| UniProt ID | EI2BA_HUMAN | |
|---|---|---|
| UniProt AC | Q14232 | |
| Protein Name | Translation initiation factor eIF-2B subunit alpha | |
| Gene Name | EIF2B1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 305 | |
| Subcellular Localization | ||
| Protein Description | Catalyzes the exchange of eukaryotic initiation factor 2-bound GDP for GTP.. | |
| Protein Sequence | MDDKELIEYFKSQMKEDPDMASAVAAIRTLLEFLKRDKGETIQGLRANLTSAIETLCGVDSSVAVSSGGELFLRFISLASLEYSDYSKCKKIMIERGELFLRRISLSRNKIADLCHTFIKDGATILTHAYSRVVLRVLEAAVAAKKRFSVYVTESQPDLSGKKMAKALCHLNVPVTVVLDAAVGYIMEKADLVIVGAEGVVENGGIINKIGTNQMAVCAKAQNKPFYVVAESFKFVRLFPLNQQDVPDKFKYKADTLKVAQTGQDLKEEHPWVDYTAPSLITLLFTDLGVLTPSAVSDELIKLYL | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 11 | Ubiquitination | KELIEYFKSQMKEDP HHHHHHHHHHHCCCC | 38.59 | 22817900 | |
| 15 | Ubiquitination | EYFKSQMKEDPDMAS HHHHHHHCCCCCHHH | 51.86 | 21890473 | |
| 15 | Acetylation | EYFKSQMKEDPDMAS HHHHHHHCCCCCHHH | 51.86 | 25953088 | |
| 15 | Ubiquitination | EYFKSQMKEDPDMAS HHHHHHHCCCCCHHH | 51.86 | 21906983 | |
| 20 | Sulfoxidation | QMKEDPDMASAVAAI HHCCCCCHHHHHHHH | 3.74 | 21406390 | |
| 29 | Phosphorylation | SAVAAIRTLLEFLKR HHHHHHHHHHHHHHH | 29.58 | 21406692 | |
| 35 | 2-Hydroxyisobutyrylation | RTLLEFLKRDKGETI HHHHHHHHHCCCCCH | 64.96 | - | |
| 35 | Ubiquitination | RTLLEFLKRDKGETI HHHHHHHHHCCCCCH | 64.96 | 22817900 | |
| 35 | Acetylation | RTLLEFLKRDKGETI HHHHHHHHHCCCCCH | 64.96 | 19608861 | |
| 35 | Ubiquitination | RTLLEFLKRDKGETI HHHHHHHHHCCCCCH | 64.96 | 21890473 | |
| 38 | Ubiquitination | LEFLKRDKGETIQGL HHHHHHCCCCCHHHH | 63.78 | 33845483 | |
| 38 | 2-Hydroxyisobutyrylation | LEFLKRDKGETIQGL HHHHHHCCCCCHHHH | 63.78 | - | |
| 38 | Ubiquitination | LEFLKRDKGETIQGL HHHHHHCCCCCHHHH | 63.78 | - | |
| 50 | Phosphorylation | QGLRANLTSAIETLC HHHHHHHHHHHHHHH | 18.87 | 22210691 | |
| 51 | Phosphorylation | GLRANLTSAIETLCG HHHHHHHHHHHHHHC | 30.34 | 22210691 | |
| 77 | Phosphorylation | ELFLRFISLASLEYS HHHHHHHHHHHCCCC | 18.38 | 29083192 | |
| 80 | Phosphorylation | LRFISLASLEYSDYS HHHHHHHHCCCCCHH | 27.33 | 29083192 | |
| 83 | Phosphorylation | ISLASLEYSDYSKCK HHHHHCCCCCHHHHC | 16.49 | 29083192 | |
| 84 | Phosphorylation | SLASLEYSDYSKCKK HHHHCCCCCHHHHCE | 22.24 | 29083192 | |
| 86 | Phosphorylation | ASLEYSDYSKCKKIM HHCCCCCHHHHCEEE | 12.23 | 21712546 | |
| 87 | Phosphorylation | SLEYSDYSKCKKIMI HCCCCCHHHHCEEEE | 36.25 | 21712546 | |
| 105 | O-linked_Glycosylation | ELFLRRISLSRNKIA HHHHHHHHCCCCHHH | 20.62 | 30379171 | |
| 105 | Phosphorylation | ELFLRRISLSRNKIA HHHHHHHHCCCCHHH | 20.62 | 20068231 | |
| 107 | Phosphorylation | FLRRISLSRNKIADL HHHHHHCCCCHHHHH | 27.32 | 24702127 | |
| 120 | Acetylation | DLCHTFIKDGATILT HHHHHHHHCCHHHHH | 46.01 | 26051181 | |
| 130 | Phosphorylation | ATILTHAYSRVVLRV HHHHHHHHHHHHHHH | 6.87 | 20393185 | |
| 145 | Acetylation | LEAAVAAKKRFSVYV HHHHHHHHHCEEEEE | 34.44 | 25953088 | |
| 145 | Ubiquitination | LEAAVAAKKRFSVYV HHHHHHHHHCEEEEE | 34.44 | 33845483 | |
| 145 | Methylation | LEAAVAAKKRFSVYV HHHHHHHHHCEEEEE | 34.44 | - | |
| 149 | Phosphorylation | VAAKKRFSVYVTESQ HHHHHCEEEEEECCC | 19.30 | 27251275 | |
| 160 | Phosphorylation | TESQPDLSGKKMAKA ECCCCCCCCHHHHHH | 56.82 | 25332170 | |
| 162 | Ubiquitination | SQPDLSGKKMAKALC CCCCCCCHHHHHHHH | 35.68 | - | |
| 163 | Acetylation | QPDLSGKKMAKALCH CCCCCCHHHHHHHHC | 47.84 | 24848925 | |
| 215 | Sulfoxidation | NKIGTNQMAVCAKAQ CEECCCCHHHHHHCC | 3.07 | 21406390 | |
| 253 | Ubiquitination | VPDKFKYKADTLKVA CCCHHHHHHHHHHCC | 40.14 | 29967540 | |
| 258 | Ubiquitination | KYKADTLKVAQTGQD HHHHHHHHCCCCCCC | 37.30 | 32015554 | |
| 258 | 2-Hydroxyisobutyrylation | KYKADTLKVAQTGQD HHHHHHHHCCCCCCC | 37.30 | - |
| 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 EI2BA_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EI2BA_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 EI2BA_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| EI2BG_HUMAN | EIF2B3 | physical | 17353931 | |
| PDIA4_HUMAN | PDIA4 | physical | 17353931 | |
| EI2BE_HUMAN | EIF2B5 | physical | 17353931 | |
| DCD_HUMAN | DCD | physical | 17353931 | |
| HNRPL_HUMAN | HNRNPL | physical | 17353931 | |
| EI2BE_HUMAN | EIF2B5 | physical | 10858531 | |
| EI2BD_YEAST | GCD2 | physical | 21795329 | |
| EI2BB_HUMAN | EIF2B2 | physical | 21795329 | |
| EI2BE_YEAST | GCD6 | physical | 21795329 | |
| EI2BA_HUMAN | EIF2B1 | physical | 25416956 | |
| GORS2_HUMAN | GORASP2 | physical | 25416956 | |
| NTAQ1_HUMAN | WDYHV1 | physical | 25416956 | |
| RD3_HUMAN | RD3 | physical | 25416956 | |
| EI2BE_HUMAN | EIF2B5 | physical | 26344197 | |
| THTM_HUMAN | MPST | physical | 26344197 | |
| SPB13_HUMAN | SERPINB13 | physical | 26344197 | |
| EI2BD_HUMAN | EIF2B4 | physical | 28514442 | |
| EI2BG_HUMAN | EIF2B3 | physical | 28514442 | |
| EI2BE_HUMAN | EIF2B5 | physical | 28514442 | |
| BZW2_HUMAN | BZW2 | physical | 27173435 | |
| MCU_HUMAN | MCU | physical | 27173435 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 603896 | Leukodystrophy with vanishing white matter (VWM) | |||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Acetylation | |
| Reference | PubMed |
| "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-35, AND MASS SPECTROMETRY. | |