Skip Header

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

rRNA 2'-O-methyltransferase fibrillarin

Gene

FBL

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

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

  • histone-glutamine methyltransferase activity Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA binding Source: ProtInc
  • rRNA methyltransferase activity Source: GO_Central

GO - Biological processi

  • box C/D snoRNA 3'-end processing Source: GO_Central
  • histone glutamine methylation Source: UniProtKB
  • osteoblast differentiation Source: UniProtKB
  • rRNA methylation Source: GO_Central
  • rRNA processing Source: ProtInc
  • tRNA processing Source: InterPro
Complete GO annotation...

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 Componentsi: Chromosome 1, Chromosome 19

Organism-specific databases

HGNCiHGNC:3599. FBL.

Subcellular locationi

GO - Cellular componenti

  • box C/D snoRNP complex Source: BHF-UCL
  • Cajal body Source: BHF-UCL
  • dense fibrillar component Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • granular component Source: Ensembl
  • membrane Source: UniProtKB
  • nucleolus Source: UniProtKB
  • nucleus Source: UniProtKB
  • small-subunit processome Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA28012.

Polymorphism and mutation databases

BioMutaiFBL.
DMDMi14549159.

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 – 1241Phosphoserine3 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

BgeeiP22087.
CleanExiHS_FBL.
ExpressionAtlasiP22087. baseline and differential.
GenevisibleiP22087. HS.

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. Interacts with PIH1D1 (PubMed:17636026).By similarity9 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi108399. 170 interactions.
DIPiDIP-27569N.
IntActiP22087. 31 interactions.
MINTiMINT-207612.
STRINGi9606.ENSP00000221801.

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:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
HOVERGENiHBG002472.
KOiK14563.
OMAiPGVYIVI.
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.
[Graphical view]
PfamiPF01269. Fibrillarin. 1 hit.
[Graphical view]
PRINTSiPR00052. FIBRILLARIN.
SUPFAMiSSF53335. SSF53335. 1 hit.
PROSITEiPS00566. FIBRILLARIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P22087-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKPGFSPRGG GFGGRGGFGD RGGRGGRGGF GGGRGRGGGF RGRGRGGGGG
60 70 80 90 100
GGGGGGGGRG GGGFHSGGNR GRGRGGKRGN QSGKNVMVEP HRHEGVFICR
110 120 130 140 150
GKEDALVTKN LVPGESVYGE KRVSISEGDD KIEYRAWNPF RSKLAAAILG
160 170 180 190 200
GVDQIHIKPG AKVLYLGAAS GTTVSHVSDI VGPDGLVYAV EFSHRSGRDL
210 220 230 240 250
INLAKKRTNI IPVIEDARHP HKYRMLIAMV DVIFADVAQP DQTRIVALNA
260 270 280 290 300
HTFLRNGGHF VISIKANCID STASAEAVFA SEVKKMQQEN MKPQEQLTLE
310 320
PYERDHAVVV GVYRPPPKVK N
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:
EMBLi
GenBanki
DDBJi
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.
ENST00000625241; ENSP00000487390; ENSG00000280548.
GeneIDi2091.
KEGGihsa:2091.
UCSCiuc002omm.1. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi108399. 170 interactions.
DIPiDIP-27569N.
IntActiP22087. 31 interactions.
MINTiMINT-207612.
STRINGi9606.ENSP00000221801.

PTM databases

PhosphoSiteiP22087.

Polymorphism and mutation databases

BioMutaiFBL.
DMDMi14549159.

2D gel databases

SWISS-2DPAGEP22087.

Proteomic databases

MaxQBiP22087.
PaxDbiP22087.
PeptideAtlasiP22087.
PRIDEiP22087.

Protocols and materials databases

DNASUi2091.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000221801; ENSP00000221801; ENSG00000105202.
ENST00000625241; ENSP00000487390; ENSG00000280548.
GeneIDi2091.
KEGGihsa:2091.
UCSCiuc002omm.1. human.

Organism-specific databases

CTDi2091.
GeneCardsiGC19M040325.
HGNCiHGNC:3599. FBL.
HPAiCAB001514.
MIMi134795. gene.
neXtProtiNX_P22087.
PharmGKBiPA28012.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1889.
GeneTreeiENSGT00550000074792.
HOGENOMiHOG000106741.
HOVERGENiHBG002472.
KOiK14563.
OMAiPGVYIVI.
PhylomeDBiP22087.
TreeFamiTF300639.

Miscellaneous databases

ChiTaRSiFBL. human.
EvolutionaryTraceiP22087.
GeneWikiiFibrillarin.
GenomeRNAii2091.
NextBioi8479.
PROiP22087.
SOURCEiSearch...

Gene expression databases

BgeeiP22087.
CleanExiHS_FBL.
ExpressionAtlasiP22087. baseline and differential.
GenevisibleiP22087. HS.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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. "A dynamic scaffold of pre-snoRNP factors facilitates human box C/D snoRNP assembly."
    McKeegan K.S., Debieux C.M., Boulon S., Bertrand E., Watkins N.J.
    Mol. Cell. Biol. 27:6782-6793(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIH1D1.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "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.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "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.
  19. "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].
  20. "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.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  23. "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.
  24. "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: July 22, 2015
This is version 160 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.