dbPTM

DNM1L_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNM1L_MOUSE
UniProt AC	Q8K1M6
Protein Name	Dynamin-1-like protein
Gene Name	Dnm1l
Organism	Mus musculus (Mouse).
Sequence Length	742
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	MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGVVTRRPLILQLVHVSPEDKRKTTGEENGKFQSWRVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKVFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAGSRDKSSKVPSALAPASQEPPPAASAEADGKLIQDNRRETKNVPSAGGGIGDGGQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEALIPVI -------CCCHHHHH	6.49	-
71	Phosphorylation	ILQLVHVSPEDKRKT EEEEEECCHHHHCCC	14.01	19854140
95	Phosphorylation	SWRVEAEEWGKFLHT EEEEEHHHHHHHHHH	69.45	-
132	Phosphorylation	SGNNKGVSPEPIHLK CCCCCCCCCCCCEEE	32.01	29899451
139	Acetylation	SPEPIHLKVFSPNVV CCCCCEEEEECCCEE	27.37	23954790
142	Phosphorylation	PIHLKVFSPNVVNLT CCEEEEECCCEEEEE	20.67	25619855
149	Phosphorylation	SPNVVNLTLVDLPGM CCCEEEEEEEECCCC	21.38	25619855
166	Ubiquitination	VPVGDQPKDIELQIR ECCCCCCCCHHHHHH	66.75	22790023
244	Ubiquitination	MGRVIPVKLGIIGVV HCCCCCEEEEEEEEE	35.32	22790023
267	Phosphorylation	NKKSVTDSIRDEYAF CCCCCCHHHHHHHHH	15.34	29514104
311	Ubiquitination	RDCLPELKTRINVLA HHHHHHHHHHHHHHH	33.81	22790023
351	S-nitrosocysteine	TKFATEYCNTIEGTA HHHHHHHHHCHHCCC	2.70	-
351	S-nitrosylation	TKFATEYCNTIEGTA HHHHHHHHHCHHCCC	2.70	21278135
367	S-nitrosocysteine	YIETSELCGGARICY HHHHHHHHCCCEEEE	4.08	-
367	S-nitrosylation	YIETSELCGGARICY HHHHHHHHCCCEEEE	4.08	19101475
428 (in isoform 4)	Phosphorylation	-	42.46	25266776
431 (in isoform 4)	Phosphorylation	-	72.41	27600695
455	Nitration	IIQHCSNYSTQELLR HHHHHCCCCHHHHHC	9.22	-
526 (in isoform 3)	Phosphorylation	-	6.34	25338131
529 (in isoform 3)	Phosphorylation	-	60.47	27818261
532	Phosphorylation	RLARELPSAGSRDKS HHHHHCCCCCCCCCC	58.86	28833060
532 (in isoform 2)	Phosphorylation	-	58.86	25266776
535 (in isoform 3)	Phosphorylation	-	36.70	23684622
535	Phosphorylation	RELPSAGSRDKSSKV HHCCCCCCCCCCCCC	36.70	26824392
535 (in isoform 2)	Phosphorylation	-	36.70	27600695
542	Phosphorylation	SRDKSSKVPSALAPA CCCCCCCCCCCCCCC	4.97	24719451
548	Phosphorylation	KVPSALAPASQEPPP CCCCCCCCCCCCCCC	33.04	-
578	Phosphorylation	RETKNVPSAGGGIGD CCCCCCCCCCCCCCC	34.95	-
591	Phosphorylation	GDGGQEPTTGNWRGM CCCCCCCCCCCCCHH	46.73	-
591	O-linked_Glycosylation	GDGGQEPTTGNWRGM CCCCCCCCCCCCCHH	46.73	28528544
592	Phosphorylation	DGGQEPTTGNWRGML CCCCCCCCCCCCHHH	38.95	-
592	O-linked_Glycosylation	DGGQEPTTGNWRGML CCCCCCCCCCCCHHH	38.95	28528544
600	Malonylation	GNWRGMLKTSKAEEL CCCCHHHCCCHHHHH	41.69	26320211
601	Phosphorylation	NWRGMLKTSKAEELL CCCHHHCCCHHHHHH	31.34	29899451
602	Phosphorylation	WRGMLKTSKAEELLA CCHHHCCCHHHHHHH	28.42	30387612
603	Acetylation	RGMLKTSKAEELLAE CHHHCCCHHHHHHHH	66.12	23806337
613	Phosphorylation	ELLAEEKSKPIPIMP HHHHHHHCCCCCCCC	47.12	25619855
622	Phosphorylation	PIPIMPASPQKGHAV CCCCCCCCCCCCCCC	23.22	24925903
643	Phosphorylation	VPVARKLSAREQRDC HHHHHHCCHHHHHHH	28.45	17721437
650	S-nitrosocysteine	SAREQRDCEVIERLI CHHHHHHHHHHHHHH	4.98	-
650	S-nitrosylation	SAREQRDCEVIERLI CHHHHHHHHHHHHHH	4.98	21278135

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
622	S	Phosphorylation	Kinase	CAMK2A	P11798	PSP
622	S	Phosphorylation	Kinase	CAMK2A	P11275	PSP
622	S	Phosphorylation	Kinase	RIPK1	Q60855	PSP
643	S	Phosphorylation	Kinase	CAMK1	Q91YS8	Uniprot
643	S	Phosphorylation	Kinase	PKA	-	Uniprot
-	K	Ubiquitination	E3 ubiquitin ligase	Marchf5	Q3KNM2	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
622	S	Phosphorylation	21183079
Phosphorylation on Ser-622 by Pink1 activates the GTPase activity and promotes mitochondrial fission.
643	S	Phosphorylation	-
It also decreases phosphorylation at Ser-643 (By similarity).
643	S	Phosphorylation	32484300
Phosphorylated in a circadian manner at Ser-643 (By similarity).
643	S	Phosphorylation	32484300
Phosphorylation on Ser-643 inhibits mitochondrial fission probably through preventing intramolecular interaction (By similarity).

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 DNM1L_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AKAP1_MOUSE	Akap1	physical	22099302
LRRK2_MOUSE	Lrrk2	physical	22639965
DNM1L_MOUSE	Dnm1l	physical	20585624

Drug and Disease Associations

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

Regulatory Network of DNM1L_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, AND MASSSPECTROMETRY.	19367708 [Abstract]

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