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Q8K1M6 (DNM1L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 108. 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

Names and origin

Protein namesRecommended name:
Dynamin-1-like protein

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

Protein attributes

Sequence length742 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into membrane-associated tubular structures that wrap around the scission site to constrict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Through its function in mitochondrial division, ensures the survival of at least some types of postmitotic neurons, including Purkinje cells, by suppressing oxidative damage. Required for normal brain development, including that of cerebellum. Facilitates developmentally regulated apoptosis during neural tube formation. Required for a normal rate of cytochrome c release and caspase activation during apoptosis; this requirement may depend upon the cell type and the physiological apoptotic cues. Also required for mitochondrial fission during mitosis. Required for formation of endocytic vesicles. Proposed to regulate synaptic vesicle membrane dynamics through association with BCL2L1 isoform Bcl-X(L)which stimulates its GTPase activity in synaptic vesicles; the function may require its recruitment by MFF to clathrin-containing vesicles. Required for programmed necrosis execution. Ref.7 Ref.8 Ref.9 Ref.10 Ref.12

Catalytic activity

GTP + H2O = GDP + phosphate. Ref.12

Subunit structure

Homotetramer; dimerizes through the N-terminal GTP-middle region of one molecule binding to the GED domain of another DNM1L molecule. Oligomerizes in a GTP-dependent manner to form membrane-associated tubules with a spiral pattern. Can also oligomerize to form multimeric ring-like structures. Interacts with GSK3B and MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in its B domain. Interacts with PPP3CA; the interaction dephosphorylates DNM1L and regulates its transition to mitochondria. Interacts with BCL2L1 isoform BCL-X(L)and CLTA; DNM1L and BCL2L1 isoform BCL-X(L)may form a complex in synaptic vesicles that also contains clathrin and MFF. Interacts with FIS1. Interacts with MIEF2. Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-656 and activation of GTPase activity and eventually to mitochondria fragmentation By similarity. Interacts with MIEF1; this regulates GTP hydrolysis and DNM1L oligomerization. Ref.12

Subcellular location

Cytoplasmcytosol. Golgi apparatus By similarity. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome By similarity. Membraneclathrin-coated pit By similarity. Cytoplasmic vesiclesecretory vesiclesynaptic vesicle membrane By similarity. Note: Mainly cytosolic. Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Colocalized with MARCH5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. Associated with peroxisomal membranes, partly recruited there by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear. In some cell types, localizes to the Golgi complex By similarity. Recruited to the mitochondrial outer membrane by interaction with MIEF1. Binds to phospholipid membranes. Ref.10 Ref.12

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

Domain

The GED domain folds back to interact, in cis, with the GTP-binding domain and middle domain, and interacts, in trans, with the GED domains of other DNM1L molecules, and is thus critical for activating GTPase activity and for DNM1L dimerization By similarity.

Post-translational modification

Phosphorylation/dephosphorylation events on two sites near the GED domain regulate mitochondrial fission. Phosphorylation on Ser-643 inhibits mitochondrial fission probably through preventing intramolecular interaction. Dephosphorylated on this site by PPP3CA which promotes mitochondrial fission. Phosphorylation on Ser-622 also promotes mitochondrial fission By similarity.

Sumoylated on various lysine residues within the B domain, probably by MUL1. Sumoylation positively regulates mitochondrial fission. Desumoylated by SENP5 during G2/M transition of mitosis. Appears to be linked to its catalytic activity By similarity.

S-nitrosylation increases DNM1L dimerization, mitochondrial fission and causes neuronal damage By similarity.

O-GlcNAcylation augments the level of the GTP-bound active form of DRP1 and induces translocation from the cytoplasm to mitochondria in cardiomyocytes. It also decreases phosphorylation at Ser-643 By similarity.

Disruption phenotype

Mutant mice show severe developmental abnormalities and die between 10.5 and 12.5 dpc. Compared to wild-type littermates, mutant embryos at 9.5-11.5 dpc have a significantly smaller body size, pulsing, but less developed cardiac structures, a poorly developed liver and a thinner neural tube cell layer. They lack trophoblastic giant cell layer in the placenta. Primary cultures of mutant neuronal cells have severe defects in synapse formation and high sensitivity to Ca2+-dependent apoptosis. Within cerebellar neurons, Purkinje cells are particularly sensitive to Dnm1l ablation. Conditional knockout in postmitotic Purkinje cells leads to 40% neuronal degeneration after 3 months and 90% after 6 months. Ref.7 Ref.8 Ref.9

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.

Ontologies

Keywords
   Biological processEndocytosis
Necrosis
   Cellular componentCell junction
Coated pit
Cytoplasm
Cytoplasmic vesicle
Golgi apparatus
Membrane
Mitochondrion
Mitochondrion outer membrane
Peroxisome
Synapse
   Coding sequence diversityAlternative splicing
   LigandGTP-binding
Lipid-binding
Nucleotide-binding
   Molecular functionHydrolase
   PTMAcetylation
Glycoprotein
Isopeptide bond
Phosphoprotein
S-nitrosylation
Ubl conjugation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processGTP catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

dynamin polymerization involved in mitochondrial fission

Inferred from sequence or structural similarity. Source: UniProtKB

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrial fission

Inferred from mutant phenotype Ref.10. Source: UniProtKB

necroptotic process

Inferred from mutant phenotype PubMed 22265414. Source: UniProtKB

peroxisome fission

Inferred from sequence or structural similarity. Source: UniProtKB

protein localization to mitochondrion

Inferred from mutant phenotype PubMed 24515348. Source: MGI

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell junction

Inferred from electronic annotation. Source: UniProtKB-KW

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from mutant phenotype Ref.10. Source: UniProtKB

mitochondrial outer membrane

Inferred from direct assay PubMed 21149567. Source: MGI

mitochondrion

Inferred from mutant phenotype Ref.10. Source: UniProtKB

peroxisome

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: UniProtKB-KW

GTPase activity

Inferred from sequence or structural similarity. Source: UniProtKB

lipid binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction PubMed 22639965PubMed 24282027. Source: IntAct

protein homodimerization activity

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Lrrk2Q5S0064EBI-2365792,EBI-2693710

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

Domain22 – 308287Dynamin-type G
Domain650 – 74192GED
Nucleotide binding32 – 398GTP By similarity
Nucleotide binding152 – 1565GTP By similarity
Nucleotide binding221 – 2244GTP By similarity
Region1 – 349349GTPase domain By similarity
Region1 – 349349N-terminal dimerization domain By similarity
Region350 – 495146Middle domain By similarity
Region454 – 691238Interaction with GSK3B By similarity
Region454 – 654201Interaction with GSK3B By similarity
Region508 – 57568B domain By similarity
Region548 – 742195C-terminal dimerization domain By similarity
Region660 – 67415Important for homodimerization By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue6031N6-acetyllysine; alternate Ref.11
Modified residue6131Phosphoserine By similarity
Modified residue6221Phosphoserine; by CDK1 By similarity
Modified residue6431Phosphoserine; by CAMK1 and PKA By similarity
Modified residue6501S-nitrosocysteine By similarity
Glycosylation5911O-linked (GlcNAc) By similarity
Glycosylation5921O-linked (GlcNAc) By similarity
Cross-link538Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link541Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link564Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link574Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link600Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link603Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO); alternate By similarity
Cross-link612Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link614Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) 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

Mutagenesis591T → A: Abolishes GTP hydrolysis. Ref.12
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 [UniParc].

Checksum: 3C922A7A135B9A37
Show »

FASTA71680,212
Isoform 3 [UniParc].

Checksum: 68ED85D93914B4DC
Show »

FASTA69978,011
Isoform 4 [UniParc].

Checksum: C5D0BCE4B4622502
Show »

FASTA61268,701
Isoform 5 [UniParc].

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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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, IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[7]"The dynamin-related GTPase Drp1 is required for embryonic and brain development in mice."
Wakabayashi J., Zhang Z., Wakabayashi N., Tamura Y., Fukaya M., Kensler T.W., Iijima M., Sesaki H.
J. Cell Biol. 186:805-816(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN PURKINJE CELLS.
[8]"Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice."
Ishihara N., Nomura M., Jofuku A., Kato H., Suzuki S.O., Masuda K., Otera H., Nakanishi Y., Nonaka I., Goto Y., Taguchi N., Morinaga H., Maeda M., Takayanagi R., Yokota S., Mihara K.
Nat. Cell Biol. 11:958-966(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE, FUNCTION.
[9]"Mitochondrial division ensures the survival of postmitotic neurons by suppressing oxidative damage."
Kageyama Y., Zhang Z., Roda R., Fukaya M., Wakabayashi J., Wakabayashi N., Kensler T.W., Reddy P.H., Iijima M., Sesaki H.
J. Cell Biol. 197:535-551(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, DISRUPTION PHENOTYPE, CONDITIONAL KNOCKOUT IN PURKINJE CELLS.
[10]"Fis1, Mff, MiD49, and MiD51 mediate Drp1 recruitment in mitochondrial fission."
Loson O.C., Song Z., Chen H., Chan D.C.
Mol. Biol. Cell 24:659-667(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-603, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
[12]"The mitochondrial fission receptor Mid51 requires ADP as a cofactor."
Loson O.C., Liu R., Rome M.E., Meng S., Kaiser J.T., Shan S.O., Chan D.C.
Structure 22:367-377(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-59, CATALYTIC ACTIVITY, INTERACTION WITH MIEF1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS27984.1. [Q8K1M6-3]
CCDS70689.1. [Q8K1M6-2]
RefSeqNP_001021118.1. NM_001025947.2. [Q8K1M6-3]
NP_001263269.1. NM_001276340.1. [Q8K1M6-2]
NP_001263270.1. NM_001276341.1. [Q8K1M6-4]
NP_690029.2. NM_152816.3.
XP_006522694.1. XM_006522631.1. [Q8K1M6-1]
UniGeneMm.218820.

3D structure databases

ProteinModelPortalQ8K1M6.
SMRQ8K1M6. Positions 1-510, 648-735.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid216417. 6 interactions.
DIPDIP-54818N.
IntActQ8K1M6. 6 interactions.
MINTMINT-1858955.

Chemistry

ChEMBLCHEMBL2331072.

PTM databases

PhosphoSiteQ8K1M6.

Proteomic databases

MaxQBQ8K1M6.
PaxDbQ8K1M6.
PRIDEQ8K1M6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000023477; ENSMUSP00000023477; ENSMUSG00000022789. [Q8K1M6-3]
ENSMUST00000115749; ENSMUSP00000111415; ENSMUSG00000022789. [Q8K1M6-2]
GeneID74006.
KEGGmmu:74006.
UCSCuc007yij.1. mouse. [Q8K1M6-1]
uc007yik.1. mouse. [Q8K1M6-4]
uc007yim.1. mouse. [Q8K1M6-3]
uc007yin.1. mouse. [Q8K1M6-2]
uc007yio.1. mouse. [Q8K1M6-5]

Organism-specific databases

CTD10059.
MGIMGI:1921256. Dnm1l.

Phylogenomic databases

eggNOGCOG0699.
GeneTreeENSGT00740000115284.
HOGENOMHOG000161068.
HOVERGENHBG107833.
InParanoidQ8K1M6.
KOK17065.
OMASANTDMA.
OrthoDBEOG7GJ6CB.
PhylomeDBQ8K1M6.
TreeFamTF352031.

Gene expression databases

ArrayExpressQ8K1M6.
BgeeQ8K1M6.
CleanExMM_DNM1L.
GenevestigatorQ8K1M6.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000375. Dynamin_central.
IPR001401. Dynamin_GTPase.
IPR019762. Dynamin_GTPase_CS.
IPR022812. Dynamin_SF.
IPR003130. GED.
IPR020850. GTPase_effector_domain_GED.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11566. PTHR11566. 1 hit.
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]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00410. G_DYNAMIN_1. 1 hit.
PS51718. G_DYNAMIN_2. 1 hit.
PS51388. GED. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio339508.
PROQ8K1M6.
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: July 9, 2014
This is version 108 of the entry and version 2 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