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P19838

- NFKB1_HUMAN

UniProt

P19838 - NFKB1_HUMAN

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Protein

Nuclear factor NF-kappa-B p105 subunit

Gene

NFKB1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

NF-kappa-B is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes 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 and the heterodimeric p65-p50 complex appears to be most abundant one. 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. NF-kappa-B heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappa-B p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3. NFKB1 appears to have dual functions such as cytoplasmic retention of attached NF-kappa-B proteins by p105 and generation of p50 by a cotranslational processing. The proteasome-mediated process ensures the production of both p50 and p105 and preserves their independent function, although processing of NFKB1/p105 also appears to occur post-translationally. p50 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. In a complex with MAP3K8, NFKB1/p105 represses MAP3K8-induced MAPK signaling; active MAP3K8 is released by proteasome-dependent degradation of NFKB1/p105.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei433 – 4342Cleavage (when cotranslationally processed)

GO - Molecular functioni

  1. double-stranded DNA binding Source: Ensembl
  2. nucleic acid binding transcription factor activity Source: UniProtKB
  3. regulatory region DNA binding Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: ProtInc
  5. transcription factor binding Source: MGI
  6. transcription regulatory region DNA binding Source: BHF-UCL
  7. transcription regulatory region sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  1. apoptotic process Source: UniProtKB-KW
  2. cellular response to interleukin-1 Source: BHF-UCL
  3. cellular response to interleukin-6 Source: BHF-UCL
  4. cellular response to lipopolysaccharide Source: MGI
  5. cellular response to mechanical stimulus Source: UniProtKB
  6. cellular response to nicotine Source: BHF-UCL
  7. cellular response to peptide hormone stimulus Source: BHF-UCL
  8. Fc-epsilon receptor signaling pathway Source: Reactome
  9. inflammatory response Source: UniProtKB
  10. innate immune response Source: Reactome
  11. membrane protein intracellular domain proteolysis Source: Reactome
  12. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
  13. MyD88-independent toll-like receptor signaling pathway Source: Reactome
  14. negative regulation of apoptotic process Source: UniProtKB
  15. negative regulation of calcidiol 1-monooxygenase activity Source: BHF-UCL
  16. negative regulation of cellular protein metabolic process Source: BHF-UCL
  17. negative regulation of cholesterol transport Source: BHF-UCL
  18. negative regulation of cytokine production Source: Ensembl
  19. negative regulation of inflammatory response Source: Ensembl
  20. negative regulation of interleukin-12 biosynthetic process Source: Ensembl
  21. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  22. negative regulation of vitamin D biosynthetic process Source: BHF-UCL
  23. neurotrophin TRK receptor signaling pathway Source: Reactome
  24. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
  25. positive regulation of hyaluronan biosynthetic process Source: UniProtKB
  26. positive regulation of lipid storage Source: BHF-UCL
  27. positive regulation of macrophage derived foam cell differentiation Source: BHF-UCL
  28. positive regulation of miRNA metabolic process Source: BHF-UCL
  29. positive regulation of NF-kappaB transcription factor activity Source: Reactome
  30. positive regulation of transcription, DNA-templated Source: UniProtKB
  31. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  32. positive regulation of type I interferon production Source: Reactome
  33. response to copper ion Source: Ensembl
  34. response to oxidative stress Source: Ensembl
  35. T cell receptor signaling pathway Source: Reactome
  36. toll-like receptor 10 signaling pathway Source: Reactome
  37. toll-like receptor 2 signaling pathway Source: Reactome
  38. toll-like receptor 3 signaling pathway Source: Reactome
  39. toll-like receptor 4 signaling pathway Source: Reactome
  40. toll-like receptor 5 signaling pathway Source: Reactome
  41. toll-like receptor 9 signaling pathway Source: Reactome
  42. toll-like receptor signaling pathway Source: Reactome
  43. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
  44. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
  45. transcription from RNA polymerase II promoter Source: UniProtKB
  46. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_13443. Regulated proteolysis of p75NTR.
REACT_13696. NF-kB is activated and signals survival.
REACT_163994. FCERI mediated NF-kB activation.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_22442. Interleukin-1 signaling.
REACT_23950. Interleukin-1 processing.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinkiP19838.

Names & Taxonomyi

Protein namesi
Recommended name:
Nuclear factor NF-kappa-B p105 subunit
Alternative name(s):
DNA-binding factor KBF1
EBP-1
Nuclear factor of kappa light polypeptide gene enhancer in B-cells 1
Cleaved into the following chain:
Gene namesi
Name:NFKB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 4

Organism-specific databases

HGNCiHGNC:7794. NFKB1.

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

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. I-kappaB/NF-kappaB complex Source: BHF-UCL
  4. mitochondrion Source: HPA
  5. nucleoplasm Source: Reactome
  6. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi61 – 611C → S: Suppresses S-nitrosylation-induced inhibition of DNA-binding activity. Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of DNA-binding activity. 2 Publications
Mutagenesisi678 – 6781N → A: Fails to promote HIF1AN-dependent 2-oxoglutarate decarboxylation. 1 Publication
Mutagenesisi903 – 9031S → A: Prevents p105 proteolysis in response to TNF-alpha. 1 Publication
Mutagenesisi907 – 9071S → A: Prevents p105 proteolysis in response to TNF-alpha. 1 Publication
Mutagenesisi921 – 9211S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-923 and A-932. 1 Publication
Mutagenesisi923 – 9231S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-932. 1 Publication
Mutagenesisi932 – 9321S → A: Decrease in stimuli-induced phosphorylation. Loss of phosphorylation; when associated with A-921 and A-923. 1 Publication

Organism-specific databases

PharmGKBiPA248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 968968Nuclear factor NF-kappa-B p105 subunitPRO_0000030310Add
BLAST
Chaini1 – 433433Nuclear factor NF-kappa-B p50 subunitPRO_0000030311Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611S-nitrosocysteine; alternate1 Publication
Lipidationi61 – 611S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate1 Publication
Modified residuei337 – 3371Phosphoserine; by PKASequence Analysis
Modified residuei431 – 4311N6-acetyllysine; by EP3001 Publication
Modified residuei440 – 4401N6-acetyllysine; by EP3001 Publication
Modified residuei441 – 4411N6-acetyllysine; by EP3001 Publication
Modified residuei678 – 6781(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
Modified residuei903 – 9031Phosphoserine; by GSK3-beta; in vitro1 Publication
Modified residuei907 – 9071Phosphoserine; by GSK3-beta; in vitro1 Publication
Modified residuei927 – 9271Phosphoserine; by IKKB2 Publications
Modified residuei932 – 9321Phosphoserine; by IKKB1 Publication
Modified residuei937 – 9371Phosphoserine1 Publication

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.1 Publication
Phosphorylation at 'Ser-903' and 'Ser-907' primes p105 for proteolytic processing in response to TNF-alpha stimulation. Phosphorylation at 'Ser-927' and 'Ser-932' are required for BTRC/BTRCP-mediated proteolysis.5 Publications
Polyubiquitination seems to allow p105 processing.2 Publications
S-nitrosylation of Cys-61 affects DNA binding.2 Publications
The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation.

Keywords - PTMi

Acetylation, Hydroxylation, Lipoprotein, Phosphoprotein, S-nitrosylation, Ubl conjugation

Proteomic databases

MaxQBiP19838.
PaxDbiP19838.
PRIDEiP19838.

PTM databases

PhosphoSiteiP19838.

Miscellaneous databases

PMAP-CutDBP19838.

Expressioni

Inductioni

By phorbol ester and TNF.

Gene expression databases

BgeeiP19838.
CleanExiHS_NFKB1.
ExpressionAtlasiP19838. baseline and differential.
GenevestigatoriP19838.

Organism-specific databases

HPAiCAB004031.
HPA027305.

Interactioni

Subunit structurei

Component of the NF-kappa-B p65-p50 complex. Component of the NF-kappa-B p65-p50 complex. Homodimer; component of the NF-kappa-B p50-p50 complex. Component of the NF-kappa-B p105-p50 complex. Component of the NF-kappa-B p50-c-Rel complex. Component of a complex consisting of the NF-kappa-B p50-p50 homodimer and BCL3. Also interacts with MAP3K8. NF-kappa-B p50 subunit interacts with NCOA3 coactivator, which may coactivate NF-kappa-B dependent expression via its histone acetyltransferase activity. Interacts with DSIPI; this interaction prevents nuclear translocation and DNA-binding. Interacts with SPAG9 and UNC5CL. NFKB1/p105 interacts with CFLAR; the interaction inhibits p105 processing into p50. NFKB1/p105 forms a ternary complex with MAP3K8 and TNIP2. Interacts with GSK3B; the interaction prevents processing of p105 to p50. NFKB1/p50 interacts with NFKBIE. NFKB1/p50 interacts with NFKBIZ. Nuclear factor NF-kappa-B p50 subunit interacts with NFKBID (By similarity). Directly interacts with MEN1. Interacts with HIF1AN.By similarity17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ABCC2Q928873EBI-300010,EBI-3916193
CTNNB1P352223EBI-300010,EBI-491549
ESR1P033723EBI-697771,EBI-78473
HDAC1Q135475EBI-300010,EBI-301834
MAP3K8P412792EBI-300010,EBI-354900
NFKB2Q006534EBI-300010,EBI-307326
NFKBIAP259632EBI-300010,EBI-307386
NOTCH1P465312EBI-300010,EBI-636374
PDCD11Q146902EBI-300010,EBI-300028
PELP1Q8IZL82EBI-300010,EBI-716449
PLD3Q8IV082EBI-300010,EBI-2689908
RELAQ042069EBI-300010,EBI-73886
RELBQ012014EBI-300010,EBI-357837
RPS3P233962EBI-300010,EBI-351193
TNIP2Q8NFZ58EBI-1452239,EBI-359372
UL42P102264EBI-300010,EBI-1029310From a different organism.

Protein-protein interaction databases

BioGridi110857. 131 interactions.
DIPiDIP-106N.
IntActiP19838. 246 interactions.
MINTiMINT-85658.
STRINGi9606.ENSP00000226574.

Structurei

Secondary structure

1
968
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi43 – 486
Beta strandi52 – 543
Helixi60 – 623
Beta strandi83 – 886
Beta strandi94 – 1007
Beta strandi103 – 1053
Beta strandi110 – 1156
Beta strandi122 – 1265
Beta strandi133 – 1353
Beta strandi138 – 1436
Helixi146 – 1483
Helixi149 – 16315
Helixi167 – 1704
Helixi173 – 1786
Beta strandi180 – 1823
Turni184 – 1874
Helixi190 – 20415
Beta strandi211 – 22111
Beta strandi223 – 2253
Beta strandi227 – 2304
Beta strandi234 – 2407
Helixi245 – 2473
Beta strandi252 – 2565
Beta strandi258 – 2614
Beta strandi267 – 2748
Helixi277 – 2793
Beta strandi281 – 2888
Turni289 – 2913
Beta strandi292 – 2976
Helixi302 – 3043
Turni307 – 3093
Beta strandi310 – 3145
Beta strandi319 – 3224
Beta strandi327 – 3348
Turni336 – 3383
Beta strandi345 – 3506
Helixi813 – 82311
Helixi832 – 8398
Helixi842 – 8443
Helixi845 – 8506
Helixi854 – 86411
Helixi869 – 87911
Helixi883 – 89210

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1MDINMR-B55-67[»]
1MDJNMR-B55-67[»]
1MDKNMR-B55-67[»]
1NFIX-ray2.70B/D248-354[»]
1SVCX-ray2.60P2-365[»]
2DBFNMR-A806-893[»]
2O61X-ray2.80B40-352[»]
3GUTX-ray3.59B/D/F/H41-352[»]
ProteinModelPortaliP19838.
SMRiP19838. Positions 42-353, 494-790, 804-889.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19838.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini42 – 367326RHDPROSITE-ProRule annotationAdd
BLAST
Repeati542 – 57130ANK 1Add
BLAST
Repeati581 – 61030ANK 2Add
BLAST
Repeati614 – 64330ANK 3Add
BLAST
Repeati650 – 67930ANK 4Add
BLAST
Repeati684 – 71431ANK 5Add
BLAST
Repeati718 – 74730ANK 6Add
BLAST
Repeati771 – 80131ANK 7Add
BLAST
Domaini805 – 89288DeathAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni372 – 39423GRRAdd
BLAST
Regioni435 – 968534Interaction with CFLARAdd
BLAST
Regioni650 – 68435Essential for interaction with HIF1ANAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi360 – 3656Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi375 – 43359Gly-richAdd
BLAST

Domaini

The C-terminus of p105 might be involved in cytoplasmic retention, inhibition of DNA-binding, and transcription activation.
Glycine-rich region (GRR) appears to be a critical element in the generation of p50.

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

eggNOGiCOG0666.
GeneTreeiENSGT00500000044765.
HOGENOMiHOG000004822.
HOVERGENiHBG052613.
InParanoidiP19838.
KOiK02580.
OMAiPGYGFPH.
OrthoDBiEOG7W154S.
PhylomeDBiP19838.
TreeFamiTF325632.

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.
IPR000451. NF_Rel_Dor.
IPR008967. p53-like_TF_DNA-bd.
IPR011539. RHD.
[Graphical view]
PfamiPF00023. Ank. 3 hits.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF00554. RHD. 1 hit.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
PR00057. NFKBTNSCPFCT.
SMARTiSM00248. ANK. 6 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. Align

Isoform 1 (identifier: P19838) [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
MAEDDPYLGR PEQMFHLDPS LTHTIFNPEV FQPQMALPTD GPYLQILEQP
60 70 80 90 100
KQRGFRFRYV CEGPSHGGLP GASSEKNKKS YPQVKICNYV GPAKVIVQLV
110 120 130 140 150
TNGKNIHLHA HSLVGKHCED GICTVTAGPK DMVVGFANLG ILHVTKKKVF
160 170 180 190 200
ETLEARMTEA CIRGYNPGLL VHPDLAYLQA EGGGDRQLGD REKELIRQAA
210 220 230 240 250
LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR LEPVVSDAIY DSKAPNASNL
260 270 280 290 300
KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI QIRFYEEEEN GGVWEGFGDF
310 320 330 340 350
SPTDVHRQFA IVFKTPKYKD INITKPASVF VQLRRKSDLE TSEPKPFLYY
360 370 380 390 400
PEIKDKEEVQ RKRQKLMPNF SDSFGGGSGA GAGGGGMFGS GGGGGGTGST
410 420 430 440 450
GPGYSFPHYG FPTYGGITFH PGTTKSNAGM KHGTMDTESK KDPEGCDKSD
460 470 480 490 500
DKNTVNLFGK VIETTEQDQE PSEATVGNGE VTLTYATGTK EESAGVQDNL
510 520 530 540 550
FLEKAMQLAK RHANALFDYA VTGDVKMLLA VQRHLTAVQD ENGDSVLHLA
560 570 580 590 600
IIHLHSQLVR DLLEVTSGLI SDDIINMRND LYQTPLHLAV ITKQEDVVED
610 620 630 640 650
LLRAGADLSL LDRLGNSVLH LAAKEGHDKV LSILLKHKKA ALLLDHPNGD
660 670 680 690 700
GLNAIHLAMM SNSLPCLLLL VAAGADVNAQ EQKSGRTALH LAVEHDNISL
710 720 730 740 750
AGCLLLEGDA HVDSTTYDGT TPLHIAAGRG STRLAALLKA AGADPLVENF
760 770 780 790 800
EPLYDLDDSW ENAGEDEGVV PGTTPLDMAT SWQVFDILNG KPYEPEFTSD
810 820 830 840 850
DLLAQGDMKQ LAEDVKLQLY KLLEIPDPDK NWATLAQKLG LGILNNAFRL
860 870 880 890 900
SPAPSKTLMD NYEVSGGTVR ELVEALRQMG YTEAIEVIQA ASSPVKTTSQ
910 920 930 940 950
AHSLPLSPAS TRQQIDELRD SDSVCDSGVE TSFRKLSFTE SLTSGASLLT
960
LNKMPHDYGQ EGPLEGKI
Length:968
Mass (Da):105,356
Last modified:June 20, 2002 - v2
Checksum:i2A7C8FF86A10D1A8
GO
Isoform 2 (identifier: P19838-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     39-39: T → TA

Show »
Length:969
Mass (Da):105,427
Checksum:iB4D57AC8A410941D
GO
Isoform 3 (identifier: P19838-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-180: Missing.
     181-189: EGGGDRQLG → MNGLCCMAL

Note: No experimental confirmation available.

Show »
Length:788
Mass (Da):85,520
Checksum:i7B9913B97F25DD3F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti243 – 2431K → SE in CAB94757. (PubMed:8825636)Curated
Sequence conflicti361 – 3611R → G in CAH18336. (PubMed:17974005)Curated
Sequence conflicti551 – 5522II → SS in CAB94757. (PubMed:8825636)Curated
Sequence conflicti573 – 5731D → G in BAF84139. (PubMed:14702039)Curated
Sequence conflicti726 – 7261A → V in CAB94757. (PubMed:8825636)Curated
Sequence conflicti825 – 8251I → T in CAH18336. (PubMed:17974005)Curated
Sequence conflicti869 – 8691V → I in CAB94757. (PubMed:8825636)Curated
Sequence conflicti927 – 9271S → T in AAA36361. (PubMed:2203531)Curated
Sequence conflicti927 – 9271S → T in AAA36360. (PubMed:1992489)Curated
Sequence conflicti927 – 9271S → T in CAB94757. (PubMed:8825636)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti489 – 4891T → I.1 Publication
Corresponds to variant rs4648065 [ dbSNP | Ensembl ].
VAR_016268
Natural varianti506 – 5061M → V.1 Publication
Corresponds to variant rs4648072 [ dbSNP | Ensembl ].
VAR_016269
Natural varianti566 – 5661T → I.1 Publication
Corresponds to variant rs4648085 [ dbSNP | Ensembl ].
VAR_016270
Natural varianti578 – 5781R → K.1 Publication
Corresponds to variant rs4648086 [ dbSNP | Ensembl ].
VAR_016271
Natural varianti711 – 7111H → Q.1 Publication
Corresponds to variant rs4648099 [ dbSNP | Ensembl ].
VAR_016272
Natural varianti901 – 9011A → T.1 Publication
Corresponds to variant rs4648118 [ dbSNP | Ensembl ].
VAR_016273

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 180180Missing in isoform 3. 1 PublicationVSP_042869Add
BLAST
Alternative sequencei39 – 391T → TA in isoform 2. 3 PublicationsVSP_021025
Alternative sequencei181 – 1899EGGGDRQLG → MNGLCCMAL in isoform 3. 1 PublicationVSP_042870

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55643 mRNA. Translation: AAA36361.1.
M58603 mRNA. Translation: AAA36360.1.
Z47748
, Z47749, Z47750, Z47751, Z47752, Z47753, Z47754, Z47755, Z47734, Z47735, Z47736, Z47737, Z47738, Z47739, Z47740, Z47741, Z47742, Z47743, Z47744 Genomic DNA. Translation: CAB94757.1.
AF213884 Genomic DNA. Translation: AAF35232.1.
AK122850 mRNA. Translation: BAG53760.1.
AK291450 mRNA. Translation: BAF84139.1.
CR749522 mRNA. Translation: CAH18336.1.
AY223820 Genomic DNA. Translation: AAO30127.1.
BC033210 mRNA. Translation: AAH33210.1.
BC051765 mRNA. Translation: AAH51765.1.
CCDSiCCDS3657.1. [P19838-2]
CCDS54783.1. [P19838-1]
PIRiA37867.
RefSeqiNP_001158884.1. NM_001165412.1. [P19838-1]
NP_003989.2. NM_003998.3. [P19838-2]
UniGeneiHs.618430.

Genome annotation databases

EnsembliENST00000226574; ENSP00000226574; ENSG00000109320. [P19838-2]
ENST00000394820; ENSP00000378297; ENSG00000109320. [P19838-1]
ENST00000505458; ENSP00000424790; ENSG00000109320. [P19838-1]
ENST00000600343; ENSP00000469340; ENSG00000109320. [P19838-3]
GeneIDi4790.
KEGGihsa:4790.
UCSCiuc011cep.2. human. [P19838-2]
uc011ceq.2. human. [P19838-1]
uc011cer.2. human. [P19838-3]

Polymorphism databases

DMDMi21542418.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M55643 mRNA. Translation: AAA36361.1 .
M58603 mRNA. Translation: AAA36360.1 .
Z47748
, Z47749 , Z47750 , Z47751 , Z47752 , Z47753 , Z47754 , Z47755 , Z47734 , Z47735 , Z47736 , Z47737 , Z47738 , Z47739 , Z47740 , Z47741 , Z47742 , Z47743 , Z47744 Genomic DNA. Translation: CAB94757.1 .
AF213884 Genomic DNA. Translation: AAF35232.1 .
AK122850 mRNA. Translation: BAG53760.1 .
AK291450 mRNA. Translation: BAF84139.1 .
CR749522 mRNA. Translation: CAH18336.1 .
AY223820 Genomic DNA. Translation: AAO30127.1 .
BC033210 mRNA. Translation: AAH33210.1 .
BC051765 mRNA. Translation: AAH51765.1 .
CCDSi CCDS3657.1. [P19838-2 ]
CCDS54783.1. [P19838-1 ]
PIRi A37867.
RefSeqi NP_001158884.1. NM_001165412.1. [P19838-1 ]
NP_003989.2. NM_003998.3. [P19838-2 ]
UniGenei Hs.618430.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1MDI NMR - B 55-67 [» ]
1MDJ NMR - B 55-67 [» ]
1MDK NMR - B 55-67 [» ]
1NFI X-ray 2.70 B/D 248-354 [» ]
1SVC X-ray 2.60 P 2-365 [» ]
2DBF NMR - A 806-893 [» ]
2O61 X-ray 2.80 B 40-352 [» ]
3GUT X-ray 3.59 B/D/F/H 41-352 [» ]
ProteinModelPortali P19838.
SMRi P19838. Positions 42-353, 494-790, 804-889.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110857. 131 interactions.
DIPi DIP-106N.
IntActi P19838. 246 interactions.
MINTi MINT-85658.
STRINGi 9606.ENSP00000226574.

Chemistry

BindingDBi P19838.
ChEMBLi CHEMBL2094258.
DrugBanki DB00945. Acetylsalicylic acid.
DB01411. Pranlukast.
DB01041. Thalidomide.
DB08814. Triflusal.

PTM databases

PhosphoSitei P19838.

Polymorphism databases

DMDMi 21542418.

Proteomic databases

MaxQBi P19838.
PaxDbi P19838.
PRIDEi P19838.

Protocols and materials databases

DNASUi 4790.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000226574 ; ENSP00000226574 ; ENSG00000109320 . [P19838-2 ]
ENST00000394820 ; ENSP00000378297 ; ENSG00000109320 . [P19838-1 ]
ENST00000505458 ; ENSP00000424790 ; ENSG00000109320 . [P19838-1 ]
ENST00000600343 ; ENSP00000469340 ; ENSG00000109320 . [P19838-3 ]
GeneIDi 4790.
KEGGi hsa:4790.
UCSCi uc011cep.2. human. [P19838-2 ]
uc011ceq.2. human. [P19838-1 ]
uc011cer.2. human. [P19838-3 ]

Organism-specific databases

CTDi 4790.
GeneCardsi GC04P103422.
HGNCi HGNC:7794. NFKB1.
HPAi CAB004031.
HPA027305.
MIMi 164011. gene.
neXtProti NX_P19838.
PharmGKBi PA248.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0666.
GeneTreei ENSGT00500000044765.
HOGENOMi HOG000004822.
HOVERGENi HBG052613.
InParanoidi P19838.
KOi K02580.
OMAi PGYGFPH.
OrthoDBi EOG7W154S.
PhylomeDBi P19838.
TreeFami TF325632.

Enzyme and pathway databases

Reactomei REACT_118563. RIP-mediated NFkB activation via ZBP1.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_12555. Downstream TCR signaling.
REACT_13443. Regulated proteolysis of p75NTR.
REACT_13696. NF-kB is activated and signals survival.
REACT_163994. FCERI mediated NF-kB activation.
REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
REACT_22442. Interleukin-1 signaling.
REACT_23950. Interleukin-1 processing.
REACT_24969. TRAF6 mediated NF-kB activation.
REACT_27161. Transcriptional regulation of white adipocyte differentiation.
SignaLinki P19838.

Miscellaneous databases

ChiTaRSi NFKB1. human.
EvolutionaryTracei P19838.
GeneWikii NFKB1.
GenomeRNAii 4790.
NextBioi 18454.
PMAP-CutDB P19838.
PROi P19838.
SOURCEi Search...

Gene expression databases

Bgeei P19838.
CleanExi HS_NFKB1.
ExpressionAtlasi P19838. baseline and differential.
Genevestigatori P19838.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
1.25.40.20. 1 hit.
2.60.40.10. 1 hit.
2.60.40.340. 1 hit.
InterProi IPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
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 PF00023. Ank. 3 hits.
PF12796. Ank_2. 1 hit.
PF00531. Death. 1 hit.
PF00554. RHD. 1 hit.
[Graphical view ]
PRINTSi PR01415. ANKYRIN.
PR00057. NFKBTNSCPFCT.
SMARTi SM00248. ANK. 6 hits.
SM00005. DEATH. 1 hit.
SM00429. IPT. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
SSF48403. SSF48403. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF81296. SSF81296. 1 hit.
PROSITEi PS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
PS01204. REL_1. 1 hit.
PS50254. REL_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA binding subunit of NF-kappa B is identical to factor KBF1 and homologous to the rel oncogene product."
    Kieran M., Blank V., Logeat F., Vandekerckhove J., Lottspeich F., le Bail O., Urban M.B., Kourilsky P., Baeuerle P.A., Israel A.
    Cell 62:1007-1018(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE.
  2. "Cloning of a mitogen-inducible gene encoding a kappa B DNA-binding protein with homology to the rel oncogene and to cell-cycle motifs."
    Bours V., Villalobos J., Burd P.R., Kelly K., Siebenlist U.
    Nature 348:76-80(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Cloning of the DNA-binding subunit of human nuclear factor kappa B: the level of its mRNA is strongly regulated by phorbol ester or tumor necrosis factor alpha."
    Meyer R., Hatada E.N., Hohmann H.-P., Haiker M., Bartsch C., Roethlisberger U., Lahm H.-W., Schlaeger E.J., van Loon A.P.G.M., Scheidereit C.
    Proc. Natl. Acad. Sci. U.S.A. 88:966-970(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
  4. "The complete exon-intron structure of the 156-kb human gene NFKB1, which encodes the p105 and p50 proteins of transcription factors NF-kappa B and I kappa B-gamma: implications for NF-kappa B-mediated signal transduction."
    Heron E., Deloukas P., van Loon A.P.G.M.
    Genomics 30:493-505(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Genome sequencing of the chromosome 4q region implicated in human hepatocellular carcinoma pathogenesis."
    Chang H.-M., Tsai S.-F.
    Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Brain and Hippocampus.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Rectum tumor.
  8. NIEHS SNPs program
    Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-489; VAL-506; ILE-566; LYS-578; GLN-711 AND THR-901.
  9. "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: Muscle and Uterus.
  10. "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-P50 COMPLEX.
  11. "The ubiquitin-proteasome pathway is required for processing the NF-kappa B1 precursor protein and the activation of NF-kappa B."
    Palombella V.J., Rando O.J., Goldberg A.L., Maniatis T.
    Cell 78:773-785(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION.
  12. "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.
  13. "A glycine-rich region in NF-kappaB p105 functions as a processing signal for the generation of the p50 subunit."
    Lin L., Ghosh S.
    Mol. Cell. Biol. 16:2248-2254(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING OF P105, GENERATION OF P50 AND P105.
  14. Cited for: S-NITROSYLATION AT CYS-61, MUTAGENESIS OF CYS-61, IDENTIFICATION BY MASS SPECTROMETRY.
  15. "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.
  16. "Cotranslational biogenesis of NF-kappaB p50 by the 26S proteasome."
    Lin L., DeMartino G.N., Greene W.C.
    Cell 92:819-828(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: COTRANSLATIONAL FOLDING/PROCESSING OF P105, GENERATION OF P50/P105.
  17. "NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes."
    Heissmeyer V., Krappmann D., Wulczyn F.G., Scheidereit C.
    EMBO J. 18:4766-4778(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH BCL3, MUTAGENESIS OF SER-921; SER-923 AND SER-932.
  18. "TPL-2 kinase regulates the proteolysis of the NF-kappaB-inhibitory protein NF-kappaB1 p105."
    Belich M.P., Salmeron A., Johnston L.H., Ley S.C.
    Nature 397:363-368(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K8.
  19. "Cotranslational dimerization of the Rel homology domain of NF-kappaB1 generates p50-p105 heterodimers and is required for effective p50 production."
    Lin L., DeMartino G.N., Greene W.C.
    EMBO J. 19:4712-4722(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: COTRANSLATIONAL FOLDING/PROCESSING OF P105, GENERATION OF P50/P105, P50-P105 TRANSIENT HETERODIMER FORMATION.
  20. Cited for: INTERACTION WITH NCOA3.
  21. "Inhibition of NF-kappaB by S-nitrosylation."
    Marshall H.E., Stamler J.S.
    Biochemistry 40:1688-1693(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: S-NITROSYLATION.
  22. "Modulation of T-cell activation by the glucocorticoid-induced leucine zipper factor via inhibition of nuclear factor kappa B."
    Ayroldi E., Migliorati G., Bruscoli S., Marchetti C., Zollo O., Cannarile L., D'Adamio F., Riccardi C.
    Blood 98:743-753(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DSIPI.
  23. "15-Deoxy-Delta 12,14-prostaglandin J2 inhibition of NF-kappaB-DNA binding through covalent modification of the p50 subunit."
    Cernuda-Morollon E., Pineda-Molina E., Canada F.J., Perez-Sala D.
    J. Biol. Chem. 276:35530-35536(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPIDATION AT CYS-61, MUTAGENESIS OF CYS-61.
  24. "Direct phosphorylation of NF-kappa B1 p105 by the Ikappa B kinase complex on serine 927 is essential for signal-induced p105 proteolysis."
    Salmeron A., Janzen J., Soneji Y., Bump N., Kamens J., Allen H., Ley S.C.
    J. Biol. Chem. 276:22215-22222(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-927.
  25. "The tumor suppressor protein menin interacts with NF-kappaB proteins and inhibits NF-kappaB-mediated transactivation."
    Heppner C., Bilimoria K.Y., Agarwal S.K., Kester M., Whitty L.J., Guru S.C., Chandrasekharappa S.C., Collins F.S., Spiegel A.M., Marx S.J., Burns A.L.
    Oncogene 20:4917-4925(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MEN1.
  26. "Casper/c-FLIP is physically and functionally associated with NF-kappaB1 p105."
    Li Z., Zhang J., Chen D., Shu H.B.
    Biochem. Biophys. Res. Commun. 309:980-985(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CFLAR.
  27. "Enhancement of nuclear factor-kappa B acetylation by coactivator p300 and HIV-1 Tat proteins."
    Furia B., Deng L., Wu K., Baylor S., Kehn K., Li H., Donnelly R., Coleman T., Kashanchi F.
    J. Biol. Chem. 277:4973-4980(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-431; LYS-440 AND LYS-441.
  28. "Synthesis of glucocorticoid-induced leucine zipper (GILZ) by macrophages: an anti-inflammatory and immunosuppressive mechanism shared by glucocorticoids and IL-10."
    Berrebi D., Bruscoli S., Cohen N., Foussat A., Migliorati G., Bouchet-Delbos L., Maillot M.-C., Portier A., Couderc J., Galanaud P., Peuchmaur M., Riccardi C., Emilie D.
    Blood 101:729-738(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DSIPI.
  29. "Up-regulation of p300 binding and p50 acetylation in tumor necrosis factor-alpha-induced cyclooxygenase-2 promoter activation."
    Deng W.G., Zhu Y., Wu K.K.
    J. Biol. Chem. 278:4770-4777(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION.
  30. "Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105 stability."
    Demarchi F., Bertoli C., Sandy P., Schneider C.
    J. Biol. Chem. 278:39583-39590(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GSK3B, PHOSPHORYLATION AT SER-903 AND SER-907, MUTAGENESIS OF SER-903 AND SER-907.
  31. "betaTrCP-mediated proteolysis of NF-kappaB1 p105 requires phosphorylation of p105 serines 927 and 932."
    Lang V., Janzen J., Fischer G.Z., Soneji Y., Beinke S., Salmeron A., Allen H., Hay R.T., Ben-Neriah Y., Ley S.C.
    Mol. Cell. Biol. 23:402-413(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-927 AND SER-932.
  32. "Identification of a ZU5 and death domain-containing inhibitor of NF-kappaB."
    Zhang J., Xu L.-G., Han K.-J., Shu H.-B.
    J. Biol. Chem. 279:17819-17825(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH UNC5CL.
  33. "ABIN-2 forms a ternary complex with TPL-2 and NF-kappa B1 p105 and is essential for TPL-2 protein stability."
    Lang V., Symons A., Watton S.J., Janzen J., Soneji Y., Beinke S., Howell S., Ley S.C.
    Mol. Cell. Biol. 24:5235-5248(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MAP3K8 AND TNIP2.
  34. "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.
  35. "Lipopolysaccharide activation of the TPL-2/MEK/extracellular signal-regulated kinase mitogen-activated protein kinase cascade is regulated by IkappaB kinase-induced proteolysis of NF-kappaB1 p105."
    Beinke S., Robinson M.J., Hugunin M., Ley S.C.
    Mol. Cell. Biol. 24:9658-9667(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAP3K8.
  36. Cited for: INTERACTION WITH SPAG9.
  37. "Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)."
    Cockman M.E., Lancaster D.E., Stolze I.P., Hewitson K.S., McDonough M.A., Coleman M.L., Coles C.H., Yu X., Hay R.T., Ley S.C., Pugh C.W., Oldham N.J., Masson N., Schofield C.J., Ratcliffe P.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:14767-14772(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-678, MUTAGENESIS OF ASN-678.
  38. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  39. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-937, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  40. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  41. "Structure of the NF-kappa B p50 homodimer bound to DNA."
    Mueller C.W., Rey F.A., Sodeoka M., Verdine G.L., Harrison S.C.
    Nature 373:311-317(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 1-365.
  42. "Structure of an IkappaBalpha/NF-kappaB complex."
    Jacobs M.D., Harrison S.C.
    Cell 95:749-758(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 248-354.
  43. "Solution structure of the death domain in human nuclear factor NF-kappa-B p105 subunit."
    RIKEN structural genomics initiative (RSGI)
    Submitted (DEC-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 804-893.

Entry informationi

Entry nameiNFKB1_HUMAN
AccessioniPrimary (citable) accession number: P19838
Secondary accession number(s): A8K5Y5
, B3KVE8, Q68D84, Q86V43, Q8N4X7, Q9NZC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: June 20, 2002
Last modified: October 29, 2014
This is version 192 of the entry and version 2 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

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  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3