KBRS2_MOUSE
ID KBRS2_MOUSE Reviewed; 191 AA.
AC Q9CR56; Q8BWG0;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=NF-kappa-B inhibitor-interacting Ras-like protein 2;
DE AltName: Full=I-kappa-B-interacting Ras-like protein 2;
DE Short=Kappa B-Ras protein 2;
DE Short=KappaB-Ras2;
GN Name=Nkiras2;
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 NOD; TISSUE=Bone marrow, Kidney, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N, and FVB/N-3; TISSUE=Colon, and 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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear
CC whether it acts as a GTPase. Both GTP- and GDP-bound forms block
CC 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 (By 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 Ala and Leu
CC residues, respectively, and are therefore similar to the constitutively
CC active forms of oncogenic forms of Ras. This suggests that members of
CC this family are 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; AK010371; BAB26889.1; -; mRNA.
DR EMBL; AK015918; BAB30030.1; -; mRNA.
DR EMBL; AK052645; BAC35078.1; -; mRNA.
DR EMBL; AK083475; BAC38929.1; -; mRNA.
DR EMBL; AK149696; BAE29033.1; -; mRNA.
DR EMBL; AK169878; BAE41430.1; -; mRNA.
DR EMBL; BC013469; AAH13469.1; -; mRNA.
DR EMBL; BC024398; AAH24398.1; -; mRNA.
DR CCDS; CCDS25429.1; -.
DR RefSeq; NP_082300.1; NM_028024.2.
DR RefSeq; XP_017170264.1; XM_017314775.1.
DR RefSeq; XP_017170265.1; XM_017314776.1.
DR AlphaFoldDB; Q9CR56; -.
DR SMR; Q9CR56; -.
DR STRING; 10090.ENSMUSP00000017981; -.
DR iPTMnet; Q9CR56; -.
DR PhosphoSitePlus; Q9CR56; -.
DR EPD; Q9CR56; -.
DR MaxQB; Q9CR56; -.
DR PaxDb; Q9CR56; -.
DR PeptideAtlas; Q9CR56; -.
DR PRIDE; Q9CR56; -.
DR ProteomicsDB; 301752; -.
DR Antibodypedia; 79897; 219 antibodies from 31 providers.
DR DNASU; 71966; -.
DR Ensembl; ENSMUST00000017981; ENSMUSP00000017981; ENSMUSG00000017837.
DR Ensembl; ENSMUST00000051947; ENSMUSP00000059559; ENSMUSG00000017837.
DR Ensembl; ENSMUST00000107376; ENSMUSP00000102999; ENSMUSG00000017837.
DR GeneID; 71966; -.
DR KEGG; mmu:71966; -.
DR UCSC; uc007llt.1; mouse.
DR CTD; 28511; -.
DR MGI; MGI:1919216; Nkiras2.
DR VEuPathDB; HostDB:ENSMUSG00000017837; -.
DR eggNOG; KOG3883; Eukaryota.
DR GeneTree; ENSGT00940000157943; -.
DR HOGENOM; CLU_041217_17_1_1; -.
DR InParanoid; Q9CR56; -.
DR OMA; HPPQTKS; -.
DR OrthoDB; 1382000at2759; -.
DR PhylomeDB; Q9CR56; -.
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; 71966; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Nkiras2; mouse.
DR PRO; PR:Q9CR56; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9CR56; protein.
DR Bgee; ENSMUSG00000017837; Expressed in spermatocyte and 227 other tissues.
DR ExpressionAtlas; Q9CR56; baseline and differential.
DR Genevisible; Q9CR56; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:0006954; P:inflammatory response; IMP:MGI.
DR GO; GO:0048286; P:lung alveolus development; IGI:MGI.
DR GO; GO:0032484; P:Ral protein signal transduction; IGI:MGI.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IMP: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..191
FT /note="NF-kappa-B inhibitor-interacting Ras-like protein 2"
FT /id="PRO_0000225680"
FT REGION 1..191
FT /note="Small GTPase-like"
FT REGION 169..191
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 57
FT /note="V -> E (in Ref. 1; BAC35078)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 191 AA; 21494 MW; 1E429230C348C823 CRC64;
MGKSCKVVVC GQASVGKTSI LEQLLYGNHV VGSEMIETQE DIYVGSIETD RGVREQVRFY
DTRGLRDGAE LPKHCFSCTD GYVLVYSTDS RESFQRVELL KKEIDKSKDK KEVTIVVLGN
KCDLQEQRRV DPDVAQHWAK SEKVKLWEVS VADRRSLLEP FIYLASKMTQ PQSKSAFPLS
RKNKGSGSLD G
