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Q9CR56 (KBRS2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 109. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length191 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript 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 By similarity.

Subcellular location

Cytoplasm By similarity.

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.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandGTP-binding
Nucleotide-binding
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from electronic annotation. Source: InterPro

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

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 191191NF-kappa-B inhibitor-interacting Ras-like protein 2
PRO_0000225680

Regions

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

Experimental info

Sequence conflict571V → E in BAC35078. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9CR56 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 1E429230C348C823

FASTA19121,494
        10         20         30         40         50         60 
MGKSCKVVVC GQASVGKTSI LEQLLYGNHV VGSEMIETQE DIYVGSIETD RGVREQVRFY 

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

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

       190 
RKNKGSGSLD G 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone marrow, Kidney and Testis.
[2]"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].
Strain: FVB/N and FVB/N-3.
Tissue: Colon and Mammary tumor.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK010371 mRNA. Translation: BAB26889.1.
AK015918 mRNA. Translation: BAB30030.1.
AK052645 mRNA. Translation: BAC35078.1.
AK083475 mRNA. Translation: BAC38929.1.
AK149696 mRNA. Translation: BAE29033.1.
AK169878 mRNA. Translation: BAE41430.1.
BC013469 mRNA. Translation: AAH13469.1.
BC024398 mRNA. Translation: AAH24398.1.
CCDSCCDS25429.1.
RefSeqNP_082300.1. NM_028024.2.
UniGeneMm.274734.
Mm.485819.

3D structure databases

ProteinModelPortalQ9CR56.
SMRQ9CR56. Positions 6-155.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CR56.

Proteomic databases

MaxQBQ9CR56.
PaxDbQ9CR56.
PRIDEQ9CR56.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000017981; ENSMUSP00000017981; ENSMUSG00000017837.
ENSMUST00000051947; ENSMUSP00000059559; ENSMUSG00000017837.
ENSMUST00000107376; ENSMUSP00000102999; ENSMUSG00000017837.
GeneID71966.
KEGGmmu:71966.
UCSCuc007llt.1. mouse.

Organism-specific databases

CTD28511.
MGIMGI:1919216. Nkiras2.

Phylogenomic databases

eggNOGNOG302793.
GeneTreeENSGT00390000006495.
HOGENOMHOG000230991.
HOVERGENHBG105089.
InParanoidQ9CR56.
KOK17197.
OMAIEPFVYL.
OrthoDBEOG70KGQS.
PhylomeDBQ9CR56.
TreeFamTF314483.

Gene expression databases

BgeeQ9CR56.
CleanExMM_NKIRAS2.
GenevestigatorQ9CR56.

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. mouse.
NextBio335068.
PROQ9CR56.
SOURCESearch...

Entry information

Entry nameKBRS2_MOUSE
AccessionPrimary (citable) accession number: Q9CR56
Secondary accession number(s): Q8BWG0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot