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Sep. 10, 2014:
A total of 174 experimentally verified S-nitrosylation sites on 94 S-nitrosylated proteins from individualized human colorectal cancer tissues using a label-free quantitation strategy.

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Protein Name: Histone-lysine N-methyltransferase EHMT1

UniprotKB/SwissProt ID: Q9H9B1 (Q9H9B1)

Gene Name: EHMT1

Organism: Homo sapiens (Human)

Function: Histone methyltransferase that specifically mono- and dimethylates 'Lys-9' of histone H3 (H3K9me1 and H3K9me2, respectively) in euchromatin. H3K9me represents a specific tag for epigenetic transcriptional repression by recruiting HP1 proteins to methylated histones. Also weakly methylates 'Lys-27' of histone H3 (H3K27me). Also required for DNA methylation, the histone methyltransferase activity is not required for DNA methylation, suggesting that these 2 activities function independently. Probably targeted to histone H3 by different DNA-binding proteins like E2F6, MGA, MAX and/or DP1. During G0 phase, it probably contributes to silencing of MYC- and E2F-responsive genes, suggesting a role in G0/G1 transition in cell cycle. In addition to the histone methyltransferase activity, also methylates non-histone proteins: mediates dimethylation of 'Lys-373' of p53/TP53. Represses the expression of mitochondrial function-related genes, perhaps by occupying their promoter regions, working in concert with probable chromatin reader BAZ2B (By similarity)

Other Modifications: View all modification sites in dbPTM

Protein Subcellular Localization: Nucleus. Chromosome

Graphical Visualization of S-nitrosylation Sites:
InterPro ID Domain Name
IPR002110 Ankyrin_rpt
IPR036770 Ankyrin_rpt-contain_sf
IPR043550 EHMT1/EHMT2
IPR047762 EHMT_CRR
IPR007728 Pre-SET_dom
IPR001214 SET_dom
IPR046341 SET_dom_sf
IPR038035 SET_EHMT1

The S-nitrosylation sites of Q9H9B1

No. Position S-nitrosylated Peptide Secondary Structure of S-nitrosylated Peptide Solvent Accessibility of nitrosylated Site PubMed ID
1 1045 PSNYKYVSQN C VTSPMNIDRN   
2 1153 LQDIPPGTFV C EYVGELISDS   
3 19 VPARGEPQQD C CVKTELLGEE   
4 20 PARGEPQQDC C VKTELLGEET   
5 540 REITTLANNQ C MATESVDHEL   
6 553 TESVDHELGR C TNSVVKYELM