Synthesized phosho peptide around human DRP1 (Ser616)

Phospho-DRP1 (S616) Polyclonal Antibody detects endogenous levels of DRP1 protein only when phosphorylated at S616(human), S622(mouse), S635(rat).The name of modified sites may be influenced by many factors, such as species (the modified site was not originally found in human samples) and the change of protein sequence (the previous protein sequence is incomplete, and the protein sequence may be prolonged with the development of protein sequencing technology). When naming, we will use the "numbers" in historical reference to keep the sites consistent with the reports. The antibody binds to the following modification sequence (lowercase letters are modification sites):PAsPQ

DNM1L DLP1 DRP1

DRP1 (Ser616)

Dynamin-1-like protein ;
Dnm1p/Vps1p-like protein ;
DVLP ;
Dynamin family member proline-rich carboxyl-terminal domain less ;
Dymple ;
Dynamin-like protein ;
Dynamin-like protein 4 ;
Dynamin-like protein IV ;
HdynIV ;
Dynamin-related protein 1 ;

This gene encodes a member of the dynamin superfamily of GTPases. The encoded protein mediates mitochondrial and peroxisomal division , and is involved in developmentally regulated apoptosis and programmed necrosis. Dysfunction of this gene is implicated in several neurological disorders , including Alzheimer's disease. Mutations in this gene are associated with the autosomal dominant disorder , encephalopathy , lethal , due to defective mitochondrial and peroxisomal fission (EMPF) . Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq , Jun 2013] ,

Catalytic activity:GTP + H (2) O = GDP + phosphate. ,Function:Functions in mitochondrial and peroxisomal division probably by regulating membrane fission. Enzyme hydrolyzing GTP that oligomerizes to form ring-like structures and is able to remodel membranes. May also play a role on organelles of the secretory pathway. ,miscellaneous:Isoform 1 and isoform 2 inhibits peroxisomal division when overexpressed while isoform 3 and isoform 4 have no effect. ,PTM:Phosphorylated by GSK3B. ,similarity:Belongs to the dynamin family. ,similarity:Contains 1 GED domain. ,subcellular location:Mainly cytosolic. Also membrane-associated. Localizes to mitochondria at spots of division events. Associated with peroxisomal membranes , it is recruited in part by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear. ,subunit:Homotetramer; N-terminal part binds to the C-terminal part of another DNM1L. Can self-assemble in multimeric ring-like structures. Interacts with FIS1 (By similarity) . Interacts with GSK3B. ,tissue specificity:Ubiquitously expressed with highest levels found in skeletal muscles , heart , kidney and brain. Isoform 1 is brain-specific while isoform 3 and isoform 4 are predominantly expressed in testis and skeletal muscles respectively. Isoform 2 is weakly expressed in brain , heart and kidney and isoform 5 is dominantly expressed in liver , heart and kidney. ,

Cytoplasm , cytosol. Golgi apparatus. Endomembrane system; Peripheral membrane protein. Mitochondrion outer membrane ; Peripheral membrane protein. Peroxisome. Membrane , clathrin-coated pit . Cytoplasmic vesicle , secretory vesicle , synaptic vesicle membrane . Mainly cytosolic. Recruited by RALA and RALBP1 to mitochondrion during mitosis (PubMed:21822277) . Translocated to the mitochondrial membrane through O-GlcNAcylation and interaction with FIS1. Colocalized with MARCHF5 at mitochondrial membrane. Localizes to mitochondria at sites of division. Localizes to mitochondria following necrosis induction. Recruited to the mitochondrial outer membrane by interaction with MIEF1. Mitochondrial recruitment is inhibited by C11orf65/MFI (By similarity) . Associated with peroxisomal membranes , partly recruited there by PEX11B. May also be associated with endoplasmic reticulum tubules and cytoplasmic vesicles and found to be perinuclear. In some cell types , localizes to the Golgi complex (By similarity) . Binds to phospholipid membranes (By similarity) . .

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