NFRKB_MOUSE
ID NFRKB_MOUSE Reviewed; 1296 AA.
AC Q6PIJ4; Q8BWV5; Q8K0X6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nuclear factor related to kappa-B-binding protein;
DE AltName: Full=DNA-binding protein R kappa-B;
GN Name=Nfrkb;
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, and FVB/N; 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 504-1296.
RC STRAIN=C57BL/6J; TISSUE=Hippocampus;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-1288, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC 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).
CC -!- FUNCTION: Binds to the DNA consensus sequence 5'-GGGGAATCTCC-3'.
CC {ECO:0000250}.
CC -!- FUNCTION: Putative regulatory component of the chromatin remodeling
CC INO80 complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. Modulates the deubiquitinase
CC activity of UCHL5 in the INO80 complex (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the N-terminus of
CC INO80. Interacts with UCHL5 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- DOMAIN: NFRKB seems to be mostly disordered. The wing-helix like domain
CC doesn't bind DNA (By similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NFRKB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC33927.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; BC029701; AAH29701.1; -; mRNA.
DR EMBL; BC033595; AAH33595.1; -; mRNA.
DR EMBL; AK049804; BAC33927.1; ALT_INIT; mRNA.
DR CCDS; CCDS22949.1; -.
DR RefSeq; NP_766354.2; NM_172766.3.
DR AlphaFoldDB; Q6PIJ4; -.
DR SMR; Q6PIJ4; -.
DR BioGRID; 231624; 3.
DR ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR IntAct; Q6PIJ4; 4.
DR MINT; Q6PIJ4; -.
DR STRING; 10090.ENSMUSP00000083341; -.
DR iPTMnet; Q6PIJ4; -.
DR PhosphoSitePlus; Q6PIJ4; -.
DR EPD; Q6PIJ4; -.
DR jPOST; Q6PIJ4; -.
DR MaxQB; Q6PIJ4; -.
DR PaxDb; Q6PIJ4; -.
DR PeptideAtlas; Q6PIJ4; -.
DR PRIDE; Q6PIJ4; -.
DR ProteomicsDB; 287418; -.
DR Antibodypedia; 1820; 122 antibodies from 25 providers.
DR DNASU; 235134; -.
DR Ensembl; ENSMUST00000086167; ENSMUSP00000083341; ENSMUSG00000042185.
DR GeneID; 235134; -.
DR KEGG; mmu:235134; -.
DR UCSC; uc009orr.3; mouse.
DR CTD; 4798; -.
DR MGI; MGI:2442410; Nfrkb.
DR VEuPathDB; HostDB:ENSMUSG00000042185; -.
DR eggNOG; KOG1927; Eukaryota.
DR GeneTree; ENSGT00390000016213; -.
DR HOGENOM; CLU_007638_0_0_1; -.
DR InParanoid; Q6PIJ4; -.
DR OMA; DQAFCKE; -.
DR OrthoDB; 140291at2759; -.
DR PhylomeDB; Q6PIJ4; -.
DR TreeFam; TF324944; -.
DR Reactome; R-MMU-5689603; UCH proteinases.
DR Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR BioGRID-ORCS; 235134; 14 hits in 111 CRISPR screens.
DR ChiTaRS; Nfrkb; mouse.
DR PRO; PR:Q6PIJ4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q6PIJ4; protein.
DR Bgee; ENSMUSG00000042185; Expressed in secondary oocyte and 244 other tissues.
DR ExpressionAtlas; Q6PIJ4; baseline and differential.
DR Genevisible; Q6PIJ4; MM.
DR GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0002020; F:protease binding; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0045739; P:positive regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IMP:ComplexPortal.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
DR GO; GO:0045995; P:regulation of embryonic development; IMP:ComplexPortal.
DR GO; GO:0000723; P:telomere maintenance; IMP:ComplexPortal.
DR Gene3D; 1.10.10.2430; -; 1.
DR InterPro; IPR044867; DEUBAD_dom.
DR InterPro; IPR024867; NFRKB.
DR InterPro; IPR025220; NFRKB_winged_dom.
DR InterPro; IPR038106; NFRKB_winged_sf.
DR PANTHER; PTHR13052; PTHR13052; 1.
DR Pfam; PF14465; NFRKB_winged; 1.
DR PROSITE; PS51916; DEUBAD; 1.
PE 1: Evidence at protein level;
KW Acetylation; DNA damage; DNA recombination; DNA repair; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1296
FT /note="Nuclear factor related to kappa-B-binding protein"
FT /id="PRO_0000227808"
FT DOMAIN 39..156
FT /note="DEUBAD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01264"
FT REGION 165..186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..495
FT /note="Winged-helix like domain"
FT /evidence="ECO:0000250"
FT REGION 663..758
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1015..1036
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..224
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 681..715
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 716..736
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..758
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 228
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4R8"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4R8"
FT MOD_RES 1019
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4R8"
FT MOD_RES 1234
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4R8"
FT MOD_RES 1288
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 327
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P4R8"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q6P4R8"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6P4R8"
FT CROSSLNK 488
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:Q6P4R8"
SQ SEQUENCE 1296 AA; 138764 MW; ED6A42FE704DED1B CRC64;
MDSLDHMLTD PLELGPCGDG HSTGIMEDCL LGGTRVSLPE DLLEDPEIFF DVVSLSTWQE
VLSDSQREHL QQFLPRFPAD SVEQQRELIL ALFSGENFRF GNPLHIAQKL FRDGHFNPEV
VKYRQLCFKS QYKRYLNSQQ QYFHRLLKQI LASRSDLLEM ARRSGPALPF PHKHHSPSRS
PEEREWRTQQ RYLKVLREVK EECGDTALSS DEEDLSSWLP SSPARSPSPA VPLRVVPTLS
TTDMKTADKI ELGDSDLKLM LKKHHEKRKH QPDHPDLLTG DLTLSDIMTR VNAGRKGSLA
ALYDLAVLKK KVKEKEEKKK KKIKLIKSEA EDLAEPLSST EGVPTLSQAP SPLAISSIKE
EPLEDIKPCL GINEISSSFF SLLLEILLLE SQASLPMLED RVLDWQSSPA SSLNSWFSAA
PNWAELVLPA LQYLAGESRA VPSSFSPFVE FKEKTQQWKL LGQSQDNEKE LAALFHLWLE
TKDQAFCKEN EDSSDAMTPV PRVRTDYVVR PSTGEEKRVF QEQERYRYSQ PHKAFTFRMH
GFESVVGPVK GVFDKETSLN KAREHSLLRS DRPAYVTILS LVRDAAARLP NGEGTRAEIC
ELLKDSQFLA PDVTSTQVNT VVSGALDRLH YEKDPCVKYD IGRKLWIYLH RDRSEEEFER
IHQAQAAAAK ARKALQQKPK PPSKVKSSNK EGSTKGLSGP SEQSQMSLSD SSMPPTPVTP
VTPTTPALPT PISPPPVSAV NRSGSSTVSE PAQSSSGVLL VSSPTMPQLG TMLSPASIQT
PPSSQATARV VSHSSSAGLP QVRVVAQPSL PAVSQQSVGP AQPLPQMPAG PQIRVPVTAT
QTKVVPQAVM ATVPVKGQTA AASVQRPGPG QTGLTVTNLP AAVSPVSKTA MSSPGNSAPS
ASTTAVIQNV TGQNIIKQVS ITGQLGVKPQ TGSSIPLTAT NFRIQGKDVL RLPPSSITTD
AKGQTVLRIT PDMMATLAKS QVTTVKLTQD LFGAGSGTAG KGISATLHVT SNPVHAADSP
AKAPSASVPS SAPAGTTVVK VTPDLKPTET ANSAFRLMPA LGVSVADQKG KNTVASSEAK
PAATIRIVQG LGVMPPKAGQ TITVAAHAKQ GASVAGGSGT VHSSTVSLPS INAAVSKTVA
VASGATSTPI SIGTGAPTVR QVPVNTTVVS TSQSGKLPTR ITVPLSVISQ PMKGKSVVTA
PIIKGNLGAN LSGLGRNIIL TTMPAGTKLI AGNKPVSFLT AQQLQQLQQQ GQATQVRIQT
VPASHLQQGT ASGSSKAVST VVVTTAPSPK QAPEQQ
