| UniProt ID | ZN792_HUMAN | |
|---|---|---|
| UniProt AC | Q3KQV3 | |
| Protein Name | Zinc finger protein 792 | |
| Gene Name | ZNF792 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 632 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | May be involved in transcriptional regulation.. | |
| Protein Sequence | MAAAALRDPAQGCVTFEDVTIYFSQEEWVLLDEAQRLLYCDVMLENFALIASLGLISFRSHIVSQLEMGKEPWVPDSVDMTSAMARGAYGRPGSDFCHGTEGKDLPSEHNVSVEGVAQDRSPEATLCPQKTCPCDICGLRLKDILHLAEHQTTHPRQKPFVCEAYVKGSEFSANLPRKQVQQNVHNPIRTEEGQASPVKTCRDHTSDQLSTCREGGKDFVATAGFLQCEVTPSDGEPHEATEGVVDFHIALRHNKCCESGDAFNNKSTLVQHQRIHSRERPYECSKCGIFFTYAADLTQHQKVHNRGKPYECCECGKFFSQHSSLVKHRRVHTGESPHVCGDCGKFFSRSSNLIQHKRVHTGEKPYECSDCGKFFSQRSNLIHHKRVHTGRSAHECSECGKSFNCNSSLIKHWRVHTGERPYKCNECGKFFSHIASLIQHQIVHTGERPHGCGECGKAFSRSSDLMKHQRVHTGERPYECNECGKLFSQSSSLNSHRRLHTGERPYQCSECGKFFNQSSSLNNHRRLHTGERPYECSECGKTFRQRSNLRQHLKVHKPDRPYECSECGKAFNQRPTLIRHQKIHIRERSMENVLLPCSQHTPEISSENRPYQGAVNYKLKLVHPSTHPGEVP | |
| 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 |
|---|---|---|---|---|---|
| 57 | Phosphorylation | IASLGLISFRSHIVS HHHHCHHHHHHHHHH | 21.46 | 24719451 | |
| 121 | Phosphorylation | EGVAQDRSPEATLCP EEEECCCCCCCCCCC | 35.07 | 28450419 | |
| 125 | Phosphorylation | QDRSPEATLCPQKTC CCCCCCCCCCCCCCC | 27.51 | 28450419 | |
| 190 | Phosphorylation | NVHNPIRTEEGQASP HCCCCCCCCCCCCCC | 38.82 | 23186163 | |
| 196 | Phosphorylation | RTEEGQASPVKTCRD CCCCCCCCCCCCCCC | 23.49 | 30576142 | |
| 277 | Phosphorylation | VQHQRIHSRERPYEC HHHCHHHCCCCCCCC | 33.20 | - | |
| 285 | Phosphorylation | RERPYECSKCGIFFT CCCCCCCCCCCCEEE | 21.02 | - | |
| 292 | Phosphorylation | SKCGIFFTYAADLTQ CCCCCEEEEECCCHH | 11.08 | - | |
| 348 | Phosphorylation | GDCGKFFSRSSNLIQ CCHHHHHHCCCCHHC | 34.09 | 25394399 | |
| 361 | Phosphorylation | IQHKRVHTGEKPYEC HCCCEECCCCCCEEC | 44.15 | - | |
| 385 | Ubiquitination | RSNLIHHKRVHTGRS CCCCCCCCCCCCCCC | 41.79 | - | |
| 408 | Phosphorylation | KSFNCNSSLIKHWRV CCCCCCCHHHCCEEE | 21.81 | 24719451 | |
| 417 | Phosphorylation | IKHWRVHTGERPYKC HCCEEEECCCCCEEC | 37.57 | 27251275 | |
| 423 | Sumoylation | HTGERPYKCNECGKF ECCCCCEECCCHHHH | 33.01 | - | |
| 423 | Sumoylation | HTGERPYKCNECGKF ECCCCCEECCCHHHH | 33.01 | - | |
| 467 | Methylation | SRSSDLMKHQRVHTG HCCHHHHHCCCCCCC | 43.83 | - | |
| 473 | Phosphorylation | MKHQRVHTGERPYEC HHCCCCCCCCCCCCC | 37.57 | - | |
| 490 | Phosphorylation | CGKLFSQSSSLNSHR HHHHHCCCCCCCCCC | 22.24 | 30622161 | |
| 491 | Phosphorylation | GKLFSQSSSLNSHRR HHHHCCCCCCCCCCC | 31.07 | 30622161 | |
| 492 | Phosphorylation | KLFSQSSSLNSHRRL HHHCCCCCCCCCCCC | 36.50 | 30622161 | |
| 495 | Phosphorylation | SQSSSLNSHRRLHTG CCCCCCCCCCCCCCC | 24.54 | 30622161 | |
| 518 | Phosphorylation | CGKFFNQSSSLNNHR CHHHHCCCCCCCCCC | 24.01 | 28555341 |
| 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 ZN792_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZN792_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 ZN792_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| ZN792_HUMAN | ZNF792 | physical | 25416956 | |
| KR107_HUMAN | KRTAP10-7 | physical | 25416956 | |
| KR109_HUMAN | KRTAP10-9 | physical | 25416956 | |
| KR103_HUMAN | KRTAP10-3 | physical | 25416956 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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