| UniProt ID | ERIC1_HUMAN | |
|---|---|---|
| UniProt AC | Q86X53 | |
| Protein Name | Glutamate-rich protein 1 | |
| Gene Name | ERICH1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 443 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MAAHRKHVFVEKVLQRLFPPVPSGQGKREPQTLAVQNPPKKVTSEKVSQKHAEPLTDTGSETPTARRLYTASGPPEGYVPCWPEPSSCGSPENASSGDDTEDQDPHDQPKRRRIRKHKSKKKFKNPNNVLIEQAELEKQQSLLQEKSQRQHTDGTTISKNKKRKLKKKQQIKRKKAAGLAAKAAGVSFMYQPEDSSNEGEGVGEACEEDGVDTSEEDPTLAGEEDVKDTREEDGADASEEDLTRARQEEGADASEEDPTPAGEEDVKDAREEDGVDTIEEDLTRAGEEDGKDTREEDGADASEEDPTWAGEEEGADSGEEDGADASEEDDTITNEKAHSILNFLKSTQEMYFYDGVSRDAASAALADAAEELLDRLASHSMLPSDVSILYHMKTLLLLQDTERLKHALEMFPEHCTMPPDHARVISAFFSYWITHILPEKSSD | |
| 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 |
|---|---|---|---|---|---|
| 12 | Acetylation | RKHVFVEKVLQRLFP HCHHHHHHHHHHHCC | 42.83 | 19608861 | |
| 23 | Phosphorylation | RLFPPVPSGQGKREP HHCCCCCCCCCCCCC | 43.94 | - | |
| 50 | Acetylation | TSEKVSQKHAEPLTD CCHHHHHHHCCCCCC | 36.96 | 25953088 | |
| 56 | Phosphorylation | QKHAEPLTDTGSETP HHHCCCCCCCCCCCC | 42.08 | 21712546 | |
| 58 | Phosphorylation | HAEPLTDTGSETPTA HCCCCCCCCCCCCCC | 37.05 | 29396449 | |
| 60 | Phosphorylation | EPLTDTGSETPTARR CCCCCCCCCCCCCCC | 40.15 | 30576142 | |
| 62 | Phosphorylation | LTDTGSETPTARRLY CCCCCCCCCCCCCCC | 27.86 | 29255136 | |
| 64 | Phosphorylation | DTGSETPTARRLYTA CCCCCCCCCCCCCCC | 39.97 | 29255136 | |
| 118 | Acetylation | RRRIRKHKSKKKFKN HHHHHHHHCCCCCCC | 67.99 | 20167786 | |
| 121 | Acetylation | IRKHKSKKKFKNPNN HHHHHCCCCCCCCCC | 71.22 | 20167786 | |
| 124 | Ubiquitination | HKSKKKFKNPNNVLI HHCCCCCCCCCCHHH | 79.12 | - | |
| 155 | Phosphorylation | QRQHTDGTTISKNKK HHHCCCCCCCCHHHH | 24.62 | - | |
| 158 | Phosphorylation | HTDGTTISKNKKRKL CCCCCCCCHHHHHHH | 28.25 | - | |
| 229 | Phosphorylation | GEEDVKDTREEDGAD CCCCCCCCCHHCCCC | 33.97 | 24247654 | |
| 238 | Phosphorylation | EEDGADASEEDLTRA HHCCCCCCHHHHHHH | 41.91 | 29255136 | |
| 243 | Phosphorylation | DASEEDLTRARQEEG CCCHHHHHHHHHHHC | 34.31 | 23927012 | |
| 254 | Phosphorylation | QEEGADASEEDPTPA HHHCCCCCCCCCCCC | 41.91 | 29255136 | |
| 259 | Phosphorylation | DASEEDPTPAGEEDV CCCCCCCCCCCHHHH | 37.78 | 29255136 | |
| 277 | Phosphorylation | REEDGVDTIEEDLTR HHHHCCCCHHHHHHH | 28.07 | 21815630 | |
| 283 | Phosphorylation | DTIEEDLTRAGEEDG CCHHHHHHHHCCCCC | 30.69 | 27732954 | |
| 302 | Phosphorylation | EEDGADASEEDPTWA HHCCCCCCCCCCCCC | 41.91 | 25137130 | |
| 317 | Phosphorylation | GEEEGADSGEEDGAD CCCCCCCCCCCCCCC | 47.79 | 25137130 | |
| 326 | Phosphorylation | EEDGADASEEDDTIT CCCCCCCCCCCCCCC | 41.91 | 25137130 | |
| 339 | Phosphorylation | ITNEKAHSILNFLKS CCHHHHHHHHHHHHH | 33.36 | 25159151 |
| 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 ERIC1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ERIC1_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 ERIC1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ERIC1_HUMAN !! | ||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| 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-12, 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-238 AND THR-277, ANDMASS SPECTROMETRY. | |
| "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-238, AND MASSSPECTROMETRY. | |
| "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-238, AND MASSSPECTROMETRY. | |