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Reviewed, UniProtKB/Swiss-Prot Q04864 (REL_HUMAN)

Last modified November 25, 2008. Version 76. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    C-Rel proto-oncogene protein
      Short name=C-Rel protein
Gene names
Name: REL
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length619 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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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.

Subcellular location

NucleusBy similarity.

Sequence similarities

Contains 1 RHD (Rel-like) domain.

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Ontologies

Keywords

   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DiseaseProto-oncogene
   LigandDNA-binding
   Molecular functionActivator
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processpositive regulation of I-kappaB kinase/NF-kappaB cascade

Inferred from expression pattern. Source: UniProtKB

   Cellular componentnucleus

Inferred from electronic annotation. Source: InterPro

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

transcription factor activity

Non-traceable author statement. Source: ProtInc

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

COMMD1Q8N6681EBI-307352,EBI-1550112
RELAQ042062EBI-307352,EBI-73886

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 619619C-Rel proto-oncogene protein
PRO_0000205165

Regions

Region8 – 297290RHD
Motif290 – 2956Nuclear localization signal Potential

Amino acid modifications

Modified residue2671Phosphoserine; by PKA Potential
Modified residue5031Phosphoserine

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Sequences

Sequence LengthMass (Da)Tools
Q04864-1 [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

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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: 2666912] [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: 3016517] [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: 1740106] [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: 8152812] [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: 9056676] [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: 9315679] [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: 10823840] [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: 15102766] [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: 15024091] [Abstract]
Cited for: INTERACTION WITH NKIRAS1.
+Additional computationally mapped references.

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Cross-references

Sequence databases

X75042 mRNA. Translation: CAA52954.1.
DQ314888 Genomic DNA. Translation: ABC40747.1.
M11595 Genomic DNA. Translation: AAA52073.1.
PIRA60646.
RefSeqNP_002899.1.
UniGeneHs.631886

3D structure databases

HSSPHSSP built from PDB template 1GJI based on UniProtKB P16236.
SMRQ04864. Positions 8-282.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:301N.
IntActQ04864.

Genome annotation databases

EnsemblENSG00000162924. Homo sapiens. [Contig view]
GeneID5966.
KEGGhsa:5966.

Organism-specific databases

H-InvDBHIX0029962.
HGNCHGNC:9954. REL.
HPACAB004404.
MIM164910. gene.
PharmGKBPA30126.
GenAtlasSearch...
GeneCardsSearch...

Phylogenomic databases

HOGENOMQ04864.
HOVERGENQ04864.

Gene expression databases

ArrayExpressQ04864.
CleanExHS_REL.
GermOnlineENSG00000162924. Homo sapiens.

Family and domain databases

InterProIPR013783. Ig-like_fold.
IPR002909. IPT_TIG_rcpt.
IPR000451. NF_Rel_dor.
IPR011539. RHD.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:2.60.40.340. RHD. 1 hit.
PfamPF00554. RHD. 1 hit.
PF01833. TIG. 1 hit.
[Graphical view]
PRINTSPR00057. NFKBTNSCPFCT.
SMARTSM00429. IPT. 1 hit.
[Graphical view]
PROSITEPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubQ04864.
NextBio23226.
SOURCESearch...

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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: November 25, 2008
This is version 76 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 2

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

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents