| UniProt ID | NEP1_HUMAN | |
|---|---|---|
| UniProt AC | Q92979 | |
| Protein Name | Ribosomal RNA small subunit methyltransferase NEP1 {ECO:0000305|PubMed:20047967} | |
| Gene Name | EMG1 {ECO:0000303|PubMed:19463982} | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 244 | |
| Subcellular Localization | Nucleus, nucleolus . | |
| Protein Description | S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates pseudouridine at position 1248 (Psi1248) in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Is not able to methylate uridine at this position. [PubMed: 20047967 Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes (By similarity] | |
| Protein Sequence | MAAPSDGFKPRERSGGEQAQDWDALPPKRPRLGAGNKIGGRRLIVVLEGASLETVKVGKTYELLNCDKHKSILLKNGRDPGEARPDITHQSLLMLMDSPLNRAGLLQVYIHTQKNVLIEVNPQTRIPRTFDRFCGLMVQLLHKLSVRAADGPQKLLKVIKNPVSDHFPVGCMKVGTSFSIPVVSDVRELVPSSDPIVFVVGAFAHGKVSVEYTEKMVSISNYPLSAALTCAKLTTAFEEVWGVI | |
| 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 | Acetylation | ------MAAPSDGFK ------CCCCCCCCC | 28.25 | 22814378 | |
| 5 | Phosphorylation | ---MAAPSDGFKPRE ---CCCCCCCCCCCC | 45.71 | 29255136 | |
| 9 | Acetylation | AAPSDGFKPRERSGG CCCCCCCCCCCCCCC | 49.01 | 23954790 | |
| 9 | Ubiquitination | AAPSDGFKPRERSGG CCCCCCCCCCCCCCC | 49.01 | 24816145 | |
| 14 | Phosphorylation | GFKPRERSGGEQAQD CCCCCCCCCCCCCCC | 46.53 | 25159151 | |
| 28 | Acetylation | DWDALPPKRPRLGAG CCCCCCCCCCCCCCC | 73.43 | 26051181 | |
| 28 | Ubiquitination | DWDALPPKRPRLGAG CCCCCCCCCCCCCCC | 73.43 | 29967540 | |
| 37 | Acetylation | PRLGAGNKIGGRRLI CCCCCCCCCCCEEEE | 41.64 | 25953088 | |
| 37 | Ubiquitination | PRLGAGNKIGGRRLI CCCCCCCCCCCEEEE | 41.64 | 24816145 | |
| 51 | Phosphorylation | IVVLEGASLETVKVG EEEEECCCEEEEECC | 37.28 | 20068231 | |
| 54 | Phosphorylation | LEGASLETVKVGKTY EECCCEEEEECCCEE | 30.81 | 20068231 | |
| 56 | Ubiquitination | GASLETVKVGKTYEL CCCEEEEECCCEEEE | 53.33 | 23000965 | |
| 59 | Ubiquitination | LETVKVGKTYELLNC EEEEECCCEEEEECC | 51.42 | 23000965 | |
| 59 | 2-Hydroxyisobutyrylation | LETVKVGKTYELLNC EEEEECCCEEEEECC | 51.42 | - | |
| 59 | Acetylation | LETVKVGKTYELLNC EEEEECCCEEEEECC | 51.42 | 23954790 | |
| 60 | Phosphorylation | ETVKVGKTYELLNCD EEEECCCEEEEECCC | 19.12 | 21815630 | |
| 61 | Phosphorylation | TVKVGKTYELLNCDK EEECCCEEEEECCCC | 14.20 | 28152594 | |
| 68 | Ubiquitination | YELLNCDKHKSILLK EEEECCCCCCEEEEE | 55.95 | 29967540 | |
| 68 | Acetylation | YELLNCDKHKSILLK EEEECCCCCCEEEEE | 55.95 | 23749302 | |
| 70 | Acetylation | LLNCDKHKSILLKNG EECCCCCCEEEEECC | 44.95 | 26051181 | |
| 70 | Ubiquitination | LLNCDKHKSILLKNG EECCCCCCEEEEECC | 44.95 | 29967540 | |
| 75 | Acetylation | KHKSILLKNGRDPGE CCCEEEEECCCCCCC | 54.64 | 25953088 | |
| 75 | Ubiquitination | KHKSILLKNGRDPGE CCCEEEEECCCCCCC | 54.64 | 21890473 | |
| 91 | Phosphorylation | RPDITHQSLLMLMDS CCCCCHHHHHHHHCC | 18.83 | - | |
| 154 | Ubiquitination | RAADGPQKLLKVIKN HCCCCHHHHHHHHCC | 59.94 | 23000965 | |
| 154 | Acetylation | RAADGPQKLLKVIKN HCCCCHHHHHHHHCC | 59.94 | 25953088 | |
| 157 | Ubiquitination | DGPQKLLKVIKNPVS CCHHHHHHHHCCCCC | 52.96 | 23000965 | |
| 157 | Acetylation | DGPQKLLKVIKNPVS CCHHHHHHHHCCCCC | 52.96 | 26051181 | |
| 160 | Acetylation | QKLLKVIKNPVSDHF HHHHHHHCCCCCCCC | 59.18 | 26051181 | |
| 160 | Ubiquitination | QKLLKVIKNPVSDHF HHHHHHHCCCCCCCC | 59.18 | 23000965 | |
| 176 | Phosphorylation | VGCMKVGTSFSIPVV CCCEEECCCEEEEEE | 29.59 | 23186163 | |
| 177 | Phosphorylation | GCMKVGTSFSIPVVS CCEEECCCEEEEEEC | 15.86 | 23186163 | |
| 179 | Phosphorylation | MKVGTSFSIPVVSDV EEECCCEEEEEECCH | 26.25 | 23186163 | |
| 218 | Phosphorylation | EYTEKMVSISNYPLS EEEEEEEECCCCCHH | 19.46 | 28152594 | |
| 220 | Phosphorylation | TEKMVSISNYPLSAA EEEEEECCCCCHHHH | 23.86 | 28442448 | |
| 222 | Phosphorylation | KMVSISNYPLSAALT EEEECCCCCHHHHHH | 9.96 | 28152594 | |
| 225 | Phosphorylation | SISNYPLSAALTCAK ECCCCCHHHHHHHHH | 13.64 | 28442448 | |
| 229 | Phosphorylation | YPLSAALTCAKLTTA CCHHHHHHHHHHHHH | 12.99 | 28442448 | |
| 234 | Phosphorylation | ALTCAKLTTAFEEVW HHHHHHHHHHHHHHH | 18.51 | 28122231 | |
| 235 | Phosphorylation | LTCAKLTTAFEEVWG HHHHHHHHHHHHHHC | 39.52 | 28122231 |
| 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 NEP1_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NEP1_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 NEP1_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| S2538_HUMAN | SLC25A38 | physical | 16169070 | |
| KHDR1_HUMAN | KHDRBS1 | physical | 16169070 | |
| A4_HUMAN | APP | physical | 21832049 | |
| IL7RA_HUMAN | IL7R | physical | 23151878 |
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| 211180 | Bowen-Conradi syndrome (BWCNS) | |||||
| 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 |
| "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-5 AND SER-14, AND MASSSPECTROMETRY. | |