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Q05193 (DYN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynamin-1

EC=3.6.5.5
Gene names
Name:DNM1
Synonyms:DNM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length864 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

GTP + H2O = GDP + phosphate.

Subunit structure

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). Ref.4 Ref.6 Ref.7

Subcellular location

Cytoplasm. Cytoplasmcytoskeleton. Note: Microtubule-associated. Ref.4

Sequence similarities

Belongs to the dynamin family.

Contains 1 GED domain.

Contains 1 PH domain.

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q05193-1)

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.
Isoform 2 (identifier: Q05193-2)

The sequence of this isoform differs from the canonical sequence as follows:
     407-444: MAFETIVKKQ...LISTVRQCTK → LAFEATVKKQ...LTATIRKCSE
Isoform 3 (identifier: Q05193-3)

The sequence of this isoform differs from the canonical sequence as follows:
     845-864: SRSGQASPSRPESPRPPFDL → RITISDP
Isoform 4 (identifier: Q05193-4)

The sequence of this isoform differs from the canonical sequence as follows:
     846-864: RSGQASPSRPESPRPPFDL → QPIGSGKSIPS
Isoform 5 (identifier: Q05193-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 864864Dynamin-1
PRO_0000206563

Regions

Domain519 – 625107PH
Domain659 – 75092GED
Nucleotide binding38 – 458GTP By similarity
Nucleotide binding136 – 1405GTP By similarity
Nucleotide binding205 – 2084GTP By similarity

Amino acid modifications

Modified residue801Phosphotyrosine By similarity
Modified residue1251Nitrated tyrosine; alternate By similarity
Modified residue1251Phosphotyrosine; alternate By similarity
Modified residue3471Phosphoserine By similarity
Modified residue3541Phosphotyrosine By similarity
Modified residue5121Phosphoserine By similarity
Modified residue7741Phosphoserine By similarity
Modified residue7781Phosphoserine By similarity
Modified residue8221Phosphoserine By similarity
Modified residue8511Phosphoserine By similarity
Modified residue8571Phosphoserine By similarity

Natural variations

Alternative sequence407 – 44438MAFET…RQCTK → LAFEATVKKQVQKLKEPSIK CVDMVVSELTATIRKCSE in isoform 2 and isoform 5.
VSP_031518
Alternative sequence845 – 86420SRSGQ…PPFDL → RITISDP in isoform 3 and isoform 5.
VSP_031519
Alternative sequence846 – 86419RSGQA…PPFDL → QPIGSGKSIPS in isoform 4.
VSP_031520
Natural variant7441D → N. Ref.1
Corresponds to variant rs1042007 [ dbSNP | Ensembl ].
VAR_048904

Experimental info

Mutagenesis441K → A: Inhibits receptor-mediated endocytosis. Ref.1
Sequence conflict1881K → E in AAH50279. Ref.3
Sequence conflict2871N → D in AAH50279. Ref.3
Sequence conflict8091L → M in AAH50279. Ref.3

Secondary structure

..................................................................... 864
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 18, 2008. Version 2.
Checksum: 7FCD8CB572FFEAEF

FASTA86497,408
        10         20         30         40         50         60 
MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 

        70         80         90        100        110        120 
SGIVTRRPLV LQLVNATTEY AEFLHCKGKK FTDFEEVRLE IEAETDRVTG TNKGISPVPI 

       130        140        150        160        170        180 
NLRVYSPHVL NLTLVDLPGM TKVPVGDQPP DIEFQIRDML MQFVTKENCL ILAVSPANSD 

       190        200        210        220        230        240 
LANSDALKVA KEVDPQGQRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 

       250        260        270        280        290        300 
DIDGKKDITA ALAAERKFFL SHPSYRHLAD RMGTPYLQKV LNQQLTNHIR DTLPGLRNKL 

       310        320        330        340        350        360 
QSQLLSIEKE VEEYKNFRPD DPARKTKALL QMVQQFAVDF EKRIEGSGDQ IDTYELSGGA 

       370        380        390        400        410        420 
RINRIFHERF PFELVKMEFD EKELRREISY AIKNIHGIRT GLFTPDMAFE TIVKKQVKKI 

       430        440        450        460        470        480 
REPCLKCVDM VISELISTVR QCTKKLQQYP RLREEMERIV TTHIREREGR TKEQVMLLID 

       490        500        510        520        530        540 
IELAYMNTNH EDFIGFANAQ QRSNQMNKKK TSGNQDEILV IRKGWLTINN IGIMKGGSKE 

       550        560        570        580        590        600 
YWFVLTAENL SWYKDDEEKE KKYMLSVDNL KLRDVEKGFM SSKHIFALFN TEQRNVYKDY 

       610        620        630        640        650        660 
RQLELACETQ EEVDSWKASF LRAGVYPERV GDKEKASETE ENGSDSFMHS MDPQLERQVE 

       670        680        690        700        710        720 
TIRNLVDSYM AIVNKTVRDL MPKTIMHLMI NNTKEFIFSE LLANLYSCGD QNTLMEESAE 

       730        740        750        760        770        780 
QAQRRDEMLR MYHALKEALS IIGDINTTTV STPMPPPVDD SWLQVQSVPA GRRSPTSSPT 

       790        800        810        820        830        840 
PQRRAPAVPP ARPGSRGPAP GPPPAGSALG GAPPVPSRPG ASPDPFGPPP QVPSRPNRAP 

       850        860 
PGVPSRSGQA SPSRPESPRP PFDL 

« Hide

Isoform 2 [UniParc].

Checksum: DC9E3D5259D891DF
Show »

FASTA86497,263
Isoform 3 [UniParc].

Checksum: 89040FCDDAC2870C
Show »

FASTA85196,041
Isoform 4 [UniParc].

Checksum: 7FF33D80ED860B02
Show »

FASTA85696,397
Isoform 5 [UniParc].

Checksum: 4230B9970D097B20
Show »

FASTA85195,895

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Phosphoproteome of resting human platelets."
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.
J. Proteome Res. 7:526-534(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Platelet.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA40671.
RefSeqNP_001005336.1. NM_001005336.2.
NP_001275666.1. NM_001288737.1.
NP_001275667.1. NM_001288738.1.
NP_001275668.1. NM_001288739.1.
NP_004399.2. NM_004408.3.
XP_005251825.1. XM_005251768.1.
XP_005251826.1. XM_005251769.1.
UniGeneHs.522413.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DYNX-ray2.20A/B510-633[»]
2DYNX-ray2.30A/B509-630[»]
2X2EX-ray2.00A/D6-750[»]
2X2FX-ray2.00A/D6-750[»]
3SNHX-ray3.70A6-746[»]
3ZYCX-ray2.20A/D6-750[»]
3ZYSelectron microscopy12.20A/D6-750[»]
C/F518-630[»]
ProteinModelPortalQ05193.
SMRQ05193. Positions 5-743.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108099. 51 interactions.
DIPDIP-36242N.
IntActQ05193. 25 interactions.
MINTMINT-233135.
STRING9606.ENSP00000362014.

Chemistry

BindingDBQ05193.
ChEMBLCHEMBL4958.

PTM databases

PhosphoSiteQ05193.

Polymorphism databases

DMDM172046078.

Proteomic databases

PaxDbQ05193.
PRIDEQ05193.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341179; ENSP00000345680; ENSG00000106976. [Q05193-3]
ENST00000372923; ENSP00000362014; ENSG00000106976. [Q05193-1]
ENST00000393594; ENSP00000377219; ENSG00000106976. [Q05193-5]
ENST00000475805; ENSP00000419225; ENSG00000106976. [Q05193-5]
ENST00000486160; ENSP00000420045; ENSG00000106976. [Q05193-2]
GeneID1759.
KEGGhsa:1759.
UCSCuc022bnx.1. human. [Q05193-5]
uc022bny.1. human. [Q05193-3]
uc022boa.1. human. [Q05193-1]

Organism-specific databases

CTD1759.
GeneCardsGC09P130965.
H-InvDBHIX0026786.
HIX0211497.
HGNCHGNC:2972. DNM1.
HPACAB005920.
HPA049910.
MIM602377. gene.
neXtProtNX_Q05193.
PharmGKBPA27440.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0699.
HOGENOMHOG000161069.
HOVERGENHBG107833.
KOK01528.
OMAQYPHLRE.
OrthoDBEOG76MK7N.
PhylomeDBQ05193.
TreeFamTF300362.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_11123. Membrane Trafficking.
REACT_6900. Immune System.

Gene expression databases

BgeeQ05193.
CleanExHS_DNM1.
GenevestigatorQ05193.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.40.50.300. 1 hit.
InterProIPR027741. 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.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PANTHERPTHR11566. PTHR11566. 1 hit.
PTHR11566:SF32. PTHR11566:SF32. 1 hit.
PfamPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
PRINTSPR00195. DYNAMIN.
SMARTSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNM1. human.
EvolutionaryTraceQ05193.
GeneWikiDNM1.
GenomeRNAi1759.
NextBio7163.
PROQ05193.
SOURCESearch...

Entry information

Entry nameDYN1_HUMAN
AccessionPrimary (citable) accession number: Q05193
Secondary accession number(s): A6NLM6 expand/collapse secondary AC list , Q5SYX0, Q5SYX2, Q6P3T6, Q86VD2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: March 18, 2008
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM