Apbb1 amyloid beta precursor protein binding family B member 1 [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Apbb1provided by MGI
Official Full Name: amyloid beta precursor protein binding family B member 1provided by MGI
Primary source: MGI:MGI:107765
See related: Ensembl:ENSMUSG00000037032 AllianceGenome:MGI:107765
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: Rir; Fe65
Summary: Enables ubiquitin protein ligase binding activity. Involved in several processes, including double-strand break repair; positive regulation of DNA repair; and smooth muscle contraction. Acts upstream of or within several processes, including generation of neurons; negative regulation of neuron differentiation; and positive regulation of transcription by RNA polymerase II. Located in cytoplasm and nucleus. Is active in Schaffer collateral - CA1 synapse; glutamatergic synapse; and neuromuscular junction. Is expressed in several structures, including alimentary system; genitourinary system; integumental system; nervous system; and sensory organ. Human ortholog(s) of this gene implicated in Alzheimer's disease. Orthologous to human APBB1 (amyloid beta precursor protein binding family B member 1). [provided by Alliance of Genome Resources, Dec 2024]
Expression: Broad expression in cortex adult (RPKM 63.0), cerebellum adult (RPKM 56.3) and 19 other tissues See more
Orthologs: human all
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Genomic context

Location:: 7 E3; 7 55.9 cM

Exon count:: 19

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	7	NC_000073.7 (105207691..105231151, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	7	NC_000073.6 (105558465..105581924, complement)

Chromosome 7 - NC_000073.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

These data demonstrate a role for FE65 proteins at central and peripheral synapses.
Title: FE65 and FE65L1 share common synaptic functions and genetically interact with the APP family in neuromuscular junction formation.
Jagged1 is a novel binding partner of Fe65, and Fe65 may act as a novel effector of Jagged1 signaling.
Title: Fe65 negatively regulates Jagged1 signaling by decreasing Jagged1 protein stability through the E3 ligase Neuralized-like 1.
results provide strong evidence that Fe65 plays a role in DNA damage response and cell viability by epigenomic regulation of specific transcriptional programs activated upon genotoxic stress.
Title: An epigenomic role of Fe65 in the cellular response to DNA damage.
Findings show that amyloid precursor protein-binding proteins FE65 and FE65L1 are essential for the maintenance of lens transparency.
Title: FE65 and FE65L1 amyloid precursor protein-binding protein compound null mice display adult-onset cataract and muscle weakness.
our data suggest that FE65 serves as a link between VLDLR and APP
Title: FE65 as a link between VLDLR and APP to regulate their trafficking and processing.
FE65 small interfering RNA does not influence Rac1 expression or its activity, although it acts as an adaptor protein with several protein-interaction domains.
Title: Functional and molecular interactions between Rac1 and FE65.
Fe65 carries out different functions depending on its location in the regulation of Notch1 signaling.
Title: Dual regulation of notch1 signaling pathway by adaptor protein fe65.
a unique role for the 97 kDa isoform in controlling GnRH-1 neurogenesis that is not redundant with the 60 kDa isoform of FE65.
Title: A role for FE65 in controlling GnRH-1 neurogenesis.
Results confirm that megalin interacts with APP and FE65, suggesting that these three proteins form a tripartite complex.
Title: Megalin interacts with APP and the intracellular adapter protein FE65 in neurons.
Data show that the carboxyl-terminal half of FE65, which contains the PI2 domain, failed to stabilize p53, suggesting that the amino-terminal half of the protein plays an important role in the stabilization of p53 in osmotically stressed cells.
Title: Roles of the intramolecular regions of FE65 in its trans-accumulation and in p53 stabilization in the nuclear matrix of osmotically stressed cells.

Submit: New GeneRIF Correction See all GeneRIFs (27)

Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Endonuclease-mediated (3)
Targeted (4) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

Apbb1 (e-PCR), detects polymorphism
- UniSTS:141099

Apbb1-rs1 (e-PCR), detects polymorphism
- UniSTS:141100

AF206720 (e-PCR)
- UniSTS:208174

RH125131 (e-PCR)
- UniSTS:161953

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables DNA-binding transcription factor binding	ISO Inferred from Sequence Orthology more info
enables amyloid-beta binding	IBA Inferred from Biological aspect of Ancestor more info
enables amyloid-beta binding	IEA Inferred from Electronic Annotation more info
enables amyloid-beta binding	ISO Inferred from Sequence Orthology more info
enables chromatin binding	ISO Inferred from Sequence Orthology more info
enables histone binding	ISO Inferred from Sequence Orthology more info
enables molecular adaptor activity	IBA Inferred from Biological aspect of Ancestor more info
enables molecular adaptor activity	ISO Inferred from Sequence Orthology more info
enables proline-rich region binding	ISO Inferred from Sequence Orthology more info
enables protein binding	IPI Inferred from Physical Interaction more info	PubMed
enables protein-containing complex binding	ISO Inferred from Sequence Orthology more info
enables tau protein binding	ISO Inferred from Sequence Orthology more info
enables ubiquitin protein ligase binding	IPI Inferred from Physical Interaction more info	PubMed
enables ubiquitin protein ligase binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in DNA damage response	IBA Inferred from Biological aspect of Ancestor more info
involved_in DNA damage response	IDA Inferred from Direct Assay more info	PubMed
involved_in DNA damage response	ISO Inferred from Sequence Orthology more info
involved_in DNA repair-dependent chromatin remodeling	ISO Inferred from Sequence Orthology more info
involved_in apoptotic process	IEA Inferred from Electronic Annotation more info
acts_upstream_of_or_within axon guidance	IGI Inferred from Genetic Interaction more info	PubMed
involved_in chromatin organization	IEA Inferred from Electronic Annotation more info
involved_in double-strand break repair	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within extracellular matrix organization	IGI Inferred from Genetic Interaction more info	PubMed
involved_in negative regulation of cell cycle G1/S phase transition	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of cell cycle G1/S phase transition	ISS Inferred from Sequence or Structural Similarity more info
acts_upstream_of_or_within negative regulation of neuron differentiation	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in negative regulation of transcription by RNA polymerase II	ISO Inferred from Sequence Orthology more info
acts_upstream_of neuron differentiation	IMP Inferred from Mutant Phenotype more info	PubMed
acts_upstream_of_or_within neuron migration	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of DNA repair	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in positive regulation of DNA-templated transcription	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	ISS Inferred from Sequence or Structural Similarity more info
involved_in positive regulation of neuron projection development	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of protein secretion	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within positive regulation of transcription by RNA polymerase II	IGI Inferred from Genetic Interaction more info	PubMed
involved_in positive regulation of transcription by RNA polymerase II	ISO Inferred from Sequence Orthology more info
involved_in protein stabilization	NAS Non-traceable Author Statement more info	PubMed
involved_in regulation of DNA-templated transcription	IBA Inferred from Biological aspect of Ancestor more info
involved_in smooth muscle contraction	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in synapse organization	IDA Inferred from Direct Assay more info	PubMed
involved_in synapse organization	IMP Inferred from Mutant Phenotype more info	PubMed

Component	Evidence Code	Pubs
is_active_in Schaffer collateral - CA1 synapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in Schaffer collateral - CA1 synapse	IMP Inferred from Mutant Phenotype more info	PubMed
is_active_in cytoplasm	IBA Inferred from Biological aspect of Ancestor more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in dendritic spine	ISO Inferred from Sequence Orthology more info
located_in endoplasmic reticulum	ISO Inferred from Sequence Orthology more info
is_active_in glutamatergic synapse	IDA Inferred from Direct Assay more info	PubMed
is_active_in glutamatergic synapse	IMP Inferred from Mutant Phenotype more info	PubMed
located_in growth cone	ISO Inferred from Sequence Orthology more info
located_in growth cone	ISS Inferred from Sequence or Structural Similarity more info
located_in growth cone filopodium	ISO Inferred from Sequence Orthology more info
located_in growth cone lamellipodium	ISO Inferred from Sequence Orthology more info
located_in lamellipodium	ISO Inferred from Sequence Orthology more info
located_in lamellipodium	ISS Inferred from Sequence or Structural Similarity more info
located_in main axon	ISO Inferred from Sequence Orthology more info
is_active_in neuromuscular junction	IDA Inferred from Direct Assay more info	PubMed
is_active_in neuromuscular junction	IMP Inferred from Mutant Phenotype more info	PubMed
located_in neuronal cell body	ISO Inferred from Sequence Orthology more info
located_in nuclear speck	IEA Inferred from Electronic Annotation more info
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	ISO Inferred from Sequence Orthology more info
located_in perinuclear region of cytoplasm	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	IEA Inferred from Electronic Annotation more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
located_in postsynaptic membrane	ISO Inferred from Sequence Orthology more info
is_active_in presynapse	ISO Inferred from Sequence Orthology more info
located_in presynaptic membrane	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info
located_in synapse	ISO Inferred from Sequence Orthology more info
located_in synapse	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: amyloid beta precursor protein binding family B member 1

Names: amyloid beta (A4) precursor protein-binding, family B, member 1

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_001253885.2 → NP_001240814.1 amyloid beta precursor protein binding family B member 1 isoform 1

See identical proteins and their annotated locations for NP_001240814.1

Status: VALIDATED

Description

Transcript Variant: This variant (1) represents the longest transcript and encodes the longest isoform (1).

Source sequence(s)

AC125227

Consensus CDS

CCDS80776.1

UniProtKB/Swiss-Prot

E9QNW5, O08642, Q3TPU0, Q8BNF4, Q8BSR9, Q9QXJ1

UniProtKB/TrEMBL

A0A0R4J2C1

Related

ENSMUSP00000140116.2, ENSMUST00000191601.7

Conserved Domains (3) summary

cd01271
Location:535 → 660

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:368 → 507

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:255 → 283

WW; WW domain
NM_001253886.2 → NP_001240815.1 amyloid beta precursor protein binding family B member 1 isoform 2

See identical proteins and their annotated locations for NP_001240815.1

Status: VALIDATED

Description

Transcript Variant: This variant (4) lacks an in-frame exon in the coding region compared to variant 1. This results in a shorter protein (isoform 2) compared to isoform 1. Variants 2 and 4 encode the same isoform (2).

Source sequence(s)

AC125227

Consensus CDS

CCDS80775.1

UniProtKB/Swiss-Prot

E9QNW5, O08642, Q3TPU0, Q8BNF4, Q8BSR9, Q9QXJ1

UniProtKB/TrEMBL

A0A0R4J2C6

Related

ENSMUSP00000140979.2, ENSMUST00000189378.7

Conserved Domains (3) summary

cd01271
Location:533 → 658

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:368 → 505

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:255 → 283

WW; WW domain
NM_001253887.2 → NP_001240816.1 amyloid beta precursor protein binding family B member 1 isoform 3

See identical proteins and their annotated locations for NP_001240816.1

Status: VALIDATED

Description

Transcript Variant: This variant (3) differs in the 5' UTR and has multiple coding region differences compared to variant 1. These differences cause translation initiation at a downstream AUG and result in an isoform (3) with a shorter N-terminus compared to isoform 1.

Source sequence(s)

AC125227

Consensus CDS

CCDS80773.1

UniProtKB/TrEMBL

A0A087WR62, Q80Y77

Related

ENSMUSP00000140486.2, ENSMUST00000190369.7

Conserved Domains (3) summary

cd01271
Location:276 → 401

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:109 → 248

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:5 → 24

WW; WW domain
NM_001310600.2 → NP_001297529.1 amyloid beta precursor protein binding family B member 1 isoform 4

Status: VALIDATED

Description

Transcript Variant: This variant (5) differs in the 5' UTR, lacks a portion of the 5' coding region and initiates translation at an alternate start codon, compared to variant 1. It encodes isoform 4, which is shorter and has a distinct N-terminus, compared to isoform 1.

Source sequence(s)

AC125227

Consensus CDS

CCDS80774.1

UniProtKB/TrEMBL

A0A087WPS7

Related

ENSMUSP00000139899.2, ENSMUST00000187057.7

Conserved Domains (3) summary

cd01271
Location:310 → 435

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:145 → 282

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:32 → 60

WW; WW domain
NM_001411958.1 → NP_001398887.1 amyloid beta precursor protein binding family B member 1 isoform 2

Status: VALIDATED

Source sequence(s)

AC125227

UniProtKB/Swiss-Prot

E9QNW5, O08642, Q3TPU0, Q8BNF4, Q8BSR9, Q9QXJ1

UniProtKB/TrEMBL

A0A0R4J2C6
NM_001411959.1 → NP_001398888.1 amyloid beta precursor protein binding family B member 1 isoform 5

Status: VALIDATED

Source sequence(s)

AC125227

UniProtKB/TrEMBL

Q80Y77
NM_001411960.1 → NP_001398889.1 amyloid beta precursor protein binding family B member 1 isoform 5

Status: VALIDATED

Source sequence(s)

AC125227

UniProtKB/TrEMBL

Q80Y77
NM_001411961.1 → NP_001398890.1 amyloid beta precursor protein binding family B member 1 isoform 5

Status: VALIDATED

Source sequence(s)

AC125227

UniProtKB/TrEMBL

Q80Y77
NM_001411962.1 → NP_001398891.1 amyloid beta precursor protein binding family B member 1 isoform 5

Status: VALIDATED

Source sequence(s)

AC125227

UniProtKB/TrEMBL

Q80Y77
NM_001411964.1 → NP_001398893.1 amyloid beta precursor protein binding family B member 1 isoform 6

Status: VALIDATED

Source sequence(s)

AC125227
NM_009685.4 → NP_033815.1 amyloid beta precursor protein binding family B member 1 isoform 2

See identical proteins and their annotated locations for NP_033815.1

Status: VALIDATED

Description

Transcript Variant: This variant (2) differs in the 5' UTR and lacks an in-frame exon in the coding region compared to variant 1. This results in a shorter protein (isoform 2) compared to isoform 1. Variants 2, 4, and 6 all encode the same isoform (2).

Source sequence(s)

AC125227

Consensus CDS

CCDS80775.1

UniProtKB/Swiss-Prot

E9QNW5, O08642, Q3TPU0, Q8BNF4, Q8BSR9, Q9QXJ1

UniProtKB/TrEMBL

A0A0R4J2C6

Related

ENSMUSP00000140973.2, ENSMUST00000191011.7

Conserved Domains (3) summary

cd01271
Location:533 → 658

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:368 → 505

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:255 → 283

WW; WW domain

RNA

NR_177986.1 RNA Sequence

Status: VALIDATED

Source sequence(s)

AC125227

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

NC_000073.7 Reference GRCm39 C57BL/6J

Range

105207691..105231151 complement

Download

GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

XM_006507230.3 → XP_006507293.1 amyloid beta precursor protein binding family B member 1 isoform X1

See identical proteins and their annotated locations for XP_006507293.1

UniProtKB/Swiss-Prot

E9QNW5, O08642, Q3TPU0, Q8BNF4, Q8BSR9, Q9QXJ1

UniProtKB/TrEMBL

A0A0R4J2C1

Conserved Domains (3) summary

cd01271
Location:535 → 660

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:368 → 507

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:255 → 283

WW; WW domain
XM_006507231.1 → XP_006507294.1 amyloid beta precursor protein binding family B member 1 isoform X1

See identical proteins and their annotated locations for XP_006507294.1

UniProtKB/Swiss-Prot

E9QNW5, O08642, Q3TPU0, Q8BNF4, Q8BSR9, Q9QXJ1

UniProtKB/TrEMBL

A0A0R4J2C1

Conserved Domains (3) summary

cd01271
Location:535 → 660

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:368 → 507

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:255 → 283

WW; WW domain
XM_006507236.4 → XP_006507299.1 amyloid beta precursor protein binding family B member 1 isoform X6

See identical proteins and their annotated locations for XP_006507299.1

UniProtKB/TrEMBL

A0A087WR62, Q80Y77

Conserved Domains (3) summary

cd01271
Location:276 → 401

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:109 → 248

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:5 → 24

WW; WW domain
XM_006507235.4 → XP_006507298.1 amyloid beta precursor protein binding family B member 1 isoform X6

See identical proteins and their annotated locations for XP_006507298.1

UniProtKB/TrEMBL

A0A087WR62, Q80Y77

Related

ENSMUSP00000139575.2, ENSMUST00000189072.7

Conserved Domains (3) summary

cd01271
Location:276 → 401

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:109 → 248

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:5 → 24

WW; WW domain
XM_036152596.1 → XP_036008489.1 amyloid beta precursor protein binding family B member 1 isoform X6

UniProtKB/TrEMBL

A0A087WR62, Q80Y77

Conserved Domains (3) summary

cd01271
Location:276 → 401

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:109 → 248

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:5 → 24

WW; WW domain
XM_006507234.4 → XP_006507297.1 amyloid beta precursor protein binding family B member 1 isoform X6

See identical proteins and their annotated locations for XP_006507297.1

UniProtKB/TrEMBL

A0A087WR62, Q80Y77

Conserved Domains (3) summary

cd01271
Location:276 → 401

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:109 → 248

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:5 → 24

WW; WW domain
XM_017321947.3 → XP_017177436.1 amyloid beta precursor protein binding family B member 1 isoform X5

UniProtKB/TrEMBL

A0A087WPI2

Related

ENSMUSP00000139788.2, ENSMUST00000188368.7

Conserved Domains (3) summary

cd01271
Location:312 → 437

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:145 → 284

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:32 → 60

WW; WW domain
XM_036152595.1 → XP_036008488.1 amyloid beta precursor protein binding family B member 1 isoform X4

Conserved Domains (3) summary

cd01271
Location:333 → 458

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:168 → 305

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:55 → 83

WW; WW domain
XM_006507232.5 → XP_006507295.1 amyloid beta precursor protein binding family B member 1 isoform X3

Conserved Domains (3) summary

cd01271
Location:335 → 460

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:168 → 307

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:55 → 83

WW; WW domain
XM_036152597.1 → XP_036008490.1 amyloid beta precursor protein binding family B member 1 isoform X7

UniProtKB/TrEMBL

Q80Y77

Conserved Domains (3) summary

cd01271
Location:274 → 399

PTB2_Fe65; Fe65 C-terminal Phosphotyrosine-binding (PTB) domain

cd01272
Location:109 → 246

PTB1_Fe65; Fe65 N-terminal Phosphotyrosine-binding (PTB) domain

pfam00397
Location:5 → 24

WW; WW domain