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Q08J23

- NSUN2_HUMAN

UniProt

Q08J23 - NSUN2_HUMAN

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Protein

tRNA (cytosine(34)-C(5))-methyltransferase

Gene

NSUN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

S-adenosyl-L-methionine + cytosine(34) in tRNA precursor = S-adenosyl-L-homocysteine + 5-methylcytosine(34) in tRNA precursor.1 Publication

Enzyme regulationi

Inhibited by magnesium ions.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei215 – 2151S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei242 – 2421S-adenosyl-L-methioninePROSITE-ProRule annotation
Binding sitei268 – 2681S-adenosyl-L-methioninePROSITE-ProRule annotation
Active sitei321 – 3211NucleophilePROSITE-ProRule annotation

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. tRNA (cytosine-5-)-methyltransferase activity Source: UniProtKB
  3. tRNA binding Source: UniProtKB-KW

GO - Biological processi

  1. mitotic nuclear division Source: UniProtKB-KW
  2. tRNA methylation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Methyltransferase, Transferase

Keywords - Biological processi

Cell cycle, Cell division, Mitosis, tRNA processing

Keywords - Ligandi

RNA-binding, S-adenosyl-L-methionine, tRNA-binding

Enzyme and pathway databases

BioCyciMetaCyc:HS12087-MONOMER.

Names & Taxonomyi

Protein namesi
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 namesi
Name:NSUN2
Synonyms:SAKI, TRM4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:25994. NSUN2.

Subcellular locationi

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.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoskeleton Source: UniProtKB-KW
  3. nucleolus Source: UniProtKB
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti679 – 6791G → R in MRT5; impairs proper intracellular localization. 1 Publication
VAR_068530

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi139 – 1391S → A: Induces a constitutive association with NPM1. 1 Publication
Mutagenesisi139 – 1391S → E: Mimicks constitutive phosphorylation and abolishes methyltransferase activity. 1 Publication

Keywords - Diseasei

Disease mutation, Mental retardation

Organism-specific databases

MIMi611091. phenotype.
Orphaneti88616. Autosomal recessive non-syndromic intellectual disability.
235. Dubowitz syndrome.
PharmGKBiPA134953940.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 767767tRNA (cytosine(34)-C(5))-methyltransferasePRO_0000289223Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei139 – 1391Phosphoserine; by AURKB1 Publication
Modified residuei456 – 4561Phosphoserine2 Publications
Modified residuei473 – 4731Phosphoserine2 Publications
Modified residuei586 – 5861N6-acetyllysine; alternateBy similarity
Modified residuei586 – 5861N6-malonyllysine; alternate1 Publication
Modified residuei593 – 5931Phosphoserine2 Publications
Modified residuei724 – 7241PhosphoserineBy similarity
Modified residuei743 – 7431Phosphoserine6 Publications
Modified residuei751 – 7511Phosphoserine5 Publications

Post-translational modificationi

Phosphorylated at Ser-139 by AURKB during mitosis, leading to abolish methyltransferase activity and the interaction with NPM1.8 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ08J23.
PaxDbiQ08J23.
PeptideAtlasiQ08J23.
PRIDEiQ08J23.

PTM databases

PhosphoSiteiQ08J23.

Expressioni

Tissue specificityi

Expressed in adult and fetal brain and in lymphoblastoid cells.1 Publication

Gene expression databases

BgeeiQ08J23.
CleanExiHS_NSUN2.
GenevestigatoriQ08J23.

Organism-specific databases

HPAiHPA037896.

Interactioni

Subunit structurei

Interacts with NPM1 and NCL during interphase; interaction is disrupted following phosphorylation at Ser-139.1 Publication

Protein-protein interaction databases

BioGridi120236. 62 interactions.
DIPiDIP-52456N.
IntActiQ08J23. 8 interactions.
MINTiMINT-4851220.
STRINGi9606.ENSP00000264670.

Structurei

3D structure databases

ProteinModelPortaliQ08J23.
SMRiQ08J23. Positions 45-427.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni184 – 1907S-adenosyl-L-methionine bindingPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the class I-like SAM-binding methyltransferase superfamily. RsmB/NOP family. TRM4 subfamily.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0144.
GeneTreeiENSGT00660000095589.
HOGENOMiHOG000205147.
HOVERGENiHBG106711.
InParanoidiQ08J23.
KOiK15335.
OMAiPIEKFYA.
OrthoDBiEOG72VH5D.
PhylomeDBiQ08J23.
TreeFamiTF300702.

Family and domain databases

Gene3Di3.40.50.150. 2 hits.
InterProiIPR001678. Fmu/NOL1/Nop2p.
IPR023267. RCMT.
IPR023270. RCMT_NCL1.
IPR029063. SAM-dependent_MTases-like.
[Graphical view]
PfamiPF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view]
PRINTSiPR02008. RCMTFAMILY.
PR02011. RCMTNCL1.
SUPFAMiSSF53335. SSF53335. 2 hits.
PROSITEiPS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q08J23-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MGRRSRGRRL QQQQRPEDAE DGAEGGGKRG EAGWEGGYPE IVKENKLFEH
60 70 80 90 100
YYQELKIVPE GEWGQFMDAL REPLPATLRI TGYKSHAKEI LHCLKNKYFK
110 120 130 140 150
ELEDLEVDGQ KVEVPQPLSW YPEELAWHTN LSRKILRKSP HLEKFHQFLV
160 170 180 190 200
SETESGNISR QEAVSMIPPL LLNVRPHHKI LDMCAAPGSK TTQLIEMLHA
210 220 230 240 250
DMNVPFPEGF VIANDVDNKR CYLLVHQAKR LSSPCIMVVN HDASSIPRLQ
260 270 280 290 300
IDVDGRKEIL FYDRILCDVP CSGDGTMRKN IDVWKKWTTL NSLQLHGLQL
310 320 330 340 350
RIATRGAEQL AEGGRMVYST CSLNPIEDEA VIASLLEKSE GALELADVSN
360 370 380 390 400
ELPGLKWMPG ITQWKVMTKD GQWFTDWDAV PHSRHTQIRP TMFPPKDPEK
410 420 430 440 450
LQAMHLERCL RILPHHQNTG GFFVAVLVKK SSMPWNKRQP KLQGKSAETR
460 470 480 490 500
ESTQLSPADL TEGKPTDPSK LESPSFTGTG DTEIAHATED LENNGSKKDG
510 520 530 540 550
VCGPPPSKKM KLFGFKEDPF VFIPEDDPLF PPIEKFYALD PSFPRMNLLT
560 570 580 590 600
RTTEGKKRQL YMVSKELRNV LLNNSEKMKV INTGIKVWCR NNSGEEFDCA
610 620 630 640 650
FRLAQEGIYT LYPFINSRII TVSMEDVKIL LTQENPFFRK LSSETYSQAK
660 670 680 690 700
DLAKGSIVLK YEPDSANPDA LQCPIVLCGW RGKASIRTFV PKNERLHYLR
710 720 730 740 750
MMGLEVLGEK KKEGVILTNE SAASTGQPDN DVTEGQRAGE PNSPDAEEAN
760
SPDVTAGCDP AGVHPPR
Length:767
Mass (Da):86,471
Last modified:May 29, 2007 - v2
Checksum:iFE4B34309978A8D2
GO
Isoform 2 (identifier: Q08J23-2) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:732
Mass (Da):82,393
Checksum:i3C092217D0A3A22B
GO
Isoform 3 (identifier: Q08J23-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-236: Missing.

Note: No experimental confirmation available.

Show »
Length:531
Mass (Da):59,384
Checksum:i69211E04631124B4
GO

Sequence cautioni

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.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti316 – 3161M → V in BAA91075. (PubMed:14702039)Curated
Sequence conflicti327 – 3271E → G in BAF83833. (PubMed:14702039)Curated
Sequence conflicti484 – 4841I → V in BAG51521. (PubMed:14702039)Curated
Sequence conflicti594 – 5941G → D in BAB14762. (PubMed:14702039)Curated
Sequence conflicti605 – 6051Q → R in BAF34150. (PubMed:17215513)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti627 – 6271V → I.
Corresponds to variant rs2303708 [ dbSNP | Ensembl ].
VAR_032604
Natural varianti679 – 6791G → R in MRT5; impairs proper intracellular localization. 1 Publication
VAR_068530

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 236236Missing in isoform 3. 1 PublicationVSP_053598Add
BLAST
Alternative sequencei85 – 12036SHAKE…QPLSW → R in isoform 2. 1 PublicationVSP_042621Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS3869.1. [Q08J23-1]
CCDS54832.1. [Q08J23-2]
RefSeqiNP_001180384.1. NM_001193455.1. [Q08J23-2]
NP_060225.4. NM_017755.5. [Q08J23-1]
UniGeneiHs.481526.

Genome annotation databases

EnsembliENST00000264670; ENSP00000264670; ENSG00000037474. [Q08J23-1]
ENST00000506139; ENSP00000420957; ENSG00000037474. [Q08J23-2]
GeneIDi54888.
KEGGihsa:54888.
UCSCiuc003jdt.3. human. [Q08J23-1]
uc011cmk.2. human. [Q08J23-2]

Polymorphism databases

DMDMi148887180.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS3869.1. [Q08J23-1 ]
CCDS54832.1. [Q08J23-2 ]
RefSeqi NP_001180384.1. NM_001193455.1. [Q08J23-2 ]
NP_060225.4. NM_017755.5. [Q08J23-1 ]
UniGenei Hs.481526.

3D structure databases

ProteinModelPortali Q08J23.
SMRi Q08J23. Positions 45-427.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120236. 62 interactions.
DIPi DIP-52456N.
IntActi Q08J23. 8 interactions.
MINTi MINT-4851220.
STRINGi 9606.ENSP00000264670.

PTM databases

PhosphoSitei Q08J23.

Polymorphism databases

DMDMi 148887180.

Proteomic databases

MaxQBi Q08J23.
PaxDbi Q08J23.
PeptideAtlasi Q08J23.
PRIDEi Q08J23.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264670 ; ENSP00000264670 ; ENSG00000037474 . [Q08J23-1 ]
ENST00000506139 ; ENSP00000420957 ; ENSG00000037474 . [Q08J23-2 ]
GeneIDi 54888.
KEGGi hsa:54888.
UCSCi uc003jdt.3. human. [Q08J23-1 ]
uc011cmk.2. human. [Q08J23-2 ]

Organism-specific databases

CTDi 54888.
GeneCardsi GC05M006599.
H-InvDB HIX0004733.
HGNCi HGNC:25994. NSUN2.
HPAi HPA037896.
MIMi 610916. gene.
611091. phenotype.
neXtProti NX_Q08J23.
Orphaneti 88616. Autosomal recessive non-syndromic intellectual disability.
235. Dubowitz syndrome.
PharmGKBi PA134953940.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0144.
GeneTreei ENSGT00660000095589.
HOGENOMi HOG000205147.
HOVERGENi HBG106711.
InParanoidi Q08J23.
KOi K15335.
OMAi PIEKFYA.
OrthoDBi EOG72VH5D.
PhylomeDBi Q08J23.
TreeFami TF300702.

Enzyme and pathway databases

BioCyci MetaCyc:HS12087-MONOMER.

Miscellaneous databases

ChiTaRSi NSUN2. human.
GeneWikii NSUN2.
GenomeRNAii 54888.
NextBioi 27034002.
PROi Q08J23.
SOURCEi Search...

Gene expression databases

Bgeei Q08J23.
CleanExi HS_NSUN2.
Genevestigatori Q08J23.

Family and domain databases

Gene3Di 3.40.50.150. 2 hits.
InterProi IPR001678. Fmu/NOL1/Nop2p.
IPR023267. RCMT.
IPR023270. RCMT_NCL1.
IPR029063. SAM-dependent_MTases-like.
[Graphical view ]
Pfami PF01189. Nol1_Nop2_Fmu. 1 hit.
[Graphical view ]
PRINTSi PR02008. RCMTFAMILY.
PR02011. RCMTNCL1.
SUPFAMi SSF53335. SSF53335. 2 hits.
PROSITEi PS51686. SAM_MT_RSMB_NOP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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] (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.
    , 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. 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. 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. 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. Cited for: VARIANT MRT5 ARG-679, CHARACTERIZATION OF VARIANT MRT5 ARG-679.

Entry informationi

Entry nameiNSUN2_HUMAN
AccessioniPrimary (citable) accession number: Q08J23
Secondary accession number(s): A8K529
, B2RNR4, B3KP09, B4DQW2, G3V1R4, Q9BVN4, Q9H858, Q9NXD9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: October 29, 2014
This is version 87 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

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3