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O00429 (DNM1L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length736 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Also required for 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. 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.29 Ref.30 Ref.32 Ref.33 Ref.41 Ref.42 Ref.44 Ref.45

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.29 Ref.30 Ref.32 Ref.33 Ref.41 Ref.42 Ref.44 Ref.45

Catalytic activity

GTP + H2O = GDP + phosphate. Ref.8 Ref.46

Enzyme regulation

GTPase activity is increased by binding to phospholipid membranes. Ref.46

Subunit structure

Homotetramer; dimerizes through the N-terminal GTP-middle region of one molecule binding to the GED domain of another DNM1L molecule. Oligomerizes in a GTP-dependent manner to form membrane-associated tubules with a spiral pattern. Can also oligomerize to form multimeric ring-like structures. Interacts with GSK3B and MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PPP3CA; the interaction dephosphorylates DNM1L and regulates its transition to mitochondria. Interacts with BCL2L1 isoform BCL-X(L)and CLTA; DNM1L and BCL2L1 isoform BCL-X(L)may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with FIS1. Interacts with MIEF2 and MIEF1; this regulates GTP hydrolysis and DNM1L oligomerization. Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 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.29 Ref.36 Ref.37 Ref.39 Ref.42 Ref.43 Ref.44 Ref.45 Ref.46

Subcellular location

Cytoplasmcytosol. Golgi apparatus. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome. Membraneclathrin-coated pit By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity. Note: Mainly cytosolic. Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Recruited to the mitochondrial outer membrane by interaction with MIEF1. 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. Binds to phospholipid membranes. Ref.1 Ref.3 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.21 Ref.26 Ref.33 Ref.39 Ref.41 Ref.45

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 Ref.42

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.28 Ref.29 Ref.30

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.32

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.32

Sequence similarities

Belongs to the dynamin family.

Contains 1 GED domain.

Ontologies

Keywords
   Biological processEndocytosis
Necrosis
   Cellular componentCell junction
Coated pit
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
Mitochondrion
Mitochondrion outer membrane
Peroxisome
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandGTP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Glycoprotein
Isopeptide bond
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from direct assay Ref.44. Source: UniProtKB

apoptotic process

Traceable author statement. Source: Reactome

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.12Ref.44. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

membrane fission involved in mitochondrial fission

Inferred from direct assay Ref.12. Source: UniProtKB

membrane fusion

Inferred from direct assay PubMed 20850011. Source: UniProtKB

mitochondrial fission

Inferred from direct assay Ref.44. 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

necroptotic process

Inferred from mutant phenotype Ref.39. Source: UniProtKB

peroxisome fission

Inferred from direct assay Ref.14. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype PubMed 20850011. 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 mitochondrion organization

Inferred from mutant phenotype PubMed 18353969PubMed 21149567. Source: UniProtKB

regulation of peroxisome organization

Inferred from mutant phenotype PubMed 18353969. Source: UniProtKB

regulation of protein oligomerization

Inferred from direct assay PubMed 20850011. Source: UniProtKB

release of cytochrome c from mitochondria

Inferred from mutant phenotype PubMed 20850011. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from direct assay Ref.33. Source: UniProtKB

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasm

Inferred from direct assay Ref.14PubMed 21149567. Source: UniProtKB

cytosol

Inferred from direct assay Ref.39Ref.41. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

mitochondrial outer membrane

Inferred from direct assay PubMed 21149567. Source: UniProtKB

mitochondrion

Inferred from direct assay Ref.39Ref.44Ref.41. 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

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from direct assay Ref.39Ref.44. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.45PubMed 20850011. Source: IntAct

protein homodimerization activity

Inferred from direct assay Ref.39Ref.44. Source: UniProtKB

ubiquitin protein ligase binding

Inferred from physical interaction Ref.16Ref.28. Source: UniProtKB

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 736736Dynamin-1-like protein
PRO_0000206566

Regions

Domain644 – 73592GED
Nucleotide binding32 – 398GTP
Nucleotide binding146 – 1505GTP
Nucleotide binding215 – 2184GTP
Nucleotide binding246 – 2494GTP
Region1 – 343343GTPase domain
Region344 – 489146Middle domain
Region448 – 685238Interaction with GSK3B
Region502 – 56968B domain
Region654 – 66815Important for homodimerization

Amino acid modifications

Modified residue11N-acetylmethionine Ref.27 Ref.40
Modified residue5481Phosphoserine Ref.25
Modified residue5971N6-acetyllysine; alternate By similarity
Modified residue6071Phosphoserine Ref.25
Modified residue6161Phosphoserine; by CDK1 Ref.24 Ref.25 Ref.26 Ref.31 Ref.34 Ref.38
Modified residue6371Phosphoserine; by CAMK1 and PKA Ref.20 Ref.23 Ref.26 Ref.42
Modified residue6441S-nitrosocysteine Ref.32
Glycosylation5851O-linked (GlcNAc) By similarity
Glycosylation5861O-linked (GlcNAc) By similarity
Cross-link532Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.29
Cross-link535Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.29
Cross-link558Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.29
Cross-link568Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.29
Cross-link594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Cross-link597Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate Ref.29
Cross-link606Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Probable
Cross-link608Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.29

Natural variations

Alternative sequence831N → NDPATWKNSRHLSK in isoform 6.
VSP_039097
Alternative sequence533 – 56937Missing in isoform 3.
VSP_013685
Alternative sequence533 – 55826Missing in isoform 2.
VSP_013686
Alternative sequence544 – 56926Missing in isoform 5.
VSP_013687
Alternative sequence559 – 56911Missing in isoform 4.
VSP_013688
Natural variant711S → T. Ref.2 Ref.3 Ref.4
Corresponds to variant rs1064610 [ dbSNP | Ensembl ].
VAR_022446
Natural variant3951A → D in EMPF; the mutation acts in a dominant-negative manner; defects observed in both mitochondrial and peroxisomal fission. Ref.22
VAR_063704
Natural variant4261E → D.
Corresponds to variant rs2389105 [ dbSNP | Ensembl ].
VAR_030489

Experimental info

Mutagenesis341Q → A: Abolishes GTP hydrolysis. Ref.46
Mutagenesis381K → 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.29 Ref.46
Mutagenesis381K → E: Overexpression delays protein secretion. Ref.3 Ref.12 Ref.13 Ref.15 Ref.29 Ref.46
Mutagenesis391S → A: Abolishes GTP hydrolysis. Ref.8 Ref.14 Ref.46
Mutagenesis391S → I: Decreased localization to the perinuclear region. Ref.8 Ref.14 Ref.46
Mutagenesis391S → N: Reduces peroxisomal abundance. Ref.8 Ref.14 Ref.46
Mutagenesis411V → F: Temperature-sensitive. Impairs mitochondrial division. Ref.12
Mutagenesis591T → A: Abolishes GTP hydrolysis. Impairs mitochondrial division. Reduces peroxisomal abundance. Ref.12 Ref.14 Ref.46
Mutagenesis1461D → A: Abolishes GTP hydrolysis. Ref.46
Mutagenesis1491G → A: Abolishes GTP hydrolysis. Ref.46
Mutagenesis2161K → A: Abolishes GTP hydrolysis. Ref.46
Mutagenesis2181D → A: Abolishes GTP hydrolysis. Ref.46
Mutagenesis2811G → D: Temperature-sensitive. Impairs mitochondrial division. Ref.12
Mutagenesis3001C → A: No effect on S-nitrosylation. Ref.32
Mutagenesis3451C → A: No effect on S-nitrosylation. Ref.32
Mutagenesis3611C → A: No effect on S-nitrosylation. Ref.32
Mutagenesis3671C → A: No effect on S-nitrosylation. Ref.32
Mutagenesis401 – 4044GPRP → AAAA: Impairs formation of higher order oligomers, but not homodimerization. Ref.45
Mutagenesis4311C → A: No effect on S-nitrosylation. Ref.32
Mutagenesis4461C → A: No effect on S-nitrosylation. Ref.32
Mutagenesis4701C → A: No effect on S-nitrosylation. Ref.32
Mutagenesis4901E → A: Does not impair homodimerization and formation of higher order oligomers. Ref.45
Mutagenesis4901E → R: Impairs homodimerization and formation of higher order oligomers. Ref.45
Mutagenesis5051C → A: No effect on S-nitrosylation. Ref.32
Mutagenesis5321K → 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.29
Mutagenesis5351K → 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.29
Mutagenesis5581K → 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.29
Mutagenesis5681K → 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.29
Mutagenesis5941K → 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.29
Mutagenesis5971K → 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.29
Mutagenesis6061K → 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.29
Mutagenesis6081K → 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.29
Mutagenesis6161S → A: Little effect on mitochondrial morphology. Translocated to mitochondria. Ref.26
Mutagenesis6371S → A: Abolishes phosphorylation. Reduces interaction with MIEF1 and MIEF2. Promotes mitochondrial fission and cell vulnerability to apoptotic insults. Mostly mitochondrial. Disrupts, in vitro, binding to FIS1. Ref.20 Ref.23 Ref.26 Ref.42
Mutagenesis6371S → D: Impairs intramolecular, but not intermolecular interactions. Slight reduction in GTPase activity. Does not reduce interaction with MIEF1 and MIEF2. Inhibits mitochondrial fission. Retained in cytoplasm. Ref.20 Ref.23 Ref.26 Ref.42
Mutagenesis6441C → A: Abolishes S-nitrosylation. Reduced dimerization and no enhancement of GTPase activity. Ref.32
Mutagenesis6681K → A: Abolishes homodimerization and formation of higher order oligomers. Ref.45
Mutagenesis6791K → 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 conflict2081R → C in AAC35283. Ref.2
Sequence conflict2081R → C in AAD39541. Ref.4

Secondary structure

............................................................................................ 736
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (HdynIV-WT) (DLP1F) [UniParc].

Last modified February 6, 2007. Version 2.
Checksum: F9521A376B785B71

FASTA73681,877
        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 

« Hide

Isoform 4 (HdynIV-11) (DLP1c) [UniParc].

Checksum: 208E830E9F906B7F
Show »

FASTA72580,536
Isoform 2 (DLP1a) [UniParc].

Checksum: 05BC4782DACC1C63
Show »

FASTA71079,442
Isoform 3 (HdynIV-37) (DLP1b) [UniParc].

Checksum: CB252ECCC9871127
Show »

FASTA69978,100
Isoform 5 (HdynIV-26) [UniParc].

Checksum: 0021B07297C5A6CC
Show »

FASTA71079,109
Isoform 6 [UniParc].

Checksum: 64E6658C90A577AA
Show »

FASTA74983,399

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"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.
[29]"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.
[30]"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.
[31]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[32]"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.
[33]"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.
[34]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[35]"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].
[36]"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 MIEF2 AND MIEF1.
[37]"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 MIEF1.
[38]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[39]"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.
[40]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[41]"MiD49 and MiD51 can act independently of Mff and Fis1 in Drp1 recruitment and are specific for mitochondrial fission."
Palmer C.S., Elgass K.D., Parton R.G., Osellame L.D., Stojanovski D., Ryan M.T.
J. Biol. Chem. 288:27584-27593(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[42]"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
Loson O.C., Song Z., Chen H., Chan D.C.
Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MIEF2 AND MIEF1, PHOSPHORYLATION AT SER-637, MUTAGENESIS OF SER-637.
[43]"A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics during endocytosis."
Li H., Alavian K.N., Lazrove E., Mehta N., Jones A., Zhang P., Licznerski P., Graham M., Uo T., Guo J., Rahner C., Duman R.S., Morrison R.S., Jonas E.A.
Nat. Cell Biol. 15:773-785(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BCL2L1.
[44]"Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission."
Koirala S., Guo Q., Kalia R., Bui H.T., Eckert D.M., Frost A., Shaw J.M.
Proc. Natl. Acad. Sci. U.S.A. 110:E1342-E1351(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MIEF2, SUBUNIT.
[45]"Structural insights into oligomerization and mitochondrial remodelling of dynamin 1-like protein."
Frohlich C., Grabiger S., Schwefel D., Faelber K., Rosenbaum E., Mears J., Rocks O., Daumke O.
EMBO J. 32:1280-1292(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.48 ANGSTROMS), FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, MUTAGENESIS OF 401-GLY--PRO-404; GLU-490 AND LYS-668, LIPID-BINDING.
[46]"Functional mapping of human dynamin-1-like GTPase domain based on x-ray structure analyses."
Wenger J., Klinglmayr E., Frohlich C., Eibl C., Gimeno A., Hessenberger M., Puehringer S., Daumke O., Goettig P.
PLoS ONE 8:E71835-E71835(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-327 AND 711-736 IN COMPLEX WITH GTP ANALOGS, CATALYTIC ACTIVITY, MUTAGENESIS OF GLN-34; LYS-38; SER-39; THR-59; ASP-146; GLY-149; LYS-216 AND ASP-218, ENZYME REGULATION, SUBUNIT.
+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.
PIRJC5695.
RefSeqNP_001265392.1. NM_001278463.1.
NP_001265393.1. NM_001278464.1.
NP_005681.2. NM_005690.4.
NP_036192.2. NM_012062.4.
NP_036193.2. NM_012063.3.
UniGeneHs.556296.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3W6NX-ray2.00A/B1-329[»]
A/B709-736[»]
3W6OX-ray1.90A/B1-329[»]
A/B709-736[»]
3W6PX-ray1.70A/B1-329[»]
A/B709-736[»]
4BEJX-ray3.48A/B/C/D1-736[»]
4H1UX-ray2.30A711-736[»]
4H1VX-ray2.30A2-327[»]
ProteinModelPortalO00429.
SMRO00429. Positions 1-729.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115370. 35 interactions.
IntActO00429. 12 interactions.
MINTMINT-1394198.
STRING9606.ENSP00000266481.

PTM databases

PhosphoSiteO00429.

Proteomic databases

PaxDbO00429.
PRIDEO00429.

Protocols and materials databases

DNASU10059.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000266481; ENSP00000266481; ENSG00000087470. [O00429-4]
ENST00000452533; ENSP00000415131; ENSG00000087470. [O00429-3]
ENST00000547312; ENSP00000448610; ENSG00000087470. [O00429-2]
ENST00000549701; ENSP00000450399; ENSG00000087470. [O00429-1]
ENST00000553257; ENSP00000449089; ENSG00000087470. [O00429-6]
GeneID10059.
KEGGhsa:10059.
UCSCuc001rld.2. human. [O00429-1]
uc001rle.2. human. [O00429-3]
uc001rlf.2. human. [O00429-4]

Organism-specific databases

CTD10059.
GeneCardsGC12P032832.
H-InvDBHIX0010537.
HGNCHGNC:2973. DNM1L.
HPACAB009952.
HPA039324.
MIM603850. gene.
614388. phenotype.
neXtProtNX_O00429.
Orphanet330050. Lethal encephalopathy due to mitochondrial and peroxisomal fission defect.
PharmGKBPA27441.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0699.
HOVERGENHBG107833.
KOK17065.
OMARDKSYKV.
OrthoDBEOG7GJ6CB.
PhylomeDBO00429.
TreeFamTF352031.

Enzyme and pathway databases

ReactomeREACT_578. Apoptosis.

Gene expression databases

ArrayExpressO00429.
BgeeO00429.
CleanExHS_DNM1L.
GenevestigatorO00429.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR022812. Dynamin_SF.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11566. PTHR11566. 1 hit.
PfamPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSPR00195. DYNAMIN.
SMARTSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNM1L. human.
GeneWikiDNM1L.
GenomeRNAi10059.
NextBio38007.
PMAP-CutDBO00429.
PROO00429.
SOURCESearch...

Entry information

Entry nameDNM1L_HUMAN
AccessionPrimary (citable) accession number: O00429
Secondary accession number(s): A8K4X9 expand/collapse secondary AC list , 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: April 16, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM