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Protein

pre-rRNA processing protein FTSJ3

Gene

Ftsj3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation.UniRule annotation

Catalytic activityi

S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing 2'-O-methylnucleoside.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei56 – 561S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
Binding sitei58 – 581S-adenosyl-L-methionine; via amide nitrogenUniRule annotation
Binding sitei76 – 761S-adenosyl-L-methionineUniRule annotation
Binding sitei92 – 921S-adenosyl-L-methionineUniRule annotation
Binding sitei117 – 1171S-adenosyl-L-methionineUniRule annotation
Active sitei157 – 1571Proton acceptorUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Ribosome biogenesis, rRNA processing

Keywords - Ligandi

S-adenosyl-L-methionine

Names & Taxonomyi

Protein namesi
Recommended name:
pre-rRNA processing protein FTSJ3UniRule annotation (EC:2.1.1.-UniRule annotation)
Alternative name(s):
2'-O-ribose RNA methyltransferase SPB1 homologUniRule annotation
Protein ftsJ homolog 3UniRule annotation
Putative rRNA methyltransferase 3UniRule annotation
Gene namesi
Name:Ftsj3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1860295. Ftsj3.

Subcellular locationi

  • Nucleusnucleolus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 838838pre-rRNA processing protein FTSJ3PRO_0000155578Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei333 – 3331PhosphoserineCombined sources
Modified residuei335 – 3351PhosphoserineCombined sources
Modified residuei336 – 3361PhosphoserineCombined sources
Modified residuei390 – 3901Citrulline1 Publication
Modified residuei532 – 5321PhosphoserineBy similarity
Modified residuei545 – 5451PhosphoserineBy similarity
Modified residuei576 – 5761PhosphoserineBy similarity
Modified residuei667 – 6671PhosphoserineBy similarity
Modified residuei679 – 6791PhosphoserineBy similarity
Modified residuei774 – 7741Citrulline1 Publication

Post-translational modificationi

Citrullinated by PADI4.1 Publication

Keywords - PTMi

Citrullination, Phosphoprotein

Proteomic databases

EPDiQ9DBE9.
MaxQBiQ9DBE9.
PaxDbiQ9DBE9.
PRIDEiQ9DBE9.

PTM databases

iPTMnetiQ9DBE9.
PhosphoSiteiQ9DBE9.

Expressioni

Gene expression databases

BgeeiQ9DBE9.
CleanExiMM_FTSJ3.
GenevisibleiQ9DBE9. MM.

Interactioni

Subunit structurei

Interacts with NIP7.UniRule annotation

Protein-protein interaction databases

BioGridi207815. 2 interactions.
IntActiQ9DBE9. 1 interaction.
MINTiMINT-4128230.
STRINGi10090.ENSMUSP00000021048.

Structurei

3D structure databases

ProteinModelPortaliQ9DBE9.
SMRiQ9DBE9. Positions 24-184.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili730 – 76839UniRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi337 – 38044Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA methyltransferase RlmE family. SPB1 subfamily.UniRule annotation

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG1098. Eukaryota.
COG0293. LUCA.
GeneTreeiENSGT00550000075004.
HOGENOMiHOG000176256.
HOVERGENiHBG075246.
InParanoidiQ9DBE9.
KOiK14857.
OMAiPTEMADP.
OrthoDBiEOG7WX07S.
PhylomeDBiQ9DBE9.
TreeFamiTF106102.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
MF_03163. RNA_methyltr_E_SPB1.
InterProiIPR015507. rRNA-MeTfrase_E.
IPR012920. rRNA_MeTfrase_Spb1_C.
IPR024576. rRNA_MeTfrase_Spb1_DUF3381.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
IPR028589. Spb1.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 3 hits.
PTHR10920:SF13. PTHR10920:SF13. 3 hits.
PfamiPF11861. DUF3381. 1 hit.
PF01728. FtsJ. 1 hit.
PF07780. Spb1_C. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9DBE9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD
60 70 80 90 100
LCAAPGGWLQ VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ EDITTERCRQ
110 120 130 140 150
ALRKELKTWK VDVVLNDGAP NVGASWVHDA YSQAHLTLMA LRLACDFLAR
160 170 180 190 200
GGCFITKVFR SRDYQPLLWI FQQLFHRVQA TKPQASRHES AEIFVVCQGF
210 220 230 240 250
LAPDKVDAKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG YAEGDLTLYH
260 270 280 290 300
RTSVTDFLRA ANPVDFLSKA SEISIDDEEL AQHPATTEDI RVCCQDIKVL
310 320 330 340 350
GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSEEEE EGDEEEAVAE
360 370 380 390 400
TKQAPEEEEE REEEQLNRTL AEMKAQEVAE LKRKKKKLLR EQRKQRERVE
410 420 430 440 450
LKMDLPGVSI ADEGETGMFS LRTIRGQQLL EEVTQGDMNA ADTFLSDLPR
460 470 480 490 500
DDIYVSDAED DDDTSLESDL DPEELAGVRT HSDLKEQKYL RFTQVDDNKE
510 520 530 540 550
EEGENPLLVP LEEKAVLQEE QASLWFSKDG FSGIEDDADE ALEISQAQLL
560 570 580 590 600
YKSRQKEQQP TDPPPPPTNL KTEKKSPQGQ NEVPKETEAI LGTEAVTDPG
610 620 630 640 650
GEERGNSSDS DSSSSEDEDS WKVSRGVKRG RGSKADEDGF EVVPIQDPVK
660 670 680 690 700
YRILDPEGLA LGAVIASSKK AKRDLIDNSF NRYAFNEEEG ELPEWFAQEE
710 720 730 740 750
KQHRIRQLPV DKKEVEHYRK RWREINARPI KKVAEAKARK KRRVLKKLEQ
760 770 780 790 800
TKKKAEAVVN TVDISEREKV AQLRSLYKKA GLGKEKRQVT YVVAKKGVGR
810 820 830
KVRRPAGVKG HFKVVDSRMK KDQRAQQRKE QKKKHKRK
Length:838
Mass (Da):95,532
Last modified:June 1, 2001 - v1
Checksum:i9DD289A76748C28B
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti233 – 2331K → R in AAH12281 (PubMed:15489334).Curated
Sequence conflicti494 – 4941Q → K in AAH12281 (PubMed:15489334).Curated
Sequence conflicti502 – 5021E → G in AAH12281 (PubMed:15489334).Curated
Sequence conflicti555 – 5551Q → R in AAH12281 (PubMed:15489334).Curated
Sequence conflicti744 – 7441V → M in AAH12281 (PubMed:15489334).Curated
Sequence conflicti774 – 7741R → A in AAH12281 (PubMed:15489334).Curated
Sequence conflicti776 – 7794LYKK → PVHT in AAH12281 (PubMed:15489334).Curated
Sequence conflicti784 – 79512KEKRQ…YVVAK → IAVIVRVFHLAF in AAH12281 (PubMed:15489334).CuratedAdd
BLAST
Sequence conflicti799 – 80810GRKVRRPAGV → NHNNLPGCKP in AAH12281 (PubMed:15489334).Curated
Sequence conflicti812 – 8121F → A in AAH12281 (PubMed:15489334).Curated
Sequence conflicti814 – 8141V → I in AAH12281 (PubMed:15489334).Curated
Sequence conflicti816 – 8172DS → VA in AAH12281 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004996 mRNA. Translation: BAB23730.1.
AK145490 mRNA. Translation: BAE26467.1.
BC012281 mRNA. Translation: AAH12281.1.
CCDSiCCDS25552.1.
RefSeqiNP_079586.1. NM_025310.2.
UniGeneiMm.29795.

Genome annotation databases

EnsembliENSMUST00000021048; ENSMUSP00000021048; ENSMUSG00000020706.
GeneIDi56095.
KEGGimmu:56095.
UCSCiuc007lym.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004996 mRNA. Translation: BAB23730.1.
AK145490 mRNA. Translation: BAE26467.1.
BC012281 mRNA. Translation: AAH12281.1.
CCDSiCCDS25552.1.
RefSeqiNP_079586.1. NM_025310.2.
UniGeneiMm.29795.

3D structure databases

ProteinModelPortaliQ9DBE9.
SMRiQ9DBE9. Positions 24-184.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207815. 2 interactions.
IntActiQ9DBE9. 1 interaction.
MINTiMINT-4128230.
STRINGi10090.ENSMUSP00000021048.

PTM databases

iPTMnetiQ9DBE9.
PhosphoSiteiQ9DBE9.

Proteomic databases

EPDiQ9DBE9.
MaxQBiQ9DBE9.
PaxDbiQ9DBE9.
PRIDEiQ9DBE9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021048; ENSMUSP00000021048; ENSMUSG00000020706.
GeneIDi56095.
KEGGimmu:56095.
UCSCiuc007lym.1. mouse.

Organism-specific databases

CTDi117246.
MGIiMGI:1860295. Ftsj3.

Phylogenomic databases

eggNOGiKOG1098. Eukaryota.
COG0293. LUCA.
GeneTreeiENSGT00550000075004.
HOGENOMiHOG000176256.
HOVERGENiHBG075246.
InParanoidiQ9DBE9.
KOiK14857.
OMAiPTEMADP.
OrthoDBiEOG7WX07S.
PhylomeDBiQ9DBE9.
TreeFamiTF106102.

Miscellaneous databases

NextBioi311920.
PROiQ9DBE9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBE9.
CleanExiMM_FTSJ3.
GenevisibleiQ9DBE9. MM.

Family and domain databases

Gene3Di3.40.50.150. 1 hit.
HAMAPiMF_01547. RNA_methyltr_E.
MF_03163. RNA_methyltr_E_SPB1.
InterProiIPR015507. rRNA-MeTfrase_E.
IPR012920. rRNA_MeTfrase_Spb1_C.
IPR024576. rRNA_MeTfrase_Spb1_DUF3381.
IPR002877. rRNA_MeTrfase_FtsJ_dom.
IPR029063. SAM-dependent_MTases.
IPR028589. Spb1.
[Graphical view]
PANTHERiPTHR10920. PTHR10920. 3 hits.
PTHR10920:SF13. PTHR10920:SF13. 3 hits.
PfamiPF11861. DUF3381. 1 hit.
PF01728. FtsJ. 1 hit.
PF07780. Spb1_C. 1 hit.
[Graphical view]
SUPFAMiSSF53335. SSF53335. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Liver.
  2. "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].
    Strain: Czech II.
    Tissue: Mammary gland.
  3. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 226-233, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  4. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
    Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
    J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Teratocarcinoma.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335 AND SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335 AND SER-336, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  7. Cited for: CITRULLINATION AT ARG-390 AND ARG-774.

Entry informationi

Entry nameiSPB1_MOUSE
AccessioniPrimary (citable) accession number: Q9DBE9
Secondary accession number(s): Q3ULI1, Q921I7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: May 11, 2016
This is version 111 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

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 one 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.