ID NBR1_HUMAN Reviewed; 966 AA. AC Q14596; Q13173; Q15026; Q5J7Q8; Q96GB6; Q9NRF7; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 27-MAR-2024, entry version 219. DE RecName: Full=Next to BRCA1 gene 1 protein; DE AltName: Full=Cell migration-inducing gene 19 protein; DE AltName: Full=Membrane component chromosome 17 surface marker 2; DE AltName: Full=Neighbor of BRCA1 gene 1 protein; DE AltName: Full=Protein 1A1-3B; GN Name=NBR1; Synonyms=1A13B, KIAA0049, M17S2; ORFNames=MIG19; 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] (ISOFORM 1), AND VARIANT ARG-923. RC TISSUE=Ovary; RX PubMed=8069304; DOI=10.1093/hmg/3.4.589; RA Campbell I.G., Nicolai H.M., Foulkes W.D., Senger G., Stamp G.W., Allan G., RA Boyer C., Jones K., Bast R.C. Jr., Solomon E., Trowsdale J., Black D.M.; RT "A novel gene encoding a B-box protein within the BRCA1 region at RT 17q21.1."; RL Hum. Mol. Genet. 3:589-594(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., RA Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. The RT coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of RT cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Kim J.W.; RT "Identification of a human migration inducing gene."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [5] 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 [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT ARG-923. RC TISSUE=Lymph; 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 [7] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-42, AND VARIANT ARG-923. RC TISSUE=Testis; RX PubMed=11179671; DOI=10.1016/s0378-1119(00)00549-7; RA Dimitrov S., Brennerova M., Forejt J.; RT "Expression profiles and intergenic structure of head-to-head oriented RT Brca1 and Nbr1 genes."; RL Gene 262:89-98(2001). RN [8] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 412-508. RX PubMed=7581362; DOI=10.1093/hmg/4.8.1259; RA Harshman K., Bell R., Rosenthal J., Katcher H., Miki Y., Swenson J., RA Gholami Z., Frye C., Ding W., Dayananth P., Eddington K., Norris F.H., RA Bristow P.K., Phelps R., Hattier T., Stone S., Shaffer D., Bayer S., RA Hussey C., Tran T., Lai M., Rosteck P.R. Jr., Skolnick M.H., RA Shattuck-Eidens D., Kamb A.; RT "Comparison of the positional cloning methods used to isolate the BRCA1 RT gene."; RL Hum. Mol. Genet. 4:1259-1266(1995). RN [9] RP INTERACTION WITH SQSTM1, OLIGOMERIZATION, DOMAIN, AND MUTAGENESIS OF LYS-12 RP AND ASP-50. RX PubMed=12813044; DOI=10.1074/jbc.m303221200; RA Lamark T., Perander M., Outzen H., Kristiansen K., Oevervatn A., RA Michaelsen E., Bjoerkoey G., Johansen T.; RT "Interaction codes within the family of mammalian Phox and Bem1p domain- RT containing proteins."; RL J. Biol. Chem. 278:34568-34581(2003). RN [10] RP INTERACTION WITH SQSTM1; TTN AND RNF29. RX PubMed=15802564; DOI=10.1126/science.1110463; RA Lange S., Xiang F., Yakovenko A., Vihola A., Hackman P., Rostkova E., RA Kristensen J., Brandmeier B., Franzen G., Hedberg B., Gunnarsson L.G., RA Hughes S.M., Marchand S., Sejersen T., Richard I., Edstroem L., Ehler E., RA Udd B., Gautel M.; RT "The kinase domain of titin controls muscle gene expression and protein RT turnover."; RL Science 308:1599-1603(2005). RN [11] RP PROTEOLYTIC CLEAVAGE (MICROBIAL INFECTION). RX PubMed=24331465; DOI=10.1016/j.chom.2013.11.003; RA Barnett T.C., Liebl D., Seymour L.M., Gillen C.M., Lim J.Y., Larock C.N., RA Davies M.R., Schulz B.L., Nizet V., Teasdale R.D., Walker M.J.; RT "The globally disseminated M1T1 clone of group A Streptococcus evades RT autophagy for intracellular replication."; RL Cell Host Microbe 14:675-682(2013). RN [12] RP INTERACTION WITH USP8, UBIQUITIN-BINDING, AND SUBCELLULAR LOCATION. RX PubMed=19427866; DOI=10.1016/j.febslet.2009.04.049; RA Waters S., Marchbank K., Solomon E., Whitehouse C., Gautel M.; RT "Interactions with LC3 and polyubiquitin chains link nbr1 to autophagic RT protein turnover."; RL FEBS Lett. 583:1846-1852(2009). RN [13] RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH SQSTM1; MAP1LC3A; RP MAP1LC3B; MAP1LC3C; GABARAP; GABARAPL1 AND GABARAPL2, AND MUTAGENESIS OF RP ASP-50 AND TYR-732. RX PubMed=19250911; DOI=10.1016/j.molcel.2009.01.020; RA Kirkin V., Lamark T., Sou Y.S., Bjorkoy G., Nunn J.L., Bruun J.A., RA Shvets E., McEwan D.G., Clausen T.H., Wild P., Bilusic I., Theurillat J.P., RA Overvatn A., Ishii T., Elazar Z., Komatsu M., Dikic I., Johansen T.; RT "A role for NBR1 in autophagosomal degradation of ubiquitinated RT substrates."; RL Mol. Cell 33:505-516(2009). RN [14] 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 [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116 AND SER-625, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; 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 [16] RP FUNCTION, PHOSPHORYLATION AT THR-586, MUTAGENESIS OF THR-586, AND RP SUBCELLULAR LOCATION. RX PubMed=24879152; DOI=10.4161/auto.28479; RA Nicot A.S., Lo Verso F., Ratti F., Pilot-Storck F., Streichenberger N., RA Sandri M., Schaeffer L., Goillot E.; RT "Phosphorylation of NBR1 by GSK3 modulates protein aggregation."; RL Autophagy 10:1036-1053(2014). RN [17] RP INTERACTION WITH TAX1BP1. RX PubMed=33226137; DOI=10.15252/embj.2020104948; RA Ohnstad A.E., Delgado J.M., North B.J., Nasa I., Kettenbach A.N., RA Schultz S.W., Shoemaker C.J.; RT "Receptor-mediated clustering of FIP200 bypasses the role of LC3 lipidation RT in autophagy."; RL EMBO J. 39:e104948-e104948(2020). RN [18] RP INTERACTION WITH TAX1BP1, AND FUNCTION. RX PubMed=34471133; DOI=10.1038/s41467-021-25572-w; RA Turco E., Savova A., Gere F., Ferrari L., Romanov J., Schuschnig M., RA Martens S.; RT "Reconstitution defines the roles of p62, NBR1 and TAX1BP1 in ubiquitin RT condensate formation and autophagy initiation."; RL Nat. Commun. 12:5212-5212(2021). RN [19] RP FUNCTION, AND INTERACTION WITH INFLUENZA A VIRUS PB1 (MICROBIAL INFECTION). RX PubMed=33577621; DOI=10.1371/journal.ppat.1009300; RA Zeng Y., Xu S., Wei Y., Zhang X., Wang Q., Jia Y., Wang W., Han L., RA Chen Z., Wang Z., Zhang B., Chen H., Lei C.Q., Zhu Q.; RT "The PB1 protein of influenza A virus inhibits the innate immune response RT by targeting MAVS for NBR1-mediated selective autophagic degradation."; RL PLoS Pathog. 17:e1009300-e1009300(2021). RN [20] RP FUNCTION, INTERACTION WITH IRF3, INDUCTION BY VIRAL INFECTION, AND RP SUBCELLULAR LOCATION. RX PubMed=35914352; DOI=10.1016/j.bbrc.2022.07.043; RA Cai Y., Zhu Y., Zheng J., Zhang Y., Chen W.; RT "NBR1 mediates autophagic degradation of IRF3 to negatively regulate type I RT interferon production."; RL Biochem. Biophys. Res. Commun. 623:140-147(2022). RN [21] RP STRUCTURE BY NMR OF 1-85 AND 916-956. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of RSGI RUH-024, a PB1 domain, and of RSGI RUH-046, a RT UBA domain from human next to BRCA1 gene 1 protein (KIAA0049 protein) R923H RT variant."; RL Submitted (NOV-2005) to the PDB data bank. RN [22] RP X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 1-85. RX PubMed=16376336; DOI=10.1016/j.febslet.2005.12.021; RA Mueller S., Kursula I., Zou P., Wilmanns M.; RT "Crystal structure of the PB1 domain of NBR1."; RL FEBS Lett. 580:341-344(2006). RN [23] {ECO:0007744|PDB:2MGW, ECO:0007744|PDB:2MJ5} RP STRUCTURE BY NMR OF 913-959, FUNCTION, MUTAGENESIS OF GLU-926; GLY-928 AND RP PHE-929, AND INTERACTION WITH UBIQUITIN. RX PubMed=24692539; DOI=10.1074/jbc.m114.555441; RA Walinda E., Morimoto D., Sugase K., Konuma T., Tochio H., Shirakawa M.; RT "Solution structure of the ubiquitin-associated (UBA) domain of human RT autophagy receptor NBR1 and its interaction with ubiquitin and RT polyubiquitin."; RL J. Biol. Chem. 289:13890-13902(2014). CC -!- FUNCTION: Ubiquitin-binding autophagy adapter that participates in CC different processes including host defense or intracellular homeostasis CC (PubMed:33577621, PubMed:24692539). Possesses a double function during CC the selective autophagy by acting as a shuttle bringing ubiquitinated CC proteins to autophagosomes and also by participating in the formation CC of protein aggregates (PubMed:24879152, PubMed:34471133). Plays a role CC in the regulation of the innate immune response by modulating type I CC interferon production and targeting ubiquitinated IRF3 for autophagic CC degradation (PubMed:35914352). In response to oxidative stress, CC promotes an increase in SQSTM1 levels, phosphorylation, and body CC formation by preventing its autophagic degradation (By similarity). In CC turn, activates the KEAP1-NRF2/NFE2L2 antioxidant pathway (By CC similarity). Plays also non-autophagy role by mediating the shuttle of CC IL-12 to late endosome for subsequent secretion (By similarity). CC {ECO:0000250|UniProtKB:P97432, ECO:0000269|PubMed:19250911, CC ECO:0000269|PubMed:24692539, ECO:0000269|PubMed:24879152, CC ECO:0000269|PubMed:33577621, ECO:0000269|PubMed:34471133, CC ECO:0000269|PubMed:35914352}. CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with TRIM55 (By CC similarity). Interacts with titin/TTN (By similarity). Interacts with CC RNF29, USP8, MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAP, GABARAPL1 and CC GABARAPL2 (PubMed:19250911). Binds to ubiquitin and ubiquitinated CC proteins (PubMed:24692539). Interacts with SQSTM1 (PubMed:19250911). CC Interacts with TAX1BP1 (PubMed:33226137, PubMed:34471133). Interacts CC with IRF3; this interaction mediates autophagic degradation of IRF3 CC (PubMed:35914352). Interacts with IL12A and IL12B (By similarity). CC {ECO:0000250|UniProtKB:P97432, ECO:0000250|UniProtKB:Q501R9, CC ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:15802564, CC ECO:0000269|PubMed:19250911, ECO:0000269|PubMed:19427866, CC ECO:0000269|PubMed:33226137, ECO:0000269|PubMed:34471133, CC ECO:0000269|PubMed:35914352}. CC -!- SUBUNIT: (Microbial infection) Interacts with Influenza A virus protein CC PB1; this interaction promotes NBR1-mediated selective autophagic CC degradation of MAVS. {ECO:0000269|PubMed:33577621}. CC -!- INTERACTION: CC Q14596; O95166: GABARAP; NbExp=6; IntAct=EBI-742698, EBI-712001; CC Q14596; Q9H0R8: GABARAPL1; NbExp=4; IntAct=EBI-742698, EBI-746969; CC Q14596; P60520: GABARAPL2; NbExp=11; IntAct=EBI-742698, EBI-720116; CC Q14596; P49840: GSK3A; NbExp=5; IntAct=EBI-742698, EBI-1044067; CC Q14596; P49841: GSK3B; NbExp=4; IntAct=EBI-742698, EBI-373586; CC Q14596; P42858: HTT; NbExp=3; IntAct=EBI-742698, EBI-466029; CC Q14596; Q9H492: MAP1LC3A; NbExp=5; IntAct=EBI-742698, EBI-720768; CC Q14596; Q9GZQ8: MAP1LC3B; NbExp=9; IntAct=EBI-742698, EBI-373144; CC Q14596; Q9BXW4: MAP1LC3C; NbExp=3; IntAct=EBI-742698, EBI-2603996; CC Q14596; Q13501: SQSTM1; NbExp=7; IntAct=EBI-742698, EBI-307104; CC Q14596; Q9H2B2: SYT4; NbExp=3; IntAct=EBI-742698, EBI-751132; CC Q14596; P0CG48: UBC; NbExp=3; IntAct=EBI-742698, EBI-3390054; CC Q14596; P40818: USP8; NbExp=3; IntAct=EBI-742698, EBI-1050865; CC Q14596; P38182: ATG8; Xeno; NbExp=7; IntAct=EBI-742698, EBI-2684; CC Q14596-2; A0A0S2Z4M1: AXIN1; NbExp=3; IntAct=EBI-11081753, EBI-16429430; CC Q14596-2; P53582: METAP1; NbExp=3; IntAct=EBI-11081753, EBI-1051435; CC Q14596-2; Q9H2B2: SYT4; NbExp=3; IntAct=EBI-11081753, EBI-751132; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19427866, CC ECO:0000269|PubMed:35914352}. Cytoplasmic vesicle, autophagosome CC {ECO:0000269|PubMed:19250911, ECO:0000269|PubMed:24879152}. Lysosome CC {ECO:0000269|PubMed:19250911}. Cytoplasm, myofibril, sarcomere, M line CC {ECO:0000250|UniProtKB:Q501R9}. Note=In cardiac muscles localizes to CC the sarcomeric M line (By similarity). Is targeted to lysosomes for CC degradation (PubMed:19250911). {ECO:0000250|UniProtKB:Q501R9, CC ECO:0000269|PubMed:19250911}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q14596-1; Sequence=Displayed; CC Name=2; CC IsoId=Q14596-2; Sequence=VSP_004314; CC -!- INDUCTION: Upon viral infection. {ECO:0000269|PubMed:35914352}. CC -!- DOMAIN: The PB1 domain mediates interaction with SQSTM1. CC {ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:19250911}. CC -!- PTM: (Microbial infection) Cleaved by S.pyogenes SpeB protease; leading CC to its degradation (PubMed:24331465). Degradation by SpeB prevents CC autophagy, promoting to S.pyogenes intracellular replication CC (PubMed:24331465). {ECO:0000269|PubMed:24331465}. CC -!- PTM: Phosphorylated by GSK3A; this phosphorylation inhibits NBR1 CC involvement in the formation of ubiquitinated protein aggregates. CC {ECO:0000269|PubMed:24879152}. CC -!- CAUTION: Was originally thought to be the ovarian carcinoma antigen CC CA125. {ECO:0000305|PubMed:8069304}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA06417.2; 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; X76952; CAA54274.1; -; mRNA. DR EMBL; D30756; BAA06417.2; ALT_INIT; mRNA. DR EMBL; AY450308; AAS15047.1; -; mRNA. DR EMBL; AC060780; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC109326; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471152; EAW60946.1; -; Genomic_DNA. DR EMBL; BC009808; AAH09808.1; -; mRNA. DR EMBL; AF227189; AAF74119.1; -; mRNA. DR EMBL; U25764; AAA93228.1; -; Genomic_DNA. DR CCDS; CCDS45694.1; -. [Q14596-1] DR CCDS; CCDS77037.1; -. [Q14596-2] DR RefSeq; NP_001278500.1; NM_001291571.1. [Q14596-2] DR RefSeq; NP_001278501.1; NM_001291572.1. DR RefSeq; NP_005890.2; NM_005899.4. [Q14596-1] DR RefSeq; NP_114068.1; NM_031862.3. [Q14596-1] DR RefSeq; XP_011523115.1; XM_011524813.1. [Q14596-1] DR RefSeq; XP_016880131.1; XM_017024642.1. DR PDB; 1WJ6; NMR; -; A=1-85. DR PDB; 2BKF; X-ray; 1.56 A; A=1-85. DR PDB; 2CP8; NMR; -; A=916-956. DR PDB; 2G4S; X-ray; 2.15 A; A=1-85. DR PDB; 2L8J; NMR; -; B=726-738. DR PDB; 2MGW; NMR; -; A=913-959. DR PDB; 2MJ5; NMR; -; B=913-959. DR PDB; 4OLE; X-ray; 2.52 A; A/B/C/D=365-485. DR PDBsum; 1WJ6; -. DR PDBsum; 2BKF; -. DR PDBsum; 2CP8; -. DR PDBsum; 2G4S; -. DR PDBsum; 2L8J; -. DR PDBsum; 2MGW; -. DR PDBsum; 2MJ5; -. DR PDBsum; 4OLE; -. DR AlphaFoldDB; Q14596; -. DR BMRB; Q14596; -. DR SMR; Q14596; -. DR BioGRID; 110253; 383. DR CORUM; Q14596; -. DR IntAct; Q14596; 46. DR MINT; Q14596; -. DR STRING; 9606.ENSP00000343479; -. DR GlyConnect; 363; 2 O-Linked glycans. DR GlyCosmos; Q14596; No site information, 4 glycans. DR GlyGen; Q14596; 1 site, 4 O-linked glycans (1 site). DR iPTMnet; Q14596; -. DR PhosphoSitePlus; Q14596; -. DR BioMuta; NBR1; -. DR DMDM; 296439290; -. DR EPD; Q14596; -. DR jPOST; Q14596; -. DR MassIVE; Q14596; -. DR MaxQB; Q14596; -. DR PaxDb; 9606-ENSP00000411250; -. DR PeptideAtlas; Q14596; -. DR ProteomicsDB; 60070; -. [Q14596-1] DR ProteomicsDB; 60071; -. [Q14596-2] DR Pumba; Q14596; -. DR Antibodypedia; 8116; 337 antibodies from 32 providers. DR DNASU; 4077; -. DR Ensembl; ENST00000341165.10; ENSP00000343479.5; ENSG00000188554.15. [Q14596-1] DR Ensembl; ENST00000589872.1; ENSP00000467816.1; ENSG00000188554.15. [Q14596-2] DR Ensembl; ENST00000590996.6; ENSP00000466667.1; ENSG00000188554.15. [Q14596-1] DR GeneID; 4077; -. DR KEGG; hsa:4077; -. DR MANE-Select; ENST00000590996.6; ENSP00000466667.1; NM_005899.5; NP_005890.2. DR UCSC; uc010czd.4; human. [Q14596-1] DR AGR; HGNC:6746; -. DR CTD; 4077; -. DR DisGeNET; 4077; -. DR GeneCards; NBR1; -. DR HGNC; HGNC:6746; NBR1. DR HPA; ENSG00000188554; Low tissue specificity. DR MIM; 166945; gene. DR neXtProt; NX_Q14596; -. DR OpenTargets; ENSG00000188554; -. DR PharmGKB; PA30510; -. DR VEuPathDB; HostDB:ENSG00000188554; -. DR eggNOG; KOG4351; Eukaryota. DR eggNOG; KOG4582; Eukaryota. DR GeneTree; ENSGT00390000016335; -. DR HOGENOM; CLU_014175_0_0_1; -. DR InParanoid; Q14596; -. DR OMA; SWELMEA; -. DR OrthoDB; 5399396at2759; -. DR PhylomeDB; Q14596; -. DR TreeFam; TF328428; -. DR PathwayCommons; Q14596; -. DR Reactome; R-HSA-9664873; Pexophagy. DR SignaLink; Q14596; -. DR SIGNOR; Q14596; -. DR BioGRID-ORCS; 4077; 25 hits in 1159 CRISPR screens. DR ChiTaRS; NBR1; human. DR EvolutionaryTrace; Q14596; -. DR GeneWiki; NBR1; -. DR GenomeRNAi; 4077; -. DR Pharos; Q14596; Tbio. DR PRO; PR:Q14596; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q14596; Protein. DR Bgee; ENSG00000188554; Expressed in tendon of biceps brachii and 215 other cell types or tissues. DR ExpressionAtlas; Q14596; baseline and differential. DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA. DR GO; GO:0005770; C:late endosome; ISS:UniProtKB. DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell. DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0005758; C:mitochondrial intermembrane space; IEA:Ensembl. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome. DR GO; GO:0000407; C:phagophore assembly site; IBA:GO_Central. DR GO; GO:0043235; C:receptor complex; IDA:UniProtKB. DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISS:BHF-UCL. DR GO; GO:0043130; F:ubiquitin binding; IDA:UniProtKB. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0016236; P:macroautophagy; IDA:UniProtKB. DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; ISS:BHF-UCL. DR GO; GO:0030500; P:regulation of bone mineralization; ISS:BHF-UCL. DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISS:BHF-UCL. DR CDD; cd14947; NBR1_like; 1. DR CDD; cd06396; PB1_NBR1; 1. DR CDD; cd14319; UBA_NBR1; 1. DR CDD; cd02340; ZZ_NBR1_like; 1. DR Gene3D; 3.30.60.90; -; 1. DR Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR032350; N_BRCA1_central. DR InterPro; IPR000270; PB1_dom. DR InterPro; IPR034852; PB1_NBR1. DR InterPro; IPR015940; UBA. DR InterPro; IPR009060; UBA-like_sf. DR InterPro; IPR000433; Znf_ZZ. DR InterPro; IPR043145; Znf_ZZ_sf. DR PANTHER; PTHR20930:SF2; NEXT TO BRCA1 GENE 1 PROTEIN; 1. DR PANTHER; PTHR20930; OVARIAN CARCINOMA ANTIGEN CA125-RELATED; 1. DR Pfam; PF16158; N_BRCA1_IG; 1. DR Pfam; PF00564; PB1; 1. DR Pfam; PF00569; ZZ; 1. DR SMART; SM00666; PB1; 1. DR SMART; SM00291; ZnF_ZZ; 1. DR SUPFAM; SSF54277; CAD & PB1 domains; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR SUPFAM; SSF46934; UBA-like; 1. DR PROSITE; PS51745; PB1; 1. DR PROSITE; PS50030; UBA; 1. DR PROSITE; PS01357; ZF_ZZ_1; 1. DR PROSITE; PS50135; ZF_ZZ_2; 1. DR Genevisible; Q14596; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle; KW Host-virus interaction; Lysosome; Metal-binding; Phosphoprotein; KW Reference proteome; Ubl conjugation; Zinc; Zinc-finger. FT CHAIN 1..966 FT /note="Next to BRCA1 gene 1 protein" FT /id="PRO_0000096746" FT DOMAIN 4..85 FT /note="PB1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081" FT DOMAIN 913..957 FT /note="UBA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212" FT ZN_FING 212..264 FT /note="ZZ-type" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT REGION 542..636 FT /note="ATG8 family protein-binding" FT REGION 699..728 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 727..738 FT /note="ATG8 family protein-binding" FT REGION 750..792 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 848..879 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 699..719 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 217 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 220 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 231 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 234 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 240 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 243 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 250 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT BINDING 254 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228" FT MOD_RES 116 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 586 FT /note="Phosphothreonine; by GSK3-alpha" FT /evidence="ECO:0000269|PubMed:24879152" FT MOD_RES 590 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q501R9" FT MOD_RES 596 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q501R9" FT MOD_RES 625 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 910..966 FT /note="PIISEDQTAALMAHLFEMGFCDRQLNLRLLKKHNYNILQVVTELLQLNNNDW FT YSQRY -> GLWGLLSFLHLAKKCFFLKAPSEAFSWF (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_004314" FT VARIANT 923 FT /note="H -> R (in dbSNP:rs8482)" FT /evidence="ECO:0000269|PubMed:11179671, FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:8069304" FT /id="VAR_016106" FT MUTAGEN 12 FT /note="K->A: No effect on interaction with SQSTM1." FT /evidence="ECO:0000269|PubMed:12813044" FT MUTAGEN 50 FT /note="D->R: Loss of interaction with SQSTM1." FT /evidence="ECO:0000269|PubMed:12813044, FT ECO:0000269|PubMed:19250911" FT MUTAGEN 586 FT /note="T->A: Loss of phosphorylation by GSK3A." FT /evidence="ECO:0000269|PubMed:24879152" FT MUTAGEN 732 FT /note="Y->A: Loss of interaction ATG8 family proteins." FT /evidence="ECO:0000269|PubMed:19250911" FT MUTAGEN 926 FT /note="E->A: About 3-fold weaker interaction with ubiquitin FT than WT." FT /evidence="ECO:0000269|PubMed:24692539" FT MUTAGEN 928 FT /note="G->A: About 2-fold weaker interaction with ubiquitin FT than WT." FT /evidence="ECO:0000269|PubMed:24692539" FT MUTAGEN 929 FT /note="F->A: Complete loss of interaction with ubiquitin." FT /evidence="ECO:0000269|PubMed:24692539" FT CONFLICT 746..770 FT /note="LGDSMYSSALSQPGLERGAEGKPGV -> WGILCTALRSHSQAWSEVLKASL FT GF (in Ref. 1; CAA54274)" FT /evidence="ECO:0000305" FT STRAND 5..11 FT /evidence="ECO:0007829|PDB:2BKF" FT STRAND 14..21 FT /evidence="ECO:0007829|PDB:2BKF" FT HELIX 23..25 FT /evidence="ECO:0007829|PDB:2BKF" FT HELIX 28..39 FT /evidence="ECO:0007829|PDB:2BKF" FT STRAND 42..49 FT /evidence="ECO:0007829|PDB:2BKF" FT STRAND 55..58 FT /evidence="ECO:0007829|PDB:2BKF" FT HELIX 61..73 FT /evidence="ECO:0007829|PDB:2BKF" FT TURN 74..76 FT /evidence="ECO:0007829|PDB:2BKF" FT STRAND 77..84 FT /evidence="ECO:0007829|PDB:2BKF" FT STRAND 373..380 FT /evidence="ECO:0007829|PDB:4OLE" FT STRAND 384..386 FT /evidence="ECO:0007829|PDB:4OLE" FT STRAND 391..400 FT /evidence="ECO:0007829|PDB:4OLE" FT STRAND 402..404 FT /evidence="ECO:0007829|PDB:4OLE" FT STRAND 410..418 FT /evidence="ECO:0007829|PDB:4OLE" FT STRAND 420..423 FT /evidence="ECO:0007829|PDB:4OLE" FT HELIX 425..428 FT /evidence="ECO:0007829|PDB:4OLE" FT STRAND 439..447 FT /evidence="ECO:0007829|PDB:4OLE" FT STRAND 453..463 FT /evidence="ECO:0007829|PDB:4OLE" FT STRAND 466..478 FT /evidence="ECO:0007829|PDB:4OLE" FT HELIX 917..927 FT /evidence="ECO:0007829|PDB:2CP8" FT HELIX 932..939 FT /evidence="ECO:0007829|PDB:2CP8" FT TURN 940..944 FT /evidence="ECO:0007829|PDB:2CP8" FT HELIX 946..956 FT /evidence="ECO:0007829|PDB:2CP8" SQ SEQUENCE 966 AA; 107413 MW; 6A057E67947838EF CRC64; MEPQVTLNVT FKNEIQSFLV SDPENTTWAD IEAMVKVSFD LNTIQIKYLD EENEEVSINS QGEYEEALKM AVKQGNQLQM QVHEGHHVVD EAPPPVVGAK RLAARAGKKP LAHYSSLVRV LGSDMKTPED PAVQSFPLVP CDTDQPQDKP PDWFTSYLET FREQVVNETV EKLEQKLHEK LVLQNPSLGS CPSEVSMPTS EETLFLPENQ FSWHIACNNC QRRIVGVRYQ CSLCPSYNIC EDCEAGPYGH DTNHVLLKLR RPVVGSSEPF CHSKYSTPRL PAALEQVRLQ KQVDKNFLKA EKQRLRAEKK QRKAEVKELK KQLKLHRKIH LWNSIHGLQS PKSPLGRPES LLQSNTLMLP LQPCTSVMPM LSAAFVDENL PDGTHLQPGT KFIKHWRMKN TGNVKWSADT KLKFMWGNLT LASTEKKDVL VPCLKAGHVG VVSVEFIAPA LEGTYTSHWR LSHKGQQFGP RVWCSIIVDP FPSEESPDNI EKGMISSSKT DDLTCQQEET FLLAKEERQL GEVTEQTEGT AACIPQKAKN VASERELYIP SVDLLTAQDL LSFELLDINI VQELERVPHN TPVDVTPCMS PLPHDSPLIE KPGLGQIEEE NEGAGFKALP DSMVSVKRKA ENIASVEEAE EDLSGTQFVC ETVIRSLTLD AAPDHNPPCR QKSLQMTFAL PEGPLGNEKE EIIHIAEEEA VMEEEEDEED EEEEDELKDE VQSQSSASSE DYIIILPECF DTSRPLGDSM YSSALSQPGL ERGAEGKPGV EAGQEPAEAG ERLPGGENQP QEHSISDILT TSQTLETVPL IPEVVELPPS LPRSSPCVHH HGSPGVDLPV TIPEVSSVPD QIRGEPRGSS GLVNSRQKSY DHSRHHHGSS IAGGLVKGAL SVAASAYKAL FAGPPVTAQP IISEDQTAAL MAHLFEMGFC DRQLNLRLLK KHNYNILQVV TELLQLNNND WYSQRY //