Q08J23 (NSUN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
tRNA (cytosine(34)-C(5))-methyltransferase
EC=2.1.1.203

Alternative name(s):
Myc-induced SUN domain-containing protein
Short name=Misu
NOL1/NOP2/Sun domain family member 2
Substrate of AIM1/Aurora kinase B
tRNA (cytosine-5-)-methyltransferase
tRNA methyltransferase 4 homolog
Short name=hTrm4

Gene names

Name:	NSUN2
Synonyms:	SAKI, TRM4

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	767 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RNA methyltransferase that methylates tRNAs, and possibly RNA polymerase III transcripts. Methylates cytosine to 5-methylcytosine (m5C) at position 34 of intron-containing tRNA(Leu)(CAA) precursors. Not able to modify tRNAs at positions 48 or 49. May act downstream of Myc to regulate epidermal cell growth and proliferation. Required for proper spindle assembly and chromosome segregation, independently of its methyltransferase activity. Ref.8 Ref.11
Catalytic activity	S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor. Ref.8
Subunit structure	Interacts with NPM1 and NCL during interphase; interaction is disrupted following phosphorylation at Ser-139. Ref.1
Subcellular location	Nucleus › nucleolus. Cytoplasm › cytoskeleton › spindle. Note: Concentrated in the nucleolus during interphase and translocates to the spindle during mitosis as an RNA-protein complex that includes 18S ribosomal RNA. Ref.1 Ref.11
Post-translational modification	Phosphorylated at Ser-139 by AURKB during mitosis, leading to abolish methyltransferase activity and the interaction with NPM1. Ref.1
Involvement in disease	Mental retardation, autosomal recessive 5 (MRT5) [MIM:611091]: A disorder characterized by significantly below average general intellectual functioning associated with impairments in adaptative behavior and manifested during the developmental period. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17
Sequence similarities	Belongs to the methyltransferase superfamily. RsmB/NOP family. TRM4 subfamily.
Sequence caution	The sequence BAA91075.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended. The sequence BAB14762.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis tRNA processing
Cellular component	Cytoplasm Cytoskeleton Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Mental retardation
Ligand	RNA-binding S-adenosyl-L-methionine tRNA-binding
Molecular function	Methyltransferase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from direct assay Ref.8. Source: UniProtKB nucleolus Inferred from direct assay Ref.8. Source: UniProtKB spindle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	tRNA (cytosine-5-)-methyltransferase activity Inferred from direct assay Ref.8. Source: UniProtKB tRNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q08J23-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: Q08J23-2)

The sequence of this isoform differs from the canonical sequence as follows:
     85-120: SHAKEILHCLKNKYFKELEDLEVDGQKVEVPQPLSW → R

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 767	767	tRNA (cytosine(34)-C(5))-methyltransferase		PRO_0000289223
Regions
	Region	184 – 190	7	S-adenosyl-L-methionine binding By similarity
Sites
	Active site	321	1	Nucleophile Potential
	Binding site	215	1	S-adenosyl-L-methionine By similarity
	Binding site	242	1	S-adenosyl-L-methionine By similarity
	Binding site	268	1	S-adenosyl-L-methionine By similarity
Amino acid modifications
	Modified residue	139	1	Phosphoserine; by AURKB Ref.1
	Modified residue	456	1	Phosphoserine Ref.10 Ref.13
	Modified residue	473	1	Phosphoserine Ref.10 Ref.16
	Modified residue	586	1	N6-malonyllysine Ref.15
	Modified residue	593	1	Phosphoserine Ref.13 Ref.16
	Modified residue	724	1	Phosphoserine By similarity
	Modified residue	743	1	Phosphoserine Ref.6 Ref.7 Ref.9 Ref.10 Ref.12 Ref.13
	Modified residue	751	1	Phosphoserine Ref.6 Ref.7 Ref.9 Ref.10 Ref.12
Natural variations
	Alternative sequence	85 – 120	36	SHAKE…QPLSW → R in isoform 2.		VSP_042621
	Natural variant	627	1	V → I. Corresponds to variant rs2303708 [ dbSNP | Ensembl ].		VAR_032604
	Natural variant	679	1	G → R in MRT5; impairs proper intracellular localization. Ref.17		VAR_068530
Experimental info
	Mutagenesis	139	1	S → A: Induces a constitutive association with NPM1. Ref.1
	Mutagenesis	139	1	S → E: Mimicks constitutive phosphorylation and abolishes methyltransferase activity. Ref.1
	Sequence conflict	316	1	M → V in BAA91075. Ref.2
	Sequence conflict	594	1	G → D in BAB14762. Ref.2
	Sequence conflict	605	1	Q → R in BAF34150. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 29, 2007. Version 2. Checksum: FE4B34309978A8D2	FASTA	767	86,471
	10 20 30 40 50 60 MGRRSRGRRL QQQQRPEDAE DGAEGGGKRG EAGWEGGYPE IVKENKLFEH YYQELKIVPE 70 80 90 100 110 120 GEWGQFMDAL REPLPATLRI TGYKSHAKEI LHCLKNKYFK ELEDLEVDGQ KVEVPQPLSW 130 140 150 160 170 180 YPEELAWHTN LSRKILRKSP HLEKFHQFLV SETESGNISR QEAVSMIPPL LLNVRPHHKI 190 200 210 220 230 240 LDMCAAPGSK TTQLIEMLHA DMNVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN 250 260 270 280 290 300 HDASSIPRLQ IDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL 310 320 330 340 350 360 RIATRGAEQL AEGGRMVYST CSLNPIEDEA VIASLLEKSE GALELADVSN ELPGLKWMPG 370 380 390 400 410 420 ITQWKVMTKD GQWFTDWDAV PHSRHTQIRP TMFPPKDPEK LQAMHLERCL RILPHHQNTG 430 440 450 460 470 480 GFFVAVLVKK SSMPWNKRQP KLQGKSAETR ESTQLSPADL TEGKPTDPSK LESPSFTGTG 490 500 510 520 530 540 DTEIAHATED LENNGSKKDG VCGPPPSKKM KLFGFKEDPF VFIPEDDPLF PPIEKFYALD 550 560 570 580 590 600 PSFPRMNLLT RTTEGKKRQL YMVSKELRNV LLNNSEKMKV INTGIKVWCR NNSGEEFDCA 610 620 630 640 650 660 FRLAQEGIYT LYPFINSRII TVSMEDVKIL LTQENPFFRK LSSETYSQAK DLAKGSIVLK 670 680 690 700 710 720 YEPDSANPDA LQCPIVLCGW RGKASIRTFV PKNERLHYLR MMGLEVLGEK KKEGVILTNE 730 740 750 760 SAASTGQPDN DVTEGQRAGE PNSPDAEEAN SPDVTAGCDP AGVHPPR
	Isoform 2 [UniParc]. Checksum: 3C092217D0A3A22B	FASTA	732	82,393
	10 20 30 40 50 60 MGRRSRGRRL QQQQRPEDAE DGAEGGGKRG EAGWEGGYPE IVKENKLFEH YYQELKIVPE 70 80 90 100 110 120 GEWGQFMDAL REPLPATLRI TGYKRYPEEL AWHTNLSRKI LRKSPHLEKF HQFLVSETES 130 140 150 160 170 180 GNISRQEAVS MIPPLLLNVR PHHKILDMCA APGSKTTQLI EMLHADMNVP FPEGFVIAND 190 200 210 220 230 240 VDNKRCYLLV HQAKRLSSPC IMVVNHDASS IPRLQIDVDG RKEILFYDRI LCDVPCSGDG 250 260 270 280 290 300 TMRKNIDVWK KWTTLNSLQL HGLQLRIATR GAEQLAEGGR MVYSTCSLNP IEDEAVIASL 310 320 330 340 350 360 LEKSEGALEL ADVSNELPGL KWMPGITQWK VMTKDGQWFT DWDAVPHSRH TQIRPTMFPP 370 380 390 400 410 420 KDPEKLQAMH LERCLRILPH HQNTGGFFVA VLVKKSSMPW NKRQPKLQGK SAETRESTQL 430 440 450 460 470 480 SPADLTEGKP TDPSKLESPS FTGTGDTEIA HATEDLENNG SKKDGVCGPP PSKKMKLFGF 490 500 510 520 530 540 KEDPFVFIPE DDPLFPPIEK FYALDPSFPR MNLLTRTTEG KKRQLYMVSK ELRNVLLNNS 550 560 570 580 590 600 EKMKVINTGI KVWCRNNSGE EFDCAFRLAQ EGIYTLYPFI NSRIITVSME DVKILLTQEN 610 620 630 640 650 660 PFFRKLSSET YSQAKDLAKG SIVLKYEPDS ANPDALQCPI VLCGWRGKAS IRTFVPKNER 670 680 690 700 710 720 LHYLRMMGLE VLGEKKKEGV ILTNESAAST GQPDNDVTEG QRAGEPNSPD AEEANSPDVT 730 AGCDPAGVHP PR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Aurora-B regulates RNA methyltransferase NSUN2." Sakita-Suto S., Kanda A., Suzuki F., Sato S., Takata T., Tatsuka M. Mol. Biol. Cell 18:1107-1117(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-139, INTERACTION WITH NPM1 AND NCL, MUTAGENESIS OF SER-139.
[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] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-767 (ISOFORM 1).
[3]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton 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] (ISOFORM 1). Tissue: Lung and Placenta.
[6]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"Identification of human tRNA:m5C methyltransferase catalysing intron-dependent m5C formation in the first position of the anticodon of the pre-tRNA Leu (CAA)." Brzezicha B., Schmidt M., Makalowska I., Jarmolowski A., Pienkowska J., Szweykowska-Kulinska Z. Nucleic Acids Res. 34:6034-6043(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743 AND SER-751, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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-456; SER-473; SER-743 AND SER-751, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"The nucleolar RNA methyltransferase Misu (NSun2) is required for mitotic spindle stability." Hussain S., Benavente S.B., Nascimento E., Dragoni I., Kurowski A., Gillich A., Humphreys P., Frye M. J. Cell Biol. 186:27-40(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[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-743 AND SER-751, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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-456; SER-593 AND SER-743, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"The first identification of lysine malonylation substrates and its regulatory enzyme." Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y. Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(2011) [PubMed] [Europe PMC] [Abstract] Cited for: MALONYLATION AT LYS-586.
[16]	"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-473 AND SER-593, MASS SPECTROMETRY.
[17]	"Mutation in NSUN2, which encodes an RNA methyltransferase, causes autosomal-recessive intellectual disability." Khan M.A., Rafiq M.A., Noor A., Hussain S., Flores J.V., Rupp V., Vincent A.K., Malli R., Ali G., Khan F.S., Ishak G.E., Doherty D., Weksberg R., Ayub M., Windpassinger C., Ibrahim S., Frye M., Ansar M., Vincent J.B. Am. J. Hum. Genet. 90:856-863(2012) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MRT5 ARG-679, CHARACTERIZATION OF VARIANT MRT5 ARG-679.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB255451 mRNA. Translation: BAF34150.1. AK000310 mRNA. Translation: BAA91075.1. Different initiation. AK023994 mRNA. Translation: BAB14762.1. Different initiation. AK298980 mRNA. Translation: BAG61074.1. AC010366 Genomic DNA. No translation available. AC027334 Genomic DNA. No translation available. CH471102 Genomic DNA. Translation: EAX08105.1. BC001041 mRNA. Translation: AAH01041.3. BC137083 mRNA. Translation: AAI37084.1.
IPI	IPI00306369. IPI00966877.
RefSeq	NP_001180384.1. NM_001193455.1. NP_060225.4. NM_017755.5.
UniGene	Hs.481526.
3D structure databases
ProteinModelPortal	Q08J23.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q08J23. 7 interactions.
STRING	9606.ENSP00000264670.
PTM databases
PhosphoSite	Q08J23.
Polymorphism databases
DMDM	148887180.
Proteomic databases
PaxDb	Q08J23.
PeptideAtlas	Q08J23.
PRIDE	Q08J23.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264670; ENSP00000264670; ENSG00000037474. ENST00000506139; ENSP00000420957; ENSG00000037474.
GeneID	54888.
KEGG	hsa:54888.
UCSC	uc003jdt.3. human.
Organism-specific databases
CTD	54888.
GeneCards	GC05M006654.
H-InvDB	HIX0004733.
HGNC	HGNC:25994. NSUN2.
HPA	HPA037896.
MIM	610916. gene. 611091. phenotype.
neXtProt	NX_Q08J23.
Orphanet	88616. Autosomal recessive nonsyndromic intellectual deficit. 235. Dubowitz syndrome.
PharmGKB	PA134953940.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0144.
HOGENOM	HOG000205147.
HOVERGEN	HBG106711.
InParanoid	Q08J23.
KO	K15335.
OMA	PIEKFYA.
OrthoDB	EOG4K9BBQ.
PhylomeDB	Q08J23.
Enzyme and pathway databases
BioCyc	MetaCyc:HS12087-MONOMER.
Pathway_Interaction_DB	aurora_b_pathway. Aurora B signaling.
Gene expression databases
ArrayExpress	Q08J23.
Bgee	Q08J23.
CleanEx	HS_NSUN2.
Genevestigator	Q08J23.
Family and domain databases
InterPro	IPR001678. Fmu/NOL1/Nop2p. IPR023267. RCMT. IPR023270. RCMT_NCL1. [Graphical view]
Pfam	PF01189. Nol1_Nop2_Fmu. 1 hit. [Graphical view]
PRINTS	PR02008. RCMTFAMILY. PR02011. RCMTNCL1.
PROSITE	PS01153. NOL1_NOP2_SUN. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NSUN2. human.
GenomeRNAi	54888.
NextBio	57879.
SOURCE	Search...

Entry information

Entry name

NSUN2_HUMAN

Accession

Primary (citable) accession number: Q08J23
Secondary accession number(s): B2RNR4 , B4DQW2, Q9BVN4, Q9H858, Q9NXD9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	May 29, 2007
Last modified:	May 1, 2013
This is version 71 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.