APBP2_MOUSE
ID APBP2_MOUSE Reviewed; 585 AA.
AC Q9DAX9; Q5SX12; Q80U61;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Amyloid protein-binding protein 2 {ECO:0000305};
DE AltName: Full=Amyloid beta precursor protein-binding protein 2 {ECO:0000250|UniProtKB:Q92624};
DE Short=APP-BP2 {ECO:0000250|UniProtKB:Q92624};
GN Name=Appbp2 {ECO:0000312|MGI:MGI:1914134};
GN Synonyms=Kiaa0228 {ECO:0000303|PubMed:12693553};
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].
RC STRAIN=C57BL/6J; TISSUE=Placenta;
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 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 29-585.
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
CC -!- FUNCTION: Substrate-recognition component of a Cul2-RING (CRL2) E3
CC ubiquitin-protein ligase complex of the DesCEND (destruction via C-end
CC degrons) pathway, which recognizes a C-degron located at the extreme C
CC terminus of target proteins, leading to their ubiquitination and
CC degradation. The C-degron recognized by the DesCEND pathway is usually
CC a motif of less than ten residues and can be present in full-length
CC proteins, truncated proteins or proteolytically cleaved forms. The
CC CRL2(APPBP2) complex specifically recognizes proteins with a -Arg-Xaa-
CC Xaa-Gly degron at the C-terminus, leading to their ubiquitination and
CC degradation. The CRL2(APPBP2) complex mediates ubiquitination and
CC degradation of truncated SELENOV selenoproteins produced by failed
CC UGA/Sec decoding, which end with a -Arg-Xaa-Xaa-Gly degron. May play a
CC role in intracellular protein transport: may be involved in the
CC translocation of APP along microtubules toward the cell surface.
CC {ECO:0000250|UniProtKB:Q92624}.
CC -!- ACTIVITY REGULATION: E3 ubiquitin-protein ligase activity of the
CC CRL2(APPBP2) complex is inhibited by APP.
CC {ECO:0000250|UniProtKB:Q92624}.
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000250|UniProtKB:Q92624}.
CC -!- SUBUNIT: Component of a CRL2 E3 ubiquitin-protein ligase complex, also
CC named ECS (Elongin BC-CUL2/5-SOCS-box protein) complex, composed of
CC CUL2, Elongin BC (ELOB and ELOC), RBX1 and substrate-specific adapter
CC APPBP2. Interacts with APP; APP interaction inhibits the E3 ubiquitin-
CC protein ligase activity of the CRL2(APPBP2) complex.
CC {ECO:0000250|UniProtKB:Q92624}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92624}.
CC Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q92624}. Membrane
CC {ECO:0000250|UniProtKB:Q92624}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q92624}. Note=Associated with membranes and
CC microtubules. {ECO:0000250|UniProtKB:Q92624}.
CC -!- PTM: Rapidly degraded by the proteasome upon overexpression of a C-
CC terminal fragment of APP. {ECO:0000250|UniProtKB:Q92624}.
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DR EMBL; AK005440; BAB24034.1; -; mRNA.
DR EMBL; AL596183; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018442; AAH18442.1; -; mRNA.
DR EMBL; BC019152; AAH19152.1; -; mRNA.
DR EMBL; AK122222; BAC65504.1; -; mRNA.
DR CCDS; CCDS25193.1; -.
DR RefSeq; NP_080101.1; NM_025825.3.
DR AlphaFoldDB; Q9DAX9; -.
DR SMR; Q9DAX9; -.
DR BioGRID; 211787; 3.
DR STRING; 10090.ENSMUSP00000018625; -.
DR iPTMnet; Q9DAX9; -.
DR PhosphoSitePlus; Q9DAX9; -.
DR EPD; Q9DAX9; -.
DR MaxQB; Q9DAX9; -.
DR PaxDb; Q9DAX9; -.
DR PeptideAtlas; Q9DAX9; -.
DR PRIDE; Q9DAX9; -.
DR ProteomicsDB; 296058; -.
DR Antibodypedia; 31181; 334 antibodies from 29 providers.
DR DNASU; 66884; -.
DR Ensembl; ENSMUST00000018625; ENSMUSP00000018625; ENSMUSG00000018481.
DR GeneID; 66884; -.
DR KEGG; mmu:66884; -.
DR UCSC; uc007krj.1; mouse.
DR CTD; 10513; -.
DR MGI; MGI:1914134; Appbp2.
DR VEuPathDB; HostDB:ENSMUSG00000018481; -.
DR eggNOG; KOG1840; Eukaryota.
DR GeneTree; ENSGT00390000010722; -.
DR HOGENOM; CLU_019378_1_0_1; -.
DR InParanoid; Q9DAX9; -.
DR OMA; YAESSHC; -.
DR OrthoDB; 578212at2759; -.
DR PhylomeDB; Q9DAX9; -.
DR TreeFam; TF314010; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 66884; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Appbp2; mouse.
DR PRO; PR:Q9DAX9; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9DAX9; protein.
DR Bgee; ENSMUSG00000018481; Expressed in humerus cartilage element and 243 other tissues.
DR Genevisible; Q9DAX9; MM.
DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; ISS:UniProtKB.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; ISO:MGI.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0046907; P:intracellular transport; ISO:MGI.
DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR042476; APPBP2.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR46575; PTHR46575; 1.
DR SMART; SM00028; TPR; 3.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 2.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Cytoskeleton; Membrane; Microtubule; Nucleus; Protein transport;
KW Reference proteome; Repeat; TPR repeat; Transport; Ubl conjugation pathway.
FT CHAIN 1..585
FT /note="Amyloid protein-binding protein 2"
FT /id="PRO_0000106260"
FT REPEAT 50..83
FT /note="TPR 1"
FT REPEAT 120..153
FT /note="TPR 2"
FT REPEAT 206..239
FT /note="TPR 3"
FT REPEAT 288..321
FT /note="TPR 4"
FT REPEAT 333..367
FT /note="TPR 5"
FT REPEAT 429..462
FT /note="TPR 6"
FT REPEAT 471..505
FT /note="TPR 7"
FT REPEAT 514..547
FT /note="TPR 8"
SQ SEQUENCE 585 AA; 66855 MW; 70779B567F785B81 CRC64;
MAAVELEWIP ETLYNTAISA VVDNYIRSRR DIRSLPENIQ FDVYYKLYQQ GRLCQLGSEF
CELEVFAKVL RALDKRHLLH HCFQALMDHG VKVASVLAYS FSRRCSYIAE SDAAVKEKAI
QVGFVLGGFL SDAGWYSDAE KVFLSCLQLC TLHDEMLHWF RAVECCVRLL HVRNGNCKYH
LGEETFKLAQ TYMDKLSKHG QQANRAALYG ELCALLFAKS HYDEAYKWCV EAMKEITAGL
PVKVVVDVLR QASKACVVKR EFKKAEQLIK HAVYLARDHF GSKHPKYSDT LLDYGFYLLN
VDNICQSVAI YQAALDIRQS VFGGKNIHVA TAHEDLAYSS YVHQYSSGKF DNALFHAERA
IGIITHILPE DHLLLASSKR VKALILEEIA IDCHNKETEQ RLLQEAHDLH LSSLQLAKKA
FGEFNVQTAK HYGNLGRLYQ SMRKFKEAEE MHIKAIQIKE QLLGQEDYEV ALSVGHLASL
YNYDMNQYEN AEKLYLRSIA IGKKLFGEGY SGLEYDYRGL IKLYNSIGNY EKVFEYHNVL
SNWNRLRDRQ YSVTDALEDV SSSPQSTEEV VQSFLMAQNV EGPSC
