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P50570

- DYN2_HUMAN

UniProt

P50570 - DYN2_HUMAN

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Protein

Dynamin-2

Gene

DNM2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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: Unplaced

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. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. endocytic vesicle membrane Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. focal adhesion Source: UniProtKB
  6. Golgi apparatus Source: HPA
  7. Golgi membrane Source: Reactome
  8. microtubule Source: UniProtKB
  9. plasma membrane Source: Reactome
  10. postsynaptic membrane Source: UniProtKB
Complete GO annotation...

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. 1 Publication
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

BgeeiP50570.
CleanExiHS_DNM2.
ExpressionAtlasiP50570. baseline and differential.
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. 67 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 – 5309Combined sources
Beta strandi533 – 5353Combined sources
Beta strandi540 – 5456Combined sources
Beta strandi550 – 5556Combined sources
Beta strandi560 – 5656Combined sources
Beta strandi567 – 5737Combined sources
Beta strandi585 – 5906Combined sources
Beta strandi596 – 5994Combined sources
Beta strandi601 – 6066Combined sources
Helixi610 – 62314Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2YS1NMR-A520-625[»]
ProteinModelPortaliP50570.
SMRiP50570. Positions 5-737.
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.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161069.
HOVERGENiHBG107833.
InParanoidiP50570.
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

        10         20         30         40         50
MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN
60 70 80 90 100
FVGRDFLPRG SGIVTRRPLI LQLIFSKTEH AEFLHCKSKK FTDFDEVRQE
110 120 130 140 150
IEAETDRVTG TNKGISPVPI NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP
160 170 180 190 200
DIEYQIKDMI LQFISRESSL ILAVTPANMD LANSDALKLA KEVDPQGLRT
210 220 230 240 250
IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK DIEGKKDIRA
260 270 280 290 300
ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPALRSKL
310 320 330 340 350
QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ
360 370 380 390 400
VDTLELSGGA RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT
410 420 430 440 450
GLFTPDLAFE AIVKKQVVKL KEPCLKCVDL VIQELINTVR QCTSKLSSYP
460 470 480 490 500
RLREETERIV TTYIREREGR TKDQILLLID IEQSYINTNH EDFIGFANAQ
510 520 530 540 550
QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE YWFVLTAESL
560 570 580 590 600
SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL
610 620 630 640 650
RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE
660 670 680 690 700
RQVETIRNLV DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY
710 720 730 740 750
SSADQSSLME ESADQAQRRD DMLRMYHALK EALNIIGDIS TSTVSTPVPP
760 770 780 790 800
PVDDTWLQSA SSHSPTPQRR PVSSIHPPGR PPAVRGPTPG PPLIPVPVGA
810 820 830 840 850
AASFSAPPIP SRPGPQSVFA NSDLFPAPPQ IPSRPVRIPP GIPPGVPSRR
860 870
PPAAPSRPTI IRPAEPSLLD
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. 1 Publication
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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000355667; ENSP00000347890; ENSG00000079805. [P50570-1]
ENST00000359692; ENSP00000352721; ENSG00000079805. [P50570-2]
ENST00000389253; ENSP00000373905; ENSG00000079805. [P50570-4]
ENST00000408974; ENSP00000386192; ENSG00000079805. [P50570-3]
ENST00000585892; ENSP00000468734; ENSG00000079805. [P50570-5]
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2YS1 NMR - A 520-625 [» ]
ProteinModelPortali P50570.
SMRi P50570. Positions 5-737.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108122. 67 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

Ensembli ENST00000355667 ; ENSP00000347890 ; ENSG00000079805 . [P50570-1 ]
ENST00000359692 ; ENSP00000352721 ; ENSG00000079805 . [P50570-2 ]
ENST00000389253 ; ENSP00000373905 ; ENSG00000079805 . [P50570-4 ]
ENST00000408974 ; ENSP00000386192 ; ENSG00000079805 . [P50570-3 ]
ENST00000585892 ; ENSP00000468734 ; ENSG00000079805 . [P50570-5 ]
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.
GeneTreei ENSGT00760000119213.
HOGENOMi HOG000161069.
HOVERGENi HBG107833.
InParanoidi P50570.
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

Bgeei P50570.
CleanExi HS_DNM2.
ExpressionAtlasi P50570. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 156 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

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