DNM1L_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: DNM1L_RAT
• UniProt AC: O35303
• Protein Name: Dynamin-1-like protein
• Gene Name: Dnm1l
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 755
• Subcellular Localization: Cytoplasm, cytosol. Golgi apparatus. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome. Membrane, clathrin-coated pit. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane.
• Protein Description: Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Plays an important role in mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L) which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution..
• Protein Sequence: MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGVVTRRPLILQLVHVSPEDKRKTTGEENDPATWKNSRHLSKGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKVFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDNRRETKNVASAGGGIGDGGRIGDGGQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW

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	-------MEALIPVI -------CCCHHHHH	6.49	-
95	Phosphorylation	WKNSRHLSKGVEAEE HHCCCHHHCCCCHHH	22.65	28432305
105	Acetylation	VEAEEWGKFLHTKNK CCHHHHHHHHHHCCC	45.91	22902405
139	Phosphorylation	SGNNKGVSPEPIHLK CCCCCCCCCCCCEEE	32.01	23984901
173	Ubiquitination	VPVGDQPKDIELQIR ECCCCCCCCHHHHHH	66.75	-
296	Acetylation	LANRNGTKYLARTLN HHCCCCHHHHHHHHH	39.40	22902405
355	Phosphorylation	QLITKFATEYCNTIE HHHHHHHHHHHHCHH	30.53	28689409
381	Phosphorylation	CGGARICYIFHETFG HCCCEEEEEEHHHHC	12.30	-
539	Phosphorylation	RLARELPSAVSRDKS HHHHHHHHHHHCCCC	54.66	23984901
539 (in isoform 6)	Phosphorylation	-	54.66	25575281
542 (in isoform 6)	Phosphorylation	-	34.18	25575281
542	Phosphorylation	RELPSAVSRDKSSKV HHHHHHHHCCCCCCC	34.18	22673903
548 (in isoform 6)	Phosphorylation	-	66.32	25575281
561	Phosphorylation	APASQEPSPAASAEA CCCCCCCCCCCCHHH	26.81	-
585	Phosphorylation	RETKNVASAGGGIGD HHCCCHHHCCCCCCC	24.14	-
604	O-linked_Glycosylation	GDGGQEPTTGNWRGM CCCCCCCCCCCCCHH	46.73	22745122
605	O-linked_Glycosylation	DGGQEPTTGNWRGML CCCCCCCCCCCCHHH	38.95	22745122
616	Acetylation	RGMLKTSKAEELLAE CHHHCCCHHHHHHHH	66.12	-
626	Phosphorylation	ELLAEEKSKPIPIMP HHHHHHHCCCCCCCC	47.12	28689409
635	Phosphorylation	PIPIMPASPQKGHAV CCCCCCCCCCCCCCC	23.22	23991683
656	Phosphorylation	VPVARKLSAREQRDC HHHHHHCCHHHHHHH	28.45	21637291
663	S-nitrosocysteine	SAREQRDCEVIERLI CHHHHHHHHHHHHHH	4.98	-
663	S-nitrosylation	SAREQRDCEVIERLI CHHHHHHHHHHHHHH	4.98	-

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
585	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
635	S	Phosphorylation	Kinase	CDK1	P06493	PSP
635	S	Phosphorylation	Kinase	CDK1	P39951	Uniprot
635	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
635	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
656	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
656	S	Phosphorylation	Kinase	PKACA	P27791	PSP
656	S	Phosphorylation	Kinase	CAMK1	Q14012	GPS
656	S	Phosphorylation	Kinase	CAMK1	Q63450	Uniprot
656	S	Phosphorylation	Kinase	PRKD1	Q9WTQ1	PSP
656	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
656	S	Phosphorylation	Kinase	PKA	-	Uniprot
656	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
635	S	Phosphorylation	Phosphorylation on Ser-635 by CDK1 also promotes mitochondrial fission.	17301055
635	S	Phosphorylation	Phosphorylation on Ser-635 by PINK1 activates the GTPase activity and promotes mitochondrial fission (By similarity).	17301055
656	S	Phosphorylation	It also decreases phosphorylation at Ser-656.	28463107
656	S	Phosphorylation	Phosphorylated in a circadian manner at Ser-656 (By similarity).	28463107
656	S	Phosphorylation	Phosphorylation on Ser-656 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation (By similarity).	28463107

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of DNM1L_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
B2CL1_RAT	Bcl2l1	physical	18250306

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Mitotic phosphorylation of dynamin-related GTPase Drp1 participatesin mitochondrial fission.";
Taguchi N., Ishihara N., Jofuku A., Oka T., Mihara K.;
J. Biol. Chem. 282:11521-11529(2007).
Cited for: PHOSPHORYLATION AT SER-635, FUNCTION, AND MUTAGENESIS OF SER-71;SER-139; SER-149 AND SER-635.
PubMed: 17301055