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Protein

Proto-oncogene c-Rel

Gene

Rel

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 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

  1. RNA polymerase II distal enhancer sequence-specific DNA binding Source: MGI
  2. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity involved in positive regulation of transcription Source: MGI
  3. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. cytokine production Source: MGI
  2. positive regulation of interleukin-12 biosynthetic process Source: MGI
  3. positive regulation of transcription, DNA-templated Source: MGI
  4. positive regulation of transcription from RNA polymerase II promoter Source: MGI
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene c-Rel
Gene namesi
Name:Rel
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:97897. Rel.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. nucleus Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 587586Proto-oncogene c-RelPRO_0000205166Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei267 – 2671Phosphoserine; by PKASequence Analysis

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15307.
PaxDbiP15307.
PRIDEiP15307.

PTM databases

PhosphoSiteiP15307.

Expressioni

Gene expression databases

CleanExiMM_REL.
GenevestigatoriP15307.

Interactioni

Subunit structurei

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. Interacts with NKIRAS1. Interacts with NFKBIB. Interacts with NFKBIE (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-59241N.
IntActiP15307. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP15307.
SMRiP15307. Positions 8-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini8 – 297290RHDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni403 – 46866Transriptional transactivatorAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi291 – 2966Nuclear localization signalSequence Analysis

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG119056.
HOVERGENiHBG017916.
InParanoidiP15307.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamiPF00554. RHD. 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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15307-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MASSGYNPYV EIIEQPRQRG MRFRYKCEGR SAGSIPGERS TDNNRTYPSV
60 70 80 90 100
QIMNYYGKGK IRITLVTKND PYKPHPHDLV GKDCRDGYYE AEFGPERRPL
110 120 130 140 150
FFQNLGIRCV KKKEVKGAII LRISAGINPF NVGEQQLLDI EDCDLNVVRC
160 170 180 190 200
VFMFFLPDED GNFTTALPPI VSNPIYDNRA PNTAELRICR VNKNCGSVRG
210 220 230 240 250
GDEIFLLCDK VQKDDIEVRF VLNDWEARGV FSQADVHRQV AIVFKTPPYC
260 270 280 290 300
KAILEPVTVK MQLRRPSDQE VSESMDFRYL PDEKDAYGNK SKKQKTTLIF
310 320 330 340 350
QKLLQDCGHF TEKPRTAPLG STGEGRFIKK ESNLFSHGTV LPEMPRSSGV
360 370 380 390 400
PGQAEPYYSS CGSISSGLPH HPPAIPSVAH QPTSWPPVTH PTSHPVSTNT
410 420 430 440 450
LSTFSAGTLS SNSQGILPFL EGPGVSDLSA SNSCLYNPDD LARMETPSMS
460 470 480 490 500
PTDLYSISDV NMLSTRPLSV MAPSTDGMGD TDNPRLVSIN LENPSCNARL
510 520 530 540 550
GPRDLRQLHQ MSPASLSAGT SSSSVFVSQS DAFDRSNFSC VDNGLMNEPG
560 570 580
LSDDANNPTF VQSSHYSVNT LQSEQLSDPF TYGFFKI
Length:587
Mass (Da):64,960
Last modified:October 1, 1994 - v2
Checksum:i98FC237B6D140416
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171G → E(PubMed:2204816)Curated
Sequence conflicti133 – 1331G → P(PubMed:2204816)Curated
Sequence conflicti150 – 1545CVFMF → LCFQV(PubMed:2204816)Curated
Sequence conflicti160 – 1601D → H(PubMed:2204816)Curated
Sequence conflicti567 – 5671S → SS(PubMed:2204816)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15842 mRNA. Translation: CAA33843.1. Sequence problems.
X60271 mRNA. Translation: CAA42817.1.
PIRiA60367.
UniGeneiMm.4869.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X15842 mRNA. Translation: CAA33843.1. Sequence problems.
X60271 mRNA. Translation: CAA42817.1.
PIRiA60367.
UniGeneiMm.4869.

3D structure databases

ProteinModelPortaliP15307.
SMRiP15307. Positions 8-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-59241N.
IntActiP15307. 2 interactions.

PTM databases

PhosphoSiteiP15307.

Proteomic databases

MaxQBiP15307.
PaxDbiP15307.
PRIDEiP15307.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

MGIiMGI:97897. Rel.

Phylogenomic databases

eggNOGiNOG119056.
HOVERGENiHBG017916.
InParanoidiP15307.

Miscellaneous databases

ChiTaRSiRel. mouse.
PROiP15307.
SOURCEiSearch...

Gene expression databases

CleanExiMM_REL.
GenevestigatoriP15307.

Family and domain databases

Gene3Di2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamiPF00554. RHD. 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. "Structure of a mammalian c-rel protein deduced from the nucleotide sequence of murine cDNA clones."
    Grumont R.J., Gerondakis S.
    Oncogene Res. 4:1-8(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
    Tissue: Spleen.
  2. "The murine c-rel proto-oncogene encodes two mRNAs the expression of which is modulated by lymphoid stimuli."
    Grumont R.J., Gerondakis S.
    Oncogene Res. 5:245-254(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "The mouse c-rel protein has an N-terminal regulatory domain and a C-terminal transcriptional transactivation domain."
    Bull P., Morley K.L., Hoekstra M.F., Hunter T., Verma I.M.
    Mol. Cell. Biol. 10:5473-5485(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. "Role of unphosphorylated, newly synthesized IkappaB beta in persistent activation of NF-kappaB."
    Suyang H., Phillips R.J., Douglas I., Ghosh S.
    Mol. Cell. Biol. 16:5444-5449(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBIB.

Entry informationi

Entry nameiREL_MOUSE
AccessioniPrimary (citable) accession number: P15307
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 1, 1994
Last modified: February 4, 2015
This is version 117 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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.