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Protein Page:
DYN2 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
DYN2 a cytoplasmic microtubule-associated force-producing protein involved in producing microtubule bundles and able to bind and hydrolyze GTP. Most probably involved in vesicular trafficking processes. May mediate the conventional clathrin-mediated uptake of surface receptors. Expressed in the postsynaptic density of neuronal cells. Two alternatively spliced isoforms have been described. Note: This description may include information from UniProtKB.
Protein type: Hydrolase; EC 3.6.5.5; Vesicle protein; Motility/polarity/chemotaxis; Microtubule binding protein
Cellular Component: Golgi membrane; microtubule; postsynaptic membrane; postsynaptic density; cytoplasm; plasma membrane; midbody; cytosol; cell junction
Molecular Function: GTPase activity; protein binding; enzyme binding; GTP binding; microtubule binding; phospholipid binding
Biological Process: positive regulation of apoptosis; positive regulation of transcription, DNA-dependent; synaptic vesicle transport; antigen processing and presentation of exogenous peptide antigen via MHC class II; transferrin transport; endocytosis; signal transduction; membrane organization and biogenesis; regulation of transcription, DNA-dependent; GTP catabolic process; receptor internalization; post-Golgi vesicle-mediated transport; G2/M transition of mitotic cell cycle
Reference #:  P50570 (UniProtKB)
Alt. Names/Synonyms: CMT2M; CMTDI1; CMTDIB; DI-CMTB; DNM2; DYN2; dynamin 2; dynamin II; Dynamin-2; DYNII
Gene Symbols: DNM2
Molecular weight: 98,064 Da
Basal Isoelectric point: 7.04  Predict pI for various phosphorylation states
CST Pathways:  GPCRs Signaling to MAPK/Erk
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

DYN2
Protein Structure Not Found.


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Sites Implicated In
cell cycle regulation: S764‑p
intracellular localization: S764‑p, S848‑p
molecular association, regulation: S764‑p, T766‑p, S848‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


  MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


        human

 
0 1 H80 LIFSKTEHAEFLHCK
0 7 Y125-p VPINLRVySPHVLNL
0 2 K206-u RTIGVITkLDLMDEG
0 2 K223-u ARDVLENkLLPLRRG
3 1 Y231-p LLPLRRGyIGVVNRS
0 2 K257-u AALAAERkFFLSHPA
0 1 T280-p GTPHLQKtLNQQLtN
0 1 T286-p KtLNQQLtNHIRESL
0 1 S298 ESLPALRSKLQSQLL
0 1 S302 ALRSKLQSQLLSLEK
0 1 S306 KLQSQLLSLEKEVEE
0 3 K376-u RFPFELVkMEFDEKD
0 2 K393-u REISYAIkNIHGVRT
0 1 K414-u LAFEAIVkKQVVKLK
0 1 Y449-p CTSKLSSyPRLREET
0 1 T527-p VIRRGWLtINNIsLM
0 2 S532-p WLtINNIsLMKGGSK
0 1 Y553 TAESLSWYKDEEEKE
0 1 S581-p DVEKGFMsNKHVFAI
0 1 K583 EKGFMsNKHVFAIFN
0 1 T591-p HVFAIFNtEQRNVyk
3 3 Y597-p NtEQRNVykDLRQIE
0 1 K598-a tEQRNVykDLRQIEL
0 1 Y626 SFLRAGVYPEKDQAE
0 1 S662-p TIRNLVDsyVAIINk
0 1 Y663-p IRNLVDsyVAIINkS
0 4 K669-u syVAIINkSIRDLMP
0 1 S759-p VDDTWLQsAsSHsPt
0 2 S761-p DTWLQsAsSHsPtPQ
2 3 S764-p LQsAsSHsPtPQRRP
1 3 T766-p sAsSHsPtPQRRPVS
1 0 S848-p GIPPGVPsRRPPAAP
0 1 S856 RRPPAAPSRPTIIrP
0 1 R862-m1 PSRPTIIrPAEPSLL
0 1 R862-m2 PSRPTIIrPAEPSLL
  mouse

 
Y80-p LIFSKTEyAEFLHCK
Y125 VPINLRVYSPHVLNL
K206-u RTIGVITkLDLMDEG
K223-u ARDVLENkLLPLRRG
Y231-p LLPLRRGyIGVVNRS
K257-u AALAAERkFFLSHPA
T280 GTPHLQKTLNQQLTN
T286 KTLNQQLTNHIRESL
S298-p ESLPTLRsKLQsQLL
S302-p TLRsKLQsQLLsLEK
S306-p KLQsQLLsLEKEVEE
K376-u RFPFELVkMEFDEKD
K393-u REISYAIkNIHGVRT
K414 LAFEAIVKKQVVKLK
Y449 CTSKLSSYPRLREET
T527 VIRRGWLTINNISLM
S532 WLTINNISLMKGGSK
Y553 TAESLSWYKDEEEKE
S581 DVEKGFMSNkHVFAI
K583-a EKGFMSNkHVFAIFN
T591 HVFAIFNTEQRNVyK
Y597-p NTEQRNVyKDLRQIE
K598 TEQRNVyKDLRQIEL
Y626-p SFLRAGVyPEKDQAE
S662 TIRNLVDSYVAIINk
Y663 IRNLVDSYVAIINkS
K669-u SYVAIINkSIRDLMP
N759 VDDTWLQNTsGHsPT
S761-p DTWLQNTsGHsPTPQ
S764-p LQNTsGHsPTPQRRP
T766 NTsGHsPTPQRRPVS
S848 GIPPGVPSRRAPAAP
S856-p RRAPAAPsRPTIIRP
R862 PsRPTIIRPAEPSLL
R862 PsRPTIIRPAEPSLL
  rat

 
Y80 LIFSKTEYAEFLHCK
Y125 VPINLRVYSPHVLNL
K206 RTIGVITKLDLMDEG
K223 ARDVLENKLLPLRRG
Y231-p LLPLRRGyIGVVNRS
K257 AALAAERKFFLSHPA
T280 GTPHLQKTLNQQLTN
T286 KTLNQQLTNHIRESL
S298 ESLPTLRSKLQSQLL
S302 TLRSKLQSQLLSLEK
S306 KLQSQLLSLEKEVEE
K376 RFPFELVKMEFDEKD
K393 REISYAIKNIHGVRT
K414 LAFEAIVKKQVVKLK
Y449 CTSKLSSYPRLREET
T527 VIRRGWLTINNISLM
S532 WLTINNISLMKGGSK
Y553-p TAESLSWyKDEEEKE
S581 DVEKGFMSNKHVFAI
K583 EKGFMSNKHVFAIFN
T591 HVFAIFNTEQRNVyK
Y597-p NTEQRNVyKDLRQIE
K598 TEQRNVyKDLRQIEL
Y626 SFLRAGVYPEKDQAE
S662 TIRNLVDSYVAIINK
Y663 IRNLVDSYVAIINKS
K669 SYVAIINKSIRDLMP
N759 VDDTWLQNTSSHsPT
S761 DTWLQNTSSHsPTPQ
S764-p LQNTSSHsPTPQRRP
T766 NTSSHsPTPQRRPVS
S848 GIPPGVPSRRAPAAP
S856 RRAPAAPSRPTIIRP
R862 PSRPTIIRPAEPSLL
R862 PSRPTIIRPAEPSLL
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