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Protein

Dynamin-1

Gene

DNM1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Nucleotide bindingi38 – 45GTPBy similarity8
Nucleotide bindingi136 – 140GTPBy similarity5
Nucleotide bindingi205 – 208GTPBy similarity4

GO - Molecular functioni

  • GTPase activity Source: ProtInc
  • GTP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • microtubule binding Source: GO_Central
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase binding Source: ParkinsonsUK-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Motor protein

Keywords - Biological processi

Endocytosis

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS02963-MONOMER.
BRENDAi3.6.5.5. 2681.
ReactomeiR-HSA-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-HSA-177504. Retrograde neurotrophin signalling.
R-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-437239. Recycling pathway of L1.
R-HSA-8856828. Clathrin-mediated endocytosis.
SIGNORiQ05193.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:2972. DNM1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Involvement in diseasei

Epileptic encephalopathy, early infantile, 31 (EIEE31)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of epileptic encephalopathy, a heterogeneous group of severe childhood onset epilepsies characterized by refractory seizures, neurodevelopmental impairment, and poor prognosis. Development is normal prior to seizure onset, after which cognitive and motor delays become apparent.
See also OMIM:616346
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073710177A → P in EIEE31. 1 PublicationCorresponds to variant rs587777860dbSNPEnsembl.1
Natural variantiVAR_073711206K → N in EIEE31. 1 PublicationCorresponds to variant rs587777861dbSNPEnsembl.1
Natural variantiVAR_073712237R → W in EIEE31. 1 PublicationCorresponds to variant rs760270633dbSNPEnsembl.1
Natural variantiVAR_073713359G → A in EIEE31. 1 PublicationCorresponds to variant rs587777862dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44K → A: Inhibits receptor-mediated endocytosis. 1 Publication1

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

DisGeNETi1759.
MIMi616346. phenotype.
OpenTargetsiENSG00000106976.
PharmGKBiPA27440.

Chemistry databases

ChEMBLiCHEMBL4958.

Polymorphism and mutation databases

DMDMi172046078.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002065631 – 864Dynamin-1Add BLAST864

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei80PhosphotyrosineBy similarity1
Modified residuei125Nitrated tyrosine; alternateBy similarity1
Modified residuei125Phosphotyrosine; alternateBy similarity1
Modified residuei306PhosphoserineBy similarity1
Modified residuei347PhosphoserineBy similarity1
Modified residuei354PhosphotyrosineBy similarity1
Modified residuei512PhosphoserineBy similarity1
Modified residuei774PhosphoserineBy similarity1
Modified residuei778PhosphoserineBy similarity1
Modified residuei796Omega-N-methylarginineBy similarity1
Modified residuei822PhosphoserineBy similarity1
Modified residuei851PhosphoserineBy similarity1
Modified residuei857PhosphoserineBy similarity1

Keywords - PTMi

Methylation, Nitration, Phosphoprotein

Proteomic databases

EPDiQ05193.
MaxQBiQ05193.
PaxDbiQ05193.
PeptideAtlasiQ05193.
PRIDEiQ05193.

PTM databases

iPTMnetiQ05193.
PhosphoSitePlusiQ05193.

Expressioni

Gene expression databases

BgeeiENSG00000106976.
CleanExiHS_DNM1.
ExpressionAtlasiQ05193. baseline and differential.
GenevisibleiQ05193. HS.

Organism-specific databases

HPAiCAB005920.
HPA049910.
HPA061801.

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). Interacts with DIAPH1 (PubMed:23325789).By similarity1 Publication

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
SNX33Q8WV412EBI-713135,EBI-2481535
SNX9Q9Y5X12EBI-713135,EBI-77848

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • microtubule binding Source: GO_Central
  • protein kinase binding Source: ParkinsonsUK-UCL

Protein-protein interaction databases

BioGridi108099. 65 interactors.
DIPiDIP-36242N.
IntActiQ05193. 27 interactors.
MINTiMINT-233135.
STRINGi9606.ENSP00000362014.

Chemistry databases

BindingDBiQ05193.

Structurei

Secondary structure

1864
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 21Combined sources13
Turni22 – 24Combined sources3
Helixi27 – 29Combined sources3
Beta strandi32 – 39Combined sources8
Helixi44 – 52Combined sources9
Beta strandi60 – 62Combined sources3
Beta strandi69 – 75Combined sources7
Beta strandi80 – 83Combined sources4
Helixi84 – 86Combined sources3
Helixi94 – 109Combined sources16
Turni110 – 113Combined sources4
Beta strandi120 – 126Combined sources7
Beta strandi131 – 136Combined sources6
Helixi152 – 164Combined sources13
Beta strandi169 – 176Combined sources8
Helixi181 – 183Combined sources3
Helixi185 – 193Combined sources9
Beta strandi198 – 205Combined sources8
Helixi207 – 209Combined sources3
Helixi217 – 220Combined sources4
Beta strandi231 – 233Combined sources3
Helixi239 – 243Combined sources5
Helixi248 – 261Combined sources14
Turni263 – 265Combined sources3
Helixi266 – 271Combined sources6
Helixi274 – 311Combined sources38
Helixi312 – 316Combined sources5
Beta strandi520 – 529Combined sources10
Helixi533 – 535Combined sources3
Beta strandi537 – 555Combined sources19
Beta strandi561 – 566Combined sources6
Beta strandi570 – 574Combined sources5
Beta strandi579 – 582Combined sources4
Beta strandi584 – 590Combined sources7
Beta strandi601 – 609Combined sources9
Helixi610 – 622Combined sources13
Helixi726 – 742Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5D3QX-ray1.70A/B5-320[»]
A/B726-746[»]
ProteinModelPortaliQ05193.
SMRiQ05193.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ05193.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini28 – 294Dynamin-type GAdd BLAST267
Domaini519 – 625PHPROSITE-ProRule annotationAdd BLAST107
Domaini659 – 750GEDPROSITE-ProRule annotationAdd BLAST92

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161069.
HOVERGENiHBG107833.
InParanoidiQ05193.
KOiK01528.
OrthoDBiEOG091G0EIQ.
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.
IPR030381. G_DYNAMIN_dom.
IPR003130. GED.
IPR020850. GED_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[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]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF52540. 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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

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: Q05193-5) [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

Sequence cautioni

The sequence AAA02805 differs from that shown. Probable cloning artifact.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti188K → E in AAH50279 (PubMed:15489334).Curated1
Sequence conflicti287N → D in AAH50279 (PubMed:15489334).Curated1
Sequence conflicti809L → M in AAH50279 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_073710177A → P in EIEE31. 1 PublicationCorresponds to variant rs587777860dbSNPEnsembl.1
Natural variantiVAR_073711206K → N in EIEE31. 1 PublicationCorresponds to variant rs587777861dbSNPEnsembl.1
Natural variantiVAR_073712237R → W in EIEE31. 1 PublicationCorresponds to variant rs760270633dbSNPEnsembl.1
Natural variantiVAR_073713359G → A in EIEE31. 1 PublicationCorresponds to variant rs587777862dbSNPEnsembl.1
Natural variantiVAR_048904744D → N.1 PublicationCorresponds to variant rs1042007dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_031518407 – 444MAFET…RQCTK → LAFEATVKKQVQKLKEPSIK CVDMVVSELTATIRKCSE in isoform 2 and isoform 4. 1 PublicationAdd BLAST38
Alternative sequenceiVSP_031519845 – 864SRSGQ…PPFDL → RITISDP in isoform 3 and isoform 4. 2 PublicationsAdd BLAST20

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. Sequence problems.
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_005251768.2. [Q05193-5]
XP_005251826.1. XM_005251769.2. [Q05193-3]
XP_016869860.1. XM_017014371.1. [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]
ENST00000627543; ENSP00000487310; ENSG00000106976. [Q05193-3]
GeneIDi1759.
KEGGihsa:1759.
UCSCiuc064wcg.1. human. [Q05193-1]

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. Sequence problems.
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_005251768.2. [Q05193-5]
XP_005251826.1. XM_005251769.2. [Q05193-3]
XP_016869860.1. XM_017014371.1. [Q05193-3]
UniGeneiHs.522413.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5D3QX-ray1.70A/B5-320[»]
A/B726-746[»]
ProteinModelPortaliQ05193.
SMRiQ05193.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108099. 65 interactors.
DIPiDIP-36242N.
IntActiQ05193. 27 interactors.
MINTiMINT-233135.
STRINGi9606.ENSP00000362014.

Chemistry databases

BindingDBiQ05193.
ChEMBLiCHEMBL4958.

PTM databases

iPTMnetiQ05193.
PhosphoSitePlusiQ05193.

Polymorphism and mutation databases

DMDMi172046078.

Proteomic databases

EPDiQ05193.
MaxQBiQ05193.
PaxDbiQ05193.
PeptideAtlasiQ05193.
PRIDEiQ05193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

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]
ENST00000627543; ENSP00000487310; ENSG00000106976. [Q05193-3]
GeneIDi1759.
KEGGihsa:1759.
UCSCiuc064wcg.1. human. [Q05193-1]

Organism-specific databases

CTDi1759.
DisGeNETi1759.
GeneCardsiDNM1.
H-InvDBHIX0026786.
HIX0211497.
HGNCiHGNC:2972. DNM1.
HPAiCAB005920.
HPA049910.
HPA061801.
MIMi602377. gene.
616346. phenotype.
neXtProtiNX_Q05193.
OpenTargetsiENSG00000106976.
PharmGKBiPA27440.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0446. Eukaryota.
COG0699. LUCA.
GeneTreeiENSGT00760000119213.
HOGENOMiHOG000161069.
HOVERGENiHBG107833.
InParanoidiQ05193.
KOiK01528.
OrthoDBiEOG091G0EIQ.
PhylomeDBiQ05193.
TreeFamiTF300362.

Enzyme and pathway databases

BioCyciZFISH:HS02963-MONOMER.
BRENDAi3.6.5.5. 2681.
ReactomeiR-HSA-166016. Toll Like Receptor 4 (TLR4) Cascade.
R-HSA-177504. Retrograde neurotrophin signalling.
R-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-437239. Recycling pathway of L1.
R-HSA-8856828. Clathrin-mediated endocytosis.
SIGNORiQ05193.

Miscellaneous databases

EvolutionaryTraceiQ05193.
GeneWikiiDNM1.
GenomeRNAii1759.
PROiQ05193.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000106976.
CleanExiHS_DNM1.
ExpressionAtlasiQ05193. baseline and differential.
GenevisibleiQ05193. HS.

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.
IPR030381. G_DYNAMIN_dom.
IPR003130. GED.
IPR020850. GED_dom.
IPR027417. P-loop_NTPase.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[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]
SUPFAMiSSF50729. SSF50729. 1 hit.
SSF52540. 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]
ProtoNetiSearch...

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 2, 2016
This is version 166 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.