DCPS_YEAST - dbPTM
DCPS_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCPS_YEAST
UniProt AC Q06151
Protein Name m7GpppX diphosphatase
Gene Name DCS1 {ECO:0000312|SGD:S000004260}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 350
Subcellular Localization Cytoplasm. Cytoplasm, perinuclear region. Cytoplasm, P-body. Predominantly cytoplasmic.
Protein Description Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP) or tri-methyl guanosine nucleoside monophosphate (m3(2,2,7)GMP), respectively. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to (m(7)GMP) and m3(2,2,7)GMP, respectively.3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP' target='_blank'> [PubMed: 22985415 May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCS1 to m7GMP]
Protein Sequence MSQLPTDFASLIKRFQFVSVLDSNPQTKVMSLLGTIDNKDAIITAEKTHFLFDETVRRPSQDGRSTPVLYNCENEYSCINGIQELKEITSNDIYYWGLSVIKQDMESNPTAKLNLIWPATPIHIKKYEQQNFHLVRETPEMYKRIVQPYIEEMCNNGRLKWVNNILYEGAESERVVYKDFSEENKDDGFLILPDMKWDGMNLDSLYLVAIVYRTDIKTIRDLRYSDRQWLINLNNKIRSIVPGCYNYAVHPDELRILVHYQPSYYHFHIHIVNIKHPGLGNSIAAGKAILLEDIIEMLNYLGPEGYMNKTITYAIGENHDLWKRGLEEELTKQLERDGIPKIPKIVNGFK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSQLPTDFA
------CCCCCCCHH		40.1922814378
2Phosphorylation------MSQLPTDFA
------CCCCCCCHH		40.1928152593
39AcetylationLLGTIDNKDAIITAE
HHEECCCCCCEEEEE		44.8024489116
55PhosphorylationTHFLFDETVRRPSQD
CEEECCCCCCCCCCC		22.5822369663
60PhosphorylationDETVRRPSQDGRSTP
CCCCCCCCCCCCCCC		38.8122369663
65PhosphorylationRPSQDGRSTPVLYNC
CCCCCCCCCCEEEEC		42.4622369663
66PhosphorylationPSQDGRSTPVLYNCE
CCCCCCCCCEEEECC		18.9622369663
70PhosphorylationGRSTPVLYNCENEYS
CCCCCEEEECCCHHH		20.2829136822
76PhosphorylationLYNCENEYSCINGIQ
EEECCCHHHCCCHHH		22.0321440633
77PhosphorylationYNCENEYSCINGIQE
EECCCHHHCCCHHHH		11.4421440633
112UbiquitinationMESNPTAKLNLIWPA
HHCCCCCEEEEEECC		40.1523749301
120PhosphorylationLNLIWPATPIHIKKY
EEEEECCCCEEEEEH		20.7822369663
125AcetylationPATPIHIKKYEQQNF
CCCCEEEEEHHHHCC		34.8324489116
125UbiquitinationPATPIHIKKYEQQNF
CCCCEEEEEHHHHCC		34.8322817900
126AcetylationATPIHIKKYEQQNFH
CCCEEEEEHHHHCCC		54.1124489116
126UbiquitinationATPIHIKKYEQQNFH
CCCEEEEEHHHHCCC		54.1123749301
160AcetylationMCNNGRLKWVNNILY
HCCCCCEEEEHHHHH		47.9724489116
217AcetylationIVYRTDIKTIRDLRY
EEEECCCCHHHHCCC		40.4825381059
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
66TPhosphorylationKinaseYAK1P14680
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCPS_YEAST !!
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 DCPS_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACEA_YEASTICL1physical
16554755
DCS2_YEASTDCS2physical
16554755
PUR92_YEASTADE17physical
18467557
IF4F1_YEASTTIF4631genetic
19061648
NOP12_YEASTNOP12genetic
19061648
RIT1_YEASTRIT1genetic
19061648
RXT2_YEASTRXT2genetic
19061648
HOS2_YEASTHOS2genetic
19061648
DCS2_YEASTDCS2physical
20826334
DCPS_YEASTDCS1physical
26258763
NUP57_YEASTNUP57genetic
27708008
TF2B_YEASTSUA7genetic
27708008
PEX19_YEASTPEX19genetic
27708008
ASK10_YEASTASK10genetic
27708008
VMA21_YEASTVMA21genetic
27708008
CSN12_YEASTYJR084Wgenetic
27708008
RFC5_YEASTRFC5genetic
27708008
SCC1_YEASTMCD1genetic
27708008
PRP9_YEASTPRP9genetic
27708008
CDC53_YEASTCDC53genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
GPI8_YEASTGPI8genetic
27708008
UTP5_YEASTUTP5genetic
27708008
RMRP_YEASTSNM1genetic
27708008
STT3_YEASTSTT3genetic
27708008
COPB2_YEASTSEC27genetic
27708008
ZPR1_YEASTZPR1genetic
27708008
SYMC_YEASTMES1genetic
27708008
MPPA_YEASTMAS2genetic
27708008
RPN1_YEASTRPN1genetic
27708008
UTP9_YEASTUTP9genetic
27708008
SSL1_YEASTSSL1genetic
27708008
TAF11_YEASTTAF11genetic
27708008
ERB1_YEASTERB1genetic
27708008
NOP2_YEASTNOP2genetic
27708008
DPOA_YEASTPOL1genetic
27708008
GPN2_YEASTGPN2genetic
27708008
CET1_YEASTCET1genetic
27708008
SEC8_YEASTSEC8genetic
27708008
RDS3_YEASTRDS3genetic
27708008
STE50_YEASTSTE50genetic
27708008
RL27B_YEASTRPL27Bgenetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
PCL6_YEASTPCL6genetic
27708008
SCS2_YEASTSCS2genetic
27708008
UBP3_YEASTUBP3genetic
27708008
MED5_YEASTNUT1genetic
27708008
STF2_YEASTSTF2genetic
27708008
RS23A_YEASTRPS23Agenetic
27708008
RS23B_YEASTRPS23Agenetic
27708008
CHO2_YEASTCHO2genetic
27708008
LSM1_YEASTLSM1genetic
27708008
VPS51_YEASTVPS51genetic
27708008
GBLP_YEASTASC1genetic
27708008
PSO2_YEASTPSO2genetic
27708008
TMA23_YEASTTMA23genetic
27708008
BRE5_YEASTBRE5genetic
27708008
MSB4_YEASTMSB4genetic
27708008
ULS1_YEASTULS1genetic
27708008
PUS7_YEASTPUS7genetic
27708008
VPH1_YEASTVPH1genetic
27708008
JID1_YEASTJID1genetic
27708008
HNT2_YEASTHNT2genetic
25432955
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCPS_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60; SER-65 AND THR-66,AND MASS SPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-120, AND MASSSPECTROMETRY.
"The 'scavenger' m7GpppX pyrophosphatase activity of Dcs1 modulatesnutrient-induced responses in yeast.";
Malys N., Carroll K., Miyan J., Tollervey D., McCarthy J.E.G.;
Nucleic Acids Res. 32:3590-3600(2004).
Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, INDUCTION, ANDPHOSPHORYLATION AT THR-66.

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