DCP1A_MOUSE - dbPTM
DCP1A_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DCP1A_MOUSE
UniProt AC Q91YD3
Protein Name mRNA-decapping enzyme 1A
Gene Name Dcp1a
Organism Mus musculus (Mouse).
Sequence Length 602
Subcellular Localization Cytoplasm, P-body . Nucleus . Predominantly cytoplasmic, in processing bodies (PB). Nuclear, after TGFB1 treatment. Translocation to the nucleus depends on interaction with SMAD4 (By similarity). Colocalizes with NANOS3 in the processing bodies (PubM
Protein Description Necessary for the degradation of mRNAs, both in normal mRNA turnover and in nonsense-mediated mRNA decay. Removes the 7-methyl guanine cap structure from mRNA molecules, yielding a 5'-phosphorylated mRNA fragment and 7m-GDP. Contributes to the transactivation of target genes after stimulation by TGFB1 (By similarity)..
Protein Sequence MALSCSTVRPRRRGSALRSKMELLSRAEQEMSLAALKQHDPYITSIADLTGQVALYTFCPKANQWEKTDIEGTLFVYRRSASPYHGFTIVNRLNMHNLVEPVNKDLEFQLHEPFLLYRNASLSIYSIWFYDKNDCHRIAKLMADVVEEETRRSQQAARDKQSPSQANGCSDQRPIDILEMLSRAKDEYERNQMGGSNISSPGLQPSTQLSNLGSTETLEETPSGSQDKSAPSGHKHLTVEELFGTSLPKEQPTAMGLESEDTDKLLGDASQKEPSSFLPFPFEQSGGAPQSENLGIHSAAHHTVQPEVSTPVLITPASIAQSGDKHPPSYTLPLSPVLSPTLPAEAPTTQVPHLPRNSTMIQAVKTTPRQKSPLLNQPVPELSHSSLVASQSPFRAPVSLANPAGTALPSVDLLQKLRLTPQHDQIQAQPLGKGTMAPSFSSAAGQLATPESFIEPSSKTAAARAAVSASLSNMVLAPTLQSMQQNQDPEVFSQPKVLPSAIPIAGSPLVPATTTAVSSVLLSPSVFQQTVPRAADLERKASSPSPLTVGTAESQRKPSIILSKSQLQDTLIHLIKNDSSFLSTLHAVYLQVLTKNKDNHNL
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
4Phosphorylation----MALSCSTVRPR
----CCCCCCCCCCC
9.1129895711
7Phosphorylation-MALSCSTVRPRRRG
-CCCCCCCCCCCCCC
25.51-
15PhosphorylationVRPRRRGSALRSKME
CCCCCCCHHHHHHHH
23.48-
19PhosphorylationRRGSALRSKMELLSR
CCCHHHHHHHHHHHH
36.8926026062
25PhosphorylationRSKMELLSRAEQEMS
HHHHHHHHHHHHHHH
41.9126026062
32PhosphorylationSRAEQEMSLAALKQH
HHHHHHHHHHHHHHC
17.6929899451
44PhosphorylationKQHDPYITSIADLTG
HHCCCCHHHHHHHCC
14.29-
45PhosphorylationQHDPYITSIADLTGQ
HCCCCHHHHHHHCCC
13.25-
56PhosphorylationLTGQVALYTFCPKAN
HCCCEEEEEECCCCC
6.50-
80PhosphorylationTLFVYRRSASPYHGF
EEEEEEECCCCCCCE
24.8928833060
82PhosphorylationFVYRRSASPYHGFTI
EEEEECCCCCCCEEE
27.5123684622
84PhosphorylationYRRSASPYHGFTIVN
EEECCCCCCCEEEEE
16.4528833060
88PhosphorylationASPYHGFTIVNRLNM
CCCCCCEEEEECCCC
28.7128833060
153PhosphorylationVEEETRRSQQAARDK
HHHHHHHHHHHHHHC
24.29-
162PhosphorylationQAARDKQSPSQANGC
HHHHHCCCHHHCCCC
32.0521082442
164PhosphorylationARDKQSPSQANGCSD
HHHCCCHHHCCCCCC
47.3621082442
170PhosphorylationPSQANGCSDQRPIDI
HHHCCCCCCCCCHHH
37.8725159016
182PhosphorylationIDILEMLSRAKDEYE
HHHHHHHHHCHHHHH
28.9625367039
196PhosphorylationERNQMGGSNISSPGL
HHHCCCCCCCCCCCC
25.8421743459
199PhosphorylationQMGGSNISSPGLQPS
CCCCCCCCCCCCCCC
34.4325521595
200PhosphorylationMGGSNISSPGLQPST
CCCCCCCCCCCCCCC
21.1322942356
206PhosphorylationSSPGLQPSTQLSNLG
CCCCCCCCCCHHCCC
18.8021743459
207PhosphorylationSPGLQPSTQLSNLGS
CCCCCCCCCHHCCCC
39.9721743459
210PhosphorylationLQPSTQLSNLGSTET
CCCCCCHHCCCCCCC
21.8621743459
214PhosphorylationTQLSNLGSTETLEET
CCHHCCCCCCCCCCC
26.6621743459
215PhosphorylationQLSNLGSTETLEETP
CHHCCCCCCCCCCCC
31.0621743459
217PhosphorylationSNLGSTETLEETPSG
HCCCCCCCCCCCCCC
39.2921743459
221PhosphorylationSTETLEETPSGSQDK
CCCCCCCCCCCCCCC
17.2425293948
225PhosphorylationLEETPSGSQDKSAPS
CCCCCCCCCCCCCCC
39.2725293948
245PhosphorylationTVEELFGTSLPKEQP
EHHHHHCCCCCCCCC
21.5426745281
246PhosphorylationVEELFGTSLPKEQPT
HHHHHCCCCCCCCCC
42.9526745281
253PhosphorylationSLPKEQPTAMGLESE
CCCCCCCCCCCCCCC
29.0430635358
259PhosphorylationPTAMGLESEDTDKLL
CCCCCCCCCCHHHHC
45.9030635358
262PhosphorylationMGLESEDTDKLLGDA
CCCCCCCHHHHCCCC
30.8624719451
329PhosphorylationSGDKHPPSYTLPLSP
CCCCCCCCCCCCCCC
34.8925159016
330PhosphorylationGDKHPPSYTLPLSPV
CCCCCCCCCCCCCCC
20.3325159016
331PhosphorylationDKHPPSYTLPLSPVL
CCCCCCCCCCCCCCC
26.6625159016
335PhosphorylationPSYTLPLSPVLSPTL
CCCCCCCCCCCCCCC
15.8327087446
339PhosphorylationLPLSPVLSPTLPAEA
CCCCCCCCCCCCCCC
18.9727087446
341PhosphorylationLSPVLSPTLPAEAPT
CCCCCCCCCCCCCCC
41.8325159016
348PhosphorylationTLPAEAPTTQVPHLP
CCCCCCCCCCCCCCC
36.5925159016
349PhosphorylationLPAEAPTTQVPHLPR
CCCCCCCCCCCCCCC
26.8925159016
367PhosphorylationMIQAVKTTPRQKSPL
CHHEECCCCCCCCCC
15.6829514104
372PhosphorylationKTTPRQKSPLLNQPV
CCCCCCCCCCCCCCC
16.6726824392
383PhosphorylationNQPVPELSHSSLVAS
CCCCCCCCHHHHHCC
21.4725159016
385PhosphorylationPVPELSHSSLVASQS
CCCCCCHHHHHCCCC
23.2225159016
386PhosphorylationVPELSHSSLVASQSP
CCCCCHHHHHCCCCC
22.8025159016
390PhosphorylationSHSSLVASQSPFRAP
CHHHHHCCCCCCCCC
24.5825159016
392PhosphorylationSSLVASQSPFRAPVS
HHHHCCCCCCCCCCC
24.4225159016
395MethylationVASQSPFRAPVSLAN
HCCCCCCCCCCCCCC
41.17-
395Asymmetric dimethylarginineVASQSPFRAPVSLAN
HCCCCCCCCCCCCCC
41.17-
399O-linked_GlycosylationSPFRAPVSLANPAGT
CCCCCCCCCCCCCCC
22.2430059200
420PhosphorylationLLQKLRLTPQHDQIQ
HHHHHCCCCCCCCCC
17.9226824392
439PhosphorylationGKGTMAPSFSSAAGQ
CCCCCCCCHHHCCCC
28.3728059163
441PhosphorylationGTMAPSFSSAAGQLA
CCCCCCHHHCCCCCC
24.33-
500PhosphorylationSQPKVLPSAIPIAGS
CCCCCCCCCCCCCCC
34.3725293948
507PhosphorylationSAIPIAGSPLVPATT
CCCCCCCCCCCCCCH
13.1625293948
513PhosphorylationGSPLVPATTTAVSSV
CCCCCCCCHHHHHHH
20.7125293948
514PhosphorylationSPLVPATTTAVSSVL
CCCCCCCHHHHHHHH
18.1825293948
515PhosphorylationPLVPATTTAVSSVLL
CCCCCCHHHHHHHHC
22.2525293948
518PhosphorylationPATTTAVSSVLLSPS
CCCHHHHHHHHCCHH
16.5625293948
519PhosphorylationATTTAVSSVLLSPSV
CCHHHHHHHHCCHHH
15.3625293948
523PhosphorylationAVSSVLLSPSVFQQT
HHHHHHCCHHHHCCC
15.8025293948
530PhosphorylationSPSVFQQTVPRAADL
CHHHHCCCCCCHHHH
22.9925777480
542PhosphorylationADLERKASSPSPLTV
HHHHHHCCCCCCCCC
45.9025521595
543PhosphorylationDLERKASSPSPLTVG
HHHHHCCCCCCCCCC
33.9727087446
545PhosphorylationERKASSPSPLTVGTA
HHHCCCCCCCCCCCC
34.1927087446
548PhosphorylationASSPSPLTVGTAESQ
CCCCCCCCCCCCCCC
21.9225521595
551PhosphorylationPSPLTVGTAESQRKP
CCCCCCCCCCCCCCC
23.9425619855
554PhosphorylationLTVGTAESQRKPSII
CCCCCCCCCCCCEEE
32.5925619855
559PhosphorylationAESQRKPSIILSKSQ
CCCCCCCEEEEEHHH
25.8728833060

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
335SPhosphorylationKinaseMAPK1P28482
GPS
335SPhosphorylationKinaseERK2P63085
PSP
339SPhosphorylationKinaseMAPK1P28482
GPS
339SPhosphorylationKinaseERK2P63085
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DCP1A_MOUSE !!

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 DCP1A_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DCP1A_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DCP1A_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-543 AND SER-545, ANDMASS SPECTROMETRY.

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