Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Nuclear factor NF-kappa-B p105 subunit

Gene

NFKB1

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

P105 is the precursor of the p50 subunit of the nuclear factor NF-kappa-B, which binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions. The precursor protein itself does not bind to DNA.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-GGA-1169091. Activation of NF-kappaB in B cells.
R-GGA-1227892. TRAF6 mediated NF-kB activation.
R-GGA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-GGA-434001. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-GGA-434131. NFkB activation mediated by RIP1 complexed with activated TLR3.
R-GGA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor NF-kappa-B p105 subunit
Alternative name(s):
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1
Cleaved into the following chain:
Gene namesi
Name:NFKB1
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Chromosome 4

Subcellular locationi

  • Nucleus
  • Cytoplasm

  • Note: Nuclear, but also found in the cytoplasm in an inactive form complexed to an inhibitor (I-kappa-B).

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 983983Nuclear factor NF-kappa-B p105 subunitPRO_0000030316Add
BLAST
Chaini1 – ?Nuclear factor NF-kappa-B p50 subunitBy similarityPRO_0000030317

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661S-nitrosocysteineBy similarity
Modified residuei342 – 3421Phosphoserine; by PKASequence analysis
Modified residuei938 – 9381PhosphoserineBy similarity

Post-translational modificationi

While translation occurs, the particular unfolded structure after the GRR repeat promotes the generation of p50 making it an acceptable substrate for the proteasome. This process is known as cotranslational processing. The processed form is active and the unprocessed form acts as an inhibitor (I kappa B-like), being able to form cytosolic complexes with NF-kappa B, trapping it in the cytoplasm. Complete folding of the region downstream of the GRR repeat precludes processing (By similarity).By similarity
S-nitrosylation of Cys-66 affects DNA binding.By similarity

Keywords - PTMi

Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiQ04861.

Interactioni

Subunit structurei

Active NF-kappa-B is a heterodimer of an about 50 kDa DNA-binding subunit and the weak DNA-binding subunit p65. Two heterodimers might form a labile tetramer.

GO - Molecular functioni

  • NF-kappaB binding Source: UniProtKB

Protein-protein interaction databases

STRINGi9031.ENSGALP00000020084.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini47 – 372326RHDPROSITE-ProRule annotationAdd
BLAST
Repeati540 – 56930ANK 1Add
BLAST
Repeati579 – 60830ANK 2Add
BLAST
Repeati612 – 64130ANK 3Add
BLAST
Repeati648 – 67730ANK 4Add
BLAST
Repeati682 – 71231ANK 5Add
BLAST
Repeati716 – 74530ANK 6Add
BLAST
Repeati769 – 79931ANK 7Add
BLAST
Domaini804 – 89188DeathAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni377 – 39721GRRAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi365 – 3706Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi378 – 41437Gly-richAdd
BLAST

Domaini

The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding by p50 homodimers, and/or transcription activation.

Sequence similaritiesi

Contains 7 ANK repeats.PROSITE-ProRule annotation
Contains 1 death domain.Curated
Contains 1 RHD (Rel-like) domain.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000004822.
HOVERGENiHBG052613.
InParanoidiQ04861.
KOiK02580.
OMAiDHPNGEG.
OrthoDBiEOG7W154S.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR030503. NF-kB_p105.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030492. RHD_CS.
IPR032397. RHD_dimer.
IPR011539. RHD_DNA_bind_dom.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 2 hits.
PTHR24169:SF9. PTHR24169:SF9. 2 hits.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF00531. Death. 1 hit.
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00248. ANK. 7 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q04861-1) [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
MAGEDPYIMG VSDPQMFAMD QLMGMSTIFN NTGYITSDLP LRTADGPYLQ
60 70 80 90 100
IIEQPKQRGF RFRYVCEGPS HGGLPGASSE KNKKSYPQVK ICNYVGPAKV
110 120 130 140 150
IVQLVTNGKY VHLHAHSLVG KFCEDGVCTV NAGPKDMVVG FANLGILHVT
160 170 180 190 200
KKKVFETLET RMIDACKKGY NPGLLVHPEL GYLQAEGCGD RQLTEREREI
210 220 230 240 250
IRQAAVQQTK EMDLSVVRLM FTAFLPDSNG GFTRRLDPVI SDAIYDSKAP
260 270 280 290 300
NASNLKIVRM DRTAGCVTGG EEIYLLCDKV QKDDIQIRFY EEDENGGMWE
310 320 330 340 350
GFGDFSPTDV HRQFAIVFKT PKYRDVNITK PASVFVQLRR KSDLETSEPK
360 370 380 390 400
PFLYYPEIKD KEEVQRKRQK LMPNFSDGYG GGSGAGGGGM FGGGGGGAGS
410 420 430 440 450
GFSYPSYGYS AFGGMHFHPG TTKSNAGMKH ELSNSTVKKD EESSDKQSDK
460 470 480 490 500
WDTKHDVKVE TVEKNECRTS GHNEEKEDAS LCCKDEGNKP KCGCQDGLFL
510 520 530 540 550
EKAMQLAKRH CNALFDYAVT GDVRMLLAVQ RHLTAVQDDN GDNVLHLSII
560 570 580 590 600
HLHRELVKNL LEVMPDMNYN NIINMRNDLY QTPLHLAVIT KQAEVVEDLL
610 620 630 640 650
KAGANVNLLD RHGNSVLHLA AAEGDDKILS LLLKHQKASS MIDLSNGEGL
660 670 680 690 700
SAIHMVVTAN SLSCLKLLIA AGVDVNAQEQ KSGRTALHLA VEQENVPLAG
710 720 730 740 750
CLLLEGDADV DSTTYDGTTP LHIAAGRGFT KLAAVLKAAG ADPHVENFEP
760 770 780 790 800
LFDVEEDVKD DDDDEGIVPG TTPLDMAANW EVYDILNGKP YIAAAAVSED
810 820 830 840 850
LLSQGPLREL NESSKQQLYK LLETPDPSKN WSTLAEKLGL GILNNAFRLS
860 870 880 890 900
PSPSKTLLDN YKISGGTVQE LIAALTQMDH TEAIEVIQKA LSSSQRQSHQ
910 920 930 940 950
EDNTIEAFPS LSPTSFAKEE TGELYNHKFQ DPESTCDSGV ETSFRKLSFT
960 970 980
YSDSLNSKSS ITLSKMTLGY RKAQCKAVIY LTR
Length:983
Mass (Da):107,992
Last modified:April 18, 2012 - v2
Checksum:iB8885C7716393285
GO
Isoform 2 (identifier: Q04861-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     970-970: Y → YG

Show »
Length:984
Mass (Da):108,049
Checksum:i2393F098A129B72C
GO
Isoform 3 (identifier: Q04861-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     971-983: RKAQCKAVIYLTR → GQESSVQSSYIPN

Show »
Length:983
Mass (Da):107,838
Checksum:i259C140FE1DF5994
GO

Sequence cautioni

The sequence AAB58343.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated
The sequence AAB58343.1 differs from that shown. Reason: Erroneous translation. Wrong genetic code used for translating the sequence.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111V → R in AAA49000 (PubMed:1533881).Curated
Sequence conflicti513 – 5131A → R in AAA49000 (PubMed:1533881).Curated
Sequence conflicti513 – 5131A → R in AAB58343 (PubMed:9233775).Curated
Sequence conflicti696 – 6961V → I in BAA02872 (PubMed:7916720).Curated
Sequence conflicti708 – 7103ADV → VDA in BAA02872 (PubMed:7916720).Curated
Sequence conflicti774 – 7741L → H in AAB58343 (PubMed:9233775).Curated
Sequence conflicti848 – 8481R → Q in AAA49000 (PubMed:1533881).Curated
Sequence conflicti868 – 8681V → G in AAA49000 (PubMed:1533881).Curated
Sequence conflicti875 – 8751L → F in AAA49000 (PubMed:1533881).Curated
Sequence conflicti898 – 8992SH → IY in BAA02872 (PubMed:7916720).Curated
Sequence conflicti903 – 9031N → K in AAA49000 (PubMed:1533881).Curated
Sequence conflicti938 – 9381S → T in AAB58343 (PubMed:9233775).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei970 – 9701Y → YG in isoform 2. 2 PublicationsVSP_042871
Alternative sequencei971 – 98313RKAQC…IYLTR → GQESSVQSSYIPN in isoform 3. 1 PublicationVSP_042872Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86930 mRNA. Translation: AAA49000.1.
D13719 mRNA. Translation: BAA02872.1.
AF000241 mRNA. Translation: AAB58343.1. Sequence problems.
AADN02031451 Genomic DNA. No translation available.
PIRiA41996.
RefSeqiNP_990465.1. NM_205134.1.
XP_015140901.1. XM_015285415.1. [Q04861-3]
UniGeneiGga.3531.

Genome annotation databases

EnsembliENSGALT00000037607; ENSGALP00000036814; ENSGALG00000012304. [Q04861-3]
GeneIDi396033.
KEGGigga:396033.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M86930 mRNA. Translation: AAA49000.1.
D13719 mRNA. Translation: BAA02872.1.
AF000241 mRNA. Translation: AAB58343.1. Sequence problems.
AADN02031451 Genomic DNA. No translation available.
PIRiA41996.
RefSeqiNP_990465.1. NM_205134.1.
XP_015140901.1. XM_015285415.1. [Q04861-3]
UniGeneiGga.3531.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000020084.

Proteomic databases

PaxDbiQ04861.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSGALT00000037607; ENSGALP00000036814; ENSGALG00000012304. [Q04861-3]
GeneIDi396033.
KEGGigga:396033.

Organism-specific databases

CTDi4790.

Phylogenomic databases

eggNOGiKOG0504. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000004822.
HOVERGENiHBG052613.
InParanoidiQ04861.
KOiK02580.
OMAiDHPNGEG.
OrthoDBiEOG7W154S.

Enzyme and pathway databases

ReactomeiR-GGA-1169091. Activation of NF-kappaB in B cells.
R-GGA-1227892. TRAF6 mediated NF-kB activation.
R-GGA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-GGA-434001. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-GGA-434131. NFkB activation mediated by RIP1 complexed with activated TLR3.
R-GGA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.

Miscellaneous databases

NextBioi20816095.
PROiQ04861.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
IPR013783. Ig-like_fold.
IPR014756. Ig_E-set.
IPR002909. IPT.
IPR030503. NF-kB_p105.
IPR000451. NFkB/Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR030492. RHD_CS.
IPR032397. RHD_dimer.
IPR011539. RHD_DNA_bind_dom.
[Graphical view]
PANTHERiPTHR24169. PTHR24169. 2 hits.
PTHR24169:SF9. PTHR24169:SF9. 2 hits.
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
PF00531. Death. 1 hit.
PF16179. RHD_dimer. 1 hit.
PF00554. RHD_DNA_bind. 1 hit.
[Graphical view]
PRINTSiPR00057. NFKBTNSCPFCT.
SMARTiSM00248. ANK. 7 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "p105, the NF-kappa B p50 precursor protein, is one of the cellular proteins complexed with the v-Rel oncoprotein in transformed chicken spleen cells."
    Capobianco A.J., Chang D., Mosialos G., Gilmore T.D.
    J. Virol. 66:3758-3767(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  2. "Isolation of the chicken NF-kappa B p65 subunit-encoding cDNA and characterization of its products."
    Ikeda T., Honjo K., Hirota Y., Onodera T.
    Gene 133:237-242(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
    Tissue: Spleen.
  3. "Transcriptional and post-transcriptional regulation of kappaB-controlled genes by pp60v-src."
    Cabannes E., Vives M.F., Bedard P.A.
    Oncogene 15:29-43(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Embryonic fibroblast.
  4. "Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution."
    Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A.
    , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K.
    Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Red jungle fowl.

Entry informationi

Entry nameiNFKB1_CHICK
AccessioniPrimary (citable) accession number: Q04861
Secondary accession number(s): E1C613, F1NU28, O13075
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: April 18, 2012
Last modified: May 11, 2016
This is version 136 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. 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.