P12023 (A4_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified April 16, 2014. Version 179. History...
Names and origin
|Protein names||Recommended name:|
Amyloid beta A4 protein
Alzheimer disease amyloid A4 protein homolog
Cleaved into the following 14 chains:
|Organism||Mus musculus (Mouse) [Reference proteome]|
|Taxonomic identifier||10090 [NCBI]|
|Taxonomic lineage||Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus|
|Sequence length||770 AA.|
|Sequence processing||The displayed sequence is further processed into a mature form.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibit Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity By similarity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. May be involved in copper homeostasis/oxidative stress through copper ion reduction. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV By similarity. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons By similarity. Provides Cu2+ ions for GPC1 which are required for release of nitric oxide (NO) and subsequent degradation of the heparan sulfate chains on GPC1. Ref.18
Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Binds transient metals such as copper, zinc and iron. Rat and mouse beta-amyloid peptides bind only weakly transient metals and have little reducing activity due to substitutions of transient metal chelating residues. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Also bind GPC1 in lipid rafts By similarity. Ref.18
The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis. Ref.18
N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6) By similarity. Ref.18
Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1, NUMB and DAB1. Binding to DAB1 inhibits its serine phosphorylation. Interacts (via NPXY motif) with DAB2 (via PID domain); the interaction is impaired by tyrosine phosphorylation of the NPXY motif. Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1 By similarity. In vitro, it binds MAPT via the MT-binding domains By similarity. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner By similarity. Interacts, through a C-terminal domain, with GNAO1 By similarity. Amyloid beta-42 binds CHRNA7 in hippocampal neurons By similarity. Beta-amyloid associates with HADH2 By similarity. Interacts with ANKS1B, TNFRSF21 and AGER By similarity. Interacts with CPEB1. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; this is promoted by heparin binding By similarity. Beta-amyloid protein 40 interacts with S100A9 By similarity. CTF-alpha product of APP interacts with GSAP By similarity. Interacts with SORL1. Ref.11 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.19 Ref.20
Membrane; Single-pass type I membrane protein. Membrane › clathrin-coated pit. Note: Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF59 peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FPRL1 at the cell surface and the complex is then rapidly internalized By similarity. APP sorts to the basolateral surface in epithelial cells By similarity. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment. Associates with GPC1 in perinuclear compartments. Ref.18
Isoform APP770 is expressed in kidney. Isoform APP751 is widely expressed. Isoform APP695 is expressed in brain, kidney and liver. Isoform APP695, isoform APP714 and isoform APP751 are expressed in several different brain regions including hippocampus, substania nigra pars compacta and cerebellum. In the cerebellum, these isoforms are abundantly expressed in Purkinje cells. Ref.10
The basolateral sorting signal (BaSS) is required for sorting of membrane proteins to the basolateral surface of epithelial cells.
The NPXY sequence motif found in many tyrosine-phosphorylated proteins is required for the specific binding of the PID domain. However, additional amino acids either N- or C-terminal to the NPXY motif are often required for complete interaction. The PID domain-containing proteins which bind APP require the YENPTY motif for full interaction. These interactions are independent of phosphorylation on the terminal tyrosine residue. The NPXY site is also involved in clathrin-mediated endocytosis By similarity.
Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF50, gamma-CTF57 and gamma-CTF59 By similarity.
Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-3, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides By similarity. Ref.17
N- and O-glycosylated By similarity.
Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members By similarity. Phosphorylation on Tyr-757 is required for SHC binding By similarity. Ref.12 Ref.15
Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond By similarity.
Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP) By similarity. Ref.17
Beta-amyloid peptides are degraded by IDE By similarity.
Chelation of metal ions, notably copper, iron and zinc, can induce histidine-bridging between beta-amyloid molecules resulting in beta-amyloid-metal aggregates. Rat and mouse beta-amyloid peptides have an arginine residue substituted for the bridging histidine residue and are thus less capable of forming amyloid aggregates. Extracellular zinc-binding increases binding of heparin to APP and inhibits collagen-binding By similarity.
Belongs to the APP family.
Contains 1 BPTI/Kunitz inhibitor domain.
|CALR||P15253||2||EBI-78814,EBI-9005200||From a different organism.|
|MAPK8IP1||Q9UQF2||2||EBI-78814,EBI-78404||From a different organism.|
|This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]|
Note: Additional isoforms seem to exist.
|Isoform APP770 (identifier: P12023-1) |
This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
|Isoform APP695 (identifier: P12023-2) |
The sequence of this isoform differs from the canonical sequence as follows:
289-289: E → V
|Isoform APP751 (identifier: P12023-3) |
The sequence of this isoform differs from the canonical sequence as follows:
|Isoform APP714 (identifier: P12023-4) |
The sequence of this isoform is not available.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Signal peptide||1 – 17||17||By similarity|
|Chain||18 – 770||753||Amyloid beta A4 protein||PRO_0000000114|
|Chain||18 – 687||670||Soluble APP-alpha Potential||PRO_0000000115|
|Chain||18 – 671||654||Soluble APP-beta Potential||PRO_0000000116|
|Chain||18 – 286||269||N-APP By similarity||PRO_0000381968|
|Chain||672 – 770||99||C99 By similarity||PRO_0000000117|
|Chain||672 – 713||42||Beta-amyloid protein 42 By similarity||PRO_0000000118|
|Chain||672 – 711||40||Beta-amyloid protein 40 By similarity||PRO_0000000119|
|Chain||688 – 770||83||C83 By similarity||PRO_0000000120|
|Peptide||688 – 713||26||P3(42) By similarity||PRO_0000000121|
|Peptide||688 – 711||24||P3(40) By similarity||PRO_0000000122|
|Chain||691 – 770||80||C80||PRO_0000384576|
|Chain||712 – 770||59||Gamma-secretase C-terminal fragment 59||PRO_0000000123|
|Chain||714 – 770||57||Gamma-secretase C-terminal fragment 57||PRO_0000000124|
|Chain||721 – 770||50||Gamma-secretase C-terminal fragment 50||PRO_0000000125|
|Chain||740 – 770||31||C31 By similarity||PRO_0000000126|
|Topological domain||18 – 699||682||Extracellular Potential|
|Transmembrane||700 – 723||24||Helical; Potential|
|Topological domain||724 – 770||47||Cytoplasmic Potential|
|Domain||291 – 341||51||BPTI/Kunitz inhibitor|
|Region||96 – 110||15||Heparin-binding By similarity|
|Region||181 – 188||8||Zinc-binding By similarity|
|Region||391 – 423||33||Heparin-binding By similarity|
|Region||491 – 522||32||Heparin-binding By similarity|
|Region||523 – 540||18||Collagen-binding By similarity|
|Region||732 – 751||20||Interaction with G(o)-alpha By similarity|
|Region||756 – 770||15||Interaction with DAB2|
|Motif||724 – 734||11||Basolateral sorting signal|
|Motif||759 – 762||4||NPXY motif; contains endocytosis signal|
|Compositional bias||230 – 260||31||Asp/Glu-rich (acidic)|
|Compositional bias||274 – 280||7||Poly-Thr|
|Metal binding||147||1||Copper 1 By similarity|
|Metal binding||151||1||Copper 1 By similarity|
|Metal binding||168||1||Copper 1 By similarity|
|Metal binding||677||1||Copper or zinc 2 By similarity|
|Metal binding||685||1||Copper or zinc 2 By similarity|
|Site||144||1||Required for Cu(2+) reduction By similarity|
|Site||301 – 302||2||Reactive bond By similarity|
|Site||671 – 672||2||Cleavage; by beta-secretase By similarity|
|Site||672 – 673||2||Cleavage; by caspase-6 By similarity|
|Site||687 – 688||2||Cleavage; by alpha-secretase By similarity|
|Site||690 – 691||2||Cleavage; by theta-secretase By similarity|
|Site||704||1||Implicated in free radical propagation By similarity|
|Site||706||1||Susceptible to oxidation By similarity|
|Site||711 – 712||2||Cleavage; by gamma-secretase; site 1 By similarity|
|Site||713 – 714||2||Cleavage; by gamma-secretase; site 2 By similarity|
|Site||720 – 721||2||Cleavage; by gamma-secretase; site 3 By similarity|
|Site||739 – 740||2||Cleavage; by caspase-6, caspase-8 or caspase-9 By similarity|
Amino acid modifications
|Modified residue||198||1||Phosphoserine; by CK2 By similarity|
|Modified residue||206||1||Phosphoserine; by CK1 By similarity|
|Modified residue||729||1||Phosphothreonine By similarity|
|Modified residue||730||1||Phosphoserine; by APP-kinase I By similarity|
|Modified residue||743||1||Phosphothreonine; by CDK5 and MAPK10|
|Modified residue||757||1||Phosphotyrosine; by ABL1 Ref.12|
|Glycosylation||542||1||N-linked (GlcNAc...) Probable|
|Glycosylation||571||1||N-linked (GlcNAc...) Probable|
|Disulfide bond||38 ↔ 62||By similarity|
|Disulfide bond||73 ↔ 117||By similarity|
|Disulfide bond||98 ↔ 105||By similarity|
|Disulfide bond||133 ↔ 187||By similarity|
|Disulfide bond||144 ↔ 174||By similarity|
|Disulfide bond||158 ↔ 186||By similarity|
|Disulfide bond||291 ↔ 341||By similarity|
|Disulfide bond||300 ↔ 324||By similarity|
|Disulfide bond||316 ↔ 337||By similarity|
|Alternative sequence||289||1||E → V in isoform APP695.||VSP_000012|
|Alternative sequence||290 – 364||75||Missing in isoform APP695.||VSP_000013|
|Alternative sequence||346 – 380||35||Missing in isoform APP751.||VSP_000014|
|Mutagenesis||728||1||Y → A: No effect on MAPK8IP1 binding. Ref.13|
|Mutagenesis||732 – 733||2||HH → GL or GP: Almost complete loss of binding to G(o) alpha subunit. No inhibition of GTPase activity.|
|Mutagenesis||743||1||T → E: No effect on MAPK8IP1 binding. Ref.13|
|Mutagenesis||756||1||G → F, H, N, S or W: Greatly impairs interaction with DAB2. Ref.14|
|Mutagenesis||756||1||G → Y: Impairs interaction with DAB2. Ref.14|
|Mutagenesis||757||1||Y → F: Greatly promotes interaction with DAB2. Ref.13 Ref.14|
|Mutagenesis||757||1||Y → G, H or V: Greatly impairs interaction with DAB2. Ref.13 Ref.14|
|Mutagenesis||757||1||Y → G: No MAPK8IP1 nor APBA1 nor APBB1 nor DAB1 binding. Ref.13 Ref.14|
|Mutagenesis||757||1||Y → I or W: Impairs interaction with DAB2. Ref.13 Ref.14|
|Mutagenesis||759||1||N → A: No MAPK8IP1 nor APBA1 nor Dab1 binding. No effect on APBB1 binding. Ref.13 Ref.14|
|Mutagenesis||759||1||N → G, L, M or P: Greatly impairs interaction with DAB2. Ref.13 Ref.14|
|Mutagenesis||760||1||P → E, F, I, K, L, Q, R, V, W or Y: Greatly impairs interaction with DAB2. Ref.14|
|Mutagenesis||762||1||Y → A: No MAPK8IP1 nor APBA1 nor Dab1 binding. No effect on APBB1 binding. Ref.13 Ref.14|
|Mutagenesis||762||1||Y → W: Greatly impairs interaction with DAB2. Ref.13 Ref.14|
|Sequence conflict||211||1||G → V in AAA37139. Ref.1|
|Sequence conflict||375||1||V → A in AAB41502. Ref.4|
Helix Strand Turn
|Helix||744 – 753||10|
|||"Complementary DNA for the mouse homolog of the human amyloid beta protein precursor."|
Yamada T., Sasaki H., Furuya H., Miyata T., Goto I., Sakaki Y.
Biochem. Biophys. Res. Commun. 149:665-671(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
Submitted (MAR-1988) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
|||"The amyloid beta protein precursor or proteinase nexin II from mouse is closer related to its human homolog than previously reported."|
de Strooper B., van Leuven F., van den Berghe H.
Biochim. Biophys. Acta 1129:141-143(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
|||"Molecular cloning, expression, and regulation of hippocampal amyloid precursor protein of senescence accelerated mouse (SAMP8)."|
Kumar V.B., Vyas K., Franko M., Choudhary V., Buddhiraju C., Alvarez J., Morley J.E.
Biochem. Cell Biol. 79:57-67(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM APP695).
|||"Positive and negative regulatory elements for the expression of the Alzheimer's disease amyloid precursor-encoding gene in mouse."|
Izumi R., Yamada T., Yoshikai S., Sasaki H., Hattori M., Sakai Y.
Gene 112:189-195(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
|||"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."|
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM APP770).
Tissue: Mammary tumor.
|||"Structure and expression of the alternatively-spliced forms of mRNA for the mouse homolog of Alzheimer's disease amyloid beta protein precursor."|
Yamada T., Sasaki H., Dohura K., Goto I., Sakaki Y.
Biochem. Biophys. Res. Commun. 158:906-912(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 281-380, ALTERNATIVE SPLICING.
Tissue: Brain and Kidney.
|||"Sequence of the protease inhibitor domain of the A4 amyloid protein precursor of Mus domesticus."|
Fukuchi K., Martin G.M., Deeb S.S.
Nucleic Acids Res. 17:5396-5396(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 289-364.
|||"Introduction of six mutations into the mouse genome using 'Hit and Run' gene-targeting: introduction of familial Alzheimer's disease mutations into the mouse amyloid precursor protein gene and humanization of the A-beta fragment."|
Wragg M.A., Busfield F., Duff K., Korenblat K., Capecchi M., Loring J.F., Goate A.M.
Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 656-737.
|||"Regional distribution of the alternatively spliced isoforms of beta APP RNA transcript in the brain of normal, heterozygous and homozygous weaver mutant mice as revealed by in situ hybridization histochemistry."|
Sola C., Mengod G., Ghetti B., Palacios J.M., Triarhou L.C.
Brain Res. Mol. Brain Res. 17:340-346(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY OF ALTERNATIVE SPLICED FORMS.
|||"Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I."|
Kamal A., Stokin G.B., Yang Z., Xia C.-H., Goldstein L.S.
Neuron 28:449-459(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KNS2.
|||"The beta-amyloid precursor protein APP is tyrosine-phosphorylated in cells expressing a constitutively active form of the Abl protoncogene."|
Zambrano N., Bruni P., Minopoli G., Mosca R., Molino D., Russo C., Schettini G., Sudol M., Russo T.
J. Biol. Chem. 276:19787-19792(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-757.
|||"C-jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK."|
Matsuda S., Yasukawa T., Homma Y., Ito Y., Niikura T., Hiraki T., Hirai S., Ohno S., Kita Y., Kawasumi M., Kouyama K., Yamamoto T., Kyriakis J.M., Nishimoto I.
J. Neurosci. 21:6597-6607(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: C-TERMINAL PROTEIN-PROTEIN INTERACTION, MUTAGENESIS OF TYR-728; THR-743; TYR-757; ASN-759 AND TYR-762.
|||"Disabled-2 colocalizes with the LDLR in clathrin-coated pits and interacts with AP-2."|
Morris S.M., Cooper J.A.
Traffic 2:111-123(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DAB2, MUTAGENESIS OF GLY-756; TYR-757; ASN-759; PRO-760 AND TYR-762.
|||"Interaction of Alzheimer's beta-amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade."|
Taru H., Iijima K., Hase M., Kirino Y., Yagi Y., Suzuki T.
J. Biol. Chem. 277:20070-20078(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MAPK8IP1, PHOSPHORYLATION.
|||"The gamma-secretase-generated intracellular domain of beta-amyloid precursor protein binds Numb and inhibits Notch signaling."|
Roncarati R., Sestan N., Scheinfeld M.H., Berechid B.E., Lopez P.A., Meucci O., McGlade J.C., Rakic P., D'Adamio L.
Proc. Natl. Acad. Sci. U.S.A. 99:7102-7107(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION OF CTF PEPTIDES WITH NUMB.
|||"The amyloid precursor protein (APP)-cytoplasmic fragment generated by gamma-secretase is rapidly degraded but distributes partially in a nuclear fraction of neurons in culture."|
Cupers P., Orlans I., Craessaerts K., Annaert W., De Strooper B.
J. Neurochem. 78:1168-1178(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING BY GAMMA SECRETASE, INTERACTION WITH APBB1.
|||"The amyloid precursor protein (APP) of Alzheimer disease and its paralog, APLP2, modulate the Cu/Zn-nitric oxide-catalyzed degradation of glypican-1 heparan sulfate in vivo."|
Cappai R., Cheng F., Ciccotosto G.D., Needham B.E., Masters C.L., Multhaup G., Fransson L.A., Mani K.
J. Biol. Chem. 280:13913-13920(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, FUNCTION.
|||"Amyloid precursor proteins anchor CPEB to membranes and promote polyadenylation-induced translation."|
Cao Q., Huang Y.-S., Kan M.-C., Richter J.D.
Mol. Cell. Biol. 25:10930-10939(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CPEB1.
|||"Neuronal sorting protein-related receptor sorLA/LR11 regulates processing of the amyloid precursor protein."|
Andersen O.M., Reiche J., Schmidt V., Gotthardt M., Spoelgen R., Behlke J., von Arnim C.A., Breiderhoff T., Jansen P., Wu X., Bales K.R., Cappai R., Masters C.L., Gliemann J., Mufson E.J., Hyman B.T., Paul S.M., Nykjaer A., Willnow T.E.
Proc. Natl. Acad. Sci. U.S.A. 102:13461-13466(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APP.
|+||Additional computationally mapped references.|
|M18373 mRNA. Translation: AAA37139.1.|
X59379 mRNA. No translation available.
U84012 mRNA. Translation: AAB41502.1.
D10603 Genomic DNA. Translation: BAA01456.1.
BC005490 mRNA. Translation: AAH05490.1.
M24397 mRNA. Translation: AAA39929.1.
X15210 mRNA. Translation: CAA33280.1.
U82624 Genomic DNA. Translation: AAB40919.1.
|RefSeq||NP_001185752.1. NM_001198823.1. |
3D structure databases
|SMR||P12023. Positions 26-192, 287-342, 371-566, 686-726, 741-768. |
Protein-protein interaction databases
|BioGrid||198167. 9 interactions.|
|IntAct||P12023. 77 interactions.|
Protein family/group databases
Protocols and materials databases
Genome annotation databases
|Ensembl||ENSMUST00000005406; ENSMUSP00000005406; ENSMUSG00000022892. [P12023-2]|
|UCSC||uc007ztn.2. mouse. [P12023-1]|
|MGI||MGI:88059. App. |
Gene expression databases
Family and domain databases
|Gene3D||3.30.1490.140. 1 hit. |
3.90.570.10. 1 hit.
188.8.131.52. 1 hit.
4.10.410.10. 1 hit.
|InterPro||IPR008155. Amyloid_glyco. |
|PANTHER||PTHR23103:SF7. PTHR23103:SF7. 1 hit. |
|Pfam||PF10515. APP_amyloid. 1 hit. |
PF12924. APP_Cu_bd. 1 hit.
PF12925. APP_E2. 1 hit.
PF02177. APP_N. 1 hit.
PF03494. Beta-APP. 1 hit.
PF00014. Kunitz_BPTI. 1 hit.
|PRINTS||PR00203. AMYLOIDA4. |
|SMART||SM00006. A4_EXTRA. 1 hit. |
SM00131. KU. 1 hit.
|SUPFAM||SSF109843. SSF109843. 1 hit. |
SSF56491. SSF56491. 1 hit.
SSF57362. SSF57362. 1 hit.
SSF89811. SSF89811. 1 hit.
|PROSITE||PS00319. A4_EXTRA. 1 hit. |
PS00320. A4_INTRA. 1 hit.
PS00280. BPTI_KUNITZ_1. 1 hit.
PS50279. BPTI_KUNITZ_2. 1 hit.
|ChiTaRS||app. mouse. |
|Accession||Primary (citable) accession number: P12023|
Secondary accession number(s): P97487, P97942, Q99K32
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Chordata Protein Annotation Program|