dbPTM

DYN2_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DYN2_MOUSE
UniProt AC	P39054
Protein Name	Dynamin-2
Gene Name	Dnm2
Organism	Mus musculus (Mouse).
Sequence Length	870
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton . Cell junction . Membrane, clathrin-coated pit . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell junction, synapse . Midbody . Cell projection, phagocytic cup . Cytoplasmic vesicle, phag
Protein Description	Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones (By similarity). Plays an important role in vesicular trafficking processes, in particular endocytosis. Involved in cytokinesis. [PubMed: 18923138 Regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane]
Protein Sequence	MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPTLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQNTSGHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQSVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
45	Phosphorylation	GGQSAGKSSVLENFV CCCCCCCHHHHHHHC	25.43	25521595
46	Phosphorylation	GQSAGKSSVLENFVG CCCCCCHHHHHHHCC	33.92	25521595
61	Phosphorylation	RDFLPRGSGIVTRRP CCCCCCCCCCCCCCC	26.99	29899451
80	Phosphorylation	LIFSKTEYAEFLHCK HHHCCCCHHHHHHCC	19.36	-
111	Phosphorylation	ETDRVTGTNKGISPV HHCCCCCCCCCCCCC	25.13	18779572
125	Phosphorylation	VPINLRVYSPHVLNL CCCEEEEECCEEEEE	15.28	18034455
200	Phosphorylation	VDPQGLRTIGVITKL CCCCHHEEEEEEEEH	27.42	20531401
206	Ubiquitination	RTIGVITKLDLMDEG EEEEEEEEHHHCCCC	28.95	-
223	Ubiquitination	ARDVLENKLLPLRRG HHHHHHHCCCCCCCC	41.86	-
231	Phosphorylation	LLPLRRGYIGVVNRS CCCCCCCCEEEECCC	7.84	18779572
238	Phosphorylation	YIGVVNRSQKDIEGK CEEEECCCHHHCCCH	36.06	22817900
257	Ubiquitination	AALAAERKFFLSHPA HHHHHHHHHHHCCHH	31.79	-
298	Phosphorylation	ESLPTLRSKLQSQLL HHHHHHHHHHHHHHH	40.61	17203969
299	Acetylation	SLPTLRSKLQSQLLS HHHHHHHHHHHHHHH	44.08	23806337
302	Phosphorylation	TLRSKLQSQLLSLEK HHHHHHHHHHHHHHH	32.98	17203969
306	Phosphorylation	KLQSQLLSLEKEVEE HHHHHHHHHHHHHHH	42.97	29899451
353	Phosphorylation	GSGDQVDTLELSGGA CCCCCCEEEEECCCC	24.23	21183079
376	Ubiquitination	RFPFELVKMEFDEKD CCCHHHEEEECCHHH	45.39	-
393	Ubiquitination	REISYAIKNIHGVRT HHHHHHHHHHHCCCC	41.50	-
443	Phosphorylation	ISTVRQCTSKLSSYP HHHHHHHHHHHHCCH	22.13	26643407
447	Phosphorylation	RQCTSKLSSYPRLRE HHHHHHHHCCHHHHH	31.40	26643407
448	Phosphorylation	QCTSKLSSYPRLREE HHHHHHHCCHHHHHH	49.98	26643407
463	Phosphorylation	TERIVTTYIREREGR HHHHHHHHHHHCCCC	6.66	-
527	Phosphorylation	VIRRGWLTINNISLM EEECCEEEEEEEEEE	18.36	22802335
532	Phosphorylation	WLTINNISLMKGGSK EEEEEEEEEECCCCE	25.24	22802335
562	Malonylation	DEEEKEKKYMLPLDN CHHHHHHCEEEECCC	36.66	26320211
583	Acetylation	EKGFMSNKHVFAIFN HHCCCCCCEEEEEEE	33.56	7713289
597	Phosphorylation	NTEQRNVYKDLRQIE EHHCCHHHHHHHHHH	11.44	21411625
598	Malonylation	TEQRNVYKDLRQIEL HHCCHHHHHHHHHHH	46.10	26320211
598	Acetylation	TEQRNVYKDLRQIEL HHCCHHHHHHHHHHH	46.10	-
619	Phosphorylation	DVDSWKASFLRAGVY HHHHHHHHHHHCCCC	22.53	24704852
626	Phosphorylation	SFLRAGVYPEKDQAE HHHHCCCCCCCCCCC	12.54	-
642	Phosphorylation	EDGAQENTFSMDPQL CCCCCCCCCCCCHHH	19.14	23140645
644	Phosphorylation	GAQENTFSMDPQLER CCCCCCCCCCHHHHH	21.90	23140645
669	Ubiquitination	SYVAIINKSIRDLMP HHHHHHCHHHHHHCC	36.53	-
740	Phosphorylation	LNIIGDISTSTVSTP HHHHHCCCCCCCCCC	22.50	25159016
741	Phosphorylation	NIIGDISTSTVSTPV HHHHCCCCCCCCCCC	28.84	25159016
742	Phosphorylation	IIGDISTSTVSTPVP HHHCCCCCCCCCCCC	21.74	25159016
743	Phosphorylation	IGDISTSTVSTPVPP HHCCCCCCCCCCCCC	20.68	25159016
745	Phosphorylation	DISTSTVSTPVPPPV CCCCCCCCCCCCCCC	27.38	25159016
746	Phosphorylation	ISTSTVSTPVPPPVD CCCCCCCCCCCCCCC	24.78	26160508
755	Phosphorylation	VPPPVDDTWLQNTSG CCCCCCCCCCCCCCC	24.50	26239621
760	Phosphorylation	DDTWLQNTSGHSPTP CCCCCCCCCCCCCCC	24.11	26239621
761	Phosphorylation	DTWLQNTSGHSPTPQ CCCCCCCCCCCCCCC	41.90	22942356
764	Phosphorylation	LQNTSGHSPTPQRRP CCCCCCCCCCCCCCC	33.71	27087446
766	Phosphorylation	NTSGHSPTPQRRPVS CCCCCCCCCCCCCCC	34.76	22942356
856	Phosphorylation	RRAPAAPSRPTIIRP CCCCCCCCCCCEECC	46.28	22817900

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
764	S	Phosphorylation	Kinase	CDK1	P11440	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
764	S	Phosphorylation		-
Phosphorylation at Ser-764 by CDK1 is greatly increased upon mitotic entry.

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of DYN2_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DYN2_MOUSE !!

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DYN2_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry."; Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.; J. Proteome Res. 6:250-262(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298; SER-302 ANDTYR-597, AND MASS SPECTROMETRY.	17203969 [Abstract]

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