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Dynamin-1-like protein (EC 3.6.5.5) (Dynamin-like protein)

 DNM1L_RAT               Reviewed;         755 AA.
O35303; O35318; O35319; O35320; O35321; O35322; O35323; Q5U2W1;
Q792T7; Q9R234; Q9R277;
10-MAY-2005, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
20-DEC-2017, entry version 142.
RecName: Full=Dynamin-1-like protein;
EC=3.6.5.5;
AltName: Full=Dynamin-like protein;
Name=Dnm1l; Synonyms=Dlp1, Drp1;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6), PROTEIN
SEQUENCE OF 39-48; 62-74; 113-126; 147-160; 174-180 AND 700-710,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain, and Liver;
PubMed=9472031; DOI=10.1083/jcb.140.4.779;
Yoon Y., Pitts K.R., Dahan S., McNiven M.A.;
"A novel dynamin-like protein associates with cytoplasmic vesicles and
tubules of the endoplasmic reticulum in mammalian cells.";
J. Cell Biol. 140:779-793(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 5), TISSUE SPECIFICITY,
AND INTERACTION WITH GSK3B.
TISSUE=Brain;
PubMed=10679301; DOI=10.1006/bbrc.2000.2197;
Chen C.-H., Hwang S.-L., Howng S.-L., Chou C.-K., Hong Y.-R.;
"Three rat brain alternative splicing dynamin-like protein variants:
interaction with the glycogen synthase kinase 3beta and action as a
substrate.";
Biochem. Biophys. Res. Commun. 268:893-898(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 39-48; 174-180; 252-260; 343-352; 379-389; 472-486
AND 672-678, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=Sprague-Dawley; TISSUE=Hippocampus, and Spinal cord;
Lubec G., Afjehi-Sadat L., Diao W.;
Submitted (APR-2007) to UniProtKB.
[5]
MUTAGENESIS OF LYS-38 AND ASP-231, OLIGOMERIZATION, AND FUNCTION.
PubMed=11553726; DOI=10.1091/mbc.12.9.2894;
Yoon Y., Pitts K.R., McNiven M.A.;
"Mammalian dynamin-like protein DLP1 tubulates membranes.";
Mol. Biol. Cell 12:2894-2905(2001).
[6]
SUBCELLULAR LOCATION, INDUCTION BY BEZAFIBRATE, AND FUNCTION.
PubMed=12499366; DOI=10.1074/jbc.M211761200;
Koch A., Thiemann M., Grabenbauer M., Yoon Y., McNiven M.A.,
Schrader M.;
"Dynamin-like protein 1 is involved in peroxisomal fission.";
J. Biol. Chem. 278:8597-8605(2003).
[7]
FUNCTION, INTERACTION WITH FIS1, AND SUBCELLULAR LOCATION.
PubMed=12861026; DOI=10.1128/MCB.23.15.5409-5420.2003;
Yoon Y., Krueger E.W., Oswald B.J., McNiven M.A.;
"The mitochondrial protein hFis1 regulates mitochondrial fission in
mammalian cells through an interaction with the dynamin-like protein
DLP1.";
Mol. Cell. Biol. 23:5409-5420(2003).
[8]
PHOSPHORYLATION AT SER-635, FUNCTION, AND MUTAGENESIS OF SER-71;
SER-139; SER-149 AND SER-635.
PubMed=17301055; DOI=10.1074/jbc.M607279200;
Taguchi N., Ishihara N., Jofuku A., Oka T., Mihara K.;
"Mitotic phosphorylation of dynamin-related GTPase Drp1 participates
in mitochondrial fission.";
J. Biol. Chem. 282:11521-11529(2007).
[9]
INTERACTION WITH BCL2L1, FUNCTION, AND MUTAGENESIS OF LYS-38.
PubMed=18250306; DOI=10.1073/pnas.0711647105;
Li H., Chen Y., Jones A.F., Sanger R.H., Collis L.P., Flannery R.,
McNay E.C., Yu T., Schwarzenbacher R., Bossy B., Bossy-Wetzel E.,
Bennett M.V., Pypaert M., Hickman J.A., Smith P.J., Hardwick J.M.,
Jonas E.A.;
"Bcl-xL induces Drp1-dependent synapse formation in cultured
hippocampal neurons.";
Proc. Natl. Acad. Sci. U.S.A. 105:2169-2174(2008).
[10]
GLYCOSYLATION AT THR-604 AND THR-605, AND SUBCELLULAR LOCATION.
PubMed=22745122; DOI=10.1074/jbc.M112.390682;
Gawlowski T., Suarez J., Scott B., Torres-Gonzalez M., Wang H.,
Schwappacher R., Han X., Yates J.R. III, Hoshijima M., Dillmann W.;
"Modulation of dynamin-related protein 1 (DRP1) function by increased
O-linked-beta-N-acetylglucosamine modification (O-GlcNAc) in cardiac
myocytes.";
J. Biol. Chem. 287:30024-30034(2012).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-635, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[12]
FUNCTION IN SYNAPTIC VESICLE REGULATION, INTERACTION WITH BCL2L1; CLTA
AND MFF, AND SUBCELLULAR LOCATION.
PubMed=23792689; DOI=10.1038/ncb2791;
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.;
"A Bcl-xL-Drp1 complex regulates synaptic vesicle membrane dynamics
during endocytosis.";
Nat. Cell Biol. 15:773-785(2013).
[13]
PHOSPHORYLATION AT SER-656.
PubMed=28463107; DOI=10.7554/eLife.21374;
Monterisi S., Lobo M.J., Livie C., Castle J.C., Weinberger M.,
Baillie G., Surdo N.C., Musheshe N., Stangherlin A., Gottlieb E.,
Maizels R., Bortolozzi M., Micaroni M., Zaccolo M.;
"PDE2A2 regulates mitochondria morphology and apoptotic cell death via
local modulation of cAMP/PKA signalling.";
Elife 6:0-0(2017).
-!- 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. Plays an important
role in mitochondrial fission during mitosis. Required for
formation of endocytic vesicles. Proposed to regulate synaptic
vesicle membrane dynamics through association with BCL2L1 isoform
Bcl-X(L) which stimulates its GTPase activity in synaptic
vesicles; the function may require its recruitment by MFF to
clathrin-containing vesicles. Required for programmed necrosis
execution. {ECO:0000269|PubMed:11553726,
ECO:0000269|PubMed:12499366, ECO:0000269|PubMed:12861026,
ECO:0000269|PubMed:17301055, ECO:0000269|PubMed:18250306,
ECO:0000269|PubMed:23792689}.
-!- CATALYTIC ACTIVITY: GTP + H(2)O = GDP + phosphate.
-!- SUBUNIT: 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. {ECO:0000269|PubMed:10679301,
ECO:0000269|PubMed:12861026, ECO:0000269|PubMed:18250306,
ECO:0000269|PubMed:23792689}.
-!- INTERACTION:
P53563-1:Bcl2l1; NbExp=4; IntAct=EBI-1767447, EBI-287204;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250}. Golgi
apparatus {ECO:0000250}. Endomembrane system; Peripheral membrane
protein. Mitochondrion outer membrane; Peripheral membrane
protein. Peroxisome {ECO:0000250}. Membrane, clathrin-coated pit.
Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane.
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. Binds to
phospholipid membranes (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1;
IsoId=O35303-1; Sequence=Displayed;
Name=2;
IsoId=O35303-2; Sequence=VSP_013697, VSP_013701;
Name=3; Synonyms=DLP1-37;
IsoId=O35303-3; Sequence=VSP_013698, VSP_013699;
Name=4;
IsoId=O35303-4; Sequence=VSP_013696;
Note=No experimental confirmation available.;
Name=5; Synonyms=DLP1-11;
IsoId=O35303-5; Sequence=VSP_013702;
Name=6;
IsoId=O35303-6; Sequence=VSP_013700;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in all tissues tested (at protein
level). Longer isoforms are preferentially expressed in brain.
{ECO:0000269|PubMed:10679301, ECO:0000269|PubMed:9472031}.
-!- INDUCTION: By bezafibrate. {ECO:0000269|PubMed:12499366}.
-!- 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. {ECO:0000250}.
-!- PTM: Phosphorylation/dephosphorylation events on two sites near
the GED domain regulate mitochondrial fission. Phosphorylation on
Ser-656 inhibits mitochondrial fission probably through preventing
intramolecular interaction. Dephosphorylated on this site by
PPP3CA which promotes mitochondrial fission. Phosphorylation on
Ser-635 also promotes mitochondrial fission (By similarity).
{ECO:0000250}.
-!- PTM: 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 (By similarity).
{ECO:0000250}.
-!- PTM: S-nitrosylation increases DNM1L dimerization, mitochondrial
fission and causes neuronal damage. {ECO:0000250}.
-!- PTM: Ubiquitinated by MARCH5. {ECO:0000250}.
-!- PTM: 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-656. {ECO:0000269|PubMed:17301055}.
-!- SIMILARITY: Belongs to the TRAFAC class dynamin-like GTPase
superfamily. Dynamin/Fzo/YdjA family. {ECO:0000305}.
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EMBL; AF019043; AAB72197.1; -; mRNA.
EMBL; AF020207; AAB71232.1; -; mRNA.
EMBL; AF020208; AAB71233.1; -; mRNA.
EMBL; AF020209; AAB71234.1; -; mRNA.
EMBL; AF020210; AAB71235.1; -; mRNA.
EMBL; AF020211; AAB71236.1; -; mRNA.
EMBL; AF020212; AAB71237.1; -; mRNA.
EMBL; AF020213; AAB71238.1; -; mRNA.
EMBL; AF107048; AAD22412.1; -; mRNA.
EMBL; AF132727; AAD31278.1; -; mRNA.
EMBL; BC085843; AAH85843.1; -; mRNA.
RefSeq; NP_446107.2; NM_053655.3. [O35303-2]
RefSeq; XP_006248785.1; XM_006248723.3. [O35303-6]
RefSeq; XP_008767063.1; XM_008768841.2. [O35303-1]
RefSeq; XP_008767064.1; XM_008768842.2. [O35303-4]
RefSeq; XP_008767065.1; XM_008768843.2. [O35303-5]
UniGene; Rn.216851; -.
ProteinModelPortal; O35303; -.
SMR; O35303; -.
BioGrid; 250292; 3.
CORUM; O35303; -.
DIP; DIP-29699N; -.
ELM; O35303; -.
IntAct; O35303; 5.
MINT; MINT-4582542; -.
STRING; 10116.ENSRNOP00000002478; -.
iPTMnet; O35303; -.
PhosphoSitePlus; O35303; -.
PaxDb; O35303; -.
PeptideAtlas; O35303; -.
PRIDE; O35303; -.
Ensembl; ENSRNOT00000002477; ENSRNOP00000002477; ENSRNOG00000001813. [O35303-2]
Ensembl; ENSRNOT00000002478; ENSRNOP00000002478; ENSRNOG00000001813. [O35303-1]
Ensembl; ENSRNOT00000002482; ENSRNOP00000002482; ENSRNOG00000001813. [O35303-6]
GeneID; 114114; -.
KEGG; rno:114114; -.
CTD; 10059; -.
RGD; 620416; Dnm1l.
eggNOG; KOG0446; Eukaryota.
eggNOG; COG0699; LUCA.
GeneTree; ENSGT00760000119213; -.
HOVERGEN; HBG107833; -.
InParanoid; O35303; -.
KO; K17065; -.
OMA; HHIPNRR; -.
OrthoDB; EOG091G02TQ; -.
PhylomeDB; O35303; -.
TreeFam; TF352031; -.
Reactome; R-RNO-75153; Apoptotic execution phase.
PRO; PR:O35303; -.
Proteomes; UP000002494; Chromosome 11.
Bgee; ENSRNOG00000001813; -.
Genevisible; O35303; RN.
GO; GO:0005903; C:brush border; ISO:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; ISO:RGD.
GO; GO:0005829; C:cytosol; IDA:ParkinsonsUK-UCL.
GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
GO; GO:0005794; C:Golgi apparatus; ISO:RGD.
GO; GO:0000139; C:Golgi membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:RGD.
GO; GO:0016020; C:membrane; ISO:RGD.
GO; GO:0005874; C:microtubule; ISO:RGD.
GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; IDA:RGD.
GO; GO:0099073; C:mitochondrion-derived vesicle; IEA:Ensembl.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005777; C:peroxisome; IDA:RGD.
GO; GO:0043234; C:protein complex; ISO:RGD.
GO; GO:0099503; C:secretory vesicle; IDA:ParkinsonsUK-UCL.
GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
GO; GO:0051433; F:BH2 domain binding; IPI:CAFA.
GO; GO:0030276; F:clathrin binding; IPI:CAFA.
GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
GO; GO:0030742; F:GTP-dependent protein binding; ISO:RGD.
GO; GO:0003924; F:GTPase activity; ISS:UniProtKB.
GO; GO:0042802; F:identical protein binding; ISO:RGD.
GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
GO; GO:0017137; F:Rab GTPase binding; ISO:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
GO; GO:0071396; P:cellular response to lipid; IEP:RGD.
GO; GO:0090650; P:cellular response to oxygen-glucose deprivation; IEP:RGD.
GO; GO:1904579; P:cellular response to thapsigargin; IMP:RGD.
GO; GO:0003374; P:dynamin family protein polymerization involved in mitochondrial fission; ISS:UniProtKB.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
GO; GO:0060047; P:heart contraction; ISO:RGD.
GO; GO:0048312; P:intracellular distribution of mitochondria; IMP:RGD.
GO; GO:0061025; P:membrane fusion; ISO:RGD.
GO; GO:0000266; P:mitochondrial fission; ISS:UniProtKB.
GO; GO:0043653; P:mitochondrial fragmentation involved in apoptotic process; IMP:RGD.
GO; GO:0090149; P:mitochondrial membrane fission; ISO:RGD.
GO; GO:0070584; P:mitochondrion morphogenesis; IMP:RGD.
GO; GO:0007005; P:mitochondrion organization; ISO:RGD.
GO; GO:0070266; P:necroptotic process; ISS:UniProtKB.
GO; GO:0010637; P:negative regulation of mitochondrial fusion; IMP:CAFA.
GO; GO:0016559; P:peroxisome fission; ISS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:RGD.
GO; GO:0061003; P:positive regulation of dendritic spine morphogenesis; IMP:RGD.
GO; GO:2001244; P:positive regulation of intrinsic apoptotic signaling pathway; ISO:RGD.
GO; GO:0090141; P:positive regulation of mitochondrial fission; IMP:RGD.
GO; GO:0050714; P:positive regulation of protein secretion; ISO:RGD.
GO; GO:0090200; P:positive regulation of release of cytochrome c from mitochondria; ISO:RGD.
GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; IMP:CAFA.
GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; IMP:CAFA.
GO; GO:0051260; P:protein homooligomerization; IDA:RGD.
GO; GO:0051289; P:protein homotetramerization; ISO:RGD.
GO; GO:0070585; P:protein localization to mitochondrion; ISO:RGD.
GO; GO:0051259; P:protein oligomerization; ISS:UniProtKB.
GO; GO:1903578; P:regulation of ATP metabolic process; ISO:RGD.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:RGD.
GO; GO:0010821; P:regulation of mitochondrion organization; ISO:RGD.
GO; GO:1900063; P:regulation of peroxisome organization; ISO:RGD.
GO; GO:0032459; P:regulation of protein oligomerization; ISO:RGD.
GO; GO:0001836; P:release of cytochrome c from mitochondria; ISO:RGD.
GO; GO:1905395; P:response to flavonoid; IEP:RGD.
GO; GO:1990910; P:response to hypobaric hypoxia; IEP:RGD.
GO; GO:0036466; P:synaptic vesicle recycling via endosome; IMP:CAFA.
CDD; cd08771; DLP_1; 1.
InterPro; IPR030556; DNM1L.
InterPro; IPR000375; Dynamin_central.
InterPro; IPR001401; Dynamin_GTPase.
InterPro; IPR019762; Dynamin_GTPase_CS.
InterPro; IPR022812; Dynamin_SF.
InterPro; IPR030381; G_DYNAMIN_dom.
InterPro; IPR003130; GED.
InterPro; IPR020850; GED_dom.
InterPro; IPR027417; P-loop_NTPase.
PANTHER; PTHR11566; PTHR11566; 1.
PANTHER; PTHR11566:SF39; PTHR11566:SF39; 1.
Pfam; PF01031; Dynamin_M; 1.
Pfam; PF00350; Dynamin_N; 1.
Pfam; PF02212; GED; 1.
PRINTS; PR00195; DYNAMIN.
SMART; SM00053; DYNc; 1.
SMART; SM00302; GED; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00410; G_DYNAMIN_1; 1.
PROSITE; PS51718; G_DYNAMIN_2; 1.
PROSITE; PS51388; GED; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Cell junction; Coated pit;
Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Direct protein sequencing; Endocytosis; Glycoprotein; Golgi apparatus;
GTP-binding; Hydrolase; Isopeptide bond; Lipid-binding; Membrane;
Mitochondrion; Mitochondrion outer membrane; Necrosis;
Nucleotide-binding; Peroxisome; Phosphoprotein; Reference proteome;
S-nitrosylation; Synapse; Ubl conjugation.
CHAIN 1 755 Dynamin-1-like protein.
/FTId=PRO_0000206568.
DOMAIN 22 315 Dynamin-type G.
DOMAIN 663 754 GED. {ECO:0000255|PROSITE-
ProRule:PRU00720}.
NP_BIND 32 40 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 228 234 GTP. {ECO:0000250|UniProtKB:O00429}.
NP_BIND 259 262 GTP. {ECO:0000250|UniProtKB:O00429}.
REGION 1 356 GTPase domain. {ECO:0000250}.
REGION 1 356 N-terminal dimerization domain.
{ECO:0000250}.
REGION 357 502 Middle domain. {ECO:0000250}.
REGION 461 704 Interaction with GSK3B. {ECO:0000250}.
REGION 461 667 Interaction with GSK3B. {ECO:0000250}.
REGION 515 582 B domain. {ECO:0000250}.
REGION 555 755 C-terminal dimerization domain.
{ECO:0000250}.
REGION 673 687 Important for homodimerization.
{ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000250|UniProtKB:O00429}.
MOD_RES 542 542 Phosphoserine.
{ECO:0000250|UniProtKB:O00429}.
MOD_RES 561 561 Phosphoserine.
{ECO:0000250|UniProtKB:O00429}.
MOD_RES 616 616 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:Q8K1M6}.
MOD_RES 626 626 Phosphoserine.
{ECO:0000250|UniProtKB:O00429}.
MOD_RES 635 635 Phosphoserine; by CDK1.
{ECO:0000244|PubMed:22673903,
ECO:0000269|PubMed:17301055}.
MOD_RES 656 656 Phosphoserine; by CAMK1 and PKA.
{ECO:0000269|PubMed:28463107}.
MOD_RES 663 663 S-nitrosocysteine.
{ECO:0000250|UniProtKB:O00429}.
CARBOHYD 604 604 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:22745122}.
CARBOHYD 605 605 O-linked (GlcNAc) threonine.
{ECO:0000269|PubMed:22745122}.
CROSSLNK 545 545 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 548 548 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 571 571 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 581 581 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 613 613 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 616 616 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 625 625 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
CROSSLNK 627 627 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250}.
VAR_SEQ 84 97 DPATWKNSRHLSKG -> GKFQSWR (in isoform 4).
{ECO:0000303|PubMed:9472031}.
/FTId=VSP_013696.
VAR_SEQ 84 96 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9472031}.
/FTId=VSP_013697.
VAR_SEQ 84 84 D -> GKFQSWN (in isoform 3).
{ECO:0000303|PubMed:10679301,
ECO:0000303|PubMed:9472031}.
/FTId=VSP_013698.
VAR_SEQ 546 596 SSKVPSALAPASQEPSPAASAEADGKLIQDNRRETKNVASA
GGGIGDGGRI -> VASGGGGV (in isoform 3).
{ECO:0000303|PubMed:10679301,
ECO:0000303|PubMed:9472031}.
/FTId=VSP_013699.
VAR_SEQ 546 582 Missing (in isoform 6).
{ECO:0000303|PubMed:9472031}.
/FTId=VSP_013700.
VAR_SEQ 546 571 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9472031}.
/FTId=VSP_013701.
VAR_SEQ 572 582 Missing (in isoform 5).
{ECO:0000303|PubMed:10679301,
ECO:0000303|PubMed:9472031}.
/FTId=VSP_013702.
MUTAGEN 38 38 K->A: Defective in GTP hydrolysis.
Tubulates spherical liposomes. Impairs
mitochondrial division. Decreases the
BCL2L1-mediated induction of synapse
number and size of synaptic vesicle
clusters. {ECO:0000269|PubMed:11553726,
ECO:0000269|PubMed:18250306}.
MUTAGEN 71 71 S->A: No effect on mitotic
phosphorylation.
{ECO:0000269|PubMed:17301055}.
MUTAGEN 139 139 S->A: No effect on mitotic
phosphorylation.
{ECO:0000269|PubMed:17301055}.
MUTAGEN 149 149 S->A: No effect on mitotic
phosphorylation.
{ECO:0000269|PubMed:17301055}.
MUTAGEN 231 231 D->N: Defective in GTP-binding.
{ECO:0000269|PubMed:11553726}.
MUTAGEN 635 635 S->A: Abolishes mitotic phosphorylation.
Reduced mitotic mitochondrial
fragmentation.
{ECO:0000269|PubMed:17301055}.
CONFLICT 517 517 A -> V (in Ref. 1; AAB71237).
{ECO:0000305}.
CONFLICT 600 600 G -> V (in Ref. 2; AAD31278).
{ECO:0000305}.
SEQUENCE 755 AA; 83908 MW; 0568353907794C43 CRC64;
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGVVTR
RPLILQLVHV SPEDKRKTTG EENDPATWKN SRHLSKGVEA EEWGKFLHTK NKLYTDFDEI
RQEIENETER ISGNNKGVSP EPIHLKVFSP NVVNLTLVDL PGMTKVPVGD QPKDIELQIR
ELILRFISNP NSIILAVTAA NTDMATSEAL KISREVDPDG RRTLAVITKL DLMDAGTDAM
DVLMGRVIPV KLGIIGVVNR SQLDINNKKS VTDSIRDEYA FLQKKYPSLA NRNGTKYLAR
TLNRLLMHHI RDCLPELKTR INVLAAQYQS LLNSYGEPVD DKSATLLQLI TKFATEYCNT
IEGTAKYIET SELCGGARIC YIFHETFGRT LESVDPLGGL NTIDILTAIR NATGPRPALF
VPEVSFELLV KRQIKRLEEP SLRCVELVHE EMQRIIQHCS NYSTQELLRF PKLHDAIVEV
VTCLLRKRLP VTNEMVHNLV AIELAYINTK HPDFADACGL MNNNIEEQRR NRLARELPSA
VSRDKSSKVP SALAPASQEP SPAASAEADG KLIQDNRRET KNVASAGGGI GDGGRIGDGG
QEPTTGNWRG MLKTSKAEEL LAEEKSKPIP IMPASPQKGH AVNLLDVPVP VARKLSAREQ
RDCEVIERLI KSYFLIVRKN IQDSVPKAVM HFLVNHVKDT LQSELVGQLY KSSLLDDLLT
ESEDMAQRRK EAADMLKALQ GASQIIAEIR ETHLW


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