APBA1

Last updated
APBA1
Protein APBA1 PDB 1aqc.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases APBA1 , D9S411E, LIN10, MINT1, X11, X11A, X11ALPHA, amyloid beta precursor protein binding family A member 1
External IDs OMIM: 602414 MGI: 1860297 HomoloGene: 897 GeneCards: APBA1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001163

NM_177034

RefSeq (protein)

NP_001154

NP_796008

Location (UCSC) Chr 9: 69.43 – 69.67 Mb Chr 19: 23.74 – 23.93 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Amyloid beta A4 precursor protein-binding family A member 1 is a protein that in humans is encoded by the APBA1 gene. [5] [6] [7]

Contents

Function

The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adaptor protein that interacts with the Alzheimer's disease amyloid precursor protein (APP). It stabilises APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of Alzheimer's disease patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion. [7]

Interactions

APBA1 has been shown to interact with KCNJ12, [8] [9] CCS, [10] CASK [11] [12] and Amyloid precursor protein. [13] [14]

Related Research Articles

Amyloid-beta precursor protein Mammalian protein found in Homo sapiens

Amyloid precursor protein (APP) is an integral membrane protein expressed in many tissues and concentrated in the synapses of neurons. It functions as a cell surface receptor and has been implicated as a regulator of synapse formation, neural plasticity, antimicrobial activity, and iron export. It is coded for by the gene APP and regulated by substrate presentation. APP is best known as the precursor molecule whose proteolysis generates amyloid beta (Aβ), a polypeptide containing 37 to 49 amino acid residues, whose amyloid fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients.

Gamma secretase

Gamma secretase is a multi-subunit protease complex, itself an integral membrane protein, that cleaves single-pass transmembrane proteins at residues within the transmembrane domain. Proteases of this type are known as intramembrane proteases. The most well-known substrate of gamma secretase is amyloid precursor protein, a large integral membrane protein that, when cleaved by both gamma and beta secretase, produces a short 37-43 amino acid peptide called amyloid beta whose abnormally folded fibrillar form is the primary component of amyloid plaques found in the brains of Alzheimer's disease patients. Gamma secretase is also critical in the related processing of several other type I integral membrane proteins, such as Notch, ErbB4, E-cadherin, N-cadherin, ephrin-B2, or CD44.

Erbin (protein) Protein found in humans

Erbb2 interacting protein (ERBB2IP), also known as erbin, is a protein which in humans is encoded by the ERBB2IP gene. Discovered in 1997, erbin is a 200kDa protein containing a PDZ domain.

PSEN1

Presenilin-1 (PS-1) is a presenilin protein that in humans is encoded by the PSEN1 gene. Presenilin-1 is one of the four core proteins in the gamma secretase complex, which is considered to play an important role in generation of amyloid beta (Aβ) from amyloid precursor protein (APP). Accumulation of amyloid beta is associated with the onset of Alzheimer's disease.

DAB2

Disabled homolog 2 is a protein that in humans is encoded by the DAB2 gene.

MAPK8IP1

C-jun-amino-terminal kinase-interacting protein 1 is an enzyme that in humans is encoded by the MAPK8IP1 gene.

CASK Protein-coding gene in the species Homo sapiens

Peripheral plasma membrane protein CASK is a protein that in humans is encoded by the CASK gene. This gene is also known by several other names: CMG 2, calcium/calmodulin-dependent serine protein kinase 3 and membrane-associated guanylate kinase 2.

APBB1

Amyloid beta A4 precursor protein-binding family B member 1 is a protein that in humans is encoded by the APBB1 gene.

AP1B1 Protein-coding gene in the species Homo sapiens

AP-1 complex subunit beta-1 is a protein that in humans is encoded by the AP1B1 gene.

APLP1

Amyloid-like protein 1, also known as APLP1, is a protein that in humans is encoded by the APLP1 gene. APLP1 along with APLP2 are important modulators of glucose and insulin homeostasis.

NRXN1

Neurexin-1-alpha is a protein that in humans is encoded by the NRXN1 gene.

APBA2

Amyloid beta A4 precursor protein-binding family A member 2 is a protein that in humans is encoded by the APBA2 gene.

InaD-like protein Protein-coding gene in the species Homo sapiens

InaD-like protein is a protein that in humans is encoded by the PATJ gene.

Plakophilin-4

Plakophilin-4 is a protein that in humans is encoded by the PKP4 gene.

LIN7A

Lin-7 homolog A is a protein that in humans is encoded by the LIN7A gene.

Synergin gamma 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.

PI4K2A

Phosphatidylinositol 4-kinase 2-alpha is an enzyme that in humans is encoded by the PI4K2A gene.

APBA3

Amyloid beta A4 precursor protein-binding family A member 3 is a protein that in humans is encoded by the APBA3 gene.

APBB2 Protein-coding gene in the species Homo sapiens

Amyloid beta A4 precursor protein-binding family B member 2 is a protein that in humans is encoded by the APBB2 gene.

NECAB3 Protein-coding gene in the species Homo sapiens

N-terminal EF-hand calcium-binding protein 3 is a protein that in humans is encoded by the NECAB3 gene.

References

  1. 1 2 3 ENSG00000276497 GRCh38: Ensembl release 89: ENSG00000107282, ENSG00000276497 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000024897 - 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. Duclos F, Boschert U, Sirugo G, Mandel JL, Hen R, Koenig M (February 1993). "Gene in the region of the Friedreich ataxia locus encodes a putative transmembrane protein expressed in the nervous system". Proc Natl Acad Sci U S A. 90 (1): 109–13. doi: 10.1073/pnas.90.1.109 . PMC   45609 . PMID   7678331.
  6. Duclos F, Koenig M (May 1995). "Comparison of primary structure of a neuron-specific protein, X11, between human and mouse". Mamm Genome. 6 (1): 57–8. doi:10.1007/BF00350899. PMID   7719031. S2CID   20220507.
  7. 1 2 "Entrez Gene: APBA1 amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)".
  8. Leonoudakis D, Conti LR, Anderson S, Radeke CM, McGuire LM, Adams ME, Froehner SC, Yates JR, Vandenberg CA (May 2004). "Protein trafficking and anchoring complexes revealed by proteomic analysis of inward rectifier potassium channel (Kir2.x)-associated proteins". J. Biol. Chem. 279 (21): 22331–46. doi: 10.1074/jbc.M400285200 . PMID   15024025.
  9. Leonoudakis D, Conti LR, Radeke CM, McGuire LM, Vandenberg CA (April 2004). "A multiprotein trafficking complex composed of SAP97, CASK, Veli, and Mint1 is associated with inward rectifier Kir2 potassium channels". J. Biol. Chem. 279 (18): 19051–63. doi: 10.1074/jbc.M400284200 . PMID   14960569.
  10. McLoughlin DM, Standen CL, Lau KF, Ackerley S, Bartnikas TP, Gitlin JD, Miller CC (March 2001). "The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity". J. Biol. Chem. 276 (12): 9303–7. doi: 10.1074/jbc.M010023200 . PMID   11115513.
  11. Borg JP, Straight SW, Kaech SM, de Taddéo-Borg M, Kroon DE, Karnak D, Turner RS, Kim SK, Margolis B (November 1998). "Identification of an evolutionarily conserved heterotrimeric protein complex involved in protein targeting". J. Biol. Chem. 273 (48): 31633–6. doi: 10.1074/jbc.273.48.31633 . PMID   9822620.
  12. Borg JP, Lõpez-Figueroa MO, de Taddèo-Borg M, Kroon DE, Turner RS, Watson SJ, Margolis B (February 1999). "Molecular analysis of the X11-mLin-2/CASK complex in brain". J. Neurosci. 19 (4): 1307–16. doi:10.1523/JNEUROSCI.19-04-01307.1999. PMC   6786035 . PMID   9952408.
  13. Biederer T, Cao X, Südhof TC, Liu X (September 2002). "Regulation of APP-dependent transcription complexes by Mint/X11s: differential functions of Mint isoforms". J. Neurosci. 22 (17): 7340–51. doi:10.1523/JNEUROSCI.22-17-07340.2002. PMC   6757996 . PMID   12196555.
  14. Borg JP, Ooi J, Levy E, Margolis B (November 1996). "The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein". Mol. Cell. Biol. 16 (11): 6229–41. doi:10.1128/mcb.16.11.6229. PMC   231626 . PMID   8887653.

Further reading