DDX6_HUMAN - dbPTM
DDX6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DDX6_HUMAN
UniProt AC P26196
Protein Name Probable ATP-dependent RNA helicase DDX6 {ECO:0000305}
Gene Name DDX6
Organism Homo sapiens (Human).
Sequence Length 483
Subcellular Localization Cytoplasm, P-body . Cytoplasm . Nucleus . Upon cellular stress, relocalizes to stress granules (PubMed:26184334).
Protein Description In the process of mRNA degradation, plays a role in mRNA decapping. [PubMed: 16364915 Blocks autophagy in nutrient-rich conditions by repressing the expression of ATG-related genes through degration of their transcripts]
Protein Sequence MSTARTENPVIMGLSSQNGQLRGPVKPTGGPGGGGTQTQQQMNQLKNTNTINNGTQQQAQSMTTTIKPGDDWKKTLKLPPKDLRIKTSDVTSTKGNEFEDYCLKRELLMGIFEMGWEKPSPIQEESIPIALSGRDILARAKNGTGKSGAYLIPLLERLDLKKDNIQAMVIVPTRELALQVSQICIQVSKHMGGAKVMATTGGTNLRDDIMRLDDTVHVVIATPGRILDLIKKGVAKVDHVQMIVLDEADKLLSQDFVQIMEDIILTLPKNRQILLYSATFPLSVQKFMNSHLQKPYEINLMEELTLKGVTQYYAYVTERQKVHCLNTLFSRLQINQSIIFCNSSQRVELLAKKISQLGYSCFYIHAKMRQEHRNRVFHDFRNGLCRNLVCTDLFTRGIDIQAVNVVINFDFPKLAETYLHRIGRSGRFGHLGLAINLITYDDRFNLKSIEEQLGTEIKPIPSNIDKSLYVAEYHSEPVEDEKP
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
12SulfoxidationRTENPVIMGLSSQNG
CCCCCEEEEEECCCC		4.5021406390
15PhosphorylationNPVIMGLSSQNGQLR
CCEEEEEECCCCCCC		24.9326074081
16PhosphorylationPVIMGLSSQNGQLRG
CEEEEEECCCCCCCC		32.4826074081
26UbiquitinationGQLRGPVKPTGGPGG
CCCCCCCCCCCCCCC		39.7421906983
26AcetylationGQLRGPVKPTGGPGG
CCCCCCCCCCCCCCC		39.7426051181
36PhosphorylationGGPGGGGTQTQQQMN
CCCCCCHHHHHHHHH		31.5517525332
38PhosphorylationPGGGGTQTQQQMNQL
CCCCHHHHHHHHHHH		28.3423312004
42SulfoxidationGTQTQQQMNQLKNTN
HHHHHHHHHHHCCCC		2.7621406390
61PhosphorylationGTQQQAQSMTTTIKP
CHHHHHHHCCCEECC		22.5528555341
64PhosphorylationQQAQSMTTTIKPGDD
HHHHHCCCEECCCCC		20.20-
67UbiquitinationQSMTTTIKPGDDWKK
HHCCCEECCCCCHHH		40.6421906983
67AcetylationQSMTTTIKPGDDWKK
HHCCCEECCCCCHHH		40.6426051181
73UbiquitinationIKPGDDWKKTLKLPP
ECCCCCHHHHCCCCC		42.76-
73AcetylationIKPGDDWKKTLKLPP
ECCCCCHHHHCCCCC		42.7626051181
74AcetylationKPGDDWKKTLKLPPK
CCCCCHHHHCCCCCC		55.63156027
74UbiquitinationKPGDDWKKTLKLPPK
CCCCCHHHHCCCCCC		55.63-
75PhosphorylationPGDDWKKTLKLPPKD
CCCCHHHHCCCCCCC		25.9527251275
81UbiquitinationKTLKLPPKDLRIKTS
HHCCCCCCCCEEEEC		68.41-
86UbiquitinationPPKDLRIKTSDVTST
CCCCCEEEECCCCCC		35.23-
87PhosphorylationPKDLRIKTSDVTSTK
CCCCEEEECCCCCCC		27.9923312004
88PhosphorylationKDLRIKTSDVTSTKG
CCCEEEECCCCCCCC		25.6929214152
91PhosphorylationRIKTSDVTSTKGNEF
EEEECCCCCCCCCHH		35.3526657352
92PhosphorylationIKTSDVTSTKGNEFE
EEECCCCCCCCCHHH		28.1523312004
93PhosphorylationKTSDVTSTKGNEFED
EECCCCCCCCCHHHH		33.3427794612
94UbiquitinationTSDVTSTKGNEFEDY
ECCCCCCCCCHHHHH		60.55-
101PhosphorylationKGNEFEDYCLKRELL
CCCHHHHHHHHHHHH		7.7728152594
102GlutathionylationGNEFEDYCLKRELLM
CCHHHHHHHHHHHHH		5.8222555962
104UbiquitinationEFEDYCLKRELLMGI
HHHHHHHHHHHHHHH		40.02-
1042-HydroxyisobutyrylationEFEDYCLKRELLMGI
HHHHHHHHHHHHHHH		40.02-
104AcetylationEFEDYCLKRELLMGI
HHHHHHHHHHHHHHH		40.0223749302
120PhosphorylationEMGWEKPSPIQEESI
HCCCCCCCCCCCCCC		45.7823312004
126PhosphorylationPSPIQEESIPIALSG
CCCCCCCCCCEEECC		32.6723312004
132PhosphorylationESIPIALSGRDILAR
CCCCEEECCHHHHHH		23.8223312004
144PhosphorylationLARAKNGTGKSGAYL
HHHCCCCCCCCCCCH		51.3223312004
146UbiquitinationRAKNGTGKSGAYLIP
HCCCCCCCCCCCHHH		45.6221906983
147PhosphorylationAKNGTGKSGAYLIPL
CCCCCCCCCCCHHHH		29.9621712546
162UbiquitinationLERLDLKKDNIQAMV
HHHCCCCCCCEEEEE		64.40-
181O-linked_GlycosylationRELALQVSQICIQVS
HHHHHHHHHHHHHHH		10.8128510447
1952-HydroxyisobutyrylationSKHMGGAKVMATTGG
HHHCCCCEEEEECCC		35.50-
195UbiquitinationSKHMGGAKVMATTGG
HHHCCCCEEEEECCC		35.5021906983
197SulfoxidationHMGGAKVMATTGGTN
HCCCCEEEEECCCCC		2.4321406390
199PhosphorylationGGAKVMATTGGTNLR
CCCEEEEECCCCCHH		14.1021406692
200PhosphorylationGAKVMATTGGTNLRD
CCEEEEECCCCCHHH		24.8721406692
203PhosphorylationVMATTGGTNLRDDIM
EEEECCCCCHHHHHH		32.2121406692
231UbiquitinationGRILDLIKKGVAKVD
HHHHHHHHHCCCCCC		51.2621906983
2312-HydroxyisobutyrylationGRILDLIKKGVAKVD
HHHHHHHHHCCCCCC		51.26-
231AcetylationGRILDLIKKGVAKVD
HHHHHHHHHCCCCCC		51.2625953088
232UbiquitinationRILDLIKKGVAKVDH
HHHHHHHHCCCCCCE		52.18-
296PhosphorylationNSHLQKPYEINLMEE
HHHCCCCEEECCCCH		36.1523663014
305PhosphorylationINLMEELTLKGVTQY
ECCCCHHCCCCCCEE		29.6923663014
310PhosphorylationELTLKGVTQYYAYVT
HHCCCCCCEEEEEHH		21.3723663014
312PhosphorylationTLKGVTQYYAYVTER
CCCCCCEEEEEHHHH		4.8223663014
313PhosphorylationLKGVTQYYAYVTERQ
CCCCCEEEEEHHHHH		5.0123663014
315PhosphorylationGVTQYYAYVTERQKV
CCCEEEEEHHHHHHH		7.5623663014
317PhosphorylationTQYYAYVTERQKVHC
CEEEEEHHHHHHHHH		16.8723663014
324S-nitrosocysteineTERQKVHCLNTLFSR
HHHHHHHHHHHHHHH		3.34-
324S-nitrosylationTERQKVHCLNTLFSR
HHHHHHHHHHHHHHH		3.3419483679
327PhosphorylationQKVHCLNTLFSRLQI
HHHHHHHHHHHHHCC		19.07-
330PhosphorylationHCLNTLFSRLQINQS
HHHHHHHHHHCCCCE		34.88-
3522-HydroxyisobutyrylationQRVELLAKKISQLGY
HHHHHHHHHHHHHCH		51.08-
352AcetylationQRVELLAKKISQLGY
HHHHHHHHHHHHHCH		51.0826051181
352UbiquitinationQRVELLAKKISQLGY
HHHHHHHHHHHHHCH		51.08-
353UbiquitinationRVELLAKKISQLGYS
HHHHHHHHHHHHCHH		41.82-
375MethylationMRQEHRNRVFHDFRN
HHHHHHHHHHHHHHC		32.22-
417PhosphorylationDFPKLAETYLHRIGR
CCHHHHHHHHHHHCC		26.2728152594
418PhosphorylationFPKLAETYLHRIGRS
CHHHHHHHHHHHCCC		7.6328152594
425PhosphorylationYLHRIGRSGRFGHLG
HHHHHCCCCCCCCHH		29.1624719451
439PhosphorylationGLAINLITYDDRFNL
HEEEEEEECCCCCCH		24.8626356563
440PhosphorylationLAINLITYDDRFNLK
EEEEEEECCCCCCHH		14.6227273156
447UbiquitinationYDDRFNLKSIEEQLG
CCCCCCHHHHHHHHC		50.9521906983
455PhosphorylationSIEEQLGTEIKPIPS
HHHHHHCCCEECCCC		43.0329523821
458AcetylationEQLGTEIKPIPSNID
HHHCCCEECCCCCCC		30.5726051181
458UbiquitinationEQLGTEIKPIPSNID
HHHCCCEECCCCCCC		30.572190698
462PhosphorylationTEIKPIPSNIDKSLY
CCEECCCCCCCCHHE		47.3330266825
466UbiquitinationPIPSNIDKSLYVAEY
CCCCCCCCHHEEEEE		38.27-
467PhosphorylationIPSNIDKSLYVAEYH
CCCCCCCHHEEEEEC		22.6127642862
469PhosphorylationSNIDKSLYVAEYHSE
CCCCCHHEEEEECCC		12.5227642862
472PhosphorylationDKSLYVAEYHSEPVE
CCHHEEEEECCCCCC		33.4617016520
473PhosphorylationKSLYVAEYHSEPVED
CHHEEEEECCCCCCC		10.8320007894
475PhosphorylationLYVAEYHSEPVEDEK
HEEEEECCCCCCCCC		42.5729214152
482UbiquitinationSEPVEDEKP------
CCCCCCCCC------		69.2421906983
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 DDX6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DDX6_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 DDX6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GAG_HV1H2gagphysical
19560422
AFF1_HUMANAFF1physical
21030982
RC3H1_HUMANRC3H1physical
22939629
WDR12_HUMANWDR12physical
22939629
DCP1A_HUMANDCP1Aphysical
16364915
EDC3_HUMANEDC3physical
16364915
ATX2_HUMANATXN2physical
24778252
ATX2L_HUMANATXN2Lphysical
24778252
MCRI2_HUMANFAM195Aphysical
24778252
G3BP2_HUMANG3BP2physical
24778252
MCRI1_HUMANFAM195Bphysical
24778252
LSM12_HUMANLSM12physical
24778252
LS14B_HUMANLSM14Bphysical
24778252
NUFP2_HUMANNUFIP2physical
24778252
PATL1_HUMANPATL1physical
24778252
GOGA2_HUMANGOLGA2physical
25416956
TRI37_HUMANTRIM37physical
25416956
NONO_HUMANNONOphysical
25416956
TRI27_HUMANTRIM27physical
25416956
VPS52_HUMANVPS52physical
25416956
ITF2_HUMANTCF4physical
25416956
ZNF24_HUMANZNF24physical
25416956
CACO2_HUMANCALCOCO2physical
25416956
IKZF1_HUMANIKZF1physical
25416956
SDCG3_HUMANSDCCAG3physical
25416956
RUN3A_HUMANRUNDC3Aphysical
25416956
4ET_HUMANEIF4ENIF1physical
25416956
BIRC7_HUMANBIRC7physical
25416956
EDC3_HUMANEDC3physical
25416956
CEP70_HUMANCEP70physical
25416956
PNMA5_HUMANPNMA5physical
25416956
K1C40_HUMANKRT40physical
25416956
BEND7_HUMANBEND7physical
25416956
KR108_HUMANKRTAP10-8physical
25416956
KR103_HUMANKRTAP10-3physical
25416956
ZBT8A_HUMANZBTB8Aphysical
25416956
EDC3_HUMANEDC3physical
26186194
DCP1B_HUMANDCP1Bphysical
26186194
EDC4_HUMANEDC4physical
26186194
LS14B_HUMANLSM14Bphysical
26186194
DCP1A_HUMANDCP1Aphysical
26186194
ATX2L_HUMANATXN2Lphysical
26186194
PNRC1_HUMANPNRC1physical
26186194
PAK4_HUMANPAK4physical
26186194
ATX2_HUMANATXN2physical
26186194
ARBK1_HUMANADRBK1physical
26344197
RHG17_HUMANARHGAP17physical
26344197
CNOT7_HUMANCNOT7physical
26344197
LPPRC_HUMANLRPPRCphysical
26344197
PPWD1_HUMANPPWD1physical
26344197
TIM13_HUMANTIMM13physical
26344197
TIM8B_HUMANTIMM8Bphysical
26344197
EDC3_HUMANEDC3physical
28514442
DCP1B_HUMANDCP1Bphysical
28514442
EDC4_HUMANEDC4physical
28514442
DCP1A_HUMANDCP1Aphysical
28514442
ATX2_HUMANATXN2physical
28514442
NUFP2_HUMANNUFIP2physical
28514442
PNRC1_HUMANPNRC1physical
28514442
PAK4_HUMANPAK4physical
28514442
LS14B_HUMANLSM14Bphysical
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 DDX6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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 THR-36, AND MASSSPECTROMETRY.
"An extensive survey of tyrosine phosphorylation revealing new sitesin human mammary epithelial cells.";
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A.,Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D.,Wiley H.S., Qian W.-J.;
J. Proteome Res. 8:3852-3861(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-473, AND MASSSPECTROMETRY.

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