APBB1

APBB1
	REnderização baseada em PDB 2e45.
Estruturas disponíveis
PDB	Busca de ortólogos: PDBe, RCSB
Lista de códigos PDB
	2E45, 2HO2, 2IDH, 2OEI, 3D8D, 3D8E, 3D8F, 3DXC, 3DXD, 3DXE
Identificadores
Símbolos	APBB1; FE65; MGC:9072; RIR
IDs externos	OMIM: 602709 MGI: 107765 HomoloGene: 898 GeneCards: APBB1 Gene
Ontologia do gene
Função molecular	•beta-amyloid binding; •chromatin binding; •protein binding; •transcription factor binding; •histone binding; •proline-rich region binding;
Componente celular	•núcleo; •citoplasma; •membrana plasmática; •nuclear speck; •lamellipodium; •growth cone; •presynaptic membrane; •dendritic spine; •protein complex; •synapse; •postsynaptic membrane; •perinuclear region of cytoplasm;
Processo biológico	•neuron migration; •reparação de quebras em cadeia dupla; •transcription, DNA-dependent; •regulation of transcription, DNA-dependent; •apoptotic process; •response to DNA damage stimulus; •paragem do ciclo celular; •signal transduction; •axonogenesis; •axon guidance; •visual learning; •response to iron ion; •extracellular matrix organization; •negative regulation of cell growth; •positive regulation of apoptotic process; •histone H4 acetylation; •negative regulation of neuron differentiation; •positive regulation of DNA repair; •negative regulation of S phase of mitotic cell cycle; •positive regulation of transcription, DNA-dependent; •positive regulation of transcription from RNA polymerase II promoter; •positive regulation of protein secretion; •negative regulation of thymidylate synthase biosynthetic process;
	Sources: Amigo / QuickGO
Padrões de expressão do ARN
	Mais dados de expressão
Ortólogos
	v; d; e;

APBB1 (do inglês: Amyloid beta A4 precursor protein-binding family B member 1) é uma proteína que nos humanos é codificada pelo gene com o mesmo nome.^[1]^[2]^[3]

A proteína codificada por este gene é um dos membros da família proteíca Fe65. É uma proteína adaptadora localização no núcleo celular. Interage com a proteína APP (Alzheimer's disease amyloid precursor protein), com o factor de transcrição CP2/LSF/LBP1 e com a proteína relacionada com o receptor da lipoproteína de baixa densidade (LDLr). A APP funciona como local de ancoragem no citosol que pode prevenir a translocação nuclear dos produtos genéticos. Esta proteína codificada pode desempenhar um importante papel na patogénese da doença de Alzheimer. Pensa-se que possa regular a transcrição. É também observado bloquear a progressão do ciclo celular por infrarregulação de expressão de timidilato sintase.^[3]

Interações

Foi mostrado que a APBB1 interage com APLP2,^[4]^[5] TFCP2,^[6] LRP1^[7] e proteína precursora amilóide.^[4]^[5]^[7]^[8]^[9]

Referências

↑ McLoughlin DM, Miller CC (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. PMID 8955346. doi:10.1016/S0014-5793(96)01128-3
↑ Bressler SL, Gray MD, Sopher BL, Hu Q, Hearn MG, Pham DG, Dinulos MB, Fukuchi K, Sisodia SS, Miller MA, Disteche CM, Martin GM (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. PMID 8894693. doi:10.1093/hmg/5.10.1589
↑ ^a ^b «Entrez Gene: APBB1 amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)»
↑ ^a ^b Guénette, S Y; Chen J, Jondro P D, Tanzi R E (1996). «Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 93 (20): 10832–7. ISSN 0027-8424. PMC 38241. PMID 8855266. doi:10.1073/pnas.93.20.10832
↑ ^a ^b Tanahashi, H; Tabira T (1999). «Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's beta-amyloid precursor protein». IRELAND. Neurosci. Lett. 261 (3): 143–6. ISSN 0304-3940. PMID 10081969. doi:10.1016/S0304-3940(98)00995-1
↑ Zambrano, N; Minopoli G, de Candia P, Russo T (1998). «The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1». UNITED STATES. J. Biol. Chem. 273 (32): 20128–33. ISSN 0021-9258. PMID 9685356. doi:10.1074/jbc.273.32.20128
↑ ^a ^b Trommsdorff, M; Borg J P, Margolis B, Herz J (1998). «Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein». UNITED STATES. J. Biol. Chem. 273 (50): 33556–60. ISSN 0021-9258. PMID 9837937. doi:10.1074/jbc.273.50.33556
↑ Borg, J P; Ooi J, Levy E, Margolis B (1996). «The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein». UNITED STATES. Mol. Cell. Biol. 16 (11): 6229–41. ISSN 0270-7306. PMC 231626. PMID 8887653
↑ Zambrano, N; Buxbaum J D, Minopoli G, Fiore F, De Candia P, De Renzis S, Faraonio R, Sabo S, Cheetham J, Sudol M, Russo T (1997). «Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins». UNITED STATES. J. Biol. Chem. 272 (10): 6399–405. ISSN 0021-9258. PMID 9045663. doi:10.1074/jbc.272.10.6399

Leitura adicional

Russo T, Faraonio R, Minopoli G,; et al. (1998). «Fe65 and the protein network centered around the cytosolic domain of the Alzheimer's beta-amyloid precursor protein». FEBS Lett. 434 (1–2): 1–7. PMID 9738440. doi:10.1016/S0014-5793(98)00941-7
Askanas V, Engel WK (2004). «Proposed pathogenetic cascade of inclusion-body myositis: importance of amyloid-beta, misfolded proteins, predisposing genes, and aging». Current opinion in rheumatology. 15 (6): 737–44. PMID 14569203. doi:10.1097/00002281-200311000-00009
Borg JP, Ooi J, Levy E, Margolis B (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. PMC 231626. PMID 8887653
Zambrano N, Buxbaum JD, Minopoli G,; et al. (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. PMID 9045663. doi:10.1074/jbc.272.10.6399
Ermekova KS, Zambrano N, Linn H,; et al. (1998). «The WW domain of neural protein FE65 interacts with proline-rich motifs in Mena, the mammalian homolog of Drosophila enabled». J. Biol. Chem. 272 (52): 32869–77. PMID 9407065. doi:10.1074/jbc.272.52.32869
Duilio A, Faraonio R, Minopoli G,; et al. (1998). «Fe65L2: a new member of the Fe65 protein family interacting with the intracellular domain of the Alzheimer's beta-amyloid precursor protein». Biochem. J. 330 ( Pt 1) (Pt 1): 513–9. PMC 1219167. PMID 9461550
Blanco G, Irving NG, Brown SD,; et al. (1998). «Mapping of the human and murine X11-like genes (APBA2 and apba2), the murine Fe65 gene (Apbb1), and the human Fe65-like gene (APBB2): genes encoding phosphotyrosine-binding domain proteins that interact with the Alzheimer's disease amyloid precursor protein». Mamm. Genome. 9 (6): 473–5. PMID 9585438. doi:10.1007/s003359900800
Zambrano N, Minopoli G, de Candia P, Russo T (1998). «The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1». J. Biol. Chem. 273 (32): 20128–33. PMID 9685356. doi:10.1074/jbc.273.32.20128
Hu Q, Kukull WA, Bressler SL,; et al. (1998). «The human FE65 gene: genomic structure and an intronic biallelic polymorphism associated with sporadic dementia of the Alzheimer type». Hum. Genet. 103 (3): 295–303. PMID 9799084. doi:10.1007/s004390050820
Trommsdorff M, Borg JP, Margolis B, Herz J (1999). «Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein». J. Biol. Chem. 273 (50): 33556–60. PMID 9837937. doi:10.1074/jbc.273.50.33556
Sabo SL, Lanier LM, Ikin AF,; et al. (1999). «Regulation of beta-amyloid secretion by FE65, an amyloid protein precursor-binding protein». J. Biol. Chem. 274 (12): 7952–7. PMID 10075692. doi:10.1074/jbc.274.12.7952
Hu Q, Hearn MG, Jin LW,; et al. (2000). «Alternatively spliced isoforms of FE65 serve as neuron-specific and non-neuronal markers». J. Neurosci. Res. 58 (5): 632–40. PMID 10561691. doi:10.1002/(SICI)1097-4547(19991201)58:5<632::AID-JNR4>3.0.CO;2-P
Lambrechts A, Kwiatkowski AV, Lanier LM,; et al. (2000). «cAMP-dependent protein kinase phosphorylation of EVL, a Mena/VASP relative, regulates its interaction with actin and SH3 domains». J. Biol. Chem. 275 (46): 36143–51. PMID 10945997. doi:10.1074/jbc.M006274200
Minopoli G, de Candia P, Bonetti A,; et al. (2001). «The beta-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation». J. Biol. Chem. 276 (9): 6545–50. PMID 11085987. doi:10.1074/jbc.M007340200
Lau KF, McLoughlin DM, Standen CL,; et al. (2001). «Fe65 and X11beta co-localize with and compete for binding to the amyloid precursor protein». Neuroreport. 11 (16): 3607–10. PMID 11095528. doi:10.1097/00001756-200011090-00041
McLoughlin DM, Standen CL, Lau KF,; et al. (2001). «The neuronal adaptor protein X11alpha interacts with the copper chaperone for SOD1 and regulates SOD1 activity». J. Biol. Chem. 276 (12): 9303–7. PMID 11115513. doi:10.1074/jbc.M010023200
Zambrano N, Bruni P, Minopoli G,; et al. (2001). «The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene». J. Biol. Chem. 276 (23): 19787–92. PMID 11279131. doi:10.1074/jbc.M100792200

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[pmid8955346-1] McLoughlin DM, Miller CC (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. PMID 8955346. doi:10.1016/S0014-5793(96)01128-3

[pmid8894693-2] Bressler SL, Gray MD, Sopher BL, Hu Q, Hearn MG, Pham DG, Dinulos MB, Fukuchi K, Sisodia SS, Miller MA, Disteche CM, Martin GM (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. PMID 8894693. doi:10.1093/hmg/5.10.1589

[entrez-3] «Entrez Gene: APBB1 amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65)»

[pmid8855266-4] Guénette, S Y; Chen J, Jondro P D, Tanzi R E (1996). «Association of a novel human FE65-like protein with the cytoplasmic domain of the beta-amyloid precursor protein». UNITED STATES. Proc. Natl. Acad. Sci. U.S.A. 93 (20): 10832–7. ISSN 0027-8424. PMC 38241. PMID 8855266. doi:10.1073/pnas.93.20.10832

[pmid10081969-5] Tanahashi, H; Tabira T (1999). «Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's beta-amyloid precursor protein». IRELAND. Neurosci. Lett. 261 (3): 143–6. ISSN 0304-3940. PMID 10081969. doi:10.1016/S0304-3940(98)00995-1

[pmid9685356-6] Zambrano, N; Minopoli G, de Candia P, Russo T (1998). «The Fe65 adaptor protein interacts through its PID1 domain with the transcription factor CP2/LSF/LBP1». UNITED STATES. J. Biol. Chem. 273 (32): 20128–33. ISSN 0021-9258. PMID 9685356. doi:10.1074/jbc.273.32.20128

[pmid9837937-7] Trommsdorff, M; Borg J P, Margolis B, Herz J (1998). «Interaction of cytosolic adaptor proteins with neuronal apolipoprotein E receptors and the amyloid precursor protein». UNITED STATES. J. Biol. Chem. 273 (50): 33556–60. ISSN 0021-9258. PMID 9837937. doi:10.1074/jbc.273.50.33556

[pmid8887653-8] Borg, J P; Ooi J, Levy E, Margolis B (1996). «The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein». UNITED STATES. Mol. Cell. Biol. 16 (11): 6229–41. ISSN 0270-7306. PMC 231626. PMID 8887653

[pmid9045663-9] Zambrano, N; Buxbaum J D, Minopoli G, Fiore F, De Candia P, De Renzis S, Faraonio R, Sabo S, Cheetham J, Sudol M, Russo T (1997). «Interaction of the phosphotyrosine interaction/phosphotyrosine binding-related domains of Fe65 with wild-type and mutant Alzheimer's beta-amyloid precursor proteins». UNITED STATES. J. Biol. Chem. 272 (10): 6399–405. ISSN 0021-9258. PMID 9045663. doi:10.1074/jbc.272.10.6399

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