dbPTM

EF1D_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF1D_MOUSE
UniProt AC	P57776
Protein Name	Elongation factor 1-delta
Gene Name	Eef1d
Organism	Mus musculus (Mouse).
Sequence Length	281
Subcellular Localization	Isoform 3: Nucleus .
Protein Description	Isoform 1: EF-1-beta and EF-1-delta stimulate the exchange of GDP bound to EF-1-alpha to GTP, regenerating EF-1-alpha for another round of transfer of aminoacyl-tRNAs to the ribosome.; Isoform 3: Regulates induction of heat-shock-responsive genes through association with heat shock transcription factors and direct DNA-binding at heat shock promoter elements (HSE)..
Protein Sequence	MATNFLAHEKIWFDKFKYDDAERRFYEQMNGPVTSGSRQENGASVILRDIARARENIQKSLAGSSGPGASSGPGGDHSELIVRITSLEVENQNLRGVVQDLQQAISKLEARLSSLEKSSPTPRATAPQTQHVSPMRQVEPPTKKGATPAEDDEDKDIDLFGSDEEEEDKEAARLREERLRQYAEKKAKKPTLVAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFDKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATNFLAHE ------CCCCCCCCC	15.96	-
3	Phosphorylation	-----MATNFLAHEK -----CCCCCCCCCC	25.79	25338131
10	Ubiquitination	TNFLAHEKIWFDKFK CCCCCCCCHHHHCCC	35.06	-
10	Acetylation	TNFLAHEKIWFDKFK CCCCCCCCHHHHCCC	35.06	22826441
12 (in isoform 3)	Phosphorylation	-	13.37	-
15	Acetylation	HEKIWFDKFKYDDAE CCCHHHHCCCCCHHH	33.99	22826441
15	Ubiquitination	HEKIWFDKFKYDDAE CCCHHHHCCCCCHHH	33.99	-
17	Malonylation	KIWFDKFKYDDAERR CHHHHCCCCCHHHHH	54.21	26320211
17	Acetylation	KIWFDKFKYDDAERR CHHHHCCCCCHHHHH	54.21	-
26	Phosphorylation	DDAERRFYEQMNGPV CHHHHHHHHHHCCCC	11.93	25195567
26 (in isoform 2)	Phosphorylation	-	11.93	29514104
34 (in isoform 2)	Phosphorylation	-	30.42	25168779
34	Phosphorylation	EQMNGPVTSGSRQEN HHHCCCCCCCCCCCC	30.42	29233185
35 (in isoform 2)	Phosphorylation	-	34.70	25195567
35	Phosphorylation	QMNGPVTSGSRQENG HHCCCCCCCCCCCCC	34.70	25521595
37	Phosphorylation	NGPVTSGSRQENGAS CCCCCCCCCCCCCCC	30.47	25266776
37 (in isoform 2)	Phosphorylation	-	30.47	25266776
40 (in isoform 2)	Phosphorylation	-	57.43	27566939
41 (in isoform 2)	Phosphorylation	-	42.89	26824392
44	Phosphorylation	SRQENGASVILRDIA CCCCCCCCHHHHHHH	15.87	29176673
46 (in isoform 2)	Phosphorylation	-	2.12	26745281
47 (in isoform 2)	Phosphorylation	-	3.64	26026062
59	Malonylation	RARENIQKSLAGSSG HHHHHHHHHHCCCCC	43.57	26320211
59	Ubiquitination	RARENIQKSLAGSSG HHHHHHHHHHCCCCC	43.57	-
60	Phosphorylation	ARENIQKSLAGSSGP HHHHHHHHHCCCCCC	13.69	30352176
64	Phosphorylation	IQKSLAGSSGPGASS HHHHHCCCCCCCCCC	26.89	30352176
65	Phosphorylation	QKSLAGSSGPGASSG HHHHCCCCCCCCCCC	48.35	30352176
70	Phosphorylation	GSSGPGASSGPGGDH CCCCCCCCCCCCCCH	41.57	26643407
71	Phosphorylation	SSGPGASSGPGGDHS CCCCCCCCCCCCCHH	48.77	26643407
78	Phosphorylation	SGPGGDHSELIVRIT CCCCCCHHHEEEEEE	38.55	26643407
85	Phosphorylation	SELIVRITSLEVENQ HHEEEEEEEEEECCC	19.39	18779572
86	Phosphorylation	ELIVRITSLEVENQN HEEEEEEEEEECCCC	21.84	18779572
106	Phosphorylation	QDLQQAISKLEARLS HHHHHHHHHHHHHHH	33.92	-
107	Malonylation	DLQQAISKLEARLSS HHHHHHHHHHHHHHH	44.21	26073543
107	Ubiquitination	DLQQAISKLEARLSS HHHHHHHHHHHHHHH	44.21	-
107	Acetylation	DLQQAISKLEARLSS HHHHHHHHHHHHHHH	44.21	22733758
113	Phosphorylation	SKLEARLSSLEKSSP HHHHHHHHHHHHCCC	27.59	30635358
114	Phosphorylation	KLEARLSSLEKSSPT HHHHHHHHHHHCCCC	45.18	27149854
117	Succinylation	ARLSSLEKSSPTPRA HHHHHHHHCCCCCCC	62.62	-
117	Malonylation	ARLSSLEKSSPTPRA HHHHHHHHCCCCCCC	62.62	26320211
117	Ubiquitination	ARLSSLEKSSPTPRA HHHHHHHHCCCCCCC	62.62	-
117	Succinylation	ARLSSLEKSSPTPRA HHHHHHHHCCCCCCC	62.62	23806337
117	Acetylation	ARLSSLEKSSPTPRA HHHHHHHHCCCCCCC	62.62	23806337
118	Phosphorylation	RLSSLEKSSPTPRAT HHHHHHHCCCCCCCC	31.98	23375375
119	Phosphorylation	LSSLEKSSPTPRATA HHHHHHCCCCCCCCC	43.81	26824392
121	Phosphorylation	SLEKSSPTPRATAPQ HHHHCCCCCCCCCCC	27.62	24068923
125	Phosphorylation	SSPTPRATAPQTQHV CCCCCCCCCCCCCCC	39.90	24925903
129	Phosphorylation	PRATAPQTQHVSPMR CCCCCCCCCCCCCCC	21.42	17525332
133	Phosphorylation	APQTQHVSPMRQVEP CCCCCCCCCCCCCCC	15.74	24925903
142	Phosphorylation	MRQVEPPTKKGATPA CCCCCCCCCCCCCCC	56.98	24453211
143	Malonylation	RQVEPPTKKGATPAE CCCCCCCCCCCCCCC	55.79	26320211
147	Phosphorylation	PPTKKGATPAEDDED CCCCCCCCCCCCCCC	31.53	25521595
162	Phosphorylation	KDIDLFGSDEEEEDK CCCCCCCCCHHHHHH	34.22	24925903
182	Phosphorylation	REERLRQYAEKKAKK HHHHHHHHHHHHCCC	15.42	25367039
188	Malonylation	QYAEKKAKKPTLVAK HHHHHHCCCCCEEEE	69.07	26320211
189	Malonylation	YAEKKAKKPTLVAKS HHHHHCCCCCEEEEC	48.36	26320211
196	Phosphorylation	KPTLVAKSSILLDVK CCCEEEECEEECCCC	16.93	25293948
197	Phosphorylation	PTLVAKSSILLDVKP CCEEEECEEECCCCC	19.29	25293948
209	Phosphorylation	VKPWDDETDMAQLET CCCCCCCCCHHHHHH	37.76	25293948
217	S-nitrosylation	DMAQLETCVRSIQLD CHHHHHHHHHHHCCC	1.42	22178444
217	Glutathionylation	DMAQLETCVRSIQLD CHHHHHHHHHHHCCC	1.42	24333276
217	S-nitrosocysteine	DMAQLETCVRSIQLD CHHHHHHHHHHHCCC	1.42	-
231	Phosphorylation	DGLVWGASKLVPVGY CCEEECCCCCEEECC	23.68	26643407
232	Ubiquitination	GLVWGASKLVPVGYG CEEECCCCCEEECCC	53.63	-
238	Phosphorylation	SKLVPVGYGIRKLQI CCCEEECCCEEEEEE	15.04	25367039
279	Phosphorylation	SVDIAAFDKI----- HCCHHHCCCC-----	42.91	24719451
279 (in isoform 3)	Phosphorylation	-	42.91	25890499
293 (in isoform 3)	Phosphorylation	-		29899451
370 (in isoform 3)	Phosphorylation	-		22807455
372 (in isoform 3)	Phosphorylation	-		22807455
373 (in isoform 3)	Phosphorylation	-		27149854
492	Phosphorylation	-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		24719451
498	Phosphorylation	-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		24719451
512	Phosphorylation	---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		24719451

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
162	S	Phosphorylation	Kinase	CK2-FAMILY	-	GPS
162	S	Phosphorylation	Kinase	CK2	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EF1D_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 EF1D_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EF1D_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EF1D_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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.	19131326 [Abstract]
"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.	19144319 [Abstract]
"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.	19367708 [Abstract]
"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.	18630941 [Abstract]
"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.	17525332 [Abstract]
"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.	17622165 [Abstract]
"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.	17203969 [Abstract]