O00429 (DNM1L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynamin-1-like protein
EC=3.6.5.5

Alternative name(s):
Dnm1p/Vps1p-like protein
Short name=DVLP
Dynamin family member proline-rich carboxyl-terminal domain less
Short name=Dymple
Dynamin-like protein
Dynamin-like protein 4
Dynamin-like protein IV
Short name=HdynIV
Dynamin-related protein 1

Gene names

Name:	DNM1L
Synonyms:	DLP1, DRP1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	736 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into ring-like structures which wrap around the scission site to constict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Required for normal brain development. Facilitates developmentally-regulated apoptosis during neural tube development. Required for a normal rate of cytochrome c release and caspase activation during apoptosis. Also required for mitochondrial fission during mitosis. Required for programmed necrosis execution. May be involved in vesicle transport. Ref.3 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.26 Ref.28 Ref.29 Ref.31 Ref.32 Isoform 1 and isoform 4 inhibit peroxisomal division when overexpressed. Ref.3 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.26 Ref.28 Ref.29 Ref.31 Ref.32
Catalytic activity	GTP + H2O = GDP + phosphate. Ref.8
Subunit structure	Homotetramer; dimerizes through the N-terminal GTP-middle region of one molecule binding to the GED domain of another DNM1L molecule. Can self-assemble in multimeric ring-like structures. Interacts with BCL2L1; the interaction stimulates the GTPase activity of DMN1L in synapses and increases the number of axonal mitochondria and the size and number of synaptic vesicle clusters. Interacts with FIS1 By similarity. Interacts with GSK3B and MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in ite B domain. Interacts with PPP3CA; the interaction dephosphorylates DNM1L and regulates its transition to mitochondria. Interacts witn MID49 and MID51. Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-637 and activation of GTPase activity and eventually to mitochondria fragmentation. Ref.2 Ref.4 Ref.11 Ref.12 Ref.15 Ref.16 Ref.17 Ref.20 Ref.23 Ref.26 Ref.28 Ref.35 Ref.36 Ref.38
Subcellular location	Cytoplasm › cytosol. Golgi apparatus. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Note: Mainly cytosolic. Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Colocalized with MARCH5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. Associated with peroxisomal membranes, partly recruited there by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear. In some cell types, localizes to the Golgi complex. Ref.1 Ref.3 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.21 Ref.26 Ref.32 Ref.38
Tissue specificity	Ubiquitously expressed with highest levels found in skeletal muscles, heart, kidney and brain. Isoform 1 is brain-specific. Isoform 2 and isoform 3 are predominantly expressed in testis and skeletal muscles respectively. Isoform 4 is weakly expressed in brain, heart and kidney. Isoform 5 is dominantly expressed in liver, heart and kidney. Isoform 6 is expressed in neurons. Ref.2 Ref.3 Ref.4 Ref.8 Ref.10
Domain	The GED domain folds back to interact, in cis, with the GTP-binding domain and middle domain, and interacts, in trans, with the GED domains of other DNM1L molecules, and is thus critical for activating GTPase activity and for DNM1L dimerization. Ref.15
Post-translational modification	Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-637 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-616 also promotes mitochondrial fission. Ref.19 Ref.20 Ref.23 Ref.26 Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity. Ref.27 Ref.28 Ref.29 S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage. Ubiquitination by MARCH5 affects mitochondrial morphology. O-GlcNAcylation augments the level of the GTP-bound active form of DRP1 and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-637 By similarity.
Involvement in disease	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. Ref.31 Encephalopathy, lethal, due to defective mitochondrial and peroxisomal fission (EMPF) [MIM:614388]: A rare autosomal dominant systemic disorder resulting in lack of neurologic development and death in infancy. After birth, infants present in the first week of life with poor feeding and neurologic impairment, including hypotonia, little spontaneous movement, no tendon reflexes, no response to light stimulation, and poor visual fixation. Other features include mildly elevated plasma concentration of very-long-chain fatty acids, lactic acidosis, microcephaly, deep-set eyes, optic atrophy and hypoplasia, and an abnormal gyral pattern in both frontal lobes associated with dysmyelination. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.31
Sequence similarities	Belongs to the dynamin family. Contains 1 GED domain.

Ontologies

Keywords
Biological process	Necrosis
Cellular component	Cytoplasm Golgi apparatus Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Glycoprotein Isopeptide bond Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC cellular component disassembly involved in execution phase of apoptosis Traceable author statement. Source: Reactome dynamin polymerization involved in mitochondrial fission Inferred from direct assay Ref.12. Source: UniProtKB membrane fission involved in mitochondrial fission Inferred from direct assay Ref.12. Source: UniProtKB mitochondrial fragmentation involved in apoptotic process Inferred from mutant phenotype PubMed 18353969PubMed 21149567. Source: UniProtKB mitochondrion morphogenesis Inferred from mutant phenotype PubMed 21149567. Source: MGI peroxisome fission Inferred from direct assay Ref.14. Source: UniProtKB positive regulation of intrinsic apoptotic signaling pathway Inferred from mutant phenotype PubMed 20850011. Source: UniProtKB positive regulation of mitochondrial fission Traceable author statement PubMed 20436456. Source: BHF-UCL positive regulation of protein secretion Inferred from direct assay Ref.3. Source: UniProtKB positive regulation of release of cytochrome c from mitochondria Inferred from mutant phenotype PubMed 21149567. Source: UniProtKB protein homotetramerization Inferred from direct assay PubMed 18353969. Source: UniProtKB regulation of peroxisome organization Inferred from mutant phenotype PubMed 18353969. Source: UniProtKB
Cellular_component	Golgi apparatus Inferred from direct assay Ref.32. Source: UniProtKB cytosol Traceable author statement. Source: Reactome endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell microtubule Inferred from direct assay PubMed 21525035. Source: UniProtKB mitochondrial outer membrane Inferred from direct assay PubMed 21149567. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay Ref.3. Source: UniProtKB peroxisome Inferred from direct assay Ref.14. Source: UniProtKB protein complex Inferred from direct assay PubMed 17408615. Source: UniProtKB
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESR1	P03372	2	EBI-724571,EBI-78473
LRRK2	Q5S007	7	EBI-724571,EBI-5323863

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O00429-1)

Also known as: HdynIV-WT; DLP1F;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 4 (identifier: O00429-2)

Also known as: HdynIV-11; DLP1c;

The sequence of this isoform differs from the canonical sequence as follows:
     559-569: Missing.

Isoform 2 (identifier: O00429-3)

Also known as: DLP1a;

The sequence of this isoform differs from the canonical sequence as follows:
     533-558: Missing.

Isoform 3 (identifier: O00429-4)

Also known as: HdynIV-37; DLP1b;

The sequence of this isoform differs from the canonical sequence as follows:
     533-569: Missing.

Isoform 5 (identifier: O00429-5)

Also known as: HdynIV-26;

The sequence of this isoform differs from the canonical sequence as follows:
     544-569: Missing.

Note: No experimental confirmation available.

Isoform 6 (identifier: O00429-6)

The sequence of this isoform differs from the canonical sequence as follows:
     83-83: N → NDPATWKNSRHLSK

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 736	736	Dynamin-1-like protein		PRO_0000206566
Regions
	Domain	644 – 735	92	GED
	Nucleotide binding	32 – 39	8	GTP By similarity
	Nucleotide binding	146 – 150	5	GTP By similarity
	Nucleotide binding	215 – 218	4	GTP By similarity
	Region	1 – 343	343	GTPase domain
	Region	344 – 489	146	Middle domain
	Region	448 – 685	238	Interaction with GSK3B
	Region	502 – 569	68	B domain
Amino acid modifications
	Modified residue	529	1	Phosphoserine By similarity
	Modified residue	548	1	Phosphoserine Ref.25
	Modified residue	607	1	Phosphoserine Ref.25
	Modified residue	616	1	Phosphoserine; by CDK1 Ref.24 Ref.25 Ref.26 Ref.30 Ref.33 Ref.37
	Modified residue	637	1	Phosphoserine; by CAMK1 and PKA Ref.20 Ref.23 Ref.26
	Modified residue	644	1	S-nitrosocysteine Ref.31
	Glycosylation	585	1	O-linked (GlcNAc...)
	Glycosylation	586	1	O-linked (GlcNAc...)
	Cross-link	532		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
	Cross-link	535		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
	Cross-link	558		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
	Cross-link	568		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
	Cross-link	594		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
	Cross-link	597		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
	Cross-link	606		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
	Cross-link	608		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.28
Natural variations
	Alternative sequence	83	1	N → NDPATWKNSRHLSK in isoform 6.		VSP_039097
	Alternative sequence	533 – 569	37	Missing in isoform 3.		VSP_013685
	Alternative sequence	533 – 558	26	Missing in isoform 2.		VSP_013686
	Alternative sequence	544 – 569	26	Missing in isoform 5.		VSP_013687
	Alternative sequence	559 – 569	11	Missing in isoform 4.		VSP_013688
	Natural variant	71	1	S → T. Ref.2 Ref.3 Ref.4 Corresponds to variant rs1064610 [ dbSNP | Ensembl ].		VAR_022446
	Natural variant	395	1	A → D in EMPF; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission. Ref.22		VAR_063704
	Natural variant	426	1	E → D. Corresponds to variant rs2389105 [ dbSNP | Ensembl ].		VAR_030489
Experimental info
	Mutagenesis	38	1	K → A: Loss of GTPase activity. Impairs mitochondrial division and induces changes in peroxisome morphology. No effect on oligomerization. Increase in sumoylation by SUMO3. Ref.3 Ref.12 Ref.13 Ref.15 Ref.28
	Mutagenesis	38	1	K → E: Overexpression delays protein secretion. Ref.3 Ref.12 Ref.13 Ref.15 Ref.28
	Mutagenesis	39	1	S → I: Decreased localization to the perinuclear region. Ref.8 Ref.14
	Mutagenesis	39	1	S → N: Reduces peroxisomal abundance. Ref.8 Ref.14
	Mutagenesis	41	1	V → F: Temperature-sensitive. Impairs mitochondrial division. Ref.12
	Mutagenesis	59	1	T → A: Impairs mitochondrial division. Reduces peroxisomal abundance. Ref.12 Ref.14
	Mutagenesis	281	1	G → D: Temperature-sensitive. Impairs mitochondrial division. Ref.12
	Mutagenesis	300	1	C → A: No effect on S-nitrosylation. Ref.31
	Mutagenesis	345	1	C → A: No effect on S-nitrosylation. Ref.31
	Mutagenesis	361	1	C → A: No effect on S-nitrosylation. Ref.31
	Mutagenesis	367	1	C → A: No effect on S-nitrosylation. Ref.31
	Mutagenesis	431	1	C → A: No effect on S-nitrosylation. Ref.31
	Mutagenesis	446	1	C → A: No effect on S-nitrosylation. Ref.31
	Mutagenesis	470	1	C → A: No effect on S-nitrosylation. Ref.31
	Mutagenesis	505	1	C → A: No effect on S-nitrosylation. Ref.31
	Mutagenesis	532	1	K → R: Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-535; R-558 and R-568. Ref.28
	Mutagenesis	535	1	K → R: Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-558 and R-568. Ref.28
	Mutagenesis	558	1	K → R: Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-535 and R-568. Ref.28
	Mutagenesis	568	1	K → R: Some loss of sumoylation in B domain. Complete loss of sumoylation in B domain; when associated with R-532; R-535 and R-558. Ref.28
	Mutagenesis	594	1	K → R: Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-597; R-606 and R-608. Ref.28
	Mutagenesis	597	1	K → R: Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-606 and R-608. Ref.28
	Mutagenesis	606	1	K → R: Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-597 and R-608. Ref.28
	Mutagenesis	608	1	K → R: Some loss of sumoylation in the GED domain; Complete loss of sumoylation in the GED domain; when associated with R-594; R-597 and R-606. Ref.28
	Mutagenesis	616	1	S → A: Little effect on mitochondrial morphology. Translocated to mitochondria. Ref.26
	Mutagenesis	637	1	S → A: Abolishes phosphorylation. Promotes mitochondrial fission and cell vulnerability to apoptotic insults. Mostly mitochondrial. Disrupts, in vitro, binding to FIS1. Ref.20 Ref.23 Ref.26
	Mutagenesis	637	1	S → D: Impairs intramolecular, but not intermolecular interactions. Slight reduction in GTPase activity. Inhibits mitochondrial fission. Retained in cytoplasm. Ref.20 Ref.23 Ref.26
	Mutagenesis	644	1	C → A: Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity. Ref.31
	Mutagenesis	679	1	K → A: Diminishes intermolecular interaction between GTP-middle domain and GED domain but no effect on oligomerization. Marked reduction in GTPase activity, in vitro. Decreased mitochondrial division. Ref.15
	Sequence conflict	208	1	R → C in AAC35283. Ref.2
	Sequence conflict	208	1	R → C in AAD39541. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (HdynIV-WT) (DLP1F) [UniParc]. Last modified February 6, 2007. Version 2. Checksum: F9521A376B785B71	FASTA	736	81,877
	10 20 30 40 50 60 MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR 70 80 90 100 110 120 RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 130 140 150 160 170 180 NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 190 200 210 220 230 240 ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG 250 260 270 280 290 300 IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 310 320 330 340 350 360 LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL 370 380 390 400 410 420 CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ 430 440 450 460 470 480 IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN 490 500 510 520 530 540 EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL 550 560 570 580 590 600 APASQEPSPA ASAEADGKLI QDSRRETKNV ASGGGGVGDG VQEPTTGNWR GMLKTSKAEE 610 620 630 640 650 660 LLAEEKSKPI PIMPASPQKG HAVNLLDVPV PVARKLSARE QRDCEVIERL IKSYFLIVRK 670 680 690 700 710 720 NIQDSVPKAV MHFLVNHVKD TLQSELVGQL YKSSLLDDLL TESEDMAQRR KEAADMLKAL 730 QGASQIIAEI RETHLW
	Isoform 4 (HdynIV-11) (DLP1c) [UniParc]. Checksum: 208E830E9F906B7F	FASTA	725	80,536
	10 20 30 40 50 60 MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR 70 80 90 100 110 120 RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 130 140 150 160 170 180 NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 190 200 210 220 230 240 ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG 250 260 270 280 290 300 IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 310 320 330 340 350 360 LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL 370 380 390 400 410 420 CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ 430 440 450 460 470 480 IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN 490 500 510 520 530 540 EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL 550 560 570 580 590 600 APASQEPSPA ASAEADGKVA SGGGGVGDGV QEPTTGNWRG MLKTSKAEEL LAEEKSKPIP 610 620 630 640 650 660 IMPASPQKGH AVNLLDVPVP VARKLSAREQ RDCEVIERLI KSYFLIVRKN IQDSVPKAVM 670 680 690 700 710 720 HFLVNHVKDT LQSELVGQLY KSSLLDDLLT ESEDMAQRRK EAADMLKALQ GASQIIAEIR ETHLW
	Isoform 2 (DLP1a) [UniParc]. Checksum: 05BC4782DACC1C63	FASTA	710	79,442
	10 20 30 40 50 60 MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR 70 80 90 100 110 120 RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 130 140 150 160 170 180 NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 190 200 210 220 230 240 ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG 250 260 270 280 290 300 IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 310 320 330 340 350 360 LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL 370 380 390 400 410 420 CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ 430 440 450 460 470 480 IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN 490 500 510 520 530 540 EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKLIQDSRRE 550 560 570 580 590 600 TKNVASGGGG VGDGVQEPTT GNWRGMLKTS KAEELLAEEK SKPIPIMPAS PQKGHAVNLL 610 620 630 640 650 660 DVPVPVARKL SAREQRDCEV IERLIKSYFL IVRKNIQDSV PKAVMHFLVN HVKDTLQSEL 670 680 690 700 710 VGQLYKSSLL DDLLTESEDM AQRRKEAADM LKALQGASQI IAEIRETHLW
	Isoform 3 (HdynIV-37) (DLP1b) [UniParc]. Checksum: CB252ECCC9871127	FASTA	699	78,100
	10 20 30 40 50 60 MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR 70 80 90 100 110 120 RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 130 140 150 160 170 180 NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 190 200 210 220 230 240 ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG 250 260 270 280 290 300 IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 310 320 330 340 350 360 LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL 370 380 390 400 410 420 CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ 430 440 450 460 470 480 IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN 490 500 510 520 530 540 EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKVASGGGGV 550 560 570 580 590 600 GDGVQEPTTG NWRGMLKTSK AEELLAEEKS KPIPIMPASP QKGHAVNLLD VPVPVARKLS 610 620 630 640 650 660 AREQRDCEVI ERLIKSYFLI VRKNIQDSVP KAVMHFLVNH VKDTLQSELV GQLYKSSLLD 670 680 690 DLLTESEDMA QRRKEAADML KALQGASQII AEIRETHLW
	Isoform 5 (HdynIV-26) [UniParc]. Checksum: 0021B07297C5A6CC	FASTA	710	79,109
	10 20 30 40 50 60 MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR 70 80 90 100 110 120 RPLILQLVHV SQEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 130 140 150 160 170 180 NNKGVSPEPI HLKIFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 190 200 210 220 230 240 ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG 250 260 270 280 290 300 IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 310 320 330 340 350 360 LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL 370 380 390 400 410 420 CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ 430 440 450 460 470 480 IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN 490 500 510 520 530 540 EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAVSR DKSSKVPSAL 550 560 570 580 590 600 APAVASGGGG VGDGVQEPTT GNWRGMLKTS KAEELLAEEK SKPIPIMPAS PQKGHAVNLL 610 620 630 640 650 660 DVPVPVARKL SAREQRDCEV IERLIKSYFL IVRKNIQDSV PKAVMHFLVN HVKDTLQSEL 670 680 690 700 710 VGQLYKSSLL DDLLTESEDM AQRRKEAADM LKALQGASQI IAEIRETHLW
	Isoform 6 [UniParc]. Checksum: 64E6658C90A577AA	FASTA	749	83,399
	10 20 30 40 50 60 MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGIVTR 70 80 90 100 110 120 RPLILQLVHV SQEDKRKTTG EENDPATWKN SRHLSKGVEA EEWGKFLHTK NKLYTDFDEI 130 140 150 160 170 180 RQEIENETER ISGNNKGVSP EPIHLKIFSP NVVNLTLVDL PGMTKVPVGD QPKDIELQIR 190 200 210 220 230 240 ELILRFISNP NSIILAVTAA NTDMATSEAL KISREVDPDG RRTLAVITKL DLMDAGTDAM 250 260 270 280 290 300 DVLMGRVIPV KLGIIGVVNR SQLDINNKKS VTDSIRDEYA FLQKKYPSLA NRNGTKYLAR 310 320 330 340 350 360 TLNRLLMHHI RDCLPELKTR INVLAAQYQS LLNSYGEPVD DKSATLLQLI TKFATEYCNT 370 380 390 400 410 420 IEGTAKYIET SELCGGARIC YIFHETFGRT LESVDPLGGL NTIDILTAIR NATGPRPALF 430 440 450 460 470 480 VPEVSFELLV KRQIKRLEEP SLRCVELVHE EMQRIIQHCS NYSTQELLRF PKLHDAIVEV 490 500 510 520 530 540 VTCLLRKRLP VTNEMVHNLV AIELAYINTK HPDFADACGL MNNNIEEQRR NRLARELPSA 550 560 570 580 590 600 VSRDKSSKVP SALAPASQEP SPAASAEADG KLIQDSRRET KNVASGGGGV GDGVQEPTTG 610 620 630 640 650 660 NWRGMLKTSK AEELLAEEKS KPIPIMPASP QKGHAVNLLD VPVPVARKLS AREQRDCEVI 670 680 690 700 710 720 ERLIKSYFLI VRKNIQDSVP KAVMHFLVNH VKDTLQSELV GQLYKSSLLD DLLTESEDMA 730 740 QRRKEAADML KALQGASQII AEIRETHLW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification and subcellular localization of a novel mammalian dynamin-related protein homologous to yeast Vps1p and Dnm1p." Shin H.-W., Shinotsuka C., Torii S., Murakami K., Nakayama K. J. Biochem. 122:525-530(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION. Tissue: Hepatoma.
[2]	"Human dynamin-like protein interacts with the glycogen synthase kinase 3beta." Hong Y.-R., Chen C.-H., Cheng D.-S., Howng S.-L., Chow C.-C. Biochem. Biophys. Res. Commun. 249:697-703(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), VARIANT THR-71, TISSUE SPECIFICITY, INTERACTION WITH GSK3B. Tissue: Liver.
[3]	"Identification and functional characterization of a novel human protein highly related to the yeast dynamin-like GTPase Vps1p." Imoto M., Tachibana I., Urrutia R. J. Cell Sci. 111:1341-1349(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT THR-71, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38, FUNCTION. Tissue: Brain.
[4]	"Differential expression of four human dynamin-like protein variants in brain tumors." Chen C.-H., Howng S.-L., Hwang S.-L., Chou C.-K., Liao C.-H., Hong Y.-R. DNA Cell Biol. 19:189-194(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3; 4 AND 5), VARIANT THR-71, TISSUE SPECIFICITY, INTERACTION WITH GSK3B. Tissue: Brain.
[5]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 6). Tissue: Brain.
[6]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-736 (ISOFORM 1). Tissue: Lung.
[8]	"Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells." Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M. J. Biol. Chem. 273:1044-1051(1998) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-39, TISSUE SPECIFICITY, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
[9]	"A novel dynamin-like protein associates with cytoplasmic vesicles and tubules of the endoplasmic reticulum in mammalian cells." Yoon Y., Pitts K.R., Dahan S., McNiven M.A. J. Cell Biol. 140:779-793(1998) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[10]	"A human dynamin-related protein controls the distribution of mitochondria." Smirnova E., Shurland D.-L., Ryazantsev S.N., van der Bliek A.M. J. Cell Biol. 143:351-358(1998) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION, FUNCTION.
[11]	"Intermolecular and interdomain interactions of a dynamin-related GTP-binding protein, Dnm1p/Vps1p-like protein." Shin H.-W., Takatsu H., Mukai H., Munekata E., Murakami K., Nakayama K. J. Biol. Chem. 274:2780-2785(1999) [PubMed] [Europe PMC] [Abstract] Cited for: OLIGOMERIZATION.
[12]	"Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells." Smirnova E., Griparic L., Shurland D.-L., van der Bliek A.M. Mol. Biol. Cell 12:2245-2256(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38; VAL-41; THR-59 AND GLY-281, OLIGOMERIZATION.
[13]	"Dynamin-like protein 1 is involved in peroxisomal fission." Koch A., Thiemann M., Grabenbauer M., Yoon Y., McNiven M.A., Schrader M. J. Biol. Chem. 278:8597-8605(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF LYS-38, SUBCELLULAR LOCATION, FUNCTION.
[14]	"The dynamin-like GTPase DLP1 is essential for peroxisome division and is recruited to peroxisomes in part by PEX11." Li X., Gould S.J. J. Biol. Chem. 278:17012-17020(2003) [PubMed] [Europe PMC] [Abstract] Cited for: MUTAGENESIS OF SER-39 AND THR-59, FUNCTION, SUBCELLULAR LOCATION.
[15]	"Intra- and intermolecular domain interactions of the C-terminal GTPase effector domain of the multimeric dynamin-like GTPase Drp1." Zhu P.P., Patterson A., Stadler J., Seeburg D.P., Sheng M., Blackstone C. J. Biol. Chem. 279:35967-35974(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION OF STRUCTURAL DOMAINS, OLIGOMERIZATION, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-38 AND LYS-679.
[16]	"A novel mitochondrial ubiquitin ligase plays a critical role in mitochondrial dynamics." Yonashiro R., Ishido S., Kyo S., Fukuda T., Goto E., Matsuki Y., Ohmura-Hoshino M., Sada K., Hotta H., Yamamura H., Inatome R., Yanagi S. EMBO J. 25:3618-3626(2006) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY MARCH5, INTERACTION WITH MARCH5.
[17]	"MARCH-V is a novel mitofusin 2- and Drp1-binding protein able to change mitochondrial morphology." Nakamura N., Kimura Y., Tokuda M., Honda S., Hirose S. EMBO Rep. 7:1019-1022(2006) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY MARCH5, INTERACTION WITH MARCH5.
[18]	"Inhibiting the mitochondrial fission machinery does not prevent Bax/Bak-dependent apoptosis." Parone P.A., James D.I., Da Cruz S., Mattenberger Y., Donze O., Barja F., Martinou J.C. Mol. Cell. Biol. 26:7397-7408(2006) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[19]	"Mitotic phosphorylation of dynamin-related GTPase Drp1 participates in mitochondrial fission." Taguchi N., Ishihara N., Jofuku A., Oka T., Mihara K. J. Biol. Chem. 282:11521-11529(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION, FUNCTION.
[20]	"Cyclic AMP-dependent protein kinase phosphorylation of Drp1 regulates its GTPase activity and mitochondrial morphology." Chang C.R., Blackstone C. J. Biol. Chem. 282:21583-21587(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-637, FUNCTION, SUBUNIT, MUTAGENESIS OF SER-637.
[21]	"The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division." Karbowski M., Neutzner A., Youle R.J. J. Cell Biol. 178:71-84(2007) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[22]	"A lethal defect of mitochondrial and peroxisomal fission." Waterham H.R., Koster J., van Roermund C.W., Mooyer P.A., Wanders R.J., Leonard J.V. N. Engl. J. Med. 356:1736-1741(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, VARIANT EMPF ASP-395, CHARACTERIZATION OF VARIANT EMPF ASP-395.
[23]	"CaM kinase I alpha-induced phosphorylation of Drp1 regulates mitochondrial 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-637, FUNCTION, INTERACTION WITH FIS1, MUTAGENESIS OF SER-637.
[24]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, MASS SPECTROMETRY. Tissue: Platelet.
[25]	"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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548; SER-607 AND SER-616, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[26]	"Dephosphorylation by calcineurin regulates translocation of Drp1 to mitochondria." 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-616 AND SER-637, INTERACTION WITH PPP3CA, DEPHOSPHORYLATION, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-616 AND SER-637.
[27]	"MAPL is a new mitochondrial SUMO E3 ligase that regulates mitochondrial fission." Braschi E., Zunino R., McBride H.M. EMBO Rep. 10:748-754(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION BY MUL1.
[28]	"SUMOylation of the mitochondrial fission protein Drp1 occurs at multiple nonconsensus sites within the B domain and is linked to its activity 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) [PubMed] [Europe PMC] [Abstract] 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, MUTAGENESIS OF LYS-38; LYS-532; LYS-535; LYS-558; LYS-568; LYS-594; LYS-597; LYS-606 AND LYS-608.
[29]	"Translocation of SenP5 from the nucleoli to the mitochondria modulates DRP1-dependent fission during mitosis." Zunino R., Braschi E., Xu L., McBride H.M. J. Biol. Chem. 284:17783-17795(2009) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION, DESUMOYLATION, FUNCTION.
[30]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals 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) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[31]	"S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury." Cho D.H., Nakamura T., Fang J., Cieplak P., Godzik A., Gu Z., Lipton S.A. Science 324:102-105(2009) [PubMed] [Europe PMC] [Abstract] Cited for: S-NITROSYLATION AT CYS-644, FUNCTION, ASSOCIATION WITH ALZHEIMER DISEASE, MUTAGENESIS OF CYS-300; CYS-345; CYS-361; CYS-367; CYS-431; CYS-446; CYS-470; CYS-505 AND CYS-644.
[32]	"Dynamin-like protein 1 at the Golgi complex: A novel component of the sorting/targeting machinery en route to the plasma membrane." Bonekamp N.A., Vormund K., Jacob R., Schrader M. Exp. Cell Res. 316:3454-3467(2010) [PubMed] [Europe PMC] [Abstract] Cited for: POSSIBLE FUNCTION, SUBCELLULAR LOCATION.
[33]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[34]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[35]	"MiD49 and MiD51, new components of the mitochondrial fission machinery." Palmer C.S., Osellame L.D., Laine D., Koutsopoulos O.S., Frazier A.E., Ryan M.T. EMBO Rep. 12:565-573(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MID49 AND MID51.
[36]	"Human MIEF1 recruits Drp1 to mitochondrial outer membranes and promotes mitochondrial fusion rather than fission." Zhao J., Liu T., Jin S., Wang X., Qu M., Uhlen P., Tomilin N., Shupliakov O., Lendahl U., Nister M. EMBO J. 30:2762-2778(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MID51.
[37]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-616, MASS SPECTROMETRY.
[38]	"The mitochondrial phosphatase PGAM5 functions at the convergence point of multiple necrotic death pathways." Wang Z., Jiang H., Chen S., Du F., Wang X. Cell 148:228-243(2012) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PGAM5, SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB006965 mRNA. Translation: BAA22193.1. AF061795 mRNA. Translation: AAC35283.1. AF000430 mRNA. Translation: AAC23724.1. AF151685 mRNA. Translation: AAD39541.1. AK299926 mRNA. Translation: BAG61760.1. AK291094 mRNA. Translation: BAF83783.1. AC084824 Genomic DNA. No translation available. AC087588 Genomic DNA. No translation available. BC024590 mRNA. Translation: AAH24590.1.
IPI	IPI00037283. IPI00146935. IPI00473085. IPI00555883. IPI00871742. IPI00942042.
PIR	JC5695.
RefSeq	NP_005681.2. NM_005690.3. NP_036192.2. NM_012062.3. NP_036193.2. NM_012063.2.
UniGene	Hs.556296.
3D structure databases
ProteinModelPortal	O00429.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00429. 7 interactions.
MINT	MINT-1394198.
STRING	9606.ENSP00000266481.
PTM databases
PhosphoSite	O00429.
Proteomic databases
PaxDb	O00429.
PRIDE	O00429.
Protocols and materials databases
DNASU	10059.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000266481; ENSP00000266481; ENSG00000087470. ENST00000452533; ENSP00000415131; ENSG00000087470. ENST00000547312; ENSP00000448610; ENSG00000087470. ENST00000549701; ENSP00000450399; ENSG00000087470. ENST00000553257; ENSP00000449089; ENSG00000087470.
GeneID	10059.
KEGG	hsa:10059.
UCSC	uc001rld.2. human. uc001rle.2. human. uc001rlf.2. human.
Organism-specific databases
CTD	10059.
GeneCards	GC12P032832.
H-InvDB	HIX0010537.
HGNC	HGNC:2973. DNM1L.
HPA	CAB009952.
MIM	603850. gene. 614388. phenotype.
neXtProt	NX_O00429.
PharmGKB	PA27441.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0699.
HOVERGEN	HBG107833.
KO	K01528.
OrthoDB	EOG4SN1N7.
PhylomeDB	O00429.
Enzyme and pathway databases
Reactome	REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	O00429.
Bgee	O00429.
CleanEx	HS_DNM1L.
Genevestigator	O00429.
GermOnline	ENSG00000087470. Homo sapiens.
Family and domain databases
InterPro	IPR022812. Dynamin. IPR000375. Dynamin_central. IPR001401. Dynamin_GTPase. IPR019762. Dynamin_GTPase_CS. IPR003130. GED. IPR020850. GTPase_effector_domain_GED. [Graphical view]
PANTHER	PTHR11566. PTHR11566. 1 hit.
Pfam	PF01031. Dynamin_M. 1 hit. PF00350. Dynamin_N. 1 hit. PF02212. GED. 1 hit. [Graphical view]
PRINTS	PR00195. DYNAMIN.
SMART	SM00053. DYNc. 1 hit. SM00302. GED. 1 hit. [Graphical view]
PROSITE	PS00410. DYNAMIN. 1 hit. PS51388. GED. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DNM1L. human.
GenomeRNAi	10059.
NextBio	38007.
PMAP-CutDB	O00429.
SOURCE	Search...

Entry information

Entry name

DNM1L_HUMAN

Accession

Primary (citable) accession number: O00429
Secondary accession number(s): A8K4X9 , B4DSU8, O14541, O60709, Q7L6B3, Q8TBT7, Q9BWM1, Q9Y5J2

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	February 6, 2007
Last modified:	May 1, 2013
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.