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Details on Person UniProt:Q05193 DNM1

Class:Id	ReferenceGeneProduct:54032
_chainChangeLog	chain:1-864 added on Fri February 6 2015
_displayName	UniProt:Q05193 DNM1
_timestamp	2025-02-21 18:46:17
chain	chain:1-864
checksum	7FCD8CB572FFEAEF
comment	FUNCTION Catalyzes the hydrolysis of GTP and utilizes this energy to mediate vesicle scission and participates in many forms of endocytosis, such as clathrin-mediated endocytosis or synaptic vesicle endocytosis as well as rapid endocytosis (RE) (PubMed:15703209, PubMed:20428113, PubMed:29668686, PubMed:8101525, PubMed:8910402, PubMed:9362482). Associates to the membrane, through lipid binding, and self-assembles into rings and stacks of interconnected rings through oligomerization to form a helical polymer around the vesicle membrane leading to constriction of invaginated coated pits around their necks (PubMed:30069048, PubMed:7877694, PubMed:9922133). Self-assembly of the helical polymer induces membrane tubules narrowing until the polymer reaches a length sufficient to trigger GTP hydrolysis (PubMed:19084269). Depending on the curvature imposed on the tubules, membrane detachment from the helical polymer upon GTP hydrolysis can cause spontaneous hemifission followed by complete fission (PubMed:19084269). May play a role in regulating early stages of clathrin-mediated endocytosis in non-neuronal cells through its activation by dephosphorylation via the signaling downstream of EGFR (PubMed:29668686). Controls vesicle size at a step before fission, during formation of membrane pits, at hippocampal synapses (By similarity). Controls plastic adaptation of the synaptic vesicle recycling machinery to high levels of activity (By similarity). Mediates rapid endocytosis (RE), a Ca(2+)-dependent and clathrin- and K(+)-independent process in chromaffin cells (By similarity). Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP (By similarity). Through its interaction with DNAJC6, acts during the early steps of clathrin-coated vesicle (CCV) formation (PubMed:12791276).CATALYTIC ACTIVITY GTP + H2O = GDP + phosphate + H(+)ACTIVITY REGULATION GTPase activity is activated by 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate (PubMed:8910402). GTPase activity is inhibited by the heterodimer G protein formed by GNB1 and GNG2 with an IC(50)=400 nM when DNM1 concentration is 5 nM (PubMed:8910402).SUBUNIT Homodimer; homodimerization is mediated by the dynamin-type G domain which promotes assembly-stimulated GTPase activity (PubMed:20428113, PubMed:26612256). Homo-tetramer formed from two dimers in the absence of lipid (PubMed:30069048, PubMed:9362482). Oligomerizes into a helical polymer that self-assembles around the vesicle membrane, when associated to the menbrane through lipid binding (PubMed:30069048, PubMed:7877694, PubMed:9765310). Interacts (via C-terminal proline-rich domain (PRD)) with SNX9 (via SH3 domain); this interaction allows regulation of DNM1 self-assembly during late stages of endocytic vesicle formation and supports DNM1's early functions in accelerating clathrin-coated pits (CCPs) maturation in non neuronals cell (PubMed:15703209, PubMed:29668686). Interacts (via C-terminal proline-rich domain (PRD)) with MYO1E (via SH3 domain); this interaction regulates receptor-mediated endocytosis (PubMed:17257598). Interacts with SNX33 (via SH3 domain); this interaction decreases DNM1-dependent endocytosis (PubMed:18353773). Interacts with DIAPH1 (PubMed:23325789). Interacts with GRB2 (via SH3 domain); this interaction mediates disassembly of DNM1 polymers, therefore modulates self-assembly (PubMed:9922133). Forms a complex with BIN1 (via SH3 domain) and SH3GL2 (via SH3 domain). Forms a complex with SH3GL2 (via SH3 domain) and AMPH (via SH3 domain). Forms a complex with SH3GL2 (via SH3 domain) and SYNJ1. Interacts with AMPH. Interacts (via C-terminal proline-rich domain (PRD)) with SYT1; this interaction facilitates vesicle fission during clathrin-mediated endocytosis (CME). Interacts (via C-terminal proline-rich domain (PRD)) with PLCG1 (via SH3 domain); this interaction stimulates the release of GDP from DNM1 and enhances DNM1-dependent endocytosis. Interacts with SNPH; this interaction inhibits the binding of DNM1 to AMPH and DNM1-receptor-mediated endocytosis (By similarity). Interacts with CAV1. Interacts with SH3GLB1 (via SH3 domain). Interacts with PACSIN1 (via SH3 domain), PACSIN2 (via SH3 domain) and PACSIN3 (via SH3 domain). Interacts with UNC119; this interaction decreases DNM1's GTPase activity and affects DNM1's interaction with AMPH (By similarity). Interacts (GTP-bound form) with DNAJC6; this interaction allows clathrin-coated vesicle (CCV) formation at the plasma membrane (PubMed:12791276).INTERACTION Associated to the membrane in a helical polymer shape in a GTP bound state (PubMed:30069048). Transiently recruited to endocytic clathrin-coated pits (CCPs) at a late stage of clathrin-coated vesicle (CCV) formation (PubMed:15703209).ALTERNATIVE PRODUCTS The dynamin-type G mediates homodimerization and plays a role in self-assembly.DOMAIN The C-terminal proline-rich domain (PRD) mediates interaction with SH3-binding partners (By similarity). Is required for DNM1 self-assembly (PubMed:7877694).DOMAIN The PH domain binds phosphoinositides such as 1-phosphatidyl-1D-myo-inositol 4,5-bisphosphate, 1-phosphatidyl-1D-myo-inositol 3,4-bisphosphate and 1-phosphatidyl-1D-myo-inositol 3,4,5-trisphosphate, and mediates receptor-mediated endocytosis.PTM Phosphorylation at Ser-774 by GSK3B/GSK3-beta leads to inactivation of receptor-mediated endocytosis in non-neuronal cells (PubMed:29668686). Dephosphorylation at Ser-774, through the EGFR downstream signaling, leads to activation and regulates early stages of clathrin-mediated endocytosis (CME) (PubMed:29668686). Phosphorylated by CDK5 leading to synaptic vesicle endocytosis (SVE) activation (By similarity).DISEASE The disease is caused by variants affecting the gene represented in this entry.DISEASE The disease is caused by variants affecting the gene represented in this entry.SIMILARITY Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.SEQUENCE CAUTION Probable cloning artifact.
description	recommendedName: fullName evidence="34"Dynamin-1 ecNumber evidence="10 14 27 28"3.6.5.5 alternativeName: fullName evidence="32"Dynamin alternativeName: fullName evidence="33"Dynamin I
geneName	DNM1 DNM
identifier	Q05193
isSequenceChanged	FALSE
keyword	3D-structure Alternative splicing Cell membrane Cell projection Coated pit Cytoplasmic vesicle Disease variant Endocytosis Epilepsy GTP-binding Hydrolase Membrane Methylation Microtubule Motor protein Nitration Nucleotide-binding Phosphoprotein Proteomics identification Reference proteome Synapse
modified	[InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9862192] Weiser, Joel, 2024-02-26 [InstanceEdit:9909836] Weiser, Joel, 2024-05-14 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21
name	DNM1
referenceDatabase	[ReferenceDatabase:2] UniProt
referenceGene	[ReferenceDNASequence:8988364] ENSEMBL:ENSG00000106976 DNM1 [Homo sapiens]
secondaryIdentifier	DYN1_HUMAN A6NLM6 Q5SYX0 Q5SYX2 Q6P3T6 Q86VD2
sequenceLength	864
species	[Species:48887] Homo sapiens
(isoformParent)	[ReferenceIsoform:227768] UniProt:Q05193-2 DNM1 [Homo sapiens] [ReferenceIsoform:227769] UniProt:Q05193-3 DNM1 [Homo sapiens] [ReferenceIsoform:227771] UniProt:Q05193-5 DNM1 [Homo sapiens] [ReferenceIsoform:405179] UniProt:Q05193-1 DNM1 [Homo sapiens]
(referenceEntity)	[EntityWithAccessionedSequence:177488] DNM1 [plasma membrane] [Homo sapiens] [EntityWithAccessionedSequence:196150] DNM1 [lysosomal membrane] [Homo sapiens] [EntityWithAccessionedSequence:2213182] DNM1 [cytosol] [Homo sapiens]
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No pathways have been reviewed or authored by UniProt:Q05193 DNM1 (54032)