Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  Elongation factor 1-delta  

UniProtKB / Swiss-Prot ID :  EF1D_MOUSE

Gene Name (Synonyms) : 
Eef1d  

Species :  Mus musculus (Mouse). 

Subcellular Localization :   

Protein Function :  EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP (By similarity). 

Protein Sequence MATNFLAHEKIWFDKFKYDDAERRFYEQMNGPVTSGSRQENGASVILRDIARARENIQKSLAGSSGPGAS...
Predicted Secondary Structure CCCEEEEHHHHHHHHHHHHHHHHHHHHHCCCCCCCCCCCCCCCCHHHHHHHHHHHHHHHHHHHHHCCCCC...
Protein Variant -
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Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
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Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MATNFL
---CCCEEE
15.96UniProtKB
Link-
35PhosphoserineGPVTSGSRQ
CCCCCCCCC
34.70Phosphositeplus
Link-
37PhosphoserineVTSGSRQEN
CCCCCCCCC
30.47Phosphositeplus
Link-
60PhosphoserineNIQKSLAGS
HHHHHHHHH
13.69Phosphositeplus
Link-
64PhosphoserineSLAGSSGPG
HHHHHHCCC
26.89Phosphositeplus
Link-
65PhosphoserineLAGSSGPGA
HHHHHCCCC
48.35Phosphositeplus
Link-
85PhosphothreonineIVRITSLEV
HHHHHHHHH
19.39Phosphositeplus
Link-
85PhosphothreonineIVRITSLEV
HHHHHHHHH
19.39SysPTM
Link-
86PhosphoserineVRITSLEVE
HHHHHHHHH
21.84Phosphositeplus
Link-
86PhosphoserineVRITSLEVE
HHHHHHHHH
21.84SysPTM
Link-
118PhosphoserineSLEKSSPTP
HHHCCCCCC
31.98Phosphositeplus
Link-
119PhosphoserineLEKSSPTPR
HHCCCCCCH
43.81Phosphositeplus
Link-
129PhosphothreonineTAPQTQHVS
HCCCCCCCC
21.42PhosphoELM
Link-
129PhosphothreonineTAPQTQHVS
HCCCCCCCC
21.42Phosphositeplus
Link-
129Phosphothreonine.TAPQTQHVS
HCCCCCCCC
21.42UniProtKB
Link-
133PhosphoserineTQHVSPMRQ
CCCCCCHHH
15.74PhosphoELM
Link-
133PhosphoserineTQHVSPMRQ
CCCCCCHHH
15.74Phosphositeplus
Link-
133PhosphoserineTQHVSPMRQ
CCCCCCHHH
15.74SysPTM
Link-
133Phosphoserine.TQHVSPMRQ
CCCCCCHHH
15.74UniProtKB
Link-
147PhosphothreonineKKGATPAED
CCCCCCCCC
31.53Phosphositeplus
Link-
147Phosphothreonine.KKGATPAED
CCCCCCCCC
31.53UniProtKB
Link-
162PhosphoserineDLFGSDEEE
EECCCCCCH
34.22PhosphoELM
Link-
162PhosphoserineDLFGSDEEE
EECCCCCCH
34.22Phosphositeplus
Link-
162PhosphoserineDLFGSDEEE
EECCCCCCH
34.22SysPTM
Link-
162PhosphoserineDLFGSDEEE
EECCCCCCH
34.22SysPTM
Link-
162Phosphoserine; by CK2.DLFGSDEEE
EECCCCCCH
34.22UniProtKB
Link-
217S-nitrosocysteineQLETCVRSI
HHHHHHHHH
1.42dbSNO
Link-
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Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
There are no Protein-Protein Interactions.
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Disease Reference
Drug Reference
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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133 AND SER-162, ANDMASS SPECTROMETRY.
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.
"A differential phosphoproteomic analysis of retinoic acid-treated P19cells.";
Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.;
J. Proteome Res. 6:3174-3186(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND SER-162, ANDMASS SPECTROMETRY.
"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-129 AND SER-133, ANDMASS SPECTROMETRY.
"Specific phosphopeptide enrichment with immobilized titanium ionaffinity chromatography adsorbent for phosphoproteome analysis.";
Zhou H., Ye M., Dong J., Han G., Jiang X., Wu R., Zou H.;
J. Proteome Res. 7:3957-3967(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY.
"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 THR-147 AND SER-162, ANDMASS SPECTROMETRY.
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Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures