| UniProt ID | DAB1_HUMAN | |
|---|---|---|
| UniProt AC | O75553 | |
| Protein Name | Disabled homolog 1 | |
| Gene Name | DAB1 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 588 | |
| Subcellular Localization | ||
| Protein Description | Adapter molecule functioning in neural development. May regulate SIAH1 activity.. | |
| Protein Sequence | MSTETELQVAVKTSAKKDSRKKGQDRSEATLIKRFKGEGVRYKAKLIGIDEVSAARGDKLCQDSMMKLKGVVAGARSKGEHKQKIFLTISFGGIKIFDEKTGALQHHHAVHEISYIAKDITDHRAFGYVCGKEGNHRFVAIKTAQAAEPVILDLRDLFQLIYELKQREELEKKAQKDKQCEQAVYQTILEEDVEDPVYQYIVFEAGHEPIRDPETEENIYQVPTSQKKEGVYDVPKSQPVSNGYSFEDFEERFAAATPNRNLPTDFDEIFEATKAVTQLELFGDMSTPPDITSPPTPATPGDAFIPSSSQTLPASADVFSSVPFGTAAVPSGYVAMGAVLPSFWGQQPLVQQQMVMGAQPPVAQVMPGAQPIAWGQPGLFPATQQPWPTVAGQFPPAAFMPTQTVMPLPAAMFQGPLTPLATVPGTSDSTRSSPQTDKPRQKMGKETFKDFQMAQPPPVPSRKPDQPSLTCTSEAFSSYFNKVGVAQDTDDCDDFDISQLNLTPVTSTTPSTNSPPTPAPRQSSPSKSSASHASDPTTDDIFEEGFESPSKSEEQEAPDGSQASSNSDPFGEPSGEPSGDNISPQAGS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 43 | Ubiquitination | KGEGVRYKAKLIGID CCCCCCEEEEEECCC | 28.60 | - | |
| 45 | Ubiquitination | EGVRYKAKLIGIDEV CCCCEEEEEECCCHH | 36.16 | - | |
| 64 | Phosphorylation | GDKLCQDSMMKLKGV CCCCCHHHHHHHHHH | 8.56 | 26657352 | |
| 77 | Phosphorylation | GVVAGARSKGEHKQK HHHHCCCCCCCCCCC | 44.47 | 26657352 | |
| 84 | Sumoylation | SKGEHKQKIFLTISF CCCCCCCCEEEEEEE | 39.98 | - | |
| 185 (in isoform 5) | Phosphorylation | - | 11.71 | 28674419 | |
| 185 (in isoform 4) | Phosphorylation | - | 11.71 | 28674419 | |
| 185 | Phosphorylation | KQCEQAVYQTILEED HHHHHHHHHHHHHHH | 11.71 | 10959835 | |
| 198 | Phosphorylation | EDVEDPVYQYIVFEA HHCCCCCCEEEEEEC | 10.86 | 11279201 | |
| 200 | Phosphorylation | VEDPVYQYIVFEAGH CCCCCCEEEEEECCC | 4.95 | 10959835 | |
| 220 | Phosphorylation | PETEENIYQVPTSQK CCCCCCEEECCCCCC | 18.29 | 19116273 | |
| 224 | Phosphorylation | ENIYQVPTSQKKEGV CCEEECCCCCCCCCC | 44.95 | 26434552 | |
| 225 | Phosphorylation | NIYQVPTSQKKEGVY CEEECCCCCCCCCCC | 33.65 | 26434552 | |
| 232 | Phosphorylation | SQKKEGVYDVPKSQP CCCCCCCCCCCCCCC | 23.29 | 25884760 | |
| 491 | Phosphorylation | GVAQDTDDCDDFDIS CCCCCCCCCCCCCHH | 39.58 | 12077184 | |
| 506 | Phosphorylation | QLNLTPVTSTTPSTN HCCCEECCCCCCCCC | 22.89 | - | |
| 515 | Phosphorylation | TTPSTNSPPTPAPRQ CCCCCCCCCCCCCCC | 38.56 | 12077184 | |
| 524 | Phosphorylation | TPAPRQSSPSKSSAS CCCCCCCCCCCCCCC | 25.50 | 19472218 | |
| 526 | Phosphorylation | APRQSSPSKSSASHA CCCCCCCCCCCCCCC | 47.30 | - | |
| 548 | Phosphorylation | IFEEGFESPSKSEEQ HHHHCCCCCCCCCCC | 32.01 | 12077184 |
| Modified Location | Modified Residue | Modification | Type of Upstream Proteins | Gene Name of Upstream Proteins | UniProt AC of Upstream Proteins | Sources |
|---|---|---|---|---|---|---|
| 524 | S | Phosphorylation | Kinase | CDK5 | Q00535 | Uniprot |
| 524 | S | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
| 524 | S | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
| 548 | S | Phosphorylation | Kinase | CDK-FAMILY | - | GPS |
| 548 | S | Phosphorylation | Kinase | CDK_GROUP | - | PhosphoELM |
| - | K | Ubiquitination | E3 ubiquitin ligase | SOCS4 | Q8WXH5 | PMID:24210661 |
| Modified Location | Modified Residue | Modification | Function | Reference |
|---|---|---|---|---|
| 524 | S | Phosphorylation |
| - |
* 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 DAB1_HUMAN !! | ||||||
| Kegg Disease | ||||||
|---|---|---|---|---|---|---|
| There are no disease associations of PTM sites. | ||||||
| OMIM Disease | ||||||
| There are no disease associations of PTM sites. | ||||||
| Kegg Drug | ||||||
| There are no disease associations of PTM sites. | ||||||
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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