9 (7): 527–31. doi:10.1038/nsb808. PMID 12042876. S2CID 42630285.
  11. Takatsu H, Yoshino K, Nakayama K (May 2000). "Adaptor gamma ear homology domain conserved in gamma-adaptin and GGA proteins that interact with gamma-synergin". Biochemical and Biophysical Research Communications. 271 (3): 719–25. doi:10.1006/bbrc.2000.2700. PMID 10814529.
  12. Mattera R, Ritter B, Sidhu SS, McPherson PS, Bonifacino JS (Feb 2004). "Definition of the consensus motif recognized by gamma-adaptin ear domains". The Journal of Biological Chemistry. 279 (9): 8018–28. doi:10.1074/jbc.M311873200. PMID 14665628.
  13. Mattera R, Arighi CN, Lodge R, Zerial M, Bonifacino JS (Jan 2003). "Divalent interaction of the GGAs with the Rabaptin-5-Rabex-5 complex". The EMBO Journal. 22 (1): 78–88. doi:10.1093/emboj/cdg015. PMC 140067. PMID 12505986.
  14. Horikawa HP, Kneussel M, El Far O, Betz H (Nov 2002). "Interaction of synaptophysin with the AP-1 adaptor protein gamma-adaptin". Molecular and Cellular Neurosciences. 21 (3): 454–62. doi:10.1006/mcne.2002.1191. PMID 12498786. S2CID 54366866.

Further reading

External links

PDB gallery
  • 1gyu: GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1 1gyu: GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1
  • 1gyv: GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1, L762E MUTANT 1gyv: GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1, L762E MUTANT
  • 1gyw: GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1 A753D MUTANT 1gyw: GAMMA-ADAPTIN APPENDAGE DOMAIN FROM CLATHRIN ADAPTOR AP1 A753D MUTANT
  • 1iu1: Crystal structure of human gamma1-adaptin ear domain 1iu1: Crystal structure of human gamma1-adaptin ear domain
  • 1w63: AP1 CLATHRIN ADAPTOR CORE 1w63: AP1 CLATHRIN ADAPTOR CORE
  • 2a7b: On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength 2a7b: On the Routine Use of Soft X-Rays in Macromolecular Crystallography, Part III- The Optimal Data Collection Wavelength
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