UniProt ID | ILF2_HUMAN | |
---|---|---|
UniProt AC | Q12905 | |
Protein Name | Interleukin enhancer-binding factor 2 | |
Gene Name | ILF2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 390 | |
Subcellular Localization | Nucleus, nucleolus. Cytoplasm. Nucleus. Localized in cytoplasmic mRNP granules containing untranslated mRNAs. | |
Protein Description | Appears to function predominantly as a heterodimeric complex with ILF3. This complex may regulate transcription of the IL2 gene during T-cell activation. It can also promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus.. | |
Protein Sequence | MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRILSHGGFRKILGQEGDASYLASEISTWDGVIVTPSEKAYEKPPEKKEGEEEEENTEEPPQGEEEESMETQE | |
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 |
---|---|---|---|---|---|
15 | Phosphorylation | GRGGRFGSRGGPGGG CCCCCCCCCCCCCCC | 25.66 | - | |
16 | Asymmetric dimethylarginine | RGGRFGSRGGPGGGF CCCCCCCCCCCCCCC | 55.24 | - | |
16 | Methylation | RGGRFGSRGGPGGGF CCCCCCCCCCCCCCC | 55.24 | 24129315 | |
24 | Dimethylation | GGPGGGFRPFVPHIP CCCCCCCCCCCCCCC | 27.33 | - | |
24 | Methylation | GGPGGGFRPFVPHIP CCCCCCCCCCCCCCC | 27.33 | 24129315 | |
45 | Sumoylation | EMAFPRVKPAPDETS HHHCCCCCCCCCCCC | 36.42 | - | |
45 | Sumoylation | EMAFPRVKPAPDETS HHHCCCCCCCCCCCC | 36.42 | - | |
45 | Ubiquitination | EMAFPRVKPAPDETS HHHCCCCCCCCCCCC | 36.42 | 21906983 | |
45 | Acetylation | EMAFPRVKPAPDETS HHHCCCCCCCCCCCC | 36.42 | 26051181 | |
51 | Phosphorylation | VKPAPDETSFSEALL CCCCCCCCCHHHHHH | 42.31 | 30266825 | |
52 | Phosphorylation | KPAPDETSFSEALLK CCCCCCCCHHHHHHH | 25.40 | 30266825 | |
54 | Phosphorylation | APDETSFSEALLKRN CCCCCCHHHHHHHHC | 23.02 | 30266825 | |
59 | 2-Hydroxyisobutyrylation | SFSEALLKRNQDLAP CHHHHHHHHCCCCCC | 50.59 | - | |
59 | Ubiquitination | SFSEALLKRNQDLAP CHHHHHHHHCCCCCC | 50.59 | 21906983 | |
59 | Methylation | SFSEALLKRNQDLAP CHHHHHHHHCCCCCC | 50.59 | 24625217 | |
59 | Acetylation | SFSEALLKRNQDLAP CHHHHHHHHCCCCCC | 50.59 | 23749302 | |
68 | Phosphorylation | NQDLAPNSAEQASIL CCCCCCCHHHHHHHH | 31.93 | 29255136 | |
73 | Phosphorylation | PNSAEQASILSLVTK CCHHHHHHHHHHHHH | 24.61 | 29255136 | |
76 | Phosphorylation | AEQASILSLVTKINN HHHHHHHHHHHHHHH | 21.08 | 25850435 | |
79 | Phosphorylation | ASILSLVTKINNVID HHHHHHHHHHHHHHH | 31.34 | 21406692 | |
107 | Phosphorylation | EEVRQVGSYKKGTMT EEEEECCCCCCCCCC | 34.62 | 23828894 | |
109 | 2-Hydroxyisobutyrylation | VRQVGSYKKGTMTTG EEECCCCCCCCCCCC | 46.56 | - | |
109 | Ubiquitination | VRQVGSYKKGTMTTG EEECCCCCCCCCCCC | 46.56 | - | |
110 | Ubiquitination | RQVGSYKKGTMTTGH EECCCCCCCCCCCCC | 51.92 | - | |
141 | Ubiquitination | AVAALGNKVVESLRA HHHHCCHHHHHHHHC | 45.95 | 21906983 | |
186 | Sumoylation | TVPPNLRKLDPELHL CCCCCHHCCCHHHHH | 61.48 | 28112733 | |
186 | Sumoylation | TVPPNLRKLDPELHL CCCCCHHCCCHHHHH | 61.48 | - | |
186 | Ubiquitination | TVPPNLRKLDPELHL CCCCCHHCCCHHHHH | 61.48 | 21906983 | |
186 | Acetylation | TVPPNLRKLDPELHL CCCCCHHCCCHHHHH | 61.48 | 26051181 | |
196 | Ubiquitination | PELHLDIKVLQSALA HHHHHCHHHHHHHHH | 36.24 | 21906983 | |
200 | Phosphorylation | LDIKVLQSALAAIRH HCHHHHHHHHHHHHH | 22.53 | 24850871 | |
218 | Phosphorylation | FEENASQSTVKVLIR HHHCCCHHHHHHHHH | 32.45 | 23186163 | |
219 | Phosphorylation | EENASQSTVKVLIRL HHCCCHHHHHHHHHH | 19.40 | 21815630 | |
221 | Ubiquitination | NASQSTVKVLIRLLK CCCHHHHHHHHHHHH | 31.26 | 21906983 | |
322 | Phosphorylation | QTLVRILSHGGFRKI HHHHHHHHCCCHHHH | 20.09 | 23312004 | |
328 | Ubiquitination | LSHGGFRKILGQEGD HHCCCHHHHHCCCCC | 39.77 | 21906983 | |
338 | Phosphorylation | GQEGDASYLASEIST CCCCCHHHHHHHHCC | 14.17 | - | |
352 | Phosphorylation | TWDGVIVTPSEKAYE CCCCEEECCCHHHCC | 15.24 | - | |
356 | Ubiquitination | VIVTPSEKAYEKPPE EEECCCHHHCCCCCC | 61.68 | 21906983 | |
358 | Phosphorylation | VTPSEKAYEKPPEKK ECCCHHHCCCCCCCC | 35.24 | 27642862 | |
360 | Ubiquitination | PSEKAYEKPPEKKEG CCHHHCCCCCCCCCC | 53.87 | - | |
360 | Acetylation | PSEKAYEKPPEKKEG CCHHHCCCCCCCCCC | 53.87 | 25953088 | |
364 | Sumoylation | AYEKPPEKKEGEEEE HCCCCCCCCCCCCCC | 63.00 | 28112733 | |
364 | Ubiquitination | AYEKPPEKKEGEEEE HCCCCCCCCCCCCCC | 63.00 | - | |
364 | 2-Hydroxyisobutyrylation | AYEKPPEKKEGEEEE HCCCCCCCCCCCCCC | 63.00 | - | |
364 | Acetylation | AYEKPPEKKEGEEEE HCCCCCCCCCCCCCC | 63.00 | 26051181 | |
365 | Ubiquitination | YEKPPEKKEGEEEEE CCCCCCCCCCCCCCC | 70.10 | - | |
365 | Acetylation | YEKPPEKKEGEEEEE CCCCCCCCCCCCCCC | 70.10 | 26051181 | |
374 | Phosphorylation | GEEEEENTEEPPQGE CCCCCCCCCCCCCCC | 45.03 | 30576142 | |
385 | Phosphorylation | PQGEEEESMETQE-- CCCCHHHHHCCCC-- | 25.79 | 29507054 | |
388 | Phosphorylation | EEEESMETQE----- CHHHHHCCCC----- | 29.38 | 17525332 |
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 ILF2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ILF2_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 ILF2_HUMAN !! |
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. |
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Phosphorylation | |
Reference | PubMed |
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-388, AND MASSSPECTROMETRY. |