| UniProt ID | ZN363_HUMAN | |
|---|---|---|
| UniProt AC | Q96PM5 | |
| Protein Name | RING finger and CHY zinc finger domain-containing protein 1 | |
| Gene Name | RCHY1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 261 | |
| Subcellular Localization | Nucleus. Nucleus speckle. Cytoplasm. | |
| Protein Description | Mediates E3-dependent ubiquitination and proteasomal degradation of target proteins, including p53/TP53, P73, HDAC1 and CDKN1B. Preferentially acts on tetrameric p53/TP53. Monoubiquitinates the translesion DNA polymerase POLH. Contributes to the regulation of the cell cycle progression. Increases AR transcription factor activity.. | |
| Protein Sequence | MAATAREDGASGQERGQRGCEHYDRGCLLKAPCCDKLYTCRLCHDNNEDHQLDRFKVKEVQCINCEKIQHAQQTCEECSTLFGEYYCDICHLFDKDKKQYHCENCGICRIGPKEDFFHCLKCNLCLAMNLQGRHKCIENVSRQNCPICLEDIHTSRVVAHVLPCGHLLHRTCYEEMLKEGYRCPLCMHSALDMTRYWRQLDDEVAQTPMPSEYQNMTVDILCNDCNGRSTVQFHILGMKCKICESYNTAQAGGRRISLDQQ | |
| 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 |
|---|---|---|---|---|---|
| 30 | Ubiquitination | YDRGCLLKAPCCDKL CCCCEEEECCCCCEE | 37.02 | - | |
| 36 | Ubiquitination | LKAPCCDKLYTCRLC EECCCCCEEEEEEEC | 29.49 | 29967540 | |
| 58 | Sumoylation | QLDRFKVKEVQCINC CCCCCEECEEEEECH | 53.40 | - | |
| 58 | Ubiquitination | QLDRFKVKEVQCINC CCCCCEECEEEEECH | 53.40 | 29967540 | |
| 58 | Sumoylation | QLDRFKVKEVQCINC CCCCCEECEEEEECH | 53.40 | - | |
| 95 | Ubiquitination | DICHLFDKDKKQYHC HHHHHCCCCCCCEEC | 65.20 | - | |
| 112 | Ubiquitination | CGICRIGPKEDFFHC CCCCEECCCHHHHHH | 34.20 | 22817900 | |
| 114 | Ubiquitination | ICRIGPKEDFFHCLK CCEECCCHHHHHHHH | 64.28 | 21963094 | |
| 130 | Phosphorylation | NLCLAMNLQGRHKCI HHHHHCCCCCHHHHH | 3.52 | 33259812 | |
| 135 | Ubiquitination | MNLQGRHKCIENVSR CCCCCHHHHHHCCHH | 35.23 | - | |
| 154 | Phosphorylation | ICLEDIHTSRVVAHV CCCHHHCHHHHHHHH | 20.68 | 17568776 | |
| 155 | Phosphorylation | CLEDIHTSRVVAHVL CCHHHCHHHHHHHHC | 14.65 | 17568776 | |
| 156 | Ubiquitination | LEDIHTSRVVAHVLP CHHHCHHHHHHHHCC | 28.25 | - | |
| 171 | Phosphorylation | CGHLLHRTCYEEMLK CCHHHHHHHHHHHHH | 14.53 | - | |
| 173 | Phosphorylation | HLLHRTCYEEMLKEG HHHHHHHHHHHHHCC | 17.82 | - | |
| 178 | Ubiquitination | TCYEEMLKEGYRCPL HHHHHHHHCCCCCCC | 48.02 | - | |
| 181 | Phosphorylation | EEMLKEGYRCPLCMH HHHHHCCCCCCCHHH | 15.33 | - | |
| 189 | Phosphorylation | RCPLCMHSALDMTRY CCCCHHHHHHHHHHH | 12.02 | 27251275 | |
| 190 | Ubiquitination | CPLCMHSALDMTRYW CCCHHHHHHHHHHHH | 7.91 | 22817900 | |
| 192 | Ubiquitination | LCMHSALDMTRYWRQ CHHHHHHHHHHHHHH | 35.80 | - | |
| 192 | Ubiquitination | LCMHSALDMTRYWRQ CHHHHHHHHHHHHHH | 35.80 | 21963094 | |
| 199 | Ubiquitination | DMTRYWRQLDDEVAQ HHHHHHHHCCHHHHC | 34.79 | 22817900 | |
| 201 | Ubiquitination | TRYWRQLDDEVAQTP HHHHHHCCHHHHCCC | 41.51 | 21963094 | |
| 208 | Phosphorylation | DDEVAQTPMPSEYQN CHHHHCCCCCHHHCC | 22.17 | 33259812 | |
| 211 | Phosphorylation | VAQTPMPSEYQNMTV HHCCCCCHHHCCCEE | 42.56 | - | |
| 217 | Ubiquitination | PSEYQNMTVDILCND CHHHCCCEEEEEEEC | 23.68 | 22817900 | |
| 217 | Phosphorylation | PSEYQNMTVDILCND CHHHCCCEEEEEEEC | 23.68 | 33259812 | |
| 219 | Ubiquitination | EYQNMTVDILCNDCN HHCCCEEEEEEECCC | 20.98 | 21963094 | |
| 230 | Ubiquitination | NDCNGRSTVQFHILG ECCCCCCEEEEEEEC | 19.57 | 22817900 | |
| 232 | Ubiquitination | CNGRSTVQFHILGMK CCCCCEEEEEEECCE | 25.04 | 21963094 | |
| 235 | Phosphorylation | RSTVQFHILGMKCKI CCEEEEEEECCEEEE | 3.62 | 33259812 | |
| 239 | Ubiquitination | QFHILGMKCKICESY EEEEECCEEEECCCC | 30.49 | 22817900 | |
| 241 | Ubiquitination | HILGMKCKICESYNT EEECCEEEECCCCCC | 44.89 | 21963094 | |
| 248 | Phosphorylation | KICESYNTAQAGGRR EECCCCCCCCCCCCC | 16.35 | 29514088 | |
| 257 | Phosphorylation | QAGGRRISLDQQ--- CCCCCCCCCCCC--- | 24.87 | 30266825 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 154 | T | Phosphorylation | Kinase | CAMK2A | Q9UQM7 | PSP |
| 155 | S | Phosphorylation | Kinase | CAMK2A | Q9UQM7 | PSP |
| 211 | S | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
| 217 | T | Phosphorylation | Kinase | CDK9 | P50750 | PSP |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZN363_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 ZN363_HUMAN !! | ||||||
| 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 |
| "A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASSSPECTROMETRY. | |
| "Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-257, AND MASSSPECTROMETRY. | |
