DYN2_HUMAN - dbPTM
DYN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DYN2_HUMAN
UniProt AC P50570
Protein Name Dynamin-2
Gene Name DNM2
Organism Homo sapiens (Human).
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, phagosome
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: 12498685 Regulates maturation of apoptotic cell corpse-containing phagosomes by recruiting PIK3C3 to the phagosome membrane (By similarity]
Protein Sequence MGNRGMEELIPLVNKLQDAFSSIGQSCHLDLPQIAVVGGQSAGKSSVLENFVGRDFLPRGSGIVTRRPLILQLIFSKTEHAEFLHCKSKKFTDFDEVRQEIEAETDRVTGTNKGISPVPINLRVYSPHVLNLTLIDLPGITKVPVGDQPPDIEYQIKDMILQFISRESSLILAVTPANMDLANSDALKLAKEVDPQGLRTIGVITKLDLMDEGTDARDVLENKLLPLRRGYIGVVNRSQKDIEGKKDIRAALAAERKFFLSHPAYRHMADRMGTPHLQKTLNQQLTNHIRESLPALRSKLQSQLLSLEKEVEEYKNFRPDDPTRKTKALLQMVQQFGVDFEKRIEGSGDQVDTLELSGGARINRIFHERFPFELVKMEFDEKDLRREISYAIKNIHGVRTGLFTPDLAFEAIVKKQVVKLKEPCLKCVDLVIQELINTVRQCTSKLSSYPRLREETERIVTTYIREREGRTKDQILLLIDIEQSYINTNHEDFIGFANAQQRSTQLNKKRAIPNQGEILVIRRGWLTINNISLMKGGSKEYWFVLTAESLSWYKDEEEKEKKYMLPLDNLKIRDVEKGFMSNKHVFAIFNTEQRNVYKDLRQIELACDSQEDVDSWKASFLRAGVYPEKDQAENEDGAQENTFSMDPQLERQVETIRNLVDSYVAIINKSIRDLMPKTIMHLMINNTKAFIHHELLAYLYSSADQSSLMEESADQAQRRDDMLRMYHALKEALNIIGDISTSTVSTPVPPPVDDTWLQSASSHSPTPQRRPVSSIHPPGRPPAVRGPTPGPPLIPVPVGAAASFSAPPIPSRPGPQSVFANSDLFPAPPQIPSRPVRIPPGIPPGVPSRRPPAAPSRPTIIRPAEPSLLD
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
6Sulfoxidation--MGNRGMEELIPLV
--CCCCHHHHHHHHH		3.0621406390
21PhosphorylationNKLQDAFSSIGQSCH
HHHHHHHHHHHCCCC		23.8324043423
22PhosphorylationKLQDAFSSIGQSCHL
HHHHHHHHHHCCCCC		25.0424043423
26PhosphorylationAFSSIGQSCHLDLPQ
HHHHHHCCCCCCCCE		9.7824043423
27S-nitrosocysteineFSSIGQSCHLDLPQI
HHHHHCCCCCCCCEE		2.58-
27S-nitrosylationFSSIGQSCHLDLPQI
HHHHHCCCCCCCCEE		2.5822178444
41PhosphorylationIAVVGGQSAGKSSVL
EEEECCCCCCCHHHH		42.1124043423
45PhosphorylationGGQSAGKSSVLENFV
CCCCCCCHHHHHHHC		25.4325332170
46PhosphorylationGQSAGKSSVLENFVG
CCCCCCHHHHHHHCC		33.9221712546
61PhosphorylationRDFLPRGSGIVTRRP
CCCCCCCCCCCCCCC		26.9924719451
76PhosphorylationLILQLIFSKTEHAEF
HHHHHHHCCCCCCCH		31.5124719451
86S-nitrosocysteineEHAEFLHCKSKKFTD
CCCCHHHCCCCCCCC		6.07-
86S-nitrosylationEHAEFLHCKSKKFTD
CCCCHHHCCCCCCCC		6.0722178444
87AcetylationHAEFLHCKSKKFTDF
CCCHHHCCCCCCCCH		55.3425953088
87UbiquitinationHAEFLHCKSKKFTDF
CCCHHHCCCCCCCCH		55.34-
90AcetylationFLHCKSKKFTDFDEV
HHHCCCCCCCCHHHH		61.6625953088
90UbiquitinationFLHCKSKKFTDFDEV
HHHCCCCCCCCHHHH		61.66-
113UbiquitinationDRVTGTNKGISPVPI
CCCCCCCCCCCCCCC		58.41-
116PhosphorylationTGTNKGISPVPINLR
CCCCCCCCCCCCEEE		28.6318785766
125PhosphorylationVPINLRVYSPHVLNL
CCCEEEEECCEEEEE		15.28-
126PhosphorylationPINLRVYSPHVLNLT
CCEEEEECCEEEEEE		12.9824076635
159SulfoxidationIEYQIKDMILQFISR
HHHHHHHHHHHHHCC		2.5328183972
191UbiquitinationSDALKLAKEVDPQGL
CHHHHHHHHCCCCCC		69.57-
200PhosphorylationVDPQGLRTIGVITKL
CCCCCCEEEEEEEEH		27.4218452278
200 (in isoform 2)Phosphorylation-27.42-
200 (in isoform 3)Phosphorylation-27.42-
206UbiquitinationRTIGVITKLDLMDEG
EEEEEEEEHHHCCCC		28.9521906983
206 (in isoform 1)Ubiquitination-28.9521890473
206 (in isoform 2)Ubiquitination-28.9521890473
210SulfoxidationVITKLDLMDEGTDAR
EEEEHHHCCCCCCHH		4.3821406390
214PhosphorylationLDLMDEGTDARDVLE
HHHCCCCCCHHHHHH		25.16-
217MethylationMDEGTDARDVLENKL
CCCCCCHHHHHHHCC		37.06-
223UbiquitinationARDVLENKLLPLRRG
HHHHHHHCCCCCCCC		41.8621890473
2232-HydroxyisobutyrylationARDVLENKLLPLRRG
HHHHHHHCCCCCCCC		41.86-
223UbiquitinationARDVLENKLLPLRRG
HHHHHHHCCCCCCCC		41.8621890473
223 (in isoform 1)Ubiquitination-41.8621890473
223 (in isoform 2)Ubiquitination-41.8621890473
231PhosphorylationLLPLRRGYIGVVNRS
CCCCCCCCEEEECCC		7.8421411625
240AcetylationGVVNRSQKDIEGKKD
EEECCCHHHCCCHHH		63.0223749302
257UbiquitinationAALAAERKFFLSHPA
HHHHHHHHHHHCCHH		31.7921890473
257AcetylationAALAAERKFFLSHPA
HHHHHHHHHHHCCHH		31.7925953088
257UbiquitinationAALAAERKFFLSHPA
HHHHHHHHHHHCCHH		31.7921890473
257 (in isoform 1)Ubiquitination-31.7921890473
257 (in isoform 2)Ubiquitination-31.7921890473
280PhosphorylationGTPHLQKTLNQQLTN
CCHHHHHHHHHHHHH		20.2721406692
286PhosphorylationKTLNQQLTNHIRESL
HHHHHHHHHHHHHHH		22.0321406692
292PhosphorylationLTNHIRESLPALRSK
HHHHHHHHHHHHHHH		29.7924719451
2992-HydroxyisobutyrylationSLPALRSKLQSQLLS
HHHHHHHHHHHHHHH		44.08-
299AcetylationSLPALRSKLQSQLLS
HHHHHHHHHHHHHHH		44.0823749302
299MalonylationSLPALRSKLQSQLLS
HHHHHHHHHHHHHHH		44.0826320211
299UbiquitinationSLPALRSKLQSQLLS
HHHHHHHHHHHHHHH		44.08-
315UbiquitinationEKEVEEYKNFRPDDP
HHHHHHHHCCCCCCH		53.54-
347PhosphorylationFEKRIEGSGDQVDTL
HHHHCCCCCCCCEEE		26.8020068231
353PhosphorylationGSGDQVDTLELSGGA
CCCCCCEEEEECCCC		24.2327251275
357PhosphorylationQVDTLELSGGARINR
CCEEEEECCCCCCHH		26.3021060948
376UbiquitinationRFPFELVKMEFDEKD
CCCHHHEEEECCHHH		45.39-
382UbiquitinationVKMEFDEKDLRREIS
EEEECCHHHHHHHHH		65.00-
389PhosphorylationKDLRREISYAIKNIH
HHHHHHHHHHHHHHH		12.0828102081
390PhosphorylationDLRREISYAIKNIHG
HHHHHHHHHHHHHHC		20.2928102081
393UbiquitinationREISYAIKNIHGVRT
HHHHHHHHHHHCCCC		41.5021890473
393UbiquitinationREISYAIKNIHGVRT
HHHHHHHHHHHCCCC		41.5021890473
393 (in isoform 1)Ubiquitination-41.5021890473
393 (in isoform 2)Ubiquitination-41.5021890473
400PhosphorylationKNIHGVRTGLFTPDL
HHHHCCCCCCCCCCH		35.5120860994
404PhosphorylationGVRTGLFTPDLAFEA
CCCCCCCCCCHHHHH		22.4220860994
414UbiquitinationLAFEAIVKKQVVKLK
HHHHHHHHHHHCCCC		31.2321906983
414 (in isoform 1)Ubiquitination-31.2321890473
414 (in isoform 2)Ubiquitination-31.2321890473
415UbiquitinationAFEAIVKKQVVKLKE
HHHHHHHHHHCCCCC		37.11-
4212-HydroxyisobutyrylationKKQVVKLKEPCLKCV
HHHHCCCCCHHHHHH		54.62-
445AcetylationTVRQCTSKLSSYPRL
HHHHHHHHHHCCHHH		33.9526051181
449PhosphorylationCTSKLSSYPRLREET
HHHHHHCCHHHHHHH		6.7617192257
449 (in isoform 2)Phosphorylation-6.76-
461PhosphorylationEETERIVTTYIRERE
HHHHHHHHHHHHHCC		16.1221406692
462PhosphorylationETERIVTTYIREREG
HHHHHHHHHHHHCCC		13.1724719451
463PhosphorylationTERIVTTYIREREGR
HHHHHHHHHHHCCCC		6.6624719451
527PhosphorylationVIRRGWLTINNISLM
EEECCEEEEEEEEEE		18.3627259358
528 (in isoform 2)Phosphorylation-3.30-
528 (in isoform 3)Phosphorylation-3.30-
532PhosphorylationWLTINNISLMKGGSK
EEEEEEEEEECCCCE		25.2420068231
559 (in isoform 2)Phosphorylation-77.45-
559 (in isoform 3)Phosphorylation-77.45-
562MalonylationDEEEKEKKYMLPLDN
CHHHHHHCEEEECCC		36.6626320211
562UbiquitinationDEEEKEKKYMLPLDN
CHHHHHHCEEEECCC		36.66-
563PhosphorylationEEEKEKKYMLPLDNL
HHHHHHCEEEECCCC		18.2320068231
5712-HydroxyisobutyrylationMLPLDNLKIRDVEKG
EEECCCCCCCCHHHC		41.78-
577AcetylationLKIRDVEKGFMSNKH
CCCCCHHHCCCCCCE		58.2425953088
577UbiquitinationLKIRDVEKGFMSNKH
CCCCCHHHCCCCCCE		58.24-
577 (in isoform 2)Phosphorylation-58.24-
577 (in isoform 3)Phosphorylation-58.24-
581PhosphorylationDVEKGFMSNKHVFAI
CHHHCCCCCCEEEEE		40.2320068231
587 (in isoform 2)Phosphorylation-12.36-
587 (in isoform 3)Phosphorylation-12.36-
591PhosphorylationHVFAIFNTEQRNVYK
EEEEEEEHHCCHHHH		23.8120068231
594AcetylationAIFNTEQRNVYKDLR
EEEEHHCCHHHHHHH		28.4819608861
594UbiquitinationAIFNTEQRNVYKDLR
EEEEHHCCHHHHHHH		28.4819608861
594 (in isoform 2)Acetylation-28.48-
594 (in isoform 3)Acetylation-28.48-
597PhosphorylationNTEQRNVYKDLRQIE
EHHCCHHHHHHHHHH		11.4428152594
598AcetylationTEQRNVYKDLRQIEL
HHCCHHHHHHHHHHH		46.1019608861
598MalonylationTEQRNVYKDLRQIEL
HHCCHHHHHHHHHHH		46.1026320211
598UbiquitinationTEQRNVYKDLRQIEL
HHCCHHHHHHHHHHH		46.1019608861
607S-nitrosocysteineLRQIELACDSQEDVD
HHHHHHHCCCHHHHH		8.93-
607S-nitrosylationLRQIELACDSQEDVD
HHHHHHHCCCHHHHH		8.9322178444
615PhosphorylationDSQEDVDSWKASFLR
CCHHHHHHHHHHHHH		30.2618767875
615 (in isoform 2)Phosphorylation-30.26-
615 (in isoform 3)Phosphorylation-30.26-
617UbiquitinationQEDVDSWKASFLRAG
HHHHHHHHHHHHHCC		37.80-
619PhosphorylationDVDSWKASFLRAGVY
HHHHHHHHHHHCCCC		22.5329496963
644PhosphorylationGAQENTFSMDPQLER
CCCCCCCCCCHHHHH		21.9026657352
645SulfoxidationAQENTFSMDPQLERQ
CCCCCCCCCHHHHHH		8.3428465586
658 (in isoform 2)Phosphorylation-40.33-
658 (in isoform 3)Phosphorylation-40.33-
662PhosphorylationTIRNLVDSYVAIINK
HHHHHHHHHHHHHCH		17.6420068231
663PhosphorylationIRNLVDSYVAIINKS
HHHHHHHHHHHHCHH		6.8820068231
665UbiquitinationNLVDSYVAIINKSIR
HHHHHHHHHHCHHHH		6.6821890473
665 (in isoform 2)Ubiquitination-6.6821890473
669UbiquitinationSYVAIINKSIRDLMP
HHHHHHCHHHHHHCC		36.5321890473
669 (in isoform 1)Ubiquitination-36.5321890473
678PhosphorylationIRDLMPKTIMHLMIN
HHHHCCHHHHHHHCC		20.0529255136
687PhosphorylationMHLMINNTKAFIHHE
HHHHCCCCHHHHHHH		21.1829255136
726PhosphorylationRDDMLRMYHALKEAL
HHHHHHHHHHHHHHH		4.22-
740PhosphorylationLNIIGDISTSTVSTP
HHHHHCCCCCCCCCC		22.5028176443
741PhosphorylationNIIGDISTSTVSTPV
HHHHCCCCCCCCCCC		28.8428176443
742PhosphorylationIIGDISTSTVSTPVP
HHHCCCCCCCCCCCC		21.7428176443
743PhosphorylationIGDISTSTVSTPVPP
HHCCCCCCCCCCCCC		20.6828176443
745PhosphorylationDISTSTVSTPVPPPV
CCCCCCCCCCCCCCC		27.3828176443
746PhosphorylationISTSTVSTPVPPPVD
CCCCCCCCCCCCCCC		24.7828176443
751 (in isoform 2)Phosphorylation-35.78-
751 (in isoform 3)Phosphorylation-35.78-
755PhosphorylationVPPPVDDTWLQSASS
CCCCCCCCCHHCCCC		24.5025159151
755 (in isoform 2)Phosphorylation-24.50-
755 (in isoform 3)Phosphorylation-24.50-
757 (in isoform 2)Phosphorylation-2.90-
757 (in isoform 3)Phosphorylation-2.90-
758 (in isoform 2)Phosphorylation-28.63-
758 (in isoform 3)Phosphorylation-28.63-
759PhosphorylationVDDTWLQSASSHSPT
CCCCCHHCCCCCCCC		28.1330278072
760 (in isoform 2)Phosphorylation-11.33-
760 (in isoform 3)Phosphorylation-11.33-
761PhosphorylationDTWLQSASSHSPTPQ
CCCHHCCCCCCCCCC		33.5528176443
762PhosphorylationTWLQSASSHSPTPQR
CCHHCCCCCCCCCCC		27.9230278072
762 (in isoform 2)Phosphorylation-27.92-
762 (in isoform 3)Phosphorylation-27.92-
764PhosphorylationLQSASSHSPTPQRRP
HHCCCCCCCCCCCCC		32.2030278072
766PhosphorylationSASSHSPTPQRRPVS
CCCCCCCCCCCCCCC		34.7630278072
785MethylationPGRPPAVRGPTPGPP
CCCCCCCCCCCCCCC		47.70-
848PhosphorylationGIPPGVPSRRPPAAP
CCCCCCCCCCCCCCC		38.2212205083
850MethylationPPGVPSRRPPAAPSR
CCCCCCCCCCCCCCC		45.98-
857MethylationRPPAAPSRPTIIRPA
CCCCCCCCCCEEECC		31.18-
862DimethylationPSRPTIIRPAEPSLL
CCCCCEEECCCCCCC		22.11-
862MethylationPSRPTIIRPAEPSLL
CCCCCEEECCCCCCC		22.11-
867PhosphorylationIIRPAEPSLLD----
EEECCCCCCCC----		32.8226714015
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
764SPhosphorylationKinaseCDK1P06493
Uniprot
764SPhosphorylationKinaseCDK2P24941
PSP
766TPhosphorylationKinaseCDK1P06493
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
764SPhosphorylation

-
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SHAN1_HUMANSHANK1physical
11583995
SHAN2_HUMANSHANK2physical
11583995
SNX9_HUMANSNX9physical
12952949
DX39B_HUMANDDX39Bphysical
16169070
HMGB1_HUMANHMGB1physical
21900206
DYN1_HUMANDNM1physical
21900206
RS2_HUMANRPS2physical
21900206
ATX3_HUMANATXN3physical
21900206
ZBT16_HUMANZBTB16physical
21900206
MA1B1_HUMANMAN1B1physical
21900206
TCPH_HUMANCCT7physical
21900206
RWD2B_HUMANRWDD2Bphysical
21900206
CC90B_HUMANCCDC90Bphysical
21900206
DC1I1_HUMANDYNC1I1physical
21900206
TYK2_HUMANTYK2physical
21900206
TIAM2_HUMANTIAM2physical
21900206
ITSN1_HUMANITSN1physical
21900206
GDF9_HUMANGDF9physical
21900206
SH3K1_HUMANSH3KBP1physical
20711168
AMPH_HUMANAMPHphysical
15834155
SH3G2_HUMANSH3GL2physical
15834155
ITSN1_HUMANITSN1physical
15834155
SRC_HUMANSRCphysical
15834155
GRB2_HUMANGRB2physical
15834155
A4_HUMANAPPphysical
21832049
PICAL_HUMANPICALMphysical
22939629
RBMS1_HUMANRBMS1physical
22939629
ZNT5_HUMANSLC30A5physical
22939629
AMPH_HUMANAMPHphysical
16696976
GRB2_HUMANGRB2physical
16696976
MANEA_HUMANMANEAphysical
16696976
ITSN1_HUMANITSN1physical
16696976
SNX9_HUMANSNX9physical
15703209
GRB2_HUMANGRB2physical
21988832
GLGB_HUMANGBE1physical
26344197
GGA1_HUMANGGA1physical
26344197
PTN13_HUMANPTPN13physical
26344197
RPE_HUMANRPEphysical
26344197
RTCB_HUMANRTCBphysical
26344197
SH3K1_HUMANSH3KBP1physical
26344197
PTN11_HUMANPTPN11physical
21996738
P85A_HUMANPIK3R1physical
21996738
PGFRA_HUMANPDGFRAphysical
21996738
Drug and Disease Associations
Kegg Disease
H00264 Charcot-Marie-Tooth disease (CMT); Hereditary motor and sensory neuropathy; Peroneal muscular atroph
H00700 Centronuclear myopathy
OMIM Disease
160150Myopathy, centronuclear, 1 (CNM1)
615368Lethal congenital contracture syndrome 5 (LCCS5)
606482Charcot-Marie-Tooth disease, dominant, intermediate type, B (CMTDIB)
606482Charcot-Marie-Tooth disease 2M (CMT2M)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DYN2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-598, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-449, AND MASSSPECTROMETRY.

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