Reviewed, UniProtKB/Swiss-Prot Q60778 (IKBB_MOUSE)

Names and origin

Protein names

Recommended name:
    NF-kappa-B inhibitor beta
      Short name=NF-kappa-BIB
Alternative name(s):
    I-kappa-B-beta
      Short name=IkappaBbeta
      Short name=IkB-beta
      Short name=IkB-B

Gene names

Name:	Nfkbib
Synonyms:	Ikbb

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

Protein attributes

Sequence length	359 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. However, the unphosphorylated form resynthesized after cell stimulation is able to bind NF-kappa-B allowing its transport to the nucleus and protecting it to further IKBA-dependent inactivation. Association with inhibitor kappa B-interacting NKIRAS1 and NKIRAS2 prevent its phosphorylation rendering it more resistant to degradation, explaining its slower degradation.
Subunit structure	Interacts with COMMD1 and inhibitor kappa B-interacting Ras-like NKIRAS1 and NKIRAS2 By similarity. Interacts with the ligand-binding domain of THRB. Interacts with RELA and REL. Ref.3
Subcellular location	Cytoplasm. Nucleus.
Tissue specificity	Highly expressed in testis followed by spleen.
Post-translational modification	Phosphorylated; followed by degradation. Interaction with NKIRAS1 and NKIRAS2 probably prevents phosphorylation.
Sequence similarities	Belongs to the NF-kappa-B inhibitor family. Contains 6 ANK repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Domain	ANK repeat Repeat
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 359

359

NF-kappa-B inhibitor beta

PRO_0000067005

Regions

Repeat

57 – 86

30

ANK 1

Repeat

93 – 122

30

ANK 2

Repeat

126 – 155

30

ANK 3

Repeat

206 – 235

30

ANK 4

Repeat

240 – 269

30

ANK 5

Repeat

273 – 302

30

ANK 6

Amino acid modifications

Modified residue

19

1

Phosphoserine By similarity

Modified residue

23

1

Phosphoserine By similarity

Experimental info

Sequence conflict

84

1

H → T in BAB26774. Ref.2

Secondary structure

1

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359

Helix Strand Turn

Details...

Helix

61 – 67

7

Helix

71 – 81

11

Helix

85 – 88

4

Helix

97 – 104

8

Helix

107 – 115

9

Helix

130 – 134

5

Turn

135 – 138

4

Helix

140 – 146

7

Beta strand

147 – 149

3

Helix

196 – 199

4

Helix

210 – 216

7

Helix

220 – 229

10

Turn

238 – 240

3

Helix

244 – 250

7

Helix

254 – 262

9

Helix

277 – 282

6

Helix

287 – 295

9

Helix

305 – 307

3

Sequences

	Sequence		Length	Mass (Da)
	Q60778-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: BAE306CDDA7044E6	FASTA	359	38,001
	10 20 30 40 50 60 MAGVACLGKT ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPELSWAPLV FGYVTEDGDT 70 80 90 100 110 120 ALHLAVIHQH EPFLDFLLGF SAGHEYLDLQ NDLGQTALHL AAILGEASTV EKLYAAGAGV 130 140 150 160 170 180 LVAERGGHTA LHLACRVRAH TCACVLLQPR PSHPRDASDT YLTQSQDCTP DTSHAPAAVD 190 200 210 220 230 240 SQPNPENEEE PRDEDWRLQL EAENYDGHTP LHVAVIHKDA EMVRLLRDAG ADLNKPEPTC 250 260 270 280 290 300 GRTPLHLAVE AQAASVLELL LKAGADPTAR MYGGRTPLGS ALLRPNPILA RLLRAHGAPE 310 320 330 340 350 PEDEDDKLSP CSSSGSDSDS DNRDEGDEYD DIVVHSGRSQ NRQPPSPASK PLPDDPNPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"IkappaB-beta regulates the persistent response in a biphasic activation of NF-kappaB." Thompson J.E., Phillips R.J., Erdjument-Bromage H., Tempst P., Ghosh S. Cell 80:573-582(1995) [PubMed: 7867065] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: B-cell.
[2]	"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. , 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: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Tongue.
[3]	"Role of unphosphorylated, newly synthesized IkappaB beta in persistent activation of NF-kappaB." Suyang H., Phillips R.J., Douglas I., Ghosh S. Mol. Cell. Biol. 16:5444-5449(1996) [PubMed: 8816457] [Abstract] Cited for: CHARACTERIZATION, INTERACTION WITH RELA AND REL.
[4]	"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: 10657303] [Abstract] Cited for: KAPPA B RAS-BINDING.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U19799 mRNA. Translation: AAC52166.1.
AK010218 mRNA. Translation: BAB26774.1.

IPI

IPI00310330.

RefSeq

NP_035038.2.

UniGene

Mm.220333

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1K3Z	X-ray	2.50	D	50-331	[»]
1OY3	X-ray	2.05	D	50-331	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q60778. 1 interaction.

STRING

Q60778.

PTM databases

PhosphoSite

Q60778.

Proteomic databases

PRIDE

Q60778.

Genome annotation databases

Ensembl

ENSMUST00000032815; ENSMUSP00000032815; ENSMUSG00000030595; Mus musculus. [Genome view]
ENSMUST00000085851; ENSMUSP00000083012; ENSMUSG00000030595; Mus musculus. [Genome view]

GeneID

18036.

KEGG

mmu:18036.

Organism-specific databases

CTD

18036.

MGI

MGI:104752. Nfkbib.

Phylogenomic databases

HOVERGEN

Q60778.

InParanoid

Q60778.

Gene expression databases

ArrayExpress

Q60778.

Bgee

Q60778.

Genevestigator

Q60778.

GermOnline

ENSMUSG00000030595. Mus musculus.

Family and domain databases

InterPro

IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR015681. NF_kB_inhbitor.
[Graphical view]

Gene3D

G3DSA:1.25.40.20. ANK. 1 hit.

PANTHER

PTHR18958:SF236. NF_kB_inhbitor. 1 hit.

Pfam

PF00023. Ank. 2 hits.
[Graphical view]

SMART

SM00248. ANK. 6 hits.
[Graphical view]

PROSITE

PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

SOURCE

Search...

Entry information

Entry name

IKBB_MOUSE

Accession

Primary (citable) accession number: Q60778
Secondary accession number(s): Q9D6L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	November 1, 1996
Last modified:	January 19, 2010
This is version 84 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)