KBRS1_MOUSE
ID KBRS1_MOUSE Reviewed; 192 AA.
AC Q8CEC5; Q9JKV3;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=NF-kappa-B inhibitor-interacting Ras-like protein 1;
DE AltName: Full=I-kappa-B-interacting Ras-like protein 1;
DE Short=Kappa B-Ras protein 1;
DE Short=KappaB-Ras1;
GN Name=Nkiras1;
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].
RX PubMed=10657303; DOI=10.1126/science.287.5454.869;
RA Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W., Ghosh S.;
RT "A subclass of Ras proteins that regulate the degradation of IkappaB.";
RL Science 287:869-873(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Placenta, and Skin;
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 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).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, 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).
CC -!- FUNCTION: Atypical Ras-like protein that acts as a potent regulator of
CC NF-kappa-B activity by preventing the degradation of NF-kappa-B
CC inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more
CC resistant to degradation. May act by blocking phosphorylation of NFKBIB
CC and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. It
CC is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms
CC block phosphorylation of NFKBIB (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with both NF-kappa-B inhibitor alpha (NFKBIA) and
CC beta (NFKBIB) in vitro. However, it probably only interacts with NFKBIB
CC in vivo. Forms a complex with NFKBIB and NF-kappa-B heterodimer
CC (p50/NFKB1 and p65/RELA). Also interacts with c-Rel (REL) (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: In contrast to other members of the Ras family, the members of
CC the KappaB-Ras subfamily do not contain the conserved Gly and Gln
CC residues in positions 13 and 65, which are replaced by Leu residues,
CC and are therefore similar to the constitutively active forms of
CC oncogenic forms of Ras. This suggests that members of this family are
CC clearly different from other small GTPases proteins.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC KappaB-Ras subfamily. {ECO:0000305}.
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DR EMBL; AF225707; AAF43150.1; -; mRNA.
DR EMBL; AK028539; BAC25998.1; -; mRNA.
DR EMBL; AK148040; BAE28306.1; -; mRNA.
DR EMBL; AK167340; BAE39441.1; -; mRNA.
DR EMBL; BC061092; AAH61092.1; -; mRNA.
DR CCDS; CCDS26836.1; -.
DR RefSeq; NP_001303640.1; NM_001316711.1.
DR RefSeq; NP_001303641.1; NM_001316712.1.
DR RefSeq; NP_076015.2; NM_023526.4.
DR RefSeq; XP_006518160.1; XM_006518097.3.
DR AlphaFoldDB; Q8CEC5; -.
DR SMR; Q8CEC5; -.
DR BioGRID; 213637; 4.
DR STRING; 10090.ENSMUSP00000121496; -.
DR iPTMnet; Q8CEC5; -.
DR PhosphoSitePlus; Q8CEC5; -.
DR EPD; Q8CEC5; -.
DR MaxQB; Q8CEC5; -.
DR PaxDb; Q8CEC5; -.
DR PRIDE; Q8CEC5; -.
DR ProteomicsDB; 263479; -.
DR Antibodypedia; 11367; 365 antibodies from 32 providers.
DR DNASU; 69721; -.
DR Ensembl; ENSMUST00000132374; ENSMUSP00000121496; ENSMUSG00000021772.
DR GeneID; 69721; -.
DR KEGG; mmu:69721; -.
DR UCSC; uc007shs.1; mouse.
DR CTD; 28512; -.
DR MGI; MGI:1916971; Nkiras1.
DR VEuPathDB; HostDB:ENSMUSG00000021772; -.
DR eggNOG; KOG3883; Eukaryota.
DR GeneTree; ENSGT00940000159705; -.
DR HOGENOM; CLU_041217_17_0_1; -.
DR InParanoid; Q8CEC5; -.
DR OMA; ADMAQQW; -.
DR OrthoDB; 1382000at2759; -.
DR PhylomeDB; Q8CEC5; -.
DR TreeFam; TF314483; -.
DR Reactome; R-MMU-1810476; RIP-mediated NFkB activation via ZBP1.
DR Reactome; R-MMU-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-MMU-933542; TRAF6 mediated NF-kB activation.
DR BioGRID-ORCS; 69721; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Nkiras1; mouse.
DR PRO; PR:Q8CEC5; -.
DR Proteomes; UP000000589; Chromosome 14.
DR RNAct; Q8CEC5; protein.
DR Bgee; ENSMUSG00000021772; Expressed in facial nucleus and 253 other tissues.
DR ExpressionAtlas; Q8CEC5; baseline and differential.
DR Genevisible; Q8CEC5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005783; C:endoplasmic reticulum; ISO:MGI.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0032794; F:GTPase activating protein binding; IPI:MGI.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; IEA:InterPro.
DR GO; GO:0048286; P:lung alveolus development; IGI:MGI.
DR GO; GO:0032484; P:Ral protein signal transduction; IGI:MGI.
DR GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; IGI:MGI.
DR GO; GO:0043129; P:surfactant homeostasis; IGI:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR042227; KBRS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR PANTHER; PTHR46152; PTHR46152; 1.
DR Pfam; PF00071; Ras; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; GTP-binding; Nucleotide-binding; Reference proteome.
FT CHAIN 1..192
FT /note="NF-kappa-B inhibitor-interacting Ras-like protein 1"
FT /id="PRO_0000225677"
FT REGION 58..93
FT /note="Interactions with NFKBIA and NFKBIB"
FT /evidence="ECO:0000250"
FT REGION 168..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 35..43
FT /note="Effector region"
FT BINDING 11..18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 61..65
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 120..123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 70
FT /note="E -> D (in Ref. 1; AAF43150)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 192 AA; 21662 MW; D83192A7A3949E73 CRC64;
MGKGCKVVIC GLLSVGKTAI LEQLLYGNHT IGMEDCETLE DVYMASVETD RGVKEQLHLY
DTRGLQKGVE LPKHYFSFAD GFVLVYSVNN LESFQRVELL KKEIDKFKDK KEVAIVVLGN
KLDLSEQRQV DADVAQQWAR SEKVKLWEVT VTDRRTLIEP FTLLASKLSQ PQSKSSFPLP
GRKNKGNSNP EN
