ID APBB2_MOUSE Reviewed; 760 AA. AC Q9DBR4; Q6DFX8; DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 2. DT 02-SEP-2026, entry version 163. DE RecName: Full=Amyloid beta precursor protein binding family B member 2 {ECO:0000250|UniProtKB:Q92870}; DE AltName: Full=Amyloid-beta (A4) precursor protein-binding family B member 2 {ECO:0000312|MGI:MGI:108405}; DE AltName: Full=Protein Fe65-like 1 {ECO:0000250|UniProtKB:Q92870}; GN Name=Apbb2 {ECO:0000312|MGI:MGI:108405}; GN Synonyms=Fe65l {ECO:0000250|UniProtKB:Q92870}, Fe65l1 GN {ECO:0000303|PubMed:25757569}; 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 [LARGE SCALE MRNA] (ISOFORM 1). RC STRAIN=C57BL/6J; TISSUE=Lung; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC STRAIN=C57BL/6J; TISSUE=Eye; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-334; SER-409 AND RP SER-412, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Lung, and Spleen; 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 [4] 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 [5] 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). RN [6] RP STRUCTURE BY NMR OF 582-704. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the C-terminal phosphotyrosine interaction domain of RT APBB2 from mouse."; RL Submitted (NOV-2004) to the PDB data bank. RN [7] {ECO:0007744|PDB:1WGU, ECO:0007744|PDB:2ROZ, ECO:0007744|PDB:2YSZ, ECO:0007744|PDB:2YT0, ECO:0007744|PDB:2YT1} RP STRUCTURE BY NMR OF 564-567 AND 582-704, AND INTERACTION WITH APP. RX PubMed=18650440; DOI=10.1074/jbc.m803892200; RA Li H., Koshiba S., Hayashi F., Tochio N., Tomizawa T., Kasai T., Yabuki T., RA Motoda Y., Harada T., Watanabe S., Inoue M., Hayashizaki Y., Tanaka A., RA Kigawa T., Yokoyama S.; RT "Structure of the C-terminal phosphotyrosine interaction domain of Fe65L1 RT complexed with the cytoplasmic tail of amyloid precursor protein reveals a RT novel peptide binding mode."; RL J. Biol. Chem. 283:27165-27178(2008). CC -!- FUNCTION: Plays a role in the maintenance of lens transparency, and may CC also play a role in muscle cell strength (PubMed:25757569, CC PubMed:27734846). Involved in hippocampal neurite branching and CC neuromuscular junction formation, as a result plays a role in spatial CC memory functioning (PubMed:27734846). Activates transcription of APP CC (By similarity). {ECO:0000250|UniProtKB:Q92870, CC ECO:0000269|PubMed:25757569, ECO:0000269|PubMed:27734846}. CC -!- SUBUNIT: Interacts (via C-terminus) with APP (via C-terminus) CC (PubMed:18650440). Interacts with APLP2 (via cytoplasmic domain) (By CC similarity). {ECO:0000250|UniProtKB:Q92870, CC ECO:0000269|PubMed:18650440}. CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum CC {ECO:0000250|UniProtKB:Q92870}. Golgi apparatus CC {ECO:0000250|UniProtKB:Q92870}. Early endosome CC {ECO:0000250|UniProtKB:Q92870}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q9DBR4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9DBR4-2; Sequence=VSP_011661; CC Name=3; CC IsoId=Q9DBR4-3; Sequence=VSP_011661, VSP_011662; CC -!- TISSUE SPECIFICITY: Expressed in the brain, retinal lens and muscle CC cells (at protein level). {ECO:0000269|PubMed:25757569}. CC -!- DISRUPTION PHENOTYPE: Knockout mice develop cataracts from 16 months of CC age with defects such as ulcer-like anomalies in the cornea, and CC opacity in the lens cortex or wider lens. Decreased muscle strength, CC however clasping ability is unaffected (PubMed:25757569). Impaired CC spatial memory retrieval and learning (PubMed:27734846). Reduced CC branching of hippocampal neurites and increased fragmentation of CC neuromuscular junctions (PubMed:27734846). APBB1 and APBB2 double CC knockout mice show progressive retinal lens disruption from 1 month of CC age, morphologically lenses show massive vacuolization, lens capsule CC rupture and disruption of the lens fiber cells organization. Decreased CC 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:25757569, CC ECO:0000269|PubMed:27734846}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK004792; BAB23568.2; -; mRNA. DR EMBL; BC076587; AAH76587.1; -; mRNA. DR CCDS; CCDS51510.1; -. [Q9DBR4-1] DR CCDS; CCDS57344.1; -. [Q9DBR4-3] DR RefSeq; NP_001188343.1; NM_001201414.2. DR RefSeq; NP_001188344.1; NM_001201415.2. [Q9DBR4-3] DR RefSeq; NP_033816.1; NM_009686.3. [Q9DBR4-1] DR RefSeq; XP_030109938.1; XM_030254078.2. [Q9DBR4-1] DR RefSeq; XP_030109939.1; XM_030254079.2. [Q9DBR4-1] DR RefSeq; XP_030109940.1; XM_030254080.2. [Q9DBR4-2] DR RefSeq; XP_030109941.1; XM_030254081.2. [Q9DBR4-2] DR RefSeq; XP_036020640.1; XM_036164747.1. [Q9DBR4-2] DR RefSeq; XP_036020641.1; XM_036164748.1. [Q9DBR4-3] DR PDB; 1WGU; NMR; -; A=582-704. DR PDB; 2ROZ; NMR; -; B=582-704. DR PDB; 2YSZ; NMR; -; A=582-704. DR PDB; 2YT0; NMR; -; A=564-567, A=582-704. DR PDB; 2YT1; NMR; -; A=582-704. DR AlphaFoldDB; Q9DBR4; -. DR BMRB; Q9DBR4; -. DR SMR; Q9DBR4; -. DR BioGRID; 198142; 9. DR ELM; Q9DBR4; -. DR FunCoup; Q9DBR4; 2522. DR IntAct; Q9DBR4; 1. DR MINT; Q9DBR4; -. DR STRING; 10090.ENSMUSP00000123752; -. DR GlyGen; Q9DBR4; 2 sites. DR iPTMnet; Q9DBR4; -. DR PhosphoSitePlus; Q9DBR4; -. DR SwissPalm; Q9DBR4; -. DR jPOST; Q9DBR4; -. DR PaxDb; 10090-ENSMUSP00000123752; -. DR ProteomicsDB; 296363; -. [Q9DBR4-1] DR ProteomicsDB; 296364; -. [Q9DBR4-2] DR ProteomicsDB; 296365; -. [Q9DBR4-3] DR Pumba; Q9DBR4; -. DR Antibodypedia; 5811; 172 antibodies from 31 providers. DR DNASU; 11787; -. DR Ensembl; ENSMUST00000159786.8; ENSMUSP00000125211.3; ENSMUSG00000029207.18. [Q9DBR4-3] DR Ensembl; ENSMUST00000162349.8; ENSMUSP00000123752.3; ENSMUSG00000029207.18. [Q9DBR4-1] DR GeneID; 11787; -. DR KEGG; mmu:11787; -. DR UCSC; uc008xpb.2; mouse. [Q9DBR4-3] DR UCSC; uc033ijy.1; mouse. [Q9DBR4-1] DR AGR; MGI:108405; -. DR CTD; 323; -. DR MGI; MGI:108405; Apbb2. DR VEuPathDB; HostDB:ENSMUSG00000029207; -. DR eggNOG; ENOG502QT08; Eukaryota. DR GeneTree; ENSGT00390000000002; -. DR InParanoid; Q9DBR4; -. DR OMA; NVPHADD; -. DR OrthoDB; 5969782at2759; -. DR PhylomeDB; Q9DBR4; -. DR BioGRID-ORCS; 11787; 5 hits in 76 CRISPR screens. DR EvolutionaryTrace; Q9DBR4; -. DR PRO; PR:Q9DBR4; -. DR Proteomes; UP000000589; Chromosome 5. DR RNAct; Q9DBR4; protein. DR Bgee; ENSMUSG00000029207; Expressed in undifferentiated genital tubercle and 264 other cell types or tissues. DR ExpressionAtlas; Q9DBR4; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:MGI. DR GO; GO:0005769; C:early endosome; ISS:UniProtKB. DR GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB. DR GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB. DR GO; GO:0005634; C:nucleus; ISO:GO_Central. DR GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central. DR GO; GO:0060090; F:molecular adaptor activity; IBA:GO_Central. DR GO; GO:0007411; P:axon guidance; IGI:MGI. DR GO; GO:0030198; P:extracellular matrix organization; IGI:MGI. DR GO; GO:0036438; P:maintenance of lens transparency; IMP:UniProtKB. DR GO; GO:0043066; P:negative regulation of apoptotic process; IGI:MGI. DR GO; GO:1901988; P:negative regulation of cell cycle phase transition; ISO:GO_Central. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:GO_Central. DR GO; GO:0001764; P:neuron migration; IGI:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; ISS:UniProtKB. DR GO; GO:0050821; P:protein stabilization; NAS:UniProtKB. DR GO; GO:0006355; P:regulation of DNA-templated transcription; IBA:GO_Central. DR GO; GO:0006939; P:smooth muscle contraction; IMP:UniProtKB. DR CDD; cd01272; PTB1_Fe65; 1. DR CDD; cd01271; PTB2_Fe65; 1. DR CDD; cd00201; WW; 1. DR FunFam; 2.30.29.30:FF:000019; Amyloid beta (A4) precursor protein-binding, family B, member 1 (Fe65); 1. DR FunFam; 2.20.70.10:FF:000003; amyloid beta A4 precursor protein-binding family B member 2; 1. DR FunFam; 2.30.29.30:FF:000034; amyloid beta A4 precursor protein-binding family B member 2; 1. DR Gene3D; 2.20.70.10; -; 1. DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 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; AMYLOID BETA A4 PRECURSOR PROTEIN-BINDING FAMILY B; 1. DR PANTHER; PTHR14058:SF11; AMYLOID BETA PRECURSOR PROTEIN BINDING FAMILY B MEMBER 2; 1. DR Pfam; PF00640; PID; 2. DR Pfam; PF00397; WW; 1. DR SMART; SM00462; PTB; 2. DR SMART; SM00456; WW; 1. DR SUPFAM; SSF50729; PH domain-like; 2. DR SUPFAM; SSF51045; WW domain; 1. DR PROSITE; PS01179; PID; 2. DR PROSITE; PS01159; WW_DOMAIN_1; 1. DR PROSITE; PS50020; WW_DOMAIN_2; 1. DR PDBsum; 1WGU; -. DR PDBsum; 2ROZ; -. DR PDBsum; 2YSZ; -. DR PDBsum; 2YT0; -. DR PDBsum; 2YT1; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Endoplasmic reticulum; Endosome; KW Golgi apparatus; Phosphoprotein; Reference proteome; Repeat. FT CHAIN 1..760 FT /note="Amyloid beta precursor protein binding family B FT member 2" FT /id="PRO_0000076053" FT DOMAIN 290..322 FT /note="WW" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224" FT DOMAIN 413..580 FT /note="PID 1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148" FT DOMAIN 586..738 FT /note="PID 2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148" FT REGION 177..295 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 324..351 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 212..230 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 261..275 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 123 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q92870" FT MOD_RES 160 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 334 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 409 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT MOD_RES 412 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21183079" FT VAR_SEQ 348..368 FT /note="Missing (in isoform 2 and isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011661" FT VAR_SEQ 509..510 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_011662" FT STRAND 592..601 FT /evidence="ECO:0007829|PDB:1WGU" FT STRAND 603..605 FT /evidence="ECO:0007829|PDB:2ROZ" FT HELIX 609..620 FT /evidence="ECO:0007829|PDB:1WGU" FT TURN 624..626 FT /evidence="ECO:0007829|PDB:1WGU" FT STRAND 629..635 FT /evidence="ECO:0007829|PDB:1WGU" FT STRAND 638..642 FT /evidence="ECO:0007829|PDB:1WGU" FT STRAND 650..655 FT /evidence="ECO:0007829|PDB:1WGU" FT TURN 656..658 FT /evidence="ECO:0007829|PDB:1WGU" FT STRAND 659..664 FT /evidence="ECO:0007829|PDB:1WGU" FT STRAND 671..676 FT /evidence="ECO:0007829|PDB:1WGU" FT STRAND 678..680 FT /evidence="ECO:0007829|PDB:1WGU" FT STRAND 682..688 FT /evidence="ECO:0007829|PDB:1WGU" FT HELIX 694..704 FT /evidence="ECO:0007829|PDB:1WGU" SQ SEQUENCE 760 AA; 83201 MW; 9E66E34489F4D736 CRC64; MSEVLPADSG VGTLAVFMAS SGSTDIANRN SPATPPNTLN LRSSHNELLN AEIKHSDAKN STPPKCRKKY ALTNIQAAMG LSDPAVQPLL GNGSANIKLV KNGENQLRKA AEQGQQDPNK NLSPAAVINL TSEKLEVKDP HPQESSGCEI LPSQPRRTKS FLNYYADLET SARELGQNLG PCQGVGEEKA QPGPGQAPVV IGNGDLLPQK PNKPQSSPED GQVATVSSSP ETKKDHPKTG AKTDCALHRI QNLAPSDEES SWTTLSQDSA SPSSPDETDI WSDHSFQTDP DLPPGWKRVN DIAGTYYWHI PTGTTQWERP VSIPADLHGS RKGSLSSVTP SPTPENEKQP WSDFAVLNGG KINSDIWKDL HAATVNPDPS LKEFEGATLR YASLKLRNAP HGDDDDSCSI NSDPEAKCFA VRSLGWVEMA EEDLAPGKSS VAVNNCIRQL SYCKNDIRDT VGIWGEGKDM YLSLENDMLS LVDPMDRSVL HSQPIVNIRV WGVGRDNGRE RDFAYVARDK DTRILKCHVF RCDTPAKAIA TSLHEICSKI MAERKNAKAL ACSSLQERTN MSLDVPLQVD FPTPKTELVQ KFRVQYLGML PVDRPVGMDT LNSAIENLMT SSSKEDWPSV NMNVADATVT VISEKNEEEV LVECRVRFLS FMGVGKDVHT FAFIMDTGNQ RFECHVFWCE PNAANVSEAV QAACMLRYQK CLVARPPSQK VRPPPPPADS VTRRVTTNVK RGVLSLIDTL KQKRPVTETP //