| UniProt ID | RINI_MOUSE | |
|---|---|---|
| UniProt AC | Q91VI7 | |
| Protein Name | Ribonuclease inhibitor | |
| Gene Name | Rnh1 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 456 | |
| Subcellular Localization | Cytoplasm. | |
| Protein Description | Ribonuclease inhibitor which inhibits RNASE1, RNASE2 and ANG. May play a role in redox homeostasis (By similarity).. | |
| Protein Sequence | MSLDIQCEQLSDARWTELLPLIQQYEVVRLDDCGLTEVRCKDISSAVQANPALTELSLRTNELGDGGVGLVLQGLQNPTCKIQKLSLQNCGLTEAGCGILPGMLRSLSTLRELHLNDNPMGDAGLKLLCEGLQDPQCRLEKLQLEYCNLTATSCEPLASVLRVKADFKELVLSNNDLHEPGVRILCQGLKDSACQLESLKLENCGITAANCKDLCDVVASKASLQELDLSSNKLGNAGIAALCPGLLLPSCKLRTLWLWECDITAEGCKDLCRVLRAKQSLKELSLASNELKDEGARLLCESLLEPGCQLESLWIKTCSLTAASCPYFCSVLTKSRSLLELQMSSNPLGDEGVQELCKALSQPDTVLRELWLGDCDVTNSGCSSLANVLLANRSLRELDLSNNCMGGPGVLQLLESLKQPSCTLQQLVLYDIYWTNEVEEQLRALEEERPSLRIIS | |
| 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 | -------MSLDIQCE -------CCCCCCCC | 8.95 | - | |
| 2 | Phosphorylation | ------MSLDIQCEQ ------CCCCCCCCC | 34.45 | 26824392 | |
| 11 | Phosphorylation | DIQCEQLSDARWTEL CCCCCCCCCCCHHHH | 28.99 | 25619855 | |
| 25 | Phosphorylation | LLPLIQQYEVVRLDD HHHHHHHCEEEEECC | 8.36 | 25367039 | |
| 33 | S-nitrosocysteine | EVVRLDDCGLTEVRC EEEEECCCCCEEEEE | 4.86 | - | |
| 33 | S-palmitoylation | EVVRLDDCGLTEVRC EEEEECCCCCEEEEE | 4.86 | 28526873 | |
| 33 | S-nitrosylation | EVVRLDDCGLTEVRC EEEEECCCCCEEEEE | 4.86 | 21278135 | |
| 40 | Glutathionylation | CGLTEVRCKDISSAV CCCEEEEECCHHHHH | 5.84 | 24333276 | |
| 41 | Ubiquitination | GLTEVRCKDISSAVQ CCEEEEECCHHHHHH | 47.75 | 22790023 | |
| 57 | Phosphorylation | NPALTELSLRTNELG CHHHHEEEEECCCCC | 15.01 | 25159016 | |
| 80 | S-nitrosocysteine | QGLQNPTCKIQKLSL ECCCCCCCEEEEHHC | 3.74 | - | |
| 80 | S-palmitoylation | QGLQNPTCKIQKLSL ECCCCCCCEEEEHHC | 3.74 | 28526873 | |
| 80 | S-nitrosylation | QGLQNPTCKIQKLSL ECCCCCCCEEEEHHC | 3.74 | 19483679 | |
| 80 | Glutathionylation | QGLQNPTCKIQKLSL ECCCCCCCEEEEHHC | 3.74 | 24333276 | |
| 81 | Ubiquitination | GLQNPTCKIQKLSLQ CCCCCCCEEEEHHCC | 51.12 | 22790023 | |
| 84 | Ubiquitination | NPTCKIQKLSLQNCG CCCCEEEEHHCCCCC | 43.44 | 22790023 | |
| 86 | Phosphorylation | TCKIQKLSLQNCGLT CCEEEEHHCCCCCCC | 34.64 | - | |
| 90 | Glutathionylation | QKLSLQNCGLTEAGC EEHHCCCCCCCHHCC | 2.81 | 24333276 | |
| 90 | S-palmitoylation | QKLSLQNCGLTEAGC EEHHCCCCCCCHHCC | 2.81 | 28526873 | |
| 97 | Glutathionylation | CGLTEAGCGILPGML CCCCHHCCCCHHHHH | 3.85 | 24333276 | |
| 97 | S-palmitoylation | CGLTEAGCGILPGML CCCCHHCCCCHHHHH | 3.85 | 28526873 | |
| 106 | Phosphorylation | ILPGMLRSLSTLREL CHHHHHHHHHHHHHH | 23.78 | 26060331 | |
| 108 | Phosphorylation | PGMLRSLSTLRELHL HHHHHHHHHHHHHHC | 27.00 | 23608596 | |
| 109 | Phosphorylation | GMLRSLSTLRELHLN HHHHHHHHHHHHHCC | 34.82 | 26060331 | |
| 129 | S-palmitoylation | DAGLKLLCEGLQDPQ HHHHHHHHHHCCCCC | 5.89 | 28526873 | |
| 137 | Glutathionylation | EGLQDPQCRLEKLQL HHCCCCCHHHHHHHH | 6.97 | 24333276 | |
| 137 | S-palmitoylation | EGLQDPQCRLEKLQL HHCCCCCHHHHHHHH | 6.97 | 28526873 | |
| 146 | Phosphorylation | LEKLQLEYCNLTATS HHHHHHHCCCCCCCC | 8.67 | 25367039 | |
| 147 | Glutathionylation | EKLQLEYCNLTATSC HHHHHHCCCCCCCCC | 2.16 | 24333276 | |
| 150 | Phosphorylation | QLEYCNLTATSCEPL HHHCCCCCCCCCCCH | 17.56 | 25367039 | |
| 152 | Phosphorylation | EYCNLTATSCEPLAS HCCCCCCCCCCCHHH | 28.77 | 25367039 | |
| 154 | Glutathionylation | CNLTATSCEPLASVL CCCCCCCCCCHHHHH | 5.62 | 24333276 | |
| 168 | Acetylation | LRVKADFKELVLSNN HHHCCCHHHHHHCCC | 51.16 | 22826441 | |
| 173 | Phosphorylation | DFKELVLSNNDLHEP CHHHHHHCCCCCCCC | 26.55 | 22817900 | |
| 190 | Acetylation | RILCQGLKDSACQLE HHHHCCCCCCCHHHC | 57.36 | 22826441 | |
| 194 | S-palmitoylation | QGLKDSACQLESLKL CCCCCCCHHHCCCCC | 5.70 | 28526873 | |
| 200 | Acetylation | ACQLESLKLENCGIT CHHHCCCCCCCCCCC | 64.13 | 22826441 | |
| 200 | Ubiquitination | ACQLESLKLENCGIT CHHHCCCCCCCCCCC | 64.13 | 22790023 | |
| 204 | S-palmitoylation | ESLKLENCGITAANC CCCCCCCCCCCCCCH | 2.81 | 28526873 | |
| 211 | S-palmitoylation | CGITAANCKDLCDVV CCCCCCCHHHHHHHH | 2.88 | 28526873 | |
| 215 | S-palmitoylation | AANCKDLCDVVASKA CCCHHHHHHHHHHHH | 5.53 | 28526873 | |
| 221 | Ubiquitination | LCDVVASKASLQELD HHHHHHHHHHHHHHC | 32.05 | 22790023 | |
| 223 | Phosphorylation | DVVASKASLQELDLS HHHHHHHHHHHHCCC | 34.03 | 29176673 | |
| 243 | Glutathionylation | NAGIAALCPGLLLPS HHHHHHHCCCCCCCC | 1.84 | 24333276 | |
| 243 | S-palmitoylation | NAGIAALCPGLLLPS HHHHHHHCCCCCCCC | 1.84 | 28526873 | |
| 251 | Glutathionylation | PGLLLPSCKLRTLWL CCCCCCCCCCCEEEE | 4.55 | 24333276 | |
| 251 | S-palmitoylation | PGLLLPSCKLRTLWL CCCCCCCCCCCEEEE | 4.55 | 28526873 | |
| 282 | Ubiquitination | LRAKQSLKELSLASN HHHHHHHHHHHHHCH | 62.95 | 22790023 | |
| 285 | Phosphorylation | KQSLKELSLASNELK HHHHHHHHHHCHHCH | 23.99 | 25195567 | |
| 288 | Phosphorylation | LKELSLASNELKDEG HHHHHHHCHHCHHHH | 35.81 | 25195567 | |
| 292 | Ubiquitination | SLASNELKDEGARLL HHHCHHCHHHHHHHH | 47.78 | 22790023 | |
| 292 | Acetylation | SLASNELKDEGARLL HHHCHHCHHHHHHHH | 47.78 | 23954790 | |
| 300 | Glutathionylation | DEGARLLCESLLEPG HHHHHHHHHHHCCCC | 3.85 | 24333276 | |
| 300 | S-palmitoylation | DEGARLLCESLLEPG HHHHHHHHHHHCCCC | 3.85 | 28526873 | |
| 308 | Glutathionylation | ESLLEPGCQLESLWI HHHCCCCCEEEEEEE | 6.46 | 24333276 | |
| 308 | S-palmitoylation | ESLLEPGCQLESLWI HHHCCCCCEEEEEEE | 6.46 | 28526873 | |
| 318 | S-palmitoylation | ESLWIKTCSLTAASC EEEEECCCCCHHHCC | 2.39 | 28526873 | |
| 325 | Glutathionylation | CSLTAASCPYFCSVL CCCHHHCCHHHHHHH | 2.44 | 24333276 | |
| 325 | S-palmitoylation | CSLTAASCPYFCSVL CCCHHHCCHHHHHHH | 2.44 | 28526873 | |
| 327 | Phosphorylation | LTAASCPYFCSVLTK CHHHCCHHHHHHHHC | 22.88 | 25367039 | |
| 329 | S-palmitoylation | AASCPYFCSVLTKSR HHCCHHHHHHHHCCC | 1.96 | 28526873 | |
| 335 | Phosphorylation | FCSVLTKSRSLLELQ HHHHHHCCCHHHHHH | 23.13 | 26643407 | |
| 337 | Phosphorylation | SVLTKSRSLLELQMS HHHHCCCHHHHHHHC | 44.38 | 26643407 | |
| 357 | S-palmitoylation | DEGVQELCKALSQPD HHHHHHHHHHHCCCC | 2.08 | 28526873 | |
| 357 | Glutathionylation | DEGVQELCKALSQPD HHHHHHHHHHHCCCC | 2.08 | 24333276 | |
| 361 | Phosphorylation | QELCKALSQPDTVLR HHHHHHHCCCCCHHH | 44.52 | 29176673 | |
| 375 | Glutathionylation | RELWLGDCDVTNSGC HHHHHCCCCCCCCHH | 4.26 | 24333276 | |
| 375 | S-palmitoylation | RELWLGDCDVTNSGC HHHHHCCCCCCCCHH | 4.26 | 28526873 | |
| 382 | S-palmitoylation | CDVTNSGCSSLANVL CCCCCCHHHHHHHHH | 2.21 | 28526873 | |
| 382 | Glutathionylation | CDVTNSGCSSLANVL CCCCCCHHHHHHHHH | 2.21 | 24333276 | |
| 404 | Glutathionylation | ELDLSNNCMGGPGVL CCCCCCCCCCCHHHH | 2.91 | 24333276 | |
| 404 | S-nitrosocysteine | ELDLSNNCMGGPGVL CCCCCCCCCCCHHHH | 2.91 | - | |
| 404 | S-nitrosylation | ELDLSNNCMGGPGVL CCCCCCCCCCCHHHH | 2.91 | 19483679 | |
| 404 | S-palmitoylation | ELDLSNNCMGGPGVL CCCCCCCCCCCHHHH | 2.91 | 28526873 | |
| 418 | Acetylation | LQLLESLKQPSCTLQ HHHHHHCCCCCCCHH | 70.24 | 23864654 | |
| 451 | Phosphorylation | ALEEERPSLRIIS-- HHHHHCCCCEECC-- | 36.18 | 26824392 |
| 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 RINI_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RINI_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 RINI_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of RINI_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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