NBR1_MOUSE
ID NBR1_MOUSE Reviewed; 988 AA.
AC P97432; Q9JIH9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Next to BRCA1 gene 1 protein;
DE AltName: Full=Membrane component chromosome 17 surface marker 2 homolog;
DE AltName: Full=Neighbor of BRCA1 gene 1 protein;
GN Name=Nbr1; Synonyms=M17s2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=ICR; TISSUE=Brain;
RX PubMed=8975707; DOI=10.1006/geno.1996.0633;
RA Chambers J.A., Solomon E.;
RT "Isolation of the murine Nbr1 gene adjacent to the murine Brca1 gene.";
RL Genomics 38:305-313(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv; 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Acts probably as a receptor for selective autophagosomal
CC degradation of ubiquitinated targets. {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with SQSTM1,
CC titin/TTN, TRIM55, RNF29, USP8, SQSTM1, MAP1LC3A, MAP1LC3B, MAP1LC3C,
CC GABARAP, GABARAPL1 and GABARAPL2. Binds to ubiquitin and ubiquitinated
CC proteins. {ECO:0000250}.
CC -!- INTERACTION:
CC P97432; Q9GZQ8: MAP1LC3B; Xeno; NbExp=2; IntAct=EBI-642554, EBI-373144;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q14596}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q14596}.
CC Lysosome {ECO:0000250|UniProtKB:Q14596}. 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 (By similarity).
CC {ECO:0000250|UniProtKB:Q14596, ECO:0000250|UniProtKB:Q501R9}.
CC -!- TISSUE SPECIFICITY: Expressed in brain.
CC -!- DOMAIN: The PB1 domain mediates interaction with SQSTM1. {ECO:0000250}.
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DR EMBL; U73039; AAC53025.1; -; mRNA.
DR EMBL; AF227188; AAF74118.1; -; mRNA.
DR CCDS; CCDS25475.1; -.
DR RefSeq; NP_001239149.1; NM_001252220.1.
DR RefSeq; NP_032702.1; NM_008676.3.
DR AlphaFoldDB; P97432; -.
DR SMR; P97432; -.
DR BioGRID; 201698; 14.
DR IntAct; P97432; 8.
DR MINT; P97432; -.
DR STRING; 10090.ENSMUSP00000099388; -.
DR iPTMnet; P97432; -.
DR PhosphoSitePlus; P97432; -.
DR EPD; P97432; -.
DR MaxQB; P97432; -.
DR PaxDb; P97432; -.
DR PRIDE; P97432; -.
DR ProteomicsDB; 252646; -.
DR Antibodypedia; 8116; 305 antibodies from 32 providers.
DR DNASU; 17966; -.
DR Ensembl; ENSMUST00000103098; ENSMUSP00000099387; ENSMUSG00000017119.
DR Ensembl; ENSMUST00000103099; ENSMUSP00000099388; ENSMUSG00000017119.
DR Ensembl; ENSMUST00000107218; ENSMUSP00000102836; ENSMUSG00000017119.
DR GeneID; 17966; -.
DR KEGG; mmu:17966; -.
DR UCSC; uc007lpg.2; mouse.
DR CTD; 4077; -.
DR MGI; MGI:108498; Nbr1.
DR VEuPathDB; HostDB:ENSMUSG00000017119; -.
DR eggNOG; KOG4351; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR GeneTree; ENSGT00390000016335; -.
DR InParanoid; P97432; -.
DR OMA; NSQLEYE; -.
DR OrthoDB; 1371591at2759; -.
DR PhylomeDB; P97432; -.
DR TreeFam; TF328428; -.
DR Reactome; R-MMU-9664873; Pexophagy.
DR BioGRID-ORCS; 17966; 12 hits in 71 CRISPR screens.
DR ChiTaRS; Nbr1; mouse.
DR PRO; PR:P97432; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; P97432; protein.
DR Bgee; ENSMUSG00000017119; Expressed in ciliary body and 263 other tissues.
DR ExpressionAtlas; P97432; baseline and differential.
DR Genevisible; P97432; MM.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005770; C:late endosome; IDA:UniProtKB.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031430; C:M band; IEA:UniProtKB-SubCell.
DR GO; GO:0005758; C:mitochondrial intermembrane space; IDA:MGI.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005778; C:peroxisomal membrane; TAS:Reactome.
DR GO; GO:0000407; C:phagophore assembly site; IDA:MGI.
DR GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; IDA:BHF-UCL.
DR GO; GO:0043130; F:ubiquitin binding; ISS:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR GO; GO:0045668; P:negative regulation of osteoblast differentiation; IMP:BHF-UCL.
DR GO; GO:0030500; P:regulation of bone mineralization; IMP:BHF-UCL.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IMP: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 Cytoplasm; Cytoplasmic vesicle; Lysosome; Metal-binding; Phosphoprotein;
KW Reference proteome; Zinc; Zinc-finger.
FT CHAIN 1..988
FT /note="Next to BRCA1 gene 1 protein"
FT /id="PRO_0000096747"
FT DOMAIN 4..86
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 935..979
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 213..265
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 126..150
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..637
FT /note="ATG8 family proteins-binding"
FT /evidence="ECO:0000250"
FT REGION 611..644
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 745..756
FT /note="ATG8 family proteins-binding"
FT /evidence="ECO:0000250"
FT REGION 768..822
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 841..900
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..145
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..806
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 807..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 221
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 241
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 244
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 251
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 255
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14596"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501R9"
FT MOD_RES 597
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501R9"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14596"
FT MOD_RES 860
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q501R9"
FT CONFLICT 807
FT /note="Q -> R (in Ref. 2; AAF74118)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 988 AA; 109958 MW; E5BB4B281FE33CE0 CRC64;
MEPQVTLNVT FKNETQSFLV SDPENTTWAD VEAMVKVSFD LNTIQIKYLD EENEEISINS
QGEYEEALKM ANIKQGNQLQ MQVHEGYHVV DEALPKNVVE NQAAARTGKK PLAHYSSLVR
VLGSDMKTTE EPAPEQCSSA PCDTDQPQDK PPDWFTSYLE MFREQVVKET VEKLEQRLQE
KLVLQKPLLS SSPTEVSMPI SEETLFLPEN QFSWHIACSH CQKRIVGVRY QCSLCPSYNI
CEDCEAGPYT HDTNHVLLKL RRPVVISSEP FFYSKYSAPR LPAALEQVRL QKQVDKNFVK
AEKQRLRAEK KQRKAEVKEL KKQLKLHRKI HLWNSIHGLQ SPKSPLGRPE SLLQSNTLML
PLQPCAPVMP TLSAAFVDEN LPDGTHLQPG TKFIKHWRMK NTGNVKWNTD TKLKFMWGNL
TLASTEKKDV LVPCLKAGHV GVVSVEFIAP TLEGTYTSHW RLSHKGQQFG PRVWCSIIVD
PFPSSESPDN VEGDRISSSK ADDFSCEQEE AFLLAEEEIP LGEVTKQTEG TGASASQKTR
RAASERELYI PSVDLLTAQD LLSFELLDIN IVQELERVPH NTPVDMTPCM SPLPHDSPLI
EKPGLGQIQE ESEGAGFKAP PDSTVSAKRK AETPASVEET EEDLSGTQFV CETVIRSLTL
DAAPDHNPPC RQRSPQRELQ LYSTEGQQPL VLPGFCRKDS SLKFALPEEG PRGDEREEIV
HIVEEEVVEE EEEVQDEEVQ SQSSASSEDY IIILPECFDT SRPLGDSMYS SALSQPGLER
GAEGEPGIES GLEPTEARER LPERESQPQE QSISDILTTS QPLDTVPLVP EVAGLPAALS
RSAPCGQCES SGVDSPGVDS PATMHEVPPA PDDIRGEPRG STGLANSRQR SCDHSRHHNG
SSIAGGLVKG ALSVAASAYK ALFSGPPVTA QPIVSEDQTT ALMAHLFEMG FCDRQLNLRL
LRKHNYNILQ VVTELLQVNN NDWYSHRY
