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Protein

NF-kappa-B inhibitor-interacting Ras-like protein 1

Gene

NKIRAS1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 188GTPBy similarity
Nucleotide bindingi61 – 655GTPBy similarity
Nucleotide bindingi120 – 1234GTPBy similarity

GO - Molecular functioni

  • GTPase activity Source: UniProtKB
  • GTP binding Source: UniProtKB-KW

GO - Biological processi

  • I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • metabolic process Source: GOC
  • small GTPase mediated signal transduction Source: InterPro
Complete GO annotation...

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

SignaLinkiQ9NYS0.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:NKIRAS1
Synonyms:KBRAS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:17899. NKIRAS1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi38 – 381T → A: Loss of function. 1 Publication

Organism-specific databases

PharmGKBiPA134958823.

Polymorphism and mutation databases

BioMutaiNKIRAS1.
DMDMi74753075.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 192192NF-kappa-B inhibitor-interacting Ras-like protein 1PRO_0000225675Add
BLAST

Proteomic databases

MaxQBiQ9NYS0.
PaxDbiQ9NYS0.
PRIDEiQ9NYS0.

PTM databases

PhosphoSiteiQ9NYS0.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9NYS0.
CleanExiHS_NKIRAS1.
ExpressionAtlasiQ9NYS0. baseline and differential.
GenevisibleiQ9NYS0. HS.

Interactioni

Subunit structurei

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).3 Publications

Protein-protein interaction databases

BioGridi118389. 5 interactions.
IntActiQ9NYS0. 1 interaction.
STRINGi9606.ENSP00000373411.

Structurei

3D structure databases

ProteinModelPortaliQ9NYS0.
SMRiQ9NYS0. Positions 6-170.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni58 – 9336Interactions with NFKBIA and NFKBIBAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi35 – 439Effector region

Domaini

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 similaritiesi

Phylogenomic databases

eggNOGiNOG302793.
GeneTreeiENSGT00390000006495.
HOGENOMiHOG000230991.
HOVERGENiHBG105089.
InParanoidiQ9NYS0.
KOiK17197.
OMAiQWARGEK.
OrthoDBiEOG70KGQS.
PhylomeDBiQ9NYS0.
TreeFamiTF314483.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9NYS0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKGCKVVVC GLLSVGKTAI LEQLLYGNHT IGMEDCETME DVYMASVETD
60 70 80 90 100
RGVKEQLHLY DTRGLQEGVE LPKHYFSFAD GFVLVYSVNN LESFQRVELL
110 120 130 140 150
KKEIDKFKDK KEVAIVVLGN KIDLSEQRQV DAEVAQQWAK SEKVRLWEVT
160 170 180 190
VTDRKTLIEP FTLLASKLSQ PQSKSSFPLP GRKNKGNSNS EN
Length:192
Mass (Da):21,643
Last modified:October 1, 2000 - v1
Checksum:i84948448BE0853B0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti95 – 951Q → R in BAB55341 (PubMed:14702039).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33717.1.
RefSeqiNP_065078.1. NM_020345.3.
XP_005265133.1. XM_005265076.2.
XP_005265134.1. XM_005265077.3.
XP_005265135.1. XM_005265078.2.
UniGeneiHs.173202.

Genome annotation databases

EnsembliENST00000388759; ENSP00000373411; ENSG00000197885.
ENST00000416026; ENSP00000394214; ENSG00000197885.
ENST00000421515; ENSP00000392307; ENSG00000197885.
ENST00000425478; ENSP00000400385; ENSG00000197885.
ENST00000443659; ENSP00000393785; ENSG00000197885.
ENST00000614374; ENSP00000483749; ENSG00000197885.
GeneIDi28512.
KEGGihsa:28512.
UCSCiuc003ccj.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS33717.1.
RefSeqiNP_065078.1. NM_020345.3.
XP_005265133.1. XM_005265076.2.
XP_005265134.1. XM_005265077.3.
XP_005265135.1. XM_005265078.2.
UniGeneiHs.173202.

3D structure databases

ProteinModelPortaliQ9NYS0.
SMRiQ9NYS0. Positions 6-170.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi118389. 5 interactions.
IntActiQ9NYS0. 1 interaction.
STRINGi9606.ENSP00000373411.

PTM databases

PhosphoSiteiQ9NYS0.

Polymorphism and mutation databases

BioMutaiNKIRAS1.
DMDMi74753075.

Proteomic databases

MaxQBiQ9NYS0.
PaxDbiQ9NYS0.
PRIDEiQ9NYS0.

Protocols and materials databases

DNASUi28512.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000388759; ENSP00000373411; ENSG00000197885.
ENST00000416026; ENSP00000394214; ENSG00000197885.
ENST00000421515; ENSP00000392307; ENSG00000197885.
ENST00000425478; ENSP00000400385; ENSG00000197885.
ENST00000443659; ENSP00000393785; ENSG00000197885.
ENST00000614374; ENSP00000483749; ENSG00000197885.
GeneIDi28512.
KEGGihsa:28512.
UCSCiuc003ccj.3. human.

Organism-specific databases

CTDi28512.
GeneCardsiGC03M023933.
HGNCiHGNC:17899. NKIRAS1.
MIMi604496. gene.
neXtProtiNX_Q9NYS0.
PharmGKBiPA134958823.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG302793.
GeneTreeiENSGT00390000006495.
HOGENOMiHOG000230991.
HOVERGENiHBG105089.
InParanoidiQ9NYS0.
KOiK17197.
OMAiQWARGEK.
OrthoDBiEOG70KGQS.
PhylomeDBiQ9NYS0.
TreeFamiTF314483.

Enzyme and pathway databases

SignaLinkiQ9NYS0.

Miscellaneous databases

ChiTaRSiNKIRAS1. human.
GenomeRNAii28512.
NextBioi50976.
PROiQ9NYS0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NYS0.
CleanExiHS_NKIRAS1.
ExpressionAtlasiQ9NYS0. baseline and differential.
GenevisibleiQ9NYS0. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR027417. P-loop_NTPase.
IPR005225. Small_GTP-bd_dom.
IPR001806. Small_GTPase.
IPR020849. Small_GTPase_Ras.
[Graphical view]
PANTHERiPTHR24070. PTHR24070. 1 hit.
PfamiPF00071. Ras. 1 hit.
[Graphical view]
PRINTSiPR00449. RASTRNSFRMNG.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00231. small_GTP. 1 hit.
PROSITEiPS51419. RAB. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiKBRS1_HUMAN
AccessioniPrimary (citable) accession number: Q9NYS0
Secondary accession number(s): Q96K18
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 7, 2006
Last sequence update: October 1, 2000
Last modified: July 22, 2015
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.