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P22087

- FBRL_HUMAN

UniProt

P22087 - FBRL_HUMAN

Protein

rRNA 2'-O-methyltransferase fibrillarin

Gene

FBL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (20 Jun 2001)
      Previous versions | rss
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    Functioni

    S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Site specificity is provided by a guide RNA that base pairs with the substrate. Methylation occurs at a characteristic distance from the sequence involved in base pairing with the guide RNA. Also acts as a protein methyltransferase by mediating methylation of 'Gln-105' of histone H2A (H2AQ104me), a modification that impairs binding of the FACT complex and is specifically present at 35S ribosomal DNA locus (PubMed:24352239).1 Publication

    Catalytic activityi

    S-adenosyl-L-methionine + L-glutamine-[histone] = S-adenosyl-L-homocysteine + N(5)-methyl-L-glutamine-[histone].1 Publication

    GO - Molecular functioni

    1. histone-glutamine methyltransferase activity Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. RNA binding Source: ProtInc

    GO - Biological processi

    1. histone glutamine methylation Source: UniProtKB
    2. osteoblast differentiation Source: UniProt
    3. rRNA processing Source: ProtInc
    4. snoRNA metabolic process Source: Ensembl
    5. tRNA processing Source: InterPro

    Keywords - Molecular functioni

    Methyltransferase, Ribonucleoprotein, Transferase

    Keywords - Biological processi

    rRNA processing

    Keywords - Ligandi

    RNA-binding, S-adenosyl-L-methionine

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    rRNA 2'-O-methyltransferase fibrillarin (EC:2.1.1.-)
    Alternative name(s):
    34 kDa nucleolar scleroderma antigen
    Histone-glutamine methyltransferase
    Gene namesi
    Name:FBL
    Synonyms:FIB1, FLRN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3599. FBL.

    Subcellular locationi

    Nucleusnucleolus 4 Publications
    Note: Fibrillar region of the nucleolus.

    GO - Cellular componenti

    1. box C/D snoRNP complex Source: BHF-UCL
    2. Cajal body Source: BHF-UCL
    3. extracellular vesicular exosome Source: UniProt
    4. granular component Source: Ensembl
    5. membrane Source: UniProt
    6. nucleolus Source: UniProtKB
    7. nucleus Source: UniProt

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA28012.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 321321rRNA 2'-O-methyltransferase fibrillarinPRO_0000148507Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei8 – 81Asymmetric dimethylarginineBy similarity
    Modified residuei15 – 151Asymmetric dimethylarginineBy similarity
    Modified residuei21 – 211Asymmetric dimethylarginineBy similarity
    Modified residuei24 – 241Asymmetric dimethylarginineBy similarity
    Modified residuei27 – 271Asymmetric dimethylarginineBy similarity
    Modified residuei124 – 1241Phosphoserine2 Publications

    Post-translational modificationi

    By homology to other fibrillarins, some or all of the N-terminal domain arginines are modified to asymmetric dimethylarginine (DMA).

    Keywords - PTMi

    Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP22087.
    PaxDbiP22087.
    PeptideAtlasiP22087.
    PRIDEiP22087.

    2D gel databases

    SWISS-2DPAGEP22087.

    PTM databases

    PhosphoSiteiP22087.

    Expressioni

    Gene expression databases

    ArrayExpressiP22087.
    BgeeiP22087.
    CleanExiHS_FBL.
    GenevestigatoriP22087.

    Organism-specific databases

    HPAiCAB001514.

    Interactioni

    Subunit structurei

    Interacts with NOLC1 By similarity. Component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles that contain NHP2L1, FBL, NOP5 and NOP56, plus a guide RNA. It is associated with the U3, U8, U13, X and Y small nuclear RNAs. Component of several ribosomal and nucleolar protein complexes. Interacts with PRMT5 and UTP20. Interacts with DDX5 and C1QBP. Interacts with NOL11.By similarity8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    DDX5P178446EBI-358318,EBI-351962

    Protein-protein interaction databases

    BioGridi108399. 116 interactions.
    DIPiDIP-27569N.
    IntActiP22087. 29 interactions.
    MINTiMINT-207612.

    Structurei

    Secondary structure

    1
    321
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi96 – 983
    Beta strandi107 – 1093
    Beta strandi117 – 1193
    Beta strandi122 – 1254
    Beta strandi132 – 1365
    Turni139 – 1413
    Helixi143 – 1497
    Beta strandi162 – 1665
    Helixi172 – 18110
    Beta strandi186 – 1905
    Helixi194 – 20613
    Beta strandi210 – 2134
    Helixi220 – 2267
    Beta strandi230 – 2356
    Helixi242 – 25312
    Beta strandi254 – 26512
    Helixi266 – 2694
    Beta strandi271 – 2733
    Helixi275 – 28410
    Helixi285 – 2895
    Beta strandi291 – 2988
    Turni300 – 3023
    Beta strandi303 – 31311

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IPXX-ray1.82A83-315[»]
    ProteinModelPortaliP22087.
    SMRiP22087. Positions 87-315.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP22087.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni172 – 1732S-adenosyl-L-methionine bindingBy similarity
    Regioni191 – 1922S-adenosyl-L-methionine binding
    Regioni216 – 2172S-adenosyl-L-methionine binding
    Regioni236 – 2394S-adenosyl-L-methionine binding
    Regioni274 – 30633HelicalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi8 – 7770DMA/Gly-richAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1889.
    HOGENOMiHOG000106741.
    HOVERGENiHBG002472.
    InParanoidiP22087.
    KOiK14563.
    OMAiDNIYMGP.
    PhylomeDBiP22087.
    TreeFamiTF300639.

    Family and domain databases

    Gene3Di3.40.50.150. 1 hit.
    HAMAPiMF_00351. RNA_methyltransf_FlpA.
    InterProiIPR000692. Fibrillarin.
    IPR020813. Fibrillarin_CS.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view]
    PfamiPF01269. Fibrillarin. 1 hit.
    [Graphical view]
    PIRSFiPIRSF006540. Nop17p. 1 hit.
    PRINTSiPR00052. FIBRILLARIN.
    SUPFAMiSSF53335. SSF53335. 1 hit.
    PROSITEiPS00566. FIBRILLARIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P22087-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPGFSPRGG GFGGRGGFGD RGGRGGRGGF GGGRGRGGGF RGRGRGGGGG    50
    GGGGGGGGRG GGGFHSGGNR GRGRGGKRGN QSGKNVMVEP HRHEGVFICR 100
    GKEDALVTKN LVPGESVYGE KRVSISEGDD KIEYRAWNPF RSKLAAAILG 150
    GVDQIHIKPG AKVLYLGAAS GTTVSHVSDI VGPDGLVYAV EFSHRSGRDL 200
    INLAKKRTNI IPVIEDARHP HKYRMLIAMV DVIFADVAQP DQTRIVALNA 250
    HTFLRNGGHF VISIKANCID STASAEAVFA SEVKKMQQEN MKPQEQLTLE 300
    PYERDHAVVV GVYRPPPKVK N 321
    Length:321
    Mass (Da):33,784
    Last modified:June 20, 2001 - v2
    Checksum:i2123F41E01EC557A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti132 – 1321I → F in AAA52453. (PubMed:1846968)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59849 mRNA. Translation: AAA52453.1.
    X56597 mRNA. Translation: CAA39935.1.
    BT006830 mRNA. Translation: AAP35476.1.
    BT020144 mRNA. Translation: AAV38946.1.
    CR457069 mRNA. Translation: CAG33350.1.
    AB451384 mRNA. Translation: BAG70198.1.
    AC006950 Genomic DNA. Translation: AAD15623.1.
    AC005393 Genomic DNA. Translation: AAC28913.1.
    CH471126 Genomic DNA. Translation: EAW56925.1.
    BC019260 mRNA. Translation: AAH19260.1.
    CCDSiCCDS12545.1.
    PIRiA38712.
    RefSeqiNP_001427.2. NM_001436.3.
    UniGeneiHs.299002.

    Genome annotation databases

    EnsembliENST00000221801; ENSP00000221801; ENSG00000105202.
    GeneIDi2091.
    KEGGihsa:2091.
    UCSCiuc002omm.1. human.

    Polymorphism databases

    DMDMi14549159.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M59849 mRNA. Translation: AAA52453.1 .
    X56597 mRNA. Translation: CAA39935.1 .
    BT006830 mRNA. Translation: AAP35476.1 .
    BT020144 mRNA. Translation: AAV38946.1 .
    CR457069 mRNA. Translation: CAG33350.1 .
    AB451384 mRNA. Translation: BAG70198.1 .
    AC006950 Genomic DNA. Translation: AAD15623.1 .
    AC005393 Genomic DNA. Translation: AAC28913.1 .
    CH471126 Genomic DNA. Translation: EAW56925.1 .
    BC019260 mRNA. Translation: AAH19260.1 .
    CCDSi CCDS12545.1.
    PIRi A38712.
    RefSeqi NP_001427.2. NM_001436.3.
    UniGenei Hs.299002.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IPX X-ray 1.82 A 83-315 [» ]
    ProteinModelPortali P22087.
    SMRi P22087. Positions 87-315.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108399. 116 interactions.
    DIPi DIP-27569N.
    IntActi P22087. 29 interactions.
    MINTi MINT-207612.

    PTM databases

    PhosphoSitei P22087.

    Polymorphism databases

    DMDMi 14549159.

    2D gel databases

    SWISS-2DPAGE P22087.

    Proteomic databases

    MaxQBi P22087.
    PaxDbi P22087.
    PeptideAtlasi P22087.
    PRIDEi P22087.

    Protocols and materials databases

    DNASUi 2091.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000221801 ; ENSP00000221801 ; ENSG00000105202 .
    GeneIDi 2091.
    KEGGi hsa:2091.
    UCSCi uc002omm.1. human.

    Organism-specific databases

    CTDi 2091.
    GeneCardsi GC19M040325.
    HGNCi HGNC:3599. FBL.
    HPAi CAB001514.
    MIMi 134795. gene.
    neXtProti NX_P22087.
    PharmGKBi PA28012.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1889.
    HOGENOMi HOG000106741.
    HOVERGENi HBG002472.
    InParanoidi P22087.
    KOi K14563.
    OMAi DNIYMGP.
    PhylomeDBi P22087.
    TreeFami TF300639.

    Miscellaneous databases

    ChiTaRSi FBL. human.
    EvolutionaryTracei P22087.
    GeneWikii Fibrillarin.
    GenomeRNAii 2091.
    NextBioi 8479.
    PROi P22087.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P22087.
    Bgeei P22087.
    CleanExi HS_FBL.
    Genevestigatori P22087.

    Family and domain databases

    Gene3Di 3.40.50.150. 1 hit.
    HAMAPi MF_00351. RNA_methyltransf_FlpA.
    InterProi IPR000692. Fibrillarin.
    IPR020813. Fibrillarin_CS.
    IPR029063. SAM-dependent_MTases-like.
    [Graphical view ]
    Pfami PF01269. Fibrillarin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF006540. Nop17p. 1 hit.
    PRINTSi PR00052. FIBRILLARIN.
    SUPFAMi SSF53335. SSF53335. 1 hit.
    PROSITEi PS00566. FIBRILLARIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "cDNA cloning and sequencing of human fibrillarin, a conserved nucleolar protein recognized by autoimmune antisera."
      Aris J.P., Blobel G.
      Proc. Natl. Acad. Sci. U.S.A. 88:931-935(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Evolutionary conservation of the human nucleolar protein fibrillarin and its functional expression in yeast."
      Jansen R.P., Hurt E.C., Kern H., Lehtonen H., Carmo-Fonseca M., Lapeyre B., Tollervey D.
      J. Cell Biol. 113:715-729(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Tissue: Cervix carcinoma.
    3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
      Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
      , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
      Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    6. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(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. "Purification and partial characterization of a nucleolar scleroderma antigen (Mr = 34,000; pI, 8.5) rich in NG,NG-dimethylarginine."
      Lischwe M.A., Ochs R.L., Reddy R., Cook R.G., Yeoman L.C., Tan E.M., Reichlin M., Busch H.
      J. Biol. Chem. 260:14304-14310(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, SUBCELLULAR LOCATION.
    10. "An intact Box C sequence in the U3 snRNA is required for binding of fibrillarin, the protein common to the major family of nucleolar snRNPs."
      Baserga S.J., Yang X.D., Steitz J.A.
      EMBO J. 10:2645-2651(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH SMALL NUCLEOLAR RNA U3; U8; U13; X AND Y.
    11. "The nuclear DEAD box RNA helicase p68 interacts with the nucleolar protein fibrillarin and colocalizes specifically in nascent nucleoli during telophase."
      Nicol S.M., Causevic M., Prescott A.R., Fuller-Pace F.V.
      Exp. Cell Res. 257:272-280(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDX5.
    12. "Human fibrillarin forms a sub-complex with splicing factor 2-associated p32, protein arginine methyltransferases, and tubulins alpha 3 and beta 1 that is independent of its association with preribosomal ribonucleoprotein complexes."
      Yanagida M., Hayano T., Yamauchi Y., Shinkawa T., Natsume T., Isobe T., Takahashi N.
      J. Biol. Chem. 279:1607-1614(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PRMT5, IDENTIFICATION IN A COMPLEX WITH NOP5 AND NOP56, IDENTIFICATION IN A COMPLEX WITH RIBOSOMAL PROTEINS AND WITH NUMEROUS NUCLEOLAR PROTEINS, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    13. "Human 1A6/DRIM, the homolog of yeast Utp20, functions in the 18S rRNA processing."
      Wang Y., Liu J., Zhao H., Lue W., Zhao J., Yang L., Li N., Du X., Ke Y.
      Biochim. Biophys. Acta 1773:863-868(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH UTP20.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "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-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Splicing factor 2-associated protein p32 participates in ribosome biogenesis by regulating the binding of Nop52 and fibrillarin to preribosome particles."
      Yoshikawa H., Komatsu W., Hayano T., Miura Y., Homma K., Izumikawa K., Ishikawa H., Miyazawa N., Tachikawa H., Yamauchi Y., Isobe T., Takahashi N.
      Mol. Cell. Proteomics 10:0-0(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH C1QBP.
    18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "NOL11, implicated in the pathogenesis of North American Indian childhood cirrhosis, is required for pre-rRNA transcription and processing."
      Freed E.F., Prieto J.L., McCann K.L., McStay B., Baserga S.J.
      PLoS Genet. 8:E1002892-E1002892(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NOL11.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "Glutamine methylation in histone H2A is an RNA-polymerase-I-dedicated modification."
      Tessarz P., Santos-Rosa H., Robson S.C., Sylvestersen K.B., Nelson C.J., Nielsen M.L., Kouzarides T.
      Nature 505:564-568(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY.
    22. "The crystal structure of human fibrillarin in complex with SAH."
      Structural genomics consortium (SGC)
      Submitted (FEB-2009) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 83-315 IN COMPLEX WITH S-ADENOSYL-L-HOMOCYSTEINE.

    Entry informationi

    Entry nameiFBRL_HUMAN
    AccessioniPrimary (citable) accession number: P22087
    Secondary accession number(s): B5BUE8
    , O75259, Q6IAT5, Q9UPI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1991
    Last sequence update: June 20, 2001
    Last modified: October 1, 2014
    This is version 152 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, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3