DEPOD - human DEPhOsphorylation Database

Basic Information
Phosphatases
Pathway
Interacting Proteins
Phosphorylating Kinases

Gene Name	DNM1 (QuickGO)	Interactive visualization of DNM1 structures (A quick tutorial to explore the interctive visulaization) Representative structure: 2X2F
Synonyms	DNM1, DNM
Protein Name	DNM1
Alternative Name(s)	Dynamin-1;3.6.5.5;
Protein Family	Belongs to the TRAFAC class dynamin-like GTPasesuperfamily Dynamin/Fzo/YdjA family
EntrezGene ID	1759 (Comparitive Toxicogenomics)
UniProt AC (Human)	Q05193 (protein sequence)
Enzyme Class	3.6.5.5 (BRENDA )
Molecular Weight	97408 Dalton
Protein Length	864 amino acids (AA)
Genome Browsers	NCBI \| ENSG00000106976 (Ensembl) \| UCSC
Crosslinking annotations	Query our ID-mapping table
Orthologues	Quest For Orthologues (QFO) \| GeneTree \| eggNOG - KOG0446 \| eggNOG - COG0699
Phosphorylation Network	Visualize

Domain organization, Expression, Diseases

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Localization, Function, Catalytic activity and Sequence

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Motif information from Eukaryotic Linear Motif atlas (ELM)

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Gene Ontology (P: Process; F: Function and C: Component terms)

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KEGG Pathway
Reactome Pathway

Pathway ID	Pathway Name	Pathway Description (KEGG)
hsa04072	Phospholipase D signaling pathway	Phospholipase D (PLD) is an essential enzyme responsible for the production of the lipid second messenger phosphatidic acid (PA), which is involved in fundamental cellular processes, including membrane trafficking, actin cytoskeleton remodeling, cell proliferation and cell survival. PLD activity can be stimulated by a large number of cell surface receptors and is elaborately regulated by intracellular factors, including protein kinase C isoforms, small GTPases of the ARF, Rho and Ras families and the phosphoinositide, phosphatidylinositol 4,5-bisphosphate (PIP2). The PLD-produced PA activates signaling proteins and acts as a node within the membrane to which signaling proteins translocate. Several signaling proteins, including Raf-1 and mTOR, directly bind PA to mediate translocation or activation, respectively.
hsa04144	Endocytosis	Endocytosis is a mechanism for cells to remove ligands, nutrients, and plasma membrane (PM) proteins, and lipids from the cell surface, bringing them into the cell interior. Transmembrane proteins entering through clathrin-dependent endocytosis (CDE) have sequences in their cytoplasmic domains that bind to the APs (adaptor-related protein complexes) and enable their rapid removal from the PM. In addition to APs and clathrin, there are numerous accessory proteins including dynamin. Depending on the various proteins that enter the endosome membrane, these cargoes are sorted to distinct destinations. Some cargoes, such as nutrient receptors, are recycled back to the PM. Ubiquitylated membrane proteins, such as activated growth-factor receptors, are sorted into intraluminal vesicles and eventually end up in the lysosome lumen via multivesicular endosomes (MVEs). There are distinct mechanisms of clathrin-independent endocytosis (CIE) depending upon the cargo and the cell type.
hsa04721	Synaptic vesicle cycle	Communication between neurons is mediated by the release of neurotransmitter from synaptic vesicles (SVs). At the nerve terminal, SVs cycle through repetitive episodes of exocytosis and endocytosis. SVs are filled with neurotransmitters by active transport. The loaded SVs are then docked at a specialized region of the presynaptic plasma membrane known as the active zone, where they undergo a priming reaction. Upon arrival of an action potential, Ca2+ enters through voltage-gated channels and neurotransmitter is released by exocytosis, usually in less than a millisecond. After fusion, the vesicle is retrieved by endocytosis and reloaded for another round of exocytosis.
hsa04961	Endocrine and other factor-regulated calcium reabsorption	Calcium (Ca2+) is essential for numerous physiological functions including intracellular signalling processes, neuronal excitability, muscle contraction and bone formation. Therefore, its homeostasis is finely maintained through the coordination of intestinal absorption, renal reabsorption, and bone resorption. In kidney, the late part of the distal convoluted tubule (DCT) and the connecting tubule (CNT) are the site of active Ca2+ transport and precisely regulate Ca2+ reabsorption. Following Ca2+ entry through TRPV5, Ca2+ bound to calbindin-D28K diffuses to the basolateral side, where it is extruded into the blood compartment through NCX1 and to a lesser extent PMCA1b. In the urinary compartment, both klotho and tissue kallikrein (TK) increase the apical abundance of TRPV5. In the blood compartment, PTH, 1,25(OH)2D3 and estrogen increase the transcription and protein expression of the luminal Ca2+ channels, calbindins, and the extrusion systems.
hsa05100	Bacterial invasion of epithelial cells	Many pathogenic bacteria can invade phagocytic and non-phagocytic cells and colonize them intracellularly, then become disseminated to other cells. Invasive bacteria induce their own uptake by non-phagocytic host cells (e.g. epithelial cells) using two mechanisms referred to as zipper model and trigger model. Listeria, Staphylococcus, Streptococcus, and Yersinia are examples of bacteria that enter using the zipper model. These bacteria express proteins on their surfaces that interact with cellular receptors, initiating signalling cascades that result in close apposition of the cellular membrane around the entering bacteria. Shigella and Salmonella are the examples of bacteria entering cells using the trigger model. These bacteria use type III secretion systems to inject protein effectors that interact with the actin cytoskeleton.

Pathway ID	Pathway Name	Pathway Description (KEGG)
R-HSA-166016	Toll Like Receptor 4 (TLR4) Cascade.	TLR4 is unique among the TLR family in its ability to recruit four adapters to activate two distinct signaling pathways. One pathway is activated by the pair of the adapters Mal or TIRAP (Toll/interleukin-1-receptor (TIR)-domain-containing adapter protein) and MyD88, which leads to the NFkB activation and the induction of pro-inflammatory cytokines. The second pathway is activated by the adapters TRIF (TIR-domain-containing adapter protein inducing interferon-beta) and TRAM (TRIF-related adapter molecule). The combined use of TRIF and TRAM adapters is specific for TLR4 signaling pathway and leads to the induction of type I interferons and delayed activation of NFkB. The previous model of TLR4 signaling pathway described the simultaneous activation of these two signaling pathways at the plasma membrane, however the later studies suggested that upon activation TLR4 first induces TIRAP-MyD88 signaling at the plasma membrane and is then endocytosed and activates TRAM-TRIF signaling from the early endosome [Kagan JC et al 2008; Tanimura N et al 2008; Zanoni I et al 2011]
R-HSA-177504	Retrograde neurotrophin signalling.	Neurotrophin-TRK complexes can be internalized and enter signalling vesicles, which travel retrogradely over long distances from distal nerve terminals to neuronal cell bodies. Such retrograde signalling by neurotrophin-TRK complexes regulates survival, synaptogenesis and maintenance of proper neural connectivity. The neurotrophin-TRK complex may use three distinct internalization pathways. Although Clathrin-mediated endocytosys appears to be the major internalization route, it is controversial whether it also represents the dominant pathway for retrograde transport and signalling. Pyncher-mediated endocytosis might be more relevant in this regard. Moreover, also caveolin-mediated endocytosis may play a role in NGF-TrkA internalization.Retrograde transport of TRKs is microtubule-dependent: TRKs remain activated and bound to neurotrophins during retrograde transport. The current view is reflected in the signalling endosome model. It is a specialized vesicle containing ligand (NGF, BDNF) bound to its activated TRK receptor, together with activated downstream signalling proteins, transported by motor proteins (dyneins) from nerve terminals to remote cell bodies, where the receptors trigger signalling cascades
R-HSA-190873	Gap junction degradation.	The half-life of Cx is very short (1 to 5h) compared to other junctional proteins (Laird et al., 1995 ; Fallon and Goudenough, 1981). Connexins are targeted for degradation by the proteasome and the lysosome. Degradation appears to involve the phosphorylation of Connexins as well as their interactions with other proteins (Piehl et al., 2007)
R-HSA-196025	Formation of annular gap junctions.	Until now, two kinds of annular gap junctions have been described. The first is a small vesicle like structure which permits gap junction plaque renewal without arrest of functionality [Jordan et al., 2001]. The second is a large annular structure, composed primarily of the junctional plaques of two adjacent cells (Jordan et al., 2001; Segretain et al., 2004)
R-HSA-2132295	MHC class II antigen presentation.	Antigen presenting cells (APCs) such as B cells, dendritic cells (DCs) and monocytes/macrophages express major histocompatibility complex class II molecules (MHC II) at their surface and present exogenous antigenic peptides to CD4+ T helper cells. CD4+ T cells play a central role in immune protection. On their activation they stimulate differentiation of B cells into antibody-producing B-cell blasts and initiate adaptive immune responses. MHC class II molecules are transmembrane glycoprotein heterodimers of alpha and beta subunits. Newly synthesized MHC II molecules present in the endoplasmic reticulum bind to a chaperone protein called invariant (Ii) chain. The binding of Ii prevents the premature binding of self antigens to the nascent MHC molecules in the ER and also guides MHC molecules to endocytic compartments. In the acidic endosomal environment, Ii is degraded in a stepwise manner, ultimately to free the class II peptide-binding groove for loading of antigenic peptides. Exogenous antigens are internalized by the APC by receptor mediated endocytosis, phagocytosis or pinocytosis into endocytic compartments of MHC class II positive cells, where engulfed antigens are degraded in a low pH environment by multiple acidic proteases, generating MHC class II epitopes. Antigenic peptides are then loaded into the class II ligand-binding groove. The resulting class II peptide complexes then move to the cell surface, where they are scanned by CD4+ T cells for specific recognition (Berger & Roche 2009, Zhou & Blum 2004, Watts 2004, Landsverk et al. 2009)
R-HSA-3928665	EPH-ephrin mediated repulsion of cells.	Despite high-affinity multimeric interaction between EPHs and ephrins (EFNs), the cellular response to EPH-EFN engagement is usually repulsion between the two cells and signal termination. These repulsive responses induce an EPH receptor-expressing cell to retract from an ephrin-expressing cell after establishing initial contact. The repulsive responses mediated by EPH receptors in the growth cone at the leading edge of extending axons and in axonal collateral branches contribute to the formation of selective neuronal connections. It is unclear how high affinity trans-cellular interactions between EPHs and ephrins are broken to convert adhesion into repulsion. Two possible mechanisms have been proposed for the repulsion of EPH-EFN bearing cells: the first one involves regulated cleavage of ephrin ligands or EPH receptors by transmembrane proteases following cell-cell contact, while the second one is rapid endocytosis of whole EPH:EFN complexes during the retraction of the interacting cells or neuronal growth cones (Egea & Klein 2007, Janes et al. 2005). RAC also plays an essential role during growth cone collapse by promoting actin polymerization that drives membrane internalization by endocytosis (Marston et al. 2003)
R-HSA-437239	Recycling pathway of L1.	L1 functions in many aspects of neuronal development including axon outgrowth and neuronal migration. These functions require coordination between L1 and the actin cytoskeleton. F-actin continuously moves in a retrograde direction from the P-(peripheral) domain of the growth cone towards the growth cone's C-(central) domain. L1, attached to the actin cytoskeleton via membrane cytoskeletal linkers (MCKs) such as ankyrins (Ankyrin-G, -B and -R) and members of the ERMs (ezrin, radixin, and moesin) family, link this retrograde F-actin flow with extracellular immobile ligands.Forward translocation of growth cone requires not only the CAM-actin linkage but also a gradient of cell substrate adhesion (strong adhesion at the front and weak adhesion at the rear) so that the cytoskeletal machinery is able to pull the cell forward as attachments at the rear are released. This asymmetry is achieved in part by internalizing L1 molecules as they are moved to the rear of the growth cone coupled to retrograde F-actin flow and recycling them to the leading edge plasma membrane.L1 internalization is mediated by phosphorylation and dephosphorylation. The L1 cytoplasmic domain (L1CD) carries an endocytic or sorting motif, YRSLE, that is recognized by the clathrin associated adaptor protein-2 (AP-2). AP-2 binds the YRSLE motif only when its tyrosine is not phosphorylated and triggers L1 endocytosis. SRC kinase associated with lipid rafts in the P-domain membrane phosphorylates L1 molecules on tyrosine-1176, stabilizing them in the plasma membrane. L1 endocytosis is triggered by the dephosphorylation of Y1176 within the C domain. Some of these internalized L1 molecules are transported in an anterograde direction along microtubules for reuse in the leading edge
R-HSA-8856828	Clathrin-mediated endocytosis.	Clathrin-mediated endocytosis (CME) is one of a number of process that control the uptake of material from the plasma membrane, and leads to the formation of clathrin-coated vesicles (Pearse et al, 1975; reviewed in Robinson, 2015; McMahon and Boucrot, 2011; Kirchhausen et al, 2014). CME contributes to signal transduction by regulating the cell surface expression and signaling of receptor tyrosine kinases (RTKs) and G-protein coupled receptors (GPCRs). Most RTKs exhibit a robust increase in internalization rate after binding specific ligands; however, some RTKs may also exhibit significant ligand-independent internalization (reviewed in Goh and Sorkin, 2013). CME controls RTK and GPCR signaling by organizing signaling both within the plasma membrane and on endosomes (reviewed in Eichel et al, 2016; Garay et al, 2015; Vieira et al, 1996; Sorkin and von Zastrow, 2014; Di Fiori and von Zastrow, 2014; Barbieri et al, 2016). CME also contributes to the uptake of material such as metabolites, hormones and other proteins from the extracellular space, and regulates membrane composition by recycling membrane components and/or targeting them for degradation. Clathrin-mediated endocytosis involves initiation of clathrin-coated pit (CCP) formation, cargo selection, coat assembly and stabilization, membrane scission and vesicle uncoating. Although for simplicity in this pathway, the steps leading to a mature CCP are represented in a linear and temporally distinct fashion, the formation of a clathrin-coated vesicle is a highly heterogeneous process and clear temporal boundaries between these processes may not exist (see for instance Taylor et al, 2011; Antonescu et al, 2011; reviewed in Kirchhausen et al, 2014). Cargo selection in particular is a critical aspect of the formation of a mature and stable CCP, and many of the proteins involved in the initiation and maturation of a CCP contribute to cargo selection and are themselves stabilized upon incorporation of cargo into the nascent vesicle (reviewed in Kirchhausen et al, 2014; McMahon and Boucrot, 2011).Although the clathrin triskelion was identified early as a major component of the coated vesicles, clathrin does not bind directly to membranes or to the endocytosed cargo. Vesicle formation instead relies on many proteins and adaptors that can bind the plasma membrane and interact with cargo molecules. Cargo selection depends on the recognition of endocytic signals in cytoplasmic tails of the cargo proteins by adaptors that interact with components of the vesicle's inner coat. The classic adaptor for clathrin-coated vesicles is the tetrameric AP-2 complex, which along with clathrin was identified early as a major component of the coat. Some cargo indeed bind directly to AP-2, but subsequent work has revealed a large family of proteins collectively known as CLASPs (clathrin- associated sorting proteins) that mediate the recruitment of diverse cargo into the emerging clathrin-coated vesicles (reviewed in Traub and Bonifacino, 2013). Many of these CLASP proteins themselves interact with AP-2 and clathrin, coordinating cargo recruitment with coat formation (Schmid et al, 2006; Edeling et al, 2006; reviewed in Traub and Bonifacino, 2013; Kirchhausen et al, 2014). Initiation of CCP formation is also influenced by lipid composition, regulated by clathrin-associated phosphatases and kinases (reviewed in Picas et al, 2016). The plasma membrane is enriched in PI(4,5)P2. Many of the proteins involved in initiating clathrin-coated pit formation bind to PI(4,5)P2 and induce membrane curvature through their BAR domains (reviewed in McMahon and Boucrot, 2011; Daumke et al, 2014). Epsin also contributes to early membrane curvature through its Epsin N-terminal homology (ENTH) domain, which promotes membrane curvature by inserting into the lipid bilayer (Ford et al, 2002). Following initiation, some CCPs progress to formation of vesicles, while others undergo disassembly at the cell surface without producing vesicles (Ehrlich et al, 2004; Loerke et al, 2009; Loerke et al, 2011; Aguet et al, 2013; Taylor et al, 2011). The assembly and stabilization of nascent CCPs is regulated by several proteins and lipids (Mettlen et al, 2009; Antonescu et al, 2011).Maturation of the emerging clathrin-coated vesicle is accompanied by further changes in the lipid composition of the membrane and increased membrane curvature, promoted by the recruitment of N-BAR domain containing proteins (reviewed in Daumke et al, 2014; Ferguson and De Camilli, 2012; Picas et al, 2016). Some N-BAR domain containing proteins also contribute to the recruitment of the large GTPase dynamin, which is responsible for scission of the mature vesicle from the plasma membrane (Koh et al, 2007; Lundmark and Carlsson, 2003; Soulet et al, 2005; David et al, 1996; Owen et al, 1998; Shupliakov et al, 1997; Taylor et al, 2011; Ferguson et al, 2009; Aguet et al, 2013; Posor et al, 2013; Chappie et al, 2010; Shnyrova et al, 2013; reviewed in Mettlen et al, 2009; Daumke et al, 2014). After vesicle scission, the clathrin coat is dissociated from the new vesicle by the ATPase HSPA8 (also known as HSC70) and its DNAJ cofactor auxilin, priming the vesicle for fusion with a subsequent endocytic compartment and releasing clathrin for reuse (reviewed in McMahon and Boucrot, 2011; Sousa and Laufer, 2015)

BioGRID
IntAct
MINT
ALL

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
AMPH	Affinity Capture-Western, Reconstituted Complex, enzyme linked immunosorbent assay, peptide array, pull down, surface plasmon resonance	direct interaction, physical	10542231, 11877424, 15834155, 17244534, 9148966, 9280305, 9341169, 9348539, (Europe PMC)	0.77	BioGRID, IntAct, MINT
ARRB1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	17620599, (Europe PMC)	0.35	BioGRID, IntAct
ASB13	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
BIN1	Protein-peptide, filter binding	physical, physical association	16275660, (Europe PMC)	0.40	BioGRID, IntAct
CABIN1	Affinity Capture-Western	physical	10931822, (Europe PMC)	NA	BioGRID
CDK5	Biochemical Activity	physical	15834155, (Europe PMC)	NA	BioGRID
CDKAL1	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
CEP126	Two-hybrid	physical	16169070, (Europe PMC)	NA	BioGRID
CLINT1	Reconstituted Complex	physical	12429846, (Europe PMC)	NA	BioGRID
DGUOK	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
DNAAF2	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
DNM1	Co-crystal Structure, Two-hybrid, cosedimentation in solution, cross-linking study, electron microscopy, molecular sieving, x ray scattering, x-ray crystallography	direct interaction, physical	15123615, 20428113, 20700106, 21927000, 21962517, 26302298, 7634088, (Europe PMC)	0.90	BioGRID, IntAct, MINT
DNM2	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
DNM3	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
DNMBP	Affinity Capture-Western, Reconstituted Complex	physical	14506234, (Europe PMC)	NA	BioGRID
DYRK1A	Affinity Capture-MS, Affinity Capture-Western, Reconstituted Complex	physical	11877424, 19722700, (Europe PMC)	NA	BioGRID
FANCD2	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
FER	Co-fractionation	physical	9722593, (Europe PMC)	NA	BioGRID
FNBP1	Affinity Capture-Western, Co-localization, anti tag coimmunoprecipitation, fluorescence technology, pull down	colocalization, physical, physical association	15252009, (Europe PMC)	0.58	BioGRID, IntAct
GRB2	Affinity Capture-MS, Affinity Capture-Western, Far Western, Reconstituted Complex, anti tag coimmunoprecipitation, peptide array, pull down, surface plasmon resonance	association, direct interaction, physical, physical association	10206341, 15834155, 17244534, 17474147, 19380743, 21706016, 28514442, 8119878, 9009162, (Europe PMC)	0.78	BioGRID, IntAct, MINT
HAX1	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
IQCB1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	21565611, (Europe PMC)	0.35	BioGRID, IntAct
IRF2BPL	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
ITSN1	Affinity Capture-Western, Reconstituted Complex, pull down, surface plasmon resonance	direct interaction, physical	15834155, 18539136, (Europe PMC)	0.62	BioGRID, IntAct, MINT
LYPD6	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
MAP3K10	Reconstituted Complex	physical	9742220, (Europe PMC)	NA	BioGRID
MED31	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
NCK1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, pull down	physical, physical association	10206341, 11557983, (Europe PMC)	0.52	BioGRID, IntAct
NCK2	Affinity Capture-Western	physical	11557983, (Europe PMC)	NA	BioGRID
NCL	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
NPM3	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
NTRK1	Affinity Capture-MS	physical	25921289, (Europe PMC)	NA	BioGRID
NUFIP1	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
PACSIN1	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	11082044, 15252009, (Europe PMC)	0.40	BioGRID, IntAct
PACSIN2	Reconstituted Complex	physical	11082044, (Europe PMC)	NA	BioGRID
PACSIN3	Reconstituted Complex	physical	11082044, (Europe PMC)	NA	BioGRID
PIAS1	Two-hybrid	physical	15123615, (Europe PMC)	NA	BioGRID
PIN4	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
PTK2B	Affinity Capture-Western	physical	19380485, (Europe PMC)	NA	BioGRID
RPE	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
SCN2B	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
SH3BP4	Affinity Capture-Western, Co-localization	physical	16325581, (Europe PMC)	NA	BioGRID
SH3GL1	Reconstituted Complex, peptide array	direct interaction, physical	10542231, 10764144, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SH3GL2	Reconstituted Complex, surface plasmon resonance	direct interaction, physical	15834155, 9341169, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SH3KBP1	Affinity Capture-MS	physical	19531213, (Europe PMC)	NA	BioGRID
SLC39A9	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
SNRPA1	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
SNX9	Affinity Capture-MS, Affinity Capture-Western, Biochemical Activity, Co-fractionation, Reconstituted Complex, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down	direct interaction, physical, physical association	15703209, 16137687, 18353773, 28514442, (Europe PMC)	0.78	BioGRID, IntAct, MINT
SRC	Affinity Capture-Western, Reconstituted Complex, surface plasmon resonance	direct interaction, physical	15834155, 19380485, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SUMO1	Co-crystal Structure, Two-hybrid	physical	15123615, (Europe PMC)	NA	BioGRID
TBC1D15	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
TBC1D2	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
TMEM9B	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
UBASH3A	Affinity Capture-Western, anti tag coimmunoprecipitation	physical, physical association	17382318, (Europe PMC)	0.40	BioGRID, IntAct, MINT
UBE2I	Two-hybrid	physical	15123615, (Europe PMC)	NA	BioGRID
ZBBX	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
AMPH	Affinity Capture-Western, Reconstituted Complex, enzyme linked immunosorbent assay, peptide array, pull down, surface plasmon resonance	direct interaction, physical	10542231, 11877424, 15834155, 17244534, 9148966, 9280305, 9341169, 9348539, (Europe PMC)	0.77	BioGRID, IntAct, MINT
APP	anti bait coimmunoprecipitation	association	16049941, (Europe PMC)	0.35	IntAct
ARRB1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	17620599, (Europe PMC)	0.35	BioGRID, IntAct
ASB13	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
BIN1	Protein-peptide, filter binding	physical, physical association	16275660, (Europe PMC)	0.40	BioGRID, IntAct
CEP126 {ECO:0000303\|PubMed:24867236,	two hybrid pooling approach	physical association	16169070, (Europe PMC)	0.37	IntAct
DNM1	Co-crystal Structure, Two-hybrid, cosedimentation in solution, cross-linking study, electron microscopy, molecular sieving, x ray scattering, x-ray crystallography	direct interaction, physical	15123615, 20428113, 20700106, 21927000, 21962517, 26302298, 7634088, (Europe PMC)	0.90	BioGRID, IntAct, MINT
DNM2	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
FNBP1	Affinity Capture-Western, Co-localization, anti tag coimmunoprecipitation, fluorescence technology, pull down	colocalization, physical, physical association	15252009, (Europe PMC)	0.58	BioGRID, IntAct
GRB2	Affinity Capture-MS, Affinity Capture-Western, Far Western, Reconstituted Complex, anti tag coimmunoprecipitation, peptide array, pull down, surface plasmon resonance	association, direct interaction, physical, physical association	10206341, 15834155, 17244534, 17474147, 19380743, 21706016, 28514442, 8119878, 9009162, (Europe PMC)	0.78	BioGRID, IntAct, MINT
HTT	two hybrid	physical association	17500595, (Europe PMC)	0.37	IntAct
IQCB1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	21565611, (Europe PMC)	0.35	BioGRID, IntAct
ITSN1	Affinity Capture-Western, Reconstituted Complex, pull down, surface plasmon resonance	direct interaction, physical	15834155, 18539136, (Europe PMC)	0.62	BioGRID, IntAct, MINT
LASP1	pull down	association	22665060, (Europe PMC)	0.35	IntAct
LRRK2	anti tag coimmunoprecipitation, confocal microscopy, two hybrid	colocalization, physical association	24282027, (Europe PMC)	0.54	IntAct
MED31	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
MYO1E	pull down	physical association	17257598, (Europe PMC)	0.40	IntAct, MINT
NCK1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, pull down	physical, physical association	10206341, 11557983, (Europe PMC)	0.52	BioGRID, IntAct
NME1	anti tag coimmunoprecipitation	physical association	20713695, (Europe PMC)	0.40	IntAct
NOS3	anti bait coimmunoprecipitation	physical association	16432212, (Europe PMC)	0.40	IntAct
NOSTRIN	anti tag coimmunoprecipitation, pull down	physical association	16234328, (Europe PMC)	0.52	IntAct, MINT
PACSIN1	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	11082044, 15252009, (Europe PMC)	0.40	BioGRID, IntAct
PIN4	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
SH3GL1	Reconstituted Complex, peptide array	direct interaction, physical	10542231, 10764144, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SH3GL2	Reconstituted Complex, surface plasmon resonance	direct interaction, physical	15834155, 9341169, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SNX33	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation	physical association	18353773, (Europe PMC)	0.52	IntAct
SNX9	Affinity Capture-MS, Affinity Capture-Western, Biochemical Activity, Co-fractionation, Reconstituted Complex, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down	direct interaction, physical, physical association	15703209, 16137687, 18353773, 28514442, (Europe PMC)	0.78	BioGRID, IntAct, MINT
SRC	Affinity Capture-Western, Reconstituted Complex, surface plasmon resonance	direct interaction, physical	15834155, 19380485, (Europe PMC)	0.44	BioGRID, IntAct, MINT
TIMM50	two hybrid pooling approach	physical association	16169070, (Europe PMC)	0.37	IntAct
UBASH3A	Affinity Capture-Western, anti tag coimmunoprecipitation	physical, physical association	17382318, (Europe PMC)	0.40	BioGRID, IntAct, MINT
UBE2DNL	two hybrid	physical association	19549727, (Europe PMC)	0.37	IntAct

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
DNM1	Co-crystal Structure, Two-hybrid, cosedimentation in solution, cross-linking study, electron microscopy, molecular sieving, x ray scattering, x-ray crystallography	direct interaction, physical	15123615, 20428113, 20700106, 21927000, 21962517, 26302298, 7634088, (Europe PMC)	0.90	BioGRID, IntAct, MINT
DNM2	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
GRB2	Affinity Capture-MS, Affinity Capture-Western, Far Western, Reconstituted Complex, anti tag coimmunoprecipitation, peptide array, pull down, surface plasmon resonance	association, direct interaction, physical, physical association	10206341, 15834155, 17244534, 17474147, 19380743, 21706016, 28514442, 8119878, 9009162, (Europe PMC)	0.78	BioGRID, IntAct, MINT
ITSN1	Affinity Capture-Western, Reconstituted Complex, pull down, surface plasmon resonance	direct interaction, physical	15834155, 18539136, (Europe PMC)	0.62	BioGRID, IntAct, MINT
MYO1E	pull down	physical association	17257598, (Europe PMC)	0.40	IntAct, MINT
NOSTRIN	anti tag coimmunoprecipitation, pull down	physical association	16234328, (Europe PMC)	0.52	IntAct, MINT
SH3GL1	Reconstituted Complex, peptide array	direct interaction, physical	10542231, 10764144, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SH3GL2	Reconstituted Complex, surface plasmon resonance	direct interaction, physical	15834155, 9341169, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SNX9	Affinity Capture-MS, Affinity Capture-Western, Biochemical Activity, Co-fractionation, Reconstituted Complex, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down	direct interaction, physical, physical association	15703209, 16137687, 18353773, 28514442, (Europe PMC)	0.78	BioGRID, IntAct, MINT
SRC	Affinity Capture-Western, Reconstituted Complex, surface plasmon resonance	direct interaction, physical	15834155, 19380485, (Europe PMC)	0.44	BioGRID, IntAct, MINT
UBASH3A	Affinity Capture-Western, anti tag coimmunoprecipitation	physical, physical association	17382318, (Europe PMC)	0.40	BioGRID, IntAct, MINT

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Interacting partner	Detection method	Interaction type	PubMed IDs	Interaction Score	Source
ADAM2	Affinity Capture-Western	physical	16049941, (Europe PMC)	NA	BioGRID
AMPH	Affinity Capture-Western, Reconstituted Complex, enzyme linked immunosorbent assay, peptide array, pull down, surface plasmon resonance	direct interaction, physical	10542231, 11877424, 15834155, 17244534, 9148966, 9280305, 9341169, 9348539, (Europe PMC)	0.77	BioGRID, IntAct, MINT
APP	anti bait coimmunoprecipitation	association	16049941, (Europe PMC)	0.35	IntAct
ARRB1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	17620599, (Europe PMC)	0.35	BioGRID, IntAct
ASB13	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
BIN1	Protein-peptide, filter binding	physical, physical association	16275660, (Europe PMC)	0.40	BioGRID, IntAct
CABIN1	Affinity Capture-Western	physical	10931822, (Europe PMC)	NA	BioGRID
CDK5	Biochemical Activity	physical	15834155, (Europe PMC)	NA	BioGRID
CDKAL1	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
CEP126	Two-hybrid	physical	16169070, (Europe PMC)	NA	BioGRID
CEP126 {ECO:0000303\|PubMed:24867236,	two hybrid pooling approach	physical association	16169070, (Europe PMC)	0.37	IntAct
CLINT1	Reconstituted Complex	physical	12429846, (Europe PMC)	NA	BioGRID
DGUOK	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
DNAAF2	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
DNM1	Co-crystal Structure, Two-hybrid, cosedimentation in solution, cross-linking study, electron microscopy, molecular sieving, x ray scattering, x-ray crystallography	direct interaction, physical	15123615, 20428113, 20700106, 21927000, 21962517, 26302298, 7634088, (Europe PMC)	0.90	BioGRID, IntAct, MINT
DNM2	Two-hybrid, two hybrid	physical, physical association	21900206, (Europe PMC)	0.37	BioGRID, IntAct, MINT
DNM3	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
DNMBP	Affinity Capture-Western, Reconstituted Complex	physical	14506234, (Europe PMC)	NA	BioGRID
DYRK1A	Affinity Capture-MS, Affinity Capture-Western, Reconstituted Complex	physical	11877424, 19722700, (Europe PMC)	NA	BioGRID
FANCD2	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
FER	Co-fractionation	physical	9722593, (Europe PMC)	NA	BioGRID
FNBP1	Affinity Capture-Western, Co-localization, anti tag coimmunoprecipitation, fluorescence technology, pull down	colocalization, physical, physical association	15252009, (Europe PMC)	0.58	BioGRID, IntAct
GRB2	Affinity Capture-MS, Affinity Capture-Western, Far Western, Reconstituted Complex, anti tag coimmunoprecipitation, peptide array, pull down, surface plasmon resonance	association, direct interaction, physical, physical association	10206341, 15834155, 17244534, 17474147, 19380743, 21706016, 28514442, 8119878, 9009162, (Europe PMC)	0.78	BioGRID, IntAct, MINT
HAX1	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
HTT	two hybrid	physical association	17500595, (Europe PMC)	0.37	IntAct
IQCB1	Affinity Capture-MS, anti tag coimmunoprecipitation	association, physical	21565611, (Europe PMC)	0.35	BioGRID, IntAct
IRF2BPL	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
ITSN1	Affinity Capture-Western, Reconstituted Complex, pull down, surface plasmon resonance	direct interaction, physical	15834155, 18539136, (Europe PMC)	0.62	BioGRID, IntAct, MINT
LASP1	pull down	association	22665060, (Europe PMC)	0.35	IntAct
LRRK2	anti tag coimmunoprecipitation, confocal microscopy, two hybrid	colocalization, physical association	24282027, (Europe PMC)	0.54	IntAct
LYPD6	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
MAP3K10	Reconstituted Complex	physical	9742220, (Europe PMC)	NA	BioGRID
MED31	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
MYO1E	pull down	physical association	17257598, (Europe PMC)	0.40	IntAct, MINT
NCK1	Affinity Capture-Western, Reconstituted Complex, anti bait coimmunoprecipitation, pull down	physical, physical association	10206341, 11557983, (Europe PMC)	0.52	BioGRID, IntAct
NCK2	Affinity Capture-Western	physical	11557983, (Europe PMC)	NA	BioGRID
NCL	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
NME1	anti tag coimmunoprecipitation	physical association	20713695, (Europe PMC)	0.40	IntAct
NOS3	anti bait coimmunoprecipitation	physical association	16432212, (Europe PMC)	0.40	IntAct
NOSTRIN	anti tag coimmunoprecipitation, pull down	physical association	16234328, (Europe PMC)	0.52	IntAct, MINT
NPM3	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
NTRK1	Affinity Capture-MS	physical	25921289, (Europe PMC)	NA	BioGRID
NUFIP1	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
PACSIN1	Affinity Capture-Western, Reconstituted Complex, anti tag coimmunoprecipitation	physical, physical association	11082044, 15252009, (Europe PMC)	0.40	BioGRID, IntAct
PACSIN2	Reconstituted Complex	physical	11082044, (Europe PMC)	NA	BioGRID
PACSIN3	Reconstituted Complex	physical	11082044, (Europe PMC)	NA	BioGRID
PIAS1	Two-hybrid	physical	15123615, (Europe PMC)	NA	BioGRID
PIN4	Two-hybrid, two hybrid pooling approach	physical, physical association	16169070, (Europe PMC)	0.37	BioGRID, IntAct
PTK2B	Affinity Capture-Western	physical	19380485, (Europe PMC)	NA	BioGRID
RPE	Co-fractionation	physical	26344197, (Europe PMC)	NA	BioGRID
SCN2B	Affinity Capture-MS	physical	26186194, 28514442, (Europe PMC)	NA	BioGRID
SH3BP4	Affinity Capture-Western, Co-localization	physical	16325581, (Europe PMC)	NA	BioGRID
SH3GL1	Reconstituted Complex, peptide array	direct interaction, physical	10542231, 10764144, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SH3GL2	Reconstituted Complex, surface plasmon resonance	direct interaction, physical	15834155, 9341169, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SH3KBP1	Affinity Capture-MS	physical	19531213, (Europe PMC)	NA	BioGRID
SLC39A9	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
SNRPA1	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
SNX33	anti bait coimmunoprecipitation, anti tag coimmunoprecipitation	physical association	18353773, (Europe PMC)	0.52	IntAct
SNX9	Affinity Capture-MS, Affinity Capture-Western, Biochemical Activity, Co-fractionation, Reconstituted Complex, anti bait coimmunoprecipitation, anti tag coimmunoprecipitation, pull down	direct interaction, physical, physical association	15703209, 16137687, 18353773, 28514442, (Europe PMC)	0.78	BioGRID, IntAct, MINT
SRC	Affinity Capture-Western, Reconstituted Complex, surface plasmon resonance	direct interaction, physical	15834155, 19380485, (Europe PMC)	0.44	BioGRID, IntAct, MINT
SUMO1	Co-crystal Structure, Two-hybrid	physical	15123615, (Europe PMC)	NA	BioGRID
TBC1D15	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
TBC1D2	Co-fractionation	physical	22863883, (Europe PMC)	NA	BioGRID
TIMM50	two hybrid pooling approach	physical association	16169070, (Europe PMC)	0.37	IntAct
TMEM9B	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID
UBASH3A	Affinity Capture-Western, anti tag coimmunoprecipitation	physical, physical association	17382318, (Europe PMC)	0.40	BioGRID, IntAct, MINT
UBE2DNL	two hybrid	physical association	19549727, (Europe PMC)	0.37	IntAct
UBE2I	Two-hybrid	physical	15123615, (Europe PMC)	NA	BioGRID
ZBBX	Affinity Capture-MS	physical	28514442, (Europe PMC)	NA	BioGRID

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DNM1