IF6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF6_MOUSE
• UniProt AC: O55135
• Protein Name: Eukaryotic translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_03132}
• Gene Name: Eif6
• Organism: Mus musculus (Mouse).
• 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. [PubMed: 26383020 Required for ROS-dependent megakaryocyte maturation and platelets formation, controls the expression of mitochondrial respiratory chain genes involved in reactive oxygen species (ROS) synthesis]
• Protein Sequence: MAVRASFENNCEVGCFAKLTNAYCLVAIGGSENFYSVFEGELSDAIPVVHASIAGCRIIGRMCVGNRHGLLVPNNTTDQELQHIRNSLPDSVQIRRVEERLSALGNVTTCNDYVALVHPDLDRETEEILADVLKVEVFRQTVADQVLVGSYCVFSNQGGLVHPKTSIEDQDELSSLLQVPLVAGTVNRGSEVIAAGMVVNDWCAFCGLDTTSTELSVVESVFKLNEAKPSTIATSMRDSLIDSLT

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
63	Glutathionylation	CRIIGRMCVGNRHGL CEEECEEECCCCCCE	3.23	24333276
113	Phosphorylation	NVTTCNDYVALVHPD CCCCCCCEEEEECCC	3.59	-
150	Phosphorylation	ADQVLVGSYCVFSNQ HHHEEECCEEEEECC	14.10	-
152	S-palmitoylation	QVLVGSYCVFSNQGG HEEECCEEEEECCCC	2.39	26165157
152	Glutathionylation	QVLVGSYCVFSNQGG HEEECCEEEEECCCC	2.39	24333276
165	Phosphorylation	GGLVHPKTSIEDQDE CCCCCCCCCCCCHHH	39.11	21536732
166	Phosphorylation	GLVHPKTSIEDQDEL CCCCCCCCCCCHHHH	30.06	21536732
174	Phosphorylation	IEDQDELSSLLQVPL CCCHHHHHHHHCCCE	19.52	26745281
175	Phosphorylation	EDQDELSSLLQVPLV CCHHHHHHHHCCCEE	45.80	26745281
228	Ubiquitination	VFKLNEAKPSTIATS HHCCCCCCCCHHCHH	33.07	22790023
228	Acetylation	VFKLNEAKPSTIATS HHCCCCCCCCHHCHH	33.07	23954790
230	Phosphorylation	KLNEAKPSTIATSMR CCCCCCCCHHCHHHH	31.57	26239621
231	Phosphorylation	LNEAKPSTIATSMRD CCCCCCCHHCHHHHH	24.14	23984901
234	Phosphorylation	AKPSTIATSMRDSLI CCCCHHCHHHHHHHH	21.14	26239621
235	Phosphorylation	KPSTIATSMRDSLID CCCHHCHHHHHHHHH	11.64	26239621
239	Phosphorylation	IATSMRDSLIDSLT- HCHHHHHHHHHHCC-	19.50	26824392
243	Phosphorylation	MRDSLIDSLT----- HHHHHHHHCC-----	27.24	25521595
245	Phosphorylation	DSLIDSLT------- HHHHHHCC-------	40.28	26160508

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-FAMILY	-	GPS
174	S	Phosphorylation	Kinase	CK1	-	Uniprot
175	S	Phosphorylation	Kinase	CK1-FAMILY	-	GPS
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.	21536732
175	S	Phosphorylation	Phosphorylation at Ser-174 and Ser-175 by CSNK1D/CK1 promotes nuclear export.	21536732

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_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of IF6_MOUSE !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Uncoupling of GTP hydrolysis from eIF6 release on the ribosome causesShwachman-Diamond syndrome.";
Finch A.J., Hilcenko C., Basse N., Drynan L.F., Goyenechea B.,Menne T.F., Gonzalez Fernandez A., Simpson P., D'Santos C.S.,Arends M.J., Donadieu J., Bellanne-Chantelot C., Costanzo M.,Boone C., McKenzie A.N., Freund S.M., Warren A.J.;
Genes Dev. 25:917-929(2011).
Cited for: PHOSPHORYLATION AT THR-165; SER-166; SER-174 AND SER-175,IDENTIFICATION AT THE 60S RIBOSOME SUBUNIT, AND MASS SPECTROMETRY.
PubMed: 21536732