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P39053 (DYN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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, Kiaa4093
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length867 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 By similarity.

Catalytic activity

GTP + H2O = GDP + phosphate.

Subunit structure

Binds SH3GL1, SH3GL2 and SH3GL3 By similarity. Interacts with SNX9 By similarity. Interacts with PHOCN. Interacts with MYO1E (via SH3 domain) By similarity. Interacts with CAV1 and SH3GLB1. Ref.8 Ref.9

Subcellular location

Cytoplasm. Cytoplasm › cytoskeleton. Note: Microtubule-associated.

Post-translational modification

Phosphorylated in response to EGF stimulation in cells expressing truncated EGFR. Ref.8

Sequence similarities

Belongs to the dynamin family.

Contains 1 GED domain.

Contains 1 PH domain.

Sequence caution

The sequence BAD90284.1 differs from that shown. Reason: Erroneous initiation.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Pfn2Q9JJV2-12EBI-397785,EBI-990256

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P39053-1)

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.
Note: Contains a phosphoserine at position 847.
Isoform 2 (identifier: P39053-2)

Also known as: BreDnm19;

The sequence of this isoform differs from the canonical sequence as follows:
     516-519: Missing.
     846-867: LGAWRLNSPQGKHENRAGKARL → RKAQPHLRDLQPPDQRRLPS
Isoform 3 (identifier: P39053-3)

Also known as: BraDnm8;

The sequence of this isoform differs from the canonical sequence as follows:
     407-444: MAFETIVKKQ...LISTVRQCTK → LAFEATVKKQ...LTSTIRKCSE
     845-867: SLGAWRLNSPQGKHENRAGKARL → RITISDP
Isoform 4 (identifier: P39053-4)

Also known as: BraDnm2;

The sequence of this isoform differs from the canonical sequence as follows:
     846-867: LGAWRLNSPQGKHENRAGKARL → RSGQASPSRPESPRPPFDL
Isoform 5 (identifier: P39053-5)

Also known as: BreDnm15;

The sequence of this isoform differs from the canonical sequence as follows:
     845-867: SLGAWRLNSPQGKHENRAGKARL → RITISDP
Isoform 6 (identifier: P39053-6)

The sequence of this isoform differs from the canonical sequence as follows:
     516-519: Missing.
     846-867: LGAWRLNSPQGKHENRAGKARL → RKGPASPTRPAAPRPTEAPLLDL
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 867867Dynamin-1
PRO_0000206564

Regions

Domain515 – 625111PH
Domain659 – 75092GED
Nucleotide binding38 – 458GTP By similarity
Nucleotide binding136 – 1405GTP By similarity
Nucleotide binding205 – 2084GTP By similarity

Amino acid modifications

Modified residue801Phosphotyrosine Ref.11
Modified residue1251Nitrated tyrosine; alternate Ref.10
Modified residue1251Phosphotyrosine; alternate Ref.11
Modified residue3471Phosphoserine By similarity
Modified residue3541Phosphotyrosine Ref.11
Modified residue5121Phosphoserine By similarity
Modified residue7781Phosphoserine Ref.12
Modified residue8221Phosphoserine By similarity

Natural variations

Alternative sequence407 – 44438MAFET…RQCTK → LAFEATVKKQVQKLKEPSIK CVDMVVSELTSTIRKCSE in isoform 3.
VSP_007643
Alternative sequence516 – 5194Missing in isoform 2 and isoform 6.
VSP_007644
Alternative sequence845 – 86723SLGAW…GKARL → RITISDP in isoform 3 and isoform 5.
VSP_007645
Alternative sequence846 – 86722LGAWR…GKARL → RKAQPHLRDLQPPDQRRLPS in isoform 2.
VSP_007646
Alternative sequence846 – 86722LGAWR…GKARL → RSGQASPSRPESPRPPFDL in isoform 4.
VSP_007647
Alternative sequence846 – 86722LGAWR…GKARL → RKGPASPTRPAAPRPTEAPL LDL in isoform 6.
VSP_024845

Experimental info

Sequence conflict1351V → A in AAA37318. Ref.1
Sequence conflict4501P → R in AAA37318. Ref.1
Sequence conflict5311I → S in AAA37318. Ref.1
Sequence conflict5731R → H in BAE25726. Ref.2
Sequence conflict6001Y → N in AAA37318. Ref.1
Sequence conflict7031A → V in AAH58623. Ref.5
Sequence conflict7221A → R in AAA37319. Ref.1
Sequence conflict7221A → R in AAA37323. Ref.1
Sequence conflict7221A → R in AAA37324. Ref.1

Sequences

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

Last modified June 20, 2003. Version 2.
Checksum: F48EC3DF5F39A08B

FASTA86797,803
        10         20         30         40         50         60 
MGNRGMEDLI PLVNRLQDAF SAIGQNADLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 

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

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

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

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

       310        320        330        340        350        360 
QSQLLSIEKE VDEYKNFRPD 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 
PGVPSLGAWR LNSPQGKHEN RAGKARL

« Hide

Isoform 2 (BreDnm19) [UniParc].

Checksum: 81F22599EA77FB3F
Show »

FASTA86197,281
Isoform 3 (BraDnm8) [UniParc].

Checksum: 5D9294C5D1015A88
Show »

FASTA85195,927
Isoform 4 (BraDnm2) [UniParc].

Checksum: 4E27474E413CCEE7
Show »

FASTA86497,424
Isoform 5 (BreDnm15) [UniParc].

Checksum: 5FE0938290E39F51
Show »

FASTA85196,057
Isoform 6 [UniParc].

Checksum: 12CA402BCCCF2936
Show »

FASTA86497,284

References

« Hide 'large scale' references
[1]"Dynamin genes Dnm1 and Dnm2 are located on proximal mouse chromosomes 2 and 9, respectively."
Klocke R., Augustin A., Ronsiek M., Stief A., van der Putten H., Jockusch H.
Genomics 41:290-292(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
Strain: NIH Swiss.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
Strain: C57BL/6J.
Tissue: Colon and Embryo.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene. The complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O., Koga H.
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"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 5).
Strain: C57BL/6.
Tissue: Brain and Retina.
[6]"Characterization of the mouse dynamin I gene promoter and identification of sequences that direct expression in neuronal cells."
Yoo J., Lee S.S., Jeong M.J., Lee K.I., Kwon B.M., Kim S.H., Park Y.M., Han M.Y.
Biochem. J. 351:661-668(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32.
[7]Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 5-54; 67-87; 91-107; 114-188; 207-217; 230-237; 247-266; 280-290; 300-309; 328-361; 370-376; 400-414; 511-535; 563-571; 584-594; 664-675 AND 684-694.
Strain: C57BL/6 and OF1.
Tissue: Brain and Hippocampus.
[8]"The endocytosis-linked protein dynamin associates with caveolin-1 and is tyrosine phosphorylated in response to the activation of a noninternalizing epidermal growth factor receptor mutant."
Kim Y.N., Bertics P.J.
Endocrinology 143:1726-1731(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CAV1, PHOSPHORYLATION.
[9]"Characterization of endophilin B1b, a brain-specific membrane-associated lysophosphatidic acid acyl transferase with properties distinct from endophilin A1."
Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.
J. Biol. Chem. 278:4160-4167(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SH3GLB1.
[10]"Endogenously nitrated proteins in mouse brain: links to neurodegenerative disease."
Sacksteder C.A., Qian W.-J., Knyushko T.V., Wang H., Chin M.H., Lacan G., Melega W.P., Camp D.G. II, Smith R.D., Smith D.J., Squier T.C., Bigelow D.J.
Biochemistry 45:8009-8022(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NITRATION [LARGE SCALE ANALYSIS] AT TYR-125, MASS SPECTROMETRY.
Tissue: Brain.
[11]"Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain."
Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.
J. Proteome Res. 7:311-318(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-80; TYR-125 AND TYR-354, MASS SPECTROMETRY.
Tissue: Brain.
[12]"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry."
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M.
J. Proteome Res. 7:5314-5326(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-778, MASS SPECTROMETRY.
Tissue: Melanoma.
[13]"Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-847 (ISOFORM 6), MASS SPECTROMETRY.
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L29457 mRNA. Translation: AAA37319.1.
L31395 mRNA. Translation: AAA37318.1.
L31396 mRNA. Translation: AAA37323.1.
L31397 mRNA. Translation: AAA37324.1.
AK011651 mRNA. Translation: BAB27759.1.
AK144142 mRNA. Translation: BAE25726.1.
AK220483 mRNA. Translation: BAD90284.1. Different initiation.
AL808027 Genomic DNA. Translation: CAM15852.1.
AL808027 Genomic DNA. Translation: CAM15853.1.
AL808027 Genomic DNA. Translation: CAM15855.1.
AL808027 Genomic DNA. Translation: CAM15857.1.
BC034679 mRNA. Translation: AAH34679.1.
BC058623 mRNA. Translation: AAH58623.1.
AF170568 Genomic DNA. Translation: AAF24220.1.
IPIIPI00272878.
IPI00331291.
IPI00331293.
IPI00465648.
IPI00753037.
IPI00845595.
RefSeqNP_034195.2. NM_010065.2.
UniGeneMm.44736.

3D structure databases

ProteinModelPortalP39053.
SMRP39053. Positions 6-746.
ModBaseSearch...

Protein-protein interaction databases

IntActP39053. 10 interactions.
MINTMINT-86537.

PTM databases

PhosphoSiteP39053.

Proteomic databases

PaxDbP39053.
PRIDEP39053.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000078352; ENSMUSP00000077461; ENSMUSG00000026825.
ENSMUST00000091089; ENSMUSP00000088618; ENSMUSG00000026825.
ENSMUST00000113350; ENSMUSP00000108977; ENSMUSG00000026825.
ENSMUST00000113352; ENSMUSP00000108979; ENSMUSG00000026825.
ENSMUST00000113365; ENSMUSP00000108992; ENSMUSG00000026825.
ENSMUST00000139624; ENSMUSP00000122679; ENSMUSG00000026825.
GeneID13429.
KEGGmmu:13429.
UCSCuc008jfc.1. mouse.
uc008jfd.1. mouse.

Organism-specific databases

CTD1759.
MGIMGI:107384. Dnm1.
RougeSearch...

Phylogenomic databases

eggNOGCOG0699.
GeneTreeENSGT00690000101762.
HOVERGENHBG107833.
KOK01528.
OMAQYPHLRE.
OrthoDBEOG49GKG1.

Gene expression databases

ArrayExpressP39053.
BgeeP39053.
CleanExMM_DNM1.
GenevestigatorP39053.
GermOnlineENSMUSG00000026825. Mus musculus.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
InterProIPR022812. Dynamin.
IPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PANTHERPTHR11566. PTHR11566. 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]
PROSITEPS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNM1. mouse.
NextBio283851.
SOURCESearch...

Entry information

Entry nameDYN1_MOUSE
AccessionPrimary (citable) accession number: P39053
Secondary accession number(s): A2AN50 expand/collapse secondary AC list , A2AN51, A2AN54, A2AN55, Q3UNM1, Q5DTN7, Q61358, Q61359, Q61360, Q6PDM5, Q8JZZ4, Q9CSY7, Q9QXX1
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: June 20, 2003
Last modified: May 1, 2013
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents