NBR1_HUMAN
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 03-AUG-2022, entry version 210.
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 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 [12]
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 [13]
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 [14]
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 [15]
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 [16]
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).
CC -!- FUNCTION: Acts probably as a receptor for selective autophagosomal
CC degradation of ubiquitinated targets. {ECO:0000269|PubMed:19250911}.
CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with TRIM55 (By
CC similarity). Interacts with SQSTM1, titin/TTN, RNF29, USP8, SQSTM1,
CC MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAP, GABARAPL1 and GABARAPL2. Binds
CC to ubiquitin and ubiquitinated proteins. {ECO:0000250,
CC ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:15802564,
CC ECO:0000269|PubMed:19250911, ECO:0000269|PubMed:19427866}.
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 Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:19250911}.
CC Lysosome {ECO:0000269|PubMed:19250911}. Cytoplasm, myofibril,
CC sarcomere, M line {ECO:0000250|UniProtKB:Q501R9}. Note=In cardiac
CC muscles localizes to the sarcomeric M line (By similarity). Is targeted
CC to lysosomes for degradation (PubMed:19250911).
CC {ECO:0000250|UniProtKB:Q501R9, 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 -!- DOMAIN: The PB1 domain mediates interaction with SQSTM1.
CC {ECO:0000269|PubMed:12813044, ECO:0000269|PubMed:19250911}.
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};
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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. [Q14596-1]
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; 367.
DR CORUM; Q14596; -.
DR IntAct; Q14596; 45.
DR MINT; Q14596; -.
DR STRING; 9606.ENSP00000411250; -.
DR GlyConnect; 363; 2 O-Linked 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; Q14596; -.
DR PeptideAtlas; Q14596; -.
DR PRIDE; Q14596; -.
DR ProteomicsDB; 60070; -. [Q14596-1]
DR ProteomicsDB; 60071; -. [Q14596-2]
DR Antibodypedia; 8116; 305 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 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; AMMADGI; -.
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; 23 hits in 1079 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 213 other tissues.
DR ExpressionAtlas; Q14596; baseline and differential.
DR Genevisible; Q14596; HS.
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 Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 3.30.60.90; -; 1.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR032350; N_BRCA1_central.
DR InterPro; IPR033513; NBR1.
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; PTHR20930:SF2; 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; SSF46934; SSF46934; 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.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Cytoplasmic vesicle;
KW Lysosome; Metal-binding; Phosphoprotein; Reference proteome; Zinc;
KW 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 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 732
FT /note="Y->A: Loss of interaction ATG8 family proteins."
FT /evidence="ECO:0000269|PubMed:19250911"
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
