| UniProt ID | ELAV1_HUMAN | |
|---|---|---|
| UniProt AC | Q15717 | |
| Protein Name | ELAV-like protein 1 | |
| Gene Name | ELAVL1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 326 | |
| Subcellular Localization | Cytoplasm . Nucleus . Translocates into the cytoplasm following phosphorylation by MAPKAPK2 (PubMed:14517288). Likewise, phosphorylation by PRKCD promotes translocation from the nucleus into the cytoplasm, where it is associated with free and cytoske | |
| Protein Description | RNA-binding protein that binds to the 3'-UTR region of mRNAs and increases their stability. [PubMed: 14517288] | |
| Protein Sequence | MSNGYEDHMAEDCRGDIGRTNLIVNYLPQNMTQDELRSLFSSIGEVESAKLIRDKVAGHSLGYGFVNYVTAKDAERAINTLNGLRLQSKTIKVSYARPSSEVIKDANLYISGLPRTMTQKDVEDMFSRFGRIINSRVLVDQTTGLSRGVAFIRFDKRSEAEEAITSFNGHKPPGSSEPITVKFAANPNQNKNVALLSQLYHSPARRFGGPVHHQAQRFRFSPMGVDHMSGLSGVNVPGNASSGWCIFIYNLGQDADEGILWQMFGPFGAVTNVKVIRDFNTNKCKGFGFVTMTNYEEAAMAIASLNGYRLGDKILQVSFKTNKSHK | |
| 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 |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSNGYEDHM ------CCCCCHHHC | 38.67 | 23401153 | |
| 2 | Acetylation | ------MSNGYEDHM ------CCCCCHHHC | 38.67 | 21406692 | |
| 5 | Phosphorylation | ---MSNGYEDHMAED ---CCCCCHHHCCHH | 23.57 | 28450419 | |
| 14 | Methylation | DHMAEDCRGDIGRTN HHCCHHCCCCCCCHH | 59.13 | 115480023 | |
| 20 | Phosphorylation | CRGDIGRTNLIVNYL CCCCCCCHHHHHHCC | 29.21 | 21406692 | |
| 26 | Phosphorylation | RTNLIVNYLPQNMTQ CHHHHHHCCCCCCCH | 14.63 | 20090780 | |
| 27 (in isoform 2) | Phosphorylation | - | 2.72 | 25599653 | |
| 29 (in isoform 2) | Phosphorylation | - | 50.13 | 25599653 | |
| 32 | Phosphorylation | NYLPQNMTQDELRSL HCCCCCCCHHHHHHH | 40.18 | 21406692 | |
| 32 (in isoform 2) | Phosphorylation | - | 40.18 | 25599653 | |
| 38 | Phosphorylation | MTQDELRSLFSSIGE CCHHHHHHHHHHHHH | 46.52 | 21406692 | |
| 41 | Phosphorylation | DELRSLFSSIGEVES HHHHHHHHHHHHHHH | 26.75 | 21406692 | |
| 42 | Phosphorylation | ELRSLFSSIGEVESA HHHHHHHHHHHHHHH | 27.55 | 21406692 | |
| 48 | Phosphorylation | SSIGEVESAKLIRDK HHHHHHHHHHHHHHH | 35.56 | 21406692 | |
| 50 | Ubiquitination | IGEVESAKLIRDKVA HHHHHHHHHHHHHHH | 54.44 | 21890473 | |
| 50 | Acetylation | IGEVESAKLIRDKVA HHHHHHHHHHHHHHH | 54.44 | 25953088 | |
| 50 | Ubiquitination | IGEVESAKLIRDKVA HHHHHHHHHHHHHHH | 54.44 | 23000965 | |
| 55 | Ubiquitination | SAKLIRDKVAGHSLG HHHHHHHHHHCCCCC | 24.92 | 21890473 | |
| 55 | Acetylation | SAKLIRDKVAGHSLG HHHHHHHHHHCCCCC | 24.92 | 25953088 | |
| 55 | Ubiquitination | SAKLIRDKVAGHSLG HHHHHHHHHHCCCCC | 24.92 | 23000965 | |
| 60 | Phosphorylation | RDKVAGHSLGYGFVN HHHHHCCCCCCCCEE | 23.67 | 28152594 | |
| 63 | Phosphorylation | VAGHSLGYGFVNYVT HHCCCCCCCCEEEEE | 16.81 | 20090780 | |
| 68 | Phosphorylation | LGYGFVNYVTAKDAE CCCCCEEEEEHHHHH | 8.22 | 28152594 | |
| 70 | Phosphorylation | YGFVNYVTAKDAERA CCCEEEEEHHHHHHH | 20.03 | 28152594 | |
| 72 | Ubiquitination | FVNYVTAKDAERAIN CEEEEEHHHHHHHHH | 48.37 | 21890473 | |
| 72 | Acetylation | FVNYVTAKDAERAIN CEEEEEHHHHHHHHH | 48.37 | 25953088 | |
| 72 | Ubiquitination | FVNYVTAKDAERAIN CEEEEEHHHHHHHHH | 48.37 | 23000965 | |
| 80 | Phosphorylation | DAERAINTLNGLRLQ HHHHHHHHHCCCEEC | 18.58 | - | |
| 88 | Phosphorylation | LNGLRLQSKTIKVSY HCCCEECCEEEEEEE | 36.04 | 17317627 | |
| 89 | Ubiquitination | NGLRLQSKTIKVSYA CCCEECCEEEEEEEE | 41.11 | 29967540 | |
| 92 | Ubiquitination | RLQSKTIKVSYARPS EECCEEEEEEEECCC | 30.29 | 21906983 | |
| 92 | Ubiquitination | RLQSKTIKVSYARPS EECCEEEEEEEECCC | 30.29 | 21890473 | |
| 94 | Phosphorylation | QSKTIKVSYARPSSE CCEEEEEEEECCCCH | 14.20 | 28152594 | |
| 95 | Phosphorylation | SKTIKVSYARPSSEV CEEEEEEEECCCCHH | 15.04 | 28152594 | |
| 99 | Phosphorylation | KVSYARPSSEVIKDA EEEEECCCCHHHCCC | 33.31 | 28152594 | |
| 100 | Phosphorylation | VSYARPSSEVIKDAN EEEECCCCHHHCCCC | 38.27 | 25159151 | |
| 104 | Acetylation | RPSSEVIKDANLYIS CCCCHHHCCCCEEEC | 56.83 | 26051181 | |
| 104 | Ubiquitination | RPSSEVIKDANLYIS CCCCHHHCCCCEEEC | 56.83 | 21890473 | |
| 104 | Ubiquitination | RPSSEVIKDANLYIS CCCCHHHCCCCEEEC | 56.83 | 23000965 | |
| 109 | Phosphorylation | VIKDANLYISGLPRT HHCCCCEEECCCCCC | 7.89 | 20090780 | |
| 111 | Phosphorylation | KDANLYISGLPRTMT CCCCEEECCCCCCCC | 22.26 | 28152594 | |
| 118 | Phosphorylation | SGLPRTMTQKDVEDM CCCCCCCCHHHHHHH | 31.67 | 19528229 | |
| 120 | Ubiquitination | LPRTMTQKDVEDMFS CCCCCCHHHHHHHHH | 55.35 | 23000965 | |
| 120 | Ubiquitination | LPRTMTQKDVEDMFS CCCCCCHHHHHHHHH | 55.35 | 21890473 | |
| 120 | Acetylation | LPRTMTQKDVEDMFS CCCCCCHHHHHHHHH | 55.35 | 26051181 | |
| 125 | Sulfoxidation | TQKDVEDMFSRFGRI CHHHHHHHHHHHHHH | 1.76 | 30846556 | |
| 142 | Phosphorylation | SRVLVDQTTGLSRGV CEEEEECCCCCCCCE | 20.54 | 20068231 | |
| 143 | Phosphorylation | RVLVDQTTGLSRGVA EEEEECCCCCCCCEE | 30.41 | - | |
| 146 | Phosphorylation | VDQTTGLSRGVAFIR EECCCCCCCCEEEEE | 28.47 | - | |
| 147 | Methylation | DQTTGLSRGVAFIRF ECCCCCCCCEEEEEE | 48.96 | 82955081 | |
| 158 | Phosphorylation | FIRFDKRSEAEEAIT EEEEECCHHHHHHHH | 47.07 | 18285462 | |
| 171 | Ubiquitination | ITSFNGHKPPGSSEP HHHCCCCCCCCCCCC | 55.07 | 29967540 | |
| 171 | Acetylation | ITSFNGHKPPGSSEP HHHCCCCCCCCCCCC | 55.07 | 26051181 | |
| 182 | Ubiquitination | SSEPITVKFAANPNQ CCCCEEEEEECCCCC | 22.19 | 22817900 | |
| 182 | Acetylation | SSEPITVKFAANPNQ CCCCEEEEEECCCCC | 22.19 | 25953088 | |
| 191 | Ubiquitination | AANPNQNKNVALLSQ ECCCCCCCCHHHHHH | 42.93 | 23000965 | |
| 191 | Ubiquitination | AANPNQNKNVALLSQ ECCCCCCCCHHHHHH | 42.93 | 21890473 | |
| 191 | Sumoylation | AANPNQNKNVALLSQ ECCCCCCCCHHHHHH | 42.93 | 28112733 | |
| 191 | Acetylation | AANPNQNKNVALLSQ ECCCCCCCCHHHHHH | 42.93 | 26051181 | |
| 197 | Phosphorylation | NKNVALLSQLYHSPA CCCHHHHHHHHCCHH | 20.99 | 21945579 | |
| 200 | Phosphorylation | VALLSQLYHSPARRF HHHHHHHHCCHHHHC | 7.82 | 23927012 | |
| 202 | Phosphorylation | LLSQLYHSPARRFGG HHHHHHCCHHHHCCC | 13.49 | 29255136 | |
| 205 | Methylation | QLYHSPARRFGGPVH HHHCCHHHHCCCCCC | 37.53 | 54556849 | |
| 206 | Methylation | LYHSPARRFGGPVHH HHCCHHHHCCCCCCH | 36.35 | 24381529 | |
| 209 | Ubiquitination | SPARRFGGPVHHQAQ CHHHHCCCCCCHHHH | 20.53 | - | |
| 217 | Dimethylation | PVHHQAQRFRFSPMG CCCHHHHCCCCCCCC | 27.94 | - | |
| 217 | Methylation | PVHHQAQRFRFSPMG CCCHHHHCCCCCCCC | 27.94 | 24129315 | |
| 219 | Dimethylation | HHQAQRFRFSPMGVD CHHHHCCCCCCCCCC | 33.07 | - | |
| 219 | Methylation | HHQAQRFRFSPMGVD CHHHHCCCCCCCCCC | 33.07 | 18967413 | |
| 221 | Phosphorylation | QAQRFRFSPMGVDHM HHHCCCCCCCCCCCC | 15.10 | 19528229 | |
| 242 | Phosphorylation | NVPGNASSGWCIFIY CCCCCCCCCEEEEEE | 33.62 | 22817900 | |
| 283 | Ubiquitination | IRDFNTNKCKGFGFV EEECCCCCCCCEEEE | 34.97 | 27667366 | |
| 283 | Neddylation | IRDFNTNKCKGFGFV EEECCCCCCCCEEEE | 34.97 | - | |
| 304 | Phosphorylation | EAAMAIASLNGYRLG HHHHHHHHHCCCCCC | 19.09 | - | |
| 313 | Neddylation | NGYRLGDKILQVSFK CCCCCCCEEEEEEEE | 43.44 | - | |
| 313 | Ubiquitination | NGYRLGDKILQVSFK CCCCCCCEEEEEEEE | 43.44 | 21890473 | |
| 313 | Acetylation | NGYRLGDKILQVSFK CCCCCCCEEEEEEEE | 43.44 | 25953088 | |
| 313 | Ubiquitination | NGYRLGDKILQVSFK CCCCCCCEEEEEEEE | 43.44 | 23000965 | |
| 318 | Phosphorylation | GDKILQVSFKTNKSH CCEEEEEEEECCCCC | 14.20 | 28112733 | |
| 320 | Methylation | KILQVSFKTNKSHK- EEEEEEEECCCCCC- | 43.62 | 132877 | |
| 320 | Malonylation | KILQVSFKTNKSHK- EEEEEEEECCCCCC- | 43.62 | 26320211 | |
| 320 | Acetylation | KILQVSFKTNKSHK- EEEEEEEECCCCCC- | 43.62 | 25953088 | |
| 320 | Ubiquitination | KILQVSFKTNKSHK- EEEEEEEECCCCCC- | 43.62 | 23000965 | |
| 320 | Ubiquitination | KILQVSFKTNKSHK- EEEEEEEECCCCCC- | 43.62 | 21890473 | |
| 323 | Ubiquitination | QVSFKTNKSHK---- EEEEECCCCCC---- | 60.20 | 23000965 | |
| 326 | Neddylation | FKTNKSHK------- EECCCCCC------- | 69.95 | - | |
| 326 | Ubiquitination | FKTNKSHK------- EECCCCCC------- | 69.95 | 23000965 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 63 | Y | Phosphorylation | Kinase | JAK3 | P52333 | PSP |
| 68 | Y | Phosphorylation | Kinase | JAK3 | P52333 | PSP |
| 88 | S | Phosphorylation | Kinase | P38A | Q16539 | PSP |
| 88 | S | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
| 100 | S | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
| 118 | T | Phosphorylation | Kinase | MAPK14 | Q16539 | GPS |
| 118 | T | Phosphorylation | Kinase | CHEK2 | O96017 | GPS |
| 158 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 200 | Y | Phosphorylation | Kinase | JAK3 | P52333 | PSP |
| 202 | S | Phosphorylation | Kinase | CDK1 | P06493 | PSP |
| 202 | S | Phosphorylation | Kinase | CDK6 | Q00534 | PSP |
| 202 | S | Phosphorylation | Kinase | CDK5 | Q00535 | PSP |
| 202 | S | Phosphorylation | Kinase | CDK2 | P24941 | PSP |
| 221 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 221 | S | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
| 304 | S | Phosphorylation | Kinase | CHUK | O15111 | GPS |
| 318 | S | Phosphorylation | Kinase | PRKCA | P17252 | GPS |
| 318 | S | Phosphorylation | Kinase | PRKCD | Q05655 | GPS |
| - | K | Ubiquitination | E3 ubiquitin ligase | BTRC | Q9Y297 | PMID:24658274 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 217 | R | Methylation |
| 12237300 |
* 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 ELAV1_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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| Methylation | |
| Reference | PubMed |
| "Lipopolysaccharide-induced methylation of HuR, an mRNA-stabilizingprotein, by CARM1. Coactivator-associated argininemethyltransferase."; Li H., Park S., Kilburn B., Jelinek M.A., Henschen-Edman A.,Aswad D.W., Stallcup M.R., Laird-Offringa I.A.; J. Biol. Chem. 277:44623-44630(2002). Cited for: METHYLATION AT ARG-217. | |
| 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-202, AND MASSSPECTROMETRY. | |
| "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-202, AND MASSSPECTROMETRY. | |
| "Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND MASSSPECTROMETRY. | |
| "Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND MASSSPECTROMETRY. | |
| "Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-202, AND MASSSPECTROMETRY. | |