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Q9NYR9 (KBRS2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NF-kappa-B inhibitor-interacting Ras-like protein 2
Alternative name(s):
I-kappa-B-interacting Ras-like protein 2
Short name=Kappa B-Ras protein 2
Short name=KappaB-Ras2
Gene names
Name:NKIRAS2
Synonyms:KBRAS2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and nuclear localization of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB By similarity.

Subunit structure

Interacts with both NF-kappa-B inhibitor alpha (NFKBIA) and beta (NFKBIB) in vitro. However, it probably only interacts with NFKBIB in vivo. Ref.1

Subcellular location

Cytoplasm By similarity.

Tissue specificity

Widely expressed. Ref.1

Domain

In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gly and Gln residues in positions 13 and 65, which are replaced by Ala and Leu residues, respectively, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins.

Sequence similarities

Belongs to the small GTPase superfamily. Ras family. KappaB-Ras subfamily.

Sequence caution

The sequence BAB55006.1 differs from that shown. Reason: Absence of residues from position 133 within an exon that change the frame which is not the result of an alternative splicing.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processI-kappaB kinase/NF-kappaB signaling

Non-traceable author statement Ref.1. Source: UniProtKB

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9NYR9-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9NYR9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     33-34: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q9NYR9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     57-112: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9NYR9-4)

The sequence of this isoform differs from the canonical sequence as follows:
     57-97: VRFYDTRGLR...TDSRESFQRV → IAESLFSVWS...TSVTYRSSGV
     98-191: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 191191NF-kappa-B inhibitor-interacting Ras-like protein 2
PRO_0000225679

Regions

Nucleotide binding11 – 188GTP By similarity
Nucleotide binding61 – 655GTP By similarity
Nucleotide binding120 – 1234GTP By similarity
Region1 – 191191Small GTPase-like
Motif35 – 439Effector region

Natural variations

Alternative sequence33 – 342Missing in isoform 2.
VSP_017412
Alternative sequence57 – 11256Missing in isoform 3.
VSP_043151
Alternative sequence57 – 9741VRFYD…SFQRV → IAESLFSVWSCSRRRLTNPR TRRRSPSWSLATSVTYRSSG V in isoform 4.
VSP_044873
Alternative sequence98 – 19194Missing in isoform 4.
VSP_044874

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 27429230DA563342

FASTA19121,508
        10         20         30         40         50         60 
MGKSCKVVVC GQASVGKTSI LEQLLYGNHV VGSEMIETQE DIYVGSIETD RGVREQVRFY 

        70         80         90        100        110        120 
DTRGLRDGAE LPRHCFSCTD GYVLVYSTDS RESFQRVELL KKEIDKSKDK KEVTIVVLGN 

       130        140        150        160        170        180 
KCDLQEQRRV DPDVAQHWAK SEKVKLWEVS VADRRSLLEP FVYLASKMTQ PQSKSAFPLS 

       190 
RKNKGSGSLD G 

« Hide

Isoform 2 [UniParc].

Checksum: 4857EEA02F788F38
Show »

FASTA18921,292
Isoform 3 [UniParc].

Checksum: 8B874EC8C7EF28E4
Show »

FASTA13514,910
Isoform 4 [UniParc].

Checksum: 4049375BE44AF8A5
Show »

FASTA9710,770

References

« Hide 'large scale' references
[1]"A subclass of Ras proteins that regulate the degradation of IkappaB."
Fenwick C., Na S.-Y., Voll R.E., Zhong H., Im S.-Y., Lee J.W., Ghosh S.
Science 287:869-873(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH NFKBIA AND NFKBIB.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
Tissue: Embryo and Thymus.
[3]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Testis.
[4]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain and Muscle.
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF229840 mRNA. Translation: AAF34999.1.
AK027265 mRNA. Translation: BAB55006.1. Sequence problems.
AK054571 mRNA. Translation: BAG51392.1.
AK297975 mRNA. Translation: BAG60285.1.
DB126967 mRNA. No translation available.
AL137682 mRNA. Translation: CAB70873.2.
DQ314882 Genomic DNA. Translation: ABC40741.1.
AC105024 Genomic DNA. No translation available.
CH471152 Genomic DNA. Translation: EAW60791.1.
BC007450 mRNA. Translation: AAH07450.1.
BC063498 mRNA. Translation: AAH63498.1.
PIRT46440.
RefSeqNP_001001349.1. NM_001001349.2.
NP_001138399.1. NM_001144927.1.
NP_001138400.1. NM_001144928.1.
NP_001138401.1. NM_001144929.1.
NP_060065.2. NM_017595.5.
XP_005257308.1. XM_005257251.1.
UniGeneHs.632252.

3D structure databases

ProteinModelPortalQ9NYR9.
SMRQ9NYR9. Positions 6-155.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118388. 4 interactions.
IntActQ9NYR9. 3 interactions.
MINTMINT-6945136.
STRING9606.ENSP00000303580.

PTM databases

PhosphoSiteQ9NYR9.

Polymorphism databases

DMDM74734716.

Proteomic databases

PaxDbQ9NYR9.
PRIDEQ9NYR9.

Protocols and materials databases

DNASU28511.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000307641; ENSP00000303580; ENSG00000168256. [Q9NYR9-1]
ENST00000393880; ENSP00000377458; ENSG00000168256. [Q9NYR9-1]
ENST00000393881; ENSP00000377459; ENSG00000168256. [Q9NYR9-1]
ENST00000393885; ENSP00000377463; ENSG00000168256. [Q9NYR9-1]
ENST00000449471; ENSP00000401976; ENSG00000168256. [Q9NYR9-3]
ENST00000479407; ENSP00000465633; ENSG00000168256. [Q9NYR9-4]
ENST00000561861; ENSP00000455221; ENSG00000260770. [Q9NYR9-1]
ENST00000562265; ENSP00000457014; ENSG00000260770. [Q9NYR9-1]
ENST00000563653; ENSP00000462262; ENSG00000260770. [Q9NYR9-4]
ENST00000568696; ENSP00000456949; ENSG00000260770. [Q9NYR9-1]
ENST00000569942; ENSP00000457286; ENSG00000260770. [Q9NYR9-1]
ENST00000570113; ENSP00000458054; ENSG00000260770. [Q9NYR9-3]
GeneID28511.
KEGGhsa:28511.
UCSCuc002hyq.3. human. [Q9NYR9-1]
uc010wge.2. human. [Q9NYR9-3]

Organism-specific databases

CTD28511.
GeneCardsGC17P040170.
HGNCHGNC:17898. NKIRAS2.
MIM604497. gene.
neXtProtNX_Q9NYR9.
PharmGKBPA134968907.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302793.
HOGENOMHOG000230991.
HOVERGENHBG105089.
KOK17197.
PhylomeDBQ9NYR9.
TreeFamTF314483.

Gene expression databases

ArrayExpressQ9NYR9.
BgeeQ9NYR9.
CleanExHS_NKIRAS2.
GenevestigatorQ9NYR9.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERPTHR24070. PTHR24070. 1 hit.
PfamPF00071. Ras. 1 hit.
[Graphical view]
PRINTSPR00449. RASTRNSFRMNG.
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00231. small_GTP. 1 hit.
PROSITEPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNKIRAS2. human.
GeneWikiNKIRAS2.
GenomeRNAi28511.
NextBio50970.
PROQ9NYR9.
SOURCESearch...

Entry information

Entry nameKBRS2_HUMAN
AccessionPrimary (citable) accession number: Q9NYR9
Secondary accession number(s): A6NCZ5 expand/collapse secondary AC list , B3KNN0, B4DNM3, Q6PK52, Q96KC7, Q9NSX1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM