dbPTM

DYN2_RAT - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DYN2_RAT
UniProt AC	P39052
Protein Name	Dynamin-2
Gene Name	Dnm2
Organism	Rattus norvegicus (Rat).
Sequence Length	870
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton . Cell junction . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . Cell junction, synapse . Midbody . Membrane, clathrin-coated pit . 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. [PubMed: 21210813 Plays an important role in vesicular trafficking processes, in particular endocytosis]
Protein Sequence	MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEYAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGRKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPTLRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELISTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESAEQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQNTSSHSPTPQRRPVSSVHPPGRPPAVRGPTPGPPLIPMPVGATSSFSAPPIPSRPGPQNVFANNDPFSAPPQIPSRPARIPPGIPPGVPSRRAPAAPSRPTIIRPAEPSLLD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
45	Phosphorylation	GGQSAGKSSVLENFV CCCCCCCHHHHHHHC	25.43	25403869
46	Phosphorylation	GQSAGKSSVLENFVG CCCCCCHHHHHHHCC	33.92	25403869
61	Phosphorylation	RDFLPRGSGIVTRRP CCCCCCCCCCCCCCC	26.99	25403869
111	Phosphorylation	ETDRVTGTNKGISPV HHCCCCCCCCCCCCC	25.13	18779572
116	Phosphorylation	TGTNKGISPVPINLR CCCCCCCCCCCCEEE	28.63	23984901
191	Acetylation	SDALKLAKEVDPQGL CHHHHHHHHCCCCHH	69.57	22902405
231	Phosphorylation	LLPLRRGYIGVVNRS CCCCCCCCEEEEECC	7.84	18779572
238	Phosphorylation	YIGVVNRSQKDIEGR CEEEEECCHHHCCCC	36.06	23984901
240	Acetylation	GVVNRSQKDIEGRKD EEEECCHHHCCCCHH	63.02	22902405
257	Acetylation	AALAAERKFFLSHPA HHHHHHHHHHHCCHH	31.79	44858149
295	Phosphorylation	HIRESLPTLRSKLQS HHHHHHHHHHHHHHH	39.85	30181290
299	Acetylation	SLPTLRSKLQSQLLS HHHHHHHHHHHHHHH	44.08	22902405
306	Phosphorylation	KLQSQLLSLEKEVEE HHHHHHHHHHHHHHH	42.97	27097102
562	Acetylation	DEEEKEKKYMLPLDN CHHHHHHCEEEECCC	36.66	72592201
581	Phosphorylation	DVEKGFMSNKHVFAI CHHHCCCCCCEEEEE	40.23	21373199
597	Phosphorylation	NTEQRNVYKDLRQIE EHHCCHHHHHHHHHH	11.44	21841817
598	Acetylation	TEQRNVYKDLRQIEL HHCCHHHHHHHHHHH	46.10	22902405
619	Phosphorylation	DVDSWKASFLRAGVY HHHHHHHHHHHCCCC	22.53	22673903
626	Phosphorylation	SFLRAGVYPEKDQAE HHHHCCCCCCCCCCC	12.54	25575281
642	Phosphorylation	EDGAQENTFSMDPQL CCCCCCCCCCCCHHH	19.14	25575281
644	Phosphorylation	GAQENTFSMDPQLER CCCCCCCCCCHHHHH	21.90	25575281
662	Phosphorylation	TIRNLVDSYVAIINK HHHHHHHHHHHHHCH	17.64	25575281
663	Phosphorylation	IRNLVDSYVAIINKS HHHHHHHHHHHHCHH	6.88	25575281
755	Phosphorylation	VPPPVDDTWLQNTSS CCCCCCCCCCCCCCC	24.50	28432305
760	Phosphorylation	DDTWLQNTSSHSPTP CCCCCCCCCCCCCCC	20.74	28432305
761	Phosphorylation	DTWLQNTSSHSPTPQ CCCCCCCCCCCCCCC	33.34	27097102
762	Phosphorylation	TWLQNTSSHSPTPQR CCCCCCCCCCCCCCC	26.41	27097102
764	Phosphorylation	LQNTSSHSPTPQRRP CCCCCCCCCCCCCCC	32.20	8308025
766	Phosphorylation	NTSSHSPTPQRRPVS CCCCCCCCCCCCCCC	34.76	27097102

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
231	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
597	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
764	S	Phosphorylation	Kinase	CDK1	P39951	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
764	S	Phosphorylation		21195118
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_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of DYN2_RAT !!

Drug and Disease Associations

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

Regulatory Network of DYN2_RAT

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphorylation of dynamin II at serine-764 is associated withcytokinesis."; Chircop M., Sarcevic B., Larsen M.R., Malladi C.S., Chau N.,Zavortink M., Smith C.M., Quan A., Anggono V., Hains P.G.,Graham M.E., Robinson P.J.; Biochim. Biophys. Acta 1813:1689-1699(2011). Cited for: PHOSPHORYLATION AT SER-764 BY CDK1, MUTAGENESIS OF SER-764, FUNCTION,AND SUBCELLULAR LOCATION.	21195118 [Abstract]

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