dbPTM

DNM1L_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DNM1L_HUMAN
UniProt AC	O00429
Protein Name	Dynamin-1-like protein
Gene Name	DNM1L
Organism	Homo sapiens (Human).
Sequence Length	736
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. [PubMed: 26992161 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.; Isoform 1: Inhibits peroxisomal division when overexpressed.; Isoform 4: Inhibits peroxisomal division when overexpressed.]
Protein Sequence	MEALIPVINKLQDVFNTVGADIIQLPQIVVVGTQSSGKSSVLESLVGRDLLPRGTGIVTRRPLILQLVHVSQEDKRKTTGEENGVEAEEWGKFLHTKNKLYTDFDEIRQEIENETERISGNNKGVSPEPIHLKIFSPNVVNLTLVDLPGMTKVPVGDQPKDIELQIRELILRFISNPNSIILAVTAANTDMATSEALKISREVDPDGRRTLAVITKLDLMDAGTDAMDVLMGRVIPVKLGIIGVVNRSQLDINNKKSVTDSIRDEYAFLQKKYPSLANRNGTKYLARTLNRLLMHHIRDCLPELKTRINVLAAQYQSLLNSYGEPVDDKSATLLQLITKFATEYCNTIEGTAKYIETSELCGGARICYIFHETFGRTLESVDPLGGLNTIDILTAIRNATGPRPALFVPEVSFELLVKRQIKRLEEPSLRCVELVHEEMQRIIQHCSNYSTQELLRFPKLHDAIVEVVTCLLRKRLPVTNEMVHNLVAIELAYINTKHPDFADACGLMNNNIEEQRRNRLARELPSAVSRDKSSKVPSALAPASQEPSPAASAEADGKLIQDSRRETKNVASGGGGVGDGVQEPTTGNWRGMLKTSKAEELLAEEKSKPIPIMPASPQKGHAVNLLDVPVPVARKLSAREQRDCEVIERLIKSYFLIVRKNIQDSVPKAVMHFLVNHVKDTLQSELVGQLYKSSLLDDLLTESEDMAQRRKEAADMLKALQGASQIIAEIRETHLW

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEALIPVI -------CCCHHHHH	6.49	22223895
1	Sulfoxidation	-------MEALIPVI -------CCCHHHHH	6.49	28183972
1	Sulfoxidation	-------MEALIPVI -------CCCHHHHH	6.49	28183972
38	Sumoylation	VGTQSSGKSSVLESL EEECCCCCHHHHHHH	41.32	-
40	Phosphorylation	TQSSGKSSVLESLVG ECCCCCHHHHHHHHC	33.92	21712546
44	Phosphorylation	GKSSVLESLVGRDLL CCHHHHHHHHCCCCC	24.97	21712546
55	O-linked_Glycosylation	RDLLPRGTGIVTRRP CCCCCCCCCCCCCCC	25.64	28510447
78	Phosphorylation	SQEDKRKTTGEENGV CHHHHCCCCCCCCCC	44.03	19690332
79	Phosphorylation	QEDKRKTTGEENGVE HHHHCCCCCCCCCCC	45.70	19690332
92	Ubiquitination	VEAEEWGKFLHTKNK CCHHHHHHHHHHCCC	45.91	-
92	Acetylation	VEAEEWGKFLHTKNK CCHHHHHHHHHHCCC	45.91	23236377
97	Ubiquitination	WGKFLHTKNKLYTDF HHHHHHHCCCCCCCH	41.14	-
99	Ubiquitination	KFLHTKNKLYTDFDE HHHHHCCCCCCCHHH	44.41	-
102	Phosphorylation	HTKNKLYTDFDEIRQ HHCCCCCCCHHHHHH	40.40	-
108	Methylation	YTDFDEIRQEIENET CCCHHHHHHHHHHHH	26.49	-
123	Ubiquitination	ERISGNNKGVSPEPI HHCCCCCCCCCCCCC	65.77	-
126	Phosphorylation	SGNNKGVSPEPIHLK CCCCCCCCCCCCEEE	32.01	25159151
133	Ubiquitination	SPEPIHLKIFSPNVV CCCCCEEEEECCCEE	27.78	-
136	Phosphorylation	PIHLKIFSPNVVNLT CCEEEEECCCEEEEE	21.02	-
160	Ubiquitination	VPVGDQPKDIELQIR ECCCCCCCCHHHHHH	66.75	22053931
160 (in isoform 5)	Ubiquitination	-	66.75	21890473
160 (in isoform 2)	Ubiquitination	-	66.75	-
175	Phosphorylation	ELILRFISNPNSIIL HHHHHHHHCCCCEEE	43.45	21406692
179	Phosphorylation	RFISNPNSIILAVTA HHHHCCCCEEEEEEE	16.56	20068231
185	Phosphorylation	NSIILAVTAANTDMA CCEEEEEEECCCCCC	17.91	21406692
189	Phosphorylation	LAVTAANTDMATSEA EEEEECCCCCCCHHH	23.56	21406692
193	Phosphorylation	AANTDMATSEALKIS ECCCCCCCHHHHHHH	22.06	20068231
193 (in isoform 3)	Phosphorylation	-	22.06	-
193 (in isoform 4)	Phosphorylation	-	22.06	-
194	Phosphorylation	ANTDMATSEALKISR CCCCCCCHHHHHHHC	16.01	20068231
194 (in isoform 3)	Phosphorylation	-	16.01	-
194 (in isoform 4)	Phosphorylation	-	16.01	-
198 (in isoform 2)	Ubiquitination	-	45.76	-
200	Phosphorylation	TSEALKISREVDPDG CHHHHHHHCCCCCCC	22.32	22964224
200	O-linked_Glycosylation	TSEALKISREVDPDG CHHHHHHHCCCCCCC	22.32	28510447
238	Ubiquitination	MGRVIPVKLGIIGVV HCCCCCEEEEEEEEE	35.32	21890473
238 (in isoform 1)	Ubiquitination	-	35.32	21890473
238 (in isoform 2)	Ubiquitination	-	35.32	21890473
238 (in isoform 3)	Ubiquitination	-	35.32	21890473
238 (in isoform 4)	Ubiquitination	-	35.32	21890473
238 (in isoform 5)	Ubiquitination	-	35.32	21890473
251	Ubiquitination	VVNRSQLDINNKKSV EECHHHCCCCCCCCC	33.65	21890473
251	Ubiquitination	VVNRSQLDINNKKSV EECHHHCCCCCCCCC	33.65	21890473
255	Ubiquitination	SQLDINNKKSVTDSI HHCCCCCCCCCCHHH	41.77	-
256	Ubiquitination	QLDINNKKSVTDSIR HCCCCCCCCCCHHHH	52.89	-
266	Phosphorylation	TDSIRDEYAFLQKKY CHHHHHHHHHHHHHC	13.62	28270605
271	Ubiquitination	DEYAFLQKKYPSLAN HHHHHHHHHCHHHHC	57.32	-
271	Acetylation	DEYAFLQKKYPSLAN HHHHHHHHHCHHHHC	57.32	26051181
272	Ubiquitination	EYAFLQKKYPSLANR HHHHHHHHCHHHHCC	49.81	-
283	Acetylation	LANRNGTKYLARTLN HHCCCCHHHHHHHHH	39.40	19608861
283 (in isoform 3)	Acetylation	-	39.40	-
283 (in isoform 4)	Acetylation	-	39.40	-
330	Phosphorylation	GEPVDDKSATLLQLI CCCCCCHHHHHHHHH	33.22	21712546
332	Ubiquitination	PVDDKSATLLQLITK CCCCHHHHHHHHHHH	34.78	-
338	Phosphorylation	ATLLQLITKFATEYC HHHHHHHHHHHHHHH	28.80	28842319
354	Nitration	TIEGTAKYIETSELC CHHCCCHHHHHHHHH	11.09	-
361	Glutathionylation	YIETSELCGGARICY HHHHHHHHCCCEEEE	4.08	22555962
367	S-nitrosocysteine	LCGGARICYIFHETF HHCCCEEEEEEHHHH	1.45	-
367	S-nitrosylation	LCGGARICYIFHETF HHCCCEEEEEEHHHH	1.45	22178444
368	Phosphorylation	CGGARICYIFHETFG HCCCEEEEEEHHHHC	12.30	-
394	Phosphorylation	LNTIDILTAIRNATG CCHHHHHHHHHHCCC	22.00	-
400	Phosphorylation	LTAIRNATGPRPALF HHHHHHCCCCCCCCC	51.79	-
412	Phosphorylation	ALFVPEVSFELLVKR CCCCCHHHHHHHHHH	16.02	-
449	Phosphorylation	IIQHCSNYSTQELLR HHHHHCCCCHHHHHC	9.22	-
515	Ubiquitination	MNNNIEEQRRNRLAR CCCCHHHHHHHHHHH	36.52	-
526	Phosphorylation	RLARELPSAVSRDKS HHHHHHHHHHHCCCC	54.66	30266825
526 (in isoform 3)	Phosphorylation	-	54.66	22617229
529	Phosphorylation	RELPSAVSRDKSSKV HHHHHHHHCCCCCCC	34.18	23401153
529 (in isoform 3)	Phosphorylation	-	34.18	24719451
529 (in isoform 4)	Phosphorylation	-	34.18	22496350
532	Sumoylation	PSAVSRDKSSKVPSA HHHHHCCCCCCCCCC	56.36	-
532	Sumoylation	PSAVSRDKSSKVPSA HHHHHCCCCCCCCCC	56.36	19638400
532	Ubiquitination	PSAVSRDKSSKVPSA HHHHHCCCCCCCCCC	56.36	-
535	Sumoylation	VSRDKSSKVPSALAP HHCCCCCCCCCCCCC	66.32	-
535	Sumoylation	VSRDKSSKVPSALAP HHCCCCCCCCCCCCC	66.32	19638400
535	Ubiquitination	VSRDKSSKVPSALAP HHCCCCCCCCCCCCC	66.32	-
535 (in isoform 4)	Phosphorylation	-	66.32	21712546
535 (in isoform 2)	Ubiquitination	-	66.32	-
538	Phosphorylation	DKSSKVPSALAPASQ CCCCCCCCCCCCCCC	38.61	21406692
542 (in isoform 6)	Phosphorylation	-	33.04	27251275
542	Phosphorylation	KVPSALAPASQEPSP CCCCCCCCCCCCCCC	33.04	22496350
544	Phosphorylation	PSALAPASQEPSPAA CCCCCCCCCCCCCCC	33.73	22199227
544 (in isoform 2)	Phosphorylation	-	33.73	25159151
548	Phosphorylation	APASQEPSPAASAEA CCCCCCCCCCCCHHH	26.81	25159151
548	Phosphorylation	APASQEPSPAASAEA CCCCCCCCCCCCHHH	26.81	21712546
548 (in isoform 2)	Phosphorylation	-	26.81	25159151
548 (in isoform 4)	Phosphorylation	-	26.81	22210691
549 (in isoform 4)	Phosphorylation	-	42.43	22210691
552	Phosphorylation	QEPSPAASAEADGKL CCCCCCCCHHHCCCE	28.84	22199227
557 (in isoform 8)	Phosphorylation	-	33.45	25159151
558	Sumoylation	ASAEADGKLIQDSRR CCHHHCCCEECCCHH	42.86	-
558	Sumoylation	ASAEADGKLIQDSRR CCHHHCCCEECCCHH	42.86	19638400
561 (in isoform 6)	Phosphorylation	-	53.73	27251275
561	Phosphorylation	EADGKLIQDSRRETK HHCCCEECCCHHHHC	53.73	22210691
561 (in isoform 2)	Phosphorylation	-	53.73	22210691
561 (in isoform 8)	Phosphorylation	-	53.73	25159151
562	Phosphorylation	ADGKLIQDSRRETKN HCCCEECCCHHHHCC	36.80	22210691
563	Phosphorylation	DGKLIQDSRRETKNV CCCEECCCHHHHCCC	19.50	27535140
568	Sumoylation	QDSRRETKNVASGGG CCCHHHHCCCCCCCC	44.67	-
568	Sumoylation	QDSRRETKNVASGGG CCCHHHHCCCCCCCC	44.67	19638400
568	Ubiquitination	QDSRRETKNVASGGG CCCHHHHCCCCCCCC	44.67	-
570 (in isoform 4)	Phosphorylation	-	4.83	-
572	Phosphorylation	RETKNVASGGGGVGD HHHCCCCCCCCCCCC	33.42	22199227
574 (in isoform 2)	Phosphorylation	-	27.47	22210691
574 (in isoform 8)	Phosphorylation	-	27.47	22210691
575 (in isoform 2)	Phosphorylation	-	31.01	22210691
579 (in isoform 4)	Phosphorylation	-	52.24	-
581 (in isoform 3)	Phosphorylation	-	7.48	-
585	O-linked_Glycosylation	GDGVQEPTTGNWRGM CCCCCCCCCCCCCHH	46.73	UniProtKB CARBOHYD
585	Phosphorylation	GDGVQEPTTGNWRGM CCCCCCCCCCCCCHH	46.73	28122231
586	O-linked_Glycosylation	DGVQEPTTGNWRGML CCCCCCCCCCCCHHH	38.95	UniProtKB CARBOHYD
586	Phosphorylation	DGVQEPTTGNWRGML CCCCCCCCCCCCHHH	38.95	28555341
587 (in isoform 8)	Phosphorylation	-	33.89	22210691
588 (in isoform 8)	Phosphorylation	-	24.15	22210691
590 (in isoform 3)	Phosphorylation	-	25.33	24719451
594	Sumoylation	GNWRGMLKTSKAEEL CCCCHHHCCHHHHHH	41.69	-
594	Sumoylation	GNWRGMLKTSKAEEL CCCCHHHCCHHHHHH	41.69	19638400
595	Phosphorylation	NWRGMLKTSKAEELL CCCHHHCCHHHHHHH	31.34	29214152
596	Phosphorylation	WRGMLKTSKAEELLA CCHHHCCHHHHHHHH	28.42	29214152
597	Acetylation	RGMLKTSKAEELLAE CHHHCCHHHHHHHHH	66.12	-
597	Sumoylation	RGMLKTSKAEELLAE CHHHCCHHHHHHHHH	66.12	-
597	Sumoylation	RGMLKTSKAEELLAE CHHHCCHHHHHHHHH	66.12	19638400
597	Ubiquitination	RGMLKTSKAEELLAE CHHHCCHHHHHHHHH	66.12	-
606	Sumoylation	EELLAEEKSKPIPIM HHHHHHHHCCCCCCC	56.11	-
606	Sumoylation	EELLAEEKSKPIPIM HHHHHHHHCCCCCCC	56.11	-
607	Phosphorylation	ELLAEEKSKPIPIMP HHHHHHHCCCCCCCC	47.12	23927012
608	Sumoylation	LLAEEKSKPIPIMPA HHHHHHCCCCCCCCC	59.02	-
608	Sumoylation	LLAEEKSKPIPIMPA HHHHHHCCCCCCCCC	59.02	19638400
616	Phosphorylation	PIPIMPASPQKGHAV CCCCCCCCCCCCCCC	23.22	22167270
629 (in isoform 6)	Phosphorylation	-	25.10	27251275
637	Phosphorylation	VPVARKLSAREQRDC HHHHHHCCHHHHHHH	28.45	18838687
644	S-nitrosocysteine	SAREQRDCEVIERLI CHHHHHHHHHHHHHH	4.98	-
644	S-nitrosylation	SAREQRDCEVIERLI CHHHHHHHHHHHHHH	4.98	19342591
647 (in isoform 4)	Phosphorylation	-	0.88	-
653	Phosphorylation	VIERLIKSYFLIVRK HHHHHHHHHHHHHCC	17.70	23882029
654	Phosphorylation	IERLIKSYFLIVRKN HHHHHHHHHHHHCCC	9.45	30622161
658 (in isoform 3)	Phosphorylation	-	8.51	-
681	Phosphorylation	LVNHVKDTLQSELVG HHHHHHHHHHHHHHH	22.45	20068231
684	Phosphorylation	HVKDTLQSELVGQLY HHHHHHHHHHHHHHH	35.69	20068231
691	Phosphorylation	SELVGQLYKSSLLDD HHHHHHHHHHHHHHH	10.84	20068231
693	Phosphorylation	LVGQLYKSSLLDDLL HHHHHHHHHHHHHHH	16.80	-
701	Phosphorylation	SLLDDLLTESEDMAQ HHHHHHHHCCHHHHH	44.77	-
706	Sulfoxidation	LLTESEDMAQRRKEA HHHCCHHHHHHHHHH	2.76	30846556
707 (in isoform 2)	Ubiquitination	-	16.43	-
724	Phosphorylation	LKALQGASQIIAEIR HHHHHHHHHHHHHHH	28.83	21712546

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
40	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
44	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
266	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
368	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
449	Y	Phosphorylation	Kinase	ABL1	P00519	GPS
595	T	Phosphorylation	Kinase	LRRK2	Q5S007	PSP
616	S	Phosphorylation	Kinase	CDK1	P06493	Uniprot
616	S	Phosphorylation	Kinase	CDK2	P24941	PSP
616	S	Phosphorylation	Kinase	CDK5	Q00535	PSP
616	S	Phosphorylation	Kinase	PRKCD	Q05655	GPS
616	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
616	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
637	S	Phosphorylation	Kinase	PKA_GROUP	-	PhosphoELM
637	S	Phosphorylation	Kinase	AMPKA1	Q13131	PSP
637	S	Phosphorylation	Kinase	PKA	-	Uniprot
637	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
637	S	Phosphorylation	Kinase	PIM1	P11309	PSP
637	S	Phosphorylation	Kinase	PRKD1	Q15139	PSP
637	S	Phosphorylation	Kinase	CAMK1	Q14012	Uniprot
637	S	Phosphorylation	Kinase	PRKACA	P17612	GPS
693	S	Phosphorylation	Kinase	GSK3B	P49841	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	PRKN	O60260	PMID:21292769
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:21325626
-	K	Ubiquitination	E3 ubiquitin ligase	MUL1	Q969V5	PMID:19407830
-	K	Ubiquitination	E3 ubiquitin ligase	MARCHF5	Q9NX47	PMID:16874301

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
616	S	Phosphorylation	18088087
Phosphorylation on Ser-616 by CDK1 and PINK1 activates the GTPase activity and promotes mitochondrial fission.
637	S	Phosphorylation	17553808
It also decreases phosphorylation at Ser-637 (By similarity).
637	S	Phosphorylation	17553808
Phosphorylated in a circadian manner at Ser-637.
637	S	Phosphorylation	17553808
Phosphorylation on Ser-637 by CAMK1 and PKA inhibits the GTPase activity, leading to a defect in mitochondrial fission promoting mitochondrial elongation.

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_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GSK3B_HUMAN	GSK3B	physical	9731200
FIS1_HUMAN	FIS1	physical	12861026
PRKN_HUMAN	PARK2	physical	21292769
LRRK2_HUMAN	LRRK2	physical	22228096
DNM1L_HUMAN	DNM1L	physical	23530241
MFF_HUMAN	MFF	physical	23530241
MID49_HUMAN	MIEF2	physical	23530241
ACPH_HUMAN	APEH	physical	22863883
CYHR1_HUMAN	CYHR1	physical	22863883
SYCC_HUMAN	CARS	physical	22863883
NIBL1_HUMAN	FAM129B	physical	22863883
JMJD6_HUMAN	JMJD6	physical	22863883
PSMG3_HUMAN	PSMG3	physical	22863883
SC24A_HUMAN	SEC24A	physical	22863883
LA_HUMAN	SSB	physical	22863883
VP26A_HUMAN	VPS26A	physical	22863883
MAGA1_HUMAN	MAGEA1	physical	18330356
MAGA3_HUMAN	MAGEA3	physical	18330356
RIR2_HUMAN	RRM2	physical	18330356
SCG3_HUMAN	SCG3	physical	18330356
SH3G1_HUMAN	SH3GL1	physical	18330356
ZBT24_HUMAN	ZBTB24	physical	19074440
FZR1_HUMAN	FZR1	physical	21325626
PUR9_HUMAN	ATIC	physical	26344197
TES_HUMAN	TES	physical	26344197
ML12A_HUMAN	MYL12A	physical	29128334
PROF1_HUMAN	PFN1	physical	29128334
PPIA_HUMAN	PPIA	physical	29128334
LDHB_HUMAN	LDHB	physical	29128334
RL30_HUMAN	RPL30	physical	29128334
DREB_HUMAN	DBN1	physical	29128334
NDKA_HUMAN	NME1	physical	29128334
KCRB_HUMAN	CKB	physical	29128334
TPIS_HUMAN	TPI1	physical	29128334
ALDOA_HUMAN	ALDOA	physical	29128334
SAP18_HUMAN	SAP18	physical	29128334
TCPQ_HUMAN	CCT8	physical	29128334
RL12_HUMAN	RPL12	physical	29128334
THIO_HUMAN	TXN	physical	29128334
EF2_HUMAN	EEF2	physical	29128334
1433E_HUMAN	YWHAE	physical	29128334
1433Z_HUMAN	YWHAZ	physical	29128334
1433B_HUMAN	YWHAB	physical	29128334
HPRT_HUMAN	HPRT1	physical	29128334
TCPB_HUMAN	CCT2	physical	29128334
ARF1_HUMAN	ARF1	physical	29128334
LDHA_HUMAN	LDHA	physical	29128334
IF5A1_HUMAN	EIF5A	physical	29128334
RL27_HUMAN	RPL27	physical	29128334
MDHM_HUMAN	MDH2	physical	29128334
PRDX6_HUMAN	PRDX6	physical	29128334
PRS8_HUMAN	PSMC5	physical	29128334
RA1L2_HUMAN	HNRNPA1L2	physical	29128334
EF1B_HUMAN	EEF1B2	physical	29128334
PRDX2_HUMAN	PRDX2	physical	29128334
RUVB2_HUMAN	RUVBL2	physical	29128334
PRS6A_HUMAN	PSMC3	physical	29128334
UBA1_HUMAN	UBA1	physical	29128334
EF1G_HUMAN	EEF1G	physical	29128334
TIM13_HUMAN	TIMM13	physical	29128334
TERA_HUMAN	VCP	physical	29128334
RUVB1_HUMAN	RUVBL1	physical	29128334
SF3B6_HUMAN	SF3B6	physical	29128334
LA_HUMAN	SSB	physical	29128334
ACTN4_HUMAN	ACTN4	physical	29128334
TPM1_HUMAN	TPM1	physical	29128334
TCP4_HUMAN	SUB1	physical	29128334
XRCC6_HUMAN	XRCC6	physical	29128334
HCD2_HUMAN	HSD17B10	physical	29128334
ROAA_HUMAN	HNRNPAB	physical	29128334
PABP1_HUMAN	PABPC1	physical	29128334
HSP74_HUMAN	HSPA4	physical	29128334
HNRDL_HUMAN	HNRNPDL	physical	29128334
ILF2_HUMAN	ILF2	physical	29128334
CN166_HUMAN	C14orf166	physical	29128334
EF1D_HUMAN	EEF1D	physical	29128334
PUR6_HUMAN	PAICS	physical	29128334
1433T_HUMAN	YWHAQ	physical	29128334
SAHH_HUMAN	AHCY	physical	29128334
PDIA6_HUMAN	PDIA6	physical	29128334
STIP1_HUMAN	STIP1	physical	29128334
ENPL_HUMAN	HSP90B1	physical	29128334
IMDH2_HUMAN	IMPDH2	physical	29128334
RNPS1_HUMAN	RNPS1	physical	29128334
TAGL2_HUMAN	TAGLN2	physical	29128334
ACLY_HUMAN	ACLY	physical	29128334
IMB1_HUMAN	KPNB1	physical	29128334
PGAM1_HUMAN	PGAM1	physical	29128334
CDC37_HUMAN	CDC37	physical	29128334
PIMT_HUMAN	PCMT1	physical	29128334
NP1L1_HUMAN	NAP1L1	physical	29128334
RL28_HUMAN	RPL28	physical	29128334
ACTZ_HUMAN	ACTR1A	physical	29128334
SUMO2_HUMAN	SUMO2	physical	29128334
TCPH_HUMAN	CCT7	physical	29128334
TKT_HUMAN	TKT	physical	29128334
EIF3F_HUMAN	EIF3F	physical	29128334
ERH_HUMAN	ERH	physical	29128334
PAIRB_HUMAN	SERBP1	physical	29128334
RBBP4_HUMAN	RBBP4	physical	29128334
PARK7_HUMAN	PARK7	physical	29128334
DCD_HUMAN	DCD	physical	29128334
PRS10_HUMAN	PSMC6	physical	29128334
RANG_HUMAN	RANBP1	physical	29128334
SYRC_HUMAN	RARS	physical	29128334
PTBP1_HUMAN	PTBP1	physical	29128334
UB2L3_HUMAN	UBE2L3	physical	29128334
IF4A3_HUMAN	EIF4A3	physical	29128334
ODPB_HUMAN	PDHB	physical	29128334
PSA4_HUMAN	PSMA4	physical	29128334
RFA3_HUMAN	RPA3	physical	29128334
PLST_HUMAN	PLS3	physical	29128334
GFAP_HUMAN	GFAP	physical	29128334
PRS7_HUMAN	PSMC2	physical	29128334
NACAM_HUMAN	NACA	physical	29128334
NACA_HUMAN	NACA	physical	29128334
KCD12_HUMAN	KCTD12	physical	29128334
PRS4_HUMAN	PSMC1	physical	29128334
TIF1B_HUMAN	TRIM28	physical	29128334
DNJA1_HUMAN	DNAJA1	physical	29128334
HS105_HUMAN	HSPH1	physical	29128334
HNRH3_HUMAN	HNRNPH3	physical	29128334
DCTN2_HUMAN	DCTN2	physical	29128334
RBM8A_HUMAN	RBM8A	physical	29128334
SAE1_HUMAN	SAE1	physical	29128334
ANM1_HUMAN	PRMT1	physical	29128334
C1TC_HUMAN	MTHFD1	physical	29128334
PSMD2_HUMAN	PSMD2	physical	29128334
RMXL2_HUMAN	RBMXL2	physical	29128334
IF2A_HUMAN	EIF2S1	physical	29128334
EIF3D_HUMAN	EIF3D	physical	29128334
ACTN1_HUMAN	ACTN1	physical	29128334
SKP1_HUMAN	SKP1	physical	29128334
FAS_HUMAN	FASN	physical	29128334
XRCC5_HUMAN	XRCC5	physical	29128334
EZRI_HUMAN	EZR	physical	29128334
EIF3B_HUMAN	EIF3B	physical	29128334
PFD2_HUMAN	PFDN2	physical	29128334
AHSA1_HUMAN	AHSA1	physical	29128334
DDX21_HUMAN	DDX21	physical	29128334
SYDC_HUMAN	DARS	physical	29128334
PININ_HUMAN	PNN	physical	29128334
BUB3_HUMAN	BUB3	physical	29128334
ACINU_HUMAN	ACIN1	physical	29128334
MYH11_HUMAN	MYH11	physical	29128334
RCC1_HUMAN	RCC1	physical	29128334
EIF3A_HUMAN	EIF3A	physical	29128334
DX39B_HUMAN	DDX39B	physical	29128334
PRS6B_HUMAN	PSMC4	physical	29128334
DYHC1_HUMAN	DYNC1H1	physical	29128334
CDK1_HUMAN	CDK1	physical	29128334
SYLC_HUMAN	LARS	physical	29128334
METK2_HUMAN	MAT2A	physical	29128334
TLN1_HUMAN	TLN1	physical	29128334
ABCE1_HUMAN	ABCE1	physical	29128334
GANAB_HUMAN	GANAB	physical	29128334
CAPR1_HUMAN	CAPRIN1	physical	29128334
IQGA1_HUMAN	IQGAP1	physical	29128334
SAFB1_HUMAN	SAFB	physical	29128334
H2A1B_HUMAN	HIST1H2AE	physical	29128334
KCRU_HUMAN	CKMT1B	physical	29128334

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
	Note=May be associated with Alzheimer disease through beta-amyloid-induced increased S-nitrosylation of DNM1L, which triggers, directly or indirectly, excessive mitochondrial fission, synaptic loss and neuronal damage.
614388
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DNM1L_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-616, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions."; Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.; Science 325:834-840(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-283, AND MASS SPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-616, AND MASS SPECTROMETRY.	19413330 [Abstract]
"Dephosphorylation by calcineurin regulates translocation of Drp1 tomitochondria."; Cereghetti G.M., Stangherlin A., Martins de Brito O., Chang C.R.,Blackstone C., Bernardi P., Scorrano L.; Proc. Natl. Acad. Sci. U.S.A. 105:15803-15808(2008). Cited for: PHOSPHORYLATION AT SER-616 AND SER-637, INTERACTION WITH PPP3CA,DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OFSER-616 AND SER-637.	18838687 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548 AND SER-616, ANDMASS SPECTROMETRY.	18669648 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND MASSSPECTROMETRY.	18088087 [Abstract]
"CaM kinase I alpha-induced phosphorylation of Drp1 regulatesmitochondrial morphology."; Han X.J., Lu Y.F., Li S.A., Kaitsuka T., Sato Y., Tomizawa K.,Nairn A.C., Takei K., Matsui H., Matsushita M.; J. Cell Biol. 182:573-585(2008). Cited for: PHOSPHORYLATION AT SER-637, FUNCTION, INTERACTION WITH FIS1, ANDMUTAGENESIS OF SER-637.	18695047 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND MASSSPECTROMETRY.	18187866 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, AND MASSSPECTROMETRY.	17924679 [Abstract]
"Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulatesits GTPase activity and mitochondrial morphology."; Chang C.R., Blackstone C.; J. Biol. Chem. 282:21583-21587(2007). Cited for: PHOSPHORYLATION AT SER-637, FUNCTION, SUBUNIT, AND MUTAGENESIS OFSER-637.	17553808 [Abstract]
S-nitrosylation
Reference	PubMed
"S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrialfission and neuronal injury."; Cho D.H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z.,Lipton S.A.; Science 324:102-105(2009). Cited for: S-NITROSYLATION AT CYS-644, FUNCTION, ASSOCIATION WITH ALZHEIMERDISEASE, AND MUTAGENESIS OF CYS-300; CYS-345; CYS-361; CYS-367;CYS-431; CYS-446; CYS-470; CYS-505 AND CYS-644.	19342591 [Abstract]
Sumoylation
Reference	PubMed
"SUMOylation of the mitochondrial fission protein Drp1 occurs atmultiple nonconsensus sites within the B domain and is linked to itsactivity cycle."; Figueroa-Romero C., Iniguez-Lluhi J.A., Stadler J., Chang C.R.,Arnoult D., Keller P.J., Hong Y., Blackstone C., Feldman E.L.; FASEB J. 23:3917-3927(2009). Cited for: SUMOYLATION AT LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597;LYS-606 AND LYS-608, INTERACTION WITH UBE2I, FUNCTION, AND MUTAGENESISOF LYS-38; LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597;LYS-606 AND LYS-608.	19638400 [Abstract]

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