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Q01201

- RELB_HUMAN

UniProt

Q01201 - RELB_HUMAN

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Protein
Transcription factor RelB
Gene
RELB
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc
  4. transcription corepressor activity Source: ProtInc

GO - Biological processi

  1. T-helper 1 cell differentiation Source: Ensembl
  2. antigen processing and presentation Source: Ensembl
  3. myeloid dendritic cell differentiation Source: Ensembl
  4. positive regulation of gene expression Source: Ensembl
  5. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor RelB
Alternative name(s):
I-Rel
Gene namesi
Name:RELB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:9956. RELB.

Subcellular locationi

Nucleus. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome
Note: Colocalizes with NEK6 in the centrosome.1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Ensembl
  3. microtubule organizing center Source: UniProtKB-SubCell
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34322.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 579579Transcription factor RelB
PRO_0000205173Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei37 – 371Phosphoserine2 Publications
Modified residuei573 – 5731Phosphoserine2 Publications

Post-translational modificationi

Phosphorylation at 'Thr-103' and 'Ser-573' is followed by proteasomal degradation By similarity.

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ01201.
PaxDbiQ01201.
PRIDEiQ01201.

PTM databases

PhosphoSiteiQ01201.

Expressioni

Inductioni

Up-regulated by mitogens and NUPR1.1 Publication

Gene expression databases

ArrayExpressiQ01201.
BgeeiQ01201.
CleanExiHS_RELB.
GenevestigatoriQ01201.

Organism-specific databases

HPAiCAB007753.
HPA040506.

Interactioni

Subunit structurei

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.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COMMD1Q8N6682EBI-357837,EBI-1550112
GSK3BP498414EBI-357837,EBI-373586
NFKB1P198384EBI-357837,EBI-300010
NFKB2Q006533EBI-357837,EBI-307326

Protein-protein interaction databases

BioGridi111903. 45 interactions.
DIPiDIP-27531N.
IntActiQ01201. 33 interactions.
MINTiMINT-1131428.
STRINGi9606.ENSP00000221452.

Structurei

3D structure databases

ProteinModelPortaliQ01201.
SMRiQ01201. Positions 123-400.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini125 – 440316RHD
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni40 – 6829Leucine-zipper
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi433 – 4386Nuclear localization signal Reviewed prediction

Domaini

Both N- and C-terminal domains are required for transcriptional activation.

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG119056.
HOGENOMiHOG000148598.
HOVERGENiHBG017021.
InParanoidiQ01201.
KOiK09253.
OMAiDDGFAYD.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ01201.
TreeFamiTF325632.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamiPF00554. RHD. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q01201-1 [UniParc]FASTAAdd to Basket

« Hide

MLRSGPASGP SVPTGRAMPS RRVARPPAAP ELGALGSPDL SSLSLAVSRS    50
TDELEIIDEY IKENGFGLDG GQPGPGEGLP RLVSRGAASL STVTLGPVAP 100
PATPPPWGCP LGRLVSPAPG PGPQPHLVIT EQPKQRGMRF RYECEGRSAG 150
SILGESSTEA SKTLPAIELR DCGGLREVEV TACLVWKDWP HRVHPHSLVG 200
KDCTDGICRV RLRPHVSPRH SFNNLGIQCV RKKEIEAAIE RKIQLGIDPY 250
NAGSLKNHQE VDMNVVRICF QASYRDQQGQ MRRMDPVLSE PVYDKKSTNT 300
SELRICRINK ESGPCTGGEE LYLLCDKVQK EDISVVFSRA SWEGRADFSQ 350
ADVHRQIAIV FKTPPYEDLE IVEPVTVNVF LQRLTDGVCS EPLPFTYLPR 400
DHDSYGVDKK RKRGMPDVLG ELNSSDPHGI ESKRRKKKPA ILDHFLPNHG 450
SGPFLPPSAL LPDPDFFSGT VSLPGLEPPG GPDLLDDGFA YDPTAPTLFT 500
MLDLLPPAPP HASAVVCSGG AGAVVGETPG PEPLTLDSYQ APGPGDGGTA 550
SLVGSNMFPN HYREAAFGGG LLSPGPEAT 579
Length:579
Mass (Da):62,134
Last modified:April 4, 2006 - v2
Checksum:iC2C61C2C8640513E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti396 – 3961T → M.
Corresponds to variant rs2230682 [ dbSNP | Ensembl ].
VAR_051782

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti139 – 1391R → P in AAA36127. 1 Publication
Sequence conflicti411 – 4111R → A in AAA36127. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS46110.1.
PIRiA42617.
RefSeqiNP_006500.2. NM_006509.3.
UniGeneiHs.654402.

Genome annotation databases

EnsembliENST00000221452; ENSP00000221452; ENSG00000104856.
ENST00000540120; ENSP00000445542; ENSG00000104856.
GeneIDi5971.
KEGGihsa:5971.
UCSCiuc021uvp.1. human.

Polymorphism databases

DMDMi92090634.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS46110.1.
PIRi A42617.
RefSeqi NP_006500.2. NM_006509.3.
UniGenei Hs.654402.

3D structure databases

ProteinModelPortali Q01201.
SMRi Q01201. Positions 123-400.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111903. 45 interactions.
DIPi DIP-27531N.
IntActi Q01201. 33 interactions.
MINTi MINT-1131428.
STRINGi 9606.ENSP00000221452.

PTM databases

PhosphoSitei Q01201.

Polymorphism databases

DMDMi 92090634.

Proteomic databases

MaxQBi Q01201.
PaxDbi Q01201.
PRIDEi Q01201.

Protocols and materials databases

DNASUi 5971.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000221452 ; ENSP00000221452 ; ENSG00000104856 .
ENST00000540120 ; ENSP00000445542 ; ENSG00000104856 .
GeneIDi 5971.
KEGGi hsa:5971.
UCSCi uc021uvp.1. human.

Organism-specific databases

CTDi 5971.
GeneCardsi GC19P045504.
HGNCi HGNC:9956. RELB.
HPAi CAB007753.
HPA040506.
MIMi 604758. gene.
neXtProti NX_Q01201.
PharmGKBi PA34322.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG119056.
HOGENOMi HOG000148598.
HOVERGENi HBG017021.
InParanoidi Q01201.
KOi K09253.
OMAi DDGFAYD.
OrthoDBi EOG7VHSWT.
PhylomeDBi Q01201.
TreeFami TF325632.

Miscellaneous databases

GeneWikii RELB.
GenomeRNAii 5971.
NextBioi 23245.
PROi Q01201.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q01201.
Bgeei Q01201.
CleanExi HS_RELB.
Genevestigatori Q01201.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProi IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view ]
Pfami PF00554. RHD. 1 hit.
[Graphical view ]
PRINTSi PR00057. NFKBTNSCPFCT.
SMARTi SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37 AND SER-573, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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.

Entry informationi

Entry nameiRELB_HUMAN
AccessioniPrimary (citable) accession number: Q01201
Secondary accession number(s): Q6GTX7, Q9UEI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: April 4, 2006
Last modified: July 9, 2014
This is version 144 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Caution

Was originally (1 Publication) thought to inhibit the transcriptional activity of nuclear factor NF-kappa-B.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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