UBXN1_MOUSE
ID UBXN1_MOUSE Reviewed; 297 AA.
AC Q922Y1; Q3UCP8;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=UBX domain-containing protein 1;
DE AltName: Full=Protein 2B28;
DE AltName: Full=SAPK substrate protein 1;
DE AltName: Full=UBA/UBX 33.3 kDa protein;
DE Short=mY33K;
GN Name=Ubxn1; Synonyms=D19Ertd721e, Saks1;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [3]
RP INTERACTION WITH NGLY1.
RX PubMed=11562482; DOI=10.1073/pnas.201393498;
RA Park H., Suzuki T., Lennarz W.J.;
RT "Identification of proteins that interact with mammalian peptide:N-
RT glycanase and implicate this hydrolase in the proteasome-dependent pathway
RT for protein degradation.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11163-11168(2001).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH HOMER2.
RX PubMed=15944415; DOI=10.1093/jb/mvi074;
RA Ishibashi T., Ogawa S., Hashiguchi Y., Inoue Y., Udo H., Ohzono H.,
RA Kato A., Minakami R., Sugiyama H.;
RT "A novel protein specifically interacting with Homer2 regulates ubiquitin-
RT proteasome systems.";
RL J. Biochem. 137:617-623(2005).
RN [6]
RP FUNCTION, AND INTERACTION WITH AMFR; NGLY1; RAD23B AND VCP.
RX PubMed=16709668; DOI=10.1073/pnas.0602747103;
RA Li G., Zhao G., Zhou X., Schindelin H., Lennarz W.J.;
RT "The AAA ATPase p97 links peptide N-glycanase to the endoplasmic reticulum-
RT associated E3 ligase autocrine motility factor receptor.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8348-8353(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199, AND IDENTIFICATION BY
RP 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 [10]
RP STRUCTURE BY NMR OF 2-52.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of RSGI RUH-027, a UBA domain from mouse cDNA.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Ubiquitin-binding protein that plays a role in the modulation
CC of innate immune response. Blocks both the RIG-I-like receptors (RLR)
CC and NF-kappa-B pathways. Following viral infection, UBXN1 is induced
CC and recruited to the RLR component MAVS. In turn, interferes with MAVS
CC oligomerization, and disrupts the MAVS/TRAF3/TRAF6 signalosome. This
CC function probably serves as a brake to prevent excessive RLR signaling.
CC Interferes with the TNFalpha-triggered NF-kappa-B pathway by
CC interacting with cellular inhibitors of apoptosis proteins (cIAPs) and
CC thereby inhibiting their recruitment to TNFR1. Prevents also the
CC activation of NF-kappa-B by associating with CUL1 and thus inhibiting
CC NF-kappa-B inhibitor alpha/NFKBIA degradation that remains bound to NF-
CC kappa-B. Interacts with the BRCA1-BARD1 heterodimer and regulates its
CC activity. Specifically binds 'Lys-6'-linked polyubiquitin chains.
CC Interaction with autoubiquitinated BRCA1 leads to the inhibition of the
CC E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer.
CC Component of a complex required to couple deglycosylation and
CC proteasome-mediated degradation of misfolded proteins in the
CC endoplasmic reticulum that are retrotranslocated in the cytosol.
CC {ECO:0000250|UniProtKB:Q04323, ECO:0000269|PubMed:16709668}.
CC -!- SUBUNIT: Interacts with MAVS; this interaction prevents MAVS
CC oligomerization and thus disrupts the RLR signaling pathway. Interacts
CC with CUL1; this interaction inhibits CUL1-mediated degradation of NF-
CC kappa-B inhibitors. Interacts with BIRC2/c-IAP1; this interaction
CC prevents TNFalpha-stimulated RIP1 ubiquitination and subsequent NF-
CC kappa-B activation. Component of a complex required to couple
CC retrotranslocation, ubiquitination and deglycosylation composed of
CC NGLY1, SAKS1, AMFR, VCP and RAD23B (PubMed:11562482). Interacts with
CC HOMER2 (PubMed:16709668). Interacts directly with VCP. Interacts with
CC BRCA1 and BARD1; interaction takes place when BRCA1 is not
CC autoubiquitinated but is strongly enhanced in the presence of
CC autoubiquitinated BRCA1. {ECO:0000250|UniProtKB:Q04323,
CC ECO:0000269|PubMed:11562482, ECO:0000269|PubMed:15944415,
CC ECO:0000269|PubMed:16709668}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15944415}.
CC -!- DOMAIN: The UBA domain specifically recognizes and binds 'Lys-6'-linked
CC polyubiquitin chains. {ECO:0000250}.
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DR EMBL; AK150442; BAE29564.1; -; mRNA.
DR EMBL; BC006701; AAH06701.1; -; mRNA.
DR CCDS; CCDS29553.1; -.
DR RefSeq; NP_666205.1; NM_146093.1.
DR RefSeq; XP_006526985.1; XM_006526922.1.
DR PDB; 1WHC; NMR; -; A=2-52.
DR PDBsum; 1WHC; -.
DR AlphaFoldDB; Q922Y1; -.
DR SMR; Q922Y1; -.
DR BioGRID; 230443; 24.
DR CORUM; Q922Y1; -.
DR IntAct; Q922Y1; 4.
DR MINT; Q922Y1; -.
DR STRING; 10090.ENSMUSP00000093974; -.
DR MEROPS; C19.089; -.
DR iPTMnet; Q922Y1; -.
DR PhosphoSitePlus; Q922Y1; -.
DR REPRODUCTION-2DPAGE; IPI00123589; -.
DR REPRODUCTION-2DPAGE; Q922Y1; -.
DR EPD; Q922Y1; -.
DR jPOST; Q922Y1; -.
DR MaxQB; Q922Y1; -.
DR PaxDb; Q922Y1; -.
DR PeptideAtlas; Q922Y1; -.
DR PRIDE; Q922Y1; -.
DR ProteomicsDB; 298114; -.
DR Antibodypedia; 1591; 126 antibodies from 22 providers.
DR DNASU; 225896; -.
DR Ensembl; ENSMUST00000166407; ENSMUSP00000133250; ENSMUSG00000071655.
DR Ensembl; ENSMUST00000238036; ENSMUSP00000157971; ENSMUSG00000071655.
DR GeneID; 225896; -.
DR KEGG; mmu:225896; -.
DR UCSC; uc008gnp.1; mouse.
DR CTD; 51035; -.
DR MGI; MGI:1289301; Ubxn1.
DR VEuPathDB; HostDB:ENSMUSG00000071655; -.
DR eggNOG; KOG2689; Eukaryota.
DR GeneTree; ENSGT00940000156457; -.
DR HOGENOM; CLU_047594_1_0_1; -.
DR InParanoid; Q922Y1; -.
DR OMA; AQHFPRK; -.
DR OrthoDB; 1297214at2759; -.
DR PhylomeDB; Q922Y1; -.
DR TreeFam; TF313944; -.
DR Reactome; R-MMU-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR BioGRID-ORCS; 225896; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ubxn1; mouse.
DR EvolutionaryTrace; Q922Y1; -.
DR PRO; PR:Q922Y1; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q922Y1; protein.
DR Bgee; ENSMUSG00000071655; Expressed in urinary bladder urothelium and 259 other tissues.
DR ExpressionAtlas; Q922Y1; baseline and differential.
DR Genevisible; Q922Y1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; ISO:MGI.
DR GO; GO:0071796; F:K6-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISO:MGI.
DR GO; GO:1904855; F:proteasome regulatory particle binding; ISO:MGI.
DR GO; GO:0043130; F:ubiquitin binding; ISO:MGI.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:1904293; P:negative regulation of ERAD pathway; ISO:MGI.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; ISO:MGI.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; ISO:MGI.
DR CDD; cd14302; UBA_UBXN1; 1.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041923; UBA_UBXN1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50033; UBX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Coiled coil; Cytoplasm; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT CHAIN 2..297
FT /note="UBX domain-containing protein 1"
FT /id="PRO_0000211024"
FT DOMAIN 2..42
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 209..291
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 38..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..297
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250"
FT COMPBIAS 84..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 200
FT /note="Phosphoserine; by MAPK12"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT HELIX 6..11
FT /evidence="ECO:0007829|PDB:1WHC"
FT TURN 12..14
FT /evidence="ECO:0007829|PDB:1WHC"
FT HELIX 17..27
FT /evidence="ECO:0007829|PDB:1WHC"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:1WHC"
SQ SEQUENCE 297 AA; 33573 MW; 50746EF6CF340269 CRC64;
MAELTALESL IEMGFPRGRA EKALALTGNQ GIEAAMDWLM EHEDDPDVDE PLETPLSHVL
GREPTPSEQV GPEGSGSAAG ESRPILTEEE RQEQTKRMLE LVAQKQRERE EREEREALER
EKQRRRQGQE LSVARQKLQE DEMRRAAEER RREKAEELAA RQRVREKIER DKAERAKKYG
GSVGSRSSPP ATDPGPVPSS PSQEPPTKRE YDQCRIQVRL PDGTSLTQTF RAREQLAAVR
LYVELHRGEE PGQDQDPVQL LSGFPRRAFS EADMERPLQE LGLVPSAVLI VAKKCPS
