NUB1_MOUSE
ID NUB1_MOUSE Reviewed; 614 AA.
AC P54729; Q8K3U0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 26-SEP-2003, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=NEDD8 ultimate buster 1;
DE AltName: Full=Negative regulator of ubiquitin-like proteins 1;
DE AltName: Full=Protein BS4;
GN Name=Nub1; Synonyms=Nyren18;
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 TISSUE=Fibroblast;
RA Shan B., Parsa A.T., Lewis J.A.;
RT "BS4: an interferon inducible gene with novel regulatory properties.";
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Testis;
RX PubMed=12816948; DOI=10.1074/jbc.m212057200;
RA Tanaka T., Kawashima H., Yeh E.T.H., Kamitani T.;
RT "Regulation of the NEDD8 conjugation system by a splicing variant, NUB1L.";
RL J. Biol. Chem. 278:32905-32913(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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).
RN [5]
RP STRUCTURE BY NMR OF 469-538.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-012, a UBA domain from mouse cDNA.";
RL Submitted (SEP-2004) to the PDB data bank.
CC -!- FUNCTION: Specific down-regulator of the NEDD8 conjugation system.
CC Recruits NEDD8, UBD, and their conjugates to the proteasome for
CC degradation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Directly interacts with NEDD8 and PSMD4/S5a, a member of the
CC regulatory subunit of the 26S proteasome. Interacts with AIPL1. The
CC interaction with UBD via UBA domains facilitates the linking of UBD-
CC conjugated target protein to the proteasome complex and accelerates UBD
CC degradation and that of its conjugates (By similarity).
CC {ECO:0000250|UniProtKB:Q9Y5A7}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Predominantly
CC nuclear. {ECO:0000250}.
CC -!- DEVELOPMENTAL STAGE: Strongest expression at 7 dpc. Marked decrease 11,
CC 15 and 17 dpc.
CC -!- INDUCTION: By interferon.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA68612.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U27462; AAA68612.1; ALT_FRAME; mRNA.
DR EMBL; AF534114; AAM97686.1; -; mRNA.
DR EMBL; BC037451; AAH37451.1; -; mRNA.
DR CCDS; CCDS39030.1; -.
DR RefSeq; NP_058016.2; NM_016736.3.
DR PDB; 1VEG; NMR; -; A=469-538.
DR PDBsum; 1VEG; -.
DR AlphaFoldDB; P54729; -.
DR SMR; P54729; -.
DR BioGRID; 207276; 3.
DR STRING; 10090.ENSMUSP00000070265; -.
DR iPTMnet; P54729; -.
DR PhosphoSitePlus; P54729; -.
DR EPD; P54729; -.
DR PaxDb; P54729; -.
DR PeptideAtlas; P54729; -.
DR PRIDE; P54729; -.
DR ProteomicsDB; 293803; -.
DR Antibodypedia; 33007; 373 antibodies from 31 providers.
DR DNASU; 53312; -.
DR Ensembl; ENSMUST00000068825; ENSMUSP00000070265; ENSMUSG00000028954.
DR GeneID; 53312; -.
DR KEGG; mmu:53312; -.
DR UCSC; uc008wsf.2; mouse.
DR CTD; 51667; -.
DR MGI; MGI:1889001; Nub1.
DR VEuPathDB; HostDB:ENSMUSG00000028954; -.
DR eggNOG; KOG2561; Eukaryota.
DR GeneTree; ENSGT00390000010557; -.
DR HOGENOM; CLU_030806_0_0_1; -.
DR InParanoid; P54729; -.
DR PhylomeDB; P54729; -.
DR TreeFam; TF323449; -.
DR Reactome; R-MMU-8951664; Neddylation.
DR BioGRID-ORCS; 53312; 3 hits in 58 CRISPR screens.
DR ChiTaRS; Nub1; mouse.
DR EvolutionaryTrace; P54729; -.
DR PRO; PR:P54729; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P54729; protein.
DR Bgee; ENSMUSG00000028954; Expressed in morula and 260 other tissues.
DR ExpressionAtlas; P54729; baseline and differential.
DR Genevisible; P54729; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0097413; C:Lewy body; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:MGI.
DR GO; GO:0016567; P:protein ubiquitination; ISS:UniProtKB.
DR GO; GO:2000058; P:regulation of ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR InterPro; IPR039749; NUB1.
DR InterPro; IPR041207; NUB1_ubiquitin-like_dom.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR12948; PTHR12948; 1.
DR Pfam; PF00627; UBA; 3.
DR Pfam; PF18037; Ubiquitin_5; 1.
DR SMART; SM00165; UBA; 3.
DR SUPFAM; SSF46934; SSF46934; 3.
DR SUPFAM; SSF48452; SSF48452; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Nucleus; Reference proteome; Repeat.
FT CHAIN 1..614
FT /note="NEDD8 ultimate buster 1"
FT /id="PRO_0000210993"
FT DOMAIN 373..413
FT /note="UBA 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 423..469
FT /note="UBA 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 488..528
FT /note="UBA 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 426..473
FT /note="NEDD8-binding 1"
FT /evidence="ECO:0000250"
FT REGION 531..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 549..597
FT /note="NEDD8-binding 2"
FT /evidence="ECO:0000250"
FT COILED 36..71
FT /evidence="ECO:0000255"
FT COILED 151..206
FT /evidence="ECO:0000255"
FT MOTIF 413..430
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000305"
FT COMPBIAS 537..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..590
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT STRAND 484..486
FT /evidence="ECO:0007829|PDB:1VEG"
FT HELIX 491..500
FT /evidence="ECO:0007829|PDB:1VEG"
FT HELIX 504..513
FT /evidence="ECO:0007829|PDB:1VEG"
FT TURN 514..516
FT /evidence="ECO:0007829|PDB:1VEG"
FT HELIX 518..528
FT /evidence="ECO:0007829|PDB:1VEG"
FT STRAND 536..538
FT /evidence="ECO:0007829|PDB:1VEG"
SQ SEQUENCE 614 AA; 70307 MW; 8287222F141D1B80 CRC64;
MAQKKYLQAK LTQFLREDRI QLWKPPYTKE NKEVGLAVKD LAKKYSERLE CCENEVENII
EEIRRKAIER GTGNEHYRTT GIATIEVFLP PRLRKHDKKS LLETRLHVTG RDLRCQIAET
FGFQENYIKI VINKKQLQLG KSLEEQGVTH NVKAMVLELK QSEEDVRKNL QLEEEEQNEA
ELKERRIQRT KRGLEILAER AEMVVDPETM PYLDIANQTG RSLRIPPAER KALMLAMGYH
EKGRAFLKRK EYGIALPCLL DADRYFCECK ELLDTVDNYA VLQLDIVWCY FRLEQLECLD
DAEKKLNLAQ KCFKNCYGEN HQRLVHIKGN CGKEKVLFLR LYLLQGIQNY HSGNGEEARE
YLNKARQLFK ELYIDPSKVH NLLQLGFTAQ EARLGLRACD GNVDHAATHI SNRREELAQI
RKEEKEKRRR RLENVNTLRG MGYSTQAAKQ ALHQARGNLD DALKVLLSNP HMWWLQDADP
ENNSRQASPS QESINQLVYM GFDTVVAEAA LRVFGGNVQL AAQTLAHHGG SLPPDLQFSG
EDSSPTPSTS PSDSAGTSSA STDEDMETEA VNEILEDIPE HEEDYLDSTL EDEEVIIAEY
LSYVESISSA AKNN
