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Protein

Proto-oncogene c-Rel

Gene

REL

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

GO - Molecular functioni

  • chromatin binding Source: GO_Central
  • DNA binding Source: AgBase
  • protein heterodimerization activity Source: AgBase
  • protein homodimerization activity Source: AgBase
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: GO_Central
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: GO_Central
  • transcription factor activity, sequence-specific DNA binding Source: AgBase

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene c-Rel
Alternative name(s):
p68
Gene namesi
Name:REL
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: AgBase
  • cytosol Source: GO_Central
  • I-kappaB/NF-kappaB complex Source: GO_Central
  • nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 598598Proto-oncogene c-RelPRO_0000205167Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei266 – 2661Phosphoserine; by PKASequence analysis

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiP16236.

PTM databases

iPTMnetiP16236.

Interactioni

Subunit structurei

Homodimer; component of the NF-kappa-B c-Rel-c-Rel complex. Component of the NF-KAPPA-B p65-c-Rel complex.2 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: AgBase
  • protein homodimerization activity Source: AgBase

Protein-protein interaction databases

STRINGi9031.ENSGALP00000012728.

Structurei

Secondary structure

1
598
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi8 – 136Combined sources
Beta strandi18 – 203Combined sources
Helixi25 – 273Combined sources
Beta strandi36 – 383Combined sources
Beta strandi48 – 525Combined sources
Beta strandi58 – 658Combined sources
Beta strandi67 – 704Combined sources
Beta strandi75 – 806Combined sources
Beta strandi87 – 926Combined sources
Beta strandi105 – 1084Combined sources
Turni111 – 1133Combined sources
Helixi114 – 1229Combined sources
Turni123 – 1253Combined sources
Helixi133 – 1375Combined sources
Beta strandi146 – 15611Combined sources
Beta strandi158 – 1658Combined sources
Beta strandi174 – 1763Combined sources
Turni180 – 1823Combined sources
Beta strandi187 – 1915Combined sources
Beta strandi193 – 1964Combined sources
Beta strandi202 – 2087Combined sources
Helixi212 – 2143Combined sources
Beta strandi216 – 2216Combined sources
Beta strandi224 – 2274Combined sources
Helixi232 – 2343Combined sources
Turni237 – 2393Combined sources
Beta strandi240 – 2445Combined sources
Beta strandi256 – 2638Combined sources
Helixi265 – 2673Combined sources
Beta strandi274 – 2796Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GJIX-ray2.85A/B7-281[»]
ProteinModelPortaliP16236.
SMRiP16236. Positions 7-281.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP16236.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 296290RHDPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi289 – 2946Nuclear localization signalSequence analysis

Sequence similaritiesi

Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG410IG8F. Eukaryota.
ENOG410XT64. LUCA.
HOGENOMiHOG000264257.
HOVERGENiHBG017916.
InParanoidiP16236.
KOiK09254.
PhylomeDBiP16236.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR030505. c-Rel.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030492. RHD_CS.
IPR032397. RHD_dimer.
IPR011539. RHD_DNA_bind_dom.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 2 hits.
PTHR24169:SF4. PTHR24169:SF4. 2 hits.
PfamiPF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 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.

P16236-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAGISEPYIE IFEQPRQRGM RFRYKCEGRS AGSIPGEHST DNNKTFPSIQ
60 70 80 90 100
ILNYFGKVKI RTTLVTKNEP YKPHPHDLVG KDCRDGYYEA EFGPERRVLS
110 120 130 140 150
FQNLGIQCVK KKDLKESISL RISKKINPFN VPEEQLHNID EYDLNVVRLC
160 170 180 190 200
FQAFLPDEHG NYTLALPPLI SNPIYDNRAP NTAELRICRV NKNCGSVKGG
210 220 230 240 250
DEIFILCDKV QKDDIEVRFV LDNWEAKGSF SQADVHRQVA IVFRTPPFLR
260 270 280 290 300
DITEPITVKM QLRRPSDQEV SEPMDFRYLP DEKDPYGNKA KRQRSTLAWQ
310 320 330 340 350
KLIQDCGSAV TERPKAAPIP TVNPEGKLIK KEPNMFSPTL MLPGLGTLTS
360 370 380 390 400
SSQMYPPCSQ MPHQPAQLGP GKQDTLPSCW QQLFSSSPSA SSLLSMHPHN
410 420 430 440 450
SFTAEVPQPG AQGSSSLPAF HDNPLNWPDE KDSSFYRNFG STNGMGAAMV
460 470 480 490 500
SAADMQSASS NSIVHATHQA SATAASIVNM ETNDMNCTSL NFEKYTQVLN
510 520 530 540 550
VSNHRQQLHQ APAACPPVAA PGSTPFSSQP NLADTAVYNS FLDQEVISDS
560 570 580 590
RLSTNPLQNH QNSLTLTDNQ FYDTDGVHTD ELYQSFQLDT NILQSYNH
Length:598
Mass (Da):66,847
Last modified:November 1, 1990 - v2
Checksum:i74B38AE57A8B5CD3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti74 – 741H → L in AAA48721 (PubMed:2555689).Curated
Sequence conflicti205 – 2051I → L in AAA48721 (PubMed:2555689).Curated
Sequence conflicti317 – 3171A → T in AAA48721 (PubMed:2555689).Curated
Sequence conflicti410 – 4101G → N in AAA48721 (PubMed:2555689).Curated

Mass spectrometryi

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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52193 mRNA. Translation: CAA36439.1.
M26381 mRNA. Translation: AAA48721.1.
PIRiA34098. TVCHRL.
S10893.
RefSeqiNP_001161198.1. NM_001167726.1.
UniGeneiGga.10724.

Genome annotation databases

GeneIDi396500.
KEGGigga:396500.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X52193 mRNA. Translation: CAA36439.1.
M26381 mRNA. Translation: AAA48721.1.
PIRiA34098. TVCHRL.
S10893.
RefSeqiNP_001161198.1. NM_001167726.1.
UniGeneiGga.10724.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GJIX-ray2.85A/B7-281[»]
ProteinModelPortaliP16236.
SMRiP16236. Positions 7-281.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000012728.

PTM databases

iPTMnetiP16236.

Proteomic databases

PaxDbiP16236.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396500.
KEGGigga:396500.

Organism-specific databases

CTDi5966.

Phylogenomic databases

eggNOGiENOG410IG8F. Eukaryota.
ENOG410XT64. LUCA.
HOGENOMiHOG000264257.
HOVERGENiHBG017916.
InParanoidiP16236.
KOiK09254.
PhylomeDBiP16236.

Miscellaneous databases

EvolutionaryTraceiP16236.
NextBioi20816539.
PROiP16236.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR030505. c-Rel.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030492. RHD_CS.
IPR032397. RHD_dimer.
IPR011539. RHD_DNA_bind_dom.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 2 hits.
PTHR24169:SF4. PTHR24169:SF4. 2 hits.
PfamiPF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 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]
ProtoNetiSearch...

Publicationsi

  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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 7-281 IN COMPLEX WITH IL2 DNA.

Entry informationi

Entry nameiREL_CHICK
AccessioniPrimary (citable) accession number: P16236
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: November 1, 1990
Last modified: February 17, 2016
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.