APBB1

Last updated
APBB1
Protein APBB1 PDB 2e45.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases APBB1 , amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65), FE65, MGC:9072, RIR, amyloid beta precursor protein binding family B member 1
External IDs OMIM: 602709 MGI: 107765 HomoloGene: 898 GeneCards: APBB1
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001253885
NM_001253886
NM_001253887
NM_009685
NM_001310600

RefSeq (protein)

NP_001240814
NP_001240815
NP_001240816
NP_001297529
NP_033815

Location (UCSC) Chr 11: 6.4 – 6.42 Mb Chr 7: 105.21 – 105.23 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Amyloid beta A4 precursor protein-binding family B member 1 is a protein that in humans is encoded by the APBB1 gene. [5] [6] [7]

Function

The protein encoded by this gene is a member of the Fe65 protein family. It is an adaptor protein localized in the nucleus. It interacts with the Alzheimer's disease amyloid precursor protein (APP), transcription factor CP2/LSF/LBP1 and the low-density lipoprotein receptor-related protein. APP functions as a cytosolic anchoring site that can prevent the gene product's nuclear translocation. This encoded protein could play an important role in the pathogenesis of Alzheimer's disease. It is thought to regulate transcription. Also it is observed to block cell cycle progression by downregulating thymidylate synthase expression. Multiple alternatively spliced transcript variants have been described for this gene but some of their full length sequence is not known. [7]

Interactions

APBB1 has been shown to interact with APLP2, [8] [9] TFCP2, [10] LRP1 [11] and Amyloid precursor protein. [8] [9] [11] [12] [13]

Related Research Articles

<span class="mw-page-title-main">Amyloid-beta precursor protein</span> Mammalian protein found in Homo sapiens

Amyloid-beta 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.

<span class="mw-page-title-main">DAB1</span> Protein-coding gene in the species Homo sapiens

The Disabled-1 (Dab1) gene encodes a key regulator of Reelin signaling. Reelin is a large glycoprotein secreted by neurons of the developing brain, particularly Cajal-Retzius cells. DAB1 functions downstream of Reln in a signaling pathway that controls cell positioning in the developing brain and during adult neurogenesis. It docks to the intracellular part of the Reelin very low density lipoprotein receptor (VLDLR) and apoE receptor type 2 (ApoER2) and becomes tyrosine-phosphorylated following binding of Reelin to cortical neurons. In mice, mutations of Dab1 and Reelin generate identical phenotypes. In humans, Reelin mutations are associated with brain malformations and mental retardation. In mice, Dab1 mutation results in the scrambler mouse phenotype.

<span class="mw-page-title-main">Low-density lipoprotein receptor gene family</span>

The low-density lipoprotein receptor gene family codes for a class of structurally related cell surface receptors that fulfill diverse biological functions in different organs, tissues, and cell types. The role that is most commonly associated with this evolutionarily ancient family is cholesterol homeostasis. In humans, excess cholesterol in the blood is captured by low-density lipoprotein (LDL) and removed by the liver via endocytosis of the LDL receptor. Recent evidence indicates that the members of the LDL receptor gene family are active in the cell signalling pathways between specialized cells in many, if not all, multicellular organisms.

<span class="mw-page-title-main">Gamma secretase</span>

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.

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

Adapter molecule crk also known as proto-oncogene c-Crk is a protein that in humans is encoded by the CRK gene.

<span class="mw-page-title-main">Presenilin-1</span> Protein-coding gene in the species Homo sapiens

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-beta precursor protein (APP). Accumulation of amyloid beta is associated with the onset of Alzheimer's disease.

<span class="mw-page-title-main">IRS2</span> Protein-coding gene in the species Homo sapiens

Insulin receptor substrate 2 is a protein that in humans is encoded by the IRS2 gene.

<span class="mw-page-title-main">MAPK8IP1</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">PSEN2</span> Protein-coding gene in the species Homo sapiens

Presenilin-2 is a protein that is encoded by the PSEN2 gene.

<span class="mw-page-title-main">NCK1</span> Protein-coding gene in the species Homo sapiens

Cytoplasmic protein NCK1 is a protein that in humans is encoded by the NCK1 gene.

<span class="mw-page-title-main">Laminin subunit alpha-1</span> Protein-coding gene in the species Homo sapiens

Laminin subunit alpha-1 is a protein that in humans is encoded by the LAMA1 gene.

<span class="mw-page-title-main">APBA1</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">APLP1</span> Protein-coding gene in the species Homo sapiens

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.

<span class="mw-page-title-main">TFCP2</span> Protein-coding gene in the species Homo sapiens

Alpha-globin transcription factor CP2 is a protein that in humans is encoded by the TFCP2 gene.

<span class="mw-page-title-main">APBA2</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">APBA3</span> Protein-coding gene in the species Homo sapiens

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

<span class="mw-page-title-main">APBB2</span> 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.

<span class="mw-page-title-main">APBB3</span> Protein-coding gene in the species Homo sapiens

Amyloid beta A4 precursor protein-binding family B member 3 is a protein that in humans is encoded by the APBB3 gene.

<span class="mw-page-title-main">Collagen, type XXV, alpha 1</span> Mammalian protein found in Homo sapiens

Collagen alpha-1(XXV) chain is a protein that in humans is encoded by the COL25A1 gene.

<span class="mw-page-title-main">APBB1IP</span> Protein-coding gene in the species Homo sapiens

Amyloid beta A4 precursor protein-binding family B member 1-interacting protein (APBB1IP), also known as APBB1-interacting protein 1 or Rap1-GTP-interacting adapter molecule (RIAM) is a protein that in humans is encoded by the APBB1IP gene.

References

  1. 1 2 3 GRCh38: Ensembl release 89: ENSG00000166313 - Ensembl, May 2017
  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000037032 - 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. McLoughlin DM, Miller CC (Jan 1997). "The intracellular cytoplasmic domain of the Alzheimer's disease amyloid precursor protein interacts with phosphotyrosine-binding domain proteins in the yeast two-hybrid system". FEBS Lett. 397 (2–3): 197–200. doi: 10.1016/S0014-5793(96)01128-3 . PMID   8955346.
  6. Bressler SL, Gray MD, Sopher BL, Hu Q, Hearn MG, Pham DG, Dinulos MB, Fukuchi K, Sisodia SS, Miller MA, Disteche CM, Martin GM (Feb 1997). "cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of the conserved cytoplasmic domains of the human beta-amyloid precursor protein and its homologues with the mouse Fe65 protein". Hum Mol Genet. 5 (10): 1589–98. doi: 10.1093/hmg/5.10.1589 . PMID   8894693.
  7. 1 2 "Entrez Gene: APBB1 amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)".
  8. 1 2 Guénette SY, Chen J, Jondro PD, Tanzi RE (Oct 1996). "Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein". Proceedings of the National Academy of Sciences of the United States of America . 93 (20): 10832–7. Bibcode:1996PNAS...9310832G. doi: 10.1073/pnas.93.20.10832 . PMC   38241 . PMID   8855266.
  9. 1 2 Tanahashi H, Tabira T (Feb 1999). "Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's beta-amyloid precursor protein". Neurosci. Lett. 261 (3): 143–6. doi:10.1016/S0304-3940(98)00995-1. PMID   10081969. S2CID   54307954.
  10. Zambrano N, Minopoli G, de Candia P, Russo T (Aug 1998). "The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1". J. Biol. Chem. 273 (32): 20128–33. doi: 10.1074/jbc.273.32.20128 . PMID   9685356.
  11. 1 2 Trommsdorff M, Borg JP, Margolis B, Herz J (Dec 1998). "Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein". J. Biol. Chem. 273 (50): 33556–60. doi: 10.1074/jbc.273.50.33556 . PMID   9837937.
  12. Borg JP, Ooi J, Levy E, Margolis B (Nov 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.
  13. Zambrano N, Buxbaum JD, Minopoli G, Fiore F, De Candia P, De Renzis S, Faraonio R, Sabo S, Cheetham J, Sudol M, Russo T (Mar 1997). "Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins". J. Biol. Chem. 272 (10): 6399–405. doi: 10.1074/jbc.272.10.6399 . PMID   9045663.

Further reading