dbPTM

DYN1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	DYN1_HUMAN
UniProt AC	Q05193
Protein Name	Dynamin-1
Gene Name	DNM1
Organism	Homo sapiens (Human).
Sequence Length	864
Subcellular Localization	Cytoplasm . Cytoplasm, cytoskeleton . Microtubule-associated.
Protein Description	Microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. Involved in receptor-mediated endocytosis..
Protein Sequence	MGNRGMEDLIPLVNRLQDAFSAIGQNADLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLVLQLVNATTEYAEFLHCKGKKFTDFEEVRLEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLVDLPGMTKVPVGDQPPDIEFQIRDMLMQFVTKENCLILAVSPANSDLANSDALKVAKEVDPQGQRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIDGKKDITAALAAERKFFLSHPSYRHLADRMGTPYLQKVLNQQLTNHIRDTLPGLRNKLQSQLLSIEKEVEEYKNFRPDDPARKTKALLQMVQQFAVDFEKRIEGSGDQIDTYELSGGARINRIFHERFPFELVKMEFDEKELRREISYAIKNIHGIRTGLFTPDMAFETIVKKQVKKIREPCLKCVDMVISELISTVRQCTKKLQQYPRLREEMERIVTTHIREREGRTKEQVMLLIDIELAYMNTNHEDFIGFANAQQRSNQMNKKKTSGNQDEILVIRKGWLTINNIGIMKGGSKEYWFVLTAENLSWYKDDEEKEKKYMLSVDNLKLRDVEKGFMSSKHIFALFNTEQRNVYKDYRQLELACETQEEVDSWKASFLRAGVYPERVGDKEKASETEENGSDSFMHSMDPQLERQVETIRNLVDSYMAIVNKTVRDLMPKTIMHLMINNTKEFIFSELLANLYSCGDQNTLMEESAEQAQRRDEMLRMYHALKEALSIIGDINTTTVSTPMPPPVDDSWLQVQSVPAGRRSPTSSPTPQRRAPAVPPARPGSRGPAPGPPPAGSALGGAPPVPSRPGASPDPFGPPPQVPSRPNRAPPGVPSRSGQASPSRPESPRPPFDL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
45	Phosphorylation	GGQSAGKSSVLENFV CCCCCCCHHHHHHHC	25.43	25332170
46	Phosphorylation	GQSAGKSSVLENFVG CCCCCCHHHHHHHCC	33.92	21712546
61	Phosphorylation	RDFLPRGSGIVTRRP CCCCCCCCCCCCCCC	26.99	24719451
80	Phosphorylation	LVNATTEYAEFLHCK HHHCCHHHHHHHCCC	14.89	21082442
116	Phosphorylation	TGTNKGISPVPINLR CCCCCCCCCCCEEEE	28.63	27067055
125	Nitrated tyrosine	VPINLRVYSPHVLNL CCEEEEEECCEEEEE	15.28	-
125	Phosphorylation	VPINLRVYSPHVLNL CCEEEEEECCEEEEE	15.28	21082442
125	Nitration	VPINLRVYSPHVLNL CCEEEEEECCEEEEE	15.28	-
126	Phosphorylation	PINLRVYSPHVLNLT CEEEEEECCEEEEEE	12.98	-
206 (in isoform 5)	Ubiquitination	-	28.95	21890473
206	Ubiquitination	RTIGVITKLDLMDEG EEEEEEEEHHHCCCC	28.95	-
206 (in isoform 3)	Ubiquitination	-	28.95	21890473
206 (in isoform 1)	Ubiquitination	-	28.95	21890473
206 (in isoform 2)	Ubiquitination	-	28.95	21890473
214	Phosphorylation	LDLMDEGTDARDVLE HHHCCCCCCHHHHHH	25.16	-
217	Methylation	MDEGTDARDVLENKL CCCCCCHHHHHHHCC	37.06	-
223	Ubiquitination	ARDVLENKLLPLRRG HHHHHHHCCCCCCCC	41.86	-
223 (in isoform 1)	Ubiquitination	-	41.86	21890473
223 (in isoform 2)	Ubiquitination	-	41.86	21890473
223 (in isoform 3)	Ubiquitination	-	41.86	21890473
223 (in isoform 5)	Ubiquitination	-	41.86	21890473
231	Phosphorylation	LLPLRRGYIGVVNRS CCCCCCCCEEEEECC	7.84	21411625
257	Ubiquitination	AALAAERKFFLSHPS HHHHHHHHHHHCCHH	31.79	-
261	Phosphorylation	AERKFFLSHPSYRHL HHHHHHHCCHHHHHH	28.35	24719451
264	Phosphorylation	KFFLSHPSYRHLADR HHHHCCHHHHHHHHH	29.40	24719451
271	Methylation	SYRHLADRMGTPYLQ HHHHHHHHCCCHHHH	21.59	-
274	Phosphorylation	HLADRMGTPYLQKVL HHHHHCCCHHHHHHH	10.22	27067055
276	Phosphorylation	ADRMGTPYLQKVLNQ HHHCCCHHHHHHHHH	22.92	27067055
286	Phosphorylation	KVLNQQLTNHIRDTL HHHHHHHHHHHHHHC	22.03	-
302	Phosphorylation	GLRNKLQSQLLSIEK HHHHHHHHHHHHHHH	32.98	24300666
306	Phosphorylation	KLQSQLLSIEKEVEE HHHHHHHHHHHHHHH	36.98	24300666
347	Phosphorylation	FEKRIEGSGDQIDTY HHHHCCCCCCCCEEE	26.80	17376771
353	Phosphorylation	GSGDQIDTYELSGGA CCCCCCEEEEECCCC	22.11	21945579
354	Phosphorylation	SGDQIDTYELSGGAR CCCCCEEEEECCCCC	15.89	21945579
357	Phosphorylation	QIDTYELSGGARINR CCEEEEECCCCCCHH	24.20	21945579
376	Sumoylation	RFPFELVKMEFDEKE CCCHHHEECCCCHHH	45.39	-
376	Ubiquitination	RFPFELVKMEFDEKE CCCHHHEECCCCHHH	45.39	-
389	Phosphorylation	KELRREISYAIKNIH HHHHHHHHHHHHHHH	12.08	28102081
390	Phosphorylation	ELRREISYAIKNIHG HHHHHHHHHHHHHHC	20.29	28102081
404	Phosphorylation	GIRTGLFTPDMAFET CCCCCCCCCCHHHHH	24.34	24076635
404 (in isoform 5)	Phosphorylation	-	24.34	24076635
404 (in isoform 2)	Phosphorylation	-	24.34	24076635
411	Phosphorylation	TPDMAFETIVKKQVK CCCHHHHHHHHHHHH	25.31	18491316
433	Phosphorylation	KCVDMVISELISTVR HHHHHHHHHHHHHHH	18.23	29083192
437	Phosphorylation	MVISELISTVRQCTK HHHHHHHHHHHHHHH	33.21	29083192
438	Phosphorylation	VISELISTVRQCTKK HHHHHHHHHHHHHHH	16.83	29083192
443	Phosphorylation	ISTVRQCTKKLQQYP HHHHHHHHHHHHHCH	23.91	29083192
511	Phosphorylation	NQMNKKKTSGNQDEI HHHCCCCCCCCCCCE	51.23	29214152
512	Phosphorylation	QMNKKKTSGNQDEIL HHCCCCCCCCCCCEE	44.63	17376771
523	Ubiquitination	DEILVIRKGWLTINN CCEEEEECCEEEEEC	43.23	2190698
523 (in isoform 5)	Ubiquitination	-	43.23	21890473
523 (in isoform 1)	Ubiquitination	-	43.23	21890473
523 (in isoform 2)	Ubiquitination	-	43.23	21890473
523 (in isoform 3)	Ubiquitination	-	43.23	21890473
562	Malonylation	DDEEKEKKYMLSVDN CHHHHHHHEEEEEEC	36.66	26320211
563	Phosphorylation	DEEKEKKYMLSVDNL HHHHHHHEEEEEECC	17.85	27196784
597	Phosphorylation	NTEQRNVYKDYRQLE CHHHCHHHHHHHHHH	11.16	9880482
598	Acetylation	TEQRNVYKDYRQLEL HHHCHHHHHHHHHHH	43.96	19608861
619	Phosphorylation	EVDSWKASFLRAGVY HHHHHHHHHHHHCCC	22.53	29496963
646	Phosphorylation	TEENGSDSFMHSMDP CCCCCCCCHHHHCCH	26.60	28555341
650	Phosphorylation	GSDSFMHSMDPQLER CCCCHHHHCCHHHHH	17.06	28555341
668	Phosphorylation	TIRNLVDSYMAIVNK HHHHHHHHHHHHHCH	14.88	-
669	Phosphorylation	IRNLVDSYMAIVNKT HHHHHHHHHHHHCHH	6.01	-
684	O-linked_Glycosylation	VRDLMPKTIMHLMIN HHHHCCHHHHHHHCC	20.05	30379171
684	Phosphorylation	VRDLMPKTIMHLMIN HHHHCCHHHHHHHCC	20.05	29255136
693	Phosphorylation	MHLMINNTKEFIFSE HHHHCCCCHHHHHHH	27.71	29255136
732	Phosphorylation	RDEMLRMYHALKEAL HHHHHHHHHHHHHHH	4.22	-
774	Phosphorylation	SVPAGRRSPTSSPTP CCCCCCCCCCCCCCC	31.04	22167270
776	Phosphorylation	PAGRRSPTSSPTPQR CCCCCCCCCCCCCCC	42.98	30266825
777	Phosphorylation	AGRRSPTSSPTPQRR CCCCCCCCCCCCCCC	37.39	30266825
778	Phosphorylation	GRRSPTSSPTPQRRA CCCCCCCCCCCCCCC	34.96	22167270
780	Phosphorylation	RSPTSSPTPQRRAPA CCCCCCCCCCCCCCC	33.72	21955146
795	Phosphorylation	VPPARPGSRGPAPGP CCCCCCCCCCCCCCC	36.43	10766777
796	Methylation	PPARPGSRGPAPGPP CCCCCCCCCCCCCCC	62.11	-
807	Phosphorylation	PGPPPAGSALGGAPP CCCCCCCCCCCCCCC	23.56	25002506
817	Phosphorylation	GGAPPVPSRPGASPD CCCCCCCCCCCCCCC	51.87	29978859
822	Phosphorylation	VPSRPGASPDPFGPP CCCCCCCCCCCCCCC	35.43	30206219
834	Phosphorylation	GPPPQVPSRPNRAPP CCCCCCCCCCCCCCC	62.61	29978859
847	Phosphorylation	PPGVPSRSGQASPSR CCCCCCCCCCCCCCC	39.33	23312004
851	Phosphorylation	PSRSGQASPSRPESP CCCCCCCCCCCCCCC	18.60	17376771
853	Phosphorylation	RSGQASPSRPESPRP CCCCCCCCCCCCCCC	58.95	24076635
857	Phosphorylation	ASPSRPESPRPPFDL CCCCCCCCCCCCCCC	28.97	17376771

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
774	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
774	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
778	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
778	S	Phosphorylation	Kinase	CDK-FAMILY	-	GPS
778	S	Phosphorylation	Kinase	CDK_GROUP	-	PhosphoELM
780	T	Phosphorylation	Kinase	CDK5	Q00535	PSP
795	S	Phosphorylation	Kinase	PRKCA	P05696	GPS
857	S	Phosphorylation	Kinase	DYR1A	Q13627	PhosphoELM

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of DYN1_HUMAN !!

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 DYN1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FNBP1_HUMAN	FNBP1	physical	15252009
PACN1_HUMAN	PACSIN1	physical	15252009
ASB13_HUMAN	ASB13	physical	16169070
PIN4_HUMAN	PIN4	physical	16169070
MED31_HUMAN	MED31	physical	16169070
CE126_HUMAN	KIAA1377	physical	16169070
AMPH_HUMAN	AMPH	physical	9341169
SH3G2_HUMAN	SH3GL2	physical	9341169
AMPH_HUMAN	AMPH	physical	11877424
DYN1_HUMAN	DNM1	physical	7634088
DYR1A_HUMAN	DYRK1A	physical	19722700
DYR1A_RAT	Dyrk1a	physical	15287745
AMPH_HUMAN	AMPH	physical	15834155
SH3G2_HUMAN	SH3GL2	physical	15834155
ITSN1_HUMAN	ITSN1	physical	15834155
SRC_HUMAN	SRC	physical	15834155
GRB2_HUMAN	GRB2	physical	15834155
ITSN1_HUMAN	ITSN1	physical	18539136
FAK2_HUMAN	PTK2B	physical	19380485
SRC_HUMAN	SRC	physical	19380485
SUMO1_HUMAN	SUMO1	physical	15123615
PIAS1_HUMAN	PIAS1	physical	15123615
UBC9_HUMAN	UBE2I	physical	15123615
DYN1_HUMAN	DNM1	physical	15123615
SH3B4_HUMAN	SH3BP4	physical	16325581
NCK2_HUMAN	NCK2	physical	11557983
NCK1_HUMAN	NCK1	physical	11557983
SNX9_HUMAN	SNX9	physical	15703209
I2BPL_HUMAN	IRF2BPL	physical	22863883
NUCL_HUMAN	NCL	physical	22863883
NPM3_HUMAN	NPM3	physical	22863883
RU2A_HUMAN	SNRPA1	physical	22863883
TBD2A_HUMAN	TBC1D2	physical	22863883
AMPH_HUMAN	AMPH	physical	17244534
SLA1_YEAST	SLA1	physical	17244534
GRB2_HUMAN	GRB2	physical	17244534
BIN1_HUMAN	BIN1	physical	16275660
RPE_HUMAN	RPE	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
616346	Epileptic encephalopathy, early infantile, 31 (EIEE31)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of DYN1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-774; THR-776 ANDSER-778, AND MASS SPECTROMETRY.	18088087 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-354, AND MASSSPECTROMETRY.	15592455 [Abstract]