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P22087

- FBRL_HUMAN

UniProt

P22087 - FBRL_HUMAN

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Protein
rRNA 2'-O-methyltransferase fibrillarin
Gene
FBL, FIB1, FLRN
Organism
Homo sapiens (Human)
Status
Reviewed - 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 (1 Publication).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. RNA binding Source: ProtInc
  2. histone-glutamine methyltransferase activity Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: UniProtKB
Complete GO annotation...

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
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: Chromosome 19

Organism-specific databases

HGNCiHGNC:3599. FBL.

Subcellular locationi

Nucleusnucleolus
Note: Fibrillar region of the nucleolus.4 Publications

GO - Cellular componenti

  1. Cajal body Source: BHF-UCL
  2. box C/D snoRNP complex 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
Complete GO annotation...

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 fibrillarinUniRule annotation
PRO_0000148507Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei8 – 81Asymmetric dimethylarginine By similarity
Modified residuei15 – 151Asymmetric dimethylarginine By similarity
Modified residuei21 – 211Asymmetric dimethylarginine By similarity
Modified residuei24 – 241Asymmetric dimethylarginine By similarity
Modified residuei27 – 271Asymmetric dimethylarginine By 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).UniRule annotation

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 NOL11.7 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

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.

Miscellaneous databases

EvolutionaryTraceiP22087.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni172 – 1732S-adenosyl-L-methionine binding By similarity
Regioni191 – 1922S-adenosyl-L-methionine bindingUniRule annotation
Regioni216 – 2172S-adenosyl-L-methionine bindingUniRule annotation
Regioni236 – 2394S-adenosyl-L-methionine bindingUniRule annotation
Regioni274 – 30633Helical Reviewed prediction
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi8 – 7770DMA/Gly-richUniRule annotation
Add
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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti132 – 1321I → F in AAA52453. 1 Publication

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...

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

« 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. 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: September 3, 2014
This is version 151 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

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