P50570 (DYN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynamin-2
EC=3.6.5.5

Gene names

Name:	DNM2
Synonyms:	DYN2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	870 AA.
Sequence status	Complete.
Protein existence	Evidence 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 MYO1E (via SH3 domain). Ref.5 Ref.7 Ref.8 Ref.9 Ref.10
Subcellular location	Cytoplasm. Cytoplasm › cytoskeleton. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density. Cell junction › synapse. 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.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28 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.17 Ref.23 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 regeneration 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.20 Ref.22
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 process	Endocytosis
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Microtubule Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Charcot-Marie-Tooth disease Disease mutation Neuropathy
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase Motor protein
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	G2/M transition of mitotic cell cycle Non-traceable author statement Ref.1. Source: UniProtKB antigen processing and presentation of exogenous peptide antigen via MHC class II Traceable author statement. Source: Reactome cellular membrane organization Traceable author statement. Source: Reactome positive regulation of apoptotic process Non-traceable author statement PubMed 10893263. Source: UniProtKB positive regulation of transcription, DNA-dependent 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 signal transduction Non-traceable author statement PubMed 10893263. Source: UniProtKB synaptic vesicle transport Non-traceable author statement Ref.5. Source: UniProtKB transferrin transport Inferred from mutant phenotype PubMed 14985334. Source: BHF-UCL
Cellular_component	Golgi membrane Traceable author statement. Source: Reactome cell junction Inferred from electronic annotation. Source: UniProtKB-KW cytosol Traceable author statement. Source: Reactome microtubule Inferred from direct assay PubMed 21525035. Source: UniProtKB midbody Inferred from electronic annotation. Source: UniProtKB-SubCell plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW postsynaptic density Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from direct assay Ref.5. Source: UniProtKB
Molecular_function	GTP 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 phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
AHI1	Q8N157	2	EBI-346547,EBI-1049056
GRB2	P62993	3	EBI-346547,EBI-401755

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 870

870

Dynamin-2

PRO_0000206570

Regions

Domain

519 – 625

107

PH

Domain

653 – 744

92

GED

Nucleotide binding

38 – 45

8

GTP By similarity

Nucleotide binding

136 – 140

5

GTP By similarity

Nucleotide binding

205 – 208

4

GTP By similarity

Compositional bias

747 – 866

120

Pro-rich

Amino acid modifications

Modified residue

298

1

Phosphoserine By similarity

Modified residue

302

1

Phosphoserine By similarity

Modified residue

597

1

Phosphotyrosine By similarity

Modified residue

598

1

N6-acetyllysine Ref.13

Modified residue

764

1

Phosphoserine; by CDK1 By similarity

Natural variations

Alternative sequence

407 – 444

38

LAFEA…RQCTS → MAFEAIVKKQIVKLKEPSLK CVDLVVSELATVIKKCAE in isoform 3.

VSP_044280

Alternative sequence

516 – 519

4

Missing in isoform 2 and isoform 3.

VSP_001325

Natural variant

263

1

P → L.
Corresponds to variant rs3745674 [ dbSNP | Ensembl ].

VAR_031961

Natural variant

358

1

G → R in CMT2M. Ref.22

VAR_068425

Natural variant

368

1

E → K in CNM1. Ref.18 Ref.27

VAR_031962

Natural variant

368

1

E → Q in CNM1. Ref.21

VAR_068365

Natural variant

369

1

R → Q in CNM1. Ref.18

VAR_031963

Natural variant

369

1

R → W in CNM1; reduced association with the centrosome. Ref.18

VAR_031964

Natural variant

465

1

R → W in CNM1; reduced association with the centrosome; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. Ref.18 Ref.23 Ref.27

VAR_031965

Natural variant

522

1

R → C in CNM1. Ref.28

VAR_068366

Natural variant

522

1

R → H in CNM1. Ref.27

VAR_068367

Natural variant

523

1

R → G in CNM1. Ref.28

VAR_068368

Natural variant

537

1

G → C in CMT2M. Ref.20

VAR_062574

Natural variant

555 – 557

3

Missing in CMTDIB; may affect binding to vesicles and membranes in favor of binding to microtubules; may affect receptor-mediated endocytosis.

VAR_031966

Natural variant

560

1

E → K in CNM1. Ref.24

VAR_068369

Natural variant

562

1

K → E in CMTDIB; with neutropenia; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. Ref.17 Ref.23

VAR_031967

Natural variant

570

1

L → H in CMT2M. Ref.20

VAR_062575

Natural variant

618

1

A → D in CNM1. Ref.26

VAR_068370

Natural variant

618

1

A → T in CNM1; severe. Ref.19 Ref.27

VAR_039041

Natural variant

619

1

S → L in CNM1; severe. Ref.19 Ref.27

VAR_039042

Natural variant

619

1

S → W in CNM1; severe. Ref.19

VAR_039043

Natural variant

621

1

L → P in CNM1; centronuclear myopathy with cataracts. Ref.25

VAR_068371

Natural variant

625

1

Missing in CNM1; severe; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. Ref.19 Ref.23

VAR_039044

Natural variant

627

1

P → H in CNM1. Ref.27

VAR_068372

Natural variant

627

1

P → R in CNM1. Ref.28

VAR_068373

Natural variant

650

1

E → K in CNM1; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. Ref.23

VAR_062576

Experimental info

Sequence conflict

155 – 156

2

QI → RV in AAA88025. Ref.1

Sequence conflict

316

1

N → I in AAA88025. Ref.1

Sequence conflict

324

1

R → P in AAA88025. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

870

Helix Strand Turn

Details...

Beta strand

522 – 530

9

Beta strand

533 – 535

3

Beta strand

540 – 545

6

Beta strand

550 – 555

6

Beta strand

560 – 565

6

Beta strand

567 – 573

7

Beta strand

585 – 590

6

Beta strand

596 – 599

4

Beta strand

601 – 606

6

Helix

610 – 623

14

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2004. Version 2. Checksum: 2F4567B75980935D	FASTA	870	98,064
	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
	Isoform 2 [UniParc]. Checksum: C76BA1762A012127	FASTA	866	97,652
	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 AIPNQVIRRG WLTINNISLM KGGSKEYWFV 550 560 570 580 590 600 LTAESLSWYK DEEEKEKKYM LPLDNLKIRD VEKGFMSNKH VFAIFNTEQR NVYKDLRQIE 610 620 630 640 650 660 LACDSQEDVD SWKASFLRAG VYPEKDQAEN EDGAQENTFS MDPQLERQVE TIRNLVDSYV 670 680 690 700 710 720 AIINKSIRDL MPKTIMHLMI NNTKAFIHHE LLAYLYSSAD QSSLMEESAD QAQRRDDMLR 730 740 750 760 770 780 MYHALKEALN IIGDISTSTV STPVPPPVDD TWLQSASSHS PTPQRRPVSS IHPPGRPPAV 790 800 810 820 830 840 RGPTPGPPLI PVPVGAAASF SAPPIPSRPG PQSVFANSDL FPAPPQIPSR PVRIPPGIPP 850 860 GVPSRRPPAA PSRPTIIRPA EPSLLD
	Isoform 3 [UniParc]. Checksum: 566396D3E6159245	FASTA	866	97,554
	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 GLFTPDMAFE AIVKKQIVKL 430 440 450 460 470 480 KEPSLKCVDL VVSELATVIK KCAEKLSSYP RLREETERIV TTYIREREGR TKDQILLLID 490 500 510 520 530 540 IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQVIRRG WLTINNISLM KGGSKEYWFV 550 560 570 580 590 600 LTAESLSWYK DEEEKEKKYM LPLDNLKIRD VEKGFMSNKH VFAIFNTEQR NVYKDLRQIE 610 620 630 640 650 660 LACDSQEDVD SWKASFLRAG VYPEKDQAEN EDGAQENTFS MDPQLERQVE TIRNLVDSYV 670 680 690 700 710 720 AIINKSIRDL MPKTIMHLMI NNTKAFIHHE LLAYLYSSAD QSSLMEESAD QAQRRDDMLR 730 740 750 760 770 780 MYHALKEALN IIGDISTSTV STPVPPPVDD TWLQSASSHS PTPQRRPVSS IHPPGRPPAV 790 800 810 820 830 840 RGPTPGPPLI PVPVGAAASF SAPPIPSRPG PQSVFANSDL FPAPPQIPSR PVRIPPGIPP 850 860 GVPSRRPPAA PSRPTIIRPA EPSLLD

References

	« Hide 'large scale' referencesShow '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. , 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] (ISOFORM 3). Tissue: 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. , 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 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.
[12]	"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.
[13]	"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, MASS SPECTROMETRY.
[14]	"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.
[15]	"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].
[16]	"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.
[17]	"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 AND GLU-562, CHARACTERIZATION OF VARIANT CMTDIB 555-ASP--GLU-557 DEL.
[18]	"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.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
[26]	"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.
[27]	"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. , 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.
[28]	"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. , 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.
+	Additional computationally mapped references.

Web resources

GeneReviews

The UMD-DNM2-isoform 1 mutations database

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L36983 mRNA. Translation: AAA88025.1.
AK289831 mRNA. Translation: BAF82520.1.
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.

IPI

IPI00033022.
IPI00218889.

PIR

JC4305.

RefSeq

NP_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.

UniGene

Hs.211463.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2YS1	NMR	-	A	520-625	[»]

ProteinModelPortal

P50570.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-31244N.

IntAct

P50570. 24 interactions.

MINT

MINT-5004324.

STRING

9606.ENSP00000352721.

PTM databases

PhosphoSite

P50570.

Polymorphism databases

DMDM

47117856.

Proteomic databases

PaxDb

P50570.

PRIDE

P50570.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000355667; ENSP00000347890; ENSG00000079805.
ENST00000359692; ENSP00000352721; ENSG00000079805.
ENST00000408974; ENSP00000386192; ENSG00000079805.

GeneID

1785.

KEGG

hsa:1785.

UCSC

uc002mpt.2. human.
uc002mpu.2. human.

Organism-specific databases

CTD

1785.

GeneCards

GC19P010824.

HGNC

HGNC:2974. DNM2.

HPA

HPA054246.

MIM

160150. phenotype.
602378. gene.
606482. phenotype.

neXtProt

NX_P50570.

Orphanet

169189. Autosomal dominant centronuclear myopathy.
228179. Autosomal dominant Charcot-Marie-Tooth disease type 2M.
100044. Autosomal dominant intermediate Charcot-Marie-Tooth disease type B.

PharmGKB

PA27442.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0699.

HOGENOM

HOG000161069.

HOVERGEN

HBG107833.

KO

K01528.

OMA

ERIITTH.

Enzyme and pathway databases

Pathway_Interaction_DB

arf6_traffickingpathway. Arf6 trafficking events.
pdgfrbpathway. PDGFR-beta signaling pathway.
syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P50570.

Bgee

P50570.

CleanEx

HS_DNM2.

Genevestigator

P50570.

GermOnline

ENSG00000079805. Homo sapiens.

Family and domain databases

Gene3D

2.30.29.30. 1 hit.

InterPro

IPR027188. DNM2.
IPR022812. Dynamin.
IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

PANTHER

PTHR11566. PTHR11566. 1 hit.
PTHR11566:SF23. PTHR11566:SF23. 1 hit.

Pfam

PF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]

PRINTS

PR00195. DYNAMIN.

SMART

SM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]

PROSITE

PS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P50570.

ChEMBL

CHEMBL5812.

ChiTaRS

DNM2. human.

EvolutionaryTrace

P50570.

GenomeRNAi

1785.

NextBio

7257.

SOURCE

Search...

Entry information

Entry name

DYN2_HUMAN

Accession

Primary (citable) accession number: P50570
Secondary accession number(s): A8K1B6 , E7EV30, Q5I0Y0, Q7Z5S3, Q9UPH4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	May 10, 2004
Last modified:	May 1, 2013
This is version 138 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.