IF6_HUMAN - dbPTM
IF6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IF6_HUMAN
UniProt AC P56537
Protein Name Eukaryotic translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_03132}
Gene Name EIF6 {ECO:0000255|HAMAP-Rule:MF_03132, ECO:0000312|HGNC:HGNC:6159}
Organism Homo sapiens (Human).
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. [PubMed: 10085284]
Protein Sequence MAVRASFENNCEIGCFAKLTNTYCLVAIGGSENFYSVFEGELSDTIPVVHASIAGCRIIGRMCVGNRHGLLVPNNTTDQELQHIRNSLPDTVQIRRVEERLSALGNVTTCNDYVALVHPDLDRETEEILADVLKVEVFRQTVADQVLVGSYCVFSNQGGLVHPKTSIEDQDELSSLLQVPLVAGTVNRGSEVIAAGMVVNDWCAFCGLDTTSTELSVVESVFKLNEAQPSTIATSMRDSLIDSLT
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 Orthologous
Protein Cluster
6Phosphorylation--MAVRASFENNCEI
--CCCCEECCCCCEE		23.6420873877
11S-nitrosylationRASFENNCEIGCFAK
CEECCCCCEECEEEE		6.4222178444
15S-nitrosylationENNCEIGCFAKLTNT
CCCCEECEEEECCCE		3.5422178444
40 (in isoform 2)Phosphorylation-29.6725159151
54UbiquitinationPVVHASIAGCRIIGR
CEEEHHHCCCEEECE		14.4521963094
85MethylationDQELQHIRNSLPDTV
HHHHHHHHHCCCCCC		25.26-
87PhosphorylationELQHIRNSLPDTVQI
HHHHHHHCCCCCCHH		31.2820873877
90 (in isoform 2)Phosphorylation-65.8825599653
95MethylationLPDTVQIRRVEERLS
CCCCCHHHHHHHHHH		21.36-
110S-palmitoylationALGNVTTCNDYVALV
HHCCCCCCCCEEEEE		2.3929575903
113PhosphorylationNVTTCNDYVALVHPD
CCCCCCCEEEEECCC		3.5922817900
150PhosphorylationADQVLVGSYCVFSNQ
HHHEEECCEEEEECC		14.1024719451
151PhosphorylationDQVLVGSYCVFSNQG
HHEEECCEEEEECCC		6.1628152594
165PhosphorylationGGLVHPKTSIEDQDE
CCCCCCCCCCCCHHH		39.1123663014
166PhosphorylationGLVHPKTSIEDQDEL
CCCCCCCCCCCHHHH		30.0623663014
174PhosphorylationIEDQDELSSLLQVPL
CCCHHHHHHHHCCCE		19.5212917340
175PhosphorylationEDQDELSSLLQVPLV
CCHHHHHHHHCCCEE		45.8012917340
185PhosphorylationQVPLVAGTVNRGSEV
CCCEEEEECCCCCCE		12.6021712546
216PhosphorylationDTTSTELSVVESVFK
CCCCCHHHHHHHHHC		20.2020068231
220PhosphorylationTELSVVESVFKLNEA
CHHHHHHHHHCCCCC		22.6520068231
223AcetylationSVVESVFKLNEAQPS
HHHHHHHCCCCCCCC		48.5218530469
230PhosphorylationKLNEAQPSTIATSMR
CCCCCCCCHHHHHHH		21.9928176443
230O-linked_GlycosylationKLNEAQPSTIATSMR
CCCCCCCCHHHHHHH		21.9923301498
231PhosphorylationLNEAQPSTIATSMRD
CCCCCCCHHHHHHHH		22.7025159151
231O-linked_GlycosylationLNEAQPSTIATSMRD
CCCCCCCHHHHHHHH		22.70OGP
234PhosphorylationAQPSTIATSMRDSLI
CCCCHHHHHHHHHHH		21.1425159151
235PhosphorylationQPSTIATSMRDSLID
CCCHHHHHHHHHHHH		11.6425159151
236SulfoxidationPSTIATSMRDSLIDS
CCHHHHHHHHHHHHH		4.8521406390
239PhosphorylationIATSMRDSLIDSLT-
HHHHHHHHHHHHCC-		19.5025159151
243PhosphorylationMRDSLIDSLT-----
HHHHHHHHCC-----		27.2425159151
245PhosphorylationDSLIDSLT-------
HHHHHHCC-------		40.2830278072
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
174SPhosphorylationKinaseCSNK1A1P48729
GPS
174SPhosphorylationKinaseCK1-FAMILY-GPS
174SPhosphorylationKinaseCK1-Uniprot
175SPhosphorylationKinaseCSNK1A1P48729
GPS
175SPhosphorylationKinaseCK1-FAMILY-GPS
175SPhosphorylationKinaseCK1-Uniprot
235SPhosphorylationKinasePRKCAP17252
GPS
235SPhosphorylationKinasePKCB ISO2P05771-2
PSP
235SPhosphorylationKinasePKC-FAMILY-GPS
235SPhosphorylationKinasePKC-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
174SPhosphorylation

21084295
175SPhosphorylation

21084295
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 IF6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BCCIP_HUMANBCCIPphysical
17353931
RGS10_HUMANRGS10physical
17353931
RL3_HUMANRPL3physical
17353931
NOG1_HUMANGTPBP4physical
17353931
PSA_HUMANNPEPPSphysical
17353931
RRP15_HUMANRRP15physical
17353931
FUS_HUMANFUSphysical
17353931
RL34_HUMANRPL34physical
17353931
SYYC_HUMANYARSphysical
17353931
SRBS1_HUMANSORBS1physical
17353931
HYAS1_HUMANHAS1physical
17353931
OAT_HUMANOATphysical
17353931
PUR6_HUMANPAICSphysical
17353931
RACK1_HUMANGNB2L1physical
14654845
ABCF1_HUMANABCF1physical
16169070
AKTS1_HUMANAKT1S1physical
16169070
HPF1_HUMANC4orf27physical
16169070
RT31_HUMANMRPS31physical
16169070
OFD1_HUMANOFD1physical
16169070
SEPT3_HUMANSEPT3physical
16169070
UBP33_HUMANUSP33physical
16169070
WFS1_HUMANWFS1physical
16169070
ACAP3_HUMANACAP3physical
16169070
CREL1_HUMANCRELD1physical
16169070
FUND2_HUMANFUNDC2physical
16169070
ODPA_HUMANPDHA1physical
16169070
LRIF1_HUMANLRIF1physical
16169070
RL6_HUMANRPL6physical
16169070
REN3B_HUMANUPF3Bphysical
16169070
ACTG_HUMANACTG1physical
16169070
ENOX1_HUMANENOX1physical
16169070
GIT1_HUMANGIT1physical
16169070
HIP1_HUMANHIP1physical
16169070
DPOA2_HUMANPOLA2physical
16169070
ALDH2_HUMANALDH2physical
16169070
CE126_HUMANKIAA1377physical
16169070
PSME1_HUMANPSME1physical
16169070
EIF3B_HUMANEIF3Bphysical
15946946
EIF3C_HUMANEIF3Cphysical
15946946
EIF3J_HUMANEIF3Jphysical
15946946
A4_HUMANAPPphysical
21832049
RL6_HUMANRPL6physical
22939629
RL7_HUMANRPL7physical
22939629
RL18A_HUMANRPL18Aphysical
22939629
RL5_HUMANRPL5physical
22939629
RL4_HUMANRPL4physical
22939629
NOP58_HUMANNOP58physical
22939629
RL37A_HUMANRPL37Aphysical
22939629
RL23_HUMANRPL23physical
22939629
RS24_HUMANRPS24physical
22939629
RS4X_HUMANRPS4Xphysical
22939629
RL31_HUMANRPL31physical
22939629
RL17_HUMANRPL17physical
22939629
RL9_HUMANRPL9physical
22939629
RS6_HUMANRPS6physical
22939629
RS15A_HUMANRPS15Aphysical
22939629
RS5_HUMANRPS5physical
22939629
NOP2_HUMANNOP2physical
22939629
LMNB1_HUMANLMNB1physical
22939629
RBM14_HUMANRBM14physical
22939629
ZBT26_HUMANZBTB26physical
21988832
ABHEA_HUMANABHD14Aphysical
22863883
ASNA_HUMANASNA1physical
22863883
BZW2_HUMANBZW2physical
22863883
CAN1_HUMANCAPN1physical
22863883
COF1_HUMANCFL1physical
22863883
CNBP_HUMANCNBPphysical
22863883
PSF3_HUMANGINS3physical
22863883
HPRT_HUMANHPRT1physical
22863883
PA1B2_HUMANPAFAH1B2physical
22863883
PEPD_HUMANPEPDphysical
22863883
BCCIP_HUMANBCCIPphysical
24778252
NOP53_HUMANGLTSCR2physical
24778252
NOG1_HUMANGTPBP4physical
24778252
NMD3_HUMANNMD3physical
24778252
POP1_HUMANPOP1physical
24778252
SSF1_HUMANPPANphysical
24778252
TOP2A_HUMANTOP2Aphysical
24778252
TOP2B_HUMANTOP2Bphysical
24778252
ZN622_HUMANZNF622physical
24778252
CHM4A_HUMANCHMP4Aphysical
26344197
CHM4B_HUMANCHMP4Bphysical
26344197
DDX27_HUMANDDX27physical
26344197
FBRL_HUMANFBLphysical
26344197
IMPA1_HUMANIMPA1physical
26344197
PUM3_HUMANKIAA0020physical
26344197
NH2L1_HUMANNHP2L1physical
26344197
PSA4_HUMANPSMA4physical
26344197
RL3_HUMANRPL3physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IF6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Opposing action of casein kinase 1 and calcineurin in nucleo-cytoplasmic shuttling of mammalian translation initiation factoreIF6.";
Biswas A., Mukherjee S., Das S., Shields D., Chow C.W., Maitra U.;
J. Biol. Chem. 286:3129-3138(2011).
Cited for: PHOSPHORYLATION AT SER-174 AND SER-175 BY CSNK1D/CK1, AND SUBCELLULARLOCATION.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-243, ANDMASS SPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-239; SER-243AND THR-245, AND MASS SPECTROMETRY.
"Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosomeassembly.";
Ceci M., Gaviraghi C., Gorrini C., Sala L.A., Offenhauser N.,Marchisio P.C., Biffo S.;
Nature 426:579-584(2003).
Cited for: FUNCTION, SUBUNIT, PHOSPHORYLATION AT SER-235, AND INTERACTION WITHGNB2L1.
"Phosphorylation of mammalian eukaryotic translation initiation factor6 and its Saccharomyces cerevisiae homologue Tif6p: evidence thatphosphorylation of Tif6p regulates its nucleocytoplasmic distributionand is required for yeast cell growth.";
Basu U., Si K., Deng H., Maitra U.;
Mol. Cell. Biol. 23:6187-6199(2003).
Cited for: PHOSPHORYLATION AT SER-174 AND SER-175, SUBCELLULAR LOCATION, ANDNUCLEOCYTOPLASMIC SHUTTLING.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-113, AND MASSSPECTROMETRY.

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