Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P50570 (DYN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. 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·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynamin-2

EC=3.6.5.5
Gene names
Name:DNM2
Synonyms:DYN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length870 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis. Ref.6

Catalytic activity

GTP + H2O = GDP + phosphate.

Subunit structure

Interacts with MYOF By similarity. Interacts with SHANK1, SHANK2, SH3BP4 and NOSTRIN. Interacts with SNX9. Interacts with SNX33 (via SH3 domain). Interacts with MYO1E (via SH3 domain). Interacts with PSTPIP1. Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Cell junctionsynapsepostsynaptic cell membranepostsynaptic density. Cell junctionsynapse. Midbody. Note: Microtubule-associated. Also found in the postsynaptic density of neuronal cells. Ref.6 Ref.9

Tissue specificity

Ubiquitously expressed.

Post-translational modification

Phosphorylation at Ser-764 by CDK1 is greatly increased upon mitotic entry. It regulates cytokinesis downstream of calcineurin, and does not affect clathrin-mediated endocytosis. Dephosphorylated by Calcineurin/PP2 By similarity.

Involvement in disease

Myopathy, centronuclear, 1 (CNM1) [MIM:160150]: A congenital muscle disorder characterized by progressive muscular weakness and wasting involving mainly limb girdle, trunk, and neck muscles. It may also affect distal muscles. Weakness may be present during childhood or adolescence or may not become evident until the third decade of life. Ptosis is a frequent clinical feature. The most prominent histopathologic features include high frequency of centrally located nuclei in muscle fibers not secondary to regeneration, radial arrangement of sarcoplasmic strands around the central nuclei, and predominance and hypotrophy of type 1 fibers.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.20 Ref.21 Ref.23 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30

Lethal congenital contracture syndrome 5 (LCCS5) [MIM:615368]: A form of lethal congenital contracture syndrome, an autosomal recessive disorder characterized by degeneration of anterior horn neurons, extreme skeletal muscle atrophy and congenital non-progressive joint contractures. The contractures can involve the upper or lower limbs and/or the vertebral column, leading to various degrees of flexion or extension limitations evident at birth.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31

Charcot-Marie-Tooth disease, dominant, intermediate type, B (CMTDIB) [MIM:606482]: A form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. The dominant intermediate type B is characterized by clinical and pathologic features intermediate between demyelinating and axonal peripheral neuropathies, and motor median nerve conduction velocities ranging from 25 to 45 m/sec.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19 Ref.25

Charcot-Marie-Tooth disease 2M (CMT2M) [MIM:606482]: An axonal form of Charcot-Marie-Tooth disease, a disorder of the peripheral nervous system, characterized by progressive weakness and atrophy, initially of the peroneal muscles and later of the distal muscles of the arms. Charcot-Marie-Tooth disease is classified in two main groups on the basis of electrophysiologic properties and histopathology: primary peripheral demyelinating neuropathies (designated CMT1 when they are dominantly inherited) and primary peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group are characterized by signs of axonal degeneration in the absence of obvious myelin alterations, normal or slightly reduced nerve conduction velocities, and progressive distal muscle weakness and atrophy. Nerve conduction velocities are normal or slightly reduced.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.22 Ref.24

Miscellaneous

Overexpression of CNM- and CMT-related DNM2 mutants in COS7 cells, whatever the mutated domain, led to a reduction in clathrin-mediated receptor endocytosis associated with MAPK ERK-1 and ERK-2 impairment. The membrane trafficking impairment process may represent a common pathophysiological pathway in the autosomal forms of CNM DNM2-CMT neuropathy.

Sequence similarities

Belongs to the dynamin family.

Contains 1 GED domain.

Contains 1 PH domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCell junction
Cell membrane
Cytoplasm
Cytoskeleton
Membrane
Microtubule
Postsynaptic cell membrane
Synapse
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCharcot-Marie-Tooth disease
Disease mutation
Neurodegeneration
Neuropathy
   LigandGTP-binding
Nucleotide-binding
   Molecular functionHydrolase
Motor protein
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processG2/M transition of mitotic cell cycle

Non-traceable author statement Ref.1. Source: UniProtKB

GTP catabolic process

Non-traceable author statement Ref.5. Source: GOC

antigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

endocytosis

Non-traceable author statement PubMed 10101292Ref.5. Source: UniProtKB

membrane organization

Traceable author statement. Source: Reactome

nitric oxide metabolic process

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Non-traceable author statement PubMed 10893263. Source: UniProtKB

positive regulation of transcription, DNA-templated

Non-traceable author statement PubMed 10893263. Source: UniProtKB

post-Golgi vesicle-mediated transport

Traceable author statement. Source: Reactome

receptor internalization

Inferred from mutant phenotype PubMed 14985334. Source: BHF-UCL

regulation of nitric-oxide synthase activity

Traceable author statement. Source: Reactome

regulation of transcription, DNA-templated

Non-traceable author statement PubMed 10893263. Source: UniProtKB

signal transduction

Non-traceable author statement PubMed 10893263. Source: UniProtKB

small molecule metabolic process

Traceable author statement. Source: Reactome

synaptic vesicle transport

Non-traceable author statement Ref.5. Source: UniProtKB

transferrin transport

Inferred from mutant phenotype PubMed 14985334. Source: BHF-UCL

   Cellular_componentGolgi apparatus

Inferred from direct assay. Source: HPA

Golgi membrane

Traceable author statement. Source: Reactome

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

midbody

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Traceable author statement. Source: Reactome

postsynaptic density

Inferred from electronic annotation. Source: UniProtKB-SubCell

postsynaptic membrane

Inferred from direct assay Ref.5. Source: UniProtKB

   Molecular_functionGTP binding

Non-traceable author statement Ref.1. Source: UniProtKB

GTPase activity

Non-traceable author statement Ref.5. Source: UniProtKB

enzyme binding

Non-traceable author statement Ref.5. Source: UniProtKB

microtubule binding

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P50570-1)

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 2 (identifier: P50570-2)

The sequence of this isoform differs from the canonical sequence as follows:
     516-519: Missing.
Isoform 3 (identifier: P50570-3)

The sequence of this isoform differs from the canonical sequence as follows:
     407-444: LAFEAIVKKQ...LINTVRQCTS → MAFEAIVKKQ...LATVIKKCAE
     516-519: Missing.
Isoform 4 (identifier: P50570-4)

The sequence of this isoform differs from the canonical sequence as follows:
     407-444: LAFEAIVKKQ...LINTVRQCTS → MAFEAIVKKQ...LATVIKKCAE
Note: Gene prediction based on EST data.
Isoform 5 (identifier: P50570-5)

The sequence of this isoform differs from the canonical sequence as follows:
     848-848: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 870870Dynamin-2
PRO_0000206570

Regions

Domain519 – 625107PH
Domain653 – 74492GED
Nucleotide binding38 – 458GTP By similarity
Nucleotide binding136 – 1405GTP By similarity
Nucleotide binding205 – 2084GTP By similarity
Compositional bias747 – 866120Pro-rich

Amino acid modifications

Modified residue2991N6-acetyllysine By similarity
Modified residue5981N6-acetyllysine Ref.15
Modified residue7641Phosphoserine; by CDK1 By similarity

Natural variations

Alternative sequence407 – 44438LAFEA…RQCTS → MAFEAIVKKQIVKLKEPSLK CVDLVVSELATVIKKCAE in isoform 3 and isoform 4.
VSP_044280
Alternative sequence516 – 5194Missing in isoform 2 and isoform 3.
VSP_001325
Alternative sequence8481Missing in isoform 5.
VSP_047534
Natural variant2631P → L.
Corresponds to variant rs3745674 [ dbSNP | Ensembl ].
VAR_031961
Natural variant3581G → R in CMT2M. Ref.24
VAR_068425
Natural variant3681E → K in CNM1. Ref.20 Ref.29
VAR_031962
Natural variant3681E → Q in CNM1. Ref.23
VAR_068365
Natural variant3691R → Q in CNM1. Ref.20
VAR_031963
Natural variant3691R → W in CNM1; reduced association with the centrosome. Ref.20
VAR_031964
Natural variant3791F → V in LCCS5; hypomorphic mutation impacting on endocytosis. Ref.31
VAR_070163
Natural variant4651R → W in CNM1; reduced association with the centrosome; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. Ref.20 Ref.25 Ref.29
VAR_031965
Natural variant5221R → C in CNM1. Ref.30
VAR_068366
Natural variant5221R → H in CNM1. Ref.29
VAR_068367
Natural variant5231R → G in CNM1. Ref.30
VAR_068368
Natural variant5371G → C in CMT2M. Ref.22
VAR_062574
Natural variant555 – 5573Missing in CMTDIB; may affect binding to vesicles and membranes in favor of binding to microtubules; may affect receptor-mediated endocytosis.
VAR_031966
Natural variant5601E → K in CNM1. Ref.26
VAR_068369
Natural variant5621K → E in CMTDIB; with neutropenia; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. Ref.19 Ref.25
VAR_031967
Natural variant5621Missing in CMTDIB. Ref.19
VAR_070164
Natural variant5701L → H in CMT2M. Ref.22
VAR_062575
Natural variant6181A → D in CNM1. Ref.28
VAR_068370
Natural variant6181A → T in CNM1; severe. Ref.21 Ref.29
VAR_039041
Natural variant6191S → L in CNM1; severe. Ref.21 Ref.29
VAR_039042
Natural variant6191S → W in CNM1; severe. Ref.21
VAR_039043
Natural variant6211L → P in CNM1; centronuclear myopathy with cataracts. Ref.27
VAR_068371
Natural variant6251Missing in CNM1; severe; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. Ref.21 Ref.25
VAR_039044
Natural variant6271P → H in CNM1. Ref.29
VAR_068372
Natural variant6271P → R in CNM1. Ref.30
VAR_068373
Natural variant6501E → K in CNM1; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. Ref.25
VAR_062576

Experimental info

Sequence conflict155 – 1562QI → RV in AAA88025. Ref.1
Sequence conflict2071L → P in AK312260. Ref.2
Sequence conflict3161N → I in AAA88025. Ref.1
Sequence conflict3241R → P in AAA88025. Ref.1
Sequence conflict4751I → T in AK312260. Ref.2

Secondary structure

..................... 870
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 10, 2004. Version 2.
Checksum: 2F4567B75980935D

FASTA87098,064
        10         20         30         40         50         60 
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 

        70         80         90        100        110        120 
SGIVTRRPLI LQLIFSKTEH AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI 

       130        140        150        160        170        180 
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD 

       190        200        210        220        230        240 
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 

       250        260        270        280        290        300 
DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPALRSKL 

       310        320        330        340        350        360 
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA 

       370        380        390        400        410        420 
RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL 

       430        440        450        460        470        480 
KEPCLKCVDL VIQELINTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID 

       490        500        510        520        530        540 
IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE 

       550        560        570        580        590        600 
YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL 

       610        620        630        640        650        660 
RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV 

       670        680        690        700        710        720 
DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESADQAQRRD 

       730        740        750        760        770        780 
DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQSA SSHSPTPQRR PVSSIHPPGR 

       790        800        810        820        830        840 
PPAVRGPTPG PPLIPVPVGA AASFSAPPIP SRPGPQSVFA NSDLFPAPPQ IPSRPVRIPP 

       850        860        870 
GIPPGVPSRR PPAAPSRPTI IRPAEPSLLD 

« Hide

Isoform 2 [UniParc].

Checksum: C76BA1762A012127
Show »

FASTA86697,652
Isoform 3 [UniParc].

Checksum: 566396D3E6159245
Show »

FASTA86697,554
Isoform 4 [UniParc].

Checksum: 9018503EA888A4F8
Show »

FASTA87097,966
Isoform 5 [UniParc].

Checksum: C33CD394EC8F1A6E
Show »

FASTA86997,977

References

« Hide 'large scale' references
[1]"Isolation of an ubiquitously expressed cDNA encoding human dynamin II, a member of the large GTP-binding protein family."
Diatloff-Zito C., Gordon A.J.E., Duchaud E., Merlin G.
Gene 163:301-306(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"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 5).
Tissue: Astrocyte and Brain.
[3]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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] (ISOFORMS 1 AND 2).
Tissue: Ovary and Uterus.
[5]"Dynamin isoform-specific interaction with the shank/ProSAP scaffolding proteins of the postsynaptic density and actin cytoskeleton."
Okamoto P.M., Gamby C., Wells D., Fallon J., Vallee R.B.
J. Biol. Chem. 276:48458-48465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SHANK PROTEINS.
[6]"The large GTPase dynamin associates with the spindle midzone and is required for cytokinesis."
Thompson H.M., Skop A.R., Euteneuer U., Meyer B.J., McNiven M.A.
Curr. Biol. 12:2111-2117(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION.
[7]"TTP specifically regulates the internalization of the transferrin receptor."
Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P., Tacchetti C., Di Fiore P.P.
Cell 123:875-888(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH3BP4.
[8]"NOSTRIN functions as a homotrimeric adaptor protein facilitating internalization of eNOS."
Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W., Schilling K.
J. Cell Sci. 118:5059-5069(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOSTRIN.
[9]"SNX9 regulates dynamin assembly and is required for efficient clathrin-mediated endocytosis."
Soulet F., Yarar D., Leonard M., Schmid S.L.
Mol. Biol. Cell 16:2058-2067(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH SNX9.
[10]"Myosin 1E interacts with synaptojanin-1 and dynamin and is involved in endocytosis."
Krendel M., Osterweil E.K., Mooseker M.S.
FEBS Lett. 581:644-650(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYO1E.
[11]"A novel sorting nexin modulates endocytic trafficking and alpha-secretase cleavage of the amyloid precursor protein."
Schobel S., Neumann S., Hertweck M., Dislich B., Kuhn P.H., Kremmer E., Seed B., Baumeister R., Haass C., Lichtenthaler S.F.
J. Biol. Chem. 283:14257-14268(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SNX33.
[12]"The PCH family member proline-serine-threonine phosphatase-interacting protein 1 targets to the leukocyte uropod and regulates directed cell migration."
Cooper K.M., Bennin D.A., Huttenlocher A.
Mol. Biol. Cell 19:3180-3191(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PSTPIP1.
[13]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[15]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-598, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[17]"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].
[18]"Solution structure of the PH domain of dynamin-2 from human."
RIKEN structural genomics initiative (RSGI)
Submitted (APR-2008) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 514-625.
[19]"Mutations in the pleckstrin homology domain of dynamin 2 cause dominant intermediate Charcot-Marie-Tooth disease."
Zuechner S., Noureddine M., Kennerson M., Verhoeven K., Claeys K., De Jonghe P., Merory J., Oliveira S.A., Speer M.C., Stenger J.E., Walizada G., Zhu D., Pericak-Vance M.A., Nicholson G., Timmerman V., Vance J.M.
Nat. Genet. 37:289-294(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMTDIB 555-ASP--GLU-557 DEL; LYS-562 DEL AND GLU-562, CHARACTERIZATION OF VARIANT CMTDIB 555-ASP--GLU-557 DEL.
[20]"Mutations in dynamin 2 cause dominant centronuclear myopathy."
Bitoun M., Maugenre S., Jeannet P.-Y., Lacene E., Ferrer X., Laforet P., Martin J.-J., Laporte J., Lochmueller H., Beggs A.H., Fardeau M., Eymard B., Romero N.B., Guicheney P.
Nat. Genet. 37:1207-1209(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CNM1 LYS-368; TRP-369; GLN-369 AND TRP-465, CHARACTERIZATION OF VARIANTS CNM1 TRP-369 AND TRP-465.
[21]"Dynamin 2 mutations cause sporadic centronuclear myopathy with neonatal onset."
Bitoun M., Bevilacqua J.A., Prudhon B., Maugenre S., Taratuto A.L., Monges S., Lubieniecki F., Cances C., Uro-Coste E., Mayer M., Fardeau M., Romero N.B., Guicheney P.
Ann. Neurol. 62:666-670(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CNM1 THR-618; LEU-619; TRP-619 AND VAL-625 DEL.
[22]"Two novel mutations in dynamin-2 cause axonal Charcot-Marie-Tooth disease."
Fabrizi G.M., Ferrarini M., Cavallaro T., Cabrini I., Cerini R., Bertolasi L., Rizzuto N.
Neurology 69:291-295(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CMT2M CYS-537 AND HIS-570.
[23]"Subtle central and peripheral nervous system abnormalities in a family with centronuclear myopathy and a novel dynamin 2 gene mutation."
Echaniz-Laguna A., Nicot A.S., Carre S., Franques J., Tranchant C., Dondaine N., Biancalana V., Mandel J.L., Laporte J.
Neuromuscul. Disord. 17:955-959(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CNM1 GLN-368.
[24]"Magnetic resonance imaging findings of leg musculature in Charcot-Marie-Tooth disease type 2 due to dynamin 2 mutation."
Gallardo E., Claeys K.G., Nelis E., Garcia A., Canga A., Combarros O., Timmerman V., De Jonghe P., Berciano J.
J. Neurol. 255:986-992(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMT2M ARG-358.
[25]"Dynamin 2 mutations associated with human diseases impair clathrin-mediated receptor endocytosis."
Bitoun M., Durieux A.-C., Prudhon B., Bevilacqua J.A., Herledan A., Sakanyan V., Urtizberea A., Cartier L., Romero N.B., Guicheney P.
Hum. Mutat. 30:1419-1427(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CNM1 LYS-650, CHARACTERIZATION OF VARIANTS CNM1 TRP-465; VAL-625 DEL AND LYS-650, CHARACTERIZATION OF VARIANT CMTDIB GLU-562, PATHOPHYSIOLOGICAL PATHWAY IN THE AUTOSOMAL FORMS OF CNM AND DNM2-CMT NEUROPATHY.
[26]"A new centronuclear myopathy phenotype due to a novel dynamin 2 mutation."
Bitoun M., Bevilacqua J.A., Eymard B., Prudhon B., Fardeau M., Guicheney P., Romero N.B.
Neurology 72:93-95(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CNM1 LYS-560.
[27]"Centronuclear myopathy with cataracts due to a novel dynamin 2 (DNM2) mutation."
Jungbluth H., Cullup T., Lillis S., Zhou H., Abbs S., Sewry C., Muntoni F.
Neuromuscul. Disord. 20:49-52(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CNM1 PRO-621.
[28]"Adult course in dynamin 2 dominant centronuclear myopathy with neonatal onset."
Melberg A., Kretz C., Kalimo H., Wallgren-Pettersson C., Toussaint A., Bohm J., Stalberg E., Laporte J.
Neuromuscul. Disord. 20:53-56(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CNM1 ASP-618.
[29]"Expanding the clinical, pathological and MRI phenotype of DNM2-related centronuclear myopathy."
Susman R.D., Quijano-Roy S., Yang N., Webster R., Clarke N.F., Dowling J., Kennerson M., Nicholson G., Biancalana V., Ilkovski B., Flanigan K.M., Arbuckle S., Malladi C., Robinson P., Vucic S., Mayer M., Romero N.B., Urtizberea J.A. expand/collapse author list , Garcia-Bragado F., Guicheney P., Bitoun M., Carlier R.Y., North K.N.
Neuromuscul. Disord. 20:229-237(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CNM1 LYS-368; TRP-465; HIS-522; THR-618; LEU-619 AND HIS-627.
[30]"Mutation spectrum in the large GTPase dynamin 2, and genotype-phenotype correlation in autosomal dominant centronuclear myopathy."
Bohm J., Biancalana V., Dechene E.T., Bitoun M., Pierson C.R., Schaefer E., Karasoy H., Dempsey M.A., Klein F., Dondaine N., Kretz C., Haumesser N., Poirson C., Toussaint A., Greenleaf R.S., Barger M.A., Mahoney L.J., Kang P.B. expand/collapse author list , Zanoteli E., Vissing J., Witting N., Echaniz-Laguna A., Wallgren-Pettersson C., Dowling J., Merlini L., Oldfors A., Bomme Ousager L., Melki J., Krause A., Jern C., Oliveira A.S., Petit F., Jacquette A., Chaussenot A., Mowat D., Leheup B., Cristofano M., Poza Aldea J.J., Michel F., Furby A., Llona J.E., Van Coster R., Bertini E., Urtizberea J.A., Drouin-Garraud V., Beroud C., Prudhon B., Bedford M., Mathews K., Erby L.A., Smith S.A., Roggenbuck J., Crowe C.A., Brennan Spitale A., Johal S.C., Amato A.A., Demmer L.A., Jonas J., Darras B.T., Bird T.D., Laurino M., Welt S.I., Trotter C., Guicheney P., Das S., Mandel J.L., Beggs A.H., Laporte J.
Hum. Mutat. 33:949-959(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CNM1 CYS-522; GLY-523 AND ARG-627.
[31]"Dynamin 2 homozygous mutation in humans with a lethal congenital syndrome."
Koutsopoulos O.S., Kretz C., Weller C.M., Roux A., Mojzisova H., Boehm J., Koch C., Toussaint A., Heckel E., Stemkens D., Ter Horst S.A., Thibault C., Koch M., Mehdi S.Q., Bijlsma E.K., Mandel J.L., Vermot J., Laporte J.
Eur. J. Hum. Genet. 21:637-642(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LCCS5 VAL-379.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L36983 mRNA. Translation: AAA88025.1.
AK289831 mRNA. Translation: BAF82520.1.
AK312260 mRNA. No translation available.
AC007229 Genomic DNA. Translation: AAD23604.1.
AC011475 Genomic DNA. No translation available.
AC011552 Genomic DNA. No translation available.
AC011554 Genomic DNA. No translation available.
AC112707 Genomic DNA. No translation available.
BC039596 mRNA. Translation: AAH39596.1.
BC054501 mRNA. Translation: AAH54501.1.
PIRJC4305.
RefSeqNP_001005360.1. NM_001005360.2.
NP_001005361.1. NM_001005361.2.
NP_001005362.1. NM_001005362.2.
NP_001177645.1. NM_001190716.1.
NP_004936.2. NM_004945.3.
UniGeneHs.211463.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2YS1NMR-A520-625[»]
ProteinModelPortalP50570.
SMRP50570. Positions 5-737.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108122. 61 interactions.
DIPDIP-31244N.
IntActP50570. 57 interactions.
MINTMINT-5004324.
STRING9606.ENSP00000352721.

Chemistry

BindingDBP50570.
ChEMBLCHEMBL5812.

PTM databases

PhosphoSiteP50570.

Polymorphism databases

DMDM47117856.

Proteomic databases

PaxDbP50570.
PRIDEP50570.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355667; ENSP00000347890; ENSG00000079805. [P50570-1]
ENST00000359692; ENSP00000352721; ENSG00000079805. [P50570-2]
ENST00000389253; ENSP00000373905; ENSG00000079805. [P50570-4]
ENST00000408974; ENSP00000386192; ENSG00000079805. [P50570-3]
ENST00000585892; ENSP00000468734; ENSG00000079805. [P50570-5]
GeneID1785.
KEGGhsa:1785.
UCSCuc002mpt.2. human. [P50570-1]
uc002mpu.2. human. [P50570-2]
uc002mpv.2. human. [P50570-3]

Organism-specific databases

CTD1785.
GeneCardsGC19P010824.
HGNCHGNC:2974. DNM2.
HPAHPA054246.
MIM160150. phenotype.
602378. gene.
606482. phenotype.
615368. phenotype.
neXtProtNX_P50570.
Orphanet169189. Autosomal dominant centronuclear myopathy.
228179. Autosomal dominant Charcot-Marie-Tooth disease type 2M.
100044. Autosomal dominant intermediate Charcot-Marie-Tooth disease type B.
363409. Fetal akinesia-cerebral and retinal hemorrhage syndrome.
PharmGKBPA27442.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0699.
HOGENOMHOG000161069.
HOVERGENHBG107833.
KOK01528.
OMASKLGSYP.
OrthoDBEOG76MK7N.
PhylomeDBP50570.
TreeFamTF300362.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_6900. Immune System.
SignaLinkP50570.

Gene expression databases

ArrayExpressP50570.
BgeeP50570.
CleanExHS_DNM2.
GenevestigatorP50570.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.40.50.300. 1 hit.
InterProIPR027188. DNM2.
IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR022812. Dynamin_SF.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR027417. P-loop_NTPase.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PANTHERPTHR11566. PTHR11566. 1 hit.
PTHR11566:SF23. PTHR11566:SF23. 1 hit.
PfamPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00195. DYNAMIN.
SMARTSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNM2. human.
EvolutionaryTraceP50570.
GeneWikiDNM2.
GenomeRNAi1785.
NextBio7257.
PROP50570.
SOURCESearch...

Entry information

Entry nameDYN2_HUMAN
AccessionPrimary (citable) accession number: P50570
Secondary accession number(s): A8K1B6 expand/collapse secondary AC list , E7EV30, E9PEQ4, K7ESI9, Q5I0Y0, Q7Z5S3, Q9UPH4
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2004
Last modified: April 16, 2014
This is version 149 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 19

Human chromosome 19: entries, gene names and cross-references to MIM