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P15307 (REL_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 112. 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

Names and origin

Protein namesRecommended name:
Proto-oncogene c-Rel
Gene names
Name:Rel
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length587 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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

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. Ref.4

Subcellular location

Nucleus.

Sequence similarities

Contains 1 RHD (Rel-like) domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 587586Proto-oncogene c-Rel
PRO_0000205166

Regions

Domain8 – 297290RHD
Region403 – 46866Transriptional transactivator
Motif291 – 2966Nuclear localization signal Potential

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue2671Phosphoserine; by PKA Potential

Experimental info

Sequence conflict1171G → E Ref.3
Sequence conflict1331G → P Ref.3
Sequence conflict150 – 1545CVFMF → LCFQV Ref.3
Sequence conflict1601D → H Ref.3
Sequence conflict5671S → SS Ref.3

Sequences

Sequence LengthMass (Da)Tools
P15307 [UniParc].

Last modified October 1, 1994. Version 2.
Checksum: 98FC237B6D140416

FASTA58764,960
        10         20         30         40         50         60 
MASSGYNPYV EIIEQPRQRG MRFRYKCEGR SAGSIPGERS TDNNRTYPSV QIMNYYGKGK 

        70         80         90        100        110        120 
IRITLVTKND PYKPHPHDLV GKDCRDGYYE AEFGPERRPL FFQNLGIRCV KKKEVKGAII 

       130        140        150        160        170        180 
LRISAGINPF NVGEQQLLDI EDCDLNVVRC VFMFFLPDED GNFTTALPPI VSNPIYDNRA 

       190        200        210        220        230        240 
PNTAELRICR VNKNCGSVRG GDEIFLLCDK VQKDDIEVRF VLNDWEARGV FSQADVHRQV 

       250        260        270        280        290        300 
AIVFKTPPYC KAILEPVTVK MQLRRPSDQE VSESMDFRYL PDEKDAYGNK SKKQKTTLIF 

       310        320        330        340        350        360 
QKLLQDCGHF TEKPRTAPLG STGEGRFIKK ESNLFSHGTV LPEMPRSSGV PGQAEPYYSS 

       370        380        390        400        410        420 
CGSISSGLPH HPPAIPSVAH QPTSWPPVTH PTSHPVSTNT LSTFSAGTLS SNSQGILPFL 

       430        440        450        460        470        480 
EGPGVSDLSA SNSCLYNPDD LARMETPSMS PTDLYSISDV NMLSTRPLSV MAPSTDGMGD 

       490        500        510        520        530        540 
TDNPRLVSIN LENPSCNARL GPRDLRQLHQ MSPASLSAGT SSSSVFVSQS DAFDRSNFSC 

       550        560        570        580 
VDNGLMNEPG LSDDANNPTF VQSSHYSVNT LQSEQLSDPF TYGFFKI 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15842 mRNA. Translation: CAA33843.1. Sequence problems.
X60271 mRNA. Translation: CAA42817.1.
PIRA60367.
UniGeneMm.4869.

3D structure databases

ProteinModelPortalP15307.
SMRP15307. Positions 8-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-59241N.
IntActP15307. 2 interactions.

PTM databases

PhosphoSiteP15307.

Proteomic databases

PaxDbP15307.
PRIDEP15307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:97897. Rel.

Phylogenomic databases

eggNOGNOG119056.
HOVERGENHBG017916.
InParanoidP15307.

Gene expression databases

CleanExMM_REL.
GenevestigatorP15307.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProIPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamPF00554. RHD. 1 hit.
[Graphical view]
PRINTSPR00057. NFKBTNSCPFCT.
SMARTSM00429. IPT. 1 hit.
[Graphical view]
SUPFAMSSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEPS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP15307.
SOURCESearch...

Entry information

Entry nameREL_MOUSE
AccessionPrimary (citable) accession number: P15307
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 1, 1994
Last modified: June 11, 2014
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot