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IKBE_MOUSE
ID   IKBE_MOUSE              Reviewed;         364 AA.
AC   O54910; Q3U686; Q9CZZ9; Q9D7U3;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 2.
DT   03-AUG-2022, entry version 154.
DE   RecName: Full=NF-kappa-B inhibitor epsilon;
DE            Short=NF-kappa-BIE;
DE   AltName: Full=I-kappa-B-epsilon;
DE            Short=IkB-E;
DE            Short=IkB-epsilon;
DE            Short=IkappaBepsilon;
GN   Name=Nfkbie; Synonyms=Ikbe;
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=Brain;
RX   PubMed=9405619; DOI=10.1073/pnas.94.26.14372;
RA   Simeonidis S., Liang S., Chen G., Thanos D.;
RT   "Cloning and functional characterization of mouse IkappaBepsilon.";
RL   Proc. Natl. Acad. Sci. U.S.A. 94:14372-14377(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Bone marrow, Embryo, and Stomach;
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 MRNA].
RC   STRAIN=FVB/N; TISSUE=Salivary gland;
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=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: Inhibits NF-kappa-B by complexing with and trapping it in the
CC       cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel
CC       complexes (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with RELA, REL, NFKB1 nuclear factor NF-kappa-B p50
CC       subunit and NFKB2 nuclear factor NF-kappa-B p52 subunit. {ECO:0000250}.
CC   -!- INTERACTION:
CC       O54910; O08749: Dld; NbExp=4; IntAct=EBI-6688774, EBI-773199;
CC       O54910; Q04863: Relb; NbExp=2; IntAct=EBI-6688774, EBI-1209145;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- PTM: Serine phosphorylated; followed by proteasome-dependent
CC       degradation.
CC   -!- SIMILARITY: Belongs to the NF-kappa-B inhibitor family. {ECO:0000305}.
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DR   EMBL; AF030896; AAB97517.1; -; mRNA.
DR   EMBL; AK008843; BAB25924.1; -; mRNA.
DR   EMBL; AK011965; BAB27943.1; -; mRNA.
DR   EMBL; AK151450; BAE30410.1; -; mRNA.
DR   EMBL; AK153248; BAE31839.1; -; mRNA.
DR   EMBL; BC030923; AAH30923.1; -; mRNA.
DR   CCDS; CCDS28811.1; -.
DR   RefSeq; NP_001291885.1; NM_001304956.1.
DR   RefSeq; NP_032716.2; NM_008690.4.
DR   AlphaFoldDB; O54910; -.
DR   SMR; O54910; -.
DR   IntAct; O54910; 9.
DR   STRING; 10090.ENSMUSP00000024742; -.
DR   iPTMnet; O54910; -.
DR   PhosphoSitePlus; O54910; -.
DR   EPD; O54910; -.
DR   MaxQB; O54910; -.
DR   PaxDb; O54910; -.
DR   PeptideAtlas; O54910; -.
DR   PRIDE; O54910; -.
DR   ProteomicsDB; 267307; -.
DR   Antibodypedia; 800; 500 antibodies from 37 providers.
DR   DNASU; 18037; -.
DR   Ensembl; ENSMUST00000024742; ENSMUSP00000024742; ENSMUSG00000023947.
DR   GeneID; 18037; -.
DR   KEGG; mmu:18037; -.
DR   UCSC; uc008cqv.2; mouse.
DR   CTD; 4794; -.
DR   MGI; MGI:1194908; Nfkbie.
DR   VEuPathDB; HostDB:ENSMUSG00000023947; -.
DR   eggNOG; KOG0504; Eukaryota.
DR   GeneTree; ENSGT00940000159120; -.
DR   HOGENOM; CLU_000134_6_2_1; -.
DR   InParanoid; O54910; -.
DR   OMA; SDIVEGC; -.
DR   OrthoDB; 1341288at2759; -.
DR   PhylomeDB; O54910; -.
DR   TreeFam; TF320166; -.
DR   Reactome; R-MMU-1169091; Activation of NF-kappaB in B cells.
DR   BioGRID-ORCS; 18037; 5 hits in 61 CRISPR screens.
DR   ChiTaRS; Nfkbie; mouse.
DR   PRO; PR:O54910; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; O54910; protein.
DR   Bgee; ENSMUSG00000023947; Expressed in peripheral lymph node and 154 other tissues.
DR   ExpressionAtlas; O54910; baseline and differential.
DR   Genevisible; O54910; MM.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
DR   GO; GO:0042942; P:D-serine transport; ISO:MGI.
DR   Gene3D; 1.25.40.20; -; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   Pfam; PF12796; Ank_2; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 4.
PE   1: Evidence at protein level;
KW   ANK repeat; Cytoplasm; Phosphoprotein; Reference proteome; Repeat.
FT   CHAIN           1..364
FT                   /note="NF-kappa-B inhibitor epsilon"
FT                   /id="PRO_0000067008"
FT   REPEAT          122..155
FT                   /note="ANK 1"
FT   REPEAT          157..186
FT                   /note="ANK 2"
FT   REPEAT          190..219
FT                   /note="ANK 3"
FT   REPEAT          233..262
FT                   /note="ANK 4"
FT   REPEAT          267..296
FT                   /note="ANK 5"
FT   REPEAT          300..329
FT                   /note="ANK 6"
FT   REGION          1..108
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        34..48
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..69
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        89..105
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         18
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O00221"
FT   CONFLICT        97
FT                   /note="A -> V (in Ref. 1; AAB97517)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        182..191
FT                   /note="ASRILQDQHG -> PAEFCRSAC (in Ref. 2; BAB25924)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        291
FT                   /note="G -> R (in Ref. 1; AAB97517)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        345..364
FT                   /note="LSYLPFDDLKISGKPLLCTD -> GWVPTASHLEAGSAAAAVGTQAMSPLC
FT                   (in Ref. 2; BAB27943)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   364 AA;  39200 MW;  4426B58424187F3A CRC64;
     MSDARKGPDE ADDSQCDSGI ESLRSLRSLP EPTAAPGSGS SQSGCPQPWR HAPETHKEPE
     KEDADGERAD STYASSSLTE SFPLLERPEA KDPSPPAPGS PLPPAGVLSP QQLEALTYIS
     EDGDTLLHLA VIHEAPSVLF CCLAFLPQEV LDIQNNLYQT ALHLAVHLDQ PDVVRALVLK
     GASRILQDQH GDTALHVACR RQNLACACCL LEEQPEPGRQ LSHPLDLQLK NWQGLACLHI
     ATLQRNQPLI ELLLQNGADI DVQEGTSGKT ALHLAVETQE RSLVQFLLQA GARVDARMLN
     GCTPLHLAAG RGLNSISSTL CEAGADSLLL NVEDETPQDL AEDLLSYLPF DDLKISGKPL
     LCTD
 
 
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