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Q04864 (REL_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene c-Rel
Gene names
Name:REL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Proto-oncogene that may play a role in differentiation and lymphopoiesis. 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. The NF-kappa-B heterodimer RELA/p65-c-Rel is a transcriptional activator.

Subunit structure

Component of the NF-kappa-B p65-c-Rel complex. Component of the NF-kappa-B p50-c-Rel complex. Component of the NF-kappa-B p52-c-Rel complex. Homodimer; component of the NF-kappa-B c-Rel-c-Rel complex By similarity. Interacts with NKIRAS1. Interacts with NFKBIB By similarity. Interacts with NFKBIE. Ref.4 Ref.5 Ref.6 Ref.7 Ref.9 Ref.10

Subcellular location

Nucleus By similarity.

Sequence similarities

Contains 1 RHD (Rel-like) domain.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

COMMD1Q8N6683EBI-307352,EBI-1550112
NFKB2Q006533EBI-307352,EBI-307326

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 619618Proto-oncogene c-Rel
PRO_0000205165

Regions

Domain8 – 297290RHD
Motif290 – 2956Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylalanine Ref.11
Modified residue2671Phosphoserine; by PKA Potential
Modified residue5031Phosphoserine Ref.8

Sequences

Sequence LengthMass (Da)Tools
Q04864 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 03E1033BDF7B1B30

FASTA61968,520
        10         20         30         40         50         60 
MASGAYNPYI EIIEQPRQRG MRFRYKCEGR SAGSIPGEHS TDNNRTYPSI QIMNYYGKGK 

        70         80         90        100        110        120 
VRITLVTKND PYKPHPHDLV GKDCRDGYYE AEFGQERRPL FFQNLGIRCV KKKEVKEAII 

       130        140        150        160        170        180 
TRIKAGINPF NVPEKQLNDI EDCDLNVVRL CFQVFLPDEH GNLTTALPPV VSNPIYDNRA 

       190        200        210        220        230        240 
PNTAELRICR VNKNCGSVRG GDEIFLLCDK VQKDDIEVRF VLNDWEAKGI FSQADVHRQV 

       250        260        270        280        290        300 
AIVFKTPPYC KAITEPVTVK MQLRRPSDQE VSESMDFRYL PDEKDTYGNK AKKQKTTLLF 

       310        320        330        340        350        360 
QKLCQDHVET GFRHVDQDGL ELLTSGDPPT LASQSAGITV NFPERPRPGL LGSIGEGRYF 

       370        380        390        400        410        420 
KKEPNLFSHD AVVREMPTGV SSQAESYYPS PGPISSGLSH HASMAPLPSS SWSSVAHPTP 

       430        440        450        460        470        480 
RSGNTNPLSS FSTRTLPSNS QGIPPFLRIP VGNDLNASNA CIYNNADDIV GMEASSMPSA 

       490        500        510        520        530        540 
DLYGISDPNM LSNCSVNMMT TSSDSMGETD NPRLLSMNLE NPSCNSVLDP RDLRQLHQMS 

       550        560        570        580        590        600 
SSSMSAGANS NTTVFVSQSD AFEGSDFSCA DNSMINESGP SNSTNPNSHG FVQDSQYSGI 

       610 
GSMQNEQLSD SFPYEFFQV 

« Hide

References

« Hide 'large scale' references
[1]"A human rel proto-oncogene cDNA containing an Alu fragment as a potential coding exon."
Brownell E., Mittereder N., Rice N.R.
Oncogene 4:935-942(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]NHLBI resequencing and genotyping service (RS&G)
Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Genetic characterization of human c-rel sequences."
Brownell E., O'Brien S.J., Nash W.G., Rice N.R.
Mol. Cell. Biol. 5:2826-2831(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-284.
[4]"A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a DNA element involved in the phorbol ester induction of the human urokinase gene."
Hansen S.K., Nerlov C., Zabel U., Verde P., Johnsen M., Baeuerle P.A., Blasi F.
EMBO J. 11:205-213(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
[5]"Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor necrosis factor."
Beg A.A., Baldwin A.S. Jr.
Oncogene 9:1487-1492(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P52-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
[6]"Regulation of intercellular adhesion molecule-1 gene by tumor necrosis factor-alpha is mediated by the nuclear factor-kappaB heterodimers p65/p65 and p65/c-Rel in the absence of p50."
Aoudjit F., Brochu N., Belanger B., Stratowa C., Hiscott J., Audette M.
Cell Growth Differ. 8:335-342(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
[7]"A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription."
Li Z., Nabel G.J.
Mol. Cell. Biol. 17:6184-6190(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NFKBIE.
[8]"Tumor necrosis factor-alpha activation of NF-kappa B requires the phosphorylation of Ser-471 in the transactivation domain of c-Rel."
Martin A.G., Fresno M.
J. Biol. Chem. 275:24383-24391(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-503.
[9]"Leishmania major amastigotes induce p50/c-Rel NF-kappa B transcription factor in human macrophages: involvement in cytokine synthesis."
Guizani-Tabbane L., Ben-Aissa K., Belghith M., Sassi A., Dellagi K.
Infect. Immun. 72:2582-2589(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX.
[10]"Inhibition of NF-kappaB activity by IkappaBbeta in association with kappaB-Ras."
Chen Y., Vallee S., Wu J., Vu D., Sondek J., Ghosh G.
Mol. Cell. Biol. 24:3048-3056(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NKIRAS1.
[11]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75042 mRNA. Translation: CAA52954.1.
DQ314888 Genomic DNA. Translation: ABC40747.1.
M11595 Genomic DNA. Translation: AAA52073.1.
PIRA60646.
RefSeqNP_002899.1. NM_002908.2.
UniGeneHs.631886.

3D structure databases

ProteinModelPortalQ04864.
SMRQ04864. Positions 8-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111898. 36 interactions.
DIPDIP-301N.
IntActQ04864. 19 interactions.
MINTMINT-1137552.
STRING9606.ENSP00000295025.

PTM databases

PhosphoSiteQ04864.

Polymorphism databases

DMDM548720.

Proteomic databases

PaxDbQ04864.
PRIDEQ04864.

Protocols and materials databases

DNASU5966.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000295025; ENSP00000295025; ENSG00000162924.
GeneID5966.
KEGGhsa:5966.
UCSCuc002sam.1. human.

Organism-specific databases

CTD5966.
GeneCardsGC02P061108.
HGNCHGNC:9954. REL.
HPACAB004404.
MIM164910. gene.
neXtProtNX_Q04864.
PharmGKBPA34321.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG119056.
HOGENOMHOG000264257.
HOVERGENHBG017916.
InParanoidQ04864.
KOK09254.
OMAWEAKGIF.
OrthoDBEOG7VHSWT.
PhylomeDBQ04864.
TreeFamTF325632.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.
SignaLinkQ04864.

Gene expression databases

ArrayExpressQ04864.
BgeeQ04864.
CleanExHS_REL.
GenevestigatorQ04864.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamPF00554. RHD. 1 hit.
[Graphical view]
PRINTSPR00057. NFKBTNSCPFCT.
SMARTSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiREL.
GenomeRNAi5966.
NextBio23226.
PROQ04864.
SOURCESearch...

Entry information

Entry nameREL_HUMAN
AccessionPrimary (citable) accession number: Q04864
Secondary accession number(s): Q2PNZ7, Q6LDY0
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM