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Q9NYS0 (KBRS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
NF-kappa-B inhibitor-interacting Ras-like protein 1
Alternative name(s):
I-kappa-B-interacting Ras-like protein 1
Short name=Kappa B-Ras protein 1
Short name=KappaB-Ras1
Gene names
Name:NKIRAS1
Synonyms:KBRAS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length192 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 mediating cytoplasmic retention 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. Ref.1 Ref.5 Ref.6

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. Forms a complex with NFKBIB and NF-kappa-B heterodimer (p50/NFKB1 and p65/RELA). Also interacts with c-Rel (REL). Ref.1 Ref.5 Ref.6

Subcellular location

Cytoplasm Ref.6.

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 Leu residues, 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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 192192NF-kappa-B inhibitor-interacting Ras-like protein 1
PRO_0000225675

Regions

Nucleotide binding11 – 188GTP By similarity
Nucleotide binding61 – 655GTP By similarity
Nucleotide binding120 – 1234GTP By similarity
Region58 – 9336Interactions with NFKBIA and NFKBIB
Motif35 – 439Effector region

Experimental info

Mutagenesis381T → A: Loss of function. Ref.6
Sequence conflict951Q → R in BAB55341. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9NYS0 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 84948448BE0853B0

FASTA19221,643
        10         20         30         40         50         60 
MGKGCKVVVC GLLSVGKTAI LEQLLYGNHT IGMEDCETME DVYMASVETD RGVKEQLHLY 

        70         80         90        100        110        120 
DTRGLQEGVE LPKHYFSFAD GFVLVYSVNN LESFQRVELL KKEIDKFKDK KEVAIVVLGN 

       130        140        150        160        170        180 
KIDLSEQRQV DAEVAQQWAK SEKVRLWEVT VTDRKTLIEP FTLLASKLSQ PQSKSSFPLP 

       190 
GRKNKGNSNS EN 

« Hide

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], FUNCTION, TISSUE SPECIFICITY, GTP-BINDING, 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].
Tissue: Placenta.
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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].
Tissue: Brain and Lung.
[5]"KappaB-Ras binds to the unique insert within the ankyrin repeat domain of IkappaBbeta and regulates cytoplasmic retention of IkappaBbeta.NF-kappaB complexes."
Chen Y., Wu J., Ghosh G.
J. Biol. Chem. 278:23101-23106(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NFKBIB.
[6]"Inhibition of NF-kappaB activity by IkappaBbeta in association with kappaB-Ras."
Chen Y., Vallee S., Wu J., Vu D., Sondek J., Ghosh G.
Mol. Cell. Biol. 24:3048-3056(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH REL, MUTAGENESIS OF THR-38.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF229839 mRNA. Translation: AAF34998.1.
AK027749 mRNA. Translation: BAB55341.1.
DQ314881 Genomic DNA. Translation: ABC40740.1.
BC066940 mRNA. Translation: AAH66940.1.
BC012145 mRNA. Translation: AAH12145.1.
RefSeqNP_065078.1. NM_020345.3.
XP_005265133.1. XM_005265076.1.
XP_005265134.1. XM_005265077.2.
XP_005265135.1. XM_005265078.1.
UniGeneHs.173202.

3D structure databases

ProteinModelPortalQ9NYS0.
SMRQ9NYS0. Positions 6-170.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid118389. 4 interactions.
IntActQ9NYS0. 1 interaction.
STRING9606.ENSP00000373411.

PTM databases

PhosphoSiteQ9NYS0.

Polymorphism databases

DMDM74753075.

Proteomic databases

PaxDbQ9NYS0.
PRIDEQ9NYS0.

Protocols and materials databases

DNASU28512.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000388759; ENSP00000373411; ENSG00000197885.
ENST00000416026; ENSP00000394214; ENSG00000197885.
ENST00000421515; ENSP00000392307; ENSG00000197885.
ENST00000425478; ENSP00000400385; ENSG00000197885.
ENST00000443659; ENSP00000393785; ENSG00000197885.
GeneID28512.
KEGGhsa:28512.
UCSCuc003ccj.3. human.

Organism-specific databases

CTD28512.
GeneCardsGC03M023933.
HGNCHGNC:17899. NKIRAS1.
MIM604496. gene.
neXtProtNX_Q9NYS0.
PharmGKBPA134958823.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG302793.
HOGENOMHOG000230991.
HOVERGENHBG105089.
InParanoidQ9NYS0.
KOK17197.
OMALYGNHTV.
OrthoDBEOG70KGQS.
PhylomeDBQ9NYS0.
TreeFamTF314483.

Enzyme and pathway databases

SignaLinkQ9NYS0.

Gene expression databases

ArrayExpressQ9NYS0.
BgeeQ9NYS0.
CleanExHS_NKIRAS1.
GenevestigatorQ9NYS0.

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

ChiTaRSNKIRAS1. human.
GenomeRNAi28512.
NextBio50976.
PROQ9NYS0.
SOURCESearch...

Entry information

Entry nameKBRS1_HUMAN
AccessionPrimary (citable) accession number: Q9NYS0
Secondary accession number(s): Q96K18
Entry history
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 105 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 3

Human chromosome 3: entries, gene names and cross-references to MIM