| UniProt ID | HNRPF_MOUSE | |
|---|---|---|
| UniProt AC | Q9Z2X1 | |
| Protein Name | Heterogeneous nuclear ribonucleoprotein F | |
| Gene Name | Hnrnpf | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 415 | |
| Subcellular Localization | Nucleus, nucleoplasm. | |
| Protein Description | Component of the heterogeneous nuclear ribonucleoprotein (hnRNP) complexes which provide the substrate for the processing events that pre-mRNAs undergo before becoming functional, translatable mRNAs in the cytoplasm. Plays a role in the regulation of alternative splicing events. Binds G-rich sequences in pre-mRNAs and keeps target RNA in an unfolded state (By similarity).. | |
| Protein Sequence | MMLGPEGGEGYVVKLRGLPWSCSIEDVQNFLSDCTIHDGVAGVHFIYTREGRQSGEAFVELESEDDVKLALKKDRESMGHRYIEVFKSHRTEMDWVLKHSGPNSADSANDGFVRLRGLPFGCTKEEIVQFFSGLEIVPNGITLPVDPEGKITGEAFVQFASQELAEKALGKHKERIGHRYIEVFKSSQEEVRSYSDPPLKFMSVQRPGPYDRPGTARRYIGIVKQAGLDRMRSGAYSAGYGGYEEYSGLSDGYGFTTDLFGRDLSYCLSGMYDHRYGDSEFTVQSTTGHCVHMRGLPYKATENDIYNFFSPLNPVRVHIEIGPDGRVTGEADVEFATHEEAVAAMSKDRANMQHRYIELFLNSTTGASNGAYSSQVMQGMGVSAAQATYSGLESQSVSGCYGAGYSGQNSMGGYD | |
| 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 |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MMLGPEGG -------CCCCCCCC | 4.52 | - | |
| 2 | Acetylation | ------MMLGPEGGE ------CCCCCCCCC | 6.27 | - | |
| 11 | Phosphorylation | GPEGGEGYVVKLRGL CCCCCCCEEEEECCC | 9.58 | 25293948 | |
| 14 | Acetylation | GGEGYVVKLRGLPWS CCCCEEEEECCCCCC | 23.56 | 22826441 | |
| 21 | Phosphorylation | KLRGLPWSCSIEDVQ EECCCCCCCCHHHHH | 8.96 | 26643407 | |
| 23 | Phosphorylation | RGLPWSCSIEDVQNF CCCCCCCCHHHHHHH | 24.40 | 26643407 | |
| 54 | Phosphorylation | YTREGRQSGEAFVEL EECCCCCCCEEEEEE | 36.92 | 30635358 | |
| 63 | Phosphorylation | EAFVELESEDDVKLA EEEEEECCHHHHHHH | 59.97 | 25619855 | |
| 77 | Phosphorylation | ALKKDRESMGHRYIE HHHHHHHHHCHHHHH | 30.84 | 23375375 | |
| 87 | Acetylation | HRYIEVFKSHRTEMD HHHHHHHHHCHHHCE | 50.99 | 23806337 | |
| 87 | Ubiquitination | HRYIEVFKSHRTEMD HHHHHHHHHCHHHCE | 50.99 | 22790023 | |
| 98 | Acetylation | TEMDWVLKHSGPNSA HHCEEHHHCCCCCCC | 26.55 | 23806337 | |
| 98 | Ubiquitination | TEMDWVLKHSGPNSA HHCEEHHHCCCCCCC | 26.55 | 22790023 | |
| 100 | Phosphorylation | MDWVLKHSGPNSADS CEEHHHCCCCCCCCC | 55.12 | 21082442 | |
| 104 | Phosphorylation | LKHSGPNSADSANDG HHCCCCCCCCCCCCC | 36.26 | 26824392 | |
| 107 | Phosphorylation | SGPNSADSANDGFVR CCCCCCCCCCCCCEE | 28.78 | 23684622 | |
| 123 | Phosphorylation | RGLPFGCTKEEIVQF CCCCCCCCHHHHHHH | 41.70 | 28059163 | |
| 142 | Phosphorylation | EIVPNGITLPVDPEG EECCCCEEEECCCCC | 26.80 | 28059163 | |
| 161 | Phosphorylation | EAFVQFASQELAEKA HHHHHHHCHHHHHHH | 26.02 | 22817900 | |
| 167 | Ubiquitination | ASQELAEKALGKHKE HCHHHHHHHHHHHHH | 43.22 | 22790023 | |
| 171 | Ubiquitination | LAEKALGKHKERIGH HHHHHHHHHHHHHCH | 52.97 | - | |
| 185 | Ubiquitination | HRYIEVFKSSQEEVR HHHHHHHHCCHHHHH | 55.14 | 22790023 | |
| 186 | Phosphorylation | RYIEVFKSSQEEVRS HHHHHHHCCHHHHHH | 26.28 | 25266776 | |
| 187 | Phosphorylation | YIEVFKSSQEEVRSY HHHHHHCCHHHHHHC | 42.05 | 26824392 | |
| 193 | Phosphorylation | SSQEEVRSYSDPPLK CCHHHHHHCCCCCCE | 33.88 | - | |
| 195 | Phosphorylation | QEEVRSYSDPPLKFM HHHHHHCCCCCCEEE | 44.91 | 27180971 | |
| 200 | Ubiquitination | SYSDPPLKFMSVQRP HCCCCCCEEEEECCC | 44.81 | 22790023 | |
| 200 | Acetylation | SYSDPPLKFMSVQRP HCCCCCCEEEEECCC | 44.81 | 23806337 | |
| 203 | Phosphorylation | DPPLKFMSVQRPGPY CCCCEEEEECCCCCC | 20.45 | 25367039 | |
| 210 | Phosphorylation | SVQRPGPYDRPGTAR EECCCCCCCCCCCHH | 30.42 | 25367039 | |
| 212 | Methylation | QRPGPYDRPGTARRY CCCCCCCCCCCHHHH | 26.21 | 54556611 | |
| 215 | Phosphorylation | GPYDRPGTARRYIGI CCCCCCCCHHHHHHH | 21.48 | 28066266 | |
| 219 | Phosphorylation | RPGTARRYIGIVKQA CCCCHHHHHHHHHHH | 9.65 | 29514104 | |
| 224 | Malonylation | RRYIGIVKQAGLDRM HHHHHHHHHHCHHHH | 32.29 | 26320211 | |
| 224 | Ubiquitination | RRYIGIVKQAGLDRM HHHHHHHHHHCHHHH | 32.29 | - | |
| 224 | Acetylation | RRYIGIVKQAGLDRM HHHHHHHHHHCHHHH | 32.29 | 22826441 | |
| 233 | Phosphorylation | AGLDRMRSGAYSAGY HCHHHHHCCCCCCCC | 20.59 | 27600695 | |
| 265 | Phosphorylation | DLFGRDLSYCLSGMY HHCCCCHHHHHHCCC | 20.35 | 25159016 | |
| 267 | Glutathionylation | FGRDLSYCLSGMYDH CCCCHHHHHHCCCCC | 1.88 | 24333276 | |
| 267 | S-nitrosylation | FGRDLSYCLSGMYDH CCCCHHHHHHCCCCC | 1.88 | 20925432 | |
| 267 | S-nitrosocysteine | FGRDLSYCLSGMYDH CCCCHHHHHHCCCCC | 1.88 | - | |
| 269 | Phosphorylation | RDLSYCLSGMYDHRY CCHHHHHHCCCCCCC | 20.25 | 25159016 | |
| 272 | Phosphorylation | SYCLSGMYDHRYGDS HHHHHCCCCCCCCCC | 16.48 | 25159016 | |
| 290 | S-nitrosocysteine | VQSTTGHCVHMRGLP EEECCCCEEEECCCC | 2.08 | - | |
| 290 | Glutathionylation | VQSTTGHCVHMRGLP EEECCCCEEEECCCC | 2.08 | 24333276 | |
| 290 | S-nitrosylation | VQSTTGHCVHMRGLP EEECCCCEEEECCCC | 2.08 | 20925432 | |
| 299 | Ubiquitination | HMRGLPYKATENDIY EECCCCCCCCCCCCH | 47.06 | 22790023 | |
| 301 | Phosphorylation | RGLPYKATENDIYNF CCCCCCCCCCCCHHC | 31.04 | 26239621 | |
| 306 | Phosphorylation | KATENDIYNFFSPLN CCCCCCCHHCCCCCC | 14.58 | 26239621 | |
| 310 | Phosphorylation | NDIYNFFSPLNPVRV CCCHHCCCCCCCEEE | 25.08 | 24925903 |
| 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 HNRPF_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HNRPF_MOUSE !! | ||||||
* 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 HNRPF_MOUSE !! | ||||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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