Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  m7GpppX diphosphatase  

UniProtKB / Swiss-Prot ID :  DCPS_HUMAN

Gene Name (Synonyms) : 
DCPS, DCS1, HINT5 HSPC015  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. Nucleus. 

Protein Function :  Necessary for the complete degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA fragments shorter than 10 nucleotides that are produced by 3'->5' exosome-mediated mRNA decay. Releases m7GMP. Can also degrade m7GDP to m7GMP. Has no activity towards mRNA molecules longer than 25 nucleotides. 

Protein Sequence MADAAPQLGKRKRELDVEEAHAASTEEKEAGVGNGTCAPVRLPFSGFRLQKVLRESARDKIIFLHGKVNE...
Predicted Secondary Structure CCCCCCCHHHHHHHCCHHHHCCCCCCCHHCCCCCCCCCCEECCCCCEEEEEEECCCCCCEEEEEEEEEEC...
Protein Variant
LocationDescription
73G -> E (in dbSNP:rs11557735). VAR_027958
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
Protein Variant
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MADAAP
---CCCCCC
18.36UniProtKB
Link-
128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LNDVKTTVV
CCCEEEEEE
41.14Phosphositeplus
Link
138Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PATEKHLQK
CCCHHHHHH
45.31Phosphositeplus
Link
138N6-acetyllysinePATEKHLQK
CCCHHHHHH
45.31HPRD
Link
138N6-acetyllysinePATEKHLQK
CCCHHHHHH
45.31Phosphositeplus
Link
138N6-acetyllysine.PATEKHLQK
CCCHHHHHH
45.31UniProtKB
Link
142N6-acetyllysineKHLQKYLRQ
HHHHHHHHH
53.24HPRD
Link
142N6-acetyllysineKHLQKYLRQ
HHHHHHHHH
53.24Phosphositeplus
Link
142N6-acetyllysine.KHLQKYLRQ
HHHHHHHHH
53.24UniProtKB
Link
329Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DPLLKLLQE
CHHHHHHHH
55.63Phosphositeplus
Link
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
DCPS_HUMANin vitroHPRD:16787HPRD15068804
XRN1_HUMANENSP00000263579STRING
ACE_HUMANENSP00000263579STRING
ACET_HUMANENSP00000263579STRING
LSM1_HUMANENSP00000263579STRING
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Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-138 AND LYS-142, AND MASSSPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures