Skip Header

Contribute Send feedback
Read comments (?) or add your own

P16236 (REL_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Proto-oncogene c-Rel
Alternative name(s):
p68
Gene names
Name:REL
OrganismGallus gallus (Chicken)
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
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 By similarity.

Subunit structure

Homodimer; component of the NF-kappa-B c-Rel-c-Rel complex. Component of the NF-KAPPA-B p65-c-Rel complex.

Subcellular location

Nucleus.

Sequence similarities

Contains 1 RHD (Rel-like) domain.

Mass spectrometry

Molecular mass is 63513±3 Da from positions 1 - 598. Determined by MALDI. Ref.5

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598Proto-oncogene c-Rel
PRO_0000205167

Regions

Domain7 – 296290RHD
Motif289 – 2946Nuclear localization signal Potential

Amino acid modifications

Modified residue2661Phosphoserine; by PKA Potential

Experimental info

Sequence conflict741H → L in AAA48721. Ref.3
Sequence conflict2051I → L in AAA48721. Ref.3
Sequence conflict3171A → T in AAA48721. Ref.3
Sequence conflict4101G → N in AAA48721. Ref.3

Secondary structure

1 .......................................................... 598
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P16236 [UniParc].

Last modified November 1, 1990. Version 2.
Checksum: 74B38AE57A8B5CD3

FASTA59866,847
        10         20         30         40         50         60 
MAGISEPYIE IFEQPRQRGM RFRYKCEGRS AGSIPGEHST DNNKTFPSIQ ILNYFGKVKI 

        70         80         90        100        110        120 
RTTLVTKNEP YKPHPHDLVG KDCRDGYYEA EFGPERRVLS FQNLGIQCVK KKDLKESISL 

       130        140        150        160        170        180 
RISKKINPFN VPEEQLHNID EYDLNVVRLC FQAFLPDEHG NYTLALPPLI SNPIYDNRAP 

       190        200        210        220        230        240 
NTAELRICRV NKNCGSVKGG DEIFILCDKV QKDDIEVRFV LDNWEAKGSF SQADVHRQVA 

       250        260        270        280        290        300 
IVFRTPPFLR DITEPITVKM QLRRPSDQEV SEPMDFRYLP DEKDPYGNKA KRQRSTLAWQ 

       310        320        330        340        350        360 
KLIQDCGSAV TERPKAAPIP TVNPEGKLIK KEPNMFSPTL MLPGLGTLTS SSQMYPPCSQ 

       370        380        390        400        410        420 
MPHQPAQLGP GKQDTLPSCW QQLFSSSPSA SSLLSMHPHN SFTAEVPQPG AQGSSSLPAF 

       430        440        450        460        470        480 
HDNPLNWPDE KDSSFYRNFG STNGMGAAMV SAADMQSASS NSIVHATHQA SATAASIVNM 

       490        500        510        520        530        540 
ETNDMNCTSL NFEKYTQVLN VSNHRQQLHQ APAACPPVAA PGSTPFSSQP NLADTAVYNS 

       550        560        570        580        590 
FLDQEVISDS RLSTNPLQNH QNSLTLTDNQ FYDTDGVHTD ELYQSFQLDT NILQSYNH

« Hide

References

[1]"Cloning and expression of a chicken c-rel cDNA: unlike p59v-rel, p68c-rel is a cytoplasmic protein in chicken embryo fibroblasts."
Capobianco A.J., Simmons D.L., Gilmore T.D.
Oncogene 5:257-265(1990) [PubMed: 2179815] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Fibroblast.
[2]"Characterization of a novel promoter insertion in the c-rel locus."
Kabrun N., Bumstead N., Hayman M.J., Enrietto P.J.
Mol. Cell. Biol. 10:4788-4794(1990) [PubMed: 2167440] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-7.
[3]"Transactivation of gene expression by nuclear and cytoplasmic rel proteins."
Hannink M., Temin H.M.
Mol. Cell. Biol. 9:4323-4336(1989) [PubMed: 2555689] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-598.
[4]"Isolation of the chicken NF-kappa B p65 subunit-encoding cDNA and characterization of its products."
Ikeda T., Honjo K., Hirota Y., Onodera T.
Gene 133:237-242(1993) [PubMed: 7916720] [Abstract]
Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
[5]"Proteomic analysis of the Gallus gallus embryo at stage-29 of development."
Agudo D., Gomez-Esquer F., Diaz-Gil G., Martinez-Arribas F., Delcan J., Schneider J., Palomar M.A., Linares R.
Proteomics 5:4946-4957(2005) [PubMed: 16287166] [Abstract]
Cited for: IDENTIFICATION, MASS SPECTROMETRY.
Tissue: Embryo.
[6]"X-ray crystal structure of proto-oncogene product c-Rel bound to the CD28 response element of IL-2."
Huang D.B., Chen Y.Q., Ruetsche M., Phelps C.B., Ghosh G.
Structure 9:669-678(2001) [PubMed: 11587641] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 7-281 IN COMPLEX WITH IL2 DNA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X52193 mRNA. Translation: CAA36439.1.
M26381 mRNA. Translation: AAA48721.1.
IPIIPI00572054.
PIRTVCHRL. A34098.
S10893.
RefSeqNP_001161198.1. NM_001167726.1.
UniGeneGga.10724.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GJIX-ray2.85A/B7-281[»]
ProteinModelPortalP16236.
SMRP16236. Positions 7-281.
ModBaseSearch...

Protein-protein interaction databases

STRINGP16236.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396500.
KEGGgga:396500.

Organism-specific databases

CTD5966.

Phylogenomic databases

eggNOGveNOG09204.
GeneTreeENSGT00500000044765.
HOGENOMHBG282218.
HOVERGENHBG017916.
InParanoidP16236.
OrthoDBEOG4NVZK2.

Family and domain databases

InterProIPR013783. 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]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 1 hit.
G3DSA:2.60.40.340. RHD. 1 hit.
KOK09254.
PfamPF00554. RHD. 1 hit.
[Graphical view]
PRINTSPR00057. NFKBTNSCPFCT.
SMARTSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMSSF81296. Ig_E-set. 1 hit.
SSF49417. P53_like_DNA_bnd. 1 hit.
PROSITEPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameREL_CHICK
AccessionPrimary (citable) accession number: P16236
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1990
Last modified: November 16, 2011
This is version 93 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents