| UniProt ID | HNRPM_RAT | |
|---|---|---|
| UniProt AC | Q62826 | |
| Protein Name | Heterogeneous nuclear ribonucleoprotein M | |
| Gene Name | Hnrnpm | |
| Organism | Rattus norvegicus (Rat). | |
| Sequence Length | 690 | |
| Subcellular Localization | Nucleus matrix . | |
| Protein Description | Pre-mRNA binding protein, binds avidly to poly(G) and poly(U) RNA homopolymers. Involved in splicing. Acts as a receptor for carcinoembryonic antigen in Kupffer cells, may initiate a series of signaling events leading to tyrosine phosphorylation of proteins and induction of IL-1 alpha, IL-6, IL-10 and tumor necrosis factor alpha cytokines.. | |
| Protein Sequence | MAAGVEAAAEVAATEPKMEEESGAPCVPSGNGAPVPKGEERPTQNEKRKEKNIKRGGNRFEPYANPTKRYRAFITNIPFDVKWQSLKDLVKEKVGEVTYVELLMDAEGKSRGCAVVEFKMEESMKKAAEVLNKHSLSGRPLKVKEDPDGEHARRAMQKAGRLGSTVFVANLDYKVGWKKLKEVFSMAGVVVRADILEDKDGKSRGIGTVTFEQSIEAVQAISMFNGQLLFDRPMHVKMDERALPKGDFFPPERPQQLPHGLGGIGMGLGPGGQPIDANHLNKGIGMGNLGPAGMGMEGIGFGINKIGGMEGPFGGGMENMGRFGSGMNMGRINEILSNALKRGEIIAKQGGSGAGGSVPGIERMGPGIDRISGAGMERMGAGLGHGMDRVGSEIERMGLVMDRMGSVERMGSGIERMGPLGLDHMASSIERMGQTMERIGSGVERMGAGMGFGLERMAAPIDRVGQTIERMGSGVERMGPAIERMGLSMDRMVPTGMGAGLERMGPVMDRMATGLERMGANNLERMGLERMGANSLERMGLERMGANSLERMGPAMGPALGAGIERMGLAMGGAGGASFDRTIEMERGNFGGSFAGSFGGAGGHAPGVARKACQIFVRNLPFDFTWKMLKDKFNECGHVLYADIKMENGKSKGCGVVKFESPEVAERACRMMNGMKLSGREIDVRIDRNA | |
| 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 | ------MAAGVEAAA ------CCCHHHHHH | 16.96 | - | |
| 29 | Phosphorylation | SGAPCVPSGNGAPVP CCCCCCCCCCCCCCC | 25.21 | - | |
| 85 | Phosphorylation | PFDVKWQSLKDLVKE CCCCCHHHHHHHHHH | 35.95 | 23984901 | |
| 133 | Acetylation | KAAEVLNKHSLSGRP HHHHHHHHCCCCCCC | 30.34 | - | |
| 137 | Phosphorylation | VLNKHSLSGRPLKVK HHHHCCCCCCCCCCC | 35.45 | 23984901 | |
| 144 | Succinylation | SGRPLKVKEDPDGEH CCCCCCCCCCCCHHH | 55.61 | 26843850 | |
| 164 | Phosphorylation | QKAGRLGSTVFVANL HHHCCCCCEEEEECC | 26.45 | 23984901 | |
| 165 | Phosphorylation | KAGRLGSTVFVANLD HHCCCCCEEEEECCC | 19.03 | 23984901 | |
| 199 | Succinylation | RADILEDKDGKSRGI EEEEEECCCCCCCCC | 60.03 | 26843850 | |
| 199 | Acetylation | RADILEDKDGKSRGI EEEEEECCCCCCCCC | 60.03 | 22902405 | |
| 237 | Acetylation | FDRPMHVKMDERALP ECCCEECCCCCCCCC | 26.42 | - | |
| 238 | Acetylation | DRPMHVKMDERALPK CCCEECCCCCCCCCC | 6.69 | - | |
| 325 | Phosphorylation | ENMGRFGSGMNMGRI CCCCCCCCCCCHHHH | 31.96 | 23984901 | |
| 337 | Phosphorylation | GRINEILSNALKRGE HHHHHHHHHHHHHCC | 26.22 | 23984901 | |
| 357 | Phosphorylation | GGSGAGGSVPGIERM CCCCCCCCCCCHHHC | 24.99 | - | |
| 372 | Phosphorylation | GPGIDRISGAGMERM CCCCCCCCCCCHHHH | 24.39 | 23984901 | |
| 387 | Ubiquitination | GAGLGHGMDRVGSEI CCCCCCCHHHCCHHH | 2.17 | - | |
| 392 | Phosphorylation | HGMDRVGSEIERMGL CCHHHCCHHHHHHCH | 32.32 | 29779826 | |
| 396 | Phosphorylation | RVGSEIERMGLVMDR HCCHHHHHHCHHHHC | 30.08 | - | |
| 406 | Phosphorylation | LVMDRMGSVERMGSG HHHHCCCCHHCCCCC | 16.09 | 21630457 | |
| 412 | Phosphorylation | GSVERMGSGIERMGP CCHHCCCCCHHHCCC | 27.53 | - | |
| 427 | Phosphorylation | LGLDHMASSIERMGQ CCHHHHHHHHHHHHH | 25.03 | 23984901 | |
| 428 | Phosphorylation | GLDHMASSIERMGQT CHHHHHHHHHHHHHH | 20.94 | 27097102 | |
| 431 | Phosphorylation | HMASSIERMGQTMER HHHHHHHHHHHHHHH | 32.63 | - | |
| 441 | Phosphorylation | QTMERIGSGVERMGA HHHHHHHCCHHHCCC | 36.98 | 29779826 | |
| 445 | Phosphorylation | RIGSGVERMGAGMGF HHHCCHHHCCCCCCC | 26.82 | - | |
| 456 | Methylation | GMGFGLERMAAPIDR CCCCCHHHCCCCHHH | 25.69 | - | |
| 467 | Phosphorylation | PIDRVGQTIERMGSG CHHHHHHHHHHHCCC | 20.90 | 23984901 | |
| 473 | Phosphorylation | QTIERMGSGVERMGP HHHHHHCCCHHHHHH | 30.26 | 28432305 | |
| 480 | Phosphorylation | SGVERMGPAIERMGL CCHHHHHHHHHHCCC | 22.26 | - | |
| 488 | Phosphorylation | AIERMGLSMDRMVPT HHHHCCCCCCCCCCC | 16.95 | 28432305 | |
| 495 | Methylation | SMDRMVPTGMGAGLE CCCCCCCCCCCCCHH | 28.52 | - | |
| 527 | Phosphorylation | ANNLERMGLERMGAN HHHHHHHCHHHCCCH | 30.52 | - | |
| 535 | Phosphorylation | LERMGANSLERMGLE HHHCCCHHHHHHCHH | 30.95 | 21738781 | |
| 548 | Phosphorylation | LERMGANSLERMGPA HHHCCCCHHHHHCCH | 30.95 | 21738781 | |
| 574 | Phosphorylation | MGLAMGGAGGASFDR HCCCCCCCCCCCCCC | 13.91 | - | |
| 578 | Phosphorylation | MGGAGGASFDRTIEM CCCCCCCCCCCEEEE | 30.84 | 27097102 | |
| 587 | Phosphorylation | DRTIEMERGNFGGSF CCEEEECCCCCCCCC | 44.00 | - | |
| 593 | Phosphorylation | ERGNFGGSFAGSFGG CCCCCCCCCCCCCCC | 16.59 | 27097102 | |
| 597 | Phosphorylation | FGGSFAGSFGGAGGH CCCCCCCCCCCCCCC | 19.79 | 27097102 | |
| 625 | Phosphorylation | RNLPFDFTWKMLKDK HCCCCCCHHHHHHHH | 26.48 | 23984901 | |
| 632 | Acetylation | TWKMLKDKFNECGHV HHHHHHHHHHCCCCE | 48.80 | - | |
| 658 | Acetylation | SKGCGVVKFESPEVA CCCCEEEEECCHHHH | 40.79 | 25786129 | |
| 661 | Phosphorylation | CGVVKFESPEVAERA CEEEEECCHHHHHHH | 29.50 | 27097102 | |
| 697 | Acetylation | A-------------- C-------------- | - | ||
| 700 | Phosphorylation | ----------------- ----------------- | - |
| 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 HNRPM_RAT !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HNRPM_RAT !! | ||||||
* 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 HNRPM_RAT !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| CEAM5_HUMAN | CEACAM5 | physical | 11406629 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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