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Q04864

- REL_HUMAN

UniProt

Q04864 - REL_HUMAN

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Protein

Proto-oncogene c-Rel

Gene

REL

Organism
Homo sapiens (Human)
Status
Reviewed - 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.

GO - Molecular functioni

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

GO - Biological processi

  1. cytokine production Source: Ensembl
  2. I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  3. negative regulation of neuron death Source: Ensembl
  4. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  5. positive regulation of interleukin-12 biosynthetic process Source: Ensembl
  6. positive regulation of transcription from RNA polymerase II promoter Source: NTNU_SB
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118656. Activation of NF-kappaB in B cells.
SignaLinkiQ04864.

Names & Taxonomyi

Protein namesi
Recommended name:
Proto-oncogene c-Rel
Gene namesi
Name:REL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:9954. REL.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleoplasm Source: Reactome
  3. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA34321.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 619618Proto-oncogene c-RelPRO_0000205165Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei267 – 2671Phosphoserine; by PKASequence Analysis
Modified residuei503 – 5031Phosphoserine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ04864.
PaxDbiQ04864.
PRIDEiQ04864.

PTM databases

PhosphoSiteiQ04864.

Expressioni

Gene expression databases

BgeeiQ04864.
CleanExiHS_REL.
ExpressionAtlasiQ04864. baseline and differential.
GenevestigatoriQ04864.

Organism-specific databases

HPAiCAB004404.

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 (By similarity). Interacts with NKIRAS1. Interacts with NFKBIB (By similarity). Interacts with NFKBIE.By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COMMD1Q8N6683EBI-307352,EBI-1550112
NFKB2Q006533EBI-307352,EBI-307326

Protein-protein interaction databases

BioGridi111898. 51 interactions.
DIPiDIP-301N.
IntActiQ04864. 19 interactions.
MINTiMINT-1137552.
STRINGi9606.ENSP00000295025.

Structurei

3D structure databases

ProteinModelPortaliQ04864.
SMRiQ04864. Positions 8-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi290 – 2956Nuclear localization signalSequence Analysis

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiNOG119056.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000264257.
HOVERGENiHBG017916.
InParanoidiQ04864.
KOiK09254.
OMAiWEAKGIF.
OrthoDBiEOG7VHSWT.
PhylomeDBiQ04864.
TreeFamiTF325632.

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]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q04864-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASGAYNPYI EIIEQPRQRG MRFRYKCEGR SAGSIPGEHS TDNNRTYPSI
60 70 80 90 100
QIMNYYGKGK VRITLVTKND PYKPHPHDLV GKDCRDGYYE AEFGQERRPL
110 120 130 140 150
FFQNLGIRCV KKKEVKEAII TRIKAGINPF NVPEKQLNDI EDCDLNVVRL
160 170 180 190 200
CFQVFLPDEH GNLTTALPPV VSNPIYDNRA PNTAELRICR VNKNCGSVRG
210 220 230 240 250
GDEIFLLCDK VQKDDIEVRF VLNDWEAKGI FSQADVHRQV AIVFKTPPYC
260 270 280 290 300
KAITEPVTVK MQLRRPSDQE VSESMDFRYL PDEKDTYGNK AKKQKTTLLF
310 320 330 340 350
QKLCQDHVET GFRHVDQDGL ELLTSGDPPT LASQSAGITV NFPERPRPGL
360 370 380 390 400
LGSIGEGRYF KKEPNLFSHD AVVREMPTGV SSQAESYYPS PGPISSGLSH
410 420 430 440 450
HASMAPLPSS SWSSVAHPTP RSGNTNPLSS FSTRTLPSNS QGIPPFLRIP
460 470 480 490 500
VGNDLNASNA CIYNNADDIV GMEASSMPSA DLYGISDPNM LSNCSVNMMT
510 520 530 540 550
TSSDSMGETD NPRLLSMNLE NPSCNSVLDP RDLRQLHQMS SSSMSAGANS
560 570 580 590 600
NTTVFVSQSD AFEGSDFSCA DNSMINESGP SNSTNPNSHG FVQDSQYSGI
610
GSMQNEQLSD SFPYEFFQV
Length:619
Mass (Da):68,520
Last modified:June 1, 1994 - v1
Checksum:i03E1033BDF7B1B30
GO
Isoform 2 (identifier: Q04864-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     308-339: Missing.

Note: No experimental confirmation available.

Show »
Length:587
Mass (Da):65,225
Checksum:iE312A59CF1D306A2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei308 – 33932Missing in isoform 2. 1 PublicationVSP_055857Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75042 mRNA. Translation: CAA52954.1.
DQ314888 Genomic DNA. Translation: ABC40747.1.
AC010733 Genomic DNA. No translation available.
BC117191 mRNA. Translation: AAI17192.1.
BC143885 mRNA. Translation: AAI43886.1.
M11595 Genomic DNA. Translation: AAA52073.1.
CCDSiCCDS1864.1. [Q04864-1]
CCDS74515.1. [Q04864-2]
PIRiA60646.
RefSeqiNP_001278675.1. NM_001291746.1. [Q04864-2]
NP_002899.1. NM_002908.3. [Q04864-1]
UniGeneiHs.631886.
Hs.633256.

Genome annotation databases

EnsembliENST00000295025; ENSP00000295025; ENSG00000162924. [Q04864-1]
ENST00000394479; ENSP00000377989; ENSG00000162924. [Q04864-2]
GeneIDi5966.
KEGGihsa:5966.
UCSCiuc002sam.1. human. [Q04864-1]

Polymorphism databases

DMDMi548720.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X75042 mRNA. Translation: CAA52954.1 .
DQ314888 Genomic DNA. Translation: ABC40747.1 .
AC010733 Genomic DNA. No translation available.
BC117191 mRNA. Translation: AAI17192.1 .
BC143885 mRNA. Translation: AAI43886.1 .
M11595 Genomic DNA. Translation: AAA52073.1 .
CCDSi CCDS1864.1. [Q04864-1 ]
CCDS74515.1. [Q04864-2 ]
PIRi A60646.
RefSeqi NP_001278675.1. NM_001291746.1. [Q04864-2 ]
NP_002899.1. NM_002908.3. [Q04864-1 ]
UniGenei Hs.631886.
Hs.633256.

3D structure databases

ProteinModelPortali Q04864.
SMRi Q04864. Positions 8-282.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111898. 51 interactions.
DIPi DIP-301N.
IntActi Q04864. 19 interactions.
MINTi MINT-1137552.
STRINGi 9606.ENSP00000295025.

PTM databases

PhosphoSitei Q04864.

Polymorphism databases

DMDMi 548720.

Proteomic databases

MaxQBi Q04864.
PaxDbi Q04864.
PRIDEi Q04864.

Protocols and materials databases

DNASUi 5966.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000295025 ; ENSP00000295025 ; ENSG00000162924 . [Q04864-1 ]
ENST00000394479 ; ENSP00000377989 ; ENSG00000162924 . [Q04864-2 ]
GeneIDi 5966.
KEGGi hsa:5966.
UCSCi uc002sam.1. human. [Q04864-1 ]

Organism-specific databases

CTDi 5966.
GeneCardsi GC02P061108.
HGNCi HGNC:9954. REL.
HPAi CAB004404.
MIMi 164910. gene.
neXtProti NX_Q04864.
PharmGKBi PA34321.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG119056.
GeneTreei ENSGT00500000044765.
HOGENOMi HOG000264257.
HOVERGENi HBG017916.
InParanoidi Q04864.
KOi K09254.
OMAi WEAKGIF.
OrthoDBi EOG7VHSWT.
PhylomeDBi Q04864.
TreeFami TF325632.

Enzyme and pathway databases

Reactomei REACT_118656. Activation of NF-kappaB in B cells.
SignaLinki Q04864.

Miscellaneous databases

GeneWikii REL.
GenomeRNAii 5966.
NextBioi 23226.
PROi Q04864.
SOURCEi Search...

Gene expression databases

Bgeei Q04864.
CleanExi HS_REL.
ExpressionAtlasi Q04864. baseline and differential.
Genevestigatori Q04864.

Family and domain databases

Gene3Di 2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProi IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view ]
Pfami PF00554. RHD. 1 hit.
[Graphical view ]
PRINTSi PR00057. NFKBTNSCPFCT.
SMARTi SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A human rel proto-oncogene cDNA containing an Alu fragment as a potential coding exon."
    Brownell E., Mittereder N., Rice N.R.
    Oncogene 4:935-942(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Colon.
  5. "Genetic characterization of human c-rel sequences."
    Brownell E., O'Brien S.J., Nash W.G., Rice N.R.
    Mol. Cell. Biol. 5:2826-2831(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 180-284.
  6. "A novel complex between the p65 subunit of NF-kappa B and c-Rel binds to a DNA element involved in the phorbol ester induction of the human urokinase gene."
    Hansen S.K., Nerlov C., Zabel U., Verde P., Johnsen M., Baeuerle P.A., Blasi F.
    EMBO J. 11:205-213(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
  7. "Activation of multiple NF-kappa B/Rel DNA-binding complexes by tumor necrosis factor."
    Beg A.A., Baldwin A.S. Jr.
    Oncogene 9:1487-1492(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P52-C-REL COMPLEX, IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
  8. "Regulation of intercellular adhesion molecule-1 gene by tumor necrosis factor-alpha is mediated by the nuclear factor-kappaB heterodimers p65/p65 and p65/c-Rel in the absence of p50."
    Aoudjit F., Brochu N., Belanger B., Stratowa C., Hiscott J., Audette M.
    Cell Growth Differ. 8:335-342(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P65-C-REL COMPLEX.
  9. "A new member of the IkappaB protein family, IkappaB epsilon, inhibits RelA (p65)-mediated NF-kappaB transcription."
    Li Z., Nabel G.J.
    Mol. Cell. Biol. 17:6184-6190(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NFKBIE.
  10. "Tumor necrosis factor-alpha activation of NF-kappa B requires the phosphorylation of Ser-471 in the transactivation domain of c-Rel."
    Martin A.G., Fresno M.
    J. Biol. Chem. 275:24383-24391(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-503.
  11. "Leishmania major amastigotes induce p50/c-Rel NF-kappa B transcription factor in human macrophages: involvement in cytokine synthesis."
    Guizani-Tabbane L., Ben-Aissa K., Belghith M., Sassi A., Dellagi K.
    Infect. Immun. 72:2582-2589(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NF-KAPPA-B P50-C-REL COMPLEX.
  12. "Inhibition of NF-kappaB activity by IkappaBbeta in association with kappaB-Ras."
    Chen Y., Vallee S., Wu J., Vu D., Sondek J., Ghosh G.
    Mol. Cell. Biol. 24:3048-3056(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NKIRAS1.
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiREL_HUMAN
AccessioniPrimary (citable) accession number: Q04864
Secondary accession number(s): Q17RU2, Q2PNZ7, Q6LDY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: October 29, 2014
This is version 137 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3