Q60778 (IKBB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

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=IkB-B
Short name=IkB-beta
Short name=IkappaBbeta

Gene names

Name:	Nfkbib
Synonyms:	Ikbb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › 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 NFKBIA-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.4
Subcellular location	Cytoplasm. Nucleus.
Tissue specificity	Highly expressed in testis followed by spleen.
Post-translational modification	Phosphorylated by RPS6KA1; 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 Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Rela	Q04207	8	EBI-644469,EBI-644400

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 RPS6KA1 By similarity

Modified residue

23

1

Phosphoserine; by RPS6KA1 By similarity

Modified residue

313

1

Phosphoserine By similarity

Modified residue

318

1

Phosphoserine By similarity

Experimental info

Sequence conflict

84

1

T → H in AAC52166. Ref.1

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

304 – 307

4

Sequences

	Sequence		Length	Mass (Da)
	Q60778 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: 0E2B46C89E2404EF	FASTA	359	37,965
	10 20 30 40 50 60 MAGVACLGKT ADADEWCDSG LGSLGPDAAA PGGPGLGAEL GPELSWAPLV FGYVTEDGDT 70 80 90 100 110 120 ALHLAVIHQH EPFLDFLLGF SAGTEYLDLQ 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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD. Tissue: Hypothalamus, Spleen and Tongue.
[3]	Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION, INTERACTION WITH RELA AND REL.
[5]	"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: 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.
AK038631 mRNA. Translation: BAC30071.1.
AK156731 mRNA. Translation: BAE33825.1.
CH466593 Genomic DNA. Translation: EDL24117.1.
CH466593 Genomic DNA. Translation: EDL24118.1.

IPI

IPI00310330.

RefSeq

NP_035038.2. NM_010908.4.

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	[»]

ProteinModelPortal

Q60778.

SMR

Q60778. Positions 5-303.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-37418N.

IntAct

Q60778. 1 interaction.

PTM databases

PhosphoSite

Q60778.

Proteomic databases

PaxDb

Q60778.

PRIDE

Q60778.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000032815; ENSMUSP00000032815; ENSMUSG00000030595.
ENSMUST00000085851; ENSMUSP00000083012; ENSMUSG00000030595.

GeneID

18036.

KEGG

mmu:18036.

Organism-specific databases

CTD

4793.

MGI

MGI:104752. Nfkbib.

Phylogenomic databases

eggNOG

COG0666.

GeneTree

ENSGT00550000074527.

HOGENOM

HOG000137336.

HOVERGEN

HBG019039.

InParanoid

Q564F1.

KO

K02581.

OMA

DEWCDSG.

OrthoDB

EOG4229KF.

Gene expression databases

ArrayExpress

Q60778.

Bgee

Q60778.

Genevestigator

Q60778.

GermOnline

ENSMUSG00000030595. Mus musculus.

Family and domain databases

Gene3D

1.25.40.20. 2 hits.

InterPro

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

Pfam

PF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
[Graphical view]

PRINTS

PR01415. ANKYRIN.

SMART

SM00248. ANK. 6 hits.
[Graphical view]

SUPFAM

SSF48403. ANK. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

Q60778.

NextBio

293133.

SOURCE

Search...

Entry information

Entry name

IKBB_MOUSE

Accession

Primary (citable) accession number: Q60778
Secondary accession number(s): Q564F1, Q9D6L5

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program