Q01201 (RELB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Transcription factor RelB

Alternative name(s):
I-Rel

Gene names

Name:

RELB

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	579 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. As a member of the NUPR1/RELB/IER3 survival pathway, may provide pancreatic ductal adenocarcinoma with remarkable resistance to cell stress, such as starvation or gemcitabine treatment. Ref.5 Ref.6 Ref.7 Ref.12
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. Ref.5 Ref.7
Subcellular location	Nucleus. Cytoplasm › cytoskeleton › centrosome. Note: Co-localizes with NEK6 in the centrosome. Ref.10
Induction	Up-regulated by mitogens and NUPR1. Ref.12
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	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T-helper 1 cell differentiation Inferred from electronic annotation. Source: Compara antigen processing and presentation Inferred from electronic annotation. Source: Compara myeloid dendritic cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of gene expression Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Inferred from electronic annotation. Source: Compara microtubule organizing center Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Traceable author statement PubMed 8188306. Source: ProtInc transcription corepressor activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
COMMD1	Q8N668	2	EBI-357837,EBI-1550112
GSK3B	P49841	4	EBI-357837,EBI-373586

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	125 – 440	316	RHD
	Region	40 – 68	29	Leucine-zipper
	Motif	433 – 438	6	Nuclear localization signal Potential
Amino acid modifications
	Modified residue	37	1	Phosphoserine Ref.8 Ref.11
	Modified residue	573	1	Phosphoserine Ref.8 Ref.9
Natural variations
	Natural variant	396	1	T → M. Corresponds to variant rs2230682 [ dbSNP | Ensembl ].		VAR_051782
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 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-573, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[10]	"Characterization of hNek6 interactome reveals an important role for its short N-terminal domain and colocalization with proteins at the centrosome." Vaz Meirelles G., Ferreira Lanza D.C., da Silva J.C., Santana Bernachi J., Paes Leme A.F., Kobarg J. J. Proteome Res. 9:6298-6316(2010) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[11]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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, INDUCTION BY NUPR1.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00221034.
PIR	A42617.
RefSeq	NP_006500.2. NM_006509.3.
UniGene	Hs.654402.
3D structure databases
ProteinModelPortal	Q01201.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27531N.
IntAct	Q01201. 17 interactions.
MINT	MINT-1131428.
STRING	9606.ENSP00000221452.
PTM databases
PhosphoSite	Q01201.
Polymorphism databases
DMDM	92090634.
Proteomic databases
PaxDb	Q01201.
PRIDE	Q01201.
Protocols and materials databases
DNASU	5971.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000221452; ENSP00000221452; ENSG00000104856. ENST00000540120; ENSP00000445542; ENSG00000104856.
GeneID	5971.
KEGG	hsa:5971.
UCSC	uc021uvp.1. human.
Organism-specific databases
CTD	5971.
GeneCards	GC19P045504.
HGNC	HGNC:9956. RELB.
HPA	CAB007753.
MIM	604758. gene.
neXtProt	NX_Q01201.
PharmGKB	PA34322.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG119056.
HOGENOM	HOG000148598.
HOVERGEN	HBG017021.
InParanoid	Q01201.
KO	K09253.
OMA	LDDGFAY.
OrthoDB	EOG4GQQ4T.
Enzyme and pathway databases
Pathway_Interaction_DB	nfkappabalternativepathway. Alternative NF-kappaB pathway. il12_2pathway. IL12-mediated signaling events.
Gene expression databases
ArrayExpress	Q01201.
Bgee	Q01201.
CleanEx	HS_RELB.
Genevestigator	Q01201.
GermOnline	ENSG00000104856. Homo sapiens.
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
GenomeRNAi	5971.
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:	May 1, 2013
This is version 133 of the entry and version 2 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.