Q04863 (RELB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor RelB

Gene names

Name:

Relb

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	558 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric RelB-p50 and RelB-p52 complexes are transcriptional activators. RELB neither associates with DNA nor with RELA/p65 or REL. Stimulates promoter activity in the presence of NFKB2/p49 By similarity. As a member of the NUPR1/RELB/IER3 survival pathway, may allow the development of pancreatic intraepithelial neoplasias. Ref.9
Subunit structure	Component of the NF-kappa-B RelB-p50 complex. Component of the NF-kappa-B RelB-p52 complex By similarity. Self-associates; the interaction seems to be transient and may prevent degradation allowing for heterodimer formation p50 or p52. Interacts with NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with NFKBID. Ref.7 Ref.8
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome By similarity. Note: Co-localizes with NEK6 in the centrosome By similarity.
Tissue specificity	Expressed in intestine, thymus and spleen. Undetectable in liver, bome marrow, kidney and testis.
Domain	Both N- and C-terminal domains are required for transcriptional activation.
Post-translational modification	Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation.
Sequence similarities	Contains 1 RHD (Rel-like) domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Cytoskeleton Nucleus
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T-helper 1 cell differentiation Inferred from mutant phenotype PubMed 16081776. Source: MGI antigen processing and presentation Inferred from mutant phenotype Ref.5. Source: MGI myeloid dendritic cell differentiation Inferred from mutant phenotype PubMed 14499111Ref.5. Source: MGI positive regulation of gene expression Inferred from mutant phenotype PubMed 10925280. Source: MGI transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from direct assay Ref.7. Source: MGI microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from direct assay Ref.7PubMed 21874024. Source: MGI
Molecular_function	DNA binding Inferred from direct assay PubMed 15944286. Source: MGI sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 558

558

Transcription factor RelB

PRO_0000205174

Regions

Domain

103 – 418

316

RHD

Region

22 – 50

29

Leucine-zipper

Motif

387 – 391

5

Nuclear localization signal Potential

Motif

411 – 416

6

Nuclear localization signal Potential

Amino acid modifications

Modified residue

19

1

Phosphoserine By similarity

Modified residue

84

1

Phosphothreonine Ref.6

Modified residue

552

1

Phosphoserine Ref.6

Experimental info

Mutagenesis

368

1

S → A or E: Strongly reduces transcriptional activity and interaction with NFKB1/p50 and NFKB2/p52. Ref.8

Sequence conflict

51

1

D → V in AAA40041. Ref.1

Sequence conflict

142

1

L → Q in AAA40041. Ref.1

Secondary structure

1

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558

Helix Strand Turn

Details...

Beta strand

95 – 97

3

Beta strand

104 – 109

6

Beta strand

113 – 116

4

Helix

121 – 123

3

Beta strand

132 – 134

3

Beta strand

137 – 139

3

Beta strand

145 – 149

5

Beta strand

156 – 160

5

Beta strand

165 – 168

4

Beta strand

173 – 178

6

Beta strand

182 – 184

3

Beta strand

186 – 190

5

Turn

192 – 194

3

Beta strand

197 – 199

3

Beta strand

204 – 207

4

Turn

210 – 212

3

Helix

213 – 222

10

Beta strand

234 – 236

3

Beta strand

241 – 245

5

Beta strand

250 – 252

3

Beta strand

255 – 257

3

Beta strand

270 – 274

5

Helix

276 – 278

3

Beta strand

279 – 281

3

Beta strand

283 – 287

5

Beta strand

289 – 292

4

Beta strand

297 – 299

3

Beta strand

301 – 304

4

Helix

308 – 310

3

Beta strand

314 – 317

4

Beta strand

320 – 323

4

Helix

328 – 330

3

Helix

332 – 334

3

Beta strand

335 – 340

6

Beta strand

353 – 357

5

Turn

362 – 364

3

Beta strand

371 – 375

5

Sequences

	Sequence		Length	Mass (Da)
	Q04863 [UniParc]. Last modified July 27, 2011. Version 2. Checksum: AA49781A891ED7B8	FASTA	558	60,305
	10 20 30 40 50 60 MPSRRAARES APELGALGSS DLSSLSLTVS RTTDELEIID EYIKENGFGL DGTQLSEMPR 70 80 90 100 110 120 LVPRGPASLS SVTLGPAAPP PPATPSWSCT LGRLVSPGPC PRPYLVITEQ PKQRGMRFRY 130 140 150 160 170 180 ECEGRSAGSI LGESSTEASK TLPAIELRDC GGLREVEVTA CLVWKDWPHR VHPHSLVGKD 190 200 210 220 230 240 CTDGVCRVRL RPHVSPRHSF NNLGIQCVRK KEIEAAIERK IQLGIDPYNA GSLKNHQEVD 250 260 270 280 290 300 MNVVRICFQA SYRDQQGHLH RMDPILSEPV YDKKSTNTSE LRICRINKES GPCTGGEELY 310 320 330 340 350 360 LLCDKVQKED ISVVFSTASW EGRADFSQAD VHRQIAIVFK TPPYEDLEIS EPVTVNVFLQ 370 380 390 400 410 420 RLTDGVCSEP LPFTYLPRDH DSYGVDKKRK RGLPDVLGEL SSSDPHGIES KRRKKKPVFL 430 440 450 460 470 480 DHFLPGHSSG LFLPPSALQP ADSDFFPASI SLPGLEPPGG PDLLDDGFAY DPSAPTLFTM 490 500 510 520 530 540 LDLLPPAPPL ASAVVGSGGA GATVVESSGP EPLSLDSFAA PGPGDVGTAS LVGSNMFPNQ 550 YREAAFGGGL LSPGPEAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RelB, a new Rel family transcription activator that can interact with p50-NF-kappa B." Ryseck R.P., Bull P., Takamiya M., Bours V., Siebenlist U., Dobrzanski P., Bravo R. Mol. Cell. Biol. 12:674-684(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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. Tissue: Kidney.
[3]	"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]. Strain: FVB/N. Tissue: Mammary tumor.
[4]	"Both N- and C-terminal domains of RelB are required for full transactivation: role of the N-terminal leucine zipper-like motif." Dobrzanski P., Ryseck R.P., Bravo R. Mol. Cell. Biol. 13:1572-1582(1993) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-116.
[5]	"Expression of relB is required for the development of thymic medulla and dendritic cells." Burkly L., Hession C., Ogata L., Reilly C., Marconi L.A., Olson D., Tizard R., Cate R., Lo D. Nature 373:531-536(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 309-429. Strain: C57BL/6. Tissue: Liver.
[6]	"Signal-specific and phosphorylation-dependent RelB degradation: a potential mechanism of NF-kappaB control." Marienfeld R., Berberich-Siebelt F., Berberich I., Denk A., Serfling E., Neumann M. Oncogene 20:8142-8147(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-84 AND SER-552.
[7]	"Peptide-induced negative selection of thymocytes activates transcription of an NF-kappa B inhibitor." Fiorini E., Schmitz I., Marissen W.E., Osborn S.L., Touma M., Sasada T., Reche P.A., Tibaldi E.V., Hussey R.E., Kruisbeek A.M., Reinherz E.L., Clayton L.K. Mol. Cell 9:637-648(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NFKBID.
[8]	"Critical role of RelB serine 368 for dimerization and p100 stabilization." Maier H.J., Marienfeld R., Wirth T., Baumann B. J. Biol. Chem. 278:39242-39250(2003) [PubMed] [Europe PMC] [Abstract] Cited for: SELF-ASSOCIATION, INTERACTION WITH NFKB1 AND NFKB2, MUTAGENESIS OF SER-368.
[9]	"Nuclear protein 1 promotes pancreatic cancer development and protects cells from stress by inhibiting apoptosis." Hamidi T., Algul H., Cano C.E., Sandi M.J., Molejon M.I., Riemann M., Calvo E.L., Lomberk G., Dagorn J.C., Weih F., Urrutia R., Schmid R.M., Iovanna J.L. J. Clin. Invest. 122:2092-2103(2012) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[10]	"NF-kappaB RelB forms an intertwined homodimer." Huang D.B., Vu D., Ghosh G. Structure 13:1365-1373(2005) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 277-378.
[11]	"X-ray structure of a NF-kappaB p50/RelB/DNA complex reveals assembly of multiple dimers on tandem kappaB sites." Moorthy A.K., Huang D.B., Wang V.Y., Vu D., Ghosh G. J. Mol. Biol. 373:723-734(2007) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) OF 91-378 IN COMPLEX WITH NFKB1.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M83380 mRNA. Translation: AAA40041.1.
AK146932 mRNA. Translation: BAE27543.1.
BC019765 mRNA. Translation: AAH19765.1.
BC117793 mRNA. Translation: AAI17794.1.
S56076 mRNA. Translation: AAB25493.2.
S76754 Genomic DNA. Translation: AAB33259.1.

IPI

IPI00331502.

PIR

A42023.
I58091.

RefSeq

NP_033072.2. NM_009046.2.

UniGene

Mm.1741.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZK9	X-ray	2.18	A	277-378	[»]
1ZKA	X-ray	2.20	A	277-378	[»]
2V2T	X-ray	3.05	A	91-378	[»]
3DO7	X-ray	3.05	A	88-383	[»]
3JSS	X-ray	2.60	A	278-378	[»]
3JUZ	X-ray	2.51	A	278-378	[»]
3JV0	X-ray	2.65	A	278-378	[»]
3JV4	X-ray	3.15	A/C/E	278-378	[»]
3JV6	X-ray	2.78	A/C/E	278-378	[»]

ProteinModelPortal

Q04863.

SMR

Q04863. Positions 88-383.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-39585N.

IntAct

Q04863. 1 interaction.

MINT

MINT-225343.

PTM databases

PhosphoSite

Q04863.

Proteomic databases

PRIDE

Q04863.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000094762; ENSMUSP00000092355; ENSMUSG00000002983.
ENSMUST00000098754; ENSMUSP00000096350; ENSMUSG00000002983.

GeneID

19698.

KEGG

mmu:19698.

Organism-specific databases

CTD

5971.

MGI

MGI:103289. Relb.

Phylogenomic databases

eggNOG

NOG119056.

GeneTree

ENSGT00500000044765.

HOGENOM

HOG000148598.

HOVERGEN

HBG017021.

InParanoid

Q8VE46.

KO

K09253.

OMA

LDDGFAY.

OrthoDB

EOG4GQQ4T.

Gene expression databases

ArrayExpress

Q04863.

Bgee

Q04863.

Genevestigator

Q04863.

GermOnline

ENSMUSG00000002983. Mus musculus.

Family and domain databases

Gene3D

2.60.40.10. 1 hit.
2.60.40.340. 1 hit.

InterPro

IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT_TIG_rcpt.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]

Pfam

PF00554. RHD. 1 hit.
[Graphical view]

PRINTS

PR00057. NFKBTNSCPFCT.

SMART

SM00429. IPT. 1 hit.
[Graphical view]

SUPFAM

SSF81296. Ig_E-set. 1 hit.
SSF49417. P53_like_DNA_bnd. 1 hit.

PROSITE

PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q04863.

NextBio

297052.

SOURCE

Search...

Entry information

Entry name

RELB_MOUSE

Accession

Primary (citable) accession number: Q04863
Secondary accession number(s): Q8VE46

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	July 27, 2011
Last modified:	April 3, 2013
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program