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Q16649

- NFIL3_HUMAN

UniProt

Q16649 - NFIL3_HUMAN

Protein

Nuclear factor interleukin-3-regulated protein

Gene

NFIL3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (26 Jun 2007)
      Previous versions | rss
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    Functioni

    Acts as a transcriptional regulator that recognizes and binds to the sequence 5'-[GA]TTA[CT]GTAA[CT]-3', a sequence present in many cellular and viral promoters. Represses transcription from promoters with activating transcription factor (ATF) sites. Represses promoter activity in osteoblasts By similarity. Represses transcriptional activity of PER1 By similarity. Represses transcriptional activity of PER2 via the B-site on the promoter By similarity. Activates transcription from the interleukin-3 promoter in T-cells. Competes for the same consensus-binding site with PAR DNA-binding factors (DBP, HLF and TEF) By similarity. Component of the circadian clock that acts as a negative regulator for the circadian expression of PER2 oscillation in the cell-autonomous core clock By similarity. Protects pro-B cells from programmed cell death By similarity.By similarity

    GO - Molecular functioni

    1. DNA binding Source: ProtInc
    2. RNA polymerase II core promoter proximal region sequence-specific DNA binding transcription factor activity involved in negative regulation of transcription Source: BHF-UCL
    3. RNA polymerase II core promoter sequence-specific DNA binding Source: Ensembl
    4. RNA polymerase II regulatory region sequence-specific DNA binding Source: BHF-UCL
    5. sequence-specific DNA binding transcription factor activity Source: ProtInc
    6. transcription corepressor activity Source: ProtInc

    GO - Biological processi

    1. cellular response to interleukin-4 Source: Ensembl
    2. circadian rhythm Source: InterPro
    3. immune response Source: ProtInc
    4. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    5. positive regulation of gene expression Source: Ensembl
    6. transcription from RNA polymerase II promoter Source: ProtInc

    Keywords - Molecular functioni

    Activator, Repressor

    Keywords - Biological processi

    Biological rhythms, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding

    Enzyme and pathway databases

    SignaLinkiQ16649.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Nuclear factor interleukin-3-regulated protein
    Alternative name(s):
    E4 promoter-binding protein 4
    Interleukin-3 promoter transcriptional activator
    Interleukin-3-binding protein 1
    Transcriptional activator NF-IL3A
    Gene namesi
    Name:NFIL3
    Synonyms:E4BP4, IL3BP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:7787. NFIL3.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. nucleus Source: ProtInc

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi330 – 3301K → A: Interacts with DR1 and partially affects transcriptional repression; when associated with E-332. 1 Publication
    Mutagenesisi330 – 3301K → E: Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-332. 1 Publication
    Mutagenesisi332 – 3321K → A: Interacts with DR1 and partially affects transcriptional repression; when associated with E-330. 1 Publication
    Mutagenesisi332 – 3321K → E: Does not interact with DR1 and drastically affects transcriptional repression; when associated with E-330. 1 Publication

    Organism-specific databases

    PharmGKBiPA31593.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 462462Nuclear factor interleukin-3-regulated proteinPRO_0000292667Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei301 – 3011Phosphoserine2 Publications
    Modified residuei353 – 3531Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ16649.
    PaxDbiQ16649.
    PRIDEiQ16649.

    PTM databases

    PhosphoSiteiQ16649.

    Expressioni

    Tissue specificityi

    Expressed in bladder stomach, thyroid, spinal cord, lymph node, trachea, adrenal gland, bone marrow and muscle.1 Publication

    Inductioni

    Up-regulated by PHA or TPA.1 Publication

    Gene expression databases

    BgeeiQ16649.
    CleanExiHS_NFIL3.
    GenevestigatoriQ16649.

    Organism-specific databases

    HPAiHPA003261.

    Interactioni

    Subunit structurei

    Homodimer. Binds DNA as a dimer. Interacts with DR1. Interacts with PER2 and CRY2 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi110855. 9 interactions.
    IntActiQ16649. 5 interactions.
    MINTiMINT-268122.
    STRINGi9606.ENSP00000297689.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16649.
    SMRiQ16649. Positions 79-123.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini73 – 13664bZIPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni79 – 9517Basic motifPROSITE-ProRule annotationAdd
    BLAST
    Regioni99 – 1068Leucine-zipperPROSITE-ProRule annotation
    Regioni299 – 36365Necessary for transcriptional repression and sufficient for interaction with DR1Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi155 – 21056Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the bZIP family. NFIL3 subfamily.Curated
    Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG260819.
    HOGENOMiHOG000059596.
    HOVERGENiHBG105717.
    InParanoidiQ16649.
    KOiK09059.
    OMAiWHQKELN.
    OrthoDBiEOG7GQXWM.
    PhylomeDBiQ16649.
    TreeFamiTF328374.

    Family and domain databases

    InterProiIPR004827. bZIP.
    IPR016743. TF_bZIP_E4BP4.
    IPR010533. Vert_IL3-reg_TF.
    [Graphical view]
    PfamiPF07716. bZIP_2. 1 hit.
    PF06529. Vert_IL3-reg_TF. 1 hit.
    [Graphical view]
    PIRSFiPIRSF019029. bZIP_E4BP4. 1 hit.
    SMARTiSM00338. BRLZ. 1 hit.
    [Graphical view]
    PROSITEiPS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q16649-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQLRKMQTVK KEQASLDASS NVDKMMVLNS ALTEVSEDST TGEELLLSEG    50
    SVGKNKSSAC RRKREFIPDE KKDAMYWEKR RKNNEAAKRS REKRRLNDLV 100
    LENKLIALGE ENATLKAELL SLKLKFGLIS STAYAQEIQK LSNSTAVYFQ 150
    DYQTSKSNVS SFVDEHEPSM VSSSCISVIK HSPQSSLSDV SEVSSVEHTQ 200
    ESSVQGSCRS PENKFQIIKQ EPMELESYTR EPRDDRGSYT ASIYQNYMGN 250
    SFSGYSHSPP LLQVNRSSSN SPRTSETDDG VVGKSSDGED EQQVPKGPIH 300
    SPVELKHVHA TVVKVPEVNS SALPHKLRIK AKAMQIKVEA FDNEFEATQK 350
    LSSPIDMTSK RHFELEKHSA PSMVHSSLTP FSVQVTNIQD WSLKSEHWHQ 400
    KELSGKTQNS FKTGVVEMKD SGYKVSDPEN LYLKQGIANL SAEVVSLKRL 450
    IATQPISASD SG 462
    Length:462
    Mass (Da):51,472
    Last modified:June 26, 2007 - v2
    Checksum:iD19946AAC774C3E7
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 452EL → DV in AAA93067. (PubMed:1620116)Curated
    Sequence conflicti44 – 452EL → DV in CAA45597. (PubMed:1620116)Curated
    Sequence conflicti44 – 452EL → DV in AAB35410. (PubMed:7565758)Curated
    Sequence conflicti149 – 1491F → S in CAG46846. 1 PublicationCurated
    Sequence conflicti273 – 2731R → G in AAA93067. (PubMed:1620116)Curated
    Sequence conflicti273 – 2731R → G in CAA45597. (PubMed:1620116)Curated
    Sequence conflicti273 – 2731R → G in AAB35410. (PubMed:7565758)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26173 mRNA. Translation: AAA93067.1.
    X64318 mRNA. Translation: CAA45597.1.
    S79880 mRNA. Translation: AAB35410.1.
    EF028070 Genomic DNA. Translation: ABK15691.1.
    CR542049 mRNA. Translation: CAG46846.1.
    AK313970 mRNA. Translation: BAG36685.1.
    AL353764 Genomic DNA. Translation: CAH73854.1.
    CH471089 Genomic DNA. Translation: EAW62796.1.
    BC008197 mRNA. Translation: AAH08197.1.
    CCDSiCCDS6690.1.
    PIRiG01804.
    RefSeqiNP_001276928.1. NM_001289999.1.
    NP_001276929.1. NM_001290000.1.
    NP_005375.2. NM_005384.2.
    UniGeneiHs.79334.

    Genome annotation databases

    EnsembliENST00000297689; ENSP00000297689; ENSG00000165030.
    GeneIDi4783.
    KEGGihsa:4783.
    UCSCiuc004arh.3. human.

    Polymorphism databases

    DMDMi150385077.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U26173 mRNA. Translation: AAA93067.1 .
    X64318 mRNA. Translation: CAA45597.1 .
    S79880 mRNA. Translation: AAB35410.1 .
    EF028070 Genomic DNA. Translation: ABK15691.1 .
    CR542049 mRNA. Translation: CAG46846.1 .
    AK313970 mRNA. Translation: BAG36685.1 .
    AL353764 Genomic DNA. Translation: CAH73854.1 .
    CH471089 Genomic DNA. Translation: EAW62796.1 .
    BC008197 mRNA. Translation: AAH08197.1 .
    CCDSi CCDS6690.1.
    PIRi G01804.
    RefSeqi NP_001276928.1. NM_001289999.1.
    NP_001276929.1. NM_001290000.1.
    NP_005375.2. NM_005384.2.
    UniGenei Hs.79334.

    3D structure databases

    ProteinModelPortali Q16649.
    SMRi Q16649. Positions 79-123.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110855. 9 interactions.
    IntActi Q16649. 5 interactions.
    MINTi MINT-268122.
    STRINGi 9606.ENSP00000297689.

    PTM databases

    PhosphoSitei Q16649.

    Polymorphism databases

    DMDMi 150385077.

    Proteomic databases

    MaxQBi Q16649.
    PaxDbi Q16649.
    PRIDEi Q16649.

    Protocols and materials databases

    DNASUi 4783.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000297689 ; ENSP00000297689 ; ENSG00000165030 .
    GeneIDi 4783.
    KEGGi hsa:4783.
    UCSCi uc004arh.3. human.

    Organism-specific databases

    CTDi 4783.
    GeneCardsi GC09M094171.
    H-InvDB HIX0169355.
    HGNCi HGNC:7787. NFIL3.
    HPAi HPA003261.
    MIMi 605327. gene.
    neXtProti NX_Q16649.
    PharmGKBi PA31593.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG260819.
    HOGENOMi HOG000059596.
    HOVERGENi HBG105717.
    InParanoidi Q16649.
    KOi K09059.
    OMAi WHQKELN.
    OrthoDBi EOG7GQXWM.
    PhylomeDBi Q16649.
    TreeFami TF328374.

    Enzyme and pathway databases

    SignaLinki Q16649.

    Miscellaneous databases

    ChiTaRSi NFIL3. human.
    GeneWikii NFIL3.
    GenomeRNAii 4783.
    NextBioi 18446.
    PROi Q16649.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q16649.
    CleanExi HS_NFIL3.
    Genevestigatori Q16649.

    Family and domain databases

    InterProi IPR004827. bZIP.
    IPR016743. TF_bZIP_E4BP4.
    IPR010533. Vert_IL3-reg_TF.
    [Graphical view ]
    Pfami PF07716. bZIP_2. 1 hit.
    PF06529. Vert_IL3-reg_TF. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF019029. bZIP_E4BP4. 1 hit.
    SMARTi SM00338. BRLZ. 1 hit.
    [Graphical view ]
    PROSITEi PS50217. BZIP. 1 hit.
    PS00036. BZIP_BASIC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Transcriptional repression by a novel member of the bZIP family of transcription factors."
      Cowell I.G., Skinner A., Hurst H.C.
      Mol. Cell. Biol. 12:3070-3077(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBUNIT, DNA-BINDING.
      Tissue: Placenta.
    2. "Molecular cloning and characterization of NF-IL3A, a transcriptional activator of the human interleukin-3 promoter."
      Zhang W., Zhang J., Kornuc M., Kwan K., Frank R., Nimer S.D.
      Mol. Cell. Biol. 15:6055-6063(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION, DNA-BINDING.
      Tissue: T-cell.
    3. NHLBI resequencing and genotyping service (RS&G)
      Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    5. "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].
      Tissue: Liver.
    6. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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].
      Tissue: Placenta.
    9. "Protein-protein interaction between the transcriptional repressor E4BP4 and the TBP-binding protein Dr1."
      Cowell I.G., Hurst H.C.
      Nucleic Acids Res. 24:3607-3613(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DR1, MUTAGENESIS OF LYS-330 AND LYS-332.
    10. "Exclusion of NFIL3 as the gene causing hereditary sensory neuropathy type I by mutation analysis."
      Hulme D.J., Blair I.P., Dawkins J.L., Nicholson G.A.
      Hum. Genet. 106:594-596(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    11. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    14. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-301 AND SER-353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiNFIL3_HUMAN
    AccessioniPrimary (citable) accession number: Q16649
    Secondary accession number(s): B2R9Y8
    , Q14211, Q6FGQ8, Q96HS0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 26, 2007
    Last sequence update: June 26, 2007
    Last modified: October 1, 2014
    This is version 111 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3