Q8IY81 (SPB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
pre-rRNA processing protein FTSJ3
EC=2.1.1.-

Alternative name(s):
2'-O-ribose RNA methyltransferase SPB1 homolog
Protein ftsJ homolog 3
Putative rRNA methyltransferase 3

Gene names

Name:	FTSJ3
ORF Names:	SB92

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	847 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Probable methyltransferase involved in the processing of the 34S pre-rRNA to 18S rRNA and in 40S ribosomal subunit formation. Ref.16
Catalytic activity	S-adenosyl-L-methionine + rRNA = S-adenosyl-L-homocysteine + rRNA containing 2'-O-methylnucleoside. HAMAP-Rule MF_03163
Subunit structure	Interacts with NIP7. Ref.16
Subcellular location	Nucleus › nucleolus Ref.7 Ref.16.
Sequence similarities	Belongs to the methyltransferase superfamily. RlmE family. SPB1 subfamily.
Sequence caution	The sequence BAA90924.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Ribosome biogenesis rRNA processing
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Ligand	S-adenosyl-L-methionine
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	RNA methylation Inferred from electronic annotation. Source: InterPro rRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	methyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
EIF2AK2	P19525	2	EBI-744088,EBI-640775
OAS3	Q9Y6K5	2	EBI-744088,EBI-6115729

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 847	847	pre-rRNA processing protein FTSJ3 HAMAP-Rule MF_03163		PRO_0000155577
Regions
	Coiled coil	355 – 407	53	Potential
	Coiled coil	739 – 777	39	Potential
Sites
	Active site	157	1	Proton acceptor By similarity
	Binding site	56	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	58	1	S-adenosyl-L-methionine; via amide nitrogen By similarity
	Binding site	76	1	S-adenosyl-L-methionine By similarity
	Binding site	92	1	S-adenosyl-L-methionine By similarity
	Binding site	117	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	333	1	Phosphoserine Ref.11 Ref.12 Ref.17
	Modified residue	335	1	Phosphoserine Ref.11 Ref.12 Ref.17
	Modified residue	336	1	Phosphoserine Ref.11 Ref.12 Ref.14 Ref.17
	Modified residue	347	1	Phosphoserine Ref.11
	Modified residue	356	1	Phosphoserine Ref.12
	Modified residue	371	1	Phosphothreonine Ref.12
	Modified residue	549	1	Phosphoserine Ref.12
	Modified residue	584	1	Phosphoserine Ref.12 Ref.14 Ref.17
	Modified residue	644	1	Phosphoserine Ref.12 Ref.14 Ref.17
	Modified residue	676	1	Phosphoserine Ref.14
	Modified residue	688	1	Phosphoserine Ref.14
Natural variations
	Natural variant	91	1	Q → E. Ref.1 Ref.2 Ref.5 Corresponds to variant rs2584625 [ dbSNP | Ensembl ].		VAR_023284
	Natural variant	424	1	S → C. Ref.1 Ref.2 Ref.5 Ref.6 Corresponds to variant rs2727288 [ dbSNP | Ensembl ].		VAR_023285
Experimental info
	Sequence conflict	278	1	E → I in AAL56015. Ref.1
	Sequence conflict	278	1	E → I in BAA90924. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q8IY81 [UniParc]. Last modified May 18, 2010. Version 2. Checksum: 06B2F4D28A48026F	FASTA	847	96,558
	10 20 30 40 50 60 MGKKGKVGKS RRDKFYHLAK ETGYRSRSAF KLIQLNRRFQ FLQKARALLD LCAAPGGWLQ 70 80 90 100 110 120 VAAKFMPVSS LIVGVDLVPI KPLPNVVTLQ QDITTERCRQ ALRKELKTWK VDVVLNDGAP 130 140 150 160 170 180 NVGASWVHDA YSQAHLTLMA LRLACDFLAR GGSFITKVFR SRDYQPLLWI FQQLFRRVQA 190 200 210 220 230 240 TKPQASRHES AEIFVVCQGF LAPDKVDSKF FDPKFAFKEV EVQAKTVTEL VTKKKPKAEG 250 260 270 280 290 300 YAEGDLTLYH RTSVTDFLRA ANPVDFLSKA SEIMVDDEEL AQHPATTEDI RVCCQDIRVL 310 320 330 340 350 360 GRKELRSLLN WRTKLRRYVA KKLKEQAKAL DISLSSGEED EGDEEDSTAG TTKQPSKEEE 370 380 390 400 410 420 EEEEEEQLNQ TLAEMKAQEV AELKRKKKKL LREQRKQRER VELKMDLPGV SIADEGETGM 430 440 450 460 470 480 FSLSTIRGHQ LLEEVTQGDM SAADTFLSDL PRDDIYVSDV EDDGDDTSLD SDLDPEELAG 490 500 510 520 530 540 VRGHQGLRDQ KRMRLTEVQD DKEEEEEENP LLVPLEEKAV LQEEQANLWF SKGSFAGIED 550 560 570 580 590 600 DADEALEISQ AQLLFENRRK GRQQQQKQQL PQTPPSCLKT EIMSPLYQDE APKGTEASSG 610 620 630 640 650 660 TEAATGLEGE EKDGISDSDS STSSEEEESW EPLRGKKRSR GPKSDDDGFE IVPIEDPAKH 670 680 690 700 710 720 RILDPEGLAL GAVIASSKKA KRDLIDNSFN RYTFNEDEGE LPEWFVQEEK QHRIRQLPVG 730 740 750 760 770 780 KKEVEHYRKR WREINARPIK KVAEAKARKK RRMLKRLEQT RKKAEAVVNT VDISEREKVA 790 800 810 820 830 840 QLRSLYKKAG LGKEKRHVTY VVAKKGVGRK VRRPAGVRGH FKVVDSRMKK DQRAQQRKEQ KKKHKRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	Zhang W., Li N., Wan T., Chen T., Cao T. Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLU-91 AND CYS-424.
[2]	"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], VARIANTS GLU-91 AND CYS-424. Tissue: Colon and Placenta.
[3]	"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage." Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C. Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"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], VARIANTS GLU-91 AND CYS-424. Tissue: Placenta and Skin.
[6]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-847, VARIANT CYS-424. Tissue: Melanoma.
[7]	"Functional proteomic analysis of human nucleolus." Scherl A., Coute Y., Deon C., Calle A., Kindbeiter K., Sanchez J.-C., Greco A., Hochstrasser D.F., Diaz J.-J. Mol. Biol. Cell 13:4100-4109(2002) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[8]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[9]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[10]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336 AND SER-347, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333; SER-335; SER-336; SER-356; THR-371; SER-549; SER-584 AND SER-644, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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-336; SER-584; SER-644; SER-676 AND SER-688, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]	"The human nucleolar protein FTSJ3 associates with NIP7 and functions in pre-rRNA processing." Morello L.G., Coltri P.P., Quaresma A.J., Simabuco F.M., Silva T.C., Singh G., Nickerson J.A., Oliveira C.C., Moore M.J., Zanchin N.I. PLoS ONE 6:E29174-E29174(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH NIP7, SUBCELLULAR LOCATION.
[17]	"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-333; SER-335; SER-336; SER-584 AND SER-644, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF327355 mRNA. Translation: AAL56015.1. AK000069 mRNA. Translation: BAA90924.1. Different initiation. AK315010 mRNA. Translation: BAG37502.1. AC015651 Genomic DNA. No translation available. CH471109 Genomic DNA. Translation: EAW94273.1. CH471109 Genomic DNA. Translation: EAW94274.1. CH471109 Genomic DNA. Translation: EAW94275.1. BC000131 mRNA. Translation: AAH00131.2. BC036710 mRNA. Translation: AAH36710.1. AL834482 mRNA. Translation: CAD39141.1.
IPI	IPI00217686.
RefSeq	NP_060117.3. NM_017647.3.
UniGene	Hs.463785.
3D structure databases
ProteinModelPortal	Q8IY81.
SMR	Q8IY81. Positions 24-184.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8IY81. 11 interactions.
MINT	MINT-1468947.
STRING	9606.ENSP00000337518.
PTM databases
PhosphoSite	Q8IY81.
Polymorphism databases
DMDM	296452883.
2D gel databases
SWISS-2DPAGE	Q8IY81.
Proteomic databases
PaxDb	Q8IY81.
PRIDE	Q8IY81.
Protocols and materials databases
DNASU	117246.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000427159; ENSP00000396673; ENSG00000108592. ENST00000582115; ENSP00000462347; ENSG00000108592.
GeneID	117246.
KEGG	hsa:117246.
UCSC	uc002jbz.3. human.
Organism-specific databases
CTD	117246.
GeneCards	GC17M061896.
HGNC	HGNC:17136. FTSJ3.
HPA	HPA055544.
neXtProt	NX_Q8IY81.
PharmGKB	PA28419.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0293.
HOVERGEN	HBG075246.
InParanoid	Q8IY81.
KO	K14857.
OMA	REQMLDD.
OrthoDB	EOG4RXXZS.
PhylomeDB	Q8IY81.
Gene expression databases
Bgee	Q8IY81.
CleanEx	HS_FTSJ3.
Genevestigator	Q8IY81.
GermOnline	ENSG00000108592. Homo sapiens.
Family and domain databases
HAMAP	MF_01547. RNA_methyltr_E. MF_03163. RNA_methyltr_E_SPB1.
InterPro	IPR015507. rRNA-MeTfrase_E. IPR012920. rRNA_MeTfrase_Spb1_C. IPR024576. rRNA_MeTfrase_Spb1_DUF3381. IPR002877. rRNA_MeTrfase_FtsJ_dom. [Graphical view]
PANTHER	PTHR10920. PTHR10920. 1 hit.
Pfam	PF11861. DUF3381. 1 hit. PF01728. FtsJ. 1 hit. PF07780. Spb1_C. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FTSJ3. human.
GenomeRNAi	117246.
NextBio	80174.

Entry information

Entry name

SPB1_HUMAN

Accession

Primary (citable) accession number: Q8IY81
Secondary accession number(s): B2RCA5 , D3DU22, Q8N3A3, Q8WXX1, Q9BWM4, Q9NXT6

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2005
Last sequence update:	May 18, 2010
Last modified:	May 1, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.