DIAP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DIAP1_MOUSE
• UniProt AC: O08808
• Protein Name: Protein diaphanous homolog 1
• Gene Name: Diaph1
• Organism: Mus musculus (Mouse).
• Sequence Length: 1255
• Subcellular Localization: Cell membrane . Cell projection, ruffle membrane . Cytoplasm, cytoskeleton . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome . Cytoplasm, cytoskeleton, spindle . Membrane ruffles, especially at the tip of ruffles, of motile cells.
• Protein Description: Acts in a Rho-dependent manner to recruit PFY1 to the membrane. Required for the assembly of F-actin structures, such as actin cables and stress fibers. Nucleates actin filaments. Binds to the barbed end of the actin filament and slows down actin polymerization and depolymerization. Required for cytokinesis, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics. Functions as a scaffold protein for MAPRE1 and APC to stabilize microtubules and promote cell migration. Has neurite outgrowth promoting activity. [PubMed: 10678165]
• Protein Sequence: MEPSGGGLGPGRGTRDKKKGRSPDELPATGGDGGKHKKFLERFTSMRIKKEKEKPNSAHRNSSASYGDDPTAQSLQDISDEQVLVLFEQMLVDMNLNEEKQQPLREKDIVIKREMVSQYLHTSKAGMNQKESSRSAMMYIQELRSGLRDMHLLSCLESLRVSLNNNPVSWVQTFGAEGLASLLDILKRLHDEKEETSGNYDSRNQHEIIRCLKAFMNNKFGIKTMLETEEGILLLVRAMDPAVPNMMIDAAKLLSALCILPQPEDMNERVLEAMTERAEMDEVERFQPLLDGLKSGTSIALKVGCLQLINALITPAEELDFRVHIRSELMRLGLHQVLQELREIENEDMKVQLCVFDEQGDEDFFDLKGRLDDIRMEMDDFGEVFQIILNTVKDSKAEPHFLSILQHLLLVRNDYEARPQYYKLIEECVSQIVLHKNGTDPDFKCRHLQIDIERLVDQMIDKTKVEKSEAKATELEKKLDSELTARHELQVEMKKMENDFEQKLQDLQGEKDALDSEKQQITAQKQDLEAEVSKLTGEVAKLSKELEDAKNEMASLSAVVVAPSVSSSAAVPPAPPLPGDSGTVIPPPPPPPPLPGGVVPPSPPLPPGTCIPPPPPLPGGACIPPPPQLPGSAAIPPPPPLPGVASIPPPPPLPGATAIPPPPPLPGATAIPPPPPLPGGTGIPPPPPPLPGSVGVPPPPPLPGGPGLPPPPPPFPGAPGIPPPPPGMGVPPPPPFGFGVPAAPVLPFGLTPKKVYKPEVQLRRPNWSKFVAEDLSQDCFWTKVKEDRFENNELFAKLTLAFSAQTKTSKAKKDQEGGEEKKSVQKKKVKELKVLDSKTAQNLSIFLGSFRMPYQEIKNVILEVNEAVLTESMIQNLIKQMPEPEQLKMLSELKEEYDDLAESEQFGVVMGTVPRLRPRLNAILFKLQFSEQVENIKPEIVSVTAACEELRKSENFSSLLELTLLVGNYMNAGSRNAGAFGFNISFLCKLRDTKSADQKMTLLHFLAELCENDHPEVLKFPDELAHVEKASRVSAENLQKSLDQMKKQIADVERDVQNFPAATDEKDKFVEKMTSFVKDAQEQYNKLRMMHSNMETLYKELGDYFVFDPKKLSVEEFFMDLHNFRNMFLQAVKENQKRRETEEKMRRAKLAKEKAEKERLEKQQKREQLIDMNAEGDETGVMDSLLEALQSGAAFRRKRGPRQVNRKAGCAVTSLLASELTKDDAMAPGPVKVPKKSEGVPTILEEAKELVGRAS

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
1	Acetylation	-------MEPSGGGL -------CCCCCCCC	59.92	-
14	Phosphorylation	GLGPGRGTRDKKKGR CCCCCCCCCCCCCCC	34.04	29176673
22	Phosphorylation	RDKKKGRSPDELPAT CCCCCCCCCCCCCCC	45.42	25521595
29	Phosphorylation	SPDELPATGGDGGKH CCCCCCCCCCCCCHH	39.49	23984901
45	Phosphorylation	KFLERFTSMRIKKEK HHHHHHHHHCCCCCC	11.89	30387612
415	Phosphorylation	LLLVRNDYEARPQYY HHHHCCCCCCCHHHH	18.29	22345495
494	Ubiquitination	HELQVEMKKMENDFE HHHHHHHHHHHCHHH	35.15	-
541	Ubiquitination	KLTGEVAKLSKELED HHHHHHHHHHHHHHH	59.47	-
751	Phosphorylation	PVLPFGLTPKKVYKP CCCCCCCCCCCCCCC	33.18	-
957	Phosphorylation	LRKSENFSSLLELTL HHCCCCHHHHHHHHH	31.49	-
969	Phosphorylation	LTLLVGNYMNAGSRN HHHHHHHHCCCCCCC	5.94	-
1040	Acetylation	VSAENLQKSLDQMKK CCHHHHHHHHHHHHH	57.03	-
1086	Acetylation	DAQEQYNKLRMMHSN HHHHHHHHHHHHHHC	32.32	-
1104	Phosphorylation	LYKELGDYFVFDPKK HHHHHCCCCCCCHHH	10.39	17947660
1237	Phosphorylation	PVKVPKKSEGVPTIL CCCCCCCCCCCCCHH	45.79	29176673
1255	Phosphorylation	KELVGRAS------- HHHHCCCC-------	39.12	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of DIAP1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
751	T	Phosphorylation	Phosphorylation at Thr-751 is stimulated by cAMP and regulates stability, complex formation and mitochondrial movement (By similarity).	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of DIAP1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of DIAP1_MOUSE !!

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative time-resolved phosphoproteomic analysis of mast cellsignaling.";
Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,Kawakami T., Salomon A.R.;
J. Immunol. 179:5864-5876(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1104, AND MASSSPECTROMETRY.
PubMed: 17947660