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Protein

Amyloid beta A4 precursor protein-binding family B member 1

Gene

Apbb1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Adapter protein that forms a transcriptionally active complex with the gamma-secretase-derived amyloid precursor protein (APP) intracellular domain. Plays a central role in the response to DNA damage by translocating to the nucleus and inducing apoptosis. May act by specifically recognizing and binding histone H2AX phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1. Required for histone H4 acetylation at double-strand breaks (DSBs). Its ability to specifically bind modified histones and chromatin modifying enzymes such as KAT5/TIP60, probably explains its trancription activation activity. Function in association with TSHZ3, SET and HDAC factors as a transcriptional repressor, that inhibits the expression of CASP4. Associates with chromatin in a region surrounding the CASP4 transcriptional start site(s).1 Publication

GO - Molecular functioni

  • beta-amyloid binding Source: UniProtKB
  • chromatin binding Source: MGI
  • histone acetyltransferase binding Source: UniProtKB
  • histone binding Source: MGI
  • proline-rich region binding Source: MGI
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • actin filament-based movement Source: UniProtKB
  • apoptotic process Source: UniProtKB-KW
  • axon guidance Source: MGI
  • cell cycle arrest Source: UniProtKB
  • cellular response to DNA damage stimulus Source: UniProtKB
  • double-strand break repair Source: UniProtKB
  • extracellular matrix organization Source: MGI
  • histone H4 acetylation Source: UniProtKB
  • negative regulation of cell growth Source: UniProtKB
  • negative regulation of neuron differentiation Source: MGI
  • negative regulation of thymidylate synthase biosynthetic process Source: UniProtKB
  • neuron migration Source: MGI
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of DNA repair Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein stabilization Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • visual learning Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Repressor

Keywords - Biological processi

Apoptosis, DNA damage, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Names & Taxonomyi

Protein namesi
Recommended name:
Amyloid beta A4 precursor protein-binding family B member 1
Alternative name(s):
Protein Fe65
Gene namesi
Name:Apbb1
Synonyms:Fe65
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:107765. Apbb1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • growth cone Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • nuclear speck Source: UniProtKB-SubCell
  • nucleus Source: UniProtKB
  • plasma membrane Source: MGI
  • synapse Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

No phenotype in normal conditions. Displays an increased sensitivity to genotoxic stress and exposur to DNA damaging agents.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi280 – 2801W → F: Abolishes ligand binding; when associated with A-283. 1 Publication
Mutagenesisi283 – 2831P → A: Abolishes ligand binding; when associated with F-280. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 710710Amyloid beta A4 precursor protein-binding family B member 1PRO_0000076050Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei517 – 5171PhosphoserineCombined sources
Modified residuei547 – 5471Phosphotyrosine; by ABL1By similarity
Modified residuei610 – 6101Phosphoserine; by SGK1By similarity

Post-translational modificationi

Phosphorylated following nuclear translocation. Phosphorylation at Tyr-546 enhances the transcription activation activity and reduces the affinity with RASD1/DEXRAS1. Phosphorylation at Ser-610 by SGK1 promotes its localization to the nucleus (By similarity).By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9QXJ1.
PaxDbiQ9QXJ1.
PRIDEiQ9QXJ1.

PTM databases

iPTMnetiQ9QXJ1.
PhosphoSiteiQ9QXJ1.

Expressioni

Gene expression databases

BgeeiENSMUSG00000037032.
ExpressionAtlasiQ9QXJ1. baseline and differential.
GenevisibleiQ9QXJ1. MM.

Interactioni

Subunit structurei

Interacts with SET. Found in a trimeric complex with HDAC1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by TSHZ3 (By similarity). Component of a complex, at least composed of APBB1, RASD1/DEXRAS1 and APP. Interacts (via PID domain 2) with APP (with the intracellular domain of the beta-amyloid precursor protein). Interacts (via PID domain 2) with RASD1/DEXRAS1; impairs the trancription activation activity. Interacts (via PID domain 1) with KAT5/TIP60. Interacts (via the WW domain) with histone H2AX (when phosphorylated on 'Tyr-142'). Interacts with MAPK8 (By similarity). Interacts (via the WW domain) with proline-rich regions of APBB1IP and ENAH. Interacts (via PID domain 1) with TSHZ3 (via homeobox domain). Interacts with TSHZ1 and TSHZ2. Interacts (via WWW domain) with NEK6. Interacts (via WWW domain) with ABL1 (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
AppP120232EBI-81338,EBI-78814

GO - Molecular functioni

  • histone acetyltransferase binding Source: UniProtKB
  • histone binding Source: MGI
  • proline-rich region binding Source: MGI
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198141. 6 interactions.
IntActiQ9QXJ1. 2 interactions.
MINTiMINT-142893.
STRINGi10090.ENSMUSP00000079932.

Structurei

3D structure databases

ProteinModelPortaliQ9QXJ1.
SMRiQ9QXJ1. Positions 241-290, 366-666.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini253 – 28533WWPROSITE-ProRule annotationAdd
BLAST
Domaini370 – 509140PID 1PROSITE-ProRule annotationAdd
BLAST
Domaini542 – 699158PID 2PROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi158 – 17114Glu-richAdd
BLAST

Sequence similaritiesi

Contains 2 PID domains.PROSITE-ProRule annotation
Contains 1 WW domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IEKA. Eukaryota.
ENOG410YEVS. LUCA.
GeneTreeiENSGT00390000000002.
HOGENOMiHOG000033983.
HOVERGENiHBG050524.
InParanoidiQ9QXJ1.
KOiK04529.
OrthoDBiEOG091G04HV.
TreeFamiTF314331.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00640. PID. 2 hits.
[Graphical view]
SMARTiSM00462. PTB. 2 hits.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 2 hits.
SSF51045. SSF51045. 1 hit.
PROSITEiPS01179. PID. 2 hits.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9QXJ1-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSVPSSLSQS AINANSHGGP ALSFPLPLHA AHNQLLNAKL QATAVVPKDL
60 70 80 90 100
RSAMGEGSVP EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS
110 120 130 140 150
QEAETAPLGP KGLMHLYSEL ELSAHNAANR GLHGSALIIN TQEQGPDEGE
160 170 180 190 200
EKAAGEAEED DEDEEEEEEE EDLSSPPGLP EPLENVEVPS GPQALTDGPR
210 220 230 240 250
EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT DSFWNPNAFE
260 270 280 290 300
TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL
310 320 330 340 350
TWTGFAHQEG FEEGEFWKDE PSEEAPMELG LKDPEEATLS FPAQSLSPEP
360 370 380 390 400
VPQEEEKLSQ RNANPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ
410 420 430 440 450
LSYHKNNLHD PMAGGWGEGK DLLLQLEDET LKLVEPQNQT LLHAQPIVSI
460 470 480 490 500
RVWGVGRDSG SNRDFAYVAR DKLTQMLKCH VFRCEAPAKN IATSLHEICS
510 520 530 540 550
KIMSERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV QKFQVYYLGN
560 570 580 590 600
VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV
610 620 630 640 650
LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV
660 670 680 690 700
QAACMLRYQK CLDARSQTST SCLPAPPAES VARRVGWTVR RGVQSLWGSL
710
KPKRLGSQTP
Length:710
Mass (Da):77,384
Last modified:July 27, 2011 - v3
Checksum:i9CFD571C50584979
GO
Isoform 2 (identifier: Q9QXJ1-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     462-463: Missing.

Show »
Length:708
Mass (Da):77,114
Checksum:i234B7C6D9383B148
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti92 – 921T → A in AAF20141 (Ref. 1) Curated
Sequence conflicti313 – 3131E → D in AAF20141 (Ref. 1) Curated
Sequence conflicti461 – 4622SN → RE in BAC39033 (PubMed:16141072).Curated
Sequence conflicti461 – 4622SN → RE in BAE37645 (PubMed:16141072).Curated
Sequence conflicti630 – 6301A → S in BAC39033 (PubMed:16141072).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei462 – 4632Missing in isoform 2. 2 PublicationsVSP_011659

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF206720 mRNA. Translation: AAF20141.1.
AK030748 mRNA. Translation: BAC27116.1.
AK083830 mRNA. Translation: BAC39033.1.
AK164140 mRNA. Translation: BAE37645.1.
AC125227 Genomic DNA. No translation available.
L77865 mRNA. Translation: AAB51603.1.
CCDSiCCDS80775.1. [Q9QXJ1-2]
CCDS80776.1. [Q9QXJ1-1]
RefSeqiNP_001240814.1. NM_001253885.1.
NP_001240815.1. NM_001253886.1.
NP_033815.1. NM_009685.3.
XP_006507293.1. XM_006507230.1.
XP_006507294.1. XM_006507231.1.
UniGeneiMm.38469.
Mm.490092.

Genome annotation databases

EnsembliENSMUST00000081165; ENSMUSP00000079932; ENSMUSG00000037032. [Q9QXJ1-1]
GeneIDi11785.
KEGGimmu:11785.
UCSCiuc009iyi.2. mouse. [Q9QXJ1-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF206720 mRNA. Translation: AAF20141.1.
AK030748 mRNA. Translation: BAC27116.1.
AK083830 mRNA. Translation: BAC39033.1.
AK164140 mRNA. Translation: BAE37645.1.
AC125227 Genomic DNA. No translation available.
L77865 mRNA. Translation: AAB51603.1.
CCDSiCCDS80775.1. [Q9QXJ1-2]
CCDS80776.1. [Q9QXJ1-1]
RefSeqiNP_001240814.1. NM_001253885.1.
NP_001240815.1. NM_001253886.1.
NP_033815.1. NM_009685.3.
XP_006507293.1. XM_006507230.1.
XP_006507294.1. XM_006507231.1.
UniGeneiMm.38469.
Mm.490092.

3D structure databases

ProteinModelPortaliQ9QXJ1.
SMRiQ9QXJ1. Positions 241-290, 366-666.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198141. 6 interactions.
IntActiQ9QXJ1. 2 interactions.
MINTiMINT-142893.
STRINGi10090.ENSMUSP00000079932.

PTM databases

iPTMnetiQ9QXJ1.
PhosphoSiteiQ9QXJ1.

Proteomic databases

MaxQBiQ9QXJ1.
PaxDbiQ9QXJ1.
PRIDEiQ9QXJ1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000081165; ENSMUSP00000079932; ENSMUSG00000037032. [Q9QXJ1-1]
GeneIDi11785.
KEGGimmu:11785.
UCSCiuc009iyi.2. mouse. [Q9QXJ1-2]

Organism-specific databases

CTDi322.
MGIiMGI:107765. Apbb1.

Phylogenomic databases

eggNOGiENOG410IEKA. Eukaryota.
ENOG410YEVS. LUCA.
GeneTreeiENSGT00390000000002.
HOGENOMiHOG000033983.
HOVERGENiHBG050524.
InParanoidiQ9QXJ1.
KOiK04529.
OrthoDBiEOG091G04HV.
TreeFamiTF314331.

Enzyme and pathway databases

ReactomeiR-MMU-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.

Miscellaneous databases

ChiTaRSiApbb1. mouse.
PROiQ9QXJ1.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000037032.
ExpressionAtlasiQ9QXJ1. baseline and differential.
GenevisibleiQ9QXJ1. MM.

Family and domain databases

Gene3Di2.30.29.30. 2 hits.
InterProiIPR011993. PH_dom-like.
IPR006020. PTB/PI_dom.
IPR001202. WW_dom.
[Graphical view]
PfamiPF00640. PID. 2 hits.
[Graphical view]
SMARTiSM00462. PTB. 2 hits.
SM00456. WW. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 2 hits.
SSF51045. SSF51045. 1 hit.
PROSITEiPS01179. PID. 2 hits.
PS01159. WW_DOMAIN_1. 1 hit.
PS50020. WW_DOMAIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiAPBB1_MOUSE
AccessioniPrimary (citable) accession number: Q9QXJ1
Secondary accession number(s): E9QNW5
, O08642, Q3TPU0, Q8BNF4, Q8BSR9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 130 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.