NBR1_RAT
ID NBR1_RAT Reviewed; 983 AA.
AC Q501R9; Q9JHG4;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Next to BRCA1 gene 1 protein;
DE AltName: Full=Neighbor of BRCA1 gene 1 protein;
GN Name=Nbr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-43.
RC STRAIN=SHR; 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 INTERACTION WITH SQSTM1; TTN AND TRIM55, AND SUBCELLULAR LOCATION.
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-592; SER-598 AND SER-855, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Acts probably as a receptor for selective autophagosomal
CC degradation of ubiquitinated targets. {ECO:0000250}.
CC -!- SUBUNIT: Homooligomer and heterooligomer. Interacts with RNF29, USP8,
CC SQSTM1, MAP1LC3A, MAP1LC3B, MAP1LC3C, GABARAP, GABARAPL1 and GABARAPL2
CC (By similarity). Binds to ubiquitin and ubiquitinated proteins (By
CC similarity). Interacts with SQSTM1, titin/TTN and TRIM55. {ECO:0000250,
CC ECO:0000269|PubMed:15802564}.
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:0000269|PubMed:15802564}. Note=In cardiac
CC muscles localizes to the sarcomeric M line (PubMed:15802564). Is
CC targeted to lysosomes for degradation (By similarity).
CC {ECO:0000250|UniProtKB:Q14596, ECO:0000269|PubMed:15802564}.
CC -!- DOMAIN: The PB1 domain mediates interaction with SQSTM1. {ECO:0000250}.
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DR EMBL; BC095903; AAH95903.1; -; mRNA.
DR EMBL; AF227190; AAF74120.1; -; mRNA.
DR EMBL; AF227191; AAF74121.1; -; mRNA.
DR RefSeq; NP_001019936.1; NM_001024765.1.
DR AlphaFoldDB; Q501R9; -.
DR SMR; Q501R9; -.
DR BioGRID; 257580; 5.
DR CORUM; Q501R9; -.
DR STRING; 10116.ENSRNOP00000028149; -.
DR CarbonylDB; Q501R9; -.
DR iPTMnet; Q501R9; -.
DR PhosphoSitePlus; Q501R9; -.
DR PaxDb; Q501R9; -.
DR PRIDE; Q501R9; -.
DR GeneID; 303554; -.
DR KEGG; rno:303554; -.
DR UCSC; RGD:69195; rat.
DR CTD; 4077; -.
DR RGD; 69195; Nbr1.
DR eggNOG; KOG4351; Eukaryota.
DR eggNOG; KOG4582; Eukaryota.
DR InParanoid; Q501R9; -.
DR PhylomeDB; Q501R9; -.
DR Reactome; R-RNO-9664873; Pexophagy.
DR PRO; PR:Q501R9; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
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:0005758; C:mitochondrial intermembrane space; ISO:RGD.
DR GO; GO:0000407; C:phagophore assembly site; ISO:RGD.
DR GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR GO; GO:0051019; F:mitogen-activated protein kinase binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0030500; P:regulation of bone mineralization; ISO:RGD.
DR GO; GO:0032872; P:regulation of stress-activated MAPK cascade; ISO:RGD.
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..983
FT /note="Next to BRCA1 gene 1 protein"
FT /id="PRO_0000096749"
FT DOMAIN 4..86
FT /note="PB1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01081"
FT DOMAIN 930..974
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT ZN_FING 214..266
FT /note="ZZ-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT REGION 126..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 544..638
FT /note="ATG8 family proteins-binding"
FT /evidence="ECO:0000250"
FT REGION 611..645
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..813
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 867..895
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..810
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 222
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 233
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 236
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 242
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 245
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 252
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00228"
FT BINDING 256
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 592
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 598
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 855
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 983 AA; 109829 MW; 4A80880D9EDDE729 CRC64;
MEPQVTLNVT FKNETQSFLV SDPENTTWAD VEAMVKVSFD LNTIQIKYLD EENEEISINS
QGEYEEALKM ANIKQGNQLQ MQVHEGCHVV DEVLPQTVVE KQATARTGKK PLAHYSSLVR
VLGSDMKTTE EPTAEARSPV PCDTDKPQDK PPDWFTSYLE MFREQVVKET VEKLEQRLQE
KLVLQKPPFS SSPSEVSMPI SEEETLFLPE NQFSWHIACS HCQKRIVGVR YQCSLCPSYN
ICEDCEAGPY SHDTNHILLK FRRPVVISSE PFFYSKYPTP RLPAALEQVR LQKQVDKNFV
KAEKQRLRAE KKQRKAEVKE LKKQLKLHRK IHLWNSIHGL QSPKSPLGRP ESLLQSNTLM
LPLQPCAPVM PTLSAAFVDE NLPDGTHLQP GTKFIKHWRM KNTGNVKWSA DTKLKFMWGN
LTLASTEKKD VLVPCLKAGH IGVVSVEFIA PTLEGTYTLH WRLSHKGQQF GPRVWCSIIV
DPFPSSESPV NLERDGISSS KADDFTCEQE EAFLLAEEEI PLGEVTKQTE GTGSSAPQKT
QHAASERELY IPSVDLLTAQ DLLSFELLDI NIVQELERVP HNTPVDVTPR MSPLPHDSPL
IEKPGLGRIQ EESEGAGLKA SPDSTVLTKR KAETPASVEE TEEDLSGTQF VCETVIRSLT
LDAAPDHNPP CRQRSPQREL QLYSTEEQQP LMLPGFCRKD SSLKFALPEE GPHGDEREEI
VHIAEEEAIE EEDVQDEEVQ SQSSASSEDY IIILPECFDT SRPLGDSMYS SALSQPGLER
GAEGEPGIES GQEPAEARER LPERESQPKE QSISDILTTS QHLDTVPLVP EVAGLPAALS
RSAPCGQYEA PRVDSPVTIQ EVLPVPDHVR GEPRGSTGLA NSRQKSCDHS RHHNGSSIAG
GLVKGALSVA ASAYKALFSG PPVTAQPVIS EDQTAALMAH LFEMGFCDRQ LNLRLLRKHN
HNILQVVTEL LQVNNNDWYS HRY
