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Protein

Nuclear factor NF-kappa-B p110 subunit

Gene

Rel

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Plays a key role in the humoral immune response. Rel-p68 subunit translocates to the nucleus where it binds to the promoter of the Cecropin A1 gene and probably other antimicrobial peptide genes. I-kappa-B kinase complex (ird5 and key) and PGRP-LC are essential signaling components in transmitting the lipopolysaccharide (LPS) signal leading to cact degradation for NF-kappa-B (rel) activation.4 Publications

GO - Molecular functioni

GO - Biological processi

  • cellular response to amino acid starvation Source: FlyBase
  • cellular response to DNA damage stimulus Source: FlyBase
  • defense response to Gram-negative bacterium Source: FlyBase
  • defense response to virus Source: FlyBase
  • dendrite morphogenesis Source: FlyBase
  • immune response Source: FlyBase
  • innate immune response Source: FlyBase
  • negative regulation of stem cell proliferation Source: FlyBase
  • peptidoglycan recognition protein signaling pathway Source: FlyBase
  • peripheral nervous system neuron development Source: FlyBase
  • positive regulation of antibacterial peptide biosynthetic process Source: UniProtKB
  • positive regulation of antifungal peptide biosynthetic process Source: FlyBase
  • positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria Source: FlyBase
  • positive regulation of defense response to virus by host Source: FlyBase
  • positive regulation of gene expression Source: FlyBase
  • positive regulation of innate immune response Source: FlyBase
  • positive regulation of nitric oxide biosynthetic process Source: FlyBase
  • positive regulation of transcription from RNA polymerase II promoter Source: FlyBase
  • regulation of innate immune response Source: FlyBase
  • response to bacterium Source: FlyBase
  • sensory perception of pain Source: FlyBase
  • signal transduction Source: FlyBase
  • Toll signaling pathway Source: FlyBase
  • transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Immunity, Innate immunity, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1810476. RIP-mediated NFkB activation via ZBP1.
R-DME-202424. Downstream TCR signaling.
R-DME-209560. NF-kB is activated and signals survival.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-DME-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5621575. CD209 (DC-SIGN) signaling.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-933542. TRAF6 mediated NF-kB activation.
SignaLinkiQ94527.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor NF-kappa-B p110 subunit
Alternative name(s):
Rel-p110
Relish protein
Cleaved into the following 2 chains:
Alternative name(s):
Rel-p68
Alternative name(s):
Rel-p49
Gene namesi
Name:Rel
ORF Names:CG11992
OrganismiDrosophila melanogaster (Fruit fly)Imported
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0014018. Rel.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: FlyBase
  • nuclear euchromatin Source: FlyBase
  • nucleus Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi545 – 5451D → A: Completely resistant to cleavage. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 971971Nuclear factor NF-kappa-B p110 subunit1 PublicationPRO_0000030318Add
BLAST
Chaini1 – 545545Nuclear factor NF-kappa-B p68 subunit1 PublicationPRO_0000030319Add
BLAST
Chaini546 – 971426Nuclear factor NF-kappa-B p49 subunit1 PublicationPRO_0000030320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei431 – 4311Phosphoserine; by PKASequence analysis
Modified residuei620 – 6201Phosphothreonine1 Publication
Modified residuei626 – 6261Phosphotyrosine1 Publication
Modified residuei950 – 9501PhosphoserineBy similarity

Post-translational modificationi

Phosphorylated by lipopolysaccharide (LPS)-activated I-kappa-B kinase complex before being cleaved. Rel-p110 subunit is cleaved within seconds of an immune challenge into Rel-p49 subunit and Rel-p68 subunit. Rel-p110 subunit reappears after 45 minutes.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei545 – 5462Cleavage (when cotranslationally processed)1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

PaxDbiQ94527.
PRIDEiQ94527.

PTM databases

iPTMnetiQ94527.

Expressioni

Developmental stagei

Expressed both maternally and zygotically.2 Publications

Inductioni

By bacteria and fungi.1 Publication

Gene expression databases

BgeeiQ94527.
GenevisibleiQ94527. DM.

Interactioni

Subunit structurei

Rel-p68 subunit interacts with Dredd.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
akirinQ9VS594EBI-869024,EBI-96644

Protein-protein interaction databases

BioGridi66255. 101 interactions.
DIPiDIP-60434N.
IntActiQ94527. 2 interactions.
STRINGi7227.FBpp0088375.

Structurei

3D structure databases

ProteinModelPortaliQ94527.
SMRiQ94527. Positions 150-446, 597-809.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 339193RHDPROSITE-ProRule annotationAdd
BLAST
Repeati640 – 66930ANK 1CuratedAdd
BLAST
Repeati673 – 70230ANK 2CuratedAdd
BLAST
Repeati710 – 74031ANK 3CuratedAdd
BLAST
Repeati745 – 77531ANK 4CuratedAdd
BLAST
Repeati783 – 81230ANK 5CuratedAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi452 – 4576Nuclear localization signalSequence analysis

Sequence similaritiesi

Contains 5 ANK repeats.PROSITE-ProRule annotationCurated
Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00500000044765.
InParanoidiQ94527.
KOiK09255.
OMAiMTWIPRK.
OrthoDBiEOG793B70.
PhylomeDBiQ94527.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR032397. RHD_dimer.
IPR011539. RHD_DNA_bind_dom.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 2 hits.
PfamiPF12796. Ank_2. 1 hit.
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00248. ANK. 6 hits.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
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. AlignAdd to basket

Isoform Major1 Publication (identifier: Q94527-1) [UniParc]FASTAAdd to basket

Also known as: A1 Publication

, B, C, p1101 Publication

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
MNMNQYYDLD NGKNVMFMND ASSTSGYSSS TSPNSTNRSF SPAHSPKTME
60 70 80 90 100
LQTDFANLNL PGGNSPHQPP MANSPYQNQL LNNGGICQLG ATNLINSTGV
110 120 130 140 150
SFGVANVTSF GNMYMDHQYF VPAPATVPPS QNFGYHQNGL ASDGDIKHVP
160 170 180 190 200
QLRIVEQPVE KFRFRYKSEM HGTHGSLNGA NSKRTPKTFP EVTLCNYDGP
210 220 230 240 250
AVIRCSLFQT NLDSPHSHQL VVRKDDRDVC DPHDLHVSKE RGYVAQFINM
260 270 280 290 300
GIIHTAKKYI FEELCKKKQD RLVFQMNRRE LSHKQLQELH QETEREAKDM
310 320 330 340 350
NLNQVRLCFE AFKIEDNGAW VPLAPPVYSN AINNRKSAQT GELRIVRLSK
360 370 380 390 400
PTGGVMGNDE LILLVEKVSK KNIKVRFFEE DEDGETVWEA YAKFRESDVH
410 420 430 440 450
HQYAIVCQTP PYKDKDVDRE VNVYIELIRP SDDERSFPAL PFRYKPRSVI
460 470 480 490 500
VSRKRRRTGS SANSSSSGTE SSNNSLDLPK TLGLAQPPNG LPNLSQHDQT
510 520 530 540 550
ISEEFGREKH LNEFIASEDF RKLIEHNSSD LEKICQLDMG ELQHDGHNRA
560 570 580 590 600
EVPSHRNRTI KCLDDLFEIY KQDRISPIKI SHHKVEKWFI EHALNNYNRD
610 620 630 640 650
TLLHEVISHK KDKLKLAIQT IQVMNYFNLK DVVNSTLNAD GDSALHVACQ
660 670 680 690 700
QDRAHYIRPL LGMGCNPNLK NNAGNTPLHV AVKEEHLSCV ESFLNGVPTV
710 720 730 740 750
QLDLSLTNDD GLTPLHMAIR QNKYDVAKKL ISYDRTSISV ANTMDGNNAL
760 770 780 790 800
HMAVLEQSVE LLVLILDAQN ENLTDILQAQ NAAGHTPLEL AERKANDRVV
810 820 830 840 850
QLLKNVYPEK GELAMTWIPC KVKEEIDSSS DESSDAGQLE IKSEEMDIET
860 870 880 890 900
KDEDSVELDL SSGPRRQKDE SSRDTEMDNN KLQLLLKNKF IYDRLCSLLN
910 920 930 940 950
QPLGHGSDPQ DRKWMQLARQ THLKQFAFIW LGAEDLLDHV KRKGASVEFS
960 970
TFARALQAVD PQAYALLVNP T
Length:971
Mass (Da):109,775
Last modified:February 1, 1997 - v1
Checksum:iEAF607357381AD32
GO
Isoform Maternal1 Publication (identifier: Q94527-2) [UniParc]FASTAAdd to basket

Also known as: D1 Publication

, p1001 Publication

The sequence of this isoform differs from the canonical sequence as follows:
     1-112: Missing.

Show »
Length:859
Mass (Da):97,894
Checksum:i1F9784818C642F99
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141Missing in AAF07086 (PubMed:10619029).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti82 – 821N → S in strain: Zim2. 1 Publication
Natural varianti110 – 1101F → L in strain: Zim3. 1 Publication
Natural varianti699 – 6991T → I in strain: Zim8. 1 Publication
Natural varianti845 – 8451E → G in strain: Zim1. 1 Publication
Natural varianti862 – 8621S → N in strain: Zim8. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 112112Missing in isoform Maternal. 1 PublicationVSP_050089Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62005 mRNA. Translation: AAB17264.1.
AF186073 Genomic DNA. Translation: AAF07931.1.
AF186073 Genomic DNA. Translation: AAF07932.1.
AF186077 Genomic DNA. Translation: AAF07086.1.
AF186078 Genomic DNA. Translation: AAF07087.2.
AE014297 Genomic DNA. Translation: AAF54333.2.
AE014297 Genomic DNA. Translation: AAS65130.1.
AE014297 Genomic DNA. Translation: AAS65131.1.
AE014297 Genomic DNA. Translation: AAS65132.1.
AY058264 mRNA. Translation: AAL13493.1.
AF204284 Genomic DNA. Translation: AAF20132.1.
AF204285 Genomic DNA. Translation: AAF20133.1.
AF204286 Genomic DNA. Translation: AAF20134.1.
AF204287 Genomic DNA. Translation: AAF20135.1.
AF204288 Genomic DNA. Translation: AAF20136.1.
AF204289 Genomic DNA. Translation: AAF20137.1.
RefSeqiNP_477094.1. NM_057746.4. [Q94527-1]
NP_996187.1. NM_206465.1. [Q94527-2]
NP_996188.1. NM_206466.1. [Q94527-1]
NP_996189.1. NM_206467.1. [Q94527-1]
UniGeneiDm.4154.

Genome annotation databases

EnsemblMetazoaiFBtr0089338; FBpp0088375; FBgn0014018. [Q94527-1]
FBtr0089339; FBpp0088973; FBgn0014018. [Q94527-1]
FBtr0089340; FBpp0088971; FBgn0014018. [Q94527-1]
GeneIDi41087.
KEGGidme:Dmel_CG11992.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U62005 mRNA. Translation: AAB17264.1.
AF186073 Genomic DNA. Translation: AAF07931.1.
AF186073 Genomic DNA. Translation: AAF07932.1.
AF186077 Genomic DNA. Translation: AAF07086.1.
AF186078 Genomic DNA. Translation: AAF07087.2.
AE014297 Genomic DNA. Translation: AAF54333.2.
AE014297 Genomic DNA. Translation: AAS65130.1.
AE014297 Genomic DNA. Translation: AAS65131.1.
AE014297 Genomic DNA. Translation: AAS65132.1.
AY058264 mRNA. Translation: AAL13493.1.
AF204284 Genomic DNA. Translation: AAF20132.1.
AF204285 Genomic DNA. Translation: AAF20133.1.
AF204286 Genomic DNA. Translation: AAF20134.1.
AF204287 Genomic DNA. Translation: AAF20135.1.
AF204288 Genomic DNA. Translation: AAF20136.1.
AF204289 Genomic DNA. Translation: AAF20137.1.
RefSeqiNP_477094.1. NM_057746.4. [Q94527-1]
NP_996187.1. NM_206465.1. [Q94527-2]
NP_996188.1. NM_206466.1. [Q94527-1]
NP_996189.1. NM_206467.1. [Q94527-1]
UniGeneiDm.4154.

3D structure databases

ProteinModelPortaliQ94527.
SMRiQ94527. Positions 150-446, 597-809.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi66255. 101 interactions.
DIPiDIP-60434N.
IntActiQ94527. 2 interactions.
STRINGi7227.FBpp0088375.

PTM databases

iPTMnetiQ94527.

Proteomic databases

PaxDbiQ94527.
PRIDEiQ94527.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0089338; FBpp0088375; FBgn0014018. [Q94527-1]
FBtr0089339; FBpp0088973; FBgn0014018. [Q94527-1]
FBtr0089340; FBpp0088971; FBgn0014018. [Q94527-1]
GeneIDi41087.
KEGGidme:Dmel_CG11992.

Organism-specific databases

CTDi5966.
FlyBaseiFBgn0014018. Rel.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00500000044765.
InParanoidiQ94527.
KOiK09255.
OMAiMTWIPRK.
OrthoDBiEOG793B70.
PhylomeDBiQ94527.

Enzyme and pathway databases

ReactomeiR-DME-1169091. Activation of NF-kappaB in B cells.
R-DME-1810476. RIP-mediated NFkB activation via ZBP1.
R-DME-202424. Downstream TCR signaling.
R-DME-209560. NF-kB is activated and signals survival.
R-DME-2871837. FCERI mediated NF-kB activation.
R-DME-3134963. DEx/H-box helicases activate type I IFN and inflammatory cytokines production.
R-DME-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-DME-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-DME-5607764. CLEC7A (Dectin-1) signaling.
R-DME-5621575. CD209 (DC-SIGN) signaling.
R-DME-5676590. NIK-->noncanonical NF-kB signaling.
R-DME-933542. TRAF6 mediated NF-kB activation.
SignaLinkiQ94527.

Miscellaneous databases

GenomeRNAii41087.
PROiQ94527.

Gene expression databases

BgeeiQ94527.
GenevisibleiQ94527. DM.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR032397. RHD_dimer.
IPR011539. RHD_DNA_bind_dom.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 2 hits.
PfamiPF12796. Ank_2. 1 hit.
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00248. ANK. 6 hits.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 2 hits.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Origins of immunity: Relish, a compound Rel-like gene in the antibacterial defense of Drosophila."
    Dushay M.S., Asling B., Hultmark D.
    Proc. Natl. Acad. Sci. U.S.A. 93:10343-10347(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAJOR), FUNCTION, DEVELOPMENTAL STAGE.
  2. "Relish, a central factor in the control of humoral, but not cellular immunity in Drosophila."
    Hedengren M., Asling B., Dushay M.S., Ando I., Ekengren S., Wihlborg M., Hultmark D.
    Mol. Cell 4:827-837(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS MAJOR AND MATERNAL), FUNCTION, INDUCTION.
  3. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley1 Publication.
  4. Cited for: GENOME REANNOTATION, ALTERNATIVE SPLICING.
    Strain: Berkeley.
  5. "A Drosophila full-length cDNA resource."
    Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E.
    Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MAJOR).
    Strain: Berkeley1 Publication.
    Tissue: Head1 Publication.
  6. "Adaptive evolution of relish, a Drosophila NF-kappaB/IkappaB protein."
    Begun D.J., Whitley P.
    Genetics 154:1231-1238(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 68-880, VARIANTS SER-82; LEU-110; ILE-699; GLY-845 AND ASN-862.
    Strain: Zim11 Publication, Zim21 Publication, Zim31 Publication, Zim51 Publication, Zim71 Publication and Zim81 Publication.
  7. "Activation of the Drosophila NF-kappaB factor Relish by rapid endoproteolytic cleavage."
    Stoeven S., Ando I., Kadalayil L., Engstrom Y., Hultmark D.
    EMBO Rep. 1:347-352(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 546-553, FUNCTION, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION.
  8. "The Drosophila caspase Dredd is required to resist Gram-negative bacterial infection."
    Leulier F., Rodriguez A., Khush R.S., Abrams J.M., Lemaitre B.
    EMBO Rep. 1:353-358(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, INTERACTION WITH DREDD, MUTAGENESIS OF ASP-545.
  9. "A Drosophila IkappaB kinase complex required for Relish cleavage and antibacterial immunity."
    Silverman N., Zhou R., Stoeven S., Pandey N., Hultmark D., Maniatis T.
    Genes Dev. 14:2461-2471(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  10. "Requirement for a peptidoglycan recognition protein (PGRP) in Relish activation and antibacterial immune responses in Drosophila."
    Choe K.-M., Werner T., Stoeven S., Hultmark D., Anderson K.V.
    Science 296:359-362(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-620 AND TYR-626, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.

Entry informationi

Entry nameiNFKB1_DROME
AccessioniPrimary (citable) accession number: Q94527
Secondary accession number(s): A4V2K3
, Q9U435, Q9U436, Q9U437, Q9U438, Q9U439, Q9U440, Q9U6H3, Q9U6H4, Q9U6H5, Q9VHI0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: February 1, 1997
Last modified: June 8, 2016
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  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.