Full text data of NKIRAS2
NKIRAS2
(KBRAS2)
[Confidence: low (only semi-automatic identification from reviews)]
NF-kappa-B inhibitor-interacting Ras-like protein 2 (I-kappa-B-interacting Ras-like protein 2; Kappa B-Ras protein 2; KappaB-Ras2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
NF-kappa-B inhibitor-interacting Ras-like protein 2 (I-kappa-B-interacting Ras-like protein 2; Kappa B-Ras protein 2; KappaB-Ras2)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9NYR9
ID KBRS2_HUMAN Reviewed; 191 AA.
AC Q9NYR9; A6NCZ5; B3KNN0; B4DNM3; Q6PK52; Q96KC7; Q9NSX1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 108.
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; Synonyms=KBRAS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INTERACTION WITH NFKBIA AND NFKBIB.
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.,
RA Ghosh S.;
RT "A subclass of Ras proteins that regulate the degradation of
RT IkappaB.";
RL Science 287:869-873(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Embryo, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Atypical Ras-like protein that acts as a potent
CC regulator of NF-kappa-B activity by preventing the degradation of
CC NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why
CC NFKBIB is more resistant to degradation. May act by blocking
CC phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-
CC kappa-B subunit. It is unclear whether it acts as a GTPase. Both
CC GTP- and GDP-bound forms block phosphorylation of NFKBIB (By
CC similarity).
CC -!- SUBUNIT: Interacts with both NF-kappa-B inhibitor alpha (NFKBIA)
CC and beta (NFKBIB) in vitro. However, it probably only interacts
CC with NFKBIB in vivo.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NYR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYR9-2; Sequence=VSP_017412;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9NYR9-3; Sequence=VSP_043151;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NYR9-4; Sequence=VSP_044873, VSP_044874;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: In contrast to other members of the Ras family, the
CC members of the KappaB-Ras subfamily do not contain the conserved
CC Gly and Gln residues in positions 13 and 65, which are replaced by
CC Ala and Leu residues, respectively, and are therefore similar to
CC the constitutively active forms of oncogenic forms of Ras. This
CC suggests that members of this family are clearly different from
CC other small GTPases proteins.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC KappaB-Ras subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55006.1; Type=Miscellaneous discrepancy; Note=Absence of residues from position 133 within an exon that change the frame which is not the result of an alternative splicing;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF229840; AAF34999.1; -; mRNA.
DR EMBL; AK027265; BAB55006.1; ALT_SEQ; mRNA.
DR EMBL; AK054571; BAG51392.1; -; mRNA.
DR EMBL; AK297975; BAG60285.1; -; mRNA.
DR EMBL; DB126967; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL137682; CAB70873.2; -; mRNA.
DR EMBL; DQ314882; ABC40741.1; -; Genomic_DNA.
DR EMBL; AC105024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60791.1; -; Genomic_DNA.
DR EMBL; BC007450; AAH07450.1; -; mRNA.
DR EMBL; BC063498; AAH63498.1; -; mRNA.
DR PIR; T46440; T46440.
DR RefSeq; NP_001001349.1; NM_001001349.2.
DR RefSeq; NP_001138399.1; NM_001144927.1.
DR RefSeq; NP_001138400.1; NM_001144928.1.
DR RefSeq; NP_001138401.1; NM_001144929.1.
DR RefSeq; NP_060065.2; NM_017595.5.
DR RefSeq; XP_005257308.1; XM_005257251.1.
DR RefSeq; XP_005277067.1; XM_005277010.1.
DR UniGene; Hs.632252; -.
DR ProteinModelPortal; Q9NYR9; -.
DR SMR; Q9NYR9; 6-155.
DR IntAct; Q9NYR9; 3.
DR MINT; MINT-6945136; -.
DR STRING; 9606.ENSP00000303580; -.
DR PhosphoSite; Q9NYR9; -.
DR DMDM; 74734716; -.
DR PaxDb; Q9NYR9; -.
DR PRIDE; Q9NYR9; -.
DR DNASU; 28511; -.
DR Ensembl; ENST00000307641; ENSP00000303580; ENSG00000168256.
DR Ensembl; ENST00000393880; ENSP00000377458; ENSG00000168256.
DR Ensembl; ENST00000393881; ENSP00000377459; ENSG00000168256.
DR Ensembl; ENST00000393885; ENSP00000377463; ENSG00000168256.
DR Ensembl; ENST00000449471; ENSP00000401976; ENSG00000168256.
DR Ensembl; ENST00000479407; ENSP00000465633; ENSG00000168256.
DR Ensembl; ENST00000561861; ENSP00000455221; ENSG00000260770.
DR Ensembl; ENST00000562265; ENSP00000457014; ENSG00000260770.
DR Ensembl; ENST00000563653; ENSP00000462262; ENSG00000260770.
DR Ensembl; ENST00000568696; ENSP00000456949; ENSG00000260770.
DR Ensembl; ENST00000569942; ENSP00000457286; ENSG00000260770.
DR Ensembl; ENST00000570113; ENSP00000458054; ENSG00000260770.
DR GeneID; 28511; -.
DR KEGG; hsa:28511; -.
DR UCSC; uc002hyq.3; human.
DR CTD; 28511; -.
DR GeneCards; GC17P040170; -.
DR HGNC; HGNC:17898; NKIRAS2.
DR MIM; 604497; gene.
DR neXtProt; NX_Q9NYR9; -.
DR PharmGKB; PA134968907; -.
DR eggNOG; NOG302793; -.
DR HOGENOM; HOG000230991; -.
DR HOVERGEN; HBG105089; -.
DR KO; K17197; -.
DR PhylomeDB; Q9NYR9; -.
DR ChiTaRS; NKIRAS2; human.
DR GeneWiki; NKIRAS2; -.
DR GenomeRNAi; 28511; -.
DR NextBio; 50970; -.
DR PRO; PR:Q9NYR9; -.
DR ArrayExpress; Q9NYR9; -.
DR Bgee; Q9NYR9; -.
DR CleanEx; HS_NKIRAS2; -.
DR Genevestigator; Q9NYR9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; NAS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; GTP-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1 191 NF-kappa-B inhibitor-interacting Ras-like
FT protein 2.
FT /FTId=PRO_0000225679.
FT NP_BIND 11 18 GTP (By similarity).
FT NP_BIND 61 65 GTP (By similarity).
FT NP_BIND 120 123 GTP (By similarity).
FT REGION 1 191 Small GTPase-like.
FT MOTIF 35 43 Effector region.
FT VAR_SEQ 33 34 Missing (in isoform 2).
FT /FTId=VSP_017412.
FT VAR_SEQ 57 112 Missing (in isoform 3).
FT /FTId=VSP_043151.
FT VAR_SEQ 57 97 VRFYDTRGLRDGAELPRHCFSCTDGYVLVYSTDSRESFQRV
FT -> IAESLFSVWSCSRRRLTNPRTRRRSPSWSLATSVTYRS
FT SGV (in isoform 4).
FT /FTId=VSP_044873.
FT VAR_SEQ 98 191 Missing (in isoform 4).
FT /FTId=VSP_044874.
SQ SEQUENCE 191 AA; 21508 MW; 27429230DA563342 CRC64;
MGKSCKVVVC GQASVGKTSI LEQLLYGNHV VGSEMIETQE DIYVGSIETD RGVREQVRFY
DTRGLRDGAE LPRHCFSCTD GYVLVYSTDS RESFQRVELL KKEIDKSKDK KEVTIVVLGN
KCDLQEQRRV DPDVAQHWAK SEKVKLWEVS VADRRSLLEP FVYLASKMTQ PQSKSAFPLS
RKNKGSGSLD G
//
ID KBRS2_HUMAN Reviewed; 191 AA.
AC Q9NYR9; A6NCZ5; B3KNN0; B4DNM3; Q6PK52; Q96KC7; Q9NSX1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-OCT-2000, sequence version 1.
DT 22-JAN-2014, entry version 108.
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; Synonyms=KBRAS2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP INTERACTION WITH NFKBIA AND NFKBIB.
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.,
RA Ghosh S.;
RT "A subclass of Ras proteins that regulate the degradation of
RT IkappaB.";
RL Science 287:869-873(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Embryo, and Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NHLBI resequencing and genotyping service (RS&G;);
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Atypical Ras-like protein that acts as a potent
CC regulator of NF-kappa-B activity by preventing the degradation of
CC NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why
CC NFKBIB is more resistant to degradation. May act by blocking
CC phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-
CC kappa-B subunit. It is unclear whether it acts as a GTPase. Both
CC GTP- and GDP-bound forms block phosphorylation of NFKBIB (By
CC similarity).
CC -!- SUBUNIT: Interacts with both NF-kappa-B inhibitor alpha (NFKBIA)
CC and beta (NFKBIB) in vitro. However, it probably only interacts
CC with NFKBIB in vivo.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9NYR9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NYR9-2; Sequence=VSP_017412;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9NYR9-3; Sequence=VSP_043151;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q9NYR9-4; Sequence=VSP_044873, VSP_044874;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DOMAIN: In contrast to other members of the Ras family, the
CC members of the KappaB-Ras subfamily do not contain the conserved
CC Gly and Gln residues in positions 13 and 65, which are replaced by
CC Ala and Leu residues, respectively, and are therefore similar to
CC the constitutively active forms of oncogenic forms of Ras. This
CC suggests that members of this family are clearly different from
CC other small GTPases proteins.
CC -!- SIMILARITY: Belongs to the small GTPase superfamily. Ras family.
CC KappaB-Ras subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB55006.1; Type=Miscellaneous discrepancy; Note=Absence of residues from position 133 within an exon that change the frame which is not the result of an alternative splicing;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; AF229840; AAF34999.1; -; mRNA.
DR EMBL; AK027265; BAB55006.1; ALT_SEQ; mRNA.
DR EMBL; AK054571; BAG51392.1; -; mRNA.
DR EMBL; AK297975; BAG60285.1; -; mRNA.
DR EMBL; DB126967; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AL137682; CAB70873.2; -; mRNA.
DR EMBL; DQ314882; ABC40741.1; -; Genomic_DNA.
DR EMBL; AC105024; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60791.1; -; Genomic_DNA.
DR EMBL; BC007450; AAH07450.1; -; mRNA.
DR EMBL; BC063498; AAH63498.1; -; mRNA.
DR PIR; T46440; T46440.
DR RefSeq; NP_001001349.1; NM_001001349.2.
DR RefSeq; NP_001138399.1; NM_001144927.1.
DR RefSeq; NP_001138400.1; NM_001144928.1.
DR RefSeq; NP_001138401.1; NM_001144929.1.
DR RefSeq; NP_060065.2; NM_017595.5.
DR RefSeq; XP_005257308.1; XM_005257251.1.
DR RefSeq; XP_005277067.1; XM_005277010.1.
DR UniGene; Hs.632252; -.
DR ProteinModelPortal; Q9NYR9; -.
DR SMR; Q9NYR9; 6-155.
DR IntAct; Q9NYR9; 3.
DR MINT; MINT-6945136; -.
DR STRING; 9606.ENSP00000303580; -.
DR PhosphoSite; Q9NYR9; -.
DR DMDM; 74734716; -.
DR PaxDb; Q9NYR9; -.
DR PRIDE; Q9NYR9; -.
DR DNASU; 28511; -.
DR Ensembl; ENST00000307641; ENSP00000303580; ENSG00000168256.
DR Ensembl; ENST00000393880; ENSP00000377458; ENSG00000168256.
DR Ensembl; ENST00000393881; ENSP00000377459; ENSG00000168256.
DR Ensembl; ENST00000393885; ENSP00000377463; ENSG00000168256.
DR Ensembl; ENST00000449471; ENSP00000401976; ENSG00000168256.
DR Ensembl; ENST00000479407; ENSP00000465633; ENSG00000168256.
DR Ensembl; ENST00000561861; ENSP00000455221; ENSG00000260770.
DR Ensembl; ENST00000562265; ENSP00000457014; ENSG00000260770.
DR Ensembl; ENST00000563653; ENSP00000462262; ENSG00000260770.
DR Ensembl; ENST00000568696; ENSP00000456949; ENSG00000260770.
DR Ensembl; ENST00000569942; ENSP00000457286; ENSG00000260770.
DR Ensembl; ENST00000570113; ENSP00000458054; ENSG00000260770.
DR GeneID; 28511; -.
DR KEGG; hsa:28511; -.
DR UCSC; uc002hyq.3; human.
DR CTD; 28511; -.
DR GeneCards; GC17P040170; -.
DR HGNC; HGNC:17898; NKIRAS2.
DR MIM; 604497; gene.
DR neXtProt; NX_Q9NYR9; -.
DR PharmGKB; PA134968907; -.
DR eggNOG; NOG302793; -.
DR HOGENOM; HOG000230991; -.
DR HOVERGEN; HBG105089; -.
DR KO; K17197; -.
DR PhylomeDB; Q9NYR9; -.
DR ChiTaRS; NKIRAS2; human.
DR GeneWiki; NKIRAS2; -.
DR GenomeRNAi; 28511; -.
DR NextBio; 50970; -.
DR PRO; PR:Q9NYR9; -.
DR ArrayExpress; Q9NYR9; -.
DR Bgee; Q9NYR9; -.
DR CleanEx; HS_NKIRAS2; -.
DR Genevestigator; Q9NYR9; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; NAS:UniProtKB.
DR GO; GO:0007249; P:I-kappaB kinase/NF-kappaB cascade; NAS:UniProtKB.
DR GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005225; Small_GTP-bd_dom.
DR InterPro; IPR001806; Small_GTPase.
DR InterPro; IPR020849; Small_GTPase_Ras.
DR PANTHER; PTHR24070; PTHR24070; 1.
DR Pfam; PF00071; Ras; 1.
DR PRINTS; PR00449; RASTRNSFRMNG.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51419; RAB; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm; GTP-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1 191 NF-kappa-B inhibitor-interacting Ras-like
FT protein 2.
FT /FTId=PRO_0000225679.
FT NP_BIND 11 18 GTP (By similarity).
FT NP_BIND 61 65 GTP (By similarity).
FT NP_BIND 120 123 GTP (By similarity).
FT REGION 1 191 Small GTPase-like.
FT MOTIF 35 43 Effector region.
FT VAR_SEQ 33 34 Missing (in isoform 2).
FT /FTId=VSP_017412.
FT VAR_SEQ 57 112 Missing (in isoform 3).
FT /FTId=VSP_043151.
FT VAR_SEQ 57 97 VRFYDTRGLRDGAELPRHCFSCTDGYVLVYSTDSRESFQRV
FT -> IAESLFSVWSCSRRRLTNPRTRRRSPSWSLATSVTYRS
FT SGV (in isoform 4).
FT /FTId=VSP_044873.
FT VAR_SEQ 98 191 Missing (in isoform 4).
FT /FTId=VSP_044874.
SQ SEQUENCE 191 AA; 21508 MW; 27429230DA563342 CRC64;
MGKSCKVVVC GQASVGKTSI LEQLLYGNHV VGSEMIETQE DIYVGSIETD RGVREQVRFY
DTRGLRDGAE LPRHCFSCTD GYVLVYSTDS RESFQRVELL KKEIDKSKDK KEVTIVVLGN
KCDLQEQRRV DPDVAQHWAK SEKVKLWEVS VADRRSLLEP FVYLASKMTQ PQSKSAFPLS
RKNKGSGSLD G
//
MIM
604497
*RECORD*
*FIELD* NO
604497
*FIELD* TI
*604497 NFKB INHIBITOR-INTERACTING RAS-LIKE PROTEIN 2; NKIRAS2
;;I-KAPPA-B-INTERACTING RAS-LIKE PROTEIN 2;;
read moreKAPPA-B-RAS2;;
KBRAS2
*FIELD* TX
CLONING
Using a yeast 2-hybrid interaction screen with I-kappa-B proteins as
bait to identify interacting molecules, Fenwick et al. (2000) identified
NKIRAS1 (604496) and then screened expressed sequence tag (EST)
databases and identified a related protein, NKIRAS2, which they named
kappa-B-Ras2. The 191-amino acid NKIRAS2 protein has 71% identity to
NKIRAS1. In vitro translation revealed a protein of about 22 kD. NKIRAS2
is widely expressed and is encoded by a 2.5-kb mRNA.
GENE FUNCTION
Fenwick et al. (2000) showed that NKIRAS2 interacts with the PEST domain
of I-kappa-B-alpha (164008) and I-kappa-B-beta (604495) and decreases
their rate of degradation. In cells, kappa-B-Ras proteins are associated
only with the NF-kappa-B (see 164011):I-kappa-B-beta complexes; Fenwick
et al. (2000) suggested that therefore this may provide an explanation
for the slower rate of degradation of I-kappa-B-beta compared with
I-kappa-B-alpha.
*FIELD* RF
1. Fenwick, C.; Na, S.-Y.; Voll, R. E.; Zhong, H.; Im, S.-Y.; Lee,
J. W.; Ghosh, S.: A subclass of Ras proteins that regulate the degradation
of I-kappa-B. Science 287: 869-873, 2000.
*FIELD* CD
Ada Hamosh: 2/3/2000
*FIELD* ED
wwang: 11/24/2010
alopez: 2/10/2000
alopez: 2/4/2000
alopez: 2/3/2000
*RECORD*
*FIELD* NO
604497
*FIELD* TI
*604497 NFKB INHIBITOR-INTERACTING RAS-LIKE PROTEIN 2; NKIRAS2
;;I-KAPPA-B-INTERACTING RAS-LIKE PROTEIN 2;;
read moreKAPPA-B-RAS2;;
KBRAS2
*FIELD* TX
CLONING
Using a yeast 2-hybrid interaction screen with I-kappa-B proteins as
bait to identify interacting molecules, Fenwick et al. (2000) identified
NKIRAS1 (604496) and then screened expressed sequence tag (EST)
databases and identified a related protein, NKIRAS2, which they named
kappa-B-Ras2. The 191-amino acid NKIRAS2 protein has 71% identity to
NKIRAS1. In vitro translation revealed a protein of about 22 kD. NKIRAS2
is widely expressed and is encoded by a 2.5-kb mRNA.
GENE FUNCTION
Fenwick et al. (2000) showed that NKIRAS2 interacts with the PEST domain
of I-kappa-B-alpha (164008) and I-kappa-B-beta (604495) and decreases
their rate of degradation. In cells, kappa-B-Ras proteins are associated
only with the NF-kappa-B (see 164011):I-kappa-B-beta complexes; Fenwick
et al. (2000) suggested that therefore this may provide an explanation
for the slower rate of degradation of I-kappa-B-beta compared with
I-kappa-B-alpha.
*FIELD* RF
1. Fenwick, C.; Na, S.-Y.; Voll, R. E.; Zhong, H.; Im, S.-Y.; Lee,
J. W.; Ghosh, S.: A subclass of Ras proteins that regulate the degradation
of I-kappa-B. Science 287: 869-873, 2000.
*FIELD* CD
Ada Hamosh: 2/3/2000
*FIELD* ED
wwang: 11/24/2010
alopez: 2/10/2000
alopez: 2/4/2000
alopez: 2/3/2000