APBB1_MOUSE
ID APBB1_MOUSE Reviewed; 710 AA.
AC Q9QXJ1; E9QNW5; O08642; Q3TPU0; Q8BNF4; Q8BSR9;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Amyloid beta precursor protein binding family B member 1 {ECO:0000250|UniProtKB:O00213};
DE AltName: Full=Amyloid-beta A4 precursor protein-binding family B member 1 {ECO:0000312|MGI:MGI:107765};
DE AltName: Full=Protein Fe65 {ECO:0000303|PubMed:9407065};
GN Name=Apbb1 {ECO:0000312|MGI:MGI:107765};
GN Synonyms=Fe65 {ECO:0000303|PubMed:8894693},
GN Rir {ECO:0000312|MGI:MGI:107765};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Liakicheva A.V., Ivanova N.B., Belyavsky A.V.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Hippocampus, and Spinal ganglion;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 498-674.
RC TISSUE=Embryo;
RX PubMed=8894693; DOI=10.1093/hmg/5.10.1589;
RA Bressler S.L., Gray M.D., Sopher B.L., Hu Q., Hearn M.G., Pham D.G.,
RA Dinulos M.B., Fukuchi K., Sisodia S.S., Miller M.A., Disteche C.M.,
RA Martin G.M.;
RT "cDNA cloning and chromosome mapping of the human Fe65 gene: interaction of
RT the conserved cytoplasmic domains of the human beta-amyloid precursor
RT protein and its homologues with the mouse Fe65 protein.";
RL Hum. Mol. Genet. 5:1589-1598(1996).
RN [5]
RP INTERACTION WITH APBB1IP AND ENAH, AND MUTAGENESIS OF TRP-280 AND PRO-283.
RX PubMed=9407065; DOI=10.1074/jbc.272.52.32869;
RA Ermekova K.S., Zambrano N., Linn H., Minopoli G., Gertler F., Russo T.,
RA Sudol M.;
RT "The WW domain of neural protein FE65 interacts with proline-rich motifs in
RT Mena, the mammalian homolog of Drosophila enabled.";
RL J. Biol. Chem. 272:32869-32877(1997).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND DISRUPTION PHENOTYPE.
RX PubMed=17121854; DOI=10.1074/jbc.c600276200;
RA Minopoli G., Stante M., Napolitano F., Telese F., Aloia L., De Felice M.,
RA Di Lauro R., Pacelli R., Brunetti A., Zambrano N., Russo T.;
RT "Essential roles for Fe65, Alzheimer amyloid precursor-binding protein, in
RT the cellular response to DNA damage.";
RL J. Biol. Chem. 282:831-835(2007).
RN [7]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH TSHZ1; TSHZ2 AND TSHZ3.
RX PubMed=19343227; DOI=10.1371/journal.pone.0005071;
RA Kajiwara Y., Akram A., Katsel P., Haroutunian V., Schmeidler J.,
RA Beecham G., Haines J.L., Pericak-Vance M.A., Buxbaum J.D.;
RT "FE65 binds Teashirt, inhibiting expression of the primate-specific
RT caspase-4.";
RL PLoS ONE 4:E5071-E5071(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135 AND SER-517, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, and Lung;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP INTERACTION WITH RNF157, UBIQUITINATION BY RNF157, AND FUNCTION.
RX PubMed=25342469; DOI=10.1038/cdd.2014.163;
RA Matz A., Lee S.J., Schwedhelm-Domeyer N., Zanini D., Holubowska A.,
RA Kannan M., Farnworth M., Jahn O., Goepfert M.C., Stegmueller J.;
RT "Regulation of neuronal survival and morphology by the E3 ubiquitin ligase
RT RNF157.";
RL Cell Death Differ. 22:626-642(2015).
RN [10]
RP FUNCTION, TISSUE SPECIFICITY, AND DISRUPTION PHENOTYPE.
RX PubMed=25757569; DOI=10.1096/fj.14-261453;
RA Suh J., Moncaster J.A., Wang L., Hafeez I., Herz J., Tanzi R.E.,
RA Goldstein L.E., Guenette S.Y.;
RT "FE65 and FE65L1 amyloid precursor protein-binding protein compound null
RT mice display adult-onset cataract and muscle weakness.";
RL FASEB J. 29:2628-2639(2015).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=27734846; DOI=10.1038/srep25652;
RA Strecker P., Ludewig S., Rust M., Mundinger T.A., Goerlich A.,
RA Kraechan E.G., Mehrfeld C., Herz J., Korte M., Guenette S.Y., Kins S.;
RT "FE65 and FE65L1 share common synaptic functions and genetically interact
RT with the APP family in neuromuscular junction formation.";
RL Sci. Rep. 6:25652-25652(2016).
CC -!- FUNCTION: Transcription coregulator that can have both coactivator and
CC corepressor functions (PubMed:17121854, PubMed:25342469). Adapter
CC protein that forms a transcriptionally active complex with the gamma-
CC secretase-derived amyloid precursor protein (APP) intracellular domain
CC (PubMed:17121854, PubMed:25342469). Plays a central role in the
CC response to DNA damage by translocating to the nucleus and inducing
CC apoptosis. May act by specifically recognizing and binding histone H2AX
CC phosphorylated on 'Tyr-142' (H2AXY142ph) at double-strand breaks
CC (DSBs), recruiting other pro-apoptosis factors such as MAPK8/JNK1.
CC Required for histone H4 acetylation at double-strand breaks (DSBs) (By
CC similarity). Its ability to specifically bind modified histones and
CC chromatin modifying enzymes such as KAT5/TIP60, probably explains its
CC transcription activation activity (By similarity). Functions in
CC association with TSHZ3, SET and HDAC factors as a transcriptional
CC repressor, that inhibits the expression of CASP4. Associates with
CC chromatin in a region surrounding the CASP4 transcriptional start
CC site(s) (By similarity). Involved in hippocampal neurite branching and
CC neuromuscular junction formation, as a result plays a role in spatial
CC memory functioning (PubMed:27734846). Plays a role in the maintenance
CC of lens transparency (PubMed:25757569). May play a role in muscle cell
CC strength (PubMed:25757569, PubMed:27734846).
CC {ECO:0000250|UniProtKB:O00213, ECO:0000250|UniProtKB:P46933,
CC ECO:0000269|PubMed:17121854, ECO:0000269|PubMed:25342469,
CC ECO:0000269|PubMed:25757569, ECO:0000269|PubMed:27734846}.
CC -!- SUBUNIT: Component of a complex, at least composed of APBB1,
CC RASD1/DEXRAS1 and APP (By similarity). Interacts (via PID domain 2)
CC with APP (with the intracellular domain of the amyloid-beta precursor
CC protein) (By similarity). Interacts (via PID domain 2) with
CC RASD1/DEXRAS1; impairs the transcription activation activity (By
CC similarity). Interacts (via PID domain 1) with KAT5/TIP60 (By
CC similarity). Interacts (via the WW domain) with the proline-rich region
CC of APBB1IP (PubMed:9407065). Interacts with TSHZ1 and TSHZ2
CC (PubMed:19343227). Interacts (via the WW domain) with histone H2AX
CC (when phosphorylated on 'Tyr-142') and the proline-rich region of ENAH
CC (PubMed:9407065). Interacts with MAPK8 (By similarity). Interacts (via
CC PID domain 1) with TSHZ3 (via homeobox domain) (By similarity).
CC Interacts with SET (By similarity). Found in a trimeric complex with
CC HDAC1 and TSHZ3; the interaction between HDAC1 and APBB1 is mediated by
CC TSHZ3 (By similarity). Interacts (via WWW domain) with NEK6. Interacts
CC (via WWW domain) with ABL1. Interacts with RNF157 (By similarity).
CC {ECO:0000250|UniProtKB:O00213, ECO:0000250|UniProtKB:P46933,
CC ECO:0000269|PubMed:19343227, ECO:0000269|PubMed:9407065}.
CC -!- INTERACTION:
CC Q9QXJ1; P12023: App; NbExp=2; IntAct=EBI-81338, EBI-78814;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17121854}.
CC Cytoplasm {ECO:0000269|PubMed:17121854}. Nucleus
CC {ECO:0000269|PubMed:17121854}. Cell projection, growth cone
CC {ECO:0000269|PubMed:19343227}. Nucleus speckle. Note=Colocalizes with
CC TSHZ3 in the nucleus and in axonal growth cone (PubMed:19343227).
CC Colocalizes with TSHZ3 in axonal growth cone (By similarity).
CC Colocalizes with TSHZ3 in the nucleus (By similarity). In normal
CC conditions, it mainly localizes to the cytoplasm, while a small
CC fraction is tethered to the cell membrane via its interaction with APP
CC (By similarity). Following exposure to DNA damaging agents, it is
CC released from cell membrane and translocates to the nucleus (By
CC similarity). Nuclear translocation is under the regulation of APP (By
CC similarity). Colocalizes with NEK6 at the nuclear speckles (By
CC similarity). Phosphorylation at Ser-610 by SGK1 promotes its
CC localization to the nucleus (By similarity).
CC {ECO:0000250|UniProtKB:O00213, ECO:0000250|UniProtKB:P46933,
CC ECO:0000269|PubMed:19343227}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9QXJ1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9QXJ1-2; Sequence=VSP_011659;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, retinal lens and muscle
CC cells (at protein level). {ECO:0000269|PubMed:25757569}.
CC -!- PTM: Polyubiquitination by RNF157 leads to degradation by the
CC proteasome (PubMed:25342469). {ECO:0000269|PubMed:25342469}.
CC -!- PTM: Phosphorylation at Ser-610 by SGK1 promotes its localization to
CC the nucleus (By similarity). Phosphorylated following nuclear
CC translocation. Phosphorylation at Tyr-546 by ABL1 enhances
CC transcriptional activation activity and reduces the affinity for
CC RASD1/DEXRAS1 (By similarity). {ECO:0000250|UniProtKB:O00213,
CC ECO:0000250|UniProtKB:P46933}.
CC -!- PTM: Acetylation at Lys-204 and Lys-701 by KAT5 promotes its
CC transcription activator activity. {ECO:0000250|UniProtKB:O00213}.
CC -!- DISRUPTION PHENOTYPE: No phenotype in normal conditions
CC (PubMed:17121854). Displays an increased sensitivity to genotoxic
CC stress and exposure to DNA damaging agents (PubMed:17121854). Knockout
CC mice have decreased muscle strength, however clasping ability is
CC unaffected (PubMed:25757569). Impaired spatial memory retrieval and
CC learning (PubMed:27734846). Reduced branching of hippocampal neurites
CC and increased fragmentation of neuromuscular junctions
CC (PubMed:27734846). APBB1 and APBB2 double knockout mice show
CC progressive retinal lens disruption from 1 month of age,
CC morphologically lenses show massive vacuolization, lens capsule rupture
CC and disruption of the lens fiber cells organization (PubMed:25757569).
CC Decreased muscle strength, however clasping ability is unaffected
CC (PubMed:25757569, PubMed:27734846). Defects in peripheral motor
CC function including balance and coordination, reduced environmental
CC anxiety, reduced hippocampal basal synaptic transmission and synaptic
CC plasticity (PubMed:27734846). {ECO:0000269|PubMed:17121854,
CC ECO:0000269|PubMed:25757569, ECO:0000269|PubMed:27734846}.
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DR EMBL; AF206720; AAF20141.1; -; mRNA.
DR EMBL; AK030748; BAC27116.1; -; mRNA.
DR EMBL; AK083830; BAC39033.1; -; mRNA.
DR EMBL; AK164140; BAE37645.1; -; mRNA.
DR EMBL; AC125227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; L77865; AAB51603.1; -; mRNA.
DR CCDS; CCDS80775.1; -. [Q9QXJ1-2]
DR CCDS; CCDS80776.1; -. [Q9QXJ1-1]
DR RefSeq; NP_001240814.1; NM_001253885.1.
DR RefSeq; NP_001240815.1; NM_001253886.1.
DR RefSeq; NP_033815.1; NM_009685.3.
DR RefSeq; XP_006507293.1; XM_006507230.2.
DR RefSeq; XP_006507294.1; XM_006507231.1.
DR RefSeq; XP_017177435.1; XM_017321946.1.
DR AlphaFoldDB; Q9QXJ1; -.
DR BMRB; Q9QXJ1; -.
DR SMR; Q9QXJ1; -.
DR BioGRID; 198141; 6.
DR CORUM; Q9QXJ1; -.
DR IntAct; Q9QXJ1; 3.
DR MINT; Q9QXJ1; -.
DR STRING; 10090.ENSMUSP00000140116; -.
DR iPTMnet; Q9QXJ1; -.
DR PhosphoSitePlus; Q9QXJ1; -.
DR jPOST; Q9QXJ1; -.
DR MaxQB; Q9QXJ1; -.
DR PaxDb; Q9QXJ1; -.
DR PRIDE; Q9QXJ1; -.
DR ProteomicsDB; 296328; -. [Q9QXJ1-1]
DR ProteomicsDB; 296329; -. [Q9QXJ1-2]
DR Antibodypedia; 23808; 415 antibodies from 39 providers.
DR DNASU; 11785; -.
DR Ensembl; ENSMUST00000081165; ENSMUSP00000079932; ENSMUSG00000037032. [Q9QXJ1-1]
DR GeneID; 11785; -.
DR KEGG; mmu:11785; -.
DR UCSC; uc009iyi.2; mouse. [Q9QXJ1-2]
DR CTD; 322; -.
DR MGI; MGI:107765; Apbb1.
DR VEuPathDB; HostDB:ENSMUSG00000037032; -.
DR eggNOG; ENOG502QT08; Eukaryota.
DR GeneTree; ENSGT00390000000002; -.
DR InParanoid; Q9QXJ1; -.
DR OrthoDB; 437627at2759; -.
DR TreeFam; TF314331; -.
DR Reactome; R-MMU-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR BioGRID-ORCS; 11785; 2 hits in 102 CRISPR screens.
DR ChiTaRS; Apbb1; mouse.
DR PRO; PR:Q9QXJ1; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9QXJ1; protein.
DR Bgee; ENSMUSG00000037032; Expressed in entorhinal cortex and 243 other tissues.
DR ExpressionAtlas; Q9QXJ1; baseline and differential.
DR Genevisible; Q9QXJ1; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; IDA:SynGO.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:1990812; C:growth cone filopodium; ISO:MGI.
DR GO; GO:1990761; C:growth cone lamellipodium; ISO:MGI.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0044304; C:main axon; ISO:MGI.
DR GO; GO:0031594; C:neuromuscular junction; IDA:SynGO.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0098793; C:presynapse; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IDA:SynGO.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; ISO:MGI.
DR GO; GO:0003682; F:chromatin binding; ISO:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0070064; F:proline-rich region binding; ISO:MGI.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0048156; F:tau protein binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IGI:MGI.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0006302; P:double-strand break repair; IMP:UniProtKB.
DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI.
DR GO; GO:0043967; P:histone H4 acetylation; ISS:UniProtKB.
DR GO; GO:1902807; P:negative regulation of cell cycle G1/S phase transition; ISS:UniProtKB.
DR GO; GO:0045665; P:negative regulation of neuron differentiation; IMP:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0030182; P:neuron differentiation; IMP:MGI.
DR GO; GO:0001764; P:neuron migration; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0045739; P:positive regulation of DNA repair; IMP:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; ISO:MGI.
DR GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IGI:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0050821; P:protein stabilization; NAS:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006939; P:smooth muscle contraction; IMP:UniProtKB.
DR GO; GO:0050808; P:synapse organization; IDA:SynGO.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR039576; APBB1/2/3.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR14058; PTHR14058; 1.
DR Pfam; PF00640; PID; 2.
DR Pfam; PF00397; WW; 1.
DR SMART; SM00462; PTB; 2.
DR SMART; SM00456; WW; 1.
DR SUPFAM; SSF51045; SSF51045; 1.
DR PROSITE; PS01179; PID; 2.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Activator; Alternative splicing; Apoptosis; Cell membrane;
KW Cell projection; Chromatin regulator; Cytoplasm; DNA damage; Membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..710
FT /note="Amyloid beta precursor protein binding family B
FT member 1"
FT /id="PRO_0000076050"
FT DOMAIN 253..285
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 370..509
FT /note="PID 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 542..699
FT /note="PID 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 143..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 276..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..175
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 208..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 204
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00213"
FT MOD_RES 517
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 547
FT /note="Phosphotyrosine; by ABL1"
FT /evidence="ECO:0000250|UniProtKB:O00213"
FT MOD_RES 610
FT /note="Phosphoserine; by SGK1"
FT /evidence="ECO:0000250|UniProtKB:P46933"
FT MOD_RES 701
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O00213"
FT VAR_SEQ 462..463
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_011659"
FT MUTAGEN 280
FT /note="W->F: Abolishes ligand binding; when associated with
FT A-283."
FT /evidence="ECO:0000269|PubMed:9407065"
FT MUTAGEN 283
FT /note="P->A: Abolishes ligand binding; when associated with
FT F-280."
FT /evidence="ECO:0000269|PubMed:9407065"
FT CONFLICT 92
FT /note="T -> A (in Ref. 1; AAF20141)"
FT /evidence="ECO:0000305"
FT CONFLICT 313
FT /note="E -> D (in Ref. 1; AAF20141)"
FT /evidence="ECO:0000305"
FT CONFLICT 461..462
FT /note="SN -> RE (in Ref. 2; BAC39033/BAE37645)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="A -> S (in Ref. 2; BAC39033)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 710 AA; 77384 MW; 9CFD571C50584979 CRC64;
MSVPSSLSQS AINANSHGGP ALSFPLPLHA AHNQLLNAKL QATAVVPKDL RSAMGEGSVP
EPGPANAKWL KEGQNQLRRA ATAHRDQNRN VTLTLAEEAS QEAETAPLGP KGLMHLYSEL
ELSAHNAANR GLHGSALIIN TQEQGPDEGE EKAAGEAEED DEDEEEEEEE EDLSSPPGLP
EPLENVEVPS GPQALTDGPR EHSKSASLLF GMRNSAASDE DSSWATLSQG SPSYGSPEDT
DSFWNPNAFE TDSDLPAGWM RVQDTSGTYY WHIPTGTTQW EPPGRASPSQ GSSPQEESQL
TWTGFAHQEG FEEGEFWKDE PSEEAPMELG LKDPEEATLS FPAQSLSPEP VPQEEEKLSQ
RNANPGIKCF AVRSLGWVEM TEEELAPGRS SVAVNNCIRQ LSYHKNNLHD PMAGGWGEGK
DLLLQLEDET LKLVEPQNQT LLHAQPIVSI RVWGVGRDSG SNRDFAYVAR DKLTQMLKCH
VFRCEAPAKN IATSLHEICS KIMSERRNAR CLVNGLSLDH SKLVDVPFQV EFPAPKNELV
QKFQVYYLGN VPVAKPVGVD VINGALESVL SSSSREQWTP SHVSVAPATL TILHQQTEAV
LGECRVRFLS FLAVGRDVHT FAFIMAAGPA SFCCHMFWCE PNAASLSEAV QAACMLRYQK
CLDARSQTST SCLPAPPAES VARRVGWTVR RGVQSLWGSL KPKRLGSQTP
