Q9NYS0 (KBRS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	NKIRAS1
Synonyms:	KBRAS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	192 AA.
Sequence status	Complete.
Protein existence	Evidence 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

Keywords
Cellular component	Cytoplasm
Ligand	GTP-binding Nucleotide-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	I-kappaB kinase/NF-kappaB cascade Non-traceable author statement Ref.1. Source: UniProtKB small GTPase mediated signal transduction Inferred from electronic annotation. Source: InterPro
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Inferred from electronic annotation. Source: InterPro
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Non-traceable author statement Ref.1. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 192	192	NF-kappa-B inhibitor-interacting Ras-like protein 1		PRO_0000225675
Regions
	Nucleotide binding	11 – 18	8	GTP By similarity
	Nucleotide binding	61 – 65	5	GTP By similarity
	Nucleotide binding	120 – 123	4	GTP By similarity
	Region	58 – 93	36	Interactions with NFKBIA and NFKBIB
	Motif	35 – 43	9	Effector region
Experimental info
	Mutagenesis	38	1	T → A: Loss of function. Ref.6
	Sequence conflict	95	1	Q → R in BAB55341. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9NYS0 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 84948448BE0853B0	FASTA	192	21,643
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00410705.
RefSeq	NP_065078.1. NM_020345.3.
UniGene	Hs.173202.
3D structure databases
ProteinModelPortal	Q9NYS0.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9NYS0. 1 interaction.
STRING	9606.ENSP00000373411.
PTM databases
PhosphoSite	Q9NYS0.
Polymorphism databases
DMDM	74753075.
Proteomic databases
PaxDb	Q9NYS0.
PRIDE	Q9NYS0.
Protocols and materials databases
DNASU	28512.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000388759; ENSP00000373411; ENSG00000197885. ENST00000416026; ENSP00000394214; ENSG00000197885. ENST00000421515; ENSP00000392307; ENSG00000197885. ENST00000425478; ENSP00000400385; ENSG00000197885. ENST00000443659; ENSP00000393785; ENSG00000197885.
GeneID	28512.
KEGG	hsa:28512.
UCSC	uc003ccj.3. human.
Organism-specific databases
CTD	28512.
GeneCards	GC03M023933.
HGNC	HGNC:17899. NKIRAS1.
MIM	604496. gene.
neXtProt	NX_Q9NYS0.
PharmGKB	PA134958823.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG302793.
HOGENOM	HOG000230991.
HOVERGEN	HBG105089.
InParanoid	Q9NYS0.
OMA	QWARGEK.
OrthoDB	EOG4RV2SH.
Gene expression databases
ArrayExpress	Q9NYS0.
Bgee	Q9NYS0.
CleanEx	HS_NKIRAS1.
Genevestigator	Q9NYS0.
GermOnline	ENSG00000197885. Homo sapiens.
Family and domain databases
InterPro	IPR005225. Small_GTP-bd_dom. IPR001806. Small_GTPase. IPR020849. Small_GTPase_Ras. [Graphical view]
PANTHER	PTHR24070. PTHR24070. 1 hit.
Pfam	PF00071. Ras. 1 hit. [Graphical view]
PRINTS	PR00449. RASTRNSFRMNG.
TIGRFAMs	TIGR00231. small_GTP. 1 hit.
PROSITE	PS51419. RAB. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NKIRAS1. human.
GenomeRNAi	28512.
NextBio	50976.
SOURCE	Search...

Entry information

Entry name

KBRS1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.