| UniProt ID | ZN554_HUMAN | |
|---|---|---|
| UniProt AC | Q86TJ5 | |
| Protein Name | Zinc finger protein 554 | |
| Gene Name | ZNF554 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 538 | |
| Subcellular Localization | Nucleus . | |
| Protein Description | May be involved in transcriptional regulation.. | |
| Protein Sequence | MVTCAHLGRRARLPAAQPSACPGTCFSQEERMAAGYLPRWSQELVTFEDVSMDFSQEEWELLEPAQKNLYREVMLENYRNVVSLEALKNQCTDVGIKEGPLSPAQTSQVTSLSSWTGYLLFQPVASSHLEQREALWIEEKGTPQASCSDWMTVLRNQDSTYKKVALQEEPASGINMIKLIREDGGWKQLEDSHEDPQGLLSQKASLHVVAVPQEKATAWHGFGENGNLSPALVLSQGSSKGNHLCGSELDITSLASDSVLNHHQLGYADRRPCESNECGNAIRQNSHFIQHGGKMFVYLENGQSLNHGMALTIHNKINTAEKPFECHQCGKVFNRRHSLSEHQRIHTGEKPYECQECGRAFTHSSTLTRHLRTHTGEKPYGCGECGKAFNRISSLTQHQRIHTGEKPYKCEDCGKSFCQSSYLILHKRTHTGEKPYECSECGKAFSDRSSLNQHERTHTGENPYECKQCGRAFSQRSSLVRHERTHTGEKPYRCQECGKAFSQSSSLVTHQKTHSSQKTYKIIDCGKAFYQNRHLIGY | |
| 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 |
|---|---|---|---|---|---|
| 178 | Sumoylation | ASGINMIKLIREDGG CCCCCCEEEEEECCC | 27.39 | 28112733 | |
| 229 | Phosphorylation | FGENGNLSPALVLSQ CCCCCCCCCEEEECC | 16.48 | 25159151 | |
| 338 | O-linked_Glycosylation | KVFNRRHSLSEHQRI CCCCCCCCCCCCCCC | 31.60 | OGP | |
| 338 | Phosphorylation | KVFNRRHSLSEHQRI CCCCCCCCCCCCCCC | 31.60 | 29449344 | |
| 340 | Phosphorylation | FNRRHSLSEHQRIHT CCCCCCCCCCCCCCC | 35.73 | 29449344 | |
| 340 | O-linked_Glycosylation | FNRRHSLSEHQRIHT CCCCCCCCCCCCCCC | 35.73 | OGP | |
| 347 | Phosphorylation | SEHQRIHTGEKPYEC CCCCCCCCCCCCCCC | 44.67 | 28111955 | |
| 373 | Phosphorylation | TLTRHLRTHTGEKPY HHHHHHHHCCCCCCC | 30.10 | - | |
| 375 | Phosphorylation | TRHLRTHTGEKPYGC HHHHHHCCCCCCCCC | 46.56 | - | |
| 403 | Phosphorylation | TQHQRIHTGEKPYKC CCCCCCCCCCCCCCC | 44.67 | 29496963 | |
| 406 | Ubiquitination | QRIHTGEKPYKCEDC CCCCCCCCCCCCCCC | 55.80 | - | |
| 409 | Sumoylation | HTGEKPYKCEDCGKS CCCCCCCCCCCCCCC | 39.41 | - | |
| 409 | Sumoylation | HTGEKPYKCEDCGKS CCCCCCCCCCCCCCC | 39.41 | - | |
| 409 | Ubiquitination | HTGEKPYKCEDCGKS CCCCCCCCCCCCCCC | 39.41 | - | |
| 429 | Phosphorylation | YLILHKRTHTGEKPY EEEEECCCCCCCCCE | 28.70 | - | |
| 431 | Phosphorylation | ILHKRTHTGEKPYEC EEECCCCCCCCCEEC | 46.56 | - | |
| 434 | Ubiquitination | KRTHTGEKPYECSEC CCCCCCCCCEECCCC | 55.00 | - | |
| 439 | Phosphorylation | GEKPYECSECGKAFS CCCCEECCCCCCCCC | 24.79 | - | |
| 477 | Phosphorylation | GRAFSQRSSLVRHER CCHHHHHHHHHHCCC | 22.01 | 25137130 | |
| 478 | Phosphorylation | RAFSQRSSLVRHERT CHHHHHHHHHHCCCC | 32.83 | 24719451 | |
| 485 | Phosphorylation | SLVRHERTHTGEKPY HHHHCCCCCCCCCCE | 22.32 | - | |
| 487 | Phosphorylation | VRHERTHTGEKPYRC HHCCCCCCCCCCEEH | 46.56 | 24719451 | |
| 490 | Acetylation | ERTHTGEKPYRCQEC CCCCCCCCCEEHHHH | 49.01 | 30593783 | |
| 519 | Phosphorylation | KTHSSQKTYKIIDCG CCCCCCCEEEEEECC | 23.55 | - | |
| 520 | Phosphorylation | THSSQKTYKIIDCGK CCCCCCEEEEEECCH | 13.76 | - |
| 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 ZN554_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZN554_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 ZN554_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ZN554_HUMAN !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...