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APBB2_MOUSE
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   03-AUG-2022, entry version 145.
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},
GN   Fe65l1 {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}.
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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_001201414.1.
DR   RefSeq; NP_001188344.1; NM_001201415.1. [Q9DBR4-3]
DR   RefSeq; NP_033816.1; NM_009686.2. [Q9DBR4-1]
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   PDBsum; 1WGU; -.
DR   PDBsum; 2ROZ; -.
DR   PDBsum; 2YSZ; -.
DR   PDBsum; 2YT0; -.
DR   PDBsum; 2YT1; -.
DR   AlphaFoldDB; Q9DBR4; -.
DR   BMRB; Q9DBR4; -.
DR   SMR; Q9DBR4; -.
DR   BioGRID; 198142; 6.
DR   ELM; Q9DBR4; -.
DR   IntAct; Q9DBR4; 1.
DR   MINT; Q9DBR4; -.
DR   STRING; 10090.ENSMUSP00000125211; -.
DR   iPTMnet; Q9DBR4; -.
DR   PhosphoSitePlus; Q9DBR4; -.
DR   jPOST; Q9DBR4; -.
DR   MaxQB; Q9DBR4; -.
DR   PaxDb; Q9DBR4; -.
DR   PRIDE; Q9DBR4; -.
DR   ProteomicsDB; 296363; -. [Q9DBR4-1]
DR   ProteomicsDB; 296364; -. [Q9DBR4-2]
DR   ProteomicsDB; 296365; -. [Q9DBR4-3]
DR   Antibodypedia; 5811; 180 antibodies from 30 providers.
DR   DNASU; 11787; -.
DR   Ensembl; ENSMUST00000159786; ENSMUSP00000125211; ENSMUSG00000029207. [Q9DBR4-3]
DR   Ensembl; ENSMUST00000162349; ENSMUSP00000123752; ENSMUSG00000029207. [Q9DBR4-1]
DR   GeneID; 11787; -.
DR   KEGG; mmu:11787; -.
DR   UCSC; uc008xpb.2; mouse. [Q9DBR4-3]
DR   UCSC; uc033ijy.1; mouse. [Q9DBR4-1]
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; 437627at2759; -.
DR   PhylomeDB; Q9DBR4; -.
DR   TreeFam; TF314331; -.
DR   BioGRID-ORCS; 11787; 5 hits in 71 CRISPR screens.
DR   ChiTaRS; Apbb2; mouse.
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 261 other tissues.
DR   ExpressionAtlas; Q9DBR4; baseline and differential.
DR   Genevisible; Q9DBR4; MM.
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:MGI.
DR   GO; GO:0001540; F:amyloid-beta binding; 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:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
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 transcription, DNA-templated; IBA:GO_Central.
DR   GO; GO:0006939; P:smooth muscle contraction; IMP:UniProtKB.
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   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        209..230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        254..281
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        332..348
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
 
 
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