dbPTM

EI3D1_DROME - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EI3D1_DROME
UniProt AC	Q9VCK0
Protein Name	Eukaryotic translation initiation factor 3 subunit D-1 {ECO:0000255\|HAMAP-Rule:MF_03003}
Gene Name	eIF3d1 {ECO:0000255\|HAMAP-Rule:MF_03003}
Organism	Drosophila melanogaster (Fruit fly).
Sequence Length	560
Subcellular Localization	Cytoplasm .
Protein Description	mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation. In the eIF-3 complex, eif3d specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs..
Protein Sequence	MSETINTAAQFPSFEKPTVQFNEKGWGPCELPDTFKDVPYQPFSKNDRLGKICDWTNTSNNDKKYQNKYASSFGTGIQYSYYHEEDETTFHLVDTARVQKPPHQRGRFRNMRNSRSGRGRNARGGLNTHGMTTLSGKNVKARDPRHGRGMGKKFGHRGPPPKMRESSVAVRADWASIEEMDFPRLIKLSLPNIKEGVDIVTCGTLEYYDKTYDRINVKNEKPLQKIDRIVHTVTTTDDPVIRRLSKTVGNVFATDAILATIMCSTRSNYSWDIVIEKVGDKVFMDKRDHTEFDLLTVNESSVEPPTDDDSSCNSPRNLAIEATFINHNFSQQVLKTGDQEPKYKFEESNPFISEDEDIQVASVGYRYKKWELGSDIVLVARCEHDGVLQTPSGEPQFMTIKALNEWDSKLANGVEWRQKLDTQRGAVLANELRNNACKLAKWTVQAVLAGSDQLKLGYVSRINPRDHSRHVILGTQQFKPHEFATQINLSMDNAWGILRCIIDLVMKQKDGKYLIMKDPNKPIIRLYDIPDNTFDSDDSDDGEGDDEGFQQVYNYAHNKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSETINTAA ------CCCCCCHHH	43.37	27794539
128	Phosphorylation	NARGGLNTHGMTTLS CCCCCCCCCCCCCCC	25.50	22817900
166	Phosphorylation	PPPKMRESSVAVRAD CCCCCCCCCEEEECC	21.54	19429919
167	Phosphorylation	PPKMRESSVAVRADW CCCCCCCCEEEECCC	14.89	19429919
189	Phosphorylation	FPRLIKLSLPNIKEG HHHHHHHCCCCCCCC	36.46	22817900
374	Phosphorylation	YKKWELGSDIVLVAR EEEECCCCCEEEEEE	36.47	19429919
527	Phosphorylation	NKPIIRLYDIPDNTF CCCEEEEEECCCCCC	11.28	23607784
533	Phosphorylation	LYDIPDNTFDSDDSD EEECCCCCCCCCCCC	35.88	19429919
536	Phosphorylation	IPDNTFDSDDSDDGE CCCCCCCCCCCCCCC	38.84	19429919
539	Phosphorylation	NTFDSDDSDDGEGDD CCCCCCCCCCCCCCC	42.46	19429919

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
Oops, there are no upstream regulatory protein records of EI3D1_DROME !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EI3D1_DROME !!

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 EI3D1_DROME !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
LANC3_DROME	CG2061	physical	14605208

Drug and Disease Associations

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

Regulatory Network of EI3D1_DROME

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos."; Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.; J. Proteome Res. 7:1675-1682(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-128, AND MASSSPECTROMETRY.	18327897 [Abstract]