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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)DescriptionActionsGraphical viewLength
ChainiPRO_00002051671 – 598Proto-oncogene c-RelAdd BLAST598

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei266Phosphoserine; by PKASequence analysis1

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

1598
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi8 – 13Combined sources6
Beta strandi18 – 20Combined sources3
Helixi25 – 27Combined sources3
Beta strandi36 – 38Combined sources3
Beta strandi48 – 52Combined sources5
Beta strandi58 – 65Combined sources8
Beta strandi67 – 70Combined sources4
Beta strandi75 – 80Combined sources6
Beta strandi87 – 92Combined sources6
Beta strandi105 – 108Combined sources4
Turni111 – 113Combined sources3
Helixi114 – 122Combined sources9
Turni123 – 125Combined sources3
Helixi133 – 137Combined sources5
Beta strandi146 – 156Combined sources11
Beta strandi158 – 165Combined sources8
Beta strandi174 – 176Combined sources3
Turni180 – 182Combined sources3
Beta strandi187 – 191Combined sources5
Beta strandi193 – 196Combined sources4
Beta strandi202 – 208Combined sources7
Helixi212 – 214Combined sources3
Beta strandi216 – 221Combined sources6
Beta strandi224 – 227Combined sources4
Helixi232 – 234Combined sources3
Turni237 – 239Combined sources3
Beta strandi240 – 244Combined sources5
Beta strandi256 – 263Combined sources8
Helixi265 – 267Combined sources3
Beta strandi274 – 279Combined sources6

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP16236.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini7 – 296RHDPROSITE-ProRule annotationAdd BLAST290

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi289 – 294Nuclear localization signalSequence analysis6

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

CDDicd01177. IPT_NFkappaB. 1 hit.
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.
IPR033926. IPT_NFkappaB.
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)DescriptionActionsGraphical viewLength
Sequence conflicti74H → L in AAA48721 (PubMed:2555689).Curated1
Sequence conflicti205I → L in AAA48721 (PubMed:2555689).Curated1
Sequence conflicti317A → T in AAA48721 (PubMed:2555689).Curated1
Sequence conflicti410G → N in AAA48721 (PubMed:2555689).Curated1

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1GJIX-ray2.85A/B7-281[»]
ProteinModelPortaliP16236.
SMRiP16236.
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.
PROiP16236.

Family and domain databases

CDDicd01177. IPT_NFkappaB. 1 hit.
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.
IPR033926. IPT_NFkappaB.
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...

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: November 30, 2016
This is version 124 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.