dbPTM

EF1D_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EF1D_RAT
UniProt AC	Q68FR9
Protein Name	Elongation factor 1-delta
Gene Name	Eef1d
Organism	Rattus norvegicus (Rat).
Sequence Length	281
Subcellular Localization	Isoform 2: 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 2: 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	MATNFLMHEKIWFDKFKYDDAERRFYEQMNGPVTAGSRQENGASVILRDIARARENIQKSLAGSSGPGASSGPGGDHSDLIVRIASLEVENQNLRGVVQDLQQAISKLEVRLSTLEKSSPTHRATAPQTQHVSPMRQVEPPAKKGATPAEDDEDNDIDLFGSDEEEEDKEAARLREERLRQYAEKKAKKPTLVAKSSILLDVKPWDDETDMAQLETCVRSIQLDGLVWGASKLVPVGYGIRKLQIQCVVEDDKVGTDLLEEEITKFEEHVQSVDIAAFNKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MATNFLMHE ------CCCCCCCCC	15.96	-
17	Acetylation	KIWFDKFKYDDAERR CHHHHCCCCCHHHHH	54.21	22902405
34	Phosphorylation	EQMNGPVTAGSRQEN HHHCCCCCCCCCCCC	28.56	27097102
37	Phosphorylation	NGPVTAGSRQENGAS CCCCCCCCCCCCCCC	28.46	27097102
44	Phosphorylation	SRQENGASVILRDIA CCCCCCCCHHHHHHH	15.87	-
60	Phosphorylation	ARENIQKSLAGSSGP HHHHHHHHHCCCCCC	13.69	27097102
64	Phosphorylation	IQKSLAGSSGPGASS HHHHHCCCCCCCCCC	26.89	28432305
65	Phosphorylation	QKSLAGSSGPGASSG HHHHCCCCCCCCCCC	48.35	28432305
70	Phosphorylation	GSSGPGASSGPGGDH CCCCCCCCCCCCCCH	41.57	27097102
71	Phosphorylation	SSGPGASSGPGGDHS CCCCCCCCCCCCCHH	48.77	27097102
86	Phosphorylation	DLIVRIASLEVENQN HHEEEEEEEEECCCC	23.77	27097102
106	Phosphorylation	QDLQQAISKLEVRLS HHHHHHHHHHHHHHH	33.92	22673903
107	Acetylation	DLQQAISKLEVRLST HHHHHHHHHHHHHHH	42.42	22902405
114	Phosphorylation	KLEVRLSTLEKSSPT HHHHHHHHHCCCCCC	43.45	25575281
117	Succinylation	VRLSTLEKSSPTHRA HHHHHHCCCCCCCCC	60.38	-
117	Succinylation	VRLSTLEKSSPTHRA HHHHHHCCCCCCCCC	60.38	-
117	Acetylation	VRLSTLEKSSPTHRA HHHHHHCCCCCCCCC	60.38	-
118	Phosphorylation	RLSTLEKSSPTHRAT HHHHHCCCCCCCCCC	31.98	25532521
119	Phosphorylation	LSTLEKSSPTHRATA HHHHCCCCCCCCCCC	44.90	25532521
121	Phosphorylation	TLEKSSPTHRATAPQ HHCCCCCCCCCCCCC	26.41	21373199
125	Phosphorylation	SSPTHRATAPQTQHV CCCCCCCCCCCCCCC	38.54	25403869
129	Phosphorylation	HRATAPQTQHVSPMR CCCCCCCCCCCCCCC	21.42	27097102
133	Phosphorylation	APQTQHVSPMRQVEP CCCCCCCCCCCCCCC	15.74	23712012
141 (in isoform 2)	Phosphorylation	-	43.11	28432305
147	Phosphorylation	PPAKKGATPAEDDED CCCCCCCCCCCCCCC	31.53	23712012
162	Phosphorylation	NDIDLFGSDEEEEDK CCCCCCCCCHHHHHH	34.22	23712012
240	Acetylation	LVPVGYGIRKLQIQC CEEECCCEEEEEEEE	2.36	-
240 (in isoform 2)	Acetylation	-	2.36	-
386	Acetylation	---------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------		-
475	Phosphorylation	--------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- ---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		-
476	Acetylation	---------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- ----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		-
502	Phosphorylation	------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------ ------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		-
516	Phosphorylation	-------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- --------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		-
531	Phosphorylation	----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------- -----------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------------		-

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_RAT !!

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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of EF1D_RAT !!

Drug and Disease Associations

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

Regulatory Network of EF1D_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites."; Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.; Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-162, AND MASSSPECTROMETRY (ISOFORM 2).	16641100 [Abstract]