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Q05193

- DYN1_HUMAN

UniProt

Q05193 - DYN1_HUMAN

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Protein

Dynamin-1

Gene

DNM1

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. Involved in receptor-mediated endocytosis.

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. GTPase activity Source: ProtInc
  2. GTP binding Source: UniProtKB-KW
  3. identical protein binding Source: IntAct
  4. poly(A) RNA binding Source: UniProtKB
  5. protein kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

  1. endocytosis Source: BHF-UCL
  2. endosome organization Source: BHF-UCL
  3. GTP catabolic process Source: GOC
  4. receptor internalization Source: Ensembl
  5. receptor-mediated endocytosis Source: UniProtKB
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_22365. Recycling pathway of L1.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.

Names & Taxonomyi

Protein namesi
Recommended name:
Dynamin-1 (EC:3.6.5.5)
Gene namesi
Name:DNM1
Synonyms:DNM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:2972. DNM1.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeleton 1 Publication
Note: Microtubule-associated.

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. membrane coat Source: Ensembl
  3. microtubule Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441K → A: Inhibits receptor-mediated endocytosis. 1 Publication

Organism-specific databases

PharmGKBiPA27440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 864864Dynamin-1PRO_0000206563Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei80 – 801PhosphotyrosineBy similarity
Modified residuei125 – 1251Nitrated tyrosine; alternateBy similarity
Modified residuei125 – 1251Phosphotyrosine; alternateBy similarity
Modified residuei347 – 3471PhosphoserineBy similarity
Modified residuei354 – 3541PhosphotyrosineBy similarity
Modified residuei512 – 5121PhosphoserineBy similarity
Modified residuei774 – 7741PhosphoserineBy similarity
Modified residuei778 – 7781PhosphoserineBy similarity
Modified residuei822 – 8221PhosphoserineBy similarity
Modified residuei851 – 8511PhosphoserineBy similarity
Modified residuei857 – 8571PhosphoserineBy similarity

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiQ05193.
PaxDbiQ05193.
PRIDEiQ05193.

PTM databases

PhosphoSiteiQ05193.

Expressioni

Gene expression databases

BgeeiQ05193.
CleanExiHS_DNM1.
ExpressionAtlasiQ05193. baseline and differential.
GenevestigatoriQ05193.

Organism-specific databases

HPAiCAB005920.
HPA049910.

Interactioni

Subunit structurei

Interacts with CAV1 and SH3GLB1. Binds SH3GL1, SH3GL2 and SH3GL3 (By similarity). Interacts with PHOCN. Interacts with PACSIN1, PACSIN2 and PACSIN3 (By similarity). Interacts with SNX9. Interacts with MYO1E (via SH3 domain). Interacts with SNX33 (via SH3 domain). Interacts with UNC119; leading to a decrease of DNM1 GTPase activity (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-713135,EBI-713135
ACTA1P681355EBI-8446026,EBI-367540From a different organism.
FNBP1Q96RU35EBI-713135,EBI-1111248
GRB2P629933EBI-713135,EBI-401755
HTTP428583EBI-713135,EBI-466029
LRRK2Q5S0074EBI-713135,EBI-5323863
NCK1P163332EBI-713135,EBI-389883
NOSTRINQ8IVI93EBI-713135,EBI-1391643

Protein-protein interaction databases

BioGridi108099. 59 interactions.
DIPiDIP-36242N.
IntActiQ05193. 25 interactions.
MINTiMINT-233135.
STRINGi9606.ENSP00000362014.

Structurei

Secondary structure

1
864
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi10 – 2112Combined sources
Turni22 – 243Combined sources
Helixi26 – 283Combined sources
Beta strandi33 – 375Combined sources
Helixi44 – 496Combined sources
Turni50 – 523Combined sources
Beta strandi61 – 633Combined sources
Beta strandi69 – 757Combined sources
Beta strandi80 – 834Combined sources
Helixi84 – 863Combined sources
Helixi94 – 10916Combined sources
Turni110 – 1134Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi131 – 1366Combined sources
Helixi152 – 16413Combined sources
Beta strandi169 – 1768Combined sources
Helixi181 – 1833Combined sources
Helixi185 – 1939Combined sources
Beta strandi200 – 2056Combined sources
Helixi207 – 2093Combined sources
Helixi217 – 2204Combined sources
Beta strandi231 – 2333Combined sources
Helixi239 – 2435Combined sources
Helixi248 – 26114Combined sources
Turni263 – 2653Combined sources
Helixi266 – 2716Combined sources
Helixi274 – 31744Combined sources
Beta strandi520 – 52910Combined sources
Helixi533 – 5353Combined sources
Beta strandi537 – 55519Combined sources
Beta strandi561 – 5666Combined sources
Beta strandi570 – 5745Combined sources
Beta strandi579 – 5824Combined sources
Beta strandi584 – 5907Combined sources
Beta strandi601 – 6099Combined sources
Helixi610 – 62213Combined sources
Helixi726 – 74116Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYNX-ray2.20A/B510-633[»]
2DYNX-ray2.30A/B509-630[»]
2X2EX-ray2.00A/D6-320[»]
A/D726-750[»]
2X2FX-ray2.00A/D6-320[»]
A/D726-750[»]
3SNHX-ray3.70A6-746[»]
3ZYCX-ray2.20A/D6-320[»]
A/D726-750[»]
3ZYSelectron microscopy12.20A/D6-320[»]
A/D726-750[»]
C/F518-630[»]
4UUDelectron microscopy12.50A/B/C/D/E/F/G/H/I/J/K/L1-864[»]
4UUKelectron microscopy12.50A/B/C/D/E/F/G/H/I/J/K/L1-864[»]
ProteinModelPortaliQ05193.
SMRiQ05193. Positions 6-746.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05193.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 294267Dynamin-type GAdd
BLAST
Domaini519 – 625107PHPROSITE-ProRule annotationAdd
BLAST
Domaini659 – 75092GEDPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0699.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161069.
HOVERGENiHBG107833.
InParanoidiQ05193.
KOiK01528.
OMAiQYPHLRE.
OrthoDBiEOG76MK7N.
PhylomeDBiQ05193.
TreeFamiTF300362.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
3.40.50.300. 1 hit.
InterProiIPR027741. DNM1.
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:SF32. PTHR11566:SF32. 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: Q05193-1) [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
MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN
60 70 80 90 100
FVGRDFLPRG SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE
110 120 130 140 150
IEAETDRVTG TNKGISPVPI NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP
160 170 180 190 200
DIEFQIRDML MQFVTKENCL ILAVSPANSD LANSDALKVA KEVDPQGQRT
210 220 230 240 250
IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK DIDGKKDITA
260 270 280 290 300
ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL
310 320 330 340 350
QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ
360 370 380 390 400
IDTYELSGGA RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT
410 420 430 440 450
GLFTPDMAFE TIVKKQVKKI REPCLKCVDM VISELISTVR QCTKKLQQYP
460 470 480 490 500
RLREEMERIV TTHIREREGR TKEQVMLLID IELAYMNTNH EDFIGFANAQ
510 520 530 540 550
QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE YWFVLTAENL
560 570 580 590 600
SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY
610 620 630 640 650
RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS
660 670 680 690 700
MDPQLERQVE TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE
710 720 730 740 750
LLANLYSCGD QNTLMEESAE QAQRRDEMLR MYHALKEALS IIGDINTTTV
760 770 780 790 800
STPMPPPVDD SWLQVQSVPA GRRSPTSSPT PQRRAPAVPP ARPGSRGPAP
810 820 830 840 850
GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP PGVPSRSGQA
860
SPSRPESPRP PFDL
Length:864
Mass (Da):97,408
Last modified:March 18, 2008 - v2
Checksum:i7FCD8CB572FFEAEF
GO
Isoform 2 (identifier: Q05193-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-444: MAFETIVKKQ...LISTVRQCTK → LAFEATVKKQ...LTATIRKCSE

Show »
Length:864
Mass (Da):97,263
Checksum:iDC9E3D5259D891DF
GO
Isoform 3 (identifier: Q05193-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     845-864: SRSGQASPSRPESPRPPFDL → RITISDP

Show »
Length:851
Mass (Da):96,041
Checksum:i89040FCDDAC2870C
GO
Isoform 4 (identifier: Q05193-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     846-864: RSGQASPSRPESPRPPFDL → QPIGSGKSIPS

Show »
Length:856
Mass (Da):96,397
Checksum:i7FF33D80ED860B02
GO
Isoform 5 (identifier: Q05193-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     407-444: MAFETIVKKQ...LISTVRQCTK → LAFEATVKKQ...LTATIRKCSE
     845-864: SRSGQASPSRPESPRPPFDL → RITISDP

Show »
Length:851
Mass (Da):95,895
Checksum:i4230B9970D097B20
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881K → E in AAH50279. (PubMed:15489334)Curated
Sequence conflicti287 – 2871N → D in AAH50279. (PubMed:15489334)Curated
Sequence conflicti809 – 8091L → M in AAH50279. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti744 – 7441D → N.1 Publication
Corresponds to variant rs1042007 [ dbSNP | Ensembl ].
VAR_048904

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei407 – 44438MAFET…RQCTK → LAFEATVKKQVQKLKEPSIK CVDMVVSELTATIRKCSE in isoform 2 and isoform 5. 1 PublicationVSP_031518Add
BLAST
Alternative sequencei845 – 86420SRSGQ…PPFDL → RITISDP in isoform 3 and isoform 5. 2 PublicationsVSP_031519Add
BLAST
Alternative sequencei846 – 86419RSGQA…PPFDL → QPIGSGKSIPS in isoform 4. 1 PublicationVSP_031520Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07807 mRNA. Translation: AAA02803.1.
L07808 mRNA. Translation: AAA02804.1.
L07809 mRNA. Translation: AAA02805.1.
L07810 mRNA. Translation: AAA02806.1.
AL590708 Genomic DNA. Translation: CAI13837.1.
AL590708 Genomic DNA. Translation: CAI13839.2.
BC050279 mRNA. Translation: AAH50279.2.
BC063850 mRNA. Translation: AAH63850.1.
CCDSiCCDS43882.1. [Q05193-3]
CCDS6895.1. [Q05193-1]
CCDS75911.1. [Q05193-5]
CCDS75912.1. [Q05193-2]
PIRiA40671.
RefSeqiNP_001005336.1. NM_001005336.2. [Q05193-3]
NP_001275666.1. NM_001288737.1. [Q05193-5]
NP_001275667.1. NM_001288738.1. [Q05193-5]
NP_001275668.1. NM_001288739.1. [Q05193-2]
NP_004399.2. NM_004408.3. [Q05193-1]
XP_005251825.1. XM_005251768.1. [Q05193-5]
XP_005251826.1. XM_005251769.1. [Q05193-3]
UniGeneiHs.522413.

Genome annotation databases

EnsembliENST00000341179; ENSP00000345680; ENSG00000106976. [Q05193-3]
ENST00000372923; ENSP00000362014; ENSG00000106976. [Q05193-1]
ENST00000393594; ENSP00000377219; ENSG00000106976. [Q05193-5]
ENST00000475805; ENSP00000419225; ENSG00000106976. [Q05193-5]
ENST00000486160; ENSP00000420045; ENSG00000106976. [Q05193-2]
GeneIDi1759.
KEGGihsa:1759.
UCSCiuc022bnx.1. human. [Q05193-5]
uc022bny.1. human. [Q05193-3]
uc022boa.1. human. [Q05193-1]

Polymorphism databases

DMDMi172046078.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L07807 mRNA. Translation: AAA02803.1 .
L07808 mRNA. Translation: AAA02804.1 .
L07809 mRNA. Translation: AAA02805.1 .
L07810 mRNA. Translation: AAA02806.1 .
AL590708 Genomic DNA. Translation: CAI13837.1 .
AL590708 Genomic DNA. Translation: CAI13839.2 .
BC050279 mRNA. Translation: AAH50279.2 .
BC063850 mRNA. Translation: AAH63850.1 .
CCDSi CCDS43882.1. [Q05193-3 ]
CCDS6895.1. [Q05193-1 ]
CCDS75911.1. [Q05193-5 ]
CCDS75912.1. [Q05193-2 ]
PIRi A40671.
RefSeqi NP_001005336.1. NM_001005336.2. [Q05193-3 ]
NP_001275666.1. NM_001288737.1. [Q05193-5 ]
NP_001275667.1. NM_001288738.1. [Q05193-5 ]
NP_001275668.1. NM_001288739.1. [Q05193-2 ]
NP_004399.2. NM_004408.3. [Q05193-1 ]
XP_005251825.1. XM_005251768.1. [Q05193-5 ]
XP_005251826.1. XM_005251769.1. [Q05193-3 ]
UniGenei Hs.522413.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1DYN X-ray 2.20 A/B 510-633 [» ]
2DYN X-ray 2.30 A/B 509-630 [» ]
2X2E X-ray 2.00 A/D 6-320 [» ]
A/D 726-750 [» ]
2X2F X-ray 2.00 A/D 6-320 [» ]
A/D 726-750 [» ]
3SNH X-ray 3.70 A 6-746 [» ]
3ZYC X-ray 2.20 A/D 6-320 [» ]
A/D 726-750 [» ]
3ZYS electron microscopy 12.20 A/D 6-320 [» ]
A/D 726-750 [» ]
C/F 518-630 [» ]
4UUD electron microscopy 12.50 A/B/C/D/E/F/G/H/I/J/K/L 1-864 [» ]
4UUK electron microscopy 12.50 A/B/C/D/E/F/G/H/I/J/K/L 1-864 [» ]
ProteinModelPortali Q05193.
SMRi Q05193. Positions 6-746.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108099. 59 interactions.
DIPi DIP-36242N.
IntActi Q05193. 25 interactions.
MINTi MINT-233135.
STRINGi 9606.ENSP00000362014.

Chemistry

BindingDBi Q05193.
ChEMBLi CHEMBL4958.

PTM databases

PhosphoSitei Q05193.

Polymorphism databases

DMDMi 172046078.

Proteomic databases

MaxQBi Q05193.
PaxDbi Q05193.
PRIDEi Q05193.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341179 ; ENSP00000345680 ; ENSG00000106976 . [Q05193-3 ]
ENST00000372923 ; ENSP00000362014 ; ENSG00000106976 . [Q05193-1 ]
ENST00000393594 ; ENSP00000377219 ; ENSG00000106976 . [Q05193-5 ]
ENST00000475805 ; ENSP00000419225 ; ENSG00000106976 . [Q05193-5 ]
ENST00000486160 ; ENSP00000420045 ; ENSG00000106976 . [Q05193-2 ]
GeneIDi 1759.
KEGGi hsa:1759.
UCSCi uc022bnx.1. human. [Q05193-5 ]
uc022bny.1. human. [Q05193-3 ]
uc022boa.1. human. [Q05193-1 ]

Organism-specific databases

CTDi 1759.
GeneCardsi GC09P130965.
H-InvDB HIX0026786.
HIX0211497.
HGNCi HGNC:2972. DNM1.
HPAi CAB005920.
HPA049910.
MIMi 602377. gene.
neXtProti NX_Q05193.
PharmGKBi PA27440.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0699.
GeneTreei ENSGT00760000119213.
HOGENOMi HOG000161069.
HOVERGENi HBG107833.
InParanoidi Q05193.
KOi K01528.
OMAi QYPHLRE.
OrthoDBi EOG76MK7N.
PhylomeDBi Q05193.
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_22365. Recycling pathway of L1.
REACT_228189. EPH-ephrin mediated repulsion of cells.
REACT_6894. Toll Like Receptor 4 (TLR4) Cascade.

Miscellaneous databases

EvolutionaryTracei Q05193.
GeneWikii DNM1.
GenomeRNAii 1759.
NextBioi 7163.
PROi Q05193.
SOURCEi Search...

Gene expression databases

Bgeei Q05193.
CleanExi HS_DNM1.
ExpressionAtlasi Q05193. baseline and differential.
Genevestigatori Q05193.

Family and domain databases

Gene3Di 2.30.29.30. 1 hit.
3.40.50.300. 1 hit.
InterProi IPR027741. DNM1.
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:SF32. PTHR11566:SF32. 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. "Mutations in human dynamin block an intermediate stage in coated vesicle formation."
    van der Bliek A.M., Redelmeier T.E., Tisdale E.J., Meyerowitz E.M., Schmid S.L.
    J. Cell Biol. 122:553-563(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 387-466 (ISOFORM 2), NUCLEOTIDE SEQUENCE [MRNA] OF 726-856 (ISOFORMS 3 AND 4), MUTAGENESIS OF LYS-44, VARIANT ASN-744.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 3).
    Tissue: Brain and PNS.
  4. "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.
  5. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  6. "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.
  7. "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.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Three-dimensional solution structure of the pleckstrin homology domain from dynamin."
    Downing A.K., Driscoll P.C., Gout I., Salim K., Zvelebil M.J., Waterfield M.D.
    Curr. Biol. 4:884-891(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 511-630.
  11. "Crystal structure at 2.2-A resolution of the pleckstrin homology domain from human dynamin."
    Ferguson K.M., Lemmon M.A., Schlessinger J., Sigler P.B.
    Cell 79:199-209(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 509-633.
  12. "Crystal structure of the pleckstrin homology domain from dynamin."
    Timm D., Salim K., Gout I., Guruprasad L., Waterfield M., Blundell T.
    Nat. Struct. Biol. 1:782-788(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 509-630.

Entry informationi

Entry nameiDYN1_HUMAN
AccessioniPrimary (citable) accession number: Q05193
Secondary accession number(s): A6NLM6
, Q5SYX0, Q5SYX2, Q6P3T6, Q86VD2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 18, 2008
Last modified: November 26, 2014
This is version 144 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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