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Protein
Submitted name:

Protein Rela

Gene

Rela

Organism
Rattus norvegicus (Rat)
Status
Unreviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

GO - Biological processi

  • acetaldehyde metabolic process Source: RGD
  • aging Source: RGD
  • cellular response to hydrogen peroxide Source: Ensembl
  • cellular response to interleukin-1 Source: Ensembl
  • cellular response to interleukin-6 Source: Ensembl
  • cellular response to lipopolysaccharide Source: RGD
  • cellular response to nicotine Source: Ensembl
  • cellular response to peptide hormone stimulus Source: Ensembl
  • cellular response to tumor necrosis factor Source: Ensembl
  • cytokine-mediated signaling pathway Source: Ensembl
  • hair follicle development Source: Ensembl
  • I-kappaB kinase/NF-kappaB signaling Source: GO_Central
  • inflammatory response Source: GO_Central
  • innate immune response Source: GO_Central
  • liver development Source: Ensembl
  • negative regulation of extrinsic apoptotic signaling pathway Source: Ensembl
  • negative regulation of insulin receptor signaling pathway Source: RGD
  • negative regulation of protein catabolic process Source: Ensembl
  • negative regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • NIK/NF-kappaB signaling Source: GO_Central
  • nucleotide-binding oligomerization domain containing 2 signaling pathway Source: Ensembl
  • organ morphogenesis Source: Ensembl
  • positive regulation of cell proliferation Source: RGD
  • positive regulation of chondrocyte differentiation Source: RGD
  • positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Ensembl
  • positive regulation of interleukin-12 biosynthetic process Source: Ensembl
  • positive regulation of miRNA metabolic process Source: Ensembl
  • positive regulation of NF-kappaB transcription factor activity Source: Ensembl
  • positive regulation of Schwann cell differentiation Source: RGD
  • positive regulation of transcription from RNA polymerase II promoter Source: GO_Central
  • regulation of inflammatory response Source: Ensembl
  • response to amino acid Source: RGD
  • response to cAMP Source: RGD
  • response to cobalamin Source: RGD
  • response to cytokine Source: RGD
  • response to drug Source: RGD
  • response to hydrogen peroxide Source: RGD
  • response to inorganic substance Source: RGD
  • response to insulin Source: RGD
  • response to lipopolysaccharide Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to morphine Source: RGD
  • response to muramyl dipeptide Source: Ensembl
  • response to organic cyclic compound Source: RGD
  • response to organic substance Source: RGD
  • response to progesterone Source: RGD
  • response to UV-B Source: Ensembl
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_278187. FCERI mediated NF-kB activation.
REACT_281972. Regulated proteolysis of p75NTR.
REACT_309187. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
REACT_318052. Activation of NF-kappaB in B cells.
REACT_324145. Senescence-Associated Secretory Phenotype (SASP).
REACT_327898. Interleukin-1 processing.
REACT_332189. RIP-mediated NFkB activation via ZBP1.
REACT_332863. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_336922. TRAF6 mediated NF-kB activation.
REACT_342970. Downstream TCR signaling.
REACT_348171. NF-kB is activated and signals survival.
REACT_359478. CD209 (DC-SIGN) signaling.
REACT_359556. CLEC7A (Dectin-1) signaling.

Names & Taxonomyi

Protein namesi
Submitted name:
Protein RelaImported
Submitted name:
RELAImported
Submitted name:
V-rel reticuloendotheliosis viral oncogene homolog A (Avian)Imported
Gene namesi
Name:RelaImported
Synonyms:RelAImported
ORF Names:rCG_48632Imported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 1

Organism-specific databases

RGDi727889. Rela.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: RGD
  • cytosol Source: RGD
  • I-kappaB/NF-kappaB complex Source: GO_Central
  • NF-kappaB complex Source: InterPro
  • nucleoplasm Source: GO_Central
  • nucleus Source: RGD
  • protein complex Source: RGD
  • transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

NucleusUniRule annotation

Interactioni

Protein-protein interaction databases

DIPiDIP-38953N.
STRINGi10116.ENSRNOP00000044552.

Family & Domainsi

Sequence similaritiesi

Contains 1 RHD (Rel-like) domain.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00500000044765.
HOGENOMiHOG000230474.
HOVERGENiHBG017916.
KOiK04735.
OMAiEFSPMVF.
OrthoDBiEOG7VHSWT.
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. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030495. RelA.
IPR011539. RHD.
IPR030492. RHD_CS.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF1. PTHR24169:SF1. 1 hit.
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.

Q7TQN4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDDLFPLIFP SEPAQASGPY VEIIEQPKQR GMRFRYKCEG RSAGSIPGER
60 70 80 90 100
STDTTKTHPT IKINGYTGPG TVRISLVTKD PPHRPHPHEL VGKDCRDGFY
110 120 130 140 150
EAELCPDRCI HSFQNLGIQC VKKRDLEQAI SQRIQTNNNP FQVPIEEQRG
160 170 180 190 200
DYDLNAVRLC FQVTVRDPSG RPLRLTPVLS HPIFDNRAPN TAELKICRVN
210 220 230 240 250
RNSGSCLGGD EIFLLCDKVQ KEDIEVYFTG PGWEARGSFS QADVHRQVAI
260 270 280 290 300
VFRTPPYADP SLQAPVRVSM QLRRPSDREL SEPMEFQYLP DTDDRHRIEE
310 320 330 340 350
KRKRTYETFK SIMKKSPFNG PTEPRPPPRR IAVPSRGPTS VPKPAPQPYA
360 370 380 390 400
FSTSLSTINF DEFSPMVLPP GQISNQALAL APSSAPVLAQ TMVPSSAMVP
410 420 430 440 450
SLAQPPAPVP VLAPGPPQSL SAPVPKSTQA GEGTLSEALL HLQFDADEDL
460 470 480 490 500
GALLGNNTDP GVFTDLASVD NSEFQQLLNQ GVAMSHSTAE PMLMEYPEAI
510 520 530 540 550
TRLVTGSQRP PDPAPATLGT SGLPNGLSGD EDFSSIADMD FSALLSQISS
Length:550
Mass (Da):60,267
Last modified:October 1, 2003 - v1
Checksum:i2C6A8FD68F667A64
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06009537 Genomic DNA. No translation available.
BC079457 mRNA. Translation: AAH79457.1.
AY307375 mRNA. Translation: AAP72180.1.
CH473953 Genomic DNA. Translation: EDM12513.1.
RefSeqiNP_954888.1. NM_199267.2.
UniGeneiRn.19480.

Genome annotation databases

EnsembliENSRNOT00000045233; ENSRNOP00000044552; ENSRNOG00000030888.
GeneIDi309165.
KEGGirno:309165.
UCSCiRGD:727889. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR06009537 Genomic DNA. No translation available.
BC079457 mRNA. Translation: AAH79457.1.
AY307375 mRNA. Translation: AAP72180.1.
CH473953 Genomic DNA. Translation: EDM12513.1.
RefSeqiNP_954888.1. NM_199267.2.
UniGeneiRn.19480.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-38953N.
STRINGi10116.ENSRNOP00000044552.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000045233; ENSRNOP00000044552; ENSRNOG00000030888.
GeneIDi309165.
KEGGirno:309165.
UCSCiRGD:727889. rat.

Organism-specific databases

CTDi5970.
RGDi727889. Rela.

Phylogenomic databases

GeneTreeiENSGT00500000044765.
HOGENOMiHOG000230474.
HOVERGENiHBG017916.
KOiK04735.
OMAiEFSPMVF.
OrthoDBiEOG7VHSWT.
TreeFamiTF325632.

Enzyme and pathway databases

ReactomeiREACT_278187. FCERI mediated NF-kB activation.
REACT_281972. Regulated proteolysis of p75NTR.
REACT_309187. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
REACT_318052. Activation of NF-kappaB in B cells.
REACT_324145. Senescence-Associated Secretory Phenotype (SASP).
REACT_327898. Interleukin-1 processing.
REACT_332189. RIP-mediated NFkB activation via ZBP1.
REACT_332863. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_336922. TRAF6 mediated NF-kB activation.
REACT_342970. Downstream TCR signaling.
REACT_348171. NF-kB is activated and signals survival.
REACT_359478. CD209 (DC-SIGN) signaling.
REACT_359556. CLEC7A (Dectin-1) signaling.

Miscellaneous databases

NextBioi660308.
PROiQ7TQN4.

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. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030495. RelA.
IPR011539. RHD.
IPR030492. RHD_CS.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 1 hit.
PTHR24169:SF1. PTHR24169:SF1. 1 hit.
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

« Hide 'large scale' publications
  1. "Cloning RelA gene from rat microglia and cortical neurons."
    Mao X., Barger S.W.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: Sprague-DawleyImported.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M.
    , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: LungImported.
  3. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Rat Genome Sequencing Project Consortium
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown NorwayImported.
  4. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  5. Cited for: NUCLEOTIDE SEQUENCE.
    Strain: BNImported.
  6. Ensembl
    Submitted (FEB-2012) to UniProtKB
    Cited for: IDENTIFICATION.
    Strain: Brown NorwayImported.

Entry informationi

Entry nameiQ7TQN4_RAT
AccessioniPrimary (citable) accession number: Q7TQN4
Entry historyi
Integrated into UniProtKB/TrEMBL: October 1, 2003
Last sequence update: October 1, 2003
Last modified: June 24, 2015
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteome, Proteomics identificationCombined sources, Reference proteomeImported

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.