| UniProt ID | DLGP5_MOUSE | |
|---|---|---|
| UniProt AC | Q8K4R9 | |
| Protein Name | Disks large-associated protein 5 | |
| Gene Name | Dlgap5 | |
| Organism | Mus musculus (Mouse). | |
| Sequence Length | 808 | |
| Subcellular Localization | Nucleus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Localizes to the spindle in mitotic cells. Colocalizes with CDH1 at sites of cell-cell contact in intestinal epithelial cells (By similarity).. | |
| Protein Description | Potential cell cycle regulator that may play a role in carcinogenesis of cancer cells. Mitotic phosphoprotein regulated by the ubiquitin-proteasome pathway. Key regulator of adherens junction integrity and differentiation that may be involved in CDH1-mediated adhesion and signaling in epithelial cells (By similarity).. | |
| Protein Sequence | MLVSRFASRFRKDSSTEMVRTNLAHRKSLSQKENRHRVYERNRHFGLKDVNIPLEGRELGNIHETSQDLSPEKASSKTRSVKMVLSDQRKQLLQKYKEEKQLQKLKEQREKAKRGVFKVGLYRPAAPGFLVTDQRGAKAEPEKAFPHTGRITRSKTKEYMEQTKIGSRNVPKATQSDQRQTSEKQPLDRERKVMQPVLFTSGKGTESAATQRAKLMARTVSSTTRKPVTRATNEKGSERMRPSGGRPAKKPEGKPDKVIPSKVERDEKHLDSQTRETSEMGPLGVFREVESLPATAPAQGKERKSFAPKHCVFQPPCGLKSYQVAPLSPRSANAFLTPNCDWNQLRPEVFSTTTQDKANEILVQQGLESLTDRSKEHVLNQKGASTSDSNHASVKGVPCSEGSEGQTSQPPHDVPYFRKILQSETDRLTSHCLEWEGKLDLDISDEAKGLIRTTVGQTRLLIKERFRQFEGLVDNCEYKRGEKETTCTDLDGFWDMVSFQVDDVNQKFNNLIKLEASGWKDSNNPSKKVLRKKIVPGRTSKAKQDDDGRAAARSRLAAIKNAMKGRPQQEVQAHAAAPETTKEVDKIVFDAGFFRIESPVKSFSVLSSERRSQRFGTPLSASKVVPEGRAAGDLLRQKMPLKKPDPQSSKSEHVDRTFSDGLESRCHVEDTPCPGEQDSSDIEHDVNKINVKMDCFSVETNLPLPAGDANTNQKEAISAVEGASTAVTSQDLLMSNPETNTSSQSNTSQEEAEASQSVLLHKSLTSECHLLEPPGLSCTSPCTREETRQPDRSRQFSFGGDLILFSPL | |
| 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 |
|---|---|---|---|---|---|
| 65 | Phosphorylation | ELGNIHETSQDLSPE ECCCCCCCCCCCCHH | 19.95 | 22942356 | |
| 66 | Phosphorylation | LGNIHETSQDLSPEK CCCCCCCCCCCCHHH | 20.79 | 27566939 | |
| 70 | Phosphorylation | HETSQDLSPEKASSK CCCCCCCCHHHHCCC | 39.02 | 27087446 | |
| 75 | Phosphorylation | DLSPEKASSKTRSVK CCCHHHHCCCCCHHH | 43.36 | 25619855 | |
| 76 | Phosphorylation | LSPEKASSKTRSVKM CCHHHHCCCCCHHHH | 42.79 | 25619855 | |
| 80 | Phosphorylation | KASSKTRSVKMVLSD HHCCCCCHHHHHHHH | 31.18 | - | |
| 156 | Phosphorylation | GRITRSKTKEYMEQT CCCCHHHCHHHHHHH | 30.29 | 25266776 | |
| 167 | Phosphorylation | MEQTKIGSRNVPKAT HHHHCCCCCCCCCCC | 24.93 | - | |
| 201 | Phosphorylation | MQPVLFTSGKGTESA HCCEEECCCCCCHHH | 31.04 | - | |
| 219 | Phosphorylation | RAKLMARTVSSTTRK HHHHHHHHCCCCCCC | 18.40 | 14729942 | |
| 224 | Phosphorylation | ARTVSSTTRKPVTRA HHHCCCCCCCCCCCC | 38.35 | 14729942 | |
| 291 | Phosphorylation | GVFREVESLPATAPA CHHEEEECCCCCCCC | 44.84 | - | |
| 321 | Phosphorylation | QPPCGLKSYQVAPLS CCCCCCCEEEECCCC | 26.32 | 26643407 | |
| 322 | Phosphorylation | PPCGLKSYQVAPLSP CCCCCCEEEECCCCC | 12.86 | 26643407 | |
| 328 | Phosphorylation | SYQVAPLSPRSANAF EEEECCCCCCCCCCC | 19.74 | 26824392 | |
| 331 | Phosphorylation | VAPLSPRSANAFLTP ECCCCCCCCCCCCCC | 29.29 | 26643407 | |
| 337 | Phosphorylation | RSANAFLTPNCDWNQ CCCCCCCCCCCCHHH | 13.15 | 26643407 | |
| 386 | Phosphorylation | LNQKGASTSDSNHAS HHCCCCCCCCCCCCE | 35.70 | - | |
| 598 | Phosphorylation | AGFFRIESPVKSFSV CCCEEEECCCCEEEE | 32.40 | 26239621 | |
| 607 | Phosphorylation | VKSFSVLSSERRSQR CCEEEECCCHHHHHH | 28.18 | - | |
| 612 | Phosphorylation | VLSSERRSQRFGTPL ECCCHHHHHHCCCCC | 31.74 | 24759943 | |
| 617 | Phosphorylation | RRSQRFGTPLSASKV HHHHHCCCCCCHHHC | 20.53 | 21659605 | |
| 620 | Phosphorylation | QRFGTPLSASKVVPE HHCCCCCCHHHCCCC | 31.53 | 21082442 | |
| 622 | Phosphorylation | FGTPLSASKVVPEGR CCCCCCHHHCCCCCH | 23.70 | 28066266 | |
| 657 | Phosphorylation | KSEHVDRTFSDGLES CCCCCCHHHCCCCHH | 24.03 | 25266776 | |
| 659 | Phosphorylation | EHVDRTFSDGLESRC CCCCHHHCCCCHHCC | 30.10 | 22942356 | |
| 671 | Phosphorylation | SRCHVEDTPCPGEQD HCCCCCCCCCCCCCC | 17.18 | 25619855 | |
| 679 | Phosphorylation | PCPGEQDSSDIEHDV CCCCCCCCHHCCCCH | 29.60 | 27087446 | |
| 680 | Phosphorylation | CPGEQDSSDIEHDVN CCCCCCCHHCCCCHH | 51.39 | 27087446 | |
| 728 | Phosphorylation | EGASTAVTSQDLLMS CCCCCCCCCHHHHHC | 20.43 | - | |
| 743 | Phosphorylation | NPETNTSSQSNTSQE CCCCCCCCCCCCCHH | 35.27 | - | |
| 777 | Phosphorylation | LLEPPGLSCTSPCTR CCCCCCCCCCCCCCC | 22.67 | 25619855 | |
| 779 | Phosphorylation | EPPGLSCTSPCTREE CCCCCCCCCCCCCCC | 32.12 | 25619855 | |
| 780 | Phosphorylation | PPGLSCTSPCTREET CCCCCCCCCCCCCCC | 23.46 | 25619855 | |
| 783 | Phosphorylation | LSCTSPCTREETRQP CCCCCCCCCCCCCCC | 44.49 | 25619855 | |
| 797 | Phosphorylation | PDRSRQFSFGGDLIL CCCCCCCCCCCCEEE | 18.04 | 27600695 | |
| 806 | Phosphorylation | GGDLILFSPL----- CCCEEEEECC----- | 23.11 | 26370283 |
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of DLGP5_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 DLGP5_MOUSE !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of DLGP5_MOUSE !! | ||||
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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| Phosphorylation | |
| Reference | PubMed |
| "Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry."; Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.; Mol. Cell. Proteomics 8:904-912(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-328, AND MASSSPECTROMETRY. | |
| "Identification of phosphoproteins and their phosphorylation sites inthe WEHI-231 B lymphoma cell line."; Shu H., Chen S., Bi Q., Mumby M., Brekken D.L.; Mol. Cell. Proteomics 3:279-286(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-219 AND THR-224, ANDMASS SPECTROMETRY. | |