DCP1B_HUMAN - dbPTM
DCP1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCP1B_HUMAN
UniProt AC Q8IZD4
Protein Name mRNA-decapping enzyme 1B
Gene Name DCP1B
Organism Homo sapiens (Human).
Sequence Length 617
Subcellular Localization Cytoplasm . Nucleus.
Protein Description May play a role in the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. May remove the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP (By similarity)..
Protein Sequence MAAVAAGGLVGKGRDISLAALQRHDPYINRIVDVASQVALYTFGHRANEWEKTDVEGTLFVYTRSASPKHGFTIMNRLSMENRTEPITKDLDFQLQDPFLLYRNARLSIYGIWFYDKEECQRIAELMKNLTQYEQLKAHQGTGAGISPVILNSGEGKEVDILRMLIKAKDEYTKCKTCSEPKKITSSSAIYDNPNLIKPIPVKPSENQQQRIPQPNQTLDPEPQHLSLTALFGKQDKATCQETVEPPQTLHQQQQQQQQQQEKLPIRQGVVRSLSYEEPRRHSPPIEKQLCPAIQKLMVRSADLHPLSELPENRPCENGSTHSAGEFFTGPVQPGSPHNIGTSRGVQNASRTQNLFEKLQSTPGAANKCDPSTPAPASSAALNRSRAPTSVTPVAPGKGLAQPPQAYFNGSLPPQTVGHQAHGREQSTLPRQTLPISGSQTGSSGVISPQELLKKLQIVQQEQQLHASNRPALAAKFPVLAQSSGTGKPLESWINKTPNTEQQTPLFQVISPQRIPATAAPSLLMSPMVFAQPTSVPPKERESGLLPVGGQEPPAAATSLLLPIQSPEPSVITSSPLTKLQLQEALLYLIQNDDNFLNIIYEAYLFSMTQAAMKKTM
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------MAAVAAGGL
------CCCCCCCCC		15.6222223895
12UbiquitinationAAGGLVGKGRDISLA
CCCCCCCCCCCCHHH		43.20-
15UbiquitinationGLVGKGRDISLAALQ
CCCCCCCCCHHHHHH		43.42-
26UbiquitinationAALQRHDPYINRIVD
HHHHHCCHHHHHHHH		26.27-
35UbiquitinationINRIVDVASQVALYT
HHHHHHHHHHHHHHH		6.98-
55UbiquitinationNEWEKTDVEGTLFVY
CCCEECCCCCEEEEE		9.89-
65PhosphorylationTLFVYTRSASPKHGF
EEEEEEECCCCCCCE		25.8721949786
67PhosphorylationFVYTRSASPKHGFTI
EEEEECCCCCCCEEH		35.4128464451
69UbiquitinationYTRSASPKHGFTIMN
EEECCCCCCCEEHHH		54.59-
73PhosphorylationASPKHGFTIMNRLSM
CCCCCCEEHHHCCCC		24.7421949786
89UbiquitinationNRTEPITKDLDFQLQ
CCCCCCCCCCCCCCC		57.952190698
110PhosphorylationRNARLSIYGIWFYDK
CCCEEEEEEEEECCH		10.1325147952
117UbiquitinationYGIWFYDKEECQRIA
EEEEECCHHHHHHHH		43.99-
128UbiquitinationQRIAELMKNLTQYEQ
HHHHHHHHHHHHHHH		62.52-
132UbiquitinationELMKNLTQYEQLKAH
HHHHHHHHHHHHHHH		42.82-
133PhosphorylationLMKNLTQYEQLKAHQ
HHHHHHHHHHHHHHC		10.6220090780
137UbiquitinationLTQYEQLKAHQGTGA
HHHHHHHHHHCCCCC		43.44-
142PhosphorylationQLKAHQGTGAGISPV
HHHHHCCCCCCCCCE		19.7930266825
147PhosphorylationQGTGAGISPVILNSG
CCCCCCCCCEEECCC		16.5223927012
153PhosphorylationISPVILNSGEGKEVD
CCCEEECCCCCCCHH		34.4728464451
157UbiquitinationILNSGEGKEVDILRM
EECCCCCCCHHHHHH		50.71-
172PhosphorylationLIKAKDEYTKCKTCS
HHHCCCCCCCCCCCC		22.9521253578
173PhosphorylationIKAKDEYTKCKTCSE
HHCCCCCCCCCCCCC		28.11-
183UbiquitinationKTCSEPKKITSSSAI
CCCCCCCCCCCCCCC		63.03-
185PhosphorylationCSEPKKITSSSAIYD
CCCCCCCCCCCCCCC		31.2821945579
186PhosphorylationSEPKKITSSSAIYDN
CCCCCCCCCCCCCCC		26.2621945579
187PhosphorylationEPKKITSSSAIYDNP
CCCCCCCCCCCCCCC		18.3521945579
188PhosphorylationPKKITSSSAIYDNPN
CCCCCCCCCCCCCCC		20.6021945579
191PhosphorylationITSSSAIYDNPNLIK
CCCCCCCCCCCCCCC		14.9121945579
198UbiquitinationYDNPNLIKPIPVKPS
CCCCCCCCCCCCCCC		39.81-
205PhosphorylationKPIPVKPSENQQQRI
CCCCCCCCCCCCCCC		43.3821945579
227PhosphorylationDPEPQHLSLTALFGK
CCCCCCCCHHHHHCC		22.8826657352
229PhosphorylationEPQHLSLTALFGKQD
CCCCCCHHHHHCCCC		20.2428857561
234UbiquitinationSLTALFGKQDKATCQ
CHHHHHCCCCCCCHH		48.25-
273PhosphorylationIRQGVVRSLSYEEPR
HHHHHHHHCCCCCHH		15.2821955146
275PhosphorylationQGVVRSLSYEEPRRH
HHHHHHCCCCCHHHC		31.5719664994
276PhosphorylationGVVRSLSYEEPRRHS
HHHHHCCCCCHHHCC		29.6116964243
283PhosphorylationYEEPRRHSPPIEKQL
CCCHHHCCCCHHHHH		30.4723401153
301PhosphorylationIQKLMVRSADLHPLS
HHHHHHHCCCCCCHH		18.0927080861
308PhosphorylationSADLHPLSELPENRP
CCCCCCHHHCCCCCC		41.3527080861
320PhosphorylationNRPCENGSTHSAGEF
CCCCCCCCCCCCCCC		34.2327080861
321PhosphorylationRPCENGSTHSAGEFF
CCCCCCCCCCCCCCC		22.6527080861
323PhosphorylationCENGSTHSAGEFFTG
CCCCCCCCCCCCCCC		37.7527080861
329PhosphorylationHSAGEFFTGPVQPGS
CCCCCCCCCCCCCCC		45.9926074081
336PhosphorylationTGPVQPGSPHNIGTS
CCCCCCCCCCCCCCC		29.6627422710
342PhosphorylationGSPHNIGTSRGVQNA
CCCCCCCCCCCCCCH		16.0823401153
343PhosphorylationSPHNIGTSRGVQNAS
CCCCCCCCCCCCCHH		23.0926074081
350PhosphorylationSRGVQNASRTQNLFE
CCCCCCHHHHHHHHH		43.3326074081
352PhosphorylationGVQNASRTQNLFEKL
CCCCHHHHHHHHHHH		21.2226074081
358UbiquitinationRTQNLFEKLQSTPGA
HHHHHHHHHHCCCCH		44.48-
361PhosphorylationNLFEKLQSTPGAANK
HHHHHHHCCCCHHHC		47.1822199227
362PhosphorylationLFEKLQSTPGAANKC
HHHHHHCCCCHHHCC		16.8722199227
372PhosphorylationAANKCDPSTPAPASS
HHHCCCCCCCCCCCH		33.5027273156
373PhosphorylationANKCDPSTPAPASSA
HHCCCCCCCCCCCHH		28.9426552605
378PhosphorylationPSTPAPASSAALNRS
CCCCCCCCHHHHHCC		21.3223312004
379PhosphorylationSTPAPASSAALNRSR
CCCCCCCHHHHHCCC		21.4823312004
385PhosphorylationSSAALNRSRAPTSVT
CHHHHHCCCCCCCCC		31.5522199227
389PhosphorylationLNRSRAPTSVTPVAP
HHCCCCCCCCCCCCC		34.5429255136
390PhosphorylationNRSRAPTSVTPVAPG
HCCCCCCCCCCCCCC		23.9629255136
392PhosphorylationSRAPTSVTPVAPGKG
CCCCCCCCCCCCCCC		16.2929255136
433PhosphorylationQSTLPRQTLPISGSQ
CCCCCCCCCCCCCCC		35.4628450419
437PhosphorylationPRQTLPISGSQTGSS
CCCCCCCCCCCCCCC		30.3829255136
439PhosphorylationQTLPISGSQTGSSGV
CCCCCCCCCCCCCCC		20.1329255136
441PhosphorylationLPISGSQTGSSGVIS
CCCCCCCCCCCCCCC		40.5029255136
443PhosphorylationISGSQTGSSGVISPQ
CCCCCCCCCCCCCHH		27.5729255136
444PhosphorylationSGSQTGSSGVISPQE
CCCCCCCCCCCCHHH		38.1229255136
448PhosphorylationTGSSGVISPQELLKK
CCCCCCCCHHHHHHH		20.3729255136
455UbiquitinationSPQELLKKLQIVQQE
CHHHHHHHHHHHHHH		45.66-
488UbiquitinationAQSSGTGKPLESWIN
ECCCCCCCCHHHHHH		46.39-
497PhosphorylationLESWINKTPNTEQQT
HHHHHHCCCCCCCCC		19.7927050516
500PhosphorylationWINKTPNTEQQTPLF
HHHCCCCCCCCCCCE		36.0526074081
504PhosphorylationTPNTEQQTPLFQVIS
CCCCCCCCCCEEECC		22.9626074081
511O-linked_GlycosylationTPLFQVISPQRIPAT
CCCEEECCCCCCCCC		19.0023301498
511PhosphorylationTPLFQVISPQRIPAT
CCCEEECCCCCCCCC		19.0030266825
518O-linked_GlycosylationSPQRIPATAAPSLLM
CCCCCCCCCCCHHHC		20.2823301498
522O-linked_GlycosylationIPATAAPSLLMSPMV
CCCCCCCHHHCCCCE		29.4323301498
558PhosphorylationQEPPAAATSLLLPIQ
CCCCCCCEEEEEECC		18.3827080861
559PhosphorylationEPPAAATSLLLPIQS
CCCCCCEEEEEECCC		16.5828450419
566PhosphorylationSLLLPIQSPEPSVIT
EEEEECCCCCCCCCC		31.7626657352
570PhosphorylationPIQSPEPSVITSSPL
ECCCCCCCCCCCCCC		25.2128450419
573PhosphorylationSPEPSVITSSPLTKL
CCCCCCCCCCCCCHH		22.4629523821
574PhosphorylationPEPSVITSSPLTKLQ
CCCCCCCCCCCCHHH		20.8729523821
575PhosphorylationEPSVITSSPLTKLQL
CCCCCCCCCCCHHHH		18.4528450419
578PhosphorylationVITSSPLTKLQLQEA
CCCCCCCCHHHHHHH		32.8528450419
588PhosphorylationQLQEALLYLIQNDDN
HHHHHHHHHHHCCCC		11.5618083107
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 DCP1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCP1B_HUMAN !!
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 DCP1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX6_HUMANDDX6physical
16364915
EDC3_HUMANEDC3physical
16364915
HS71L_HUMANHSPA1Lphysical
16364915
DCP1A_HUMANDCP1Aphysical
16364915
DCP2_HUMANDCP2physical
15231747
LSM8_HUMANLSM8physical
15231747
BAG4_HUMANBAG4physical
24778252
DCP1A_HUMANDCP1Aphysical
24778252
EDC3_HUMANEDC3physical
24778252
KANK2_HUMANKANK2physical
24778252
PNRC1_HUMANPNRC1physical
24778252
DCP1A_HUMANDCP1Aphysical
25036637
DDX6_HUMANDDX6physical
25036637
EDC3_HUMANEDC3physical
25036637
EDC4_HUMANEDC4physical
25036637
E2F7_HUMANE2F7physical
25036637
PPM1A_HUMANPPM1Aphysical
25036637
EDC3_HUMANEDC3physical
21516116
CING_HUMANCGNphysical
27173435
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 DCP1B_HUMAN

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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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-275 AND SER-448, AND MASS SPECTROMETRY.
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-448 AND SER-511, ANDMASS SPECTROMETRY.
"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, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-275 AND SER-448, AND MASS SPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-275, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-110; TYR-133 ANDTYR-191, AND MASS SPECTROMETRY.

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