P39054 (DYN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Dynamin-2
EC=3.6.5.5

Alternative name(s):
Dynamin UDNM

Gene names

Name:	Dnm2
Synonyms:	Dyn2

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	870 AA.
Sequence status	Complete.
Protein existence	Evidence 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. Involved in cytokinesis. Ref.7
Catalytic activity	GTP + H2O = GDP + phosphate.
Subunit structure	Interacts with SHANK1, SHANK2 and NOSTRIN By similarity. Interacts with SNX9. Interacts with MYO1E (via SH3 domain) By similarity. Interacts with MYOF and SH3BP4. Ref.4 Ref.5
Subcellular location	Cytoplasm By similarity. Cytoplasm › cytoskeleton By similarity. Cell junction › synapse › postsynaptic cell membrane › postsynaptic density By similarity. Cell junction › synapse By similarity. Midbody By similarity. Note: Microtubule-associated. Also found in the postsynaptic density of neuronal cells By similarity.
Post-translational modification	Phosphorylation at Ser-764 by CDK1 is greatly increased upon mitotic entry. It regulates cytokinesis downstream of calcineurin, and does not affect clathrin-mediated endocytosis. Dephosphorylated by Calcineurin/PP2 By similarity.
Disruption phenotype	Exhibits growth and cytokinesis defects. Ref.7
Sequence similarities	Belongs to the dynamin family. Contains 1 GED domain. Contains 1 PH domain.

Ontologies

Keywords
Biological process	Endocytosis
Cellular component	Cell junction Cell membrane Cytoplasm Cytoskeleton Membrane Microtubule Postsynaptic cell membrane Synapse
Coding sequence diversity	Alternative splicing
Ligand	GTP-binding Nucleotide-binding
Molecular function	Hydrolase Motor protein
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	GTP catabolic process Inferred from electronic annotation. Source: GOC receptor-mediated endocytosis Inferred from electronic annotation. Source: Compara
Cellular_component	cell junction Inferred from electronic annotation. Source: UniProtKB-KW clathrin-coated endocytic vesicle Inferred from electronic annotation. Source: Compara microtubule Inferred from electronic annotation. Source: UniProtKB-KW midbody Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: Compara plasma membrane Inferred from electronic annotation. Source: UniProtKB-KW postsynaptic density Inferred from electronic annotation. Source: UniProtKB-SubCell postsynaptic membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW GTPase activity Inferred from electronic annotation. Source: InterPro phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cttn	Q60598	2	EBI-642337,EBI-397955
CTTN1	Q01406	2	EBI-642337,EBI-2530463	From a different organism.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P39054-1)

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: P39054-2)

The sequence of this isoform differs from the canonical sequence as follows:
     516-519: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 870	870	Dynamin-2		PRO_0000206571
Regions
	Domain	519 – 625	107	PH
	Domain	653 – 744	92	GED
	Nucleotide binding	38 – 45	8	GTP By similarity
	Nucleotide binding	136 – 140	5	GTP By similarity
	Nucleotide binding	205 – 208	4	GTP By similarity
	Compositional bias	747 – 866	120	Pro-rich
Amino acid modifications
	Modified residue	298	1	Phosphoserine Ref.6
	Modified residue	302	1	Phosphoserine Ref.6
	Modified residue	597	1	Phosphotyrosine Ref.6
	Modified residue	598	1	N6-acetyllysine By similarity
	Modified residue	764	1	Phosphoserine; by CDK1 By similarity
Natural variations
	Alternative sequence	516 – 519	4	Missing in isoform 2.		VSP_001326
Experimental info
	Sequence conflict	297 – 298	2	RS → HG in AAA40523. Ref.1
	Sequence conflict	848 – 870	23	SRRAP…PSLLD → RRPPPLAPARPFF in BAB23745. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 26, 2002. Version 2. Checksum: E80864AF94B8F778	FASTA	870	98,145
	10 20 30 40 50 60 MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 70 80 90 100 110 120 SGIVTRRPLI LQLIFSKTEY AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI 130 140 150 160 170 180 NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD 190 200 210 220 230 240 LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 250 260 270 280 290 300 DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPTLRSKL 310 320 330 340 350 360 QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA 370 380 390 400 410 420 RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL 430 440 450 460 470 480 KEPCLKCVDL VIQELISTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID 490 500 510 520 530 540 IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQGEILV IRRGWLTINN ISLMKGGSKE 550 560 570 580 590 600 YWFVLTAESL SWYKDEEEKE KKYMLPLDNL KIRDVEKGFM SNKHVFAIFN TEQRNVYKDL 610 620 630 640 650 660 RQIELACDSQ EDVDSWKASF LRAGVYPEKD QAENEDGAQE NTFSMDPQLE RQVETIRNLV 670 680 690 700 710 720 DSYVAIINKS IRDLMPKTIM HLMINNTKAF IHHELLAYLY SSADQSSLME ESAEQAQRRD 730 740 750 760 770 780 DMLRMYHALK EALNIIGDIS TSTVSTPVPP PVDDTWLQNT SGHSPTPQRR PVSSVHPPGR 790 800 810 820 830 840 PPAVRGPTPG PPLIPMPVGA TSSFSAPPIP SRPGPQSVFA NNDPFSAPPQ IPSRPARIPP 850 860 870 GIPPGVPSRR APAAPSRPTI IRPAEPSLLD
	Isoform 2 [UniParc]. Checksum: CA0BEB6FA5E5028D	FASTA	866	97,733
	10 20 30 40 50 60 MGNRGMEELI PLVNKLQDAF SSIGQSCHLD LPQIAVVGGQ SAGKSSVLEN FVGRDFLPRG 70 80 90 100 110 120 SGIVTRRPLI LQLIFSKTEY AEFLHCKSKK FTDFDEVRQE IEAETDRVTG TNKGISPVPI 130 140 150 160 170 180 NLRVYSPHVL NLTLIDLPGI TKVPVGDQPP DIEYQIKDMI LQFISRESSL ILAVTPANMD 190 200 210 220 230 240 LANSDALKLA KEVDPQGLRT IGVITKLDLM DEGTDARDVL ENKLLPLRRG YIGVVNRSQK 250 260 270 280 290 300 DIEGKKDIRA ALAAERKFFL SHPAYRHMAD RMGTPHLQKT LNQQLTNHIR ESLPTLRSKL 310 320 330 340 350 360 QSQLLSLEKE VEEYKNFRPD DPTRKTKALL QMVQQFGVDF EKRIEGSGDQ VDTLELSGGA 370 380 390 400 410 420 RINRIFHERF PFELVKMEFD EKDLRREISY AIKNIHGVRT GLFTPDLAFE AIVKKQVVKL 430 440 450 460 470 480 KEPCLKCVDL VIQELISTVR QCTSKLSSYP RLREETERIV TTYIREREGR TKDQILLLID 490 500 510 520 530 540 IEQSYINTNH EDFIGFANAQ QRSTQLNKKR AIPNQVIRRG WLTINNISLM KGGSKEYWFV 550 560 570 580 590 600 LTAESLSWYK DEEEKEKKYM LPLDNLKIRD VEKGFMSNKH VFAIFNTEQR NVYKDLRQIE 610 620 630 640 650 660 LACDSQEDVD SWKASFLRAG VYPEKDQAEN EDGAQENTFS MDPQLERQVE TIRNLVDSYV 670 680 690 700 710 720 AIINKSIRDL MPKTIMHLMI NNTKAFIHHE LLAYLYSSAD QSSLMEESAE QAQRRDDMLR 730 740 750 760 770 780 MYHALKEALN IIGDISTSTV STPVPPPVDD TWLQNTSGHS PTPQRRPVSS VHPPGRPPAV 790 800 810 820 830 840 RGPTPGPPLI PMPVGATSSF SAPPIPSRPG PQSVFANNDP FSAPPQIPSR PARIPPGIPP 850 860 GVPSRRAPAA PSRPTIIRPA EPSLLD

References

	« Hide 'large scale' referencesShow '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] (ISOFORM 2). Strain: NIH Swiss.
[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 1). Strain: C57BL/6J. Tissue: Liver.
[3]	Lubec G., Kang S.U. Submitted (APR-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 45-54; 91-107; 114-142; 207-217; 230-237; 300-309; 370-376 AND 678-688, MASS SPECTROMETRY. Strain: C57BL/6. Tissue: Brain.
[4]	"TTP specifically regulates the internalization of the transferrin receptor." Tosoni D., Puri C., Confalonieri S., Salcini A.E., De Camilli P., Tacchetti C., Di Fiore P.P. Cell 123:875-888(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SH3BP4.
[5]	"Myoferlin regulates vascular endothelial growth factor receptor-2 stability and function." Bernatchez P.N., Acevedo L., Fernandez-Hernando C., Murata T., Chalouni C., Kim J., Erdjument-Bromage H., Shah V., Gratton J.-P., McNally E.M., Tempst P., Sessa W.C. J. Biol. Chem. 282:30745-30753(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MYOF.
[6]	"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry." Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. J. Proteome Res. 6:250-262(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-302 AND TYR-597, MASS SPECTROMETRY. Tissue: Liver.
[7]	"Isoform and splice-variant specific functions of dynamin-2 revealed by analysis of conditional knock-out cells." Liu Y.W., Surka M.C., Schroeter T., Lukiyanchuk V., Schmid S.L. Mol. Biol. Cell 19:5347-5359(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	L31398 mRNA. Translation: AAA40523.1. AK005012 mRNA. Translation: BAB23745.1.
IPI	IPI00131445. IPI00314883.
RefSeq	NP_001240822.1. NM_001253893.1. NP_001240823.1. NM_001253894.1. NP_031897.2. NM_007871.2.
UniGene	Mm.433257.
3D structure databases
ProteinModelPortal	P39054.
SMR	P39054. Positions 5-737.
ModBase	Search...
Protein-protein interaction databases
IntAct	P39054. 9 interactions.
PTM databases
PhosphoSite	P39054.
2D gel databases
REPRODUCTION-2DPAGE	IPI00131445.
Proteomic databases
PaxDb	P39054.
PRIDE	P39054.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000091087; ENSMUSP00000088616; ENSMUSG00000033335. ENSMUST00000172482; ENSMUSP00000133564; ENSMUSG00000033335.
GeneID	13430.
KEGG	mmu:13430.
UCSC	uc009olk.1. mouse.
Organism-specific databases
CTD	1785.
MGI	MGI:109547. Dnm2.
Phylogenomic databases
eggNOG	COG0699.
GeneTree	ENSGT00690000101762.
HOGENOM	HOG000161069.
HOVERGEN	HBG107833.
InParanoid	P39054.
KO	K01528.
Gene expression databases
ArrayExpress	P39054.
Bgee	P39054.
CleanEx	MM_DNM2.
Genevestigator	P39054.
GermOnline	ENSMUSG00000033335. Mus musculus.
Family and domain databases
Gene3D	2.30.29.30. 1 hit.
InterPro	IPR027188. DNM2. IPR022812. 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]
PANTHER	PTHR11566. PTHR11566. 1 hit. PTHR11566:SF23. PTHR11566:SF23. 1 hit.
Pfam	PF01031. Dynamin_M. 1 hit. PF00350. Dynamin_N. 1 hit. PF02212. GED. 1 hit. PF00169. PH. 1 hit. [Graphical view]
PRINTS	PR00195. DYNAMIN.
SMART	SM00053. DYNc. 1 hit. SM00302. GED. 1 hit. SM00233. PH. 1 hit. [Graphical view]
PROSITE	PS00410. DYNAMIN. 1 hit. PS51388. GED. 1 hit. PS50003. PH_DOMAIN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	DNM2. mouse.
NextBio	283855.
SOURCE	Search...

Entry information

Entry name

DYN2_MOUSE

Accession

Primary (citable) accession number: P39054
Secondary accession number(s): Q9DBE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1995
Last sequence update:	July 26, 2002
Last modified:	May 1, 2013
This is version 123 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program