AP1B1

Last updated
AP1B1
PDB 1w63 EBI.jpg
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases AP1B1 , ADTB1, AP105A, BAM22, CLAPB2, adaptor related protein complex 1 beta 1 subunit, adaptor related protein complex 1 subunit beta 1, KIDAR
External IDs OMIM: 600157; MGI: 1096368; HomoloGene: 21972; GeneCards: AP1B1; OMA:AP1B1 - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_145730
NM_001127
NM_001166019

NM_001243043
NM_001243044
NM_007454
NM_001355659
NM_001355660

Contents

RefSeq (protein)

NP_001229972
NP_001229973
NP_031480
NP_001342588
NP_001342589

Location (UCSC) Chr 22: 29.33 – 29.42 Mb Chr 11: 4.94 – 4.99 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

AP-1 complex subunit beta-1 is a protein that in humans is encoded by the AP1B1 gene. [5] [6] [7]

Adaptor protein complex 1 is found at the cytoplasmic face of coated vesicles located at the Golgi complex, where it mediates both the recruitment of clathrin to the membrane and the recognition of sorting signals within the cytosolic tails of transmembrane receptors. This complex is a heterotetramer composed of two large, one medium, and one small adaptin subunit. The protein encoded by this gene serves as one of the large subunits of this complex and is a member of the adaptin protein family. [8] This gene is a candidate meningioma gene. Two transcript variants encoding different isoforms have been found for this gene, and variants utilizing alternative polyadenylation signals exist. [7]

Interactions

AP1B1 has been shown to interact with KIF13A [9] and AP1G1. [10] [11] [12]

Related Research Articles

<span class="mw-page-title-main">Vesicular transport adaptor protein</span>

Vesicular transport adaptor proteins are proteins involved in forming complexes that function in the trafficking of molecules from one subcellular location to another. These complexes concentrate the correct cargo molecules in vesicles that bud or extrude off of one organelle and travel to another location, where the cargo is delivered. While some of the details of how these adaptor proteins achieve their trafficking specificity has been worked out, there is still much to be learned.

<span class="mw-page-title-main">GGA1</span> Protein-coding gene in the species Homo sapiens

ADP-ribosylation factor-binding protein GGA1 is a protein that in humans is encoded by the GGA1 gene.

<span class="mw-page-title-main">AP2M1</span> Protein-coding gene in the species Homo sapiens

AP-2 complex subunit mu is a protein that in humans is encoded by the AP2M1 gene.

<span class="mw-page-title-main">COPB1</span> Protein-coding gene in humans

Coatomer subunit beta is a protein that in humans is encoded by the COPB1 gene.

<span class="mw-page-title-main">Adaptor-related protein complex 2, alpha 1</span> Protein-coding gene in the species Homo sapiens

AP-2 complex subunit alpha-1 is a protein that in humans is encoded by the AP2A1 gene.

<span class="mw-page-title-main">AP1M1</span> Protein-coding gene in the species Homo sapiens

AP-1 complex subunit mu-1 is a protein that in humans is encoded by the AP1M1 gene.

<span class="mw-page-title-main">AP1G1</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">CLTC</span> Protein-coding gene in the species Homo sapiens

Clathrin heavy chain 1 is a protein that in humans is encoded by the CLTC gene.

<span class="mw-page-title-main">AP2B1</span> Protein-coding gene in the species Homo sapiens

AP-2 complex subunit beta is a protein that in humans is encoded by the AP2B1 gene.

<span class="mw-page-title-main">AP3D1</span> Protein-coding gene in the species Homo sapiens

AP-3 complex subunit delta-1 is a protein that in humans is encoded by the AP3D1 gene.

<span class="mw-page-title-main">AP1S1</span> Protein-coding gene in the species Homo sapiens

AP-1 complex subunit sigma-1A is a protein that in humans is encoded by the AP1S1 gene.

<span class="mw-page-title-main">COPG2</span> Protein-coding gene in humans

Coatomer subunit gamma-2 is a protein that in humans is encoded by the COPG2 gene.

<span class="mw-page-title-main">AP1G2</span> Protein-coding gene in the species Homo sapiens

AP-1 complex subunit gamma-like 2 is a protein that in humans is encoded by the AP1G2 gene.

<span class="mw-page-title-main">AP3M1</span> Protein-coding gene in humans

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

<span class="mw-page-title-main">AP1S2</span> Protein-coding gene in humans

AP-1 complex subunit sigma-2 is a protein that in humans is encoded by the AP1S2 gene.

<span class="mw-page-title-main">Synergin gamma</span> Protein-coding gene in the species Homo sapiens

Synergin gamma also known as AP1 subunit gamma-binding protein 1 (AP1GBP1) is a protein that in humans is encoded by the SYNRG gene.

<span class="mw-page-title-main">AP3S2</span> Protein-coding gene in the species Homo sapiens

AP-3 complex subunit sigma-2 is a protein that in humans is encoded by the AP3S2 gene.

<span class="mw-page-title-main">AP2S1</span> Protein-coding gene in the species Homo sapiens

AP-2 complex subunit sigma is a protein that in humans is encoded by the AP2S1 gene.

Clathrin adaptor proteins, also known as adaptins, are vesicular transport adaptor proteins associated with clathrin. The association between adaptins and clathrin are important for vesicular cargo selection and transporting. Clathrin coats contain both clathrin and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Therefore, adaptor proteins are responsible for the recruitment of cargo molecules into a growing clathrin-coated pits. The two major types of clathrin adaptor complexes are the heterotetrameric vesicular transport adaptor proteins (AP1-5), and the monomeric GGA adaptors. Adaptins are distantly related to the other main type of vesicular transport proteins, the coatomer subunits, sharing between 16% and 26% of their amino acid sequence.

<span class="mw-page-title-main">Beta2-adaptin C-terminal domain</span>

The C-terminal domain ofBeta2-adaptin is a protein domain is involved in cell trafficking by aiding import and export of substances in and out of the cell.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000100280 Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000009090 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. Peyrard M, Fransson I, Xie YG, Han FY, Ruttledge MH, Swahn S, Collins JE, Dunham I, Collins VP, Dumanski JP (January 1995). "Characterization of a new member of the human beta-adaptin gene family from chromosome 22q12, a candidate meningioma gene". Hum Mol Genet. 3 (8): 1393–9. doi:10.1093/hmg/3.8.1393. PMID   7987321.
  6. Peyrard M, Pan HQ, Kedra D, Fransson I, Swahn S, Hartman K, Clifton SW, Roe BA, Dumanski JP (February 1997). "Structure of the promoter and genomic organization of the human beta'-adaptin gene (BAM22) from chromosome 22q12". Genomics. 36 (1): 112–7. doi:10.1006/geno.1996.0431. PMID   8812422.
  7. 1 2 "Entrez Gene: AP1B1 adaptor-related protein complex 1, beta 1 subunit".
  8. "AP1S1 adaptor related protein complex 1 subunit sigma 1 [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved 2024-11-30.
  9. Nakagawa, T; Setou M; Seog D; Ogasawara K; Dohmae N; Takio K; Hirokawa N (November 2000). "A novel motor, KIF13A, transports mannose-6-phosphate receptor to plasma membrane through direct interaction with AP-1 complex". Cell. 103 (4). UNITED STATES: 569–81. doi: 10.1016/S0092-8674(00)00161-6 . ISSN   0092-8674. PMID   11106728.
  10. Takatsu, H; Sakurai M; Shin H W; Murakami K; Nakayama K (September 1998). "Identification and characterization of novel clathrin adaptor-related proteins". J. Biol. Chem. 273 (38). UNITED STATES: 24693–700. doi: 10.1074/jbc.273.38.24693 . ISSN   0021-9258. PMID   9733768.
  11. Fölsch, H; Ohno H; Bonifacino J S; Mellman I (October 1999). "A novel clathrin adaptor complex mediates basolateral targeting in polarized epithelial cells". Cell. 99 (2). UNITED STATES: 189–98. doi: 10.1016/S0092-8674(00)81650-5 . ISSN   0092-8674. PMID   10535737.
  12. Page, L J; Robinson M S (November 1995). "Targeting signals and subunit interactions in coated vesicle adaptor complexes". J. Cell Biol. 131 (3). UNITED STATES: 619–30. doi:10.1083/jcb.131.3.619. ISSN   0021-9525. PMC   2120623 . PMID   7593184.

Further reading