UBIM_MOUSE
ID UBIM_MOUSE Reviewed; 74 AA.
AC P35545; Q9JJ24;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Ubiquitin-like protein FUBI;
DE AltName: Full=Monoclonal non-specific suppressor factor beta;
DE Short=MNSF-beta;
GN Name=Fau;
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=SWR/J;
RX PubMed=8395683;
RA Michiels L., van der Rauwelaert E., van Hasselt F., Kas K., Merregaert J.;
RT "fau cDNA encodes a ubiquitin-like-S30 fusion protein and is expressed as
RT an antisense sequence in the Finkel-Biskis-Reilly murine sarcoma virus.";
RL Oncogene 8:2537-2546(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ;
RX PubMed=7724584; DOI=10.1073/pnas.92.8.3463;
RA Nakamura M., Xavier R.M., Tsunematsu T., Tanigawa Y.;
RT "Molecular cloning and characterization of a cDNA encoding monoclonal
RT nonspecific suppressor factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:3463-3467(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=BALB/cJ; TISSUE=Liver;
RX PubMed=7774934; DOI=10.1016/0888-7543(95)80140-h;
RA Casteels D., Poirier C., Guenet J.-L., Merregaert J.;
RT "The mouse Fau gene: genomic structure, chromosomal localization, and
RT characterization of two retropseudogenes.";
RL Genomics 25:291-294(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Swiss OB;
RA Nie G.-Y., Li Y., Salamonsen L.A., Clements J.A., Findlay J.K.;
RT "Identification of monoclonal non-specific suppressor factor beta as one of
RT the genes differentially expressed at implantation sites compared to
RT interimplantation sites in the mouse uterus.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Kidney, and Small intestine;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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).
CC -!- INTERACTION:
CC P35545; Q9CPT0: Bcl2l14; NbExp=4; IntAct=EBI-309546, EBI-8296066;
CC P35545; Q62419: Sh3gl1; NbExp=3; IntAct=EBI-309546, EBI-642935;
CC -!- MISCELLANEOUS: This protein is synthesized with ribosomal S30 as its C-
CC terminal extension.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; X65922; CAA46715.1; ALT_TERM; mRNA.
DR EMBL; D26610; BAA05655.1; ALT_TERM; mRNA.
DR EMBL; L33715; AAA91564.1; ALT_TERM; Genomic_DNA.
DR EMBL; AF147745; AAF80246.1; ALT_TERM; mRNA.
DR EMBL; AK002355; BAB22034.1; ALT_TERM; mRNA.
DR EMBL; AK008466; BAB25684.1; ALT_TERM; mRNA.
DR EMBL; BC058691; AAH58691.1; ALT_TERM; mRNA.
DR EMBL; BC062873; AAH62873.1; ALT_TERM; mRNA.
DR PIR; I48346; I48346.
DR RefSeq; NP_001153711.1; NM_001160239.2.
DR RefSeq; NP_001177365.1; NM_001190436.1.
DR RefSeq; NP_032016.1; NM_007990.3.
DR AlphaFoldDB; P35545; -.
DR SMR; P35545; -.
DR BioGRID; 199600; 6.
DR IntAct; P35545; 3.
DR MINT; P35545; -.
DR STRING; 10090.ENSMUSP00000128416; -.
DR EPD; P35545; -.
DR MaxQB; P35545; -.
DR PaxDb; P35545; -.
DR PeptideAtlas; P35545; -.
DR PRIDE; P35545; -.
DR ProteomicsDB; 298353; -.
DR DNASU; 14109; -.
DR GeneID; 14109; -.
DR KEGG; mmu:14109; -.
DR CTD; 2197; -.
DR MGI; MGI:102547; Fau.
DR eggNOG; KOG0001; Eukaryota.
DR eggNOG; KOG0009; Eukaryota.
DR InParanoid; P35545; -.
DR OrthoDB; 1484551at2759; -.
DR BioGRID-ORCS; 14109; 28 hits in 58 CRISPR screens.
DR ChiTaRS; Fau; mouse.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; P35545; protein.
DR GO; GO:0022626; C:cytosolic ribosome; ISO:MGI.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0003735; F:structural constituent of ribosome; ISO:MGI.
DR GO; GO:0019731; P:antibacterial humoral response; ISO:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR GO; GO:0050830; P:defense response to Gram-positive bacterium; IDA:UniProtKB.
DR GO; GO:0002227; P:innate immune response in mucosa; ISO:MGI.
DR GO; GO:0000028; P:ribosomal small subunit assembly; ISO:MGI.
DR CDD; cd01793; Ubl_FUBI; 1.
DR InterPro; IPR039415; FUBI.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 1.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00299; UBIQUITIN_1; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Reference proteome.
FT CHAIN 1..74
FT /note="Ubiquitin-like protein FUBI"
FT /id="PRO_0000114883"
SQ SEQUENCE 74 AA; 7786 MW; 315D314C260BEB87 CRC64;
MQLFVRAQEL HTLEVTGQET VAQIKDHVAS LEGIAPEDQV VLLAGSPLED EATLGQCGVE
ALTTLEVAGR MLGG
