DCP2_HUMAN - dbPTM
DCP2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCP2_HUMAN
UniProt AC Q8IU60
Protein Name m7GpppN-mRNA hydrolase {ECO:0000305}
Gene Name DCP2
Organism Homo sapiens (Human).
Sequence Length 420
Subcellular Localization Cytoplasm, P-body . Nucleus . Predominantly cytoplasmic, in processing bodies (PB) (PubMed:15273322). A minor amount is nuclear (PubMed:15273322).
Protein Description Decapping metalloenzyme that catalyzes the cleavage of the cap structure on mRNAs. [PubMed: 12417715]
Protein Sequence METKRVEIPGSVLDDFCSRFILHIPSEERDNAIRVCFQIELAHWFYLDFYMQNTPGLPQCGIRDFAKAVFSHCPFLLPQGEDVEKVLDEWKEYKMGVPTYGAIILDETLENVLLVQGYLAKSGWGFPKGKVNKEEAPHDCAAREVFEETGFDIKDYICKDDYIELRINDQLARLYIIPGIPKDTKFNPKTRREIRNIEWFSIEKLPCHRNDMTPKSKLGLAPNKFFMAIPFIRPLRDWLSRRFGDSSDSDNGFSSTGSTPAKPTVEKLSRTKFRHSQQLFPDGSPGDQWVKHRQPLQQKPYNNHSEMSDLLKGKNQSMRGNGRKQYQDSPNQKKRTNGLQPAKQQNSLMKCEKKLHPRKLQDNFETDAVYDLPSSSEDQLLEHAEGQPVACNGHCKFPFSSRAFLSFKFDHNAIMKILDL
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
85UbiquitinationPQGEDVEKVLDEWKE
CCCCCHHHHHHHHHH		48.2029967540
91UbiquitinationEKVLDEWKEYKMGVP
HHHHHHHHHHCCCCC		49.4729967540
93PhosphorylationVLDEWKEYKMGVPTY
HHHHHHHHCCCCCCC		11.5322817900
100PhosphorylationYKMGVPTYGAIILDE
HCCCCCCCCCHHHCH		9.8622817900
128UbiquitinationKSGWGFPKGKVNKEE
HCCCCCCCCCCCHHH		69.93-
130UbiquitinationGWGFPKGKVNKEEAP
CCCCCCCCCCHHHCC		49.08-
154UbiquitinationEETGFDIKDYICKDD
HHHCCCHHHHCCCCC		46.4529967540
159UbiquitinationDIKDYICKDDYIELR
CHHHHCCCCCEEEEE		44.0429967540
162PhosphorylationDYICKDDYIELRIND
HHCCCCCEEEEEECH		13.3625147952
204UbiquitinationIEWFSIEKLPCHRND
CCEEEEEECCCCCCC		56.9429967540
213PhosphorylationPCHRNDMTPKSKLGL
CCCCCCCCCHHHCCC		30.3524719451
215AcetylationHRNDMTPKSKLGLAP
CCCCCCCHHHCCCCC		51.5619813427
217UbiquitinationNDMTPKSKLGLAPNK
CCCCCHHHCCCCCCC		53.3429967540
246PhosphorylationLSRRFGDSSDSDNGF
HHHHHCCCCCCCCCC		36.1026503892
247PhosphorylationSRRFGDSSDSDNGFS
HHHHCCCCCCCCCCC		45.9626503892
249PhosphorylationRFGDSSDSDNGFSST
HHCCCCCCCCCCCCC		34.6226503892
254PhosphorylationSDSDNGFSSTGSTPA
CCCCCCCCCCCCCCC		28.5223927012
255PhosphorylationDSDNGFSSTGSTPAK
CCCCCCCCCCCCCCC		34.2323927012
256PhosphorylationSDNGFSSTGSTPAKP
CCCCCCCCCCCCCCC		33.6723927012
258PhosphorylationNGFSSTGSTPAKPTV
CCCCCCCCCCCCCHH		31.1623663014
259PhosphorylationGFSSTGSTPAKPTVE
CCCCCCCCCCCCHHH		28.7223663014
264PhosphorylationGSTPAKPTVEKLSRT
CCCCCCCHHHHHHCC		40.3620873877
276PhosphorylationSRTKFRHSQQLFPDG
HCCCCCCHHCCCCCC		18.5017525332
284PhosphorylationQQLFPDGSPGDQWVK
HCCCCCCCCCCHHHH		32.8425159151
291UbiquitinationSPGDQWVKHRQPLQQ
CCCCHHHHCCCCCCC		30.0629967540
299UbiquitinationHRQPLQQKPYNNHSE
CCCCCCCCCCCCCHH		36.1929967540
308PhosphorylationYNNHSEMSDLLKGKN
CCCCHHHHHHHCCCC		22.5125159151
312MethylationSEMSDLLKGKNQSMR
HHHHHHHCCCCCCCC		75.12-
312UbiquitinationSEMSDLLKGKNQSMR
HHHHHHHCCCCCCCC		75.1229967540
314MethylationMSDLLKGKNQSMRGN
HHHHHCCCCCCCCCC		50.67-
319UbiquitinationKGKNQSMRGNGRKQY
CCCCCCCCCCCCCCC		40.4424816145
319MethylationKGKNQSMRGNGRKQY
CCCCCCCCCCCCCCC		40.44-
326PhosphorylationRGNGRKQYQDSPNQK
CCCCCCCCCCCCCHH		19.81-
329PhosphorylationGRKQYQDSPNQKKRT
CCCCCCCCCCHHHHC		15.3830576142
334UbiquitinationQDSPNQKKRTNGLQP
CCCCCHHHHCCCCCH		55.4824816145
336PhosphorylationSPNQKKRTNGLQPAK
CCCHHHHCCCCCHHH		42.3828674151
347PhosphorylationQPAKQQNSLMKCEKK
CHHHHHHHHHHHHHH		26.0422817900
366PhosphorylationKLQDNFETDAVYDLP
CCCCCCCCCCEECCC		25.7228122231
370PhosphorylationNFETDAVYDLPSSSE
CCCCCCEECCCCCCH		17.3028796482
374PhosphorylationDAVYDLPSSSEDQLL
CCEECCCCCCHHHHH		54.5228122231
375PhosphorylationAVYDLPSSSEDQLLE
CEECCCCCCHHHHHH		35.4925159151
376PhosphorylationVYDLPSSSEDQLLEH
EECCCCCCHHHHHHH		49.9130576142
381UbiquitinationSSSEDQLLEHAEGQP
CCCHHHHHHHHCCCC		3.6329967540
406PhosphorylationFSSRAFLSFKFDHNA
CCCCEEEEEEECHHH		21.6723186163
416UbiquitinationFDHNAIMKILDL---
ECHHHHHHHHCC---		33.7229967540
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

Oops, there are no upstream regulatory protein records of DCP2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
249SPhosphorylation

26098573
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 DCP2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
PSB1_HUMANPSMB1physical
15231747
DCP1A_HUMANDCP1Aphysical
12417715
RENT1_HUMANUPF1physical
12417715
RO52_HUMANTRIM21physical
18361920
DCP1A_HUMANDCP1Aphysical
16364915
DCP1B_HUMANDCP1Bphysical
16364915
EDC4_HUMANEDC4physical
16364915
DPOA2_HUMANPOLA2physical
15231747
NAGK_HUMANNAGKphysical
15231747
EDC4_HUMANEDC4physical
15231747
DCP1A_HUMANDCP1Aphysical
15231747
DCP1B_HUMANDCP1Bphysical
15231747
ABCE1_HUMANABCE1physical
24778252
ANGE2_HUMANANGEL2physical
24778252
AP1M1_HUMANAP1M1physical
24778252
ARMX5_HUMANARMCX5physical
24778252
CAN2_HUMANCAPN2physical
24778252
SYDM_HUMANDARS2physical
24778252
DCP1A_HUMANDCP1Aphysical
24778252
DCP1B_HUMANDCP1Bphysical
24778252
EDC4_HUMANEDC4physical
24778252
IF5A1_HUMANEIF5Aphysical
24778252
ELP3_HUMANELP3physical
24778252
FACD2_HUMANFANCD2physical
24778252
FBX3_HUMANFBXO3physical
24778252
GARS_HUMANGARSphysical
24778252
GFPT1_HUMANGFPT1physical
24778252
GFPT2_HUMANGFPT2physical
24778252
VKGC_HUMANGGCXphysical
24778252
GGT7_HUMANGGT7physical
24778252
DHE3_HUMANGLUD1physical
24778252
GTPB2_HUMANGTPBP2physical
24778252
IDE_HUMANIDEphysical
24778252
ELP1_HUMANIKBKAPphysical
24778252
INT7_HUMANINTS7physical
24778252
PFKAM_HUMANPFKMphysical
24778252
AGM1_HUMANPGM3physical
24778252
KPBB_HUMANPHKBphysical
24778252
DPOD3_HUMANPOLD3physical
24778252
QPCTL_HUMANQPCTLphysical
24778252
SFXN2_HUMANSFXN2physical
24778252
DIC_HUMANSLC25A10physical
24778252
SQSTM_HUMANSQSTM1physical
24778252
SYTC_HUMANTARSphysical
24778252
TRM2A_HUMANTRMT2Aphysical
24778252
TRRAP_HUMANTRRAPphysical
24778252
EDC3_HUMANEDC3physical
26186194
PCBP3_HUMANPCBP3physical
26186194
DCP1B_HUMANDCP1Bphysical
26186194
DCP1A_HUMANDCP1Aphysical
26186194
SQSTM_HUMANSQSTM1physical
26186194
EDC4_HUMANEDC4physical
26186194
TBB8_HUMANTUBB8physical
26186194
EF1A2_HUMANEEF1A2physical
26186194
G3PT_HUMANGAPDHSphysical
26186194
NIPS2_HUMANGBASphysical
26186194
DCP1B_HUMANDCP1Bphysical
28514442
EDC4_HUMANEDC4physical
28514442
EDC3_HUMANEDC3physical
28514442
PCBP3_HUMANPCBP3physical
28514442
EF1A2_HUMANEEF1A2physical
28514442
DCP1A_HUMANDCP1Aphysical
28514442
G3PT_HUMANGAPDHSphysical
28514442
GGT7_HUMANGGT7physical
28514442
SQSTM_HUMANSQSTM1physical
28514442
NIPS2_HUMANGBASphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCP2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals 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).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247; SER-249AND SER-284, AND MASS SPECTROMETRY.
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-276 AND SER-284, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-246; SER-247; SER-249AND SER-347, AND MASS SPECTROMETRY.

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