Reviewed, UniProtKB/Swiss-Prot Q01201 (RELB_HUMAN)

Names and origin

Protein names

Recommended name:
    Transcription factor RelB
      Short name=I-Rel

Gene names

Name:

RELB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	579 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subunit structure	Component of the NF-kappa-B RelB-p50 complex. Component of the NF-kappa-B RelB-p52 complex. Self-associates; the interaction seems to be transient and may prevent degradation allowing for heterodimer formation with p50 or p52. Interacts with NFKB1/p50, NFKB2/p52 and NFKB2/p100. Interacts with NFKBID By similarity.
Subcellular location	Nucleus.
Induction	By mitogens.
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 By similarity.
Sequence similarities	Contains 1 RHD (Rel-like) domain.
Caution	Was originally (Ref.1) thought to inhibit the transcriptional activity of nuclear factor NF-kappa-B.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Molecular function	Activator
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: InterPro
Molecular function	transcription corepressor activity Ref.1 Traceable author statement. Source: ProtInc transcription factor activity Traceable author statement. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
COMMD1	Q8N668	1	EBI-357837,EBI-1550112

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 579	579	Transcription factor RelB		PRO_0000205173
Regions
	Domain	40 – 68	29	Leucine-zipper
	Domain	125 – 440	316	RHD
	Motif	433 – 438	6	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	37	1	Phosphoserine
	Modified residue	103	1	Phosphothreonine By similarity
	Modified residue	573	1	Phosphoserine
Experimental info
	Sequence conflict	139	1	R → P in AAA36127. Ref.1
	Sequence conflict	411	1	R → A in AAA36127. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q01201-1 [UniParc]. Last modified April 4, 2006. Version 2. Checksum: C2C61C2C8640513E	FASTA	579	62,134
	10 20 30 40 50 60 MLRSGPASGP SVPTGRAMPS RRVARPPAAP ELGALGSPDL SSLSLAVSRS TDELEIIDEY 70 80 90 100 110 120 IKENGFGLDG GQPGPGEGLP RLVSRGAASL STVTLGPVAP PATPPPWGCP LGRLVSPAPG 130 140 150 160 170 180 PGPQPHLVIT EQPKQRGMRF RYECEGRSAG SILGESSTEA SKTLPAIELR DCGGLREVEV 190 200 210 220 230 240 TACLVWKDWP HRVHPHSLVG KDCTDGICRV RLRPHVSPRH SFNNLGIQCV RKKEIEAAIE 250 260 270 280 290 300 RKIQLGIDPY NAGSLKNHQE VDMNVVRICF QASYRDQQGQ MRRMDPVLSE PVYDKKSTNT 310 320 330 340 350 360 SELRICRINK ESGPCTGGEE LYLLCDKVQK EDISVVFSRA SWEGRADFSQ ADVHRQIAIV 370 380 390 400 410 420 FKTPPYEDLE IVEPVTVNVF LQRLTDGVCS EPLPFTYLPR DHDSYGVDKK RKRGMPDVLG 430 440 450 460 470 480 ELNSSDPHGI ESKRRKKKPA ILDHFLPNHG SGPFLPPSAL LPDPDFFSGT VSLPGLEPPG 490 500 510 520 530 540 GPDLLDDGFA YDPTAPTLFT MLDLLPPAPP HASAVVCSGG AGAVVGETPG PEPLTLDSYQ 550 560 570 APGPGDGGTA SLVGSNMFPN HYREAAFGGG LLSPGPEAT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"I-Rel: a novel rel-related protein that inhibits NF-kappa B transcriptional activity." Ruben S.M., Klement J.F., Maher M., Coleman T.A., Chen C.H., Rosen C.A. Genes Dev. 6:745-760(1992) [PubMed: 1577270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: T-cell.
[2]	"A transcriptional map in the region of 19q13 derived using direct sequencing and exon trapping." Yoshiura K., Murray J.C. Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Blood.
[5]	"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: 1732739] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P50 COMPLEX.
[6]	"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: 8441398] [Abstract] Cited for: FUNCTION.
[7]	"Differential interactions of Rel-NF-kappa B complexes with I kappa B alpha determine pools of constitutive and inducible NF-kappa B activity." Dobrzanski P., Ryseck R.P., Bravo R. EMBO J. 13:4608-4616(1994) [PubMed: 7925301] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN THE NF-KAPPA-B RELB-P50 COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B RELB-P52 COMPLEX.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-573, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBLGenBankDDBJ	M83221 mRNA. Translation: AAA36127.1. AF043463 , AF043454, AF043455, AF043456, AF043457, AF043458, AF043459, AF043460, AF043461, AF043462 Genomic DNA. Translation: AAC82346.1. DQ314887 Genomic DNA. Translation: ABC40746.1. BC028013 mRNA. Translation: AAH28013.1.
PIR	A42617.
RefSeq	NP_006500.2.
UniGene	Hs.654402
3D structure databases
HSSP	HSSP built from PDB template 1MY7 based on UniProtKB Q04207.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:27531N.
IntAct	Q01201.
PTM databases
PhosphoSite	Q01201.
Genome annotation databases
Ensembl	ENSG00000104856. Homo sapiens. [Contig view]
GeneID	5971.
KEGG	hsa:5971.
Organism-specific databases
H-InvDB	HIX0015220.
HGNC	HGNC:9956. RELB.
HPA	CAB007753.
MIM	604758. gene.
PharmGKB	PA34322.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOGENOM	Q01201.
HOVERGEN	Q01201.
Gene expression databases
ArrayExpress	Q01201.
CleanEx	HS_RELB.
GermOnline	ENSG00000104856. Homo sapiens.
Family and domain databases
InterPro	IPR013783. Ig-like_fold. IPR002909. IPT_TIG_rcpt. IPR000451. NF_Rel_dor. IPR011539. RHD. [Graphical view]
Gene3D	G3DSA:2.60.40.10. Ig-like_fold. 1 hit. G3DSA:2.60.40.340. RHD. 1 hit.
Pfam	PF00554. RHD. 1 hit. PF01833. TIG. 1 hit. [Graphical view]
PRINTS	PR00057. NFKBTNSCPFCT.
SMART	SM00429. IPT. 1 hit. [Graphical view]
PROSITE	PS01204. REL_1. 1 hit. PS50254. REL_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	23245.
SOURCE	Search...

Entry information

Entry name

RELB_HUMAN

Accession

Primary (citable) accession number: Q01201
Secondary accession number(s): Q6GTX7, Q9UEI7

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1993
Last sequence update:	April 4, 2006
Last modified:	November 25, 2008
This is version 87 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)