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P50570

- DYN2_HUMAN

UniProt

P50570 - DYN2_HUMAN

Protein

Dynamin-2

Gene

DNM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (10 May 2004)
      Previous versions | rss
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    Functioni

    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.1 Publication

    Catalytic activityi

    GTP + H2O = GDP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 458GTPBy similarity
    Nucleotide bindingi136 – 1405GTPBy similarity
    Nucleotide bindingi205 – 2084GTPBy similarity

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. GTPase activity Source: UniProtKB
    3. GTP binding Source: UniProtKB
    4. microtubule binding Source: UniProtKB
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
    2. cell death Source: UniProtKB-KW
    3. endocytosis Source: UniProtKB
    4. G2/M transition of mitotic cell cycle Source: UniProtKB
    5. GTP catabolic process Source: GOC
    6. membrane organization Source: Reactome
    7. nitric oxide metabolic process Source: Reactome
    8. positive regulation of apoptotic process Source: UniProtKB
    9. positive regulation of transcription, DNA-templated Source: UniProtKB
    10. post-Golgi vesicle-mediated transport Source: Reactome
    11. receptor internalization Source: BHF-UCL
    12. regulation of nitric-oxide synthase activity Source: Reactome
    13. regulation of transcription, DNA-templated Source: UniProtKB
    14. signal transduction Source: UniProtKB
    15. small molecule metabolic process Source: Reactome
    16. synaptic vesicle transport Source: UniProtKB
    17. transferrin transport Source: BHF-UCL

    Keywords - Molecular functioni

    Hydrolase, Motor protein

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    GTP-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_11035. Gap junction degradation.
    REACT_11049. Formation of annular gap junctions.
    REACT_121399. MHC class II antigen presentation.
    REACT_12435. Retrograde neurotrophin signalling.
    REACT_12541. NOSTRIN mediated eNOS trafficking.
    REACT_19287. Lysosome Vesicle Biogenesis.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_22365. Recycling pathway of L1.
    REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
    SignaLinkiP50570.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Dynamin-2 (EC:3.6.5.5)
    Gene namesi
    Name:DNM2
    Synonyms:DYN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:2974. DNM2.

    Subcellular locationi

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

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytoplasm Source: HPA
    3. cytosol Source: Reactome
    4. endocytic vesicle membrane Source: Reactome
    5. extracellular vesicular exosome Source: UniProt
    6. Golgi apparatus Source: HPA
    7. Golgi membrane Source: Reactome
    8. microtubule Source: UniProtKB
    9. midbody Source: UniProtKB-SubCell
    10. plasma membrane Source: Reactome
    11. postsynaptic density Source: UniProtKB-SubCell
    12. postsynaptic membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cytoplasm, Cytoskeleton, Membrane, Microtubule, Postsynaptic cell membrane, Synapse

    Pathology & Biotechi

    Involvement in diseasei

    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.9 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti368 – 3681E → K in CNM1. 2 Publications
    VAR_031962
    Natural varianti368 – 3681E → Q in CNM1. 1 Publication
    VAR_068365
    Natural varianti369 – 3691R → Q in CNM1. 1 Publication
    VAR_031963
    Natural varianti369 – 3691R → W in CNM1; reduced association with the centrosome. 1 Publication
    VAR_031964
    Natural varianti465 – 4651R → W in CNM1; reduced association with the centrosome; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. 2 Publications
    VAR_031965
    Natural varianti522 – 5221R → C in CNM1. 1 Publication
    VAR_068366
    Natural varianti522 – 5221R → H in CNM1. 1 Publication
    VAR_068367
    Natural varianti523 – 5231R → G in CNM1. 1 Publication
    VAR_068368
    Natural varianti560 – 5601E → K in CNM1. 1 Publication
    VAR_068369
    Natural varianti618 – 6181A → D in CNM1. 1 Publication
    VAR_068370
    Natural varianti618 – 6181A → T in CNM1; severe. 2 Publications
    VAR_039041
    Natural varianti619 – 6191S → L in CNM1; severe. 2 Publications
    VAR_039042
    Natural varianti619 – 6191S → W in CNM1; severe. 1 Publication
    VAR_039043
    Natural varianti621 – 6211L → P in CNM1; centronuclear myopathy with cataracts. 1 Publication
    VAR_068371
    Natural varianti625 – 6251Missing in CNM1; severe; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. 1 Publication
    VAR_039044
    Natural varianti627 – 6271P → H in CNM1. 1 Publication
    VAR_068372
    Natural varianti627 – 6271P → R in CNM1. 1 Publication
    VAR_068373
    Natural varianti650 – 6501E → K in CNM1; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. 1 Publication
    VAR_062576
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti379 – 3791F → V in LCCS5; hypomorphic mutation impacting on endocytosis. 1 Publication
    VAR_070163
    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti555 – 5573Missing in CMTDIB; may affect binding to vesicles and membranes in favor of binding to microtubules; may affect receptor-mediated endocytosis.
    VAR_031966
    Natural varianti562 – 5621K → E in CMTDIB; with neutropenia; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. 1 Publication
    VAR_031967
    Natural varianti562 – 5621Missing in CMTDIB. 1 Publication
    VAR_070164
    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.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti358 – 3581G → R in CMT2M. 1 Publication
    VAR_068425
    Natural varianti537 – 5371G → C in CMT2M. 1 Publication
    VAR_062574
    Natural varianti570 – 5701L → H in CMT2M. 1 Publication
    VAR_062575

    Keywords - Diseasei

    Charcot-Marie-Tooth disease, Disease mutation, Neurodegeneration, Neuropathy

    Organism-specific databases

    MIMi160150. phenotype.
    606482. phenotype.
    615368. phenotype.
    Orphaneti169189. 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.
    PharmGKBiPA27442.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 870870Dynamin-2PRO_0000206570Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei299 – 2991N6-acetyllysineBy similarity
    Modified residuei598 – 5981N6-acetyllysine1 Publication
    Modified residuei764 – 7641Phosphoserine; by CDK1By similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP50570.
    PaxDbiP50570.
    PRIDEiP50570.

    PTM databases

    PhosphoSiteiP50570.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed.

    Gene expression databases

    ArrayExpressiP50570.
    BgeeiP50570.
    CleanExiHS_DNM2.
    GenevestigatoriP50570.

    Organism-specific databases

    HPAiHPA054246.

    Interactioni

    Subunit structurei

    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.By similarity7 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AHI1Q8N1572EBI-346547,EBI-1049056
    CTTNQ142475EBI-346547,EBI-351886
    GRB2P629934EBI-346547,EBI-401755
    ITSN1Q158112EBI-346547,EBI-602041
    MYO1EQ129652EBI-346547,EBI-4279548
    PACSIN2Q9UNF04EBI-346547,EBI-742503
    SH3BP4Q9P0V33EBI-346547,EBI-1049513
    SH3GL2Q999622EBI-346547,EBI-77938
    SH3KBP1Q96B975EBI-346547,EBI-346595
    SNX9Q9Y5X12EBI-346547,EBI-77848

    Protein-protein interaction databases

    BioGridi108122. 62 interactions.
    DIPiDIP-31244N.
    IntActiP50570. 57 interactions.
    MINTiMINT-5004324.
    STRINGi9606.ENSP00000352721.

    Structurei

    Secondary structure

    1
    870
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi522 – 5309
    Beta strandi533 – 5353
    Beta strandi540 – 5456
    Beta strandi550 – 5556
    Beta strandi560 – 5656
    Beta strandi567 – 5737
    Beta strandi585 – 5906
    Beta strandi596 – 5994
    Beta strandi601 – 6066
    Helixi610 – 62314

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2YS1NMR-A520-625[»]
    ProteinModelPortaliP50570.
    SMRiP50570. Positions 6-740.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50570.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 294267Dynamin-type GAdd
    BLAST
    Domaini519 – 625107PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini653 – 74492GEDPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi747 – 866120Pro-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 GED domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0699.
    HOGENOMiHOG000161069.
    HOVERGENiHBG107833.
    KOiK01528.
    OrthoDBiEOG76MK7N.
    PhylomeDBiP50570.
    TreeFamiTF300362.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    3.40.50.300. 1 hit.
    InterProiIPR027188. 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.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PANTHERiPTHR11566. PTHR11566. 1 hit.
    PTHR11566:SF23. PTHR11566:SF23. 1 hit.
    PfamiPF01031. Dynamin_M. 1 hit.
    PF00350. Dynamin_N. 1 hit.
    PF02212. GED. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view]
    PRINTSiPR00195. DYNAMIN.
    SMARTiSM00053. DYNc. 1 hit.
    SM00302. GED. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00410. G_DYNAMIN_1. 1 hit.
    PS51718. G_DYNAMIN_2. 1 hit.
    PS51388. GED. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P50570-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN    50
    FVGRDFLPRG SGIVTRRPLI LQLIFSKTEH AEFLHCKSKK FTDFDEVRQE 100
    IEAETDRVTG TNKGISPVPI NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP 150
    DIEYQIKDMI LQFISRESSL ILAVTPANMD LANSDALKLA KEVDPQGLRT 200
    IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK DIEGKKDIRA 250
    ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPALRSKL 300
    QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ 350
    VDTLELSGGA RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT 400
    GLFTPDLAFE AIVKKQVVKL KEPCLKCVDL VIQELINTVR QCTSKLSSYP 450
    RLREETERIV TTYIREREGR TKDQILLLID IEQSYINTNH EDFIGFANAQ 500
    QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE YWFVLTAESL 550
    SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL 600
    RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE 650
    RQVETIRNLV DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY 700
    SSADQSSLME ESADQAQRRD DMLRMYHALK EALNIIGDIS TSTVSTPVPP 750
    PVDDTWLQSA SSHSPTPQRR PVSSIHPPGR PPAVRGPTPG PPLIPVPVGA 800
    AASFSAPPIP SRPGPQSVFA NSDLFPAPPQ IPSRPVRIPP GIPPGVPSRR 850
    PPAAPSRPTI IRPAEPSLLD 870
    Length:870
    Mass (Da):98,064
    Last modified:May 10, 2004 - v2
    Checksum:i2F4567B75980935D
    GO
    Isoform 2 (identifier: P50570-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         516-519: Missing.

    Show »
    Length:866
    Mass (Da):97,652
    Checksum:iC76BA1762A012127
    GO
    Isoform 3 (identifier: P50570-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:866
    Mass (Da):97,554
    Checksum:i566396D3E6159245
    GO
    Isoform 4 (identifier: P50570-4) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:870
    Mass (Da):97,966
    Checksum:i9018503EA888A4F8
    GO
    Isoform 5 (identifier: P50570-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         848-848: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:869
    Mass (Da):97,977
    Checksum:iC33CD394EC8F1A6E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti155 – 1562QI → RV in AAA88025. (PubMed:7590285)Curated
    Sequence conflicti207 – 2071L → P in AK312260. (PubMed:14702039)Curated
    Sequence conflicti316 – 3161N → I in AAA88025. (PubMed:7590285)Curated
    Sequence conflicti324 – 3241R → P in AAA88025. (PubMed:7590285)Curated
    Sequence conflicti475 – 4751I → T in AK312260. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti263 – 2631P → L.
    Corresponds to variant rs3745674 [ dbSNP | Ensembl ].
    VAR_031961
    Natural varianti358 – 3581G → R in CMT2M. 1 Publication
    VAR_068425
    Natural varianti368 – 3681E → K in CNM1. 2 Publications
    VAR_031962
    Natural varianti368 – 3681E → Q in CNM1. 1 Publication
    VAR_068365
    Natural varianti369 – 3691R → Q in CNM1. 1 Publication
    VAR_031963
    Natural varianti369 – 3691R → W in CNM1; reduced association with the centrosome. 1 Publication
    VAR_031964
    Natural varianti379 – 3791F → V in LCCS5; hypomorphic mutation impacting on endocytosis. 1 Publication
    VAR_070163
    Natural varianti465 – 4651R → W in CNM1; reduced association with the centrosome; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. 2 Publications
    VAR_031965
    Natural varianti522 – 5221R → C in CNM1. 1 Publication
    VAR_068366
    Natural varianti522 – 5221R → H in CNM1. 1 Publication
    VAR_068367
    Natural varianti523 – 5231R → G in CNM1. 1 Publication
    VAR_068368
    Natural varianti537 – 5371G → C in CMT2M. 1 Publication
    VAR_062574
    Natural varianti555 – 5573Missing in CMTDIB; may affect binding to vesicles and membranes in favor of binding to microtubules; may affect receptor-mediated endocytosis.
    VAR_031966
    Natural varianti560 – 5601E → K in CNM1. 1 Publication
    VAR_068369
    Natural varianti562 – 5621K → E in CMTDIB; with neutropenia; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. 1 Publication
    VAR_031967
    Natural varianti562 – 5621Missing in CMTDIB. 1 Publication
    VAR_070164
    Natural varianti570 – 5701L → H in CMT2M. 1 Publication
    VAR_062575
    Natural varianti618 – 6181A → D in CNM1. 1 Publication
    VAR_068370
    Natural varianti618 – 6181A → T in CNM1; severe. 2 Publications
    VAR_039041
    Natural varianti619 – 6191S → L in CNM1; severe. 2 Publications
    VAR_039042
    Natural varianti619 – 6191S → W in CNM1; severe. 1 Publication
    VAR_039043
    Natural varianti621 – 6211L → P in CNM1; centronuclear myopathy with cataracts. 1 Publication
    VAR_068371
    Natural varianti625 – 6251Missing in CNM1; severe; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. 1 Publication
    VAR_039044
    Natural varianti627 – 6271P → H in CNM1. 1 Publication
    VAR_068372
    Natural varianti627 – 6271P → R in CNM1. 1 Publication
    VAR_068373
    Natural varianti650 – 6501E → K in CNM1; COS7 cells show a reduced uptake of transferrin and low-density lipoprotein complex. 1 Publication
    VAR_062576

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei407 – 44438LAFEA…RQCTS → MAFEAIVKKQIVKLKEPSLK CVDLVVSELATVIKKCAE in isoform 3 and isoform 4. 1 PublicationVSP_044280Add
    BLAST
    Alternative sequencei516 – 5194Missing in isoform 2 and isoform 3. 3 PublicationsVSP_001325
    Alternative sequencei848 – 8481Missing in isoform 5. 1 PublicationVSP_047534

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS32907.1. [P50570-2]
    CCDS32908.1. [P50570-3]
    CCDS45968.1. [P50570-1]
    CCDS45969.1. [P50570-4]
    CCDS59351.1. [P50570-5]
    PIRiJC4305.
    RefSeqiNP_001005360.1. NM_001005360.2. [P50570-1]
    NP_001005361.1. NM_001005361.2. [P50570-4]
    NP_001005362.1. NM_001005362.2. [P50570-3]
    NP_001177645.1. NM_001190716.1. [P50570-5]
    NP_004936.2. NM_004945.3. [P50570-2]
    UniGeneiHs.211463.

    Genome annotation databases

    GeneIDi1785.
    KEGGihsa:1785.
    UCSCiuc002mpt.2. human. [P50570-1]
    uc002mpu.2. human. [P50570-2]
    uc002mpv.2. human. [P50570-3]

    Polymorphism databases

    DMDMi47117856.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    The UMD-DNM2-isoform 1 mutations database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS32907.1. [P50570-2 ]
    CCDS32908.1. [P50570-3 ]
    CCDS45968.1. [P50570-1 ]
    CCDS45969.1. [P50570-4 ]
    CCDS59351.1. [P50570-5 ]
    PIRi JC4305.
    RefSeqi NP_001005360.1. NM_001005360.2. [P50570-1 ]
    NP_001005361.1. NM_001005361.2. [P50570-4 ]
    NP_001005362.1. NM_001005362.2. [P50570-3 ]
    NP_001177645.1. NM_001190716.1. [P50570-5 ]
    NP_004936.2. NM_004945.3. [P50570-2 ]
    UniGenei Hs.211463.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2YS1 NMR - A 520-625 [» ]
    ProteinModelPortali P50570.
    SMRi P50570. Positions 6-740.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108122. 62 interactions.
    DIPi DIP-31244N.
    IntActi P50570. 57 interactions.
    MINTi MINT-5004324.
    STRINGi 9606.ENSP00000352721.

    Chemistry

    BindingDBi P50570.
    ChEMBLi CHEMBL5812.

    PTM databases

    PhosphoSitei P50570.

    Polymorphism databases

    DMDMi 47117856.

    Proteomic databases

    MaxQBi P50570.
    PaxDbi P50570.
    PRIDEi P50570.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 1785.
    KEGGi hsa:1785.
    UCSCi uc002mpt.2. human. [P50570-1 ]
    uc002mpu.2. human. [P50570-2 ]
    uc002mpv.2. human. [P50570-3 ]

    Organism-specific databases

    CTDi 1785.
    GeneCardsi GC19P010824.
    GeneReviewsi DNM2.
    HGNCi HGNC:2974. DNM2.
    HPAi HPA054246.
    MIMi 160150. phenotype.
    602378. gene.
    606482. phenotype.
    615368. phenotype.
    neXtProti NX_P50570.
    Orphaneti 169189. 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.
    PharmGKBi PA27442.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0699.
    HOGENOMi HOG000161069.
    HOVERGENi HBG107833.
    KOi K01528.
    OrthoDBi EOG76MK7N.
    PhylomeDBi P50570.
    TreeFami TF300362.

    Enzyme and pathway databases

    Reactomei REACT_11035. Gap junction degradation.
    REACT_11049. Formation of annular gap junctions.
    REACT_121399. MHC class II antigen presentation.
    REACT_12435. Retrograde neurotrophin signalling.
    REACT_12541. NOSTRIN mediated eNOS trafficking.
    REACT_19287. Lysosome Vesicle Biogenesis.
    REACT_19400. Golgi Associated Vesicle Biogenesis.
    REACT_22365. Recycling pathway of L1.
    REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.
    SignaLinki P50570.

    Miscellaneous databases

    ChiTaRSi DNM2. human.
    EvolutionaryTracei P50570.
    GeneWikii DNM2.
    GenomeRNAii 1785.
    NextBioi 7257.
    PROi P50570.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50570.
    Bgeei P50570.
    CleanExi HS_DNM2.
    Genevestigatori P50570.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    3.40.50.300. 1 hit.
    InterProi IPR027188. 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.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    PANTHERi PTHR11566. PTHR11566. 1 hit.
    PTHR11566:SF23. PTHR11566:SF23. 1 hit.
    Pfami PF01031. Dynamin_M. 1 hit.
    PF00350. Dynamin_N. 1 hit.
    PF02212. GED. 1 hit.
    PF00169. PH. 1 hit.
    [Graphical view ]
    PRINTSi PR00195. DYNAMIN.
    SMARTi SM00053. DYNc. 1 hit.
    SM00302. GED. 1 hit.
    SM00233. PH. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00410. G_DYNAMIN_1. 1 hit.
    PS51718. G_DYNAMIN_2. 1 hit.
    PS51388. GED. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] (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.
      , 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. 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. 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. 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. Cited for: VARIANTS CNM1 LYS-368; TRP-369; GLN-369 AND TRP-465, CHARACTERIZATION OF VARIANTS CNM1 TRP-369 AND TRP-465.
    21. 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. 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.
      , 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. Cited for: VARIANT LCCS5 VAL-379.

    Entry informationi

    Entry nameiDYN2_HUMAN
    AccessioniPrimary (citable) accession number: P50570
    Secondary accession number(s): A8K1B6
    , E7EV30, E9PEQ4, K7ESI9, Q5I0Y0, Q7Z5S3, Q9UPH4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 10, 2004
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    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.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3