RAT:DYN1

Species (Taxon ID)	Rattus norvegicus (Rat). (10116)
Gene Name(s)	Dnm1 (synonyms: Dnm)
Protein Name(s)	Dynamin-1 B-dynamin D100 Dynamin, brain
External Links
UniProt	P21575
EMBL	X54531 CO398357 CB583951 CB708564
PIR	S11508
RefSeq	NP_542420.1
UniGene	Rn.10354
PDB	2AKA 3ZVR
PDBsum	2AKA 3ZVR
ProteinModelPortal	P21575
SMR	P21575
BioGrid	250837
DIP	DIP-30978N
IntAct	P21575
MINT	MINT-95899
STRING	10116.ENSRNOP00000046016
BindingDB	P21575
ChEMBL	CHEMBL1075191
PhosphoSite	P21575
World-2DPAGE	0004:P21575
PaxDb	P21575
PRIDE	P21575
Ensembl	ENSRNOT00000042762 ENSRNOT00000064039
GeneID	140694
KEGG	rno:140694
UCSC	RGD:71096
CTD	1759
RGD	71096
eggNOG	COG0699
GeneTree	ENSGT00760000119213
HOGENOM	HOG000161069
HOVERGEN	HBG107833
InParanoid	P21575
KO	K01528
OMA	KIKEPCL
OrthoDB	EOG76MK7N
PhylomeDB	P21575
BRENDA	3.6.5.5
Reactome	REACT_198830 REACT_235514 REACT_243437 REACT_247122 REACT_250855 REACT_262886
EvolutionaryTrace	P21575
NextBio	620679
PMAP-CutDB	P21575
Proteomes	UP000002494
ExpressionAtlas	P21575
Genevestigator	P21575
GO	GO:0005794 GO:0030117 GO:0005874 GO:0005886 GO:0043234 GO:0005525 GO:0003924 GO:0042802 GO:0050998 GO:0044822 GO:0008022 GO:0032403 GO:0007032 GO:0031623 GO:0006898
Gene3D	2.30.29.30 3.40.50.300
InterPro	IPR027741 IPR000375 IPR001401 IPR019762 IPR022812 IPR030381 IPR003130 IPR020850 IPR027417 IPR001849 IPR011993
PANTHER	PTHR11566 PTHR11566:SF32
Pfam	PF01031 PF02212 PF00169
PRINTS	PR00195
SMART	SM00053 SM00302 SM00233
SUPFAM	SSF52540
PROSITE	PS00410 PS51718 PS51388 PS50003

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0031623	receptor internalization	PMID:11100149^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0098835	presynaptic endocytic zone membrane	PMID:7877693^[2]	ECO:0006003	electron microscopy evidence used in manual assertion		C	part_of:(UBERON:0002298)	Seeded From UniProt	complete
part_of	GO:0098835	presynaptic endocytic zone membrane	PMID:7877693^[2]	ECO:0006064	cell-free assay evidence used in manual assertion		C	part_of:(UBERON:0002298)	Seeded From UniProt	complete
part_of	GO:0098835	presynaptic endocytic zone membrane	PMID:7877693^[2]	ECO:0006062	wide-field fluorescence microscopy evidence used in manual assertion		C	part_of:(UBERON:0002298)	Seeded From UniProt	complete
involved_in	GO:1904645	response to amyloid-beta	PMID:20847448^[3]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1903423	positive regulation of synaptic vesicle recycling	PMID:17880892^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900244	positive regulation of synaptic vesicle endocytosis	PMID:17437541^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:1900242	regulation of synaptic vesicle endocytosis	PMID:16648848^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0050998	nitric-oxide synthase binding	PMID:21490139^[7]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:3186	F		Seeded From UniProt	complete
part_of	GO:0045202	synapse	PMID:17880892^[4]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:9348539^[8]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:620274 RGD:621786	F		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:11563969^[9]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:3980 RGD:61857	F		Seeded From UniProt	complete
enables	GO:0044877	protein-containing complex binding	PMID:17257598^[10]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0043196	varicosity	PMID:12646135^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:17257598^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031749	D2 dopamine receptor binding	PMID:14709338^[12]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:2520	F		Seeded From UniProt	complete
enables	GO:0017124	SH3 domain binding	PMID:16648848^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:9348539^[8]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:621786	F		Seeded From UniProt	complete
enables	GO:0008022	protein C-terminus binding	PMID:9238017^[13]	ECO:0000353	physical interaction evidence used in manual assertion	RGD:708456	F		Seeded From UniProt	complete
part_of	GO:0008021	synaptic vesicle	PMID:12646135^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0006898	receptor-mediated endocytosis	PMID:12011079^[14]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:9725914^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	PMID:9725914^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:9725914^[15]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002031	G protein-coupled receptor internalization	PMID:14709338^[12]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0098884	postsynaptic neurotransmitter receptor internalization	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170172 RGD:727949	P		Seeded From UniProt	complete
part_of	GO:0098844	postsynaptic endocytic zone membrane	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170172 RGD:727949	C		Seeded From UniProt	complete
involved_in	GO:0050803	regulation of synapse structure or activity	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003392 PANTHER:PTN000170172	P		Seeded From UniProt	complete
part_of	GO:0045211	postsynaptic membrane	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170172 UniProtKB:P50570	C		Seeded From UniProt	complete
part_of	GO:0045202	synapse	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003392 PANTHER:PTN000170172 RGD:71096 RGD:727949 WB:WBGene00001130	C		Seeded From UniProt	complete
part_of	GO:0044327	dendritic spine head	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170172 RGD:727949	C		Seeded From UniProt	complete
part_of	GO:0043197	dendritic spine	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170172 RGD:727949	C		Seeded From UniProt	complete
involved_in	GO:0031623	receptor internalization	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000902093 RGD:71096 UniProtKB:P50570	P		Seeded From UniProt	complete
part_of	GO:0031410	cytoplasmic vesicle	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000902092 WB:WBGene00001130	C		Seeded From UniProt	complete
part_of	GO:0030424	axon	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170172 RGD:727949 WB:WBGene00001130	C		Seeded From UniProt	complete
involved_in	GO:0016185	synaptic vesicle budding from presynaptic endocytic zone membrane	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003392 MGI:MGI:107384 MGI:MGI:1341299 PANTHER:PTN000902093	P		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170013 TAIR:locus:2006777 TAIR:locus:2012763 UniProtKB:Q8S944	C		Seeded From UniProt	complete
part_of	GO:0014069	postsynaptic density	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170172 RGD:727949	C		Seeded From UniProt	complete
enables	GO:0008017	microtubule binding	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003392 PANTHER:PTN000170013	F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003392 PANTHER:PTN000902092 RGD:2513 RGD:71096	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0003392 MGI:MGI:1921256 PANTHER:PTN000170013 PomBase:SPBC12C2.08 RGD:2513 RGD:628821 RGD:71096 RGD:727949 TAIR:locus:2006777 UniProtKB:K7GKN2 UniProtKB:O00429 UniProtKB:P20591 UniProtKB:P27594 UniProtKB:P79135 UniProtKB:Q8IHR4 dictyBase:DDB_G0277849 dictyBase:DDB_G0277851	C		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	PMID:21873635^[16]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN000170013 RGD:2513 RGD:727949 SGD:S000001709 SGD:S000003924 UniProtKB:K7GKN2 UniProtKB:O00429 UniProtKB:O60313 UniProtKB:P27594 UniProtKB:P42697 UniProtKB:Q8S944 WB:WBGene00001130 dictyBase:DDB_G0277849	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21927001^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21575	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16432212^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P21575	F		Seeded From UniProt	complete
involved_in	GO:1901998	toxin transport	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	P		Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	C		Seeded From UniProt	complete
part_of	GO:0098835	presynaptic endocytic zone membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	C		Seeded From UniProt	complete
part_of	GO:0098684	photoreceptor ribbon synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	C		Seeded From UniProt	complete
involved_in	GO:0050804	modulation of chemical synaptic transmission	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	P		Seeded From UniProt	complete
involved_in	GO:0048488	synaptic vesicle endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	P		Seeded From UniProt	complete
part_of	GO:0030117	membrane coat	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	C		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	F		Seeded From UniProt	complete
involved_in	GO:0016185	synaptic vesicle budding from presynaptic endocytic zone membrane	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	P		Seeded From UniProt	complete
part_of	GO:0001917	photoreceptor inner segment	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P39053 ensembl:ENSMUSP00000088618	C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05193 ensembl:ENSP00000362014	F		Seeded From UniProt	complete
involved_in	GO:0007032	endosome organization	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05193 ensembl:ENSP00000362014	P		Seeded From UniProt	complete
involved_in	GO:0006898	receptor-mediated endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05193 ensembl:ENSP00000362014	P		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05193 ensembl:ENSP00000362014	P		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05193 ensembl:ENSP00000362014	C		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:Q05193 ensembl:ENSP00000362014	C		Seeded From UniProt	complete
enables	GO:0003924	GTPase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR001401 InterPro:IPR003130 InterPro:IPR027741	F		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000375 InterPro:IPR001401 InterPro:IPR003130 InterPro:IPR030381	F		Seeded From UniProt	complete
involved_in	GO:0072583	clathrin-dependent endocytosis	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR027741	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:12011079^[14]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-RNO-182041	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005874	microtubule	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0493	C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
involved_in	GO:0006897	endocytosis	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0254	P		Seeded From UniProt	complete
part_of	GO:0005794	Golgi apparatus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0333 UniProtKB-SubCell:SL-0132	C		Seeded From UniProt	complete
enables	GO:0005525	GTP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0342	F		Seeded From UniProt	complete
enables	GO:0016787	hydrolase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0378	F		Seeded From UniProt	complete
edit table

Notes

References

See Help:References for how to manage references in GONUTS.

↑ Lin, JW et al. (2000) Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization. Nat. Neurosci. 3 1282-90 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Takei, K et al. (1995) Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature 374 186-90 PubMed GONUTS page
↑ Cao, Y et al. (2010) Changed clathrin regulatory proteins in the brains of Alzheimer's disease patients and animal models. J. Alzheimers Dis. 22 329-42 PubMed GONUTS page
↑ ^4.0 ^4.1 Lu, J et al. (2007) Postsynaptic positioning of endocytic zones and AMPA receptor cycling by physical coupling of dynamin-3 to Homer. Neuron 55 874-89 PubMed GONUTS page
↑ Anggono, V & Robinson, PJ (2007) Syndapin I and endophilin I bind overlapping proline-rich regions of dynamin I: role in synaptic vesicle endocytosis. J. Neurochem. 102 931-43 PubMed GONUTS page
↑ ^6.0 ^6.1 Anggono, V et al. (2006) Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis. Nat. Neurosci. 9 752-60 PubMed GONUTS page
↑ Hyndman, KA et al. (2011) Dynamin activates NO production in rat renal inner medullary collecting ducts via protein-protein interaction with NOS1. Am. J. Physiol. Renal Physiol. 301 F118-24 PubMed GONUTS page
↑ ^8.0 ^8.1 Wigge, P et al. (1997) Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis. Mol. Biol. Cell 8 2003-15 PubMed GONUTS page
↑ Suginta, W et al. (2001) Chloride intracellular channel protein CLIC4 (p64H1) binds directly to brain dynamin I in a complex containing actin, tubulin and 14-3-3 isoforms. Biochem. J. 359 55-64 PubMed GONUTS page
↑ ^10.0 ^10.1 Krendel, M et al. (2007) Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett. 581 644-50 PubMed GONUTS page
↑ ^11.0 ^11.1 Gray, NW et al. (2003) Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer. Curr. Biol. 13 510-5 PubMed GONUTS page
↑ ^12.0 ^12.1 Kabbani, N et al. (2004) Dynamin-2 associates with the dopamine receptor signalplex and regulates internalization of activated D2 receptors. Cell. Signal. 16 497-503 PubMed GONUTS page
↑ Ringstad, N et al. (1997) The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proc. Natl. Acad. Sci. U.S.A. 94 8569-74 PubMed GONUTS page
↑ ^14.0 ^14.1 Ahn, S et al. (2002) Src-dependent tyrosine phosphorylation regulates dynamin self-assembly and ligand-induced endocytosis of the epidermal growth factor receptor. J. Biol. Chem. 277 26642-51 PubMed GONUTS page
↑ ^15.0 ^15.1 ^15.2 Cao, H et al. (1998) Differential distribution of dynamin isoforms in mammalian cells. Mol. Biol. Cell 9 2595-609 PubMed GONUTS page
↑ ^16.00 ^16.01 ^16.02 ^16.03 ^16.04 ^16.05 ^16.06 ^16.07 ^16.08 ^16.09 ^16.10 ^16.11 ^16.12 ^16.13 ^16.14 ^16.15 ^16.16 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ Ford, MG et al. (2011) The crystal structure of dynamin. Nature 477 561-6 PubMed GONUTS page
↑ Wang, G et al. (2006) Nitric oxide regulates endocytosis by S-nitrosylation of dynamin. Proc. Natl. Acad. Sci. U.S.A. 103 1295-300 PubMed GONUTS page

[PMID:11100149-1] Lin, JW et al. (2000) Distinct molecular mechanisms and divergent endocytotic pathways of AMPA receptor internalization. Nat. Neurosci. 3 1282-90 PubMed GONUTS page

[PMID:7877693-2] 2.0 ^2.1 ^2.2 Takei, K et al. (1995) Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature 374 186-90 PubMed GONUTS page

[PMID:20847448-3] Cao, Y et al. (2010) Changed clathrin regulatory proteins in the brains of Alzheimer's disease patients and animal models. J. Alzheimers Dis. 22 329-42 PubMed GONUTS page

[PMID:17880892-4] 4.0 ^4.1 Lu, J et al. (2007) Postsynaptic positioning of endocytic zones and AMPA receptor cycling by physical coupling of dynamin-3 to Homer. Neuron 55 874-89 PubMed GONUTS page

[PMID:17437541-5] Anggono, V & Robinson, PJ (2007) Syndapin I and endophilin I bind overlapping proline-rich regions of dynamin I: role in synaptic vesicle endocytosis. J. Neurochem. 102 931-43 PubMed GONUTS page

[PMID:16648848-6] 6.0 ^6.1 Anggono, V et al. (2006) Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis. Nat. Neurosci. 9 752-60 PubMed GONUTS page

[PMID:21490139-7] Hyndman, KA et al. (2011) Dynamin activates NO production in rat renal inner medullary collecting ducts via protein-protein interaction with NOS1. Am. J. Physiol. Renal Physiol. 301 F118-24 PubMed GONUTS page

[PMID:9348539-8] 8.0 ^8.1 Wigge, P et al. (1997) Amphiphysin heterodimers: potential role in clathrin-mediated endocytosis. Mol. Biol. Cell 8 2003-15 PubMed GONUTS page

[PMID:11563969-9] Suginta, W et al. (2001) Chloride intracellular channel protein CLIC4 (p64H1) binds directly to brain dynamin I in a complex containing actin, tubulin and 14-3-3 isoforms. Biochem. J. 359 55-64 PubMed GONUTS page

[PMID:17257598-10] 10.0 ^10.1 Krendel, M et al. (2007) Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis. FEBS Lett. 581 644-50 PubMed GONUTS page

[PMID:12646135-11] 11.0 ^11.1 Gray, NW et al. (2003) Dynamin 3 is a component of the postsynapse, where it interacts with mGluR5 and Homer. Curr. Biol. 13 510-5 PubMed GONUTS page

[PMID:14709338-12] 12.0 ^12.1 Kabbani, N et al. (2004) Dynamin-2 associates with the dopamine receptor signalplex and regulates internalization of activated D2 receptors. Cell. Signal. 16 497-503 PubMed GONUTS page

[PMID:9238017-13] Ringstad, N et al. (1997) The SH3p4/Sh3p8/SH3p13 protein family: binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain. Proc. Natl. Acad. Sci. U.S.A. 94 8569-74 PubMed GONUTS page

[PMID:12011079-14] 14.0 ^14.1 Ahn, S et al. (2002) Src-dependent tyrosine phosphorylation regulates dynamin self-assembly and ligand-induced endocytosis of the epidermal growth factor receptor. J. Biol. Chem. 277 26642-51 PubMed GONUTS page

[PMID:9725914-15] 15.0 ^15.1 ^15.2 Cao, H et al. (1998) Differential distribution of dynamin isoforms in mammalian cells. Mol. Biol. Cell 9 2595-609 PubMed GONUTS page

[PMID:21873635-16] 16.00 ^16.01 ^16.02 ^16.03 ^16.04 ^16.05 ^16.06 ^16.07 ^16.08 ^16.09 ^16.10 ^16.11 ^16.12 ^16.13 ^16.14 ^16.15 ^16.16 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:21927001-17] Ford, MG et al. (2011) The crystal structure of dynamin. Nature 477 561-6 PubMed GONUTS page

[PMID:16432212-18] Wang, G et al. (2006) Nitric oxide regulates endocytosis by S-nitrosylation of dynamin. Proc. Natl. Acad. Sci. U.S.A. 103 1295-300 PubMed GONUTS page

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RAT:DYN1

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