| UniProt ID | NJMU_HUMAN | |
|---|---|---|
| UniProt AC | Q9HAS0 | |
| Protein Name | Protein Njmu-R1 | |
| Gene Name | C17orf75 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 396 | |
| Subcellular Localization | ||
| Protein Description | May have a role in spermatogenesis.. | |
| Protein Sequence | MLPSLQESMDGDEKELESSEEGGSAEERRLEPPSSSHYCLYSYRGSRLAQQRGDSEDGSPSGTNAETPSGDDFSLSLADTNLPSEVEPELRSFIAKRLSRGAVFEGLGNVASVELKIPGYRVGCYYCLFQNEKLLPETVTIDSERNPSEYVVCFLGGSEKGLELFRLELDKYIQGLKNNMNCEARGLESHIKSYLSSWFEDVVCPIQRVVLLFQEKLTFLLHAALSYTPVEVKESDEKTKRDINRFLSVASLQGLIHEGTMTSLCMAMTEEQHKSVVIDCSSSQPQFCNAGSNRFCEDWMQAFLNGAKGGNPFLFRQVLENFKLKAIQDTNNLKRFIRQAEMNHYALFKCYMFLKNCGSGDILLKIVKVEHEEMPEAKNVIAVLEEFMKEALDQSF | |
| 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 |
|---|---|---|---|---|---|
| 4 | Phosphorylation | ----MLPSLQESMDG ----CCCCHHHHCCC | 38.43 | 29978859 | |
| 8 | Phosphorylation | MLPSLQESMDGDEKE CCCCHHHHCCCCHHH | 14.82 | 25159151 | |
| 18 | Phosphorylation | GDEKELESSEEGGSA CCHHHHHCCCCCCCH | 56.53 | 23401153 | |
| 19 | Phosphorylation | DEKELESSEEGGSAE CHHHHHCCCCCCCHH | 30.23 | 30278072 | |
| 24 | Phosphorylation | ESSEEGGSAEERRLE HCCCCCCCHHHHCCC | 43.28 | 23927012 | |
| 42 | Phosphorylation | SSHYCLYSYRGSRLA CCCEEEEEECCCHHH | 8.73 | 24719451 | |
| 43 | Phosphorylation | SHYCLYSYRGSRLAQ CCEEEEEECCCHHHH | 12.87 | 22817900 | |
| 55 | Phosphorylation | LAQQRGDSEDGSPSG HHHHHCCCCCCCCCC | 40.17 | 30278072 | |
| 59 | Phosphorylation | RGDSEDGSPSGTNAE HCCCCCCCCCCCCCC | 28.37 | 26657352 | |
| 61 | Phosphorylation | DSEDGSPSGTNAETP CCCCCCCCCCCCCCC | 61.01 | 29523821 | |
| 63 | Phosphorylation | EDGSPSGTNAETPSG CCCCCCCCCCCCCCC | 35.28 | 30278072 | |
| 67 | Phosphorylation | PSGTNAETPSGDDFS CCCCCCCCCCCCCCE | 21.97 | 29116813 | |
| 69 | Phosphorylation | GTNAETPSGDDFSLS CCCCCCCCCCCCEEE | 63.37 | 29116813 | |
| 74 | Phosphorylation | TPSGDDFSLSLADTN CCCCCCCEEEECCCC | 24.84 | 29496963 | |
| 76 | Phosphorylation | SGDDFSLSLADTNLP CCCCCEEEECCCCCC | 21.95 | 28102081 | |
| 80 | Phosphorylation | FSLSLADTNLPSEVE CEEEECCCCCCCCCC | 32.80 | 28102081 | |
| 92 | Phosphorylation | EVEPELRSFIAKRLS CCCHHHHHHHHHHHH | 33.36 | 24719451 | |
| 99 | Phosphorylation | SFIAKRLSRGAVFEG HHHHHHHHCCCCEEC | 32.47 | 29514088 | |
| 138 | Phosphorylation | NEKLLPETVTIDSER CCCCCCCEEEECCCC | 22.47 | - | |
| 140 | Phosphorylation | KLLPETVTIDSERNP CCCCCEEEECCCCCH | 26.87 | - | |
| 148 | Phosphorylation | IDSERNPSEYVVCFL ECCCCCHHCEEEEEE | 45.14 | - | |
| 171 | Ubiquitination | LFRLELDKYIQGLKN HHHHHHHHHHHHHHH | 57.80 | - | |
| 171 | Acetylation | LFRLELDKYIQGLKN HHHHHHHHHHHHHHH | 57.80 | 20167786 | |
| 172 | Phosphorylation | FRLELDKYIQGLKNN HHHHHHHHHHHHHHC | 9.72 | 26074081 | |
| 177 | Ubiquitination | DKYIQGLKNNMNCEA HHHHHHHHHCCCHHH | 53.77 | 29967540 | |
| 177 | Acetylation | DKYIQGLKNNMNCEA HHHHHHHHHCCCHHH | 53.77 | 20167786 | |
| 218 | Phosphorylation | LLFQEKLTFLLHAAL HHHHHHHHHHHHHHH | 24.25 | 25072903 | |
| 226 | Phosphorylation | FLLHAALSYTPVEVK HHHHHHHCCCCEECC | 23.41 | 25072903 | |
| 227 | Phosphorylation | LLHAALSYTPVEVKE HHHHHHCCCCEECCC | 18.86 | 25072903 | |
| 228 | Phosphorylation | LHAALSYTPVEVKES HHHHHCCCCEECCCC | 19.92 | 25072903 | |
| 248 | Phosphorylation | RDINRFLSVASLQGL HHHHHHHHHHHHHHH | 16.96 | 24043423 | |
| 251 | Phosphorylation | NRFLSVASLQGLIHE HHHHHHHHHHHHHCH | 21.04 | 24043423 | |
| 260 | Phosphorylation | QGLIHEGTMTSLCMA HHHHCHHHHHHHHHH | 17.81 | 24043423 | |
| 262 | Phosphorylation | LIHEGTMTSLCMAMT HHCHHHHHHHHHHCC | 20.56 | 24043423 | |
| 263 | Phosphorylation | IHEGTMTSLCMAMTE HCHHHHHHHHHHCCH | 14.56 | 24043423 | |
| 269 | Phosphorylation | TSLCMAMTEEQHKSV HHHHHHCCHHHHCCE | 27.17 | 24043423 | |
| 275 | Phosphorylation | MTEEQHKSVVIDCSS CCHHHHCCEEEECCC | 21.35 | 30177828 | |
| 281 | Phosphorylation | KSVVIDCSSSQPQFC CCEEEECCCCCCCCC | 29.31 | 30177828 | |
| 282 | Phosphorylation | SVVIDCSSSQPQFCN CEEEECCCCCCCCCC | 39.05 | 30177828 | |
| 283 | Phosphorylation | VVIDCSSSQPQFCNA EEEECCCCCCCCCCC | 29.59 | 30177828 | |
| 325 | Ubiquitination | VLENFKLKAIQDTNN HHHHCCCEEEECCCH | 43.99 | 29967540 | |
| 330 | Phosphorylation | KLKAIQDTNNLKRFI CCEEEECCCHHHHHH | 15.05 | - | |
| 334 | 2-Hydroxyisobutyrylation | IQDTNNLKRFIRQAE EECCCHHHHHHHHHH | 47.59 | - | |
| 334 | Ubiquitination | IQDTNNLKRFIRQAE EECCCHHHHHHHHHH | 47.59 | 29967540 | |
| 365 | Ubiquitination | GSGDILLKIVKVEHE CCCCEEEEEEEECHH | 41.84 | 29967540 | |
| 378 | Ubiquitination | HEEMPEAKNVIAVLE HHHCHHHHHHHHHHH | 50.51 | 29967540 | |
| 395 | Phosphorylation | MKEALDQSF------ HHHHHHHCC------ | 32.37 | 28176443 |
| 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 NJMU_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of NJMU_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 NJMU_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| WDR11_HUMAN | WDR11 | physical | 26186194 | |
| F91A1_HUMAN | FAM91A1 | physical | 26186194 | |
| F91A1_HUMAN | FAM91A1 | physical | 28514442 | |
| WDR11_HUMAN | WDR11 | physical | 28514442 | |
| AIFM1_HUMAN | AIFM1 | physical | 28514442 |
| 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 |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-395, AND MASSSPECTROMETRY. | |