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Q8BZ98 (DYN3_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dynamin-3
EC=3.6.5.5
Gene names
Name:Dnm3
Synonyms:Kiaa0820
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 length863 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, in particular endocytosis By similarity.

Catalytic activity

GTP + H2O = GDP + phosphate.

Subcellular location

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

Sequence similarities

Belongs to the TRAFAC class dynamin-like GTPase superfamily. Dynamin/Fzo/YdjA family.

Contains 1 dynamin-type G (guanine nucleotide-binding) domain.

Contains 1 GED domain.

Contains 1 PH domain.

Ontologies

Keywords
   Biological processEndocytosis
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   Molecular functionHydrolase
Motor protein
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processendocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentmicrotubule

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from direct assay PubMed 14651853. Source: MGI

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8BZ98-1)

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: Q8BZ98-2)

The sequence of this isoform differs from the canonical sequence as follows:
     628-631: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 863863Dynamin-3
PRO_0000319951

Regions

Domain28 – 294267Dynamin-type G
Domain515 – 621107PH
Domain653 – 74492GED
Nucleotide binding38 – 458GTP By similarity
Nucleotide binding136 – 1405GTP By similarity
Nucleotide binding205 – 2084GTP By similarity

Amino acid modifications

Modified residue7631Phosphoserine By similarity
Modified residue7671Phosphoserine By similarity
Modified residue8471Phosphoserine By similarity

Natural variations

Alternative sequence628 – 6314Missing in isoform 2.
VSP_031548

Experimental info

Sequence conflict1391G → A in BAE28068. Ref.1
Sequence conflict532 – 54918Missing in BAC65661. Ref.3

Sequences

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

Last modified March 1, 2003. Version 1.
Checksum: 8BDBB091CB10D264

FASTA86397,190
        10         20         30         40         50         60 
MGNREMEELI PLVNRLQDAF SALGQSCLLE LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 

        70         80         90        100        110        120 
SGIVTRRPLV LQLVTSKAEY AEFLHCKGKK FTDFDEVRHE IEAETDRVTG MNKGISSIPI 

       130        140        150        160        170        180 
NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIRDMI MQFITRENCL ILAVTPANTD 

       190        200        210        220        230        240 
LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YVGVVNRSQK 

       250        260        270        280        290        300 
DIDGKKDIKA AMLAERKFFL SHPAYRHIAD RMGTPHLQKV LNQQLTNHIR DTLPNFRNKL 

       310        320        330        340        350        360 
QGQLLSIEHE VEAFKNFKPE DPTRKTKALL QMVQQFAVDF EKRIEGSGDQ VDTLELSGGA 

       370        380        390        400        410        420 
KINRIFHERF PFEIVKMEFN EKELRREISY AIKNIHGIRT GLFTPDMAFE AIVKKQIVKL 

       430        440        450        460        470        480 
KGPSLKSVDL VMQELINTVK KCTKRLANFP RLCEETERIV ANHIREREGK TKDQVLLLID 

       490        500        510        520        530        540 
IQVSYINTNH EDFIGFANAQ QRSSQVHKKS TIGNQVIRKG WLTVSNIGIM KGGSKGYWFV 

       550        560        570        580        590        600 
LTAESLSWYK DDEEKEKKYM LPLDNLKVRD VEKGFMSSKH VFALFNTEQR NVYKDYRFLE 

       610        620        630        640        650        660 
LACDSQEDVD SWKASLLRAG VYPDKSVGSN KTENDENGQA ENFSMDPQLE RQVETIRNLV 

       670        680        690        700        710        720 
DSYMSIINKC IRDLIPKTIM HLMINNVKDF INSELLAQLY SSEDQNTLME ESAEQAQRRD 

       730        740        750        760        770        780 
EMLRMYQALK EALAIIGDIN TATVSTPAPP PVDDSWLQHS RRSPPPSPTT QRRLTISAPL 

       790        800        810        820        830        840 
PRPTSGRGPA PAIPSPGPHS GAPPVPFRPG PLPPFPNSSD SFGAPPQVPS RPTRAPPSVP 

       850        860 
SRRPPPSPTR PTIIRPLESS LLD

« Hide

Isoform 2 [UniParc].

Checksum: 591E1B65A81A26D0
Show »

FASTA85996,804

References

[1]"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] (ISOFORMS 1 AND 2).
Strain: C57BL/6.
Tissue: Brain, Cerebellum and Spinal cord.
[2]"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 1).
Tissue: Brain.
[3]"Prediction of the coding sequences of mouse homologues of KIAA gene: II. The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S., Nakajima D., Nagase T., Ohara O., Koga H.
DNA Res. 10:35-48(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 394-863 (ISOFORM 1).
Tissue: Brain.
[4]"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Brain cortex.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK036199 mRNA. Translation: BAC29343.1.
AK049724 mRNA. Translation: BAC33895.1.
AK147678 mRNA. Translation: BAE28068.1.
BC141143 mRNA. Translation: AAI41144.1.
BC141144 mRNA. Translation: AAI41145.1.
AK122379 Transcribed RNA. Translation: BAC65661.1.
CCDSCCDS48417.1. [Q8BZ98-2]
RefSeqNP_001033708.1. NM_001038619.1. [Q8BZ98-1]
NP_766234.1. NM_172646.2. [Q8BZ98-2]
UniGeneMm.441620.

3D structure databases

ProteinModelPortalQ8BZ98.
SMRQ8BZ98. Positions 6-740.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ8BZ98. 5 interactions.
MINTMINT-1856052.

PTM databases

PhosphoSiteQ8BZ98.

Proteomic databases

MaxQBQ8BZ98.
PaxDbQ8BZ98.
PRIDEQ8BZ98.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000070330; ENSMUSP00000064538; ENSMUSG00000040265. [Q8BZ98-2]
GeneID103967.
KEGGmmu:103967.
UCSCuc007dga.2. mouse. [Q8BZ98-1]
uc007dgb.2. mouse. [Q8BZ98-2]

Organism-specific databases

CTD26052.
MGIMGI:1341299. Dnm3.
RougeSearch...

Phylogenomic databases

eggNOGCOG0699.
GeneTreeENSGT00740000115253.
HOGENOMHOG000161069.
HOVERGENHBG107833.
InParanoidB2RUH0.
KOK01528.
PhylomeDBQ8BZ98.
TreeFamTF300362.

Gene expression databases

ArrayExpressQ8BZ98.
BgeeQ8BZ98.
CleanExMM_DNM3.
GenevestigatorQ8BZ98.

Family and domain databases

Gene3D2.30.29.30. 1 hit.
3.40.50.300. 1 hit.
InterProIPR027743. Dnm3.
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:SF54. PTHR11566:SF54. 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. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSDNM3. mouse.
NextBio356261.
PROQ8BZ98.
SOURCESearch...

Entry information

Entry nameDYN3_MOUSE
AccessionPrimary (citable) accession number: Q8BZ98
Secondary accession number(s): B2RUH0 expand/collapse secondary AC list , Q3UGY9, Q80TR2, Q8BWW6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 102 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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

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