DNM2


DNM2
Dynamin 2
Identifiers
Symbols DNM2; CMT2M; CMTDI1; CMTDIB; DI-CMTB; DYN2; DYNII
External IDs OMIM602378 MGI109547 HomoloGene90883 GeneCards: DNM2 Gene
EC number 3.6.5.5
Orthologs
Species Human Mouse
Entrez 1785 13430
Ensembl ENSG00000079805 ENSMUSG00000033335
UniProt P50570 Q3T9X3
RefSeq (mRNA) NM_001005360.2 NM_001039520.1
RefSeq (protein) NP_001005360.1 NP_001034609.1
Location (UCSC) Chr 19:
10.82 – 10.94 Mb
Chr 9:
21.23 – 21.31 Mb
PubMed search [1] [2]

Dynamin-2 is a protein that in humans is encoded by the DNM2 gene.[1][2]

Dynamins represent one of the subfamilies of GTP-binding proteins. These proteins share considerable sequence similarity over the N-terminal portion of the molecule, which contains the GTPase domain. Dynamins are associated with microtubules. They have been implicated in cell processes such as endocytosis and cell motility, and in alterations of the membrane that accompany certain activities such as bone resorption by osteoclasts. Dynamins bind many proteins that bind actin and other cytoskeletal proteins. Dynamins can also self-assemble, a process that stimulates GTPase activity. Four alternatively spliced transcripts encoding different proteins have been described. Additional alternatively spliced transcripts may exist, but their full-length nature has not been determined.[3]

Contents

Interactions

DNM2 has been shown to interact with SNX9,[4] SHANK1[5] and SHANK2.[5]

External Links

References

  1. ^ Diatloff-Zito C, Gordon AJ, Duchaud E, Merlin G (Nov 1995). "Isolation of an ubiquitously expressed cDNA encoding human dynamin II, a member of the large GTP-binding protein family". Gene 163 (2): 301–6. doi:10.1016/0378-1119(95)00275-B. PMID 7590285. 
  2. ^ Klocke R, Augustin A, Ronsiek M, Stief A, van der Putten H, Jockusch H (Jul 1997). "Dynamin genes Dnm1 and Dnm2 are located on proximal mouse chromosomes 2 and 9, respectively". Genomics 41 (2): 290–2. doi:10.1006/geno.1997.4634. PMID 9143510. 
  3. ^ "Entrez Gene: DNM2 dynamin 2". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1785. 
  4. ^ Lundmark, Richard; Carlsson Sven R (Nov. 2003). "Sorting nexin 9 participates in clathrin-mediated endocytosis through interactions with the core components". J. Biol. Chem. (United States) 278 (47): 46772–81. doi:10.1074/jbc.M307334200. ISSN 0021-9258. PMID 12952949. 
  5. ^ a b Okamoto, P M; Gamby C, Wells D, Fallon J, Vallee R B (Dec. 2001). "Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton". J. Biol. Chem. (United States) 276 (51): 48458–65. doi:10.1074/jbc.M104927200. ISSN 0021-9258. PMC 2715172. PMID 11583995. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2715172. 

Further reading

SYT1 · SYT2 · SYT3 · SYT4 · SYT5 · SYT6 · SYT7 · SYT8 · SYT9 · SYT10 · SYT11 · SYT12 · SYT13 · SYT14 · SYT15 · SYT16 · SYT17
Other
COPI COPII

Vesicle formation: SEC23A

Small GTPase: SAR1A
RME/Clathrin
CLTA · CLTB · CLTC
Caveolae
Caveolin (CAV1 · CAV2 · CAV3)
Other/ungrouped see also vesicular transport protein disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr

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