APBP2_HUMAN
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 03-AUG-2022, entry version 181.
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},
GN PAT1 {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; 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; B4DJ51: HEL-S-72; NbExp=3; IntAct=EBI-743771, EBI-10171450;
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; 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; O14745: SLC9A3R1; NbExp=3; IntAct=EBI-743771, EBI-349787;
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};
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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 AlphaFoldDB; Q92624; -.
DR SMR; Q92624; -.
DR BioGRID; 115769; 193.
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; Q92624; -.
DR PeptideAtlas; Q92624; -.
DR PRIDE; Q92624; -.
DR ProteomicsDB; 75379; -.
DR Antibodypedia; 31181; 334 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 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; 578212at2759; -.
DR PhylomeDB; Q92624; -.
DR TreeFam; TF314010; -.
DR PathwayCommons; Q92624; -.
DR SignaLink; Q92624; -.
DR UniPathway; UPA00143; -.
DR BioGRID-ORCS; 10513; 11 hits in 1078 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 208 other tissues.
DR ExpressionAtlas; Q92624; baseline and differential.
DR Genevisible; Q92624; HS.
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; -; 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 1: Evidence at protein 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_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
