Q8K1M6 (DNM1L_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	742 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Functions in mitochondrial and peroxisomal division. Mediates membrane fission through oligomerization into ring-like structures which wrap around the scission site to constict and sever the mitochondrial membrane through a GTP hydrolysis-dependent mechanism. Required for normal brain development. Facilitates developmentally-regulated apoptosis during neural tube development. Required for a normal rate of cytochrome c release and caspase activation during apoptosis. Also required for mitochondrial fission during mitosis. Required for programmed necrosis execution. May be involved in vesicle transport By similarity. Ref.8
Catalytic activity	GTP + H2O = GDP + phosphate.
Subunit structure	Homotetramer; dimerizes through the N-terminal GTP-middle region of one molecule binding to the GED domain of another DNM1L molecule By similarity. Can self-assemble in multimeric ring-like structures. Interacts with BCL2L1; the interaction stimulates the GTPase activity of DMN1L in synapses and increases the number of axonal mitochondria and the size and number of synaptic vesicle clusters. Interacts with FIS1. Interacts with GSK3B and MARCH5. Interacts (via the GTPase and B domains) with UBE2I; the interaction promotes sumoylation of DNM1L, mainly in ite B domain. Interacts with PPP3CA; the interaction dephosphorylates DNM1L and regulates its transition to mitochondria By similarity. Interacts with MID49 and MID51 By similarity. Interacts with PGAM5; this interaction leads to dephosphorylation at Ser-643 and activation of GTPase activity and eventually to mitochondria fragmentation By similarity.
Subcellular location	Cytoplasm › cytosol By similarity. Golgi apparatus By similarity. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane; Peripheral membrane protein 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.
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	In embryonic fibroblasts, mice show defects in trophoblast giant cells and cardiomyocytes. Extensive mitochondrial networks are formed, and peroxisomes elongated. In brain, there are developmental defects in which Purkinje cells contained few giant mitochondria. In the forebrain, there is a decreased number of neurites and defective synapse formation. Embryos undergo developmentally-regulated apoptosis during neural tube formation. Mice die by around embryonic day 12. Ref.8
Sequence similarities	Belongs to the dynamin family. Contains 1 GED domain.

Ontologies

Keywords
Biological process	Necrosis
Cellular component	Cytoplasm Golgi apparatus Membrane Mitochondrion Mitochondrion outer membrane
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase
PTM	Glycoprotein Isopeptide bond Phosphoprotein S-nitrosylation Ubl conjugation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC mitochondrial fission Inferred from mutant phenotype PubMed 20038678. Source: MGI
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from electronic annotation. Source: UniProtKB-SubCell endomembrane system Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrial outer membrane Inferred from direct assay PubMed 21149567. Source: MGI
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Lrrk2	Q5S006	3	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 742	742	Dynamin-1-like protein		PRO_0000206567
Regions
	Domain	650 – 741	92	GED
	Nucleotide binding	32 – 39	8	GTP By similarity
	Nucleotide binding	152 – 156	5	GTP By similarity
	Nucleotide binding	221 – 224	4	GTP By similarity
	Region	1 – 349	349	GTPase domain By similarity
	Region	1 – 349	349	N-terminal dimerization domain By similarity
	Region	350 – 495	146	Middle domain By similarity
	Region	454 – 691	238	Interaction with GSK3B By similarity
	Region	454 – 654	201	Interaction with GSK3B By similarity
	Region	508 – 575	68	B domain By similarity
	Region	548 – 742	195	C-terminal dimerization domain By similarity
Amino acid modifications
	Modified residue	535	1	Phosphoserine Ref.7
	Modified residue	613	1	Phosphoserine By similarity
	Modified residue	622	1	Phosphoserine; by CDK1 By similarity
	Modified residue	643	1	Phosphoserine; by CAMK1 and PKA By similarity
	Modified residue	650	1	S-nitrosocysteine By similarity
	Glycosylation	591	1	O-linked (GlcNAc...) By similarity
	Glycosylation	592	1	O-linked (GlcNAc...) By similarity
	Cross-link	538		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	541		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	564		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	574		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	600		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	603		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	612		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
	Cross-link	614		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Natural variations
	Alternative sequence	1 – 104	104	Missing in isoform 4.		VSP_013689
	Alternative sequence	85 – 90	6	Missing in isoform 3 and isoform 5.		VSP_013690
	Alternative sequence	105	1	K → M in isoform 4.		VSP_013691
	Alternative sequence	214 – 227	14	RRTLA…LDLMD → KGRCLYLMDVDLQW in isoform 5.		VSP_013692
	Alternative sequence	228 – 742	515	Missing in isoform 5.		VSP_013693
	Alternative sequence	539 – 575	37	Missing in isoform 3.		VSP_013694
	Alternative sequence	539 – 564	26	Missing in isoform 2 and isoform 4.		VSP_013695
Experimental info
	Sequence conflict	165	1	P → L in BAC06576. Ref.1
	Sequence conflict	320	1	Q → R in BAC06576. Ref.1
	Sequence conflict	519	1	E → A in BAC34640. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 10, 2005. Version 2. Checksum: 5A8679B61A444847	FASTA	742	82,658
	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
	Isoform 2 [UniParc]. Checksum: 3C922A7A135B9A37	FASTA	716	80,212
	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 PSAGSRDKLI 550 560 570 580 590 600 QDNRRETKNV PSAGGGIGDG GQEPTTGNWR GMLKTSKAEE LLAEEKSKPI PIMPASPQKG 610 620 630 640 650 660 HAVNLLDVPV PVARKLSARE QRDCEVIERL IKSYFLIVRK NIQDSVPKAV MHFLVNHVKD 670 680 690 700 710 TLQSELVGQL YKSSLLDDLL TESEDMAQRR KEAADMLKAL QGASQIIAEI RETHLW
	Isoform 3 [UniParc]. Checksum: 68ED85D93914B4DC	FASTA	699	78,011
	10 20 30 40 50 60 MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGVVTR 70 80 90 100 110 120 RPLILQLVHV SPEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 130 140 150 160 170 180 NNKGVSPEPI HLKVFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 190 200 210 220 230 240 ILAVTAANTD MATSEALKIS REVDPDGRRT LAVITKLDLM DAGTDAMDVL MGRVIPVKLG 250 260 270 280 290 300 IIGVVNRSQL DINNKKSVTD SIRDEYAFLQ KKYPSLANRN GTKYLARTLN RLLMHHIRDC 310 320 330 340 350 360 LPELKTRINV LAAQYQSLLN SYGEPVDDKS ATLLQLITKF ATEYCNTIEG TAKYIETSEL 370 380 390 400 410 420 CGGARICYIF HETFGRTLES VDPLGGLNTI DILTAIRNAT GPRPALFVPE VSFELLVKRQ 430 440 450 460 470 480 IKRLEEPSLR CVELVHEEMQ RIIQHCSNYS TQELLRFPKL HDAIVEVVTC LLRKRLPVTN 490 500 510 520 530 540 EMVHNLVAIE LAYINTKHPD FADACGLMNN NIEEQRRNRL ARELPSAGSR DKVPSAGGGI 550 560 570 580 590 600 GDGGQEPTTG NWRGMLKTSK AEELLAEEKS KPIPIMPASP QKGHAVNLLD VPVPVARKLS 610 620 630 640 650 660 AREQRDCEVI ERLIKSYFLI VRKNIQDSVP KAVMHFLVNH VKDTLQSELV GQLYKSSLLD 670 680 690 DLLTESEDMA QRRKEAADML KALQGASQII AEIRETHLW
	Isoform 4 [UniParc]. Checksum: C5D0BCE4B4622502	FASTA	612	68,701
	10 20 30 40 50 60 MLYTDFDEIR QEIENETERI SGNNKGVSPE PIHLKVFSPN VVNLTLVDLP GMTKVPVGDQ 70 80 90 100 110 120 PKDIELQIRE LILRFISNPN SIILAVTAAN TDMATSEALK ISREVDPDGR RTLAVITKLD 130 140 150 160 170 180 LMDAGTDAMD VLMGRVIPVK LGIIGVVNRS QLDINNKKSV TDSIRDEYAF LQKKYPSLAN 190 200 210 220 230 240 RNGTKYLART LNRLLMHHIR DCLPELKTRI NVLAAQYQSL LNSYGEPVDD KSATLLQLIT 250 260 270 280 290 300 KFATEYCNTI EGTAKYIETS ELCGGARICY IFHETFGRTL ESVDPLGGLN TIDILTAIRN 310 320 330 340 350 360 ATGPRPALFV PEVSFELLVK RQIKRLEEPS LRCVELVHEE MQRIIQHCSN YSTQELLRFP 370 380 390 400 410 420 KLHDAIVEVV TCLLRKRLPV TNEMVHNLVA IELAYINTKH PDFADACGLM NNNIEEQRRN 430 440 450 460 470 480 RLARELPSAG SRDKLIQDNR RETKNVPSAG GGIGDGGQEP TTGNWRGMLK TSKAEELLAE 490 500 510 520 530 540 EKSKPIPIMP ASPQKGHAVN LLDVPVPVAR KLSAREQRDC EVIERLIKSY FLIVRKNIQD 550 560 570 580 590 600 SVPKAVMHFL VNHVKDTLQS ELVGQLYKSS LLDDLLTESE DMAQRRKEAA DMLKALQGAS 610 QIIAEIRETH LW
	Isoform 5 [UniParc]. Checksum: 29C66A3A04924F55	FASTA	221	24,488
	10 20 30 40 50 60 MEALIPVINK LQDVFNTVGA DIIQLPQIVV VGTQSSGKSS VLESLVGRDL LPRGTGVVTR 70 80 90 100 110 120 RPLILQLVHV SPEDKRKTTG EENGVEAEEW GKFLHTKNKL YTDFDEIRQE IENETERISG 130 140 150 160 170 180 NNKGVSPEPI HLKVFSPNVV NLTLVDLPGM TKVPVGDQPK DIELQIRELI LRFISNPNSI 190 200 210 220 ILAVTAANTD MATSEALKIS REVDPDGKGR CLYLMDVDLQ W

References

	« Hide 'large scale' referencesShow '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. , 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, 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]	"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-535, MASS SPECTROMETRY. Tissue: Melanoma.
[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.
+	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.
IPI	IPI00172221. IPI00471349. IPI00556723. IPI00556781. IPI00556857.
RefSeq	NP_001021118.1. NM_001025947.2. NP_001263269.1. NM_001276340.1. NP_001263270.1. NM_001276341.1.
UniGene	Mm.218820.
3D structure databases
ProteinModelPortal	Q8K1M6.
SMR	Q8K1M6. Positions 1-507, 647-734.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q8K1M6. 2 interactions.
PTM databases
PhosphoSite	Q8K1M6.
Proteomic databases
PaxDb	Q8K1M6.
PRIDE	Q8K1M6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000023477; ENSMUSP00000023477; ENSMUSG00000022789. ENSMUST00000115749; ENSMUSP00000111415; ENSMUSG00000022789.
GeneID	74006.
KEGG	mmu:74006.
UCSC	uc007yik.1. mouse. uc007yil.1. mouse. uc007yin.1. mouse. uc007yio.1. mouse.
Organism-specific databases
CTD	10059.
MGI	MGI:1921256. Dnm1l.
Phylogenomic databases
eggNOG	COG0699.
GeneTree	ENSGT00690000102205.
HOGENOM	HOG000161068.
HOVERGEN	HBG107833.
InParanoid	Q8K1M6.
KO	K01528.
OMA	ENDPATW.
OrthoDB	EOG4SN1N7.
Gene expression databases
ArrayExpress	Q8K1M6.
Bgee	Q8K1M6.
CleanEx	MM_DNM1L.
Genevestigator	Q8K1M6.
GermOnline	ENSMUSG00000022789. Mus musculus.
Family and domain databases
InterPro	IPR022812. Dynamin. IPR000375. Dynamin_central. IPR001401. Dynamin_GTPase. IPR019762. Dynamin_GTPase_CS. IPR003130. GED. IPR020850. GTPase_effector_domain_GED. [Graphical view]
PANTHER	PTHR11566. PTHR11566. 1 hit.
Pfam	PF01031. Dynamin_M. 1 hit. PF00350. Dynamin_N. 1 hit. PF02212. GED. 1 hit. [Graphical view]
PRINTS	PR00195. DYNAMIN.
SMART	SM00053. DYNc. 1 hit. SM00302. GED. 1 hit. [Graphical view]
PROSITE	PS00410. DYNAMIN. 1 hit. PS51388. GED. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	339508.
SOURCE	Search...

Entry information

Entry name

DNM1L_MOUSE

Accession

Primary (citable) accession number: Q8K1M6
Secondary accession number(s): Q8BNQ5 , Q8BQ64, Q8CGD0, Q8K1A1

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 10, 2005
Last sequence update:	May 10, 2005
Last modified:	May 1, 2013
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program