IF6_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF6_RAT
• UniProt AC: Q3KRD8
• Protein Name: Eukaryotic translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_03132}
• Gene Name: Eif6
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 245
• Subcellular Localization: Cytoplasm . Nucleus, nucleolus . Shuttles between cytoplasm and nucleus/nucleolus.
• Protein Description: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Behaves as a stimulatory translation initiation factor downstream insulin/growth factors. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by a RACK1 (RACK1)-dependent protein kinase C activity. In tissues responsive to insulin, controls fatty acid synthesis and glycolysis by exerting translational control of adipogenic transcription factors such as CEBPB, CEBPD and ATF4 that have G/C rich or uORF in their 5'UTR. Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis. Involved in miRNA-mediated gene silencing by the RNA-induced silencing complex (RISC). Required for both miRNA-mediated translational repression and miRNA-mediated cleavage of complementary mRNAs by RISC. Modulates cell cycle progression and global translation of pre-B cells, its activation seems to be rate-limiting in tumorigenesis and tumor growth..
• Protein Sequence: MAVRASFENNCEVGCFAKLTNTYCLVAIGGSENFYSVFEGELSDTIPVVHASIAGCRIIGRMCVGNRHGLLVPNNTTDQELQHIRNSLPDSVQIRRVEERLSALGNVTTCNDYVALVHPDLDRETEEILADVLKVEVFRQTVADQVLVGSYCVFSNQGGLVHPKTSIEDQDELSSLLQVPLVAGTVNRGSEVIAAGMVVNDWCAFCGLDTTSTELSVVESVFKLNEAKPSTIATSMRDSLIDSLT

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
6	Phosphorylation	--MAVRASFENNCEV --CCCCEECCCCCCC	23.64	23984901
113	Phosphorylation	NVTTCNDYVALVHPD CCCCCCCEEEEECCC	3.59	-
165	Phosphorylation	GGLVHPKTSIEDQDE CCCCCCCCCCCCHHH	39.11	23984901
166	Phosphorylation	GLVHPKTSIEDQDEL CCCCCCCCCCCHHHH	30.06	23984901
174	Phosphorylation	IEDQDELSSLLQVPL CCCHHHHHHHHCCCE	19.52	23984901
175	Phosphorylation	EDQDELSSLLQVPLV CCHHHHHHHHCCCEE	45.80	23984901
230	Phosphorylation	KLNEAKPSTIATSMR CCCCCCCCHHCHHHH	31.57	27097102
231	Phosphorylation	LNEAKPSTIATSMRD CCCCCCCHHCHHHHH	24.14	27097102
234	Phosphorylation	AKPSTIATSMRDSLI CCCCHHCHHHHHHHH	21.14	23984901
235	Phosphorylation	KPSTIATSMRDSLID CCCHHCHHHHHHHHH	11.64	23984901
239	Phosphorylation	IATSMRDSLIDSLT- HCHHHHHHHHHHCC-	19.50	27097102
243	Phosphorylation	MRDSLIDSLT----- HHHHHHHHCC-----	27.24	29779826
245	Phosphorylation	DSLIDSLT------- HHHHHHCC-------	40.28	27097102

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
174	S	Phosphorylation	Kinase	CK1	-	Uniprot
175	S	Phosphorylation	Kinase	CK1	-	Uniprot
235	S	Phosphorylation	Kinase	PKC	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
174	S	Phosphorylation	Phosphorylation at Ser-174 and Ser-175 by CSNK1D/CK1 promotes nuclear export.	-
175	S	Phosphorylation	Phosphorylation at Ser-174 and Ser-175 by CSNK1D/CK1 promotes nuclear export.	-

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of IF6_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of IF6_RAT !!

Drug and Disease Associations

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