EIF3D_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3D_RAT
• UniProt AC: Q6AYK8
• Protein Name: Eukaryotic translation initiation factor 3 subunit D {ECO:0000255|HAMAP-Rule:MF_03003}
• Gene Name: Eif3d
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 548
• Subcellular Localization: Cytoplasm .
• Protein Description: mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression. In the eIF-3 complex, EIF3D specifically recognizes and binds the 7-methylguanosine cap of a subset of mRNAs..
• Protein Sequence: MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDETSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMVQFNLQTLPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYINHNFSQQCLRMGRERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDDIDLIVRCEHDGVMTGANGEVSFINIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQFKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYSLPDGTFSSEEDEEDEEEEEEEEEEEET

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
34	Phosphorylation	DMPYQPFSKGDRLGK CCCCCCCCCCCCCCC	42.27	28432305
53	Acetylation	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	-
121	Phosphorylation	MVQFNLQTLPKSAKQ HHHHHHHHCCCCHHH	48.47	23984901
160	Phosphorylation	KSQKPRDSSVEVRSD CCCCCCCCCCCCCCC	37.25	22673903
161	Phosphorylation	SQKPRDSSVEVRSDW CCCCCCCCCCCCCCC	26.96	28432305
258	S-nitrosocysteine	ILATLMSCTRSVYSW HHHHHHHCCCCCCCH	1.98	-
258	S-nitrosylation	ILATLMSCTRSVYSW HHHHHHHCCCCCCCH	1.98	21278135
275	Acetylation	VVQRVGSKLFFDKRD HEEEECCCCEEECCC	43.30	22902405
520	Phosphorylation	NKQVIRVYSLPDGTF CCCEEEEEECCCCCC	8.47	28551015
521	Phosphorylation	KQVIRVYSLPDGTFS CCEEEEEECCCCCCC	30.48	28551015
526	Phosphorylation	VYSLPDGTFSSEEDE EEECCCCCCCCCCCC	27.94	28551015
528	Phosphorylation	SLPDGTFSSEEDEED ECCCCCCCCCCCCCC	36.36	29779826
529	Phosphorylation	LPDGTFSSEEDEEDE CCCCCCCCCCCCCCH	40.59	28551015
548	Phosphorylation	EEEEEEET------- HHHHHHCC-------	47.38	29779826

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EIF3D_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3D_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EIF3D_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3D_RAT !!

Drug and Disease Associations

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