dbPTM

NSUN2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	NSUN2_MOUSE
UniProt AC	Q1HFZ0
Protein Name	tRNA (cytosine(34)-C(5))-methyltransferase
Gene Name	Nsun2
Organism	Mus musculus (Mouse).
Sequence Length	757
Subcellular Localization	Nucleus, nucleolus. Cytoplasm, cytoskeleton, spindle. Concentrated in the nucleolus during interphase and translocates to the spindle during mitosis as an RNA-protein complex that includes 18S ribosomal RNA.
Protein Description	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 (By similarity). 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..
Protein Sequence	MGRRARGRRFQQPPQPEGEEDASDGGRKRGQAGWEGGYPEIVKENKLFEHYYQELKIVPEGEWDQFMESLREPLPATLRITGYKSHAKEILHCLKNKYFKELEDLEVDGQKVEVPQPLSWYPEELAWHTNLSRKILRKSPLLAKFHQFLVSETESGNISRQEAVSMIPPLLLNVEPHHKILDMCAAPGSKTTQLIEMLHADMSVPFPEGFVIANDVDNKRCYLLVHQAKRLSSPCIMVVNHDASSIPRLTVDVDGRKEILFYDRILCDVPCSGDGTMRKNIDVWKKWTTLNSLQLHGLQLRIATRGAEQLAEGGRMVYSTCSLNPVEDEAVIAALLEKSEGALELADVSAELPGLKWMPGVSQWKVMTRDGQWFADWHEVPQGRHTQIRPTMFPPTDLEKLQAMHLERCLRILPHHQNTGGFFVAVLVKKAPMPWNKRQPKVQNKSAEAREPRVSSHVAATEGNPSDQSELESQMITGAGDSETAHNTENTESNEKKDGVCGPPPSKKMKLFGFKEDPFVFIPEDDPLFPPIEKFYALDPSFPRMNLLTRTTEGKKRQLYMVSKELRNVLLNNSEKMKVINTGIKVWCRNNSGEEFDCAFRLAQEGIYTLYPFINSRIITVSMEDVKTLLTQENPFFRKLSSEAYSQVKDLAKGSVVLKYEPDSANPDTLQCPIVLCGWRGKASIRTFVPKNERLHYLRMMGLEVLGEKKKEGVILTNENAASPEQPGDEDAKQTAQDPCVPDSVPGCDAAAAEPSR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
23	Phosphorylation	PEGEEDASDGGRKRG CCCCCCCCCCCCCCC	49.46	27087446
46	Ubiquitination	PEIVKENKLFEHYYQ HHHHHHCCCHHHHHH	56.49	22790023
52	Phosphorylation	NKLFEHYYQELKIVP CCCHHHHHHHCCCCC	9.45	-
69	Phosphorylation	EWDQFMESLREPLPA HHHHHHHHHHCCCCC	22.42	27566939
139	Phosphorylation	SRKILRKSPLLAKFH HHHHHHHCHHHHHHH	17.85	-
144	Ubiquitination	RKSPLLAKFHQFLVS HHCHHHHHHHHHHHC	43.26	22790023
235	Glutathionylation	AKRLSSPCIMVVNHD HHCCCCCEEEEECCC	3.19	24333276
286	Acetylation	KNIDVWKKWTTLNSL CCHHHHHHHEECHHH	33.78	22826441
321	Glutathionylation	GRMVYSTCSLNPVED CEEEEEECCCCCCCC	3.42	24333276
365	Ubiquitination	MPGVSQWKVMTRDGQ CCCCCEEEEEECCCC	17.94	22790023
445	Acetylation	RQPKVQNKSAEAREP CCCCCCCCCHHHCCC	33.67	23806337
455	Phosphorylation	EAREPRVSSHVAATE HHCCCCHHHCCEECC	18.92	25777480
456	Phosphorylation	AREPRVSSHVAATEG HCCCCHHHCCEECCC	21.08	25777480
461	Phosphorylation	VSSHVAATEGNPSDQ HHHCCEECCCCCCCH	34.39	25777480
466	Phosphorylation	AATEGNPSDQSELES EECCCCCCCHHHHHH	52.89	25777480
469	Phosphorylation	EGNPSDQSELESQMI CCCCCCHHHHHHHCC	49.49	25777480
473	Phosphorylation	SDQSELESQMITGAG CCHHHHHHHCCCCCC	37.36	25777480
477	Phosphorylation	ELESQMITGAGDSET HHHHHCCCCCCCCCC	18.68	25777480
482	Phosphorylation	MITGAGDSETAHNTE CCCCCCCCCCCCCCC	35.61	25777480
484	Phosphorylation	TGAGDSETAHNTENT CCCCCCCCCCCCCCC	36.85	25777480
488	Phosphorylation	DSETAHNTENTESNE CCCCCCCCCCCCCCC	22.27	25777480
491	Phosphorylation	TAHNTENTESNEKKD CCCCCCCCCCCCCCC	34.26	25777480
493	Phosphorylation	HNTENTESNEKKDGV CCCCCCCCCCCCCCC	48.53	25777480
585	Acetylation	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	23806337
585	Malonylation	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	26320211
585	N6-malonyllysine	KVINTGIKVWCRNNS EEEECCCEEEEECCC	30.90	-
592	Phosphorylation	KVWCRNNSGEEFDCA EEEEECCCCCCCHHH	51.64	23684622
608	Phosphorylation	RLAQEGIYTLYPFIN HHHHCCHHHHHHHHC	11.10	22817900
622	Phosphorylation	NSRIITVSMEDVKTL CCEEEEEEHHHHHHH	14.06	29514104
639	Ubiquitination	QENPFFRKLSSEAYS CCCHHHHHHCHHHHH	47.79	22790023
645	Phosphorylation	RKLSSEAYSQVKDLA HHHCHHHHHHHHHHH	8.79	-
655	Phosphorylation	VKDLAKGSVVLKYEP HHHHHCCCEEEEECC	14.35	29176673
672	Glutathionylation	ANPDTLQCPIVLCGW CCCCCCCCCEEEECC	2.53	24333276
717	Phosphorylation	KKEGVILTNENAASP CCCCEEEECCCCCCC	29.39	24925903
723	Phosphorylation	LTNENAASPEQPGDE EECCCCCCCCCCCCC	26.93	24925903
735	Phosphorylation	GDEDAKQTAQDPCVP CCCCHHHHCCCCCCC	26.11	25159016
744	Phosphorylation	QDPCVPDSVPGCDAA CCCCCCCCCCCCCHH	24.92	26239621
756	Phosphorylation	DAAAAEPSR------ CHHHCCCCC------	41.97	25777480

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
139	S	Phosphorylation	Kinase	AURKB	O70126	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
139	S	Phosphorylation		-
Phosphorylated at Ser-139 by AURKB during mitosis, leading to abolish methyltransferase activity and the interaction with NPM1.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of NSUN2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of NSUN2_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of NSUN2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Phosphoproteomic analysis of the developing mouse brain."; Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.; Mol. Cell. Proteomics 3:1093-1101(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-723, AND MASSSPECTROMETRY.	15345747 [Abstract]

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