| UniProt ID | RPR1A_HUMAN | |
|---|---|---|
| UniProt AC | Q96P16 | |
| Protein Name | Regulation of nuclear pre-mRNA domain-containing protein 1A | |
| Gene Name | RPRD1A | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 312 | |
| Subcellular Localization | ||
| Protein Description | Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. May act as a negative regulator of cyclin-D1 (CCND1) and cyclin-E (CCNE1) in the cell cycle.. | |
| Protein Sequence | MSAFSEAALEKKLSELSNSQQSVQTLSLWLIHHRKHSRPIVTVWERELRKAKPNRKLTFLYLANDVIQNSKRKGPEFTKDFAPVIVEAFKHVSSETDESCKKHLGRVLSIWEERSVYENDVLEQLKQALYGDKKPRKRTYEQIKVDENENCSSLGSPSEPPQTLDLVRALQDLENAASGDAAVHQRIASLPVEVQEVSLLDKITDKESGERLSKMVEDACMLLADYNGRLAAEIDDRKQLTRMLADFLRCQKEALAEKEHKLEEYKRKLARVSLVRKELRSRIQSLPDLSRLPNVTGSHMHLPFAGDIYSED | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
|
|
||
* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 2 | Phosphorylation | ------MSAFSEAAL ------CCHHHHHHH | 37.71 | 19413330 | |
| 2 | Acetylation | ------MSAFSEAAL ------CCHHHHHHH | 37.71 | 19413330 | |
| 5 | Phosphorylation | ---MSAFSEAALEKK ---CCHHHHHHHHHH | 26.49 | 28509920 | |
| 12 | Sumoylation | SEAALEKKLSELSNS HHHHHHHHHHHHCCC | 48.12 | - | |
| 12 | Sumoylation | SEAALEKKLSELSNS HHHHHHHHHHHHCCC | 48.12 | - | |
| 12 | Ubiquitination | SEAALEKKLSELSNS HHHHHHHHHHHHCCC | 48.12 | - | |
| 14 | Phosphorylation | AALEKKLSELSNSQQ HHHHHHHHHHCCCHH | 45.42 | 29759185 | |
| 17 | Phosphorylation | EKKLSELSNSQQSVQ HHHHHHHCCCHHHHH | 30.31 | 29759185 | |
| 19 | Phosphorylation | KLSELSNSQQSVQTL HHHHHCCCHHHHHHH | 26.65 | 29759185 | |
| 25 | Phosphorylation | NSQQSVQTLSLWLIH CCHHHHHHHHHHHHH | 19.03 | 29759185 | |
| 27 | Phosphorylation | QQSVQTLSLWLIHHR HHHHHHHHHHHHHCC | 22.38 | 29759185 | |
| 37 | Phosphorylation | LIHHRKHSRPIVTVW HHHCCCCCCCCEEHH | 42.67 | - | |
| 52 | Acetylation | ERELRKAKPNRKLTF HHHHHHCCCCCCEEE | 45.95 | 30591095 | |
| 56 | Ubiquitination | RKAKPNRKLTFLYLA HHCCCCCCEEEEHHH | 59.52 | - | |
| 56 | Acetylation | RKAKPNRKLTFLYLA HHCCCCCCEEEEHHH | 59.52 | 30591101 | |
| 71 | Ubiquitination | NDVIQNSKRKGPEFT HHHHHHCHHCCCCCC | 66.72 | - | |
| 79 | Ubiquitination | RKGPEFTKDFAPVIV HCCCCCCCCCHHHHH | 57.05 | - | |
| 90 | Ubiquitination | PVIVEAFKHVSSETD HHHHHHHHHCCCCCC | 50.58 | - | |
| 109 | Phosphorylation | KHLGRVLSIWEERSV HHHHHHHHHHHHCCH | 23.85 | 28857561 | |
| 114 | Methylation | VLSIWEERSVYENDV HHHHHHHCCHHCHHH | 21.65 | 115486127 | |
| 126 | Ubiquitination | NDVLEQLKQALYGDK HHHHHHHHHHHHCCC | 32.97 | - | |
| 139 | Phosphorylation | DKKPRKRTYEQIKVD CCCCCCCCCCCCCCC | 34.15 | 27966365 | |
| 140 | Phosphorylation | KKPRKRTYEQIKVDE CCCCCCCCCCCCCCC | 15.18 | 30624053 | |
| 150 | N-linked_Glycosylation | IKVDENENCSSLGSP CCCCCCCCCCCCCCC | 42.42 | 12470661 | |
| 150 | N-linked_Glycosylation | IKVDENENCSSLGSP CCCCCCCCCCCCCCC | 42.42 | - | |
| 152 | Phosphorylation | VDENENCSSLGSPSE CCCCCCCCCCCCCCC | 39.93 | 30266825 | |
| 153 | Phosphorylation | DENENCSSLGSPSEP CCCCCCCCCCCCCCC | 38.66 | 30266825 | |
| 156 | Phosphorylation | ENCSSLGSPSEPPQT CCCCCCCCCCCCCCH | 30.46 | 25159151 | |
| 158 | Phosphorylation | CSSLGSPSEPPQTLD CCCCCCCCCCCCHHH | 65.51 | 30266825 | |
| 163 | Phosphorylation | SPSEPPQTLDLVRAL CCCCCCCHHHHHHHH | 28.19 | 30266825 | |
| 189 | Phosphorylation | AVHQRIASLPVEVQE HHHHHHHCCCCEEEE | 30.73 | - | |
| 198 | Phosphorylation | PVEVQEVSLLDKITD CCEEEEEHHHHHHCC | 23.59 | - | |
| 202 | Ubiquitination | QEVSLLDKITDKESG EEEHHHHHHCCCCCC | 47.69 | - | |
| 204 | Phosphorylation | VSLLDKITDKESGER EHHHHHHCCCCCCHH | 46.92 | - | |
| 285 | Phosphorylation | ELRSRIQSLPDLSRL HHHHHHHCCCCHHHC | 39.23 | 25850435 | |
| 290 | Phosphorylation | IQSLPDLSRLPNVTG HHCCCCHHHCCCCCC | 38.87 | 23186163 | |
| 294 | N-linked_Glycosylation | PDLSRLPNVTGSHMH CCHHHCCCCCCCCCC | 48.88 | - | |
| 294 | N-linked_Glycosylation | PDLSRLPNVTGSHMH CCHHHCCCCCCCCCC | 48.88 | 12470661 | |
| 298 | Phosphorylation | RLPNVTGSHMHLPFA HCCCCCCCCCCCCCC | 14.31 | 28555341 | |
| 309 | Phosphorylation | LPFAGDIYSED---- CCCCCCCCCCC---- | 15.67 | 28796482 | |
| 310 | Phosphorylation | PFAGDIYSED----- CCCCCCCCCC----- | 35.31 | 29978859 |
| 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 RPR1A_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of RPR1A_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 RPR1A_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| 1433Z_HUMAN | YWHAZ | physical | 21988832 | |
| KDM1A_HUMAN | KDM1A | physical | 23455924 | |
| ANKY2_HUMAN | ANKMY2 | physical | 22863883 | |
| HSF1_HUMAN | HSF1 | physical | 22863883 | |
| NPL4_HUMAN | NPLOC4 | physical | 22863883 | |
| PLIN3_HUMAN | PLIN3 | physical | 22863883 | |
| DPH2_HUMAN | DPH2 | physical | 26344197 | |
| DXO_HUMAN | DXO | physical | 26344197 | |
| MITD1_HUMAN | MITD1 | physical | 26344197 | |
| VP37B_HUMAN | VPS37B | physical | 26344197 | |
| CAVN1_HUMAN | PTRF | physical | 27173435 | |
| VPS50_HUMAN | CCDC132 | physical | 27173435 | |
| PKN3_HUMAN | PKN3 | physical | 27173435 | |
| RABX5_HUMAN | RABGEF1 | physical | 27173435 |
| 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. | ||||||
loading...