| UniProt ID | DCAF1_MOUSE | |
|---|---|---|
| UniProt AC | Q80TR8 | |
| Protein Name | DDB1- and CUL4-associated factor 1 {ECO:0000250|UniProtKB:Q9Y4B6} | |
| Gene Name | Dcaf1 {ECO:0000250|UniProtKB:Q9Y4B6} | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 1506 | |
| Subcellular Localization | Cytoplasm. Nucleus. Associated with chromatin in a DDB1-independent and cell cycle-dependent manner: recruited to chromatin as DNA is being replicated and is released from chromatin before mitosis.. | |
| Protein Description | Acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation and histone modification. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex. The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition. Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down-regulates their transcription and is present at high level in a number of tumors. Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2.. | |
| Protein Sequence | MTTVVVHVDSKAELTTLLEQWEKDHGSGQDMVPILTRMSELIEKETEEYRKGDPDPFDDRHPGRADPECMLGHLLRILFKNDDFMNALVNAYVMTSREPPLNTAACRLLLDIMPGLETAVVFQEKEGIVENLFKWAREADQPLRTYSTGLLGGAMENQDIAANYRDENSQLVAIVLRRLRELQLQEVALRQDSKRPSPRKLSSEPLLPLDEEAVDMDYGDMAVDVVDGEQESSRDMEISFRLDSSHKTSSRVNSATKPEEGGLKKNKSAKHGDRENFRKAKQKLGFSSSDPDRVFVELSNSSWSEMSPWVIGTNYTLYPMTPAIEQRLILQYLTPLGEYQELLPIFMQLGSRELMMFYIDLKQTNDVLLTFEALKHLASLLLHNKFATEFVAHGGVQKLLEIPRPSMAATGVSMCLYYLSYNQDAMERVCMHPHNVLSDVVNYTLWLMECSHASGCCHATMFFSICFSFRAVLELFDRYDGLRRLVNLISTLEILNLEDQGALLSDDEIFASRQTGKHTCMALRKYFEAHLAIKLEQVKQSLQRTEGGILVHPQPPYKACSYTHEQIVEMMEFLIEYGPAQLYWEPAEVFLKLSCVQLLLQLISIACNWKTYYARNDTVRFALDVLAILTVVPKIQLQLAESVDVLDEAGSAVSTVGISIILGVAEGEFFIHDAEIQKSALQIIINCVCGPDNRISSIGKFISGTPRRKLSQTPKSSEHTLAKMWNVVQSNNGIKVLLSLLSIKMPITDADQIRALACKALVGLSRSSTVRQIISKLPLFSSCQIQQLMKEPVLQDKRSDHVKFCKYAAELIERVSGKPLLIGTDVSLARLQKADVVAQSRISFPEKELLLLIRNHLISKGLGETATVLTREADLPMTAASHSSAFTPVTAAASPVSLPRTPRIANGIASRLGSHATVGASAPSAPPAHPPPRPPQGSLPLPGPSYAGNSPLIGRISFIRERPSPCNGRKIRVLRQKSDHGAYSQSPAIKKQLDRHLPSPPTLDSIITEYLREQHARCKNPVATCPPFSLFTPHQCPEPKQRRQAPINFTSRLNRRASFPKYGGVDGGCFDRHLIFSRFRPISVFREANEDESGFTCCAFSARERFLMLGTCTGQLKLYNVFSGQEEASYNCHNSAITHLEPSRDGSLLLTSATWSQPLSALWGMKSVFDMKHSFTEDHYVEFSKHSQDRVIGTKGDIAHIYDIQTGNKLLTLFNPDLANNYKRNCATFNPTDDLVLNDGVLWDVRSAQAIHKFDKFNMNISGVFHPNGLEVIINTEIWDLRTFHLLHTVPALDQCRVVFNHTGTVMYGAMLQADDEDDLLEERMKSPFGSSFRTFNATDYKPIATIDVKRNIFDLCTDTKDCYLAVIENQGSMDALNMDTVCRLYEVGRQRLAEDEDEEEDQEEEEQEEEDDDEDDDDTDDLDELDTDQLLEAELEEDDNNENAGEDGDNDFSPSDEELANLLEEGEEGEDEDSDADEEVELILGDTDSSDNSDLEDDIILSLNE | |
| 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 |
|---|---|---|---|---|---|
| 10 | Phosphorylation | TVVVHVDSKAELTTL EEEEEECCHHHHHHH | 22817900 | ||
| 193 | Phosphorylation | EVALRQDSKRPSPRK HHHHHCCCCCCCCCC | - | ||
| 197 | Phosphorylation | RQDSKRPSPRKLSSE HCCCCCCCCCCCCCC | 25266776 | ||
| 202 | Phosphorylation | RPSPRKLSSEPLLPL CCCCCCCCCCCCCCC | 25338131 | ||
| 203 | Phosphorylation | PSPRKLSSEPLLPLD CCCCCCCCCCCCCCC | 25338131 | ||
| 239 | Phosphorylation | SSRDMEISFRLDSSH CCCCCEEEEEECCCC | 28066266 | ||
| 244 | Phosphorylation | EISFRLDSSHKTSSR EEEEEECCCCCCCCC | 27149854 | ||
| 245 | Phosphorylation | ISFRLDSSHKTSSRV EEEEECCCCCCCCCC | 23140645 | ||
| 248 | Phosphorylation | RLDSSHKTSSRVNSA EECCCCCCCCCCCCC | 23140645 | ||
| 249 | Phosphorylation | LDSSHKTSSRVNSAT ECCCCCCCCCCCCCC | 23140645 | ||
| 250 | Phosphorylation | DSSHKTSSRVNSATK CCCCCCCCCCCCCCC | 23140645 | ||
| 254 | Phosphorylation | KTSSRVNSATKPEEG CCCCCCCCCCCCCCC | 25266776 | ||
| 256 | Phosphorylation | SSRVNSATKPEEGGL CCCCCCCCCCCCCCC | 28066266 | ||
| 512 | Phosphorylation | SDDEIFASRQTGKHT CCHHHHHCCCCCHHH | 24759943 | ||
| 700 | Acetylation | NRISSIGKFISGTPR CCHHHHHHHHCCCCC | 23806337 | ||
| 703 | Phosphorylation | SSIGKFISGTPRRKL HHHHHHHCCCCCCCC | 24453211 | ||
| 705 | Phosphorylation | IGKFISGTPRRKLSQ HHHHHCCCCCCCCCC | 24453211 | ||
| 711 | Phosphorylation | GTPRRKLSQTPKSSE CCCCCCCCCCCCCCH | 28833060 | ||
| 713 | Phosphorylation | PRRKLSQTPKSSEHT CCCCCCCCCCCCHHH | 28576409 | ||
| 818 | Ubiquitination | LIERVSGKPLLIGTD HHHHHCCCCEEEECC | 22790023 | ||
| 827 | Phosphorylation | LLIGTDVSLARLQKA EEEECCCHHHHHHHC | - | ||
| 887 | Phosphorylation | ASHSSAFTPVTAAAS CCCCCCCCCCCCCCC | - | ||
| 890 | Phosphorylation | SSAFTPVTAAASPVS CCCCCCCCCCCCCCC | 28066266 | ||
| 894 | Phosphorylation | TPVTAAASPVSLPRT CCCCCCCCCCCCCCC | 26239621 | ||
| 897 | Phosphorylation | TAAASPVSLPRTPRI CCCCCCCCCCCCHHH | 28066266 | ||
| 978 | Phosphorylation | IRVLRQKSDHGAYSQ EEEEEECCCCCCCCC | 23375375 | ||
| 983 | Phosphorylation | QKSDHGAYSQSPAIK ECCCCCCCCCCHHHH | 28833060 | ||
| 986 | Phosphorylation | DHGAYSQSPAIKKQL CCCCCCCCHHHHHHH | - | ||
| 999 | Phosphorylation | QLDRHLPSPPTLDSI HHHHCCCCCCCHHHH | 26824392 | ||
| 1002 | Phosphorylation | RHLPSPPTLDSIITE HCCCCCCCHHHHHHH | 25177544 | ||
| 1005 | Phosphorylation | PSPPTLDSIITEYLR CCCCCHHHHHHHHHH | 26239621 | ||
| 1008 | Phosphorylation | PTLDSIITEYLREQH CCHHHHHHHHHHHHH | 25777480 | ||
| 1058 | Phosphorylation | SRLNRRASFPKYGGV HHHHHCCCCCCCCCC | - | ||
| 1160 | Phosphorylation | ATWSQPLSALWGMKS EEECCCHHHHHCCCC | 28576409 | ||
| 1247 | O-linked_Glycosylation | GVLWDVRSAQAIHKF CCEEEHHHHHHHHHH | 30016717 | ||
| 1327 | Phosphorylation | LLEERMKSPFGSSFR HHHHHHCCCCCCCCC | 24899341 |
| 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 DCAF1_MOUSE !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DCAF1_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 DCAF1_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DCAF1_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
loading...
