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Q08J23 (NSUN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length767 AA.
Sequence statusComplete.
Protein existenceEvidence 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 positions 34 and 48 of intron-containing tRNA(Leu)(CAA) precursors, and at positions 48, 49 and 50 of tRNA(Gly)(GCC) precursors. 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.12 Ref.19

Catalytic activity

S-adenosyl-L-methionine + cytosine34 in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine34 in tRNA precursor. Ref.8

Enzyme regulation

Inhibited by magnesium ions. Ref.19

Subunit structure

Interacts with NPM1 and NCL during interphase; interaction is disrupted following phosphorylation at Ser-139. Ref.1

Subcellular location

Nucleusnucleolus. Cytoplasmcytoskeletonspindle. 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.12

Tissue specificity

Expressed in adult and fetal brain and in lymphoblastoid cells. Ref.18

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 adaptive behavior and manifested during the developmental period.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18 Ref.20

Sequence similarities

Belongs to the class I-like SAM-binding 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.

Alternative products

This entry describes 3 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.
Isoform 3 (identifier: Q08J23-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-236: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 767767tRNA (cytosine(34)-C(5))-methyltransferase
PRO_0000289223

Regions

Region184 – 1907S-adenosyl-L-methionine binding By similarity

Sites

Active site3211Nucleophile By similarity
Binding site2151S-adenosyl-L-methionine By similarity
Binding site2421S-adenosyl-L-methionine By similarity
Binding site2681S-adenosyl-L-methionine By similarity

Amino acid modifications

Modified residue1391Phosphoserine; by AURKB Ref.1
Modified residue4561Phosphoserine Ref.10 Ref.14
Modified residue4731Phosphoserine Ref.10 Ref.17
Modified residue5861N6-acetyllysine; alternate By similarity
Modified residue5861N6-malonyllysine; alternate Ref.16
Modified residue5931Phosphoserine Ref.14 Ref.17
Modified residue7241Phosphoserine By similarity
Modified residue7431Phosphoserine Ref.6 Ref.7 Ref.9 Ref.10 Ref.13 Ref.14
Modified residue7511Phosphoserine Ref.6 Ref.7 Ref.9 Ref.10 Ref.13

Natural variations

Alternative sequence1 – 236236Missing in isoform 3.
VSP_053598
Alternative sequence85 – 12036SHAKE…QPLSW → R in isoform 2.
VSP_042621
Natural variant6271V → I.
Corresponds to variant rs2303708 [ dbSNP | Ensembl ].
VAR_032604
Natural variant6791G → R in MRT5; impairs proper intracellular localization. Ref.20
VAR_068530

Experimental info

Mutagenesis1391S → A: Induces a constitutive association with NPM1. Ref.1
Mutagenesis1391S → E: Mimicks constitutive phosphorylation and abolishes methyltransferase activity. Ref.1
Sequence conflict3161M → V in BAA91075. Ref.2
Sequence conflict3271E → G in BAF83833. Ref.2
Sequence conflict4841I → V in BAG51521. Ref.2
Sequence conflict5941G → D in BAB14762. Ref.2
Sequence conflict6051Q → R in BAF34150. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 29, 2007. Version 2.
Checksum: FE4B34309978A8D2

FASTA76786,471
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 3C092217D0A3A22B
Show »

FASTA73282,393
Isoform 3 [UniParc].

Checksum: 69211E04631124B4
Show »

FASTA53159,384

References

« Hide '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. expand/collapse author list , 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] (ISOFORMS 1; 2 AND 3).
[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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"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.
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[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-456; SER-593 AND SER-743, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 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.
[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-473 AND SER-593, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[18]"Mutations in NSUN2 cause autosomal-recessive intellectual disability."
Abbasi-Moheb L., Mertel S., Gonsior M., Nouri-Vahid L., Kahrizi K., Cirak S., Wieczorek D., Motazacker M.M., Esmaeeli-Nieh S., Cremer K., Weissmann R., Tzschach A., Garshasbi M., Abedini S.S., Najmabadi H., Ropers H.H., Sigrist S.J., Kuss A.W.
Am. J. Hum. Genet. 90:847-855(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN MRT5, TISSUE SPECIFICITY.
[19]"The human tRNA m (5) C methyltransferase Misu is multisite-specific."
Auxilien S., Guerineau V., Szweykowska-Kulinska Z., Golinelli-Pimpaneau B.
RNA Biol. 9:1331-1338(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION.
[20]"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.
AK055456 mRNA. Translation: BAG51521.1.
AK291144 mRNA. Translation: BAF83833.1.
AK298980 mRNA. Translation: BAG61074.1.
AC010366 Genomic DNA. No translation available.
AC027334 Genomic DNA. No translation available.
CH471102 Genomic DNA. Translation: EAX08105.1.
CH471102 Genomic DNA. Translation: EAX08106.1.
BC001041 mRNA. Translation: AAH01041.3.
BC137083 mRNA. Translation: AAI37084.1.
CCDSCCDS3869.1. [Q08J23-1]
CCDS54832.1. [Q08J23-2]
RefSeqNP_001180384.1. NM_001193455.1. [Q08J23-2]
NP_060225.4. NM_017755.5. [Q08J23-1]
UniGeneHs.481526.

3D structure databases

ProteinModelPortalQ08J23.
SMRQ08J23. Positions 45-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120236. 58 interactions.
DIPDIP-52456N.
IntActQ08J23. 8 interactions.
MINTMINT-4851220.
STRING9606.ENSP00000264670.

PTM databases

PhosphoSiteQ08J23.

Polymorphism databases

DMDM148887180.

Proteomic databases

MaxQBQ08J23.
PaxDbQ08J23.
PeptideAtlasQ08J23.
PRIDEQ08J23.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264670; ENSP00000264670; ENSG00000037474. [Q08J23-1]
ENST00000506139; ENSP00000420957; ENSG00000037474. [Q08J23-2]
ENST00000539938; ENSP00000444338; ENSG00000037474. [Q08J23-3]
GeneID54888.
KEGGhsa:54888.
UCSCuc003jdt.3. human. [Q08J23-1]
uc011cmk.2. human. [Q08J23-2]

Organism-specific databases

CTD54888.
GeneCardsGC05M006654.
H-InvDBHIX0004733.
HGNCHGNC:25994. NSUN2.
HPAHPA037896.
MIM610916. gene.
611091. phenotype.
neXtProtNX_Q08J23.
Orphanet88616. Autosomal recessive nonsyndromic intellectual disability.
235. Dubowitz syndrome.
PharmGKBPA134953940.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0144.
HOGENOMHOG000205147.
HOVERGENHBG106711.
InParanoidQ08J23.
KOK15335.
OMAPIEKFYA.
OrthoDBEOG72VH5D.
PhylomeDBQ08J23.
TreeFamTF300702.

Enzyme and pathway databases

BioCycMetaCyc:HS12087-MONOMER.

Gene expression databases

ArrayExpressQ08J23.
BgeeQ08J23.
CleanExHS_NSUN2.
GenevestigatorQ08J23.

Family and domain databases

Gene3D3.40.50.150. 2 hits.
InterProIPR001678. Fmu/NOL1/Nop2p.
IPR023267. RCMT.
IPR023270. RCMT_NCL1.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamPF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view]
PRINTSPR02008. RCMTFAMILY.
PR02011. RCMTNCL1.
SUPFAMSSF53335. SSF53335. 2 hits.
PROSITEPS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSNSUN2. human.
GeneWikiNSUN2.
GenomeRNAi54888.
NextBio27034002.
PROQ08J23.
SOURCESearch...

Entry information

Entry nameNSUN2_HUMAN
AccessionPrimary (citable) accession number: Q08J23
Secondary accession number(s): A8K529 expand/collapse secondary AC list , B2RNR4, B3KP09, B4DQW2, G3V1R4, Q9BVN4, Q9H858, Q9NXD9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: July 9, 2014
This is version 84 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM