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Reviewed, UniProtKB/Swiss-Prot Q8K1M6 (DNM1L_MOUSE)

Last modified November 3, 2009. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dynamin-1-like protein
    EC=3.6.5.5
Alternative name(s):
    Dynamin-related protein 1
    Dynamin family member proline-rich carboxyl-terminal domain less
      Short name=Dymple
Gene names
Name: Dnm1l
Synonyms: Drp1
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length742 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Functions in mitochondrial and peroxisomal division probably by regulating membrane fission. Enzyme hydrolyzing GTP that oligomerizes to form ring-like structures and is able to remodel membranes. May also play a role on organelles of the secretory pathway By similarity.

Catalytic activity

GTP + H2O = GDP + phosphate.

Subunit structure

Homotetramer; N-terminal part binds to the C-terminal part of another DNM1L. Can self-assemble in multimeric ring-like structures. Interacts with GSK3B and FIS1 By similarity.

Subcellular location

Cytoplasmcytosol By similarity. Endomembrane system; Peripheral membrane protein By similarity. Note: Mainly cytosolic By similarity. Also membrane-associated. Localizes to mitochondria at spots of division events. Associated with peroxisomal membranes, it is recruited in part by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear By similarity.

Tissue specificity

Expressed in the cerebellum and in several regions of the cerebrum and diencephalon. Strongly expressed in the cerebellar Purkinje cells and in the pontile giant neurons. Ref.6

Post-translational modification

Phosphorylated by GSK3B By similarity.

Sequence similarities

Belongs to the dynamin family.

Contains 1 GED domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Phosphoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Cellular componentcytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8K1M6-1)

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: No experimental confirmation available.
Isoform 2 (identifier: Q8K1M6-2)

The sequence of this isoform differs from the canonical sequence as follows:
     539-564: Missing.
Isoform 3 (identifier: Q8K1M6-3)

The sequence of this isoform differs from the canonical sequence as follows:
     85-90: Missing.
     539-575: Missing.
Isoform 4 (identifier: Q8K1M6-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-104: Missing.
     105-105: K → M
     539-564: Missing.
Isoform 5 (identifier: Q8K1M6-5)

The sequence of this isoform differs from the canonical sequence as follows:
     85-90: Missing.
     214-227: RRTLAVITKLDLMD → KGRCLYLMDVDLQW
     228-742: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 742742Dynamin-1-like protein
PRO_0000206567

Regions

Domain650 – 74192GED
Nucleotide binding32 – 398GTP By similarity
Nucleotide binding152 – 1565GTP By similarity
Nucleotide binding221 – 2244GTP By similarity
Region1 – 349349N-terminal dimerization domain By similarity
Region454 – 654201Interaction with GSK3B By similarity
Region548 – 742195C-terminal dimerization domain By similarity

Amino acid modifications

Modified residue2891N6-acetyllysine By similarity
Modified residue5351Phosphoserine Ref.7
Modified residue6221Phosphoserine By similarity

Natural variations

Alternative sequence1 – 104104Missing in isoform 4.
VSP_013689
Alternative sequence85 – 906Missing in isoform 3 and isoform 5.
VSP_013690
Alternative sequence1051K → M in isoform 4.
VSP_013691
Alternative sequence214 – 22714RRTLA…LDLMD → KGRCLYLMDVDLQW in isoform 5.
VSP_013692
Alternative sequence228 – 742515Missing in isoform 5.
VSP_013693
Alternative sequence539 – 57537Missing in isoform 3.
VSP_013694
Alternative sequence539 – 56426Missing in isoform 2 and isoform 4.
VSP_013695

Experimental info

Sequence conflict1651P → L in BAC06576. Ref.1
Sequence conflict3201Q → R in BAC06576. Ref.1
Sequence conflict5191E → A in BAC34640. Ref.2

Sequences

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

Last modified May 10, 2005. Version 2.
Checksum: 5A8679B61A444847

FASTA74282,658
        10         20         30         40         50         60 
MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGVVTR 

        70         80         90        100        110        120 
RPLILQLVHV SPEDKRKTTG EENGKFQSWR VEAEEWGKFL HTKNKLYTDF DEIRQEIENE 

       130        140        150        160        170        180 
TERISGNNKG VSPEPIHLKV FSPNVVNLTL VDLPGMTKVP VGDQPKDIEL QIRELILRFI 

       190        200        210        220        230        240 
SNPNSIILAV TAANTDMATS EALKISREVD PDGRRTLAVI TKLDLMDAGT DAMDVLMGRV 

       250        260        270        280        290        300 
IPVKLGIIGV VNRSQLDINN KKSVTDSIRD EYAFLQKKYP SLANRNGTKY LARTLNRLLM 

       310        320        330        340        350        360 
HHIRDCLPEL KTRINVLAAQ YQSLLNSYGE PVDDKSATLL QLITKFATEY CNTIEGTAKY 

       370        380        390        400        410        420 
IETSELCGGA RICYIFHETF GRTLESVDPL GGLNTIDILT AIRNATGPRP ALFVPEVSFE 

       430        440        450        460        470        480 
LLVKRQIKRL EEPSLRCVEL VHEEMQRIIQ HCSNYSTQEL LRFPKLHDAI VEVVTCLLRK 

       490        500        510        520        530        540 
RLPVTNEMVH NLVAIELAYI NTKHPDFADA CGLMNNNIEE QRRNRLAREL PSAGSRDKSS 

       550        560        570        580        590        600 
KVPSALAPAS QEPPPAASAE ADGKLIQDNR RETKNVPSAG GGIGDGGQEP TTGNWRGMLK 

       610        620        630        640        650        660 
TSKAEELLAE EKSKPIPIMP ASPQKGHAVN LLDVPVPVAR KLSAREQRDC EVIERLIKSY 

       670        680        690        700        710        720 
FLIVRKNIQD SVPKAVMHFL VNHVKDTLQS ELVGQLYKSS LLDDLLTESE DMAQRRKEAA 

       730        740 
DMLKALQGAS QIIAEIRETH LW 

« Hide

Isoform 2.

Checksum: 3C922A7A135B9A37
Show »

FASTA71680,212
Isoform 3.

Checksum: 68ED85D93914B4DC
Show »

FASTA69978,011
Isoform 4.

Checksum: C5D0BCE4B4622502
Show »

FASTA61268,701
Isoform 5.

Checksum: 29C66A3A04924F55
Show »

FASTA22124,488

References

« Hide 'large scale' references
[1]"Stage-specific enhanced expression of mitochondrial fusion and fission factors during spermatogenesis in rat testis."
Honda S., Hirose S.
Biochem. Biophys. Res. Commun. 311:424-432(2003) [PubMed: 14592431] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Osteoclast.
[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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
Strain: C57BL/6J.
Tissue: Adipose tissue and Spinal ganglion.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
Strain: C57BL/6.
Tissue: Brain, Mammary gland and Thymus.
[4]"Construction of long-transcript enriched cDNA libraries from submicrogram amounts of total RNAs by a universal PCR amplification method."
Piao Y., Ko N.T., Lim M.K., Ko M.S.H.
Genome Res. 11:1553-1558(2001) [PubMed: 11544199] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 448-659 (ISOFORM 1).
[5]Lubec G., Klug S.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 626-640 AND 725-737, MASS SPECTROMETRY.
Tissue: Hippocampus.
[6]"Dymple, a novel dynamin-like high molecular weight GTPase lacking a proline-rich carboxyl-terminal domain in mammalian cells."
Kamimoto T., Nagai Y., Onogi H., Muro Y., Wakabayashi T., Hagiwara M.
J. Biol. Chem. 273:1044-1051(1998) [PubMed: 9422767] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"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: 18973353] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-535, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB079133 mRNA. Translation: BAC06576.1.
AK051443 mRNA. Translation: BAC34640.1.
AK080871 mRNA. Translation: BAC38054.1.
BC027538 mRNA. Translation: AAH27538.1.
BC040777 mRNA. Translation: AAH40777.1.
BC079635 mRNA. Translation: AAH79635.1.
CF914619 mRNA. No translation available.
IPIIPI00172221.
IPI00471349.
IPI00556723.
IPI00556781.
IPI00556857.
RefSeqNP_001021118.1.
NP_690029.2.
UniGeneMm.218820

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ8K1M6. 1 interaction.
STRINGQ8K1M6.

PTM databases

PhosphoSiteQ8K1M6.

Proteomic databases

PRIDEQ8K1M6.

Genome annotation databases

EnsemblENSMUST00000023477; ENSMUSP00000023477; ENSMUSG00000022789; Mus musculus. [Genome view]
ENSMUST00000047122; ENSMUSP00000093944; ENSMUSG00000022789; Mus musculus. [Genome view]
ENSMUST00000115749; ENSMUSP00000111415; ENSMUSG00000022789; Mus musculus. [Genome view]
GeneID74006.
KEGGmmu:74006.
UCSCuc007yik.1. mouse.
uc007yil.1. mouse.
uc007yin.1. mouse.
uc007yio.1. mouse.

Organism-specific databases

CTD74006.
MGIMGI:1921256. Dnm1l.

Phylogenomic databases

HOGENOMQ8K1M6.
HOVERGENQ8K1M6.
OMANDPATWK.

Enzyme and pathway databases

BRENDA3.6.5.5. 244.

Gene expression databases

ArrayExpressQ8K1M6.
BgeeQ8K1M6.
CleanExMM_DNM1L.
GenevestigatorQ8K1M6.
GermOnlineENSMUSG00000022789. Mus musculus.

Family and domain databases

InterProIPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR003130. GED.
[Graphical view]
PfamPF01031. Dynamin_M. 1 hit.
PF00350. Dynamin_N. 1 hit.
PF02212. GED. 1 hit.
[Graphical view]
PRINTSPR00195. DYNAMIN.
SMARTSM00053. DYNc. 1 hit.
SM00302. GED. 1 hit.
[Graphical view]
PROSITEPS00410. DYNAMIN. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio339508.
SOURCESearch...

Entry information

Entry nameDNM1L_MOUSE
AccessionPrimary (citable) accession number: Q8K1M6
Secondary accession number(s): Q8BNQ5 expand/collapse secondary AC list , Q8BQ64, Q8CGD0, Q8K1A1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2005
Last sequence update: May 10, 2005
Last modified: November 3, 2009
This is version 63 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents