UniProt ID | SMYD1_HUMAN | |
---|---|---|
UniProt AC | Q8NB12 | |
Protein Name | Histone-lysine N-methyltransferase SMYD1 | |
Gene Name | SMYD1 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 490 | |
Subcellular Localization | Cytoplasm. Nucleus. | |
Protein Description | Methylates histone H3 at 'Lys-4' (H3K4me), seems able to perform both mono-, di-, and trimethylation. Acts as a transcriptional repressor. Essential for cardiomyocyte differentiation and cardiac morphogenesis.. | |
Protein Sequence | MTIGRMENVEVFTAEGKGRGLKATKEFWAADIIFAERAYSAVVFDSLVNFVCHTCFKRQEKLHRCGQCKFAHYCDRTCQKDAWLNHKNECSAIKRYGKVPNENIRLAARIMWRVEREGTGLTEGCLVSVDDLQNHVEHFGEEEQKDLRVDVDTFLQYWPPQSQQFSMQYISHIFGVINCNGFTLSDQRGLQAVGVGIFPNLGLVNHDCWPNCTVIFNNGNHEAVKSMFHTQMRIELRALGKISEGEELTVSYIDFLNVSEERKRQLKKQYYFDCTCEHCQKKLKDDLFLGVKDNPKPSQEVVKEMIQFSKDTLEKIDKARSEGLYHEVVKLCRECLEKQEPVFADTNIYMLRMLSIVSEVLSYLQAFEEASFYARRMVDGYMKLYHPNNAQLGMAVMRAGLTNWHAGNIEVGHGMICKAYAILLVTHGPSHPITKDLEAMRVQTEMELRMFRQNEFMYYKMREAALNNQPMQVMAEPSNEPSPALFHKKQ | |
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 |
---|---|---|---|---|---|
2 | O-linked_Glycosylation | ------MTIGRMENV ------CCCCCCCCE | 31.94 | 30379171 | |
39 | Phosphorylation | IIFAERAYSAVVFDS HHHHHHHHHHHHHHH | 11.90 | - | |
40 | Phosphorylation | IFAERAYSAVVFDSL HHHHHHHHHHHHHHH | 17.38 | - | |
46 | Phosphorylation | YSAVVFDSLVNFVCH HHHHHHHHHHHHHHH | 23.81 | - | |
54 | Phosphorylation | LVNFVCHTCFKRQEK HHHHHHHHHHHHHHH | 17.95 | - | |
91 | Phosphorylation | LNHKNECSAIKRYGK HCCCCCHHHHHHHCC | 27.18 | 26437602 | |
128 | Phosphorylation | LTEGCLVSVDDLQNH CCCCEEEEHHHHHHH | 13.59 | - | |
226 | Phosphorylation | GNHEAVKSMFHTQMR CCHHHHHHHHHHHHH | 21.78 | 26437602 | |
298 | Phosphorylation | VKDNPKPSQEVVKEM CCCCCCCCHHHHHHH | 45.13 | 26437602 | |
309 | Phosphorylation | VKEMIQFSKDTLEKI HHHHHHHCHHHHHHH | 17.16 | 26503514 | |
312 | Phosphorylation | MIQFSKDTLEKIDKA HHHHCHHHHHHHHHH | 40.32 | 26503514 | |
321 | Phosphorylation | EKIDKARSEGLYHEV HHHHHHHHCCHHHHH | 40.66 | 26437602 | |
325 | Phosphorylation | KARSEGLYHEVVKLC HHHHCCHHHHHHHHH | 13.54 | 25404012 | |
346 | Phosphorylation | QEPVFADTNIYMLRM CCCCCCCCHHHHHHH | 21.78 | 22673903 | |
349 | Phosphorylation | VFADTNIYMLRMLSI CCCCCHHHHHHHHHH | 7.68 | 26437602 | |
355 | Phosphorylation | IYMLRMLSIVSEVLS HHHHHHHHHHHHHHH | 16.17 | 25262027 | |
358 | Phosphorylation | LRMLSIVSEVLSYLQ HHHHHHHHHHHHHHH | 21.96 | 25262027 | |
362 | Phosphorylation | SIVSEVLSYLQAFEE HHHHHHHHHHHHHHH | 29.04 | 25262027 | |
363 | Phosphorylation | IVSEVLSYLQAFEEA HHHHHHHHHHHHHHH | 9.93 | 25262027 | |
371 | Phosphorylation | LQAFEEASFYARRMV HHHHHHHHHHHHHHH | 23.28 | 25262027 | |
373 | Phosphorylation | AFEEASFYARRMVDG HHHHHHHHHHHHHCC | 9.19 | 25262027 | |
381 | Phosphorylation | ARRMVDGYMKLYHPN HHHHHCCCHHEECCC | 6.14 | 23607784 | |
385 | Phosphorylation | VDGYMKLYHPNNAQL HCCCHHEECCCHHHH | 15.09 | 23607784 |
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 SMYD1_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of SMYD1_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 SMYD1_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
SCRN3_HUMAN | SCRN3 | physical | 28514442 | |
PURA2_HUMAN | ADSS | physical | 28514442 | |
SPSB3_HUMAN | SPSB3 | physical | 28514442 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
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