DLGP5_MOUSE - dbPTM
DLGP5_MOUSE - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
65PhosphorylationELGNIHETSQDLSPE
ECCCCCCCCCCCCHH
19.9522942356
66PhosphorylationLGNIHETSQDLSPEK
CCCCCCCCCCCCHHH
20.7927566939
70PhosphorylationHETSQDLSPEKASSK
CCCCCCCCHHHHCCC
39.0227087446
75PhosphorylationDLSPEKASSKTRSVK
CCCHHHHCCCCCHHH
43.3625619855
76PhosphorylationLSPEKASSKTRSVKM
CCHHHHCCCCCHHHH
42.7925619855
80PhosphorylationKASSKTRSVKMVLSD
HHCCCCCHHHHHHHH
31.18-
156PhosphorylationGRITRSKTKEYMEQT
CCCCHHHCHHHHHHH
30.2925266776
167PhosphorylationMEQTKIGSRNVPKAT
HHHHCCCCCCCCCCC
24.93-
201PhosphorylationMQPVLFTSGKGTESA
HCCEEECCCCCCHHH
31.04-
219PhosphorylationRAKLMARTVSSTTRK
HHHHHHHHCCCCCCC
18.4014729942
224PhosphorylationARTVSSTTRKPVTRA
HHHCCCCCCCCCCCC
38.3514729942
291PhosphorylationGVFREVESLPATAPA
CHHEEEECCCCCCCC
44.84-
321PhosphorylationQPPCGLKSYQVAPLS
CCCCCCCEEEECCCC
26.3226643407
322PhosphorylationPPCGLKSYQVAPLSP
CCCCCCEEEECCCCC
12.8626643407
328PhosphorylationSYQVAPLSPRSANAF
EEEECCCCCCCCCCC
19.7426824392
331PhosphorylationVAPLSPRSANAFLTP
ECCCCCCCCCCCCCC
29.2926643407
337PhosphorylationRSANAFLTPNCDWNQ
CCCCCCCCCCCCHHH
13.1526643407
386PhosphorylationLNQKGASTSDSNHAS
HHCCCCCCCCCCCCE
35.70-
598PhosphorylationAGFFRIESPVKSFSV
CCCEEEECCCCEEEE
32.4026239621
607PhosphorylationVKSFSVLSSERRSQR
CCEEEECCCHHHHHH
28.18-
612PhosphorylationVLSSERRSQRFGTPL
ECCCHHHHHHCCCCC
31.7424759943
617PhosphorylationRRSQRFGTPLSASKV
HHHHHCCCCCCHHHC
20.5321659605
620PhosphorylationQRFGTPLSASKVVPE
HHCCCCCCHHHCCCC
31.5321082442
622PhosphorylationFGTPLSASKVVPEGR
CCCCCCHHHCCCCCH
23.7028066266
657PhosphorylationKSEHVDRTFSDGLES
CCCCCCHHHCCCCHH
24.0325266776
659PhosphorylationEHVDRTFSDGLESRC
CCCCHHHCCCCHHCC
30.1022942356
671PhosphorylationSRCHVEDTPCPGEQD
HCCCCCCCCCCCCCC
17.1825619855
679PhosphorylationPCPGEQDSSDIEHDV
CCCCCCCCHHCCCCH
29.6027087446
680PhosphorylationCPGEQDSSDIEHDVN
CCCCCCCHHCCCCHH
51.3927087446
728PhosphorylationEGASTAVTSQDLLMS
CCCCCCCCCHHHHHC
20.43-
743PhosphorylationNPETNTSSQSNTSQE
CCCCCCCCCCCCCHH
35.27-
777PhosphorylationLLEPPGLSCTSPCTR
CCCCCCCCCCCCCCC
22.6725619855
779PhosphorylationEPPGLSCTSPCTREE
CCCCCCCCCCCCCCC
32.1225619855
780PhosphorylationPPGLSCTSPCTREET
CCCCCCCCCCCCCCC
23.4625619855
783PhosphorylationLSCTSPCTREETRQP
CCCCCCCCCCCCCCC
44.4925619855
797PhosphorylationPDRSRQFSFGGDLIL
CCCCCCCCCCCCEEE
18.0427600695
806PhosphorylationGGDLILFSPL-----
CCCEEEEECC-----
23.1126370283

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources
328SPhosphorylationKinaseMAPK1P63085
GPS
607SPhosphorylationKinaseAURKAP97477
Uniprot
797SPhosphorylationKinaseAURKAP97477
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DLGP5_MOUSE !!

Disease-associated PTM Sites based on SAP

* 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 !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of DLGP5_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DLGP5_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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.

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