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Protein Page:
DDX6 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
g O-GlcNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
DDX6 an oncogenic ATP-dependent helicase of the DEAD box family. Interacts with argonaute proteins, Ago1 and Ago2, and is a general repressor of translation in human cells by miRNA-induced gene silencing. In the process of mRNA degradation, may play a role in mRNA decapping. Note: This description may include information from UniProtKB.
Protein type: Helicase; RNA binding protein; EC 3.6.4.13; EC 3.6.1.-; RNA processing
Cellular Component: stress granule; cytosol
Molecular Function: protein binding; RNA binding; ATP-dependent helicase activity; helicase activity; ATP binding; RNA helicase activity
Biological Process: RNA metabolic process; gene expression; cytoplasmic mRNA processing body assembly; mRNA metabolic process; mRNA catabolic process, deadenylation-dependent decay
Reference #:  P26196 (UniProtKB)
Alt. Names/Synonyms: ATP-dependent RNA helicase p54; DDX6; DEAD (Asp-Glu-Ala-Asp) box polypeptide 6; DEAD box protein 6; DEAD box-6; DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 6 (RNA helicase, 54kD); FLJ36338; HLR2; Oncogene RCK; P54; Probable ATP-dependent RNA helicase DDX6; RCK
Gene Symbols: DDX6
Molecular weight: 54,417 Da
Basal Isoelectric point: 8.85  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DDX6
Protein Structure Not Found.


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Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 5 S16-p PVIMGLSsQNGQLRG
0 1 K26-u GQLRGPVkPTGGPGG
0 9 T36-p GGPGGGGtQtQQQMN
0 2 T38-p PGGGGtQtQQQMNQL
0 1 T55 TNTINNGTQQQAQSM
0 1 T65 QAQSMTTTIkPGDDW
0 18 K67-a QSMTTTIkPGDDWkk
0 1 K67-u QSMTTTIkPGDDWkk
0 17 K73-a IkPGDDWkkTLKLPP
0 10 K74-a kPGDDWkkTLKLPPK
0 1 T75 PGDDWkkTLKLPPKD
0 20 T87-p PKDLRIKtSDVTSTK
0 2 K104-a EFEDYCLkRELLMGI
0 1 K146-u RAKNGTGkSGAYLIP
0 2 K195-u SKHMGGAkVMAtTGG
0 2 T199-p GGAkVMAtTGGTNLR
0 1 K232 RILDLIKKGVAKVDH
0 1 K236 LIKKGVAKVDHVQMI
0 1 K250 IVLDEADKLLSQDFV
0 37 Y312-p TLKGVTQyyAYVTER
0 18 Y313-p LKGVTQyyAYVTERQ
0 1 Y315 GVTQyyAYVTERQKV
0 1 T327-p QKVHCLNtLFsRLQI
0 1 S330-p HCLNtLFsRLQINQS
0 4 T439-p GLAINLItyDDRFNL
0 27 Y440-p LAINLItyDDRFNLk
0 1 K447-u yDDRFNLkSIEEQLG
0 1 K458-u EQLGTEIkPIPSNID
0 1 Y469-p SNIDKSLyVAEyHsE
0 120 Y473-p KSLyVAEyHsEPVED
0 14 S475-p LyVAEyHsEPVEDEk
0 1 K482-u sEPVEDEkP______
  mouse

 
S16 PVIMGLSSQNGQLRG
K26 GQLRGPVKASAGPGG
T36 AGPGGGGTQPQPQLN
P38 PGGGGTQPQPQLNQL
T55 TSTINNGTPQQAQSM
T65 QAQSMAATIkPGDDW
K67-a QSMAATIkPGDDWkK
K67 QSMAATIKPGDDWkK
K73-a IkPGDDWkKTLKLPP
K74 kPGDDWkKTLKLPPK
T75 PGDDWkKTLKLPPKD
T87 PKDLRIKTSDVTSTK
K104 EFEDYCLKRELLMGI
K146 RAKNGTGKSGAYLIP
K195 SKHMGGAKVMATTGG
T199 GGAKVMATTGGTNLR
K232-a RILDLIKkGVAkVDH
K236-a LIKkGVAkVDHVQMI
K250-a IVLDEADkLLSQDFV
Y312-p TLKGVTQyyAyVTER
Y313-p LKGVTQyyAyVTERQ
Y315-p GVTQyyAyVTERQKV
T327 QKVHCLNTLFSRLQI
S330 HCLNTLFSRLQINQS
T439 GLAINLITYDDRFNL
Y440 LAINLITYDDRFNLK
K447 YDDRFNLKSIEEQLG
K458 EQLGTEIKPIPSNID
Y469 SNIDKSLYVAEYHSE
Y473 KSLYVAEYHSEPAED
S475 LYVAEYHSEPAEDEK
K482 SEPAEDEKP______
  rat

 
S16 PVIMGLSSQNGQLRG
K26 GQLRGPVKASAGPGG
P36 AGPGGGGPQTQTQMN
T38 PGGGGPQTQTQMNQL
T55-p TSTINNGtQQQAQSM
T65-p QAQSMAAtIKPGDDW
K67 QSMAAtIKPGDDWKK
K67 QSMAAtIKPGDDWKK
K73 IKPGDDWKKtLKLPP
K74 KPGDDWKKtLKLPPK
T75-p PGDDWKKtLKLPPKD
T87 PKDLRIKTSDVTSTK
K104 EFEDYCLKRELLMGI
K146 RAKNGTGKSGAYLIP
K195 SKHMGGAKVMATTGG
T199 GGAKVMATTGGTNLR
K232 RILDLIKKGVAKVDH
K236 LIKKGVAKVDHVQMI
K250 IVLDEADKLLSQDFV
Y312 TLKGVTQYYAYVTER
Y313 LKGVTQYYAYVTERQ
Y315 GVTQYYAYVTERQKV
T327 QKVHCLNTLFSRLQI
S330 HCLNTLFSRLQINQS
T439 GLAINLITYDDRFNL
Y440 LAINLITYDDRFNLK
K447 YDDRFNLKSIEEQLG
K458 EQLGTEIKPIPSNID
Y469 SNIDKSLYVAEYHSE
Y473 KSLYVAEYHSEPAED
S475 LYVAEYHSEPAEDEK
K482 SEPAEDEKP______
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