APBB2_HUMAN
ID APBB2_HUMAN Reviewed; 758 AA.
AC Q92870; B4DSL4; E9PG87; Q8IUI6;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Amyloid beta precursor protein binding family B member 2 {ECO:0000312|HGNC:HGNC:582};
DE AltName: Full=Amyloid-beta (A4) precursor protein-binding family B member 2 {ECO:0000250|UniProtKB:Q9DBR4};
DE AltName: Full=Protein Fe65-like 1 {ECO:0000312|HGNC:HGNC:582};
GN Name=APBB2 {ECO:0000312|HGNC:HGNC:582};
GN Synonyms=FE65L {ECO:0000312|HGNC:HGNC:582},
GN FE65L1 {ECO:0000303|PubMed:14527950};
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 [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND VARIANT GLN-179.
RC TISSUE=Aortic endothelium;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RT "Homo sapiens protein coding cDNA.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT GLN-179.
RC TISSUE=Lung;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 66-758 (ISOFORM 1), INTERACTION WITH APLP2
RP AND APP, AND TISSUE SPECIFICITY.
RC TISSUE=Fetal brain, and Kidney;
RX PubMed=8855266; DOI=10.1073/pnas.93.20.10832;
RA Guenette S.Y., Chen J., Jondro P.D., Tanzi R.E.;
RT "Association of a novel human FE65-like protein with the cytoplasmic domain
RT of the amyloid-beta precursor protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:10832-10837(1996).
RN [6]
RP FUNCTION, INTERACTION WITH APP, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
RP CYS-702.
RX PubMed=14527950; DOI=10.1074/jbc.m309561200;
RA Chang Y., Tesco G., Jeong W.J., Lindsley L., Eckman E.A., Eckman C.B.,
RA Tanzi R.E., Guenette S.Y.;
RT "Generation of the beta-amyloid peptide and the amyloid precursor protein
RT C-terminal fragment gamma are potentiated by FE65L1.";
RL J. Biol. Chem. 278:51100-51107(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-334, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Plays a role in the maintenance of lens transparency, and may
CC also play a role in muscle cell strength (By similarity). Involved in
CC hippocampal neurite branching and neuromuscular junction formation, as
CC a result plays a role in spatial memory functioning (By similarity).
CC Activates transcription of APP (PubMed:14527950).
CC {ECO:0000250|UniProtKB:Q9DBR4, ECO:0000269|PubMed:14527950}.
CC -!- SUBUNIT: Interacts (via C-terminus) with APP (via C-terminus)
CC (PubMed:8855266, PubMed:14527950). Interacts with APLP2 (via
CC cytoplasmic domain) (PubMed:8855266). {ECO:0000269|PubMed:14527950,
CC ECO:0000269|PubMed:8855266}.
CC -!- INTERACTION:
CC Q92870; P05067: APP; NbExp=3; IntAct=EBI-79277, EBI-77613;
CC Q92870; P00533: EGFR; NbExp=7; IntAct=EBI-79277, EBI-297353;
CC Q92870-2; Q6PCB6: ABHD17C; NbExp=3; IntAct=EBI-21535880, EBI-22011868;
CC Q92870-2; O43488: AKR7A2; NbExp=3; IntAct=EBI-21535880, EBI-748855;
CC Q92870-2; P63010-2: AP2B1; NbExp=3; IntAct=EBI-21535880, EBI-11529439;
CC Q92870-2; D3DTF8: APLN; NbExp=3; IntAct=EBI-21535880, EBI-22002556;
CC Q92870-2; P05067: APP; NbExp=3; IntAct=EBI-21535880, EBI-77613;
CC Q92870-2; Q8N6T3-3: ARFGAP1; NbExp=3; IntAct=EBI-21535880, EBI-10694449;
CC Q92870-2; Q0P5N6: ARL16; NbExp=3; IntAct=EBI-21535880, EBI-10186132;
CC Q92870-2; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-21535880, EBI-10254793;
CC Q92870-2; Q96FT7-4: ASIC4; NbExp=3; IntAct=EBI-21535880, EBI-9089489;
CC Q92870-2; P18847: ATF3; NbExp=3; IntAct=EBI-21535880, EBI-712767;
CC Q92870-2; Q9BUW7: BBLN; NbExp=3; IntAct=EBI-21535880, EBI-752084;
CC Q92870-2; O15392: BIRC5; NbExp=3; IntAct=EBI-21535880, EBI-518823;
CC Q92870-2; Q96LC9: BMF; NbExp=3; IntAct=EBI-21535880, EBI-3919268;
CC Q92870-2; Q8N865: C7orf31; NbExp=3; IntAct=EBI-21535880, EBI-10174456;
CC Q92870-2; Q9UQM7: CAMK2A; NbExp=3; IntAct=EBI-21535880, EBI-1383687;
CC Q92870-2; Q5JTY5: CBWD3; NbExp=3; IntAct=EBI-21535880, EBI-723434;
CC Q92870-2; P24863: CCNC; NbExp=3; IntAct=EBI-21535880, EBI-395261;
CC Q92870-2; O95674: CDS2; NbExp=3; IntAct=EBI-21535880, EBI-3913685;
CC Q92870-2; Q9UER7: DAXX; NbExp=3; IntAct=EBI-21535880, EBI-77321;
CC Q92870-2; O60479: DLX3; NbExp=3; IntAct=EBI-21535880, EBI-3908248;
CC Q92870-2; Q92782-2: DPF1; NbExp=3; IntAct=EBI-21535880, EBI-23669343;
CC Q92870-2; A0AVK6: E2F8; NbExp=3; IntAct=EBI-21535880, EBI-7779316;
CC Q92870-2; O00472: ELL2; NbExp=3; IntAct=EBI-21535880, EBI-395274;
CC Q92870-2; Q8TC29: ENKUR; NbExp=3; IntAct=EBI-21535880, EBI-9246952;
CC Q92870-2; Q6NXG1-3: ESRP1; NbExp=3; IntAct=EBI-21535880, EBI-21567429;
CC Q92870-2; Q99504: EYA3; NbExp=3; IntAct=EBI-21535880, EBI-9089567;
CC Q92870-2; Q5XKR9-2: FAM104B; NbExp=3; IntAct=EBI-21535880, EBI-19946114;
CC Q92870-2; O15287: FANCG; NbExp=3; IntAct=EBI-21535880, EBI-81610;
CC Q92870-2; Q6PIV2: FOXR1; NbExp=3; IntAct=EBI-21535880, EBI-10253815;
CC Q92870-2; P06241: FYN; NbExp=3; IntAct=EBI-21535880, EBI-515315;
CC Q92870-2; Q969S8: HDAC10; NbExp=3; IntAct=EBI-21535880, EBI-301762;
CC Q92870-2; P52790: HK3; NbExp=3; IntAct=EBI-21535880, EBI-2965780;
CC Q92870-2; P20719: HOXA5; NbExp=3; IntAct=EBI-21535880, EBI-8470697;
CC Q92870-2; Q6DN90-2: IQSEC1; NbExp=3; IntAct=EBI-21535880, EBI-21911304;
CC Q92870-2; Q96SI1-2: KCTD15; NbExp=3; IntAct=EBI-21535880, EBI-12382297;
CC Q92870-2; Q8N5Z5: KCTD17; NbExp=3; IntAct=EBI-21535880, EBI-743960;
CC Q92870-2; Q6P597: KLC3; NbExp=3; IntAct=EBI-21535880, EBI-1643885;
CC Q92870-2; Q8IUB9: KRTAP19-1; NbExp=3; IntAct=EBI-21535880, EBI-12811111;
CC Q92870-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-21535880, EBI-10261141;
CC Q92870-2; Q8N0U6: LINC00518; NbExp=3; IntAct=EBI-21535880, EBI-10264791;
CC Q92870-2; Q6ZP95: LOC642947; NbExp=3; IntAct=EBI-21535880, EBI-25831954;
CC Q92870-2; Q03112-9: MECOM; NbExp=3; IntAct=EBI-21535880, EBI-23820194;
CC Q92870-2; P50221: MEOX1; NbExp=3; IntAct=EBI-21535880, EBI-2864512;
CC Q92870-2; Q8TDB4: MGARP; NbExp=3; IntAct=EBI-21535880, EBI-4397720;
CC Q92870-2; A4FUJ8: MKL1; NbExp=3; IntAct=EBI-21535880, EBI-21250407;
CC Q92870-2; Q13064: MKRN3; NbExp=3; IntAct=EBI-21535880, EBI-2340269;
CC Q92870-2; Q9Y605: MRFAP1; NbExp=3; IntAct=EBI-21535880, EBI-995714;
CC Q92870-2; Q9Y3D2: MSRB2; NbExp=3; IntAct=EBI-21535880, EBI-9092052;
CC Q92870-2; Q8WY64: MYLIP; NbExp=3; IntAct=EBI-21535880, EBI-6952711;
CC Q92870-2; Q69YI7-2: NAIF1; NbExp=3; IntAct=EBI-21535880, EBI-18040878;
CC Q92870-2; Q9Y2A7: NCKAP1; NbExp=3; IntAct=EBI-21535880, EBI-389845;
CC Q92870-2; Q6PHZ7: NR2C2; NbExp=3; IntAct=EBI-21535880, EBI-2802743;
CC Q92870-2; Q16656-4: NRF1; NbExp=3; IntAct=EBI-21535880, EBI-11742836;
CC Q92870-2; Q9NPJ8-3: NXT2; NbExp=3; IntAct=EBI-21535880, EBI-10698339;
CC Q92870-2; O43482: OIP5; NbExp=3; IntAct=EBI-21535880, EBI-536879;
CC Q92870-2; Q96CV9-2: OPTN; NbExp=3; IntAct=EBI-21535880, EBI-9091423;
CC Q92870-2; Q6VY07: PACS1; NbExp=3; IntAct=EBI-21535880, EBI-2555014;
CC Q92870-2; P22061-2: PCMT1; NbExp=3; IntAct=EBI-21535880, EBI-12386584;
CC Q92870-2; O15534: PER1; NbExp=3; IntAct=EBI-21535880, EBI-2557276;
CC Q92870-2; O75925: PIAS1; NbExp=3; IntAct=EBI-21535880, EBI-629434;
CC Q92870-2; P78337: PITX1; NbExp=3; IntAct=EBI-21535880, EBI-748265;
CC Q92870-2; Q6ZR37: PLEKHG7; NbExp=3; IntAct=EBI-21535880, EBI-12891828;
CC Q92870-2; Q9H1D9: POLR3F; NbExp=3; IntAct=EBI-21535880, EBI-710067;
CC Q92870-2; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-21535880, EBI-710402;
CC Q92870-2; P17612: PRKACA; NbExp=3; IntAct=EBI-21535880, EBI-476586;
CC Q92870-2; A0A0C4DFM3: PRUNE2; NbExp=3; IntAct=EBI-21535880, EBI-25830870;
CC Q92870-2; Q9H0N0: RAB6C; NbExp=3; IntAct=EBI-21535880, EBI-2856714;
CC Q92870-2; Q96D59: RNF183; NbExp=3; IntAct=EBI-21535880, EBI-743938;
CC Q92870-2; O75446: SAP30; NbExp=3; IntAct=EBI-21535880, EBI-632609;
CC Q92870-2; Q6UVJ0: SASS6; NbExp=3; IntAct=EBI-21535880, EBI-1570153;
CC Q92870-2; Q8IYI0: SHLD1; NbExp=3; IntAct=EBI-21535880, EBI-2560428;
CC Q92870-2; Q9NSD5-3: SLC6A13; NbExp=3; IntAct=EBI-21535880, EBI-25831241;
CC Q92870-2; Q9BT81: SOX7; NbExp=3; IntAct=EBI-21535880, EBI-7239117;
CC Q92870-2; Q7Z6I5: SPATA12; NbExp=3; IntAct=EBI-21535880, EBI-10696971;
CC Q92870-2; Q8IUW3: SPATA2L; NbExp=3; IntAct=EBI-21535880, EBI-2510414;
CC Q92870-2; Q7Z698: SPRED2; NbExp=3; IntAct=EBI-21535880, EBI-7082156;
CC Q92870-2; O75886: STAM2; NbExp=3; IntAct=EBI-21535880, EBI-373258;
CC Q92870-2; Q9BR01-2: SULT4A1; NbExp=3; IntAct=EBI-21535880, EBI-25831443;
CC Q92870-2; Q8NBJ7: SUMF2; NbExp=3; IntAct=EBI-21535880, EBI-723091;
CC Q92870-2; Q13569: TDG; NbExp=3; IntAct=EBI-21535880, EBI-348333;
CC Q92870-2; Q96MW7: TIGD1; NbExp=3; IntAct=EBI-21535880, EBI-9091586;
CC Q92870-2; Q53NU3: tmp_locus_54; NbExp=3; IntAct=EBI-21535880, EBI-10242677;
CC Q92870-2; Q71RG4-4: TMUB2; NbExp=3; IntAct=EBI-21535880, EBI-25831574;
CC Q92870-2; Q13404: UBE2V1; NbExp=3; IntAct=EBI-21535880, EBI-1050671;
CC Q92870-2; P45880: VDAC2; NbExp=3; IntAct=EBI-21535880, EBI-354022;
CC Q92870-2; P58304: VSX2; NbExp=3; IntAct=EBI-21535880, EBI-6427899;
CC Q92870-2; Q13105: ZBTB17; NbExp=3; IntAct=EBI-21535880, EBI-372156;
CC Q92870-2; Q96K21: ZFYVE19; NbExp=3; IntAct=EBI-21535880, EBI-6448240;
CC Q92870-2; Q96EF9: ZHX1-C8orf76; NbExp=3; IntAct=EBI-21535880, EBI-25830993;
CC Q92870-2; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-21535880, EBI-2682299;
CC Q92870-2; Q8N895: ZNF366; NbExp=3; IntAct=EBI-21535880, EBI-2813661;
CC Q92870-2; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-21535880, EBI-25831733;
CC Q92870-2; O43257: ZNHIT1; NbExp=3; IntAct=EBI-21535880, EBI-347522;
CC Q92870-2; A8K878; NbExp=3; IntAct=EBI-21535880, EBI-25831303;
CC Q92870-2; B7Z3E8; NbExp=3; IntAct=EBI-21535880, EBI-25831617;
CC Q92870-2; Q7L8T7; NbExp=3; IntAct=EBI-21535880, EBI-25831943;
CC Q92870-2; Q7Z637; NbExp=3; IntAct=EBI-21535880, EBI-25831475;
CC Q92870-2; Q9H669; NbExp=3; IntAct=EBI-21535880, EBI-10307430;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum
CC {ECO:0000269|PubMed:14527950}. Golgi apparatus
CC {ECO:0000269|PubMed:14527950}. Early endosome
CC {ECO:0000269|PubMed:14527950}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q92870-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q92870-2; Sequence=VSP_040354, VSP_040355;
CC Name=3;
CC IsoId=Q92870-3; Sequence=VSP_044232;
CC Name=4;
CC IsoId=Q92870-4; Sequence=VSP_045042;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:8855266}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC50805.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Sequence of unknown origin in the N-terminal part.; Evidence={ECO:0000305};
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DR EMBL; AK299800; BAG61676.1; -; mRNA.
DR EMBL; AK226179; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC093804; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC096712; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC108937; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC131953; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027946; AAH27946.2; -; mRNA.
DR EMBL; U62325; AAC50805.1; ALT_SEQ; mRNA.
DR CCDS; CCDS43224.1; -. [Q92870-2]
DR CCDS; CCDS54760.1; -. [Q92870-3]
DR CCDS; CCDS54761.1; -. [Q92870-1]
DR CCDS; CCDS54762.1; -. [Q92870-4]
DR RefSeq; NP_001159522.1; NM_001166050.1. [Q92870-1]
DR RefSeq; NP_001159523.1; NM_001166051.1. [Q92870-3]
DR RefSeq; NP_001159524.1; NM_001166052.1. [Q92870-3]
DR RefSeq; NP_001159525.1; NM_001166053.1. [Q92870-3]
DR RefSeq; NP_001159526.1; NM_001166054.1. [Q92870-3]
DR RefSeq; NP_001317585.1; NM_001330656.1.
DR RefSeq; NP_001317587.1; NM_001330658.1.
DR RefSeq; NP_775098.2; NM_173075.4. [Q92870-2]
DR RefSeq; XP_016863634.1; XM_017008145.1. [Q92870-4]
DR AlphaFoldDB; Q92870; -.
DR SMR; Q92870; -.
DR BioGRID; 106820; 78.
DR IntAct; Q92870; 125.
DR MINT; Q92870; -.
DR STRING; 9606.ENSP00000427211; -.
DR iPTMnet; Q92870; -.
DR PhosphoSitePlus; Q92870; -.
DR BioMuta; APBB2; -.
DR DMDM; 317373476; -.
DR EPD; Q92870; -.
DR jPOST; Q92870; -.
DR MassIVE; Q92870; -.
DR MaxQB; Q92870; -.
DR PaxDb; Q92870; -.
DR PeptideAtlas; Q92870; -.
DR PRIDE; Q92870; -.
DR ProteomicsDB; 20267; -.
DR ProteomicsDB; 5034; -.
DR ProteomicsDB; 75555; -. [Q92870-1]
DR ProteomicsDB; 75556; -. [Q92870-2]
DR Antibodypedia; 5811; 180 antibodies from 30 providers.
DR DNASU; 323; -.
DR Ensembl; ENST00000295974.12; ENSP00000295974.8; ENSG00000163697.17. [Q92870-1]
DR Ensembl; ENST00000502841.5; ENSP00000425802.1; ENSG00000163697.17. [Q92870-3]
DR Ensembl; ENST00000504305.5; ENSP00000423765.1; ENSG00000163697.17. [Q92870-3]
DR Ensembl; ENST00000508593.6; ENSP00000427211.1; ENSG00000163697.17. [Q92870-4]
DR Ensembl; ENST00000513140.5; ENSP00000426018.1; ENSG00000163697.17. [Q92870-2]
DR Ensembl; ENST00000543538.5; ENSP00000439357.1; ENSG00000163697.17. [Q92870-3]
DR GeneID; 323; -.
DR KEGG; hsa:323; -.
DR MANE-Select; ENST00000508593.6; ENSP00000427211.1; NM_004307.2; NP_004298.1. [Q92870-4]
DR UCSC; uc003gvk.4; human. [Q92870-1]
DR CTD; 323; -.
DR DisGeNET; 323; -.
DR GeneCards; APBB2; -.
DR HGNC; HGNC:582; APBB2.
DR HPA; ENSG00000163697; Tissue enhanced (brain).
DR MIM; 602710; gene.
DR neXtProt; NX_Q92870; -.
DR OpenTargets; ENSG00000163697; -.
DR PharmGKB; PA24874; -.
DR VEuPathDB; HostDB:ENSG00000163697; -.
DR eggNOG; ENOG502QT08; Eukaryota.
DR GeneTree; ENSGT00390000000002; -.
DR HOGENOM; CLU_092267_0_0_1; -.
DR InParanoid; Q92870; -.
DR OMA; NVPHADD; -.
DR OrthoDB; 437627at2759; -.
DR PhylomeDB; Q92870; -.
DR TreeFam; TF314331; -.
DR PathwayCommons; Q92870; -.
DR SignaLink; Q92870; -.
DR BioGRID-ORCS; 323; 4 hits in 1068 CRISPR screens.
DR ChiTaRS; APBB2; human.
DR GeneWiki; APBB2; -.
DR GenomeRNAi; 323; -.
DR Pharos; Q92870; Tbio.
DR PRO; PR:Q92870; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q92870; protein.
DR Bgee; ENSG00000163697; Expressed in buccal mucosa cell and 198 other tissues.
DR ExpressionAtlas; Q92870; baseline and differential.
DR Genevisible; Q92870; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; ISS:UniProtKB.
DR GO; GO:0001540; F:amyloid-beta binding; IBA:GO_Central.
DR GO; GO:0035556; P:intracellular signal transduction; NAS:UniProtKB.
DR GO; GO:0036438; P:maintenance of lens transparency; ISS:UniProtKB.
DR GO; GO:1901988; P:negative regulation of cell cycle phase transition; IDA:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR GO; GO:0006939; P:smooth muscle contraction; ISS:UniProtKB.
DR GO; GO:0050808; P:synapse organization; ISS:ARUK-UCL.
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 Alternative splicing; Endoplasmic reticulum; Endosome; Golgi apparatus;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..758
FT /note="Amyloid beta precursor protein binding family B
FT member 2"
FT /id="PRO_0000076052"
FT DOMAIN 290..322
FT /note="WW"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 413..578
FT /note="PID 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 584..736
FT /note="PID 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT REGION 134..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 176..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 326..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..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 329..348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 334
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBR4"
FT MOD_RES 412
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBR4"
FT VAR_SEQ 1..548
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044232"
FT VAR_SEQ 278
FT /note="T -> TA (in isoform 4)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_045042"
FT VAR_SEQ 348..368
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040354"
FT VAR_SEQ 577
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040355"
FT VARIANT 179
FT /note="R -> Q (in dbSNP:rs4861358)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_069029"
FT MUTAGEN 702
FT /note="C->V: Abolishes interaction with APP and gamma-
FT secretase-dependent processing of the APP membrane-anchored
FT C-terminal fragment C83."
FT /evidence="ECO:0000269|PubMed:14527950"
FT CONFLICT 490
FT /note="L -> W (in Ref. 5; AAC50805)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 83374 MW; 453521022CD548D5 CRC64;
MSEVLPADSG VDTLAVFMAS SGTTDVTNRN SPATPPNTLN LRSSHNELLN AEIKHTETKN
STPPKCRKKY ALTNIQAAMG LSDPAAQPLL GNGSANIKLV KNGENQLRKA AEQGQQDPNK
NLSPTAVINI TSEKLEGKEP HPQDSSSCEI LPSQPRRTKS FLNYYADLET SARELEQNRG
NHHGTAEEKS QPVQGQASTI IGNGDLLLQK PNRPQSSPED GQVATVSSSP ETKKDHPKTG
AKTDCALHRI QNLAPSDEES SWTTLSQDSA SPSSPDETDI WSDHSFQTDP DLPPGWKRVS
DIAGTYYWHI PTGTTQWERP VSIPADLQGS RKGSLSSVTP SPTPENEKQP WSDFAVLNGG
KINSDIWKDL HAATVNPDPS LKEFEGATLR YASLKLRNAP HPDDDDSCSI NSDPEAKCFA
VRSLGWVEMA EEDLAPGKSS VAVNNCIRQL SYCKNDIRDT VGIWGEGKDM YLILENDMLS
LVDPMDRSVL HSQPIVSIRV WGVGRDNGRD FAYVARDKDT RILKCHVFRC DTPAKAIATS
LHEICSKIMA ERKNAKALAC SSLQERANVN LDVPLQVDFP TPKTELVQKF HVQYLGMLPV
DKPVGMDILN SAIENLMTSS NKEDWLSVNM NVADATVTVI SEKNEEEVLV ECRVRFLSFM
GVGKDVHTFA FIMDTGNQRF ECHVFWCEPN AGNVSEAVQA ACMLRYQKCL VARPPSQKVR
PPPPPADSVT RRVTTNVKRG VLSLIDTLKQ KRPVTEMP
