UniProt ID | IF4H_HUMAN | |
---|---|---|
UniProt AC | Q15056 | |
Protein Name | Eukaryotic translation initiation factor 4H | |
Gene Name | EIF4H | |
Organism | Homo sapiens (Human). | |
Sequence Length | 248 | |
Subcellular Localization | Cytoplasm, perinuclear region. | |
Protein Description | Stimulates the RNA helicase activity of EIF4A in the translation initiation complex. Binds weakly mRNA.. | |
Protein Sequence | MADFDTYDDRAYSSFGGGRGSRGSAGGHGSRSQKELPTEPPYTAYVGNLPFNTVQGDIDAIFKDLSIRSVRLVRDKDTDKFKGFCYVEFDEVDSLKEALTYDGALLGDRSLRVDIAEGRKQDKGGFGFRKGGPDDRGMGSSRESRGGWDSRDDFNSGFRDDFLGGRGGSRPGDRRTGPPMGSRFRDGPPLRGSNMDFREPTEEERAQRPRLQLKPRTVATPLNQVANPNSAIFGGARPREEVVQKEQE | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
2 | Acetylation | ------MADFDTYDD ------CCCCCCCCC | 26.61 | 19413330 | |
6 | Phosphorylation | --MADFDTYDDRAYS --CCCCCCCCCCHHH | 28.92 | 28796482 | |
7 | Phosphorylation | -MADFDTYDDRAYSS -CCCCCCCCCCHHHC | 20.07 | 28796482 | |
10 | Dimethylation | DFDTYDDRAYSSFGG CCCCCCCCHHHCCCC | 32.31 | - | |
10 | Methylation | DFDTYDDRAYSSFGG CCCCCCCCHHHCCCC | 32.31 | - | |
12 | Nitration | DTYDDRAYSSFGGGR CCCCCCHHHCCCCCC | 13.02 | - | |
12 | Phosphorylation | DTYDDRAYSSFGGGR CCCCCCHHHCCCCCC | 13.02 | 27273156 | |
12 (in isoform 2) | Phosphorylation | - | 13.02 | - | |
13 (in isoform 2) | Phosphorylation | - | 20.43 | - | |
13 | Phosphorylation | TYDDRAYSSFGGGRG CCCCCHHHCCCCCCC | 20.43 | 22167270 | |
14 | Phosphorylation | YDDRAYSSFGGGRGS CCCCHHHCCCCCCCC | 18.42 | 23401153 | |
14 (in isoform 2) | Phosphorylation | - | 18.42 | - | |
19 | Dimethylation | YSSFGGGRGSRGSAG HHCCCCCCCCCCCCC | 43.09 | - | |
19 | Methylation | YSSFGGGRGSRGSAG HHCCCCCCCCCCCCC | 43.09 | - | |
21 | Phosphorylation | SFGGGRGSRGSAGGH CCCCCCCCCCCCCCC | 31.91 | 22167270 | |
21 (in isoform 2) | Phosphorylation | - | 31.91 | 21406692 | |
22 | Methylation | FGGGRGSRGSAGGHG CCCCCCCCCCCCCCC | 46.00 | - | |
24 | Phosphorylation | GGRGSRGSAGGHGSR CCCCCCCCCCCCCCC | 23.72 | 25159151 | |
24 (in isoform 2) | Phosphorylation | - | 23.72 | - | |
30 | Phosphorylation | GSAGGHGSRSQKELP CCCCCCCCCCCCCCC | 24.08 | 30242111 | |
31 | Methylation | SAGGHGSRSQKELPT CCCCCCCCCCCCCCC | 47.93 | - | |
32 | Phosphorylation | AGGHGSRSQKELPTE CCCCCCCCCCCCCCC | 47.50 | 28464451 | |
34 | Ubiquitination | GHGSRSQKELPTEPP CCCCCCCCCCCCCCC | 63.57 | 29967540 | |
38 | Phosphorylation | RSQKELPTEPPYTAY CCCCCCCCCCCCEEE | 73.98 | 26434776 | |
42 | Phosphorylation | ELPTEPPYTAYVGNL CCCCCCCCEEEECCC | 18.08 | 20090780 | |
43 | Phosphorylation | LPTEPPYTAYVGNLP CCCCCCCEEEECCCC | 19.79 | 19690332 | |
45 (in isoform 2) | Phosphorylation | - | 10.90 | - | |
45 | Phosphorylation | TEPPYTAYVGNLPFN CCCCCEEEECCCCCC | 10.90 | 20090780 | |
53 | O-linked_Glycosylation | VGNLPFNTVQGDIDA ECCCCCCCCCCCHHH | 18.00 | OGP | |
66 | Phosphorylation | DAIFKDLSIRSVRLV HHHHHCCCCCEEEEE | 26.53 | 24719451 | |
68 | Methylation | IFKDLSIRSVRLVRD HHHCCCCCEEEEEEE | 26.23 | - | |
69 | Phosphorylation | FKDLSIRSVRLVRDK HHCCCCCEEEEEEEC | 15.21 | 21712546 | |
76 | Ubiquitination | SVRLVRDKDTDKFKG EEEEEEECCCCCCCC | 52.54 | 22817900 | |
78 | Ubiquitination | RLVRDKDTDKFKGFC EEEEECCCCCCCCEE | 46.99 | 22817900 | |
80 (in isoform 1) | Ubiquitination | - | 51.58 | 21906983 | |
80 | Acetylation | VRDKDTDKFKGFCYV EEECCCCCCCCEEEE | 51.58 | 23749302 | |
80 | Ubiquitination | VRDKDTDKFKGFCYV EEECCCCCCCCEEEE | 51.58 | 22817900 | |
80 | 2-Hydroxyisobutyrylation | VRDKDTDKFKGFCYV EEECCCCCCCCEEEE | 51.58 | - | |
82 | Ubiquitination | DKDTDKFKGFCYVEF ECCCCCCCCEEEEEE | 57.74 | 22817900 | |
84 | Ubiquitination | DTDKFKGFCYVEFDE CCCCCCCEEEEEECC | 2.54 | 22817900 | |
86 | Nitration | DKFKGFCYVEFDEVD CCCCCEEEEEECCCC | 10.76 | - | |
86 | Phosphorylation | DKFKGFCYVEFDEVD CCCCCEEEEEECCCC | 10.76 | 28796482 | |
94 | Phosphorylation | VEFDEVDSLKEALTY EEECCCCHHHHHHCC | 46.66 | 27499020 | |
100 | Phosphorylation | DSLKEALTYDGALLG CHHHHHHCCCCCCCC | 26.98 | 21945579 | |
101 | Phosphorylation | SLKEALTYDGALLGD HHHHHHCCCCCCCCC | 17.15 | 21945579 | |
101 | Nitration | SLKEALTYDGALLGD HHHHHHCCCCCCCCC | 17.15 | - | |
101 (in isoform 2) | Phosphorylation | - | 17.15 | - | |
109 | Methylation | DGALLGDRSLRVDIA CCCCCCCCEEEEEEC | 35.47 | - | |
110 (in isoform 2) | Phosphorylation | - | 25.85 | - | |
110 | Phosphorylation | GALLGDRSLRVDIAE CCCCCCCEEEEEECC | 25.85 | 20068231 | |
120 | Ubiquitination | VDIAEGRKQDKGGFG EEECCCCCCCCCCCC | 73.95 | 29967540 | |
123 | Ubiquitination | AEGRKQDKGGFGFRK CCCCCCCCCCCCCCC | 59.44 | 27667366 | |
123 | 2-Hydroxyisobutyrylation | AEGRKQDKGGFGFRK CCCCCCCCCCCCCCC | 59.44 | - | |
123 | Acetylation | AEGRKQDKGGFGFRK CCCCCCCCCCCCCCC | 59.44 | 25953088 | |
123 | Malonylation | AEGRKQDKGGFGFRK CCCCCCCCCCCCCCC | 59.44 | 26320211 | |
125 | Ubiquitination | GRKQDKGGFGFRKGG CCCCCCCCCCCCCCC | 25.83 | 24816145 | |
130 | Methylation | KGGFGFRKGGPDDRG CCCCCCCCCCCCCCC | 66.99 | - | |
136 (in isoform 2) | Methylation | - | 44.36 | - | |
136 | Methylation | RKGGPDDRGMGSSRE CCCCCCCCCCCCCCC | 44.36 | - | |
140 | Phosphorylation | PDDRGMGSSRESRGG CCCCCCCCCCCCCCC | 19.82 | 27135362 | |
145 | Methylation | MGSSRESRGGWDSRD CCCCCCCCCCCCCCC | 42.78 | - | |
146 (in isoform 2) | Ubiquitination | - | 51.31 | 21906983 | |
150 | Phosphorylation | ESRGGWDSRDDFNSG CCCCCCCCCCCCCCC | 30.97 | 20873877 | |
166 | Dimethylation | RDDFLGGRGGSRPGD CCCCCCCCCCCCCCC | 44.49 | - | |
166 | Methylation | RDDFLGGRGGSRPGD CCCCCCCCCCCCCCC | 44.49 | 24129315 | |
170 | Methylation | LGGRGGSRPGDRRTG CCCCCCCCCCCCCCC | 42.36 | - | |
173 (in isoform 2) | Phosphorylation | - | 39.30 | - | |
174 | Methylation | GGSRPGDRRTGPPMG CCCCCCCCCCCCCCC | 43.93 | - | |
175 | Methylation | GSRPGDRRTGPPMGS CCCCCCCCCCCCCCC | 49.10 | - | |
176 | Phosphorylation | SRPGDRRTGPPMGSR CCCCCCCCCCCCCCC | 55.74 | 23186163 | |
182 | Phosphorylation | RTGPPMGSRFRDGPP CCCCCCCCCCCCCCC | 23.22 | 28857561 | |
183 | Methylation | TGPPMGSRFRDGPPL CCCCCCCCCCCCCCC | 25.53 | - | |
185 | Methylation | PPMGSRFRDGPPLRG CCCCCCCCCCCCCCC | 47.03 | - | |
191 | Methylation | FRDGPPLRGSNMDFR CCCCCCCCCCCCCCC | 52.87 | - | |
193 | Phosphorylation | DGPPLRGSNMDFREP CCCCCCCCCCCCCCC | 23.65 | 23401153 | |
195 | Sulfoxidation | PPLRGSNMDFREPTE CCCCCCCCCCCCCCH | 5.73 | 28465586 | |
198 | Methylation | RGSNMDFREPTEEER CCCCCCCCCCCHHHH | 44.73 | - | |
201 | Phosphorylation | NMDFREPTEEERAQR CCCCCCCCHHHHHHC | 51.80 | 28857561 | |
214 | Sumoylation | QRPRLQLKPRTVATP HCCCCCCCCCCEECC | 21.35 | - | |
214 | Acetylation | QRPRLQLKPRTVATP HCCCCCCCCCCEECC | 21.35 | 21339330 | |
214 | Sumoylation | QRPRLQLKPRTVATP HCCCCCCCCCCEECC | 21.35 | - | |
214 | Ubiquitination | QRPRLQLKPRTVATP HCCCCCCCCCCEECC | 21.35 | - | |
217 | Phosphorylation | RLQLKPRTVATPLNQ CCCCCCCCEECCHHH | 24.03 | 22322096 | |
220 | Phosphorylation | LKPRTVATPLNQVAN CCCCCEECCHHHCCC | 24.79 | 22322096 | |
225 (in isoform 2) | Acetylation | - | 5.60 | - | |
225 | Ubiquitination | VATPLNQVANPNSAI EECCHHHCCCCCCCC | 5.60 | 33845483 | |
225 | Acetylation | VATPLNQVANPNSAI EECCHHHCCCCCCCC | 5.60 | 19608861 | |
227 | Ubiquitination | TPLNQVANPNSAIFG CCHHHCCCCCCCCCC | 37.11 | 24816145 | |
230 | Phosphorylation | NQVANPNSAIFGGAR HHCCCCCCCCCCCCC | 24.81 | 22322096 | |
237 | Methylation | SAIFGGARPREEVVQ CCCCCCCCCHHHHHH | 33.80 | - | |
239 | Methylation | IFGGARPREEVVQKE CCCCCCCHHHHHHHH | 47.34 | - | |
245 (in isoform 1) | Ubiquitination | - | 50.16 | 21906983 | |
245 | Acetylation | PREEVVQKEQE---- CHHHHHHHHCC---- | 50.16 | 23749302 | |
245 | Ubiquitination | PREEVVQKEQE---- CHHHHHHHHCC---- | 50.16 | 33845483 | |
247 | Ubiquitination | EEVVQKEQE------ HHHHHHHCC------ | 69.59 | 24816145 |
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 IF4H_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of IF4H_HUMAN !! |
* 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 IF4H_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
CK068_HUMAN | C11orf68 | physical | 16189514 | |
TRA2B_HUMAN | TRA2B | physical | 22939629 | |
ROA0_HUMAN | HNRNPA0 | physical | 22939629 | |
SRSF3_HUMAN | SRSF3 | physical | 22939629 | |
RBMS2_HUMAN | RBMS2 | physical | 22939629 | |
PUF60_HUMAN | PUF60 | physical | 22939629 | |
RM09_HUMAN | MRPL9 | physical | 22939629 | |
RM44_HUMAN | MRPL44 | physical | 22939629 | |
NDRG1_HUMAN | NDRG1 | physical | 22863883 | |
6PGD_HUMAN | PGD | physical | 22863883 | |
CK068_HUMAN | C11orf68 | physical | 25416956 | |
LNX1_HUMAN | LNX1 | physical | 25416956 | |
FA98B_HUMAN | FAM98B | physical | 26344197 | |
KDM3A_HUMAN | KDM3A | physical | 26344197 | |
LIX1L_HUMAN | LIX1L | physical | 26344197 | |
MESD_HUMAN | MESDC2 | physical | 26344197 | |
RT36_HUMAN | MRPS36 | physical | 26344197 | |
PA1B2_HUMAN | PAFAH1B2 | physical | 26344197 | |
RAVR1_HUMAN | RAVER1 | physical | 26344197 |
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. |
loading...
Acetylation | |
Reference | PubMed |
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY. | |
"Exploring proteomes and analyzing protein processing by massspectrometric identification of sorted N-terminal peptides."; Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,Thomas G.R., Vandekerckhove J.; Nat. Biotechnol. 21:566-569(2003). Cited for: PROTEIN SEQUENCE OF 2-10, AND ACETYLATION AT ALA-2. | |
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-245, AND MASS SPECTROMETRY. | |
Phosphorylation | |
Reference | PubMed |
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32, AND MASSSPECTROMETRY. | |
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-193, AND MASSSPECTROMETRY. | |
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer."; Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; Cell 131:1190-1203(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-45, AND MASSSPECTROMETRY. | |
"Quantitative phosphoproteome analysis using a dendrimer conjugationchemistry and tandem mass spectrometry."; Tao W.A., Wollscheid B., O'Brien R., Eng J.K., Li X.-J.,Bodenmiller B., Watts J.D., Hood L., Aebersold R.; Nat. Methods 2:591-598(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, AND MASSSPECTROMETRY. | |
"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-12; TYR-45 AND TYR-101,AND MASS SPECTROMETRY. |