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Protein Page:
EDC3 (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
EDC3 Binds single-stranded RNA. In the process of mRNA degradation, may play a role in mRNA decapping. May play a role in spermiogenesis and oogenesis. Belongs to the EDC3 family. Note: This description may include information from UniProtKB.
Protein type: RNA processing
Cellular Component: cytosol
Molecular Function: identical protein binding; protein binding; RNA binding
Biological Process: RNA metabolic process; gene expression; mRNA metabolic process; mRNA catabolic process, deadenylation-dependent decay
Reference #:  Q96F86 (UniProtKB)
Alt. Names/Synonyms: EDC3; enhancer of mRNA decapping 3 homolog (S. cerevisiae); Enhancer of mRNA-decapping protein 3; FLJ21128; FLJ31777; hYjeF_N2; hYjeF_N2-15q23; LSM16; LSM16 homolog; LSM16 homolog (EDC3, S. cerevisiae); YJDC; yjeF domain containing; YjeF domain-containing protein 1; YjeF N-terminal domain-containing protein 2; YjeF_N2; YJEFN2
Gene Symbols: EDC3
Molecular weight: 56,078 Da
Basal Isoelectric point: 6.65  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

EDC3

Protein Structure Not Found.


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Sites Implicated In
molecular association, regulation: S161‑p

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 6 T100-p VGINQNGtGKFVKKP
1 2 S109-p KFVKKPAsSSSAPQN
0 5 S125-p PKRTDVKsQDVAVsP
1 47 S131-p KsQDVAVsPQQQQCs
0 3 S138-p sPQQQQCsKsYVDRH
0 4 S140-p QQQQCsKsYVDRHME
0 4 S148-p YVDRHMEsLsQSKsF
0 5 S150-p DRHMEsLsQSKsFRR
0 7 S154-p EsLsQSKsFRRRHNs
1 319 S161-p sFRRRHNsWssssRH
0 30 S163-p RRRHNsWssssRHPN
0 5 S164-p RRHNsWssssRHPNQ
0 8 S165-p RHNsWssssRHPNQA
0 5 S166-p HNsWssssRHPNQAt
1 67 T173-p sRHPNQAtPKKSGLK
0 4 T224-p AVFEEIDtyERRSGT
1 59 Y225-p VFEEIDtyERRSGTR
0 1 S229 IDtyERRSGTRSRGI
0 62 Y258-p LESEPIVyRRIIVPH
0 1 T300-p VAEKHGLtLERRLEM
0 1 S386-p TNELSLFsKTQGQQV
0 1 K426-ub LRDQPWYkAAVAWAN
  mouse

 
T100 MSISQNGTGKVVKKP
S109 KVVKKPASSSSAPQS
S125-p PKRTDVKsQDVAIsP
S131-p KsQDVAIsPQQQQCs
S138-p sPQQQQCsKsYVDRH
S140-p QQQQCsKsYVDRHME
S148 YVDRHMESLSQSKSF
S150 DRHMESLSQSKSFRR
S154 ESLSQSKSFRRRHNs
S161-p SFRRRHNsWsSssRH
S163-p RRRHNsWsSssRHPN
S164 RRHNsWsSssRHPNQ
S165-p RHNsWsSssRHPNQA
S166-p HNsWsSssRHPNQAt
T173-p sRHPNQAtPKKSGLK
T224 AVFEEIDTYERRsGS
Y225 VFEEIDTYERRsGSR
S229-p IDTYERRsGSRSRGV
Y258-p LESEPIVyRRITVPH
T300 VAEKHGLTLERRLEM
S386 TNELSLFSKTQGQQV
K426 LRDQPWYKAAVAWAN
  rat

 
T99 MSINQNGTGKVVKKP
S108 KVVKKPASSSSAPQS
S124 PKRTDMKSQDVAIsP
S130-p KSQDVAIsPQQQQCS
S137 sPQQQQCSKSYVDRH
S139 QQQQCSKSYVDRHME
S147 YVDRHMESLSQSKSF
S149 DRHMESLSQSKSFRR
S153 ESLSQSKSFRRRHNS
S160 SFRRRHNSWSSSSRH
S162 RRRHNSWSSSSRHPN
S163 RRHNSWSSSSRHPNQ
S164 RHNSWSSSSRHPNQA
S165 HNSWSSSSRHPNQAT
T172 SRHPNQATPKKSGLK
T223 AVFEEIDTYERRSGS
Y224 VFEEIDTYERRSGSR
S228 IDTYERRSGSRSRGV
Y257 LESEPIVYRRITVPH
T299 VAEKHGLTLERRLEM
S385 TNELSLFSKTQGQQV
K425 LRDQPWYKAAVAWAN
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