ID APBP2_HUMAN Reviewed; 585 AA. AC Q92624; A8K862; O95095; Q8WVC9; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 19-JUL-2004, sequence version 2. DT 27-MAR-2024, entry version 190. DE RecName: Full=Amyloid protein-binding protein 2 {ECO:0000305}; DE AltName: Full=Amyloid beta precursor protein-binding protein 2 {ECO:0000303|PubMed:26138980}; DE Short=APP-BP2 {ECO:0000303|PubMed:26138980}; DE AltName: Full=Protein interacting with APP tail 1 {ECO:0000303|PubMed:9843960}; GN Name=APPBP2 {ECO:0000303|PubMed:26138980, ECO:0000312|HGNC:HGNC:622}; GN Synonyms=KIAA0228 {ECO:0000303|PubMed:9039502}, PAT1 GN {ECO:0000303|PubMed:9843960}; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH APP, AND SUBCELLULAR RP LOCATION. RC TISSUE=Cervix carcinoma; RX PubMed=9843960; DOI=10.1073/pnas.95.25.14745; RA Zheng P., Eastman J., Vande Pol S., Pimplikar S.W.; RT "PAT1, a microtubule-interacting protein, recognizes the basolateral RT sorting signal of amyloid precursor protein."; RL Proc. Natl. Acad. Sci. U.S.A. 95:14745-14750(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow; RX PubMed=9039502; DOI=10.1093/dnares/3.5.321; RA Nagase T., Seki N., Ishikawa K., Ohira M., Kawarabayasi Y., Ohara O., RA Tanaka A., Kotani H., Miyajima N., Nomura N.; RT "Prediction of the coding sequences of unidentified human genes. VI. The RT coding sequences of 80 new genes (KIAA0201-KIAA0280) deduced by analysis of RT cDNA clones from cell line KG-1 and brain."; RL DNA Res. 3:321-329(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Skin; 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 [6] RP PROTEASOMAL DEGRADATION, AND SUBCELLULAR LOCATION. RX PubMed=11742091; DOI=10.1073/pnas.261463298; RA Gao Y., Pimplikar S.W.; RT "The gamma -secretase-cleaved C-terminal fragment of amyloid precursor RT protein mediates signaling to the nucleus."; RL Proc. Natl. Acad. Sci. U.S.A. 98:14979-14984(2001). RN [7] RP FUNCTION. RX PubMed=26138980; DOI=10.1126/science.aab0515; RA Lin H.C., Ho S.C., Chen Y.Y., Khoo K.H., Hsu P.H., Yen H.C.; RT "SELENOPROTEINS. CRL2 aids elimination of truncated selenoproteins produced RT by failed UGA/Sec decoding."; RL Science 349:91-95(2015). RN [8] RP FUNCTION, PATHWAY, AND IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE RP COMPLEX. RX PubMed=29779948; DOI=10.1016/j.cell.2018.04.028; RA Koren I., Timms R.T., Kula T., Xu Q., Li M.Z., Elledge S.J.; RT "The eukaryotic proteome is shaped by E3 ubiquitin ligases targeting C- RT terminal degrons."; RL Cell 173:1622-1635(2018). RN [9] RP FUNCTION, PATHWAY, IDENTIFICATION IN A CRL2 E3 UBIQUITIN-PROTEIN LIGASE RP COMPLEX, INTERACTION WITH APP, AND ACTIVITY REGULATION. RX PubMed=29775578; DOI=10.1016/j.molcel.2018.04.006; RA Lin H.C., Yeh C.W., Chen Y.F., Lee T.T., Hsieh P.Y., Rusnac D.V., Lin S.Y., RA Elledge S.J., Zheng N., Yen H.S.; RT "C-terminal end-directed protein elimination by CRL2 ubiquitin ligases."; RL Mol. Cell 70:602-613(2018). 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 (PubMed:29779948, PubMed:29775578). The C-degron recognized CC by the DesCEND pathway is usually a motif of less than ten residues and CC can be present in full-length proteins, truncated proteins or CC proteolytically cleaved forms (PubMed:29779948, PubMed:29775578). 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 (PubMed:29779948, PubMed:29775578). The CRL2(APPBP2) CC complex mediates ubiquitination and degradation of truncated SELENOV CC selenoproteins produced by failed UGA/Sec decoding, which end with a CC -Arg-Xaa-Xaa-Gly degron (PubMed:26138980). May play a role in CC intracellular protein transport: may be involved in the translocation CC of APP along microtubules toward the cell surface (PubMed:9843960). CC {ECO:0000269|PubMed:26138980, ECO:0000269|PubMed:29775578, CC ECO:0000269|PubMed:29779948, ECO:0000269|PubMed:9843960}. CC -!- ACTIVITY REGULATION: E3 ubiquitin-protein ligase activity of the CC CRL2(APPBP2) complex is inhibited by APP. CC {ECO:0000269|PubMed:29775578}. CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948}. 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 (PubMed:29779948, PubMed:29775578). Interacts with APP; APP CC interaction inhibits the E3 ubiquitin-protein ligase activity of the CC CRL2(APPBP2) complex (PubMed:9843960, PubMed:29775578). CC {ECO:0000269|PubMed:29775578, ECO:0000269|PubMed:29779948, CC ECO:0000269|PubMed:9843960}. CC -!- INTERACTION: CC Q92624; P22760: AADAC; NbExp=3; IntAct=EBI-743771, EBI-13217105; CC Q92624; P12814: ACTN1; NbExp=3; IntAct=EBI-743771, EBI-351710; CC Q92624; P23526: AHCY; NbExp=3; IntAct=EBI-743771, EBI-1053240; CC Q92624; Q9UIJ7: AK3; NbExp=6; IntAct=EBI-743771, EBI-3916527; CC Q92624; O75891-4: ALDH1L1; NbExp=3; IntAct=EBI-743771, EBI-12400198; CC Q92624; Q8IUW1: ANKRD10; NbExp=3; IntAct=EBI-743771, EBI-10261416; CC Q92624; Q9NXR5: ANKRD10; NbExp=3; IntAct=EBI-743771, EBI-10316475; CC Q92624; P05067: APP; NbExp=3; IntAct=EBI-743771, EBI-77613; CC Q92624; Q6P1M9: ARMCX5; NbExp=6; IntAct=EBI-743771, EBI-10252512; CC Q92624; Q9HD20-3: ATP13A1; NbExp=3; IntAct=EBI-743771, EBI-12069500; CC Q92624; Q4VC05-2: BCL7A; NbExp=3; IntAct=EBI-743771, EBI-12065992; CC Q92624; Q9UBW5: BIN2; NbExp=3; IntAct=EBI-743771, EBI-2042570; CC Q92624; Q9BTE2: C16orf35; NbExp=3; IntAct=EBI-743771, EBI-10298364; CC Q92624; Q9BV19: C1orf50; NbExp=6; IntAct=EBI-743771, EBI-2874661; CC Q92624; Q5I0X4: C6orf226; NbExp=6; IntAct=EBI-743771, EBI-10244057; CC Q92624; B4DJ51: CALM1; NbExp=3; IntAct=EBI-743771, EBI-10171450; CC Q92624; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-743771, EBI-9083477; CC Q92624; Q9UK58: CCNL1; NbExp=3; IntAct=EBI-743771, EBI-2836773; CC Q92624; Q00536: CDK16; NbExp=3; IntAct=EBI-743771, EBI-726261; CC Q92624; P35523: CLCN1; NbExp=6; IntAct=EBI-743771, EBI-10206780; CC Q92624; Q17RW2: COL24A1; NbExp=6; IntAct=EBI-743771, EBI-2529266; CC Q92624; Q9UQ03: CORO2B; NbExp=6; IntAct=EBI-743771, EBI-723376; CC Q92624; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-743771, EBI-9087876; CC Q92624; P78368: CSNK1G2; NbExp=3; IntAct=EBI-743771, EBI-748380; CC Q92624; P09228: CST2; NbExp=3; IntAct=EBI-743771, EBI-8832659; CC Q92624; Q2NKJ3: CTC1; NbExp=3; IntAct=EBI-743771, EBI-2562802; CC Q92624; P81605: DCD; NbExp=3; IntAct=EBI-743771, EBI-395625; CC Q92624; Q13268: DHRS2; NbExp=3; IntAct=EBI-743771, EBI-354324; CC Q92624; Q9UPQ8: DOLK; NbExp=3; IntAct=EBI-743771, EBI-8645574; CC Q92624; P16444: DPEP1; NbExp=3; IntAct=EBI-743771, EBI-749514; CC Q92624; Q14117: DPYS; NbExp=3; IntAct=EBI-743771, EBI-12275416; CC Q92624; Q96HE7: ERO1A; NbExp=3; IntAct=EBI-743771, EBI-2564539; CC Q92624; Q12841: FSTL1; NbExp=8; IntAct=EBI-743771, EBI-2349801; CC Q92624; P58549: FXYD7; NbExp=6; IntAct=EBI-743771, EBI-10216171; CC Q92624; Q14435-2: GALNT3; NbExp=3; IntAct=EBI-743771, EBI-10232904; CC Q92624; Q8N6F7: GCSAM; NbExp=6; IntAct=EBI-743771, EBI-10267082; CC Q92624; A0A0C4DFY5: GPRC5C; NbExp=3; IntAct=EBI-743771, EBI-12364679; CC Q92624; P09211: GSTP1; NbExp=6; IntAct=EBI-743771, EBI-353467; CC Q92624; Q04756: HGFAC; NbExp=3; IntAct=EBI-743771, EBI-1041722; CC Q92624; Q8NE63: HIPK4; NbExp=3; IntAct=EBI-743771, EBI-6381114; CC Q92624; A4FTV9: HIST1H2AK; NbExp=3; IntAct=EBI-743771, EBI-10173457; CC Q92624; Q9H2F3: HSD3B7; NbExp=3; IntAct=EBI-743771, EBI-3918847; CC Q92624; P34932: HSPA4; NbExp=6; IntAct=EBI-743771, EBI-356933; CC Q92624; Q14164: IKBKE; NbExp=4; IntAct=EBI-743771, EBI-307369; CC Q92624; P16144-2: ITGB4; NbExp=3; IntAct=EBI-743771, EBI-11051601; CC Q92624; P18084: ITGB5; NbExp=3; IntAct=EBI-743771, EBI-1223434; CC Q92624; P50053-2: KHK; NbExp=3; IntAct=EBI-743771, EBI-12204387; CC Q92624; Q6ZMV9: KIF6; NbExp=3; IntAct=EBI-743771, EBI-751100; CC Q92624; O14901: KLF11; NbExp=3; IntAct=EBI-743771, EBI-948266; CC Q92624; Q6PF15: KLHL35; NbExp=6; IntAct=EBI-743771, EBI-9477654; CC Q92624; Q9NS86: LANCL2; NbExp=6; IntAct=EBI-743771, EBI-2510837; CC Q92624; Q496Y0: LONRF3; NbExp=3; IntAct=EBI-743771, EBI-2690768; CC Q92624; Q9Y383: LUC7L2; NbExp=6; IntAct=EBI-743771, EBI-352851; CC Q92624; Q9P127: LUZP4; NbExp=6; IntAct=EBI-743771, EBI-10198848; CC Q92624; Q9Y2E5: MAN2B2; NbExp=3; IntAct=EBI-743771, EBI-12243024; CC Q92624; Q9GZU1: MCOLN1; NbExp=3; IntAct=EBI-743771, EBI-721209; CC Q92624; Q9UQ53: MGAT4B; NbExp=3; IntAct=EBI-743771, EBI-725713; CC Q92624; P42568: MLLT3; NbExp=4; IntAct=EBI-743771, EBI-716132; CC Q92624; C0H5X0: MMP28; NbExp=3; IntAct=EBI-743771, EBI-12286419; CC Q92624; P43246: MSH2; NbExp=3; IntAct=EBI-743771, EBI-355888; CC Q92624; Q13421-3: MSLN; NbExp=3; IntAct=EBI-743771, EBI-12303989; CC Q92624; Q969V5: MUL1; NbExp=6; IntAct=EBI-743771, EBI-744120; CC Q92624; Q15746-7: MYLK; NbExp=3; IntAct=EBI-743771, EBI-12189939; CC Q92624; P23511: NFYA; NbExp=3; IntAct=EBI-743771, EBI-389739; CC Q92624; O14745: NHERF1; NbExp=3; IntAct=EBI-743771, EBI-349787; CC Q92624; Q9BRL4: PCTK1; NbExp=3; IntAct=EBI-743771, EBI-10296950; CC Q92624; Q7Z6Z6: PNPLA5; NbExp=3; IntAct=EBI-743771, EBI-12241582; CC Q92624; Q8IXY8: PPIL6; NbExp=3; IntAct=EBI-743771, EBI-12226639; CC Q92624; Q12972: PPP1R8; NbExp=3; IntAct=EBI-743771, EBI-716633; CC Q92624; Q12972-2: PPP1R8; NbExp=3; IntAct=EBI-743771, EBI-12252736; CC Q92624; P54646: PRKAA2; NbExp=3; IntAct=EBI-743771, EBI-1383852; CC Q92624; P22694: PRKACB; NbExp=3; IntAct=EBI-743771, EBI-2679622; CC Q92624; P07602: PSAP; NbExp=3; IntAct=EBI-743771, EBI-716699; CC Q92624; Q13635-3: PTCH1; NbExp=3; IntAct=EBI-743771, EBI-14199621; CC Q92624; Q8N2H3: PYROXD2; NbExp=3; IntAct=EBI-743771, EBI-3919450; CC Q92624; Q96AH8: RAB7B; NbExp=3; IntAct=EBI-743771, EBI-3924400; CC Q92624; Q15382: RHEB; NbExp=3; IntAct=EBI-743771, EBI-1055287; CC Q92624; Q5EBL4-3: RILPL1; NbExp=3; IntAct=EBI-743771, EBI-12072024; CC Q92624; Q8TEB7: RNF128; NbExp=3; IntAct=EBI-743771, EBI-2341619; CC Q92624; Q969K3: RNF34; NbExp=3; IntAct=EBI-743771, EBI-2340642; CC Q92624; O60942: RNGTT; NbExp=3; IntAct=EBI-743771, EBI-1237132; CC Q92624; Q15050: RRS1; NbExp=7; IntAct=EBI-743771, EBI-749186; CC Q92624; P59797: SELENOV; NbExp=3; IntAct=EBI-743771, EBI-10216195; CC Q92624; Q8WU57: SELI; NbExp=3; IntAct=EBI-743771, EBI-751012; CC Q92624; Q4U2R8: SLC22A6; NbExp=3; IntAct=EBI-743771, EBI-749741; CC Q92624; Q9BV35: SLC25A23; NbExp=3; IntAct=EBI-743771, EBI-2933255; CC Q92624; Q9NS82: SLC7A10; NbExp=3; IntAct=EBI-743771, EBI-12068238; CC Q92624; Q9Y5X3: SNX5; NbExp=3; IntAct=EBI-743771, EBI-715760; CC Q92624; Q9Y5X3-2: SNX5; NbExp=3; IntAct=EBI-743771, EBI-12229025; CC Q92624; P0CI01: SPDYE6; NbExp=3; IntAct=EBI-743771, EBI-11960469; CC Q92624; O15466: ST8SIA5; NbExp=3; IntAct=EBI-743771, EBI-10182857; CC Q92624; Q9UMZ2: SYNRG; NbExp=3; IntAct=EBI-743771, EBI-7240490; CC Q92624; Q9UMZ2-8: SYNRG; NbExp=3; IntAct=EBI-743771, EBI-12353261; CC Q92624; Q9BT88: SYT11; NbExp=3; IntAct=EBI-743771, EBI-751770; CC Q92624; Q15544: TAF11; NbExp=6; IntAct=EBI-743771, EBI-1027005; CC Q92624; Q96LR4: TAFA4; NbExp=3; IntAct=EBI-743771, EBI-10290841; CC Q92624; Q12788: TBL3; NbExp=4; IntAct=EBI-743771, EBI-715766; CC Q92624; Q9BQ70: TCF25; NbExp=3; IntAct=EBI-743771, EBI-745182; CC Q92624; Q05952: TNP2; NbExp=3; IntAct=EBI-743771, EBI-12039775; CC Q92624; Q8IZ69: TRMT2A; NbExp=3; IntAct=EBI-743771, EBI-2515774; CC Q92624; Q712K3: UBE2R2; NbExp=3; IntAct=EBI-743771, EBI-2340879; CC Q92624; Q9NYU1: UGGT2; NbExp=3; IntAct=EBI-743771, EBI-1054215; CC Q92624; P42768: WAS; NbExp=3; IntAct=EBI-743771, EBI-346375; CC Q92624; Q96S15: WDR24; NbExp=4; IntAct=EBI-743771, EBI-746424; CC Q92624; Q96NZ8: WFIKKN1; NbExp=3; IntAct=EBI-743771, EBI-2363713; CC Q92624; Q96K80: ZC3H10; NbExp=3; IntAct=EBI-743771, EBI-742550; CC Q92624; Q9BV97: ZNF747; NbExp=3; IntAct=EBI-743771, EBI-4395497; CC Q92624; Q9H669; NbExp=3; IntAct=EBI-743771, EBI-10307430; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11742091}. Cytoplasm, CC cytoskeleton {ECO:0000269|PubMed:9843960}. Membrane CC {ECO:0000269|PubMed:9843960}; Peripheral membrane protein CC {ECO:0000269|PubMed:9843960}. Note=Associated with membranes and CC microtubules. {ECO:0000269|PubMed:9843960}. CC -!- PTM: Rapidly degraded by the proteasome upon overexpression of a C- CC terminal fragment of APP. {ECO:0000269|PubMed:11742091}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA13217.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; AF017782; AAC83973.1; -; mRNA. DR EMBL; D86981; BAA13217.1; ALT_INIT; mRNA. DR EMBL; AK292227; BAF84916.1; -; mRNA. DR EMBL; CH471179; EAW51406.1; -; Genomic_DNA. DR EMBL; BC018121; AAH18121.1; -; mRNA. DR CCDS; CCDS32699.1; -. DR RefSeq; NP_001269405.1; NM_001282476.1. DR RefSeq; NP_006371.2; NM_006380.3. DR PDB; 8JAL; EM; 3.30 A; A/B=1-585. DR PDB; 8JAQ; EM; 3.26 A; A/B/J/K=1-578. DR PDB; 8JAR; EM; 3.30 A; A/B=1-579. DR PDB; 8JAS; EM; 3.54 A; A/B/J/K=1-585. DR PDB; 8JAU; EM; 3.22 A; A/B=1-585. DR PDB; 8JAV; EM; 3.44 A; A/B/J/K=1-585. DR PDBsum; 8JAL; -. DR PDBsum; 8JAQ; -. DR PDBsum; 8JAR; -. DR PDBsum; 8JAS; -. DR PDBsum; 8JAU; -. DR PDBsum; 8JAV; -. DR AlphaFoldDB; Q92624; -. DR EMDB; EMD-36129; -. DR EMDB; EMD-36131; -. DR EMDB; EMD-36132; -. DR EMDB; EMD-36133; -. DR EMDB; EMD-36134; -. DR EMDB; EMD-36135; -. DR SMR; Q92624; -. DR BioGRID; 115769; 194. DR ComplexPortal; CPX-2221; APPBP2-Elongin C-Elongin B E3 ubiquitin ligase complex. DR IntAct; Q92624; 155. DR MINT; Q92624; -. DR STRING; 9606.ENSP00000083182; -. DR iPTMnet; Q92624; -. DR PhosphoSitePlus; Q92624; -. DR BioMuta; APPBP2; -. DR DMDM; 50400598; -. DR EPD; Q92624; -. DR jPOST; Q92624; -. DR MassIVE; Q92624; -. DR MaxQB; Q92624; -. DR PaxDb; 9606-ENSP00000083182; -. DR PeptideAtlas; Q92624; -. DR ProteomicsDB; 75379; -. DR Pumba; Q92624; -. DR Antibodypedia; 31181; 364 antibodies from 29 providers. DR DNASU; 10513; -. DR Ensembl; ENST00000083182.8; ENSP00000083182.3; ENSG00000062725.10. DR GeneID; 10513; -. DR KEGG; hsa:10513; -. DR MANE-Select; ENST00000083182.8; ENSP00000083182.3; NM_006380.5; NP_006371.2. DR UCSC; uc002iys.3; human. DR AGR; HGNC:622; -. DR CTD; 10513; -. DR DisGeNET; 10513; -. DR GeneCards; APPBP2; -. DR HGNC; HGNC:622; APPBP2. DR HPA; ENSG00000062725; Low tissue specificity. DR MIM; 605324; gene. DR neXtProt; NX_Q92624; -. DR OpenTargets; ENSG00000062725; -. DR PharmGKB; PA24912; -. DR VEuPathDB; HostDB:ENSG00000062725; -. DR eggNOG; KOG1840; Eukaryota. DR GeneTree; ENSGT00390000010722; -. DR HOGENOM; CLU_019378_1_0_1; -. DR InParanoid; Q92624; -. DR OMA; YAESSHC; -. DR OrthoDB; 2901491at2759; -. DR PhylomeDB; Q92624; -. DR TreeFam; TF314010; -. DR PathwayCommons; Q92624; -. DR SignaLink; Q92624; -. DR UniPathway; UPA00143; -. DR BioGRID-ORCS; 10513; 12 hits in 1158 CRISPR screens. DR ChiTaRS; APPBP2; human. DR GeneWiki; APPBP2; -. DR GenomeRNAi; 10513; -. DR Pharos; Q92624; Tbio. DR PRO; PR:Q92624; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q92624; Protein. DR Bgee; ENSG00000062725; Expressed in endothelial cell and 210 other cell types or tissues. DR ExpressionAtlas; Q92624; baseline and differential. DR GO; GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB. DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc. DR GO; GO:0030659; C:cytoplasmic vesicle membrane; IDA:MGI. DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW. DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:UniProtKB. DR GO; GO:0003777; F:microtubule motor activity; TAS:ProtInc. DR GO; GO:1990756; F:ubiquitin ligase-substrate adaptor activity; IDA:UniProtKB. DR GO; GO:0006886; P:intracellular protein transport; TAS:ProtInc. DR GO; GO:0046907; P:intracellular transport; IDA:MGI. DR GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IDA:UniProtKB. DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2. DR InterPro; IPR042476; APPBP2. DR InterPro; IPR011990; TPR-like_helical_dom_sf. DR InterPro; IPR019734; TPR_repeat. DR PANTHER; PTHR46575; AMYLOID PROTEIN-BINDING PROTEIN 2; 1. DR PANTHER; PTHR46575:SF1; AMYLOID PROTEIN-BINDING PROTEIN 2; 1. DR Pfam; PF13374; TPR_10; 1. DR Pfam; PF13424; TPR_12; 1. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; TPR-like; 2. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 1. DR Genevisible; Q92624; HS. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Cytoskeleton; Membrane; Microtubule; Nucleus; KW Protein transport; Reference proteome; Repeat; TPR repeat; Transport; KW Ubl conjugation pathway. FT CHAIN 1..585 FT /note="Amyloid protein-binding protein 2" FT /id="PRO_0000106259" 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" FT VARIANT 561 FT /note="S -> N (in dbSNP:rs34146848)" FT /id="VAR_052606" FT CONFLICT 296 FT /note="F -> L (in Ref. 1; AAC83973)" FT /evidence="ECO:0000305" FT CONFLICT 325 FT /note="K -> R (in Ref. 1; AAC83973)" FT /evidence="ECO:0000305" FT CONFLICT 340 FT /note="S -> C (in Ref. 1; AAC83973)" FT /evidence="ECO:0000305" FT CONFLICT 354 FT /note="L -> V (in Ref. 1; AAC83973)" FT /evidence="ECO:0000305" FT CONFLICT 369 FT /note="P -> R (in Ref. 1; AAC83973)" FT /evidence="ECO:0000305" FT CONFLICT 542 FT /note="N -> K (in Ref. 1; AAC83973)" FT /evidence="ECO:0000305" SQ SEQUENCE 585 AA; 66853 MW; 849A120807DA2438 CRC64; MAAVELEWIP ETLYNTAISA VVDNYIRSRR DIRSLPENIQ FDVYYKLYQQ GRLCQLGSEF CELEVFAKVL RALDKRHLLH HCFQALMDHG VKVASVLAYS FSRRCSYIAE SDAAVKEKAI QVGFVLGGFL SDAGWYSDAE KVFLSCLQLC TLHDEMLHWF RAVECCVRLL HVRNGNCKYH LGEETFKLAQ TYMDKLSKHG QQANKAALYG ELCALLFAKS HYDEAYKWCI 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 STSPQSTEEV VQSFLISQNV EGPSC //