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Q05193

- DYN1_HUMAN

UniProt

Q05193 - DYN1_HUMAN

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Protein
Dynamin-1
Gene
DNM1, DNM
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 – 458GTP By similarity
Nucleotide bindingi136 – 1405GTP By similarity
Nucleotide bindingi205 – 2084GTP By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. GTP catabolic process Source: GOC
  2. endocytosis Source: BHF-UCL
  3. endosome organization Source: BHF-UCL
  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_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. Cytoplasmcytoskeleton
Note: Microtubule-associated.1 Publication

GO - Cellular componenti

  1. membrane coat Source: Ensembl
  2. 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-1
PRO_0000206563Add
BLAST

Amino acid modifications

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

Keywords - PTMi

Nitration, Phosphoprotein

Proteomic databases

MaxQBiQ05193.
PaxDbiQ05193.
PRIDEiQ05193.

PTM databases

PhosphoSiteiQ05193.

Expressioni

Gene expression databases

BgeeiQ05193.
CleanExiHS_DNM1.
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).3 Publications

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

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortaliQ05193.
SMRiQ05193. Positions 6-746.

Miscellaneous databases

EvolutionaryTraceiQ05193.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 294267Dynamin-type G
Add
BLAST
Domaini519 – 625107PH
Add
BLAST
Domaini659 – 75092GED
Add
BLAST

Sequence similaritiesi

Contains 1 GED domain.
Contains 1 PH domain.

Phylogenomic databases

eggNOGiCOG0699.
HOGENOMiHOG000161069.
HOVERGENiHBG107833.
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

MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN    50
FVGRDFLPRG SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE 100
IEAETDRVTG TNKGISPVPI NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP 150
DIEFQIRDML MQFVTKENCL ILAVSPANSD LANSDALKVA KEVDPQGQRT 200
IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK DIDGKKDITA 250
ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL 300
QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ 350
IDTYELSGGA RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT 400
GLFTPDMAFE TIVKKQVKKI REPCLKCVDM VISELISTVR QCTKKLQQYP 450
RLREEMERIV TTHIREREGR TKEQVMLLID IELAYMNTNH EDFIGFANAQ 500
QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE YWFVLTAENL 550
SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY 600
RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS 650
MDPQLERQVE TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE 700
LLANLYSCGD QNTLMEESAE QAQRRDEMLR MYHALKEALS IIGDINTTTV 750
STPMPPPVDD SWLQVQSVPA GRRSPTSSPT PQRRAPAVPP ARPGSRGPAP 800
GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP PGVPSRSGQA 850
SPSRPESPRP PFDL 864
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

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.
VSP_031518Add
BLAST
Alternative sequencei845 – 86420SRSGQ…PPFDL → RITISDP in isoform 3 and isoform 5.
VSP_031519Add
BLAST
Alternative sequencei846 – 86419RSGQA…PPFDL → QPIGSGKSIPS in isoform 4.
VSP_031520Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti188 – 1881K → E in AAH50279. 1 Publication
Sequence conflicti287 – 2871N → D in AAH50279. 1 Publication
Sequence conflicti809 – 8091L → M in AAH50279. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]
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:
EMBL
GenBank
DDBJ
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 ]
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:
PDBe
RCSB PDB
PDBj
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 [» ]
ProteinModelPortali Q05193.
SMRi Q05193. Positions 6-746.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108099. 51 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.
HOGENOMi HOG000161069.
HOVERGENi HBG107833.
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_6894. Toll Like Receptor 4 (TLR4) Cascade.

Miscellaneous databases

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

Gene expression databases

Bgeei Q05193.
CleanExi HS_DNM1.
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: September 3, 2014
This is version 141 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

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