UniProt ID | EPC2_MOUSE | |
---|---|---|
UniProt AC | Q8C0I4 | |
Protein Name | Enhancer of polycomb homolog 2 | |
Gene Name | Epc2 | |
Organism | Mus musculus (Mouse). | |
Sequence Length | 808 | |
Subcellular Localization | Nucleus. | |
Protein Description | May play a role in transcription or DNA repair.. | |
Protein Sequence | MSKLSFRARALDAAKPLPIYRGKDMPDLNDCVSINRAVPQMPTGMEKEEESEHHLQRAISAQQVFREKKESMVIPVPEAESNVNYYNRLYKGEFKQPKQFIHIQPFNLDNEQPDYDMDSEDETLLNRLNRKMEIKPLQFEIMIDRLEKASSNQLVTLQEAKLLLNEDDYLIKAVYDYWVRKRKNCRGPSLIPQIKQEKRDGSTNNDPYVAFRRRTEKMQTRKNRKNDEASYEKMLKLRREFSRAITILEMIKRREKTKRELLHLTLEVVEKRYHLGDYGGEILNEVKVNRSEKELYASPATLHNGNHHKVQECKTKHPHHLSLKEEASDVVRQKKKYPKKPKAEAGIAPQQPTPETLPVINKSDIKQYDFQSSDEDEFPQVLSPASEAEEENDPDGSCAFRRRAGCQYYAPRLDQANNHMCENSELADLDKLRYKHCLTTLTVPRRCIGFARRRIGRGGRVIMDRISTEHDPVLKQIDPEMLNGFSSSSQTIDFSSNFSRTNASSKPCENRLSLSEILSNIRSCRLQCFQPRLLNVQDIDSEECTSRKPGQTVSSKRVSAASVALLNTSKNGISVTGGITEEQFQTHQQQLVQMQRQQLAQLHQKQQSQHSSQQTHPKAQGSSTSDCMSKTLDSASAHFAASAVVSAPVPSRSEGSKEQNTGHNNMNGVVQPSGPSKTLYSTNMALSSSPGISAVQLVRTVGHTTTNHLIPALCTSSPQTLPMNNSCLTNAVHLNNVSVVSPVNVHINTRTSAPSPTALKLATVAASMDRVPKVTPSSAISSIARENHEPERLGLNGLAETTVAMEVT | |
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 |
---|---|---|---|---|---|
23 | Acetylation | PLPIYRGKDMPDLND CCCCCCCCCCCCHHH | 41.68 | 23806337 | |
51 | Phosphorylation | GMEKEEESEHHLQRA CCCCHHHCHHHHHHH | 45.57 | 28059163 | |
60 | Phosphorylation | HHLQRAISAQQVFRE HHHHHHHHHHHHHHH | 21.02 | 29176673 | |
115 | Phosphorylation | LDNEQPDYDMDSEDE CCCCCCCCCCCCCHH | 21.61 | 26745281 | |
119 | Phosphorylation | QPDYDMDSEDETLLN CCCCCCCCCHHHHHH | 40.07 | 26745281 | |
123 | Phosphorylation | DMDSEDETLLNRLNR CCCCCHHHHHHHHHH | 49.20 | 24759943 | |
383 | Phosphorylation | DEFPQVLSPASEAEE CCCCCCCCCHHHHHH | 21.40 | 24759943 | |
386 | Phosphorylation | PQVLSPASEAEEEND CCCCCCHHHHHHHCC | 40.50 | 24759943 | |
434 | Phosphorylation | ADLDKLRYKHCLTTL CCHHHHHHCHHHCCC | 18.60 | 20139300 | |
552 | Phosphorylation | TSRKPGQTVSSKRVS CCCCCCCCCCCHHHC | 28.42 | 25367039 | |
556 | Acetylation | PGQTVSSKRVSAASV CCCCCCCHHHCHHHH | 49.68 | 30985921 | |
636 | Phosphorylation | SKTLDSASAHFAASA HHHHHHHHHHHHHHH | 26.65 | 28059163 | |
642 | Phosphorylation | ASAHFAASAVVSAPV HHHHHHHHHHEECCC | 20.40 | 28059163 | |
653 | Phosphorylation | SAPVPSRSEGSKEQN ECCCCCCCCCCCCCC | 51.12 | 30635358 | |
656 | Phosphorylation | VPSRSEGSKEQNTGH CCCCCCCCCCCCCCC | 29.03 | 30635358 | |
661 | Phosphorylation | EGSKEQNTGHNNMNG CCCCCCCCCCCCCCC | 39.24 | 30635358 | |
673 | Phosphorylation | MNGVVQPSGPSKTLY CCCCCCCCCCCCCEE | 46.36 | 30635358 | |
676 | Phosphorylation | VVQPSGPSKTLYSTN CCCCCCCCCCEEECC | 41.62 | 30635358 | |
677 | Acetylation | VQPSGPSKTLYSTNM CCCCCCCCCEEECCC | 45.76 | 23236377 | |
751 | Phosphorylation | NVHINTRTSAPSPTA EEEECCCCCCCCCHH | 27.48 | 30635358 | |
755 | Phosphorylation | NTRTSAPSPTALKLA CCCCCCCCCHHHHHH | 34.30 | 27149854 | |
757 | Phosphorylation | RTSAPSPTALKLATV CCCCCCCHHHHHHHH | 49.30 | 30635358 |
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 EPC2_MOUSE !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of EPC2_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 EPC2_MOUSE !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
Oops, there are no PPI records of EPC2_MOUSE !! |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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