APBA2BP

From Wikipedia, the free encyclopedia

Amyloid beta (A4) precursor protein-binding, family A, member 2 binding protein

Identifiers

APBA2BP; NIP1; EFCBP3; NECAB3; SYTIP2; XB51; dJ63M2.4; dJ63M2.5

External IDs

Gene ontology
Molecular Function:	• calcium ion binding • protein binding • oxidoreductase activity
Cellular Component:	• Golgi cis cisterna • nucleus • cytoplasm • endoplasmic reticulum • endoplasmic reticulum membrane
Biological Process:	• protein secretion • antibiotic biosynthetic process • protein metabolic process • regulation of amyloid precursor protein biosynthetic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_031231 (mRNA)
NP_112508 (protein)

NM_021546 (mRNA)
NP_067521 (protein)

Location

Chr 20: 31.71 - 31.73 Mb

Chr 2: 154.24 - 154.25 Mb

Pubmed search

[1]

[2]

Amyloid beta (A4) precursor protein-binding, family A, member 2 binding protein, also known as APBA2BP, is a human gene.^[1]

The protein encoded by this gene interacts with the amino-terminal domain of the neuron-specific X11-like protein (X11L), inhibits the association of X11L with amyloid precursor protein through a non-competitive mechanism, and abolishes the suppression of beta-amyloid production by X11L. This protein, together with X11L, may play an important role in the regulatory system of amyloid precursor protein metabolism and beta-amyloid generation. This gene consists of at least 13 exons and its alternative splicing generates at least 2 transcript variants.^[1]

[edit] References

^ ^a ^b Entrez Gene: APBA2BP amyloid beta (A4) precursor protein-binding, family A, member 2 binding protein.

[edit] Further reading

Büssow K, Cahill D, Nietfeld W, et al. (1998). "A method for global protein expression and antibody screening on high-density filters of an arrayed cDNA library.". Nucleic Acids Res. 26 (21): 5007–8. PMID 9776767.
Sugita S, Südhof TC (2000). "Specificity of Ca2+-dependent protein interactions mediated by the C2A domains of synaptotagmins.". Biochemistry 39 (11): 2940–9. PMID 10715114.
Lee DS, Tomita S, Kirino Y, Suzuki T (2000). "Regulation of X11L-dependent amyloid precursor protein metabolism by XB51, a novel X11L-binding protein.". J. Biol. Chem. 275 (30): 23134–8. doi:10.1074/jbc.C000302200. PMID 10833507.
Deloukas P, Matthews LH, Ashurst J, et al. (2002). "The DNA sequence and comparative analysis of human chromosome 20.". Nature 414 (6866): 865–71. doi:10.1038/414865a. PMID 11780052.
Sugita S, Ho A, Südhof TC (2002). "NECABs: a family of neuronal Ca(2+)-binding proteins with an unusual domain structure and a restricted expression pattern.". Neuroscience 112 (1): 51–63. PMID 12044471.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Sumioka A, Imoto S, Martins RN, et al. (2003). "XB51 isoforms mediate Alzheimer's beta-amyloid peptide production by X11L (X11-like protein)-dependent and -independent mechanisms.". Biochem. J. 374 (Pt 1): 261–8. doi:10.1042/BJ20030489. PMID 12780348.
Yoo JC, Chang JR, Kim SH, et al. (2004). "NIP1/XB51/NECAB3 is a potential substrate of Nek2, suggesting specific roles of Nek2 in Golgi.". Exp. Cell Res. 292 (2): 393–402. PMID 14697346.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs.". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID 14702039.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMID 15489334.