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P19838

- NFKB1_HUMAN

UniProt

P19838 - NFKB1_HUMAN

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
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    • History
      Entry version 191 (01 Oct 2014)
      Sequence version 2 (20 Jun 2002)
      Previous versions | rss
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    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. protein binding Source: IntAct
    4. regulatory region DNA binding Source: UniProtKB
    5. sequence-specific DNA binding transcription factor activity Source: ProtInc
    6. transcription factor binding Source: MGI
    7. transcription regulatory region DNA binding Source: BHF-UCL
    8. 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

    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

    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; alternate2 Publications
    Lipidationi61 – 611S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine; alternate1 Publication
    Modified residuei337 – 3371Phosphoserine; by PKASequence Analysis
    Modified residuei431 – 4311N6-acetyllysine; by EP3002 Publications
    Modified residuei440 – 4401N6-acetyllysine; by EP3002 Publications
    Modified residuei441 – 4411N6-acetyllysine; by EP3002 Publications
    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

    ArrayExpressiP19838.
    BgeeiP19838.
    CleanExiHS_NFKB1.
    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. 127 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, 514-796, 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.
    HOGENOMiHOG000004822.
    HOVERGENiHBG052613.
    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: P19838-1) [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

    MAEDDPYLGR PEQMFHLDPS LTHTIFNPEV FQPQMALPTD GPYLQILEQP    50
    KQRGFRFRYV CEGPSHGGLP GASSEKNKKS YPQVKICNYV GPAKVIVQLV 100
    TNGKNIHLHA HSLVGKHCED GICTVTAGPK DMVVGFANLG ILHVTKKKVF 150
    ETLEARMTEA CIRGYNPGLL VHPDLAYLQA EGGGDRQLGD REKELIRQAA 200
    LQQTKEMDLS VVRLMFTAFL PDSTGSFTRR LEPVVSDAIY DSKAPNASNL 250
    KIVRMDRTAG CVTGGEEIYL LCDKVQKDDI QIRFYEEEEN GGVWEGFGDF 300
    SPTDVHRQFA IVFKTPKYKD INITKPASVF VQLRRKSDLE TSEPKPFLYY 350
    PEIKDKEEVQ RKRQKLMPNF SDSFGGGSGA GAGGGGMFGS GGGGGGTGST 400
    GPGYSFPHYG FPTYGGITFH PGTTKSNAGM KHGTMDTESK KDPEGCDKSD 450
    DKNTVNLFGK VIETTEQDQE PSEATVGNGE VTLTYATGTK EESAGVQDNL 500
    FLEKAMQLAK RHANALFDYA VTGDVKMLLA VQRHLTAVQD ENGDSVLHLA 550
    IIHLHSQLVR DLLEVTSGLI SDDIINMRND LYQTPLHLAV ITKQEDVVED 600
    LLRAGADLSL LDRLGNSVLH LAAKEGHDKV LSILLKHKKA ALLLDHPNGD 650
    GLNAIHLAMM SNSLPCLLLL VAAGADVNAQ EQKSGRTALH LAVEHDNISL 700
    AGCLLLEGDA HVDSTTYDGT TPLHIAAGRG STRLAALLKA AGADPLVENF 750
    EPLYDLDDSW ENAGEDEGVV PGTTPLDMAT SWQVFDILNG KPYEPEFTSD 800
    DLLAQGDMKQ LAEDVKLQLY KLLEIPDPDK NWATLAQKLG LGILNNAFRL 850
    SPAPSKTLMD NYEVSGGTVR ELVEALRQMG YTEAIEVIQA ASSPVKTTSQ 900
    AHSLPLSPAS TRQQIDELRD SDSVCDSGVE TSFRKLSFTE SLTSGASLLT 950
    LNKMPHDYGQ EGPLEGKI 968
    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, 514-796, 804-889.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110857. 127 interactions.
    DIPi DIP-106N.
    IntActi P19838. 246 interactions.
    MINTi MINT-85658.
    STRINGi 9606.ENSP00000226574.

    Chemistry

    BindingDBi P19838.
    ChEMBLi CHEMBL3251.
    DrugBanki DB01234. Dexamethasone.
    DB01411. Pranlukast.
    DB01041. Thalidomide.

    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.
    HOGENOMi HOG000004822.
    HOVERGENi HBG052613.
    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

    ArrayExpressi P19838.
    Bgeei P19838.
    CleanExi HS_NFKB1.
    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

    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 1, 2014
    This is version 191 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

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    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