UniProt ID | ZBT18_MOUSE | |
---|---|---|
UniProt AC | Q9WUK6 | |
Protein Name | Zinc finger and BTB domain-containing protein 18 | |
Gene Name | Zbtb18 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 522 | |
Subcellular Localization | Nucleus. Associates with condensed chromatin. | |
Protein Description | Transcriptional repressor that plays a role in various developmental processes such as myogenesis and brain development. Specifically binds the consensus DNA sequence 5'-[AC]ACATCTG[GT][AC]-3' which contains the E box core, and acts by recruiting chromatin remodeling multiprotein complexes. Plays a key role in myogenesis by directly repressing the expression of ID2 and ID3, 2 inhibitors of skeletal myogenesis. Also involved in controlling cell division of progenitor cells and regulating the survival of postmitotic cortical neurons. May also play a role in the organization of chromosomes in the nucleus.. | |
Protein Sequence | MEFPDHSRHLLQCLSEQRHQGFLCDCTVLVGDAQFRAHRAVLASCSMYFHLFYKDQLDKRDIVHLNSDIVTAPAFALLLEFMYEGKLQFKDLPIEDVLAAASYLHMYDIVKVCKKKLKEKATTEADSTKKEEDASSCSDKVESLSDGSSHMAGDLPSDEDEGEDDKLNILPSKRDLAAEPGNMWMRLPSDSAGIPQAGGEAEPHATAAGKTVASPCSSTESLSQRSVTSVRDSADVDCVLDLSVKSSLSGVENLNSSYFSSQDVLRSNLVQVKVEKEASCDESDVGTNDYDMEHSTVKESVSTNNRVQYEPAHLAPLREDSVLRELDREDKASDDEMMTPESERVQVEGGMENSLLPYVSNILSPAGQIFMCPLCNKVFPSPHILQIHLSTHFREQDGIRSKPAADVNVPTCSLCGKTFSCMYTLKRHERTHSGEKPYTCTQCGKSFQYSHNLSRHAVVHTREKPHACKWCERRFTQSGDLYRHIRKFHCELVNSLSVKSEALSLPTVRDWTLEDSSQELWK | |
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 |
---|---|---|---|---|---|
118 | Acetylation | KVCKKKLKEKATTEA HHHHHHHHHHCCCCC | 6571697 | ||
120 | Acetylation | CKKKLKEKATTEADS HHHHHHHHCCCCCCC | 6571619 | ||
129 | Acetylation | TTEADSTKKEEDASS CCCCCCCCHHHHHHH | 6571745 | ||
157 | Phosphorylation | HMAGDLPSDEDEGED CCCCCCCCCCCCCCC | 25338131 | ||
211 | Phosphorylation | HATAAGKTVASPCSS CCCCCCCEEECCCCC | 23527152 | ||
214 | Phosphorylation | AAGKTVASPCSSTES CCCCEEECCCCCCHH | 25521595 | ||
217 | Phosphorylation | KTVASPCSSTESLSQ CEEECCCCCCHHHHH | 21183079 | ||
218 | Phosphorylation | TVASPCSSTESLSQR EEECCCCCCHHHHHC | 19060867 | ||
219 | Phosphorylation | VASPCSSTESLSQRS EECCCCCCHHHHHCC | 21183079 | ||
221 | Phosphorylation | SPCSSTESLSQRSVT CCCCCCHHHHHCCCC | 25293948 | ||
223 | Phosphorylation | CSSTESLSQRSVTSV CCCCHHHHHCCCCCH | 24719451 | ||
279 | Phosphorylation | VKVEKEASCDESDVG EEEEECCCCCHHCCC | 19060867 | ||
283 | Phosphorylation | KEASCDESDVGTNDY ECCCCCHHCCCCCCC | 29899451 | ||
321 | Phosphorylation | LAPLREDSVLRELDR HHCCCCCHHHHHHCC | 29899451 | ||
333 | Phosphorylation | LDREDKASDDEMMTP HCCCCCCCCCCCCCC | 25521595 | ||
339 | Phosphorylation | ASDDEMMTPESERVQ CCCCCCCCCHHHCEE | 30635358 | ||
507 | Phosphorylation | SEALSLPTVRDWTLE CCCCCCCCCCCCCCC | - | ||
516 | Phosphorylation | RDWTLEDSSQELWK- CCCCCCCCHHHHCC- | - | ||
517 | Phosphorylation | DWTLEDSSQELWK-- CCCCCCCHHHHCC-- | 21082442 | ||
525 | Phosphorylation | QELWK---------- HHHCC---------- | 24719451 |
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 ZBT18_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZBT18_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 ZBT18_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of ZBT18_MOUSE !! |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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