DYLT1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DYLT1_MOUSE
• UniProt AC: P51807
• Protein Name: Dynein light chain Tctex-type 1
• Gene Name: Dynlt1
• Organism: Mus musculus (Mouse).
• Sequence Length: 113
• Subcellular Localization: Golgi apparatus. Cytoplasm. Cytoplasm, cytoskeleton, spindle. Localizes to mitotic spindles..
• Protein Description: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. Binds to transport cargos and is involved in apical cargo transport such as rhodopsin-bearing vesicles in polarized epithelia (By similarity). May also be a accessory component of axonemal dynein. Plays an important role in male germ cell development and function. Candidate for involvement in male sterility.; Plays a role in neuronal morphogenesis; the function is independent of cytoplasmic dynein and seems to be coupled to regulation of the actin cytoskeleton by enhancing Rac1 activity. The function in neurogenesis may be regulated by association with a G-protein beta-gamma dimer. May function as a receptor-independent activator of heterotrimeric G-protein signaling; the activation appears to be independent of a nucleotide exchange. Plays a role in regulating neurogenesis; inhibits the genesis of neurons from precursor cells during cortical development presumably by antagonizing ARHGEF2. Unrelated to the role in retrograde microtubule-associated movement may play a role in the dimerization of cytoplasmic proteins/domains such as for ACVR2B. Binds to the cytoplasmic domain of ACVR2B and, in vitro, inhibits ACVR2B signaling. Involved in the regulation of mitotic spindle orientation..
• Protein Sequence: MEDFQASEETAFVVDEVSSIVKEAIESAIGGNAYQHSKVNQWTTNVLEQTLSQLTKLGRPFKYIVTCVIMQKNGAGLHSASSCFWDSSTDGSCTVRWENKTMYCIVSTFGLSI

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	-------MEDFQASE -------CCCCCCCH	11.42	-
7	Phosphorylation	-MEDFQASEETAFVV -CCCCCCCHHHEEEH	25.78	30387612
38	Ubiquitination	GNAYQHSKVNQWTTN CCCCCHHHHCHHHHH	42.98	-
56	Ubiquitination	QTLSQLTKLGRPFKY HHHHHHHHCCCCCEE	58.50	-
62	Ubiquitination	TKLGRPFKYIVTCVI HHCCCCCEEEEEEEE	36.43	-
94	Phosphorylation	SSTDGSCTVRWENKT CCCCCCEEEEEECCC	18.14	22405273
100	Ubiquitination	CTVRWENKTMYCIVS EEEEEECCCEEEEEE	24.13	-

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

Oops, there are no upstream regulatory protein records of DYLT1_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of DYLT1_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DYLT1_MOUSE !!

Protein-Protein Interaction

Oops, there are no PPI records of DYLT1_MOUSE !!

Drug and Disease Associations

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