NFX1_MOUSE
ID NFX1_MOUSE Reviewed; 1114 AA.
AC B1AY10; Q3U2A7; Q3UK95; Q3UMW1; Q7TPT4; Q8CC59; Q9DBC8; Q9JKW7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Transcriptional repressor NF-X1;
DE Short=m-Nfx.1;
DE EC=2.3.2.-;
DE AltName: Full=Nuclear transcription factor, X box-binding protein 1;
GN Name=Nfx1;
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] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12047746; DOI=10.1046/j.1365-2567.2002.01416.x;
RA Arlotta P., Miyazaki D., Copeland N.G., Gilbert D.J., Jenkins N.A.,
RA Ono S.J.;
RT "Murine NFX.1: isolation and characterization of its messenger RNA, mapping
RT of its chromosomal location and assessment of its developmental
RT expression.";
RL Immunology 106:173-181(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Diencephalon, Liver, Lung, and Placenta;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Egg;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-81; SER-126 AND SER-130, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Pancreas, and Spleen;
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: Binds to the X-box motif of MHC class II genes and represses
CC their expression. May play an important role in regulating the duration
CC of an inflammatory response by limiting the period in which MHC class
CC II molecules are induced by interferon-gamma. Together with PABPC1 or
CC PABPC4, acts as a coactivator for TERT expression. Mediates E2-
CC dependent ubiquitination. {ECO:0000269|PubMed:12047746}.
CC -!- SUBUNIT: Interacts with PABPC1 and PABPC4. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=B1AY10-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B1AY10-2; Sequence=VSP_033694, VSP_033695;
CC Name=3;
CC IsoId=B1AY10-3; Sequence=VSP_033693, VSP_033696;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed, with highest levels in
CC thymus. {ECO:0000269|PubMed:12047746}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed at 12 dpc and 14 dpc.
CC {ECO:0000269|PubMed:12047746}.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an ubiquitin-
CC conjugating enzyme (E2) and facilitates ubiquitination. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NFX1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF34700.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF223576; AAF34700.1; ALT_FRAME; mRNA.
DR EMBL; AK005038; BAB23765.1; -; mRNA.
DR EMBL; AK033850; BAC28494.1; -; mRNA.
DR EMBL; AK144647; BAE25987.1; -; mRNA.
DR EMBL; AK146108; BAE26907.1; -; mRNA.
DR EMBL; AK155387; BAE33235.1; -; mRNA.
DR EMBL; AL837521; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053709; AAH53709.1; -; mRNA.
DR CCDS; CCDS18054.1; -. [B1AY10-1]
DR CCDS; CCDS71359.1; -. [B1AY10-2]
DR CCDS; CCDS71360.1; -. [B1AY10-3]
DR RefSeq; NP_001277377.1; NM_001290448.1. [B1AY10-3]
DR RefSeq; NP_001277378.1; NM_001290449.1. [B1AY10-2]
DR RefSeq; NP_076228.2; NM_023739.3. [B1AY10-1]
DR AlphaFoldDB; B1AY10; -.
DR SMR; B1AY10; -.
DR BioGRID; 216539; 18.
DR IntAct; B1AY10; 2.
DR MINT; B1AY10; -.
DR STRING; 10090.ENSMUSP00000095747; -.
DR iPTMnet; B1AY10; -.
DR PhosphoSitePlus; B1AY10; -.
DR SwissPalm; B1AY10; -.
DR EPD; B1AY10; -.
DR jPOST; B1AY10; -.
DR MaxQB; B1AY10; -.
DR PaxDb; B1AY10; -.
DR PeptideAtlas; B1AY10; -.
DR PRIDE; B1AY10; -.
DR ProteomicsDB; 287501; -. [B1AY10-1]
DR ProteomicsDB; 287502; -. [B1AY10-2]
DR ProteomicsDB; 287503; -. [B1AY10-3]
DR Antibodypedia; 25201; 146 antibodies from 29 providers.
DR DNASU; 74164; -.
DR Ensembl; ENSMUST00000030133; ENSMUSP00000030133; ENSMUSG00000028423. [B1AY10-3]
DR Ensembl; ENSMUST00000091614; ENSMUSP00000089203; ENSMUSG00000028423. [B1AY10-2]
DR Ensembl; ENSMUST00000098143; ENSMUSP00000095747; ENSMUSG00000028423. [B1AY10-1]
DR GeneID; 74164; -.
DR KEGG; mmu:74164; -.
DR UCSC; uc008sic.2; mouse. [B1AY10-2]
DR UCSC; uc008sid.2; mouse. [B1AY10-3]
DR UCSC; uc008sie.2; mouse. [B1AY10-1]
DR CTD; 4799; -.
DR MGI; MGI:1921414; Nfx1.
DR VEuPathDB; HostDB:ENSMUSG00000028423; -.
DR eggNOG; KOG1952; Eukaryota.
DR GeneTree; ENSGT00940000156325; -.
DR HOGENOM; CLU_005714_1_2_1; -.
DR InParanoid; B1AY10; -.
DR OMA; WCEKEVD; -.
DR OrthoDB; 299100at2759; -.
DR PhylomeDB; B1AY10; -.
DR TreeFam; TF105889; -.
DR BioGRID-ORCS; 74164; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Nfx1; mouse.
DR PRO; PR:B1AY10; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; B1AY10; protein.
DR Bgee; ENSMUSG00000028423; Expressed in cumulus cell and 255 other tissues.
DR Genevisible; B1AY10; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:MGI.
DR GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IDA:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0051865; P:protein autoubiquitination; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central.
DR CDD; cd02643; R3H_NF-X1; 1.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR034078; NFX1_fam.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR034076; R3H_NF-X1.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12360; PTHR12360; 1.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 7.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00438; ZnF_NFX; 9.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; DNA-binding; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Transcription;
KW Transcription regulation; Transferase; Ubl conjugation pathway; Zinc;
KW Zinc-finger.
FT CHAIN 1..1114
FT /note="Transcriptional repressor NF-X1"
FT /id="PRO_0000334614"
FT DOMAIN 988..1056
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT ZN_FING 352..403
FT /note="RING-type; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175"
FT ZN_FING 447..465
FT /note="NF-X1-type 1"
FT ZN_FING 500..519
FT /note="NF-X1-type 2"
FT ZN_FING 561..580
FT /note="NF-X1-type 3"
FT ZN_FING 626..649
FT /note="NF-X1-type 4"
FT ZN_FING 688..707
FT /note="NF-X1-type 5"
FT ZN_FING 715..734
FT /note="NF-X1-type 6"
FT ZN_FING 826..848
FT /note="NF-X1-type 7"
FT ZN_FING 857..878
FT /note="NF-X1-type 8"
FT REGION 9..26
FT /note="Interaction with PABPC1 and PABC4"
FT /evidence="ECO:0000250"
FT REGION 20..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..287
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1071..1095
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..48
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..106
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 118..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..205
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 50
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12986"
FT MOD_RES 81
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12986"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 130
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12986"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q12986"
FT VAR_SEQ 803..818
FT /note="LRSNIPCHLVDISCGL -> ELTIKKLWTFKETLDF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033693"
FT VAR_SEQ 803..804
FT /note="LR -> RQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033694"
FT VAR_SEQ 805..1114
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_033695"
FT VAR_SEQ 819..1114
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033696"
FT CONFLICT 49
FT /note="S -> N (in Ref. 2; BAC28494)"
FT /evidence="ECO:0000305"
FT CONFLICT 141
FT /note="T -> A (in Ref. 2; BAE33235)"
FT /evidence="ECO:0000305"
FT CONFLICT 273
FT /note="S -> P (in Ref. 4; AAH53709)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="C -> Y (in Ref. 2; BAE33235)"
FT /evidence="ECO:0000305"
FT CONFLICT 590
FT /note="C -> R (in Ref. 4; AAH53709)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1114 AA; 123811 MW; A31013ACC6FB31F4 CRC64;
MAEAPPVSGT FKFNTDAAEF IPQERKTSGL NCGTQRRLDS SRIGRRNYSS SPPCHLPRHI
PYEDISAVHQ HSYASGSKPK SPQGFFQSSN KSLKNHGLQN QPWQKARNEK HQNRNKKAQG
LSEQTSDTSS LESVARSESG TNPREHSPSE SEKEVVIADP RGAKPKKAAQ LTYNYGRGPK
AKGRLRSEWG NRMSPKSEDE NTRPVAISHT DSSDASCRKP VVDPCVCRRN EQRRYPQKRP
PWEVEGARPR PGRNPPKQES QRHINAGPKT NMSPIPKDNL RERPTKSACD TGNLAVVSKS
SRRVNQEKTA VRRQDPQVLS PFPRGKQNHM LKNVETHTGS LIEQLTTEKY ECMVCCELVQ
VTAPVWSCQS CFHVFHLNCI KKWARSPASH ADGQSGWRCP ACQNVSAHVP NTYTCFCGKV
KNPEWSRNEI PHSCGEVCRK KQPGQDCPHS CNLLCHPGPC PPCPAFTTKT CECGRTRHTV
RCGQPVSVHC SNACENILNC GQHHCAELCH GGQCQPCRII LNQVCYCGST SRDVLCGTDV
GKSDGFGDFS CLKICGKDLK CGSHTCSQVC HPQPCQPCPR LPHLVRYCPC GQTPLSQLLE
HGSNARKTCM DPVPSCGKVC GKPLACGSSD FIHTCEKLCH EGDCGPCSRT SVISCRCSFR
TKELPCTSLK SEDATFMCDK RCNKKRLCGR HKCNEICCVD KEHKCPLICG RKLRCGLHRC
EEPCHRGNCQ TCWQASFDEL TCHCGASVIY PPVPCGTRPP ECTQTCARIH ECDHPVYHSC
HSEEKCPPCT FLTQKWCMGK HELRSNIPCH LVDISCGLPC SAMLPCGMHK CQRLCHKGEC
LVDEACKQPC TTPRGDCGHP CMAPCHPSLP CPVTACKAKV ELQCECGRRK EMVICSEASG
TYQRIVAISM ASKITDMQLG DSVEISKLIT KKEVQQARLQ CDEECAALER RKRLAEAFDI
TDDSDPFNVR SSASKFSDSL KDDARKDLKF VSDVEKEMET LVEAVNKGKN NKKSHCFPPM
NRDHRRIIHD LAQVYGLESI SYDSEPKRNV VVTAVRGKSV CPPTTLTSVI ERETQTRPPP
PIPHHRHQAD KAPGSSTLQK IVKEAVIDYF DVQD
