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Search results 401 to 500 out of 594 for Eps15

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Type Details Score
Publication
33478555 | J:303868
First Author: Gomez K
Year: 2021
Journal: Mol Brain
Title: Non-SUMOylated CRMP2 decreases NaV1.7 currents via the endocytic proteins Numb, Nedd4-2 and Eps15.
Volume: 14
Issue: 1
Pages: 20
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Publication
23211419 | J:213895
First Author: Krieger JR
Year: 2013
Journal: Mol Cell Proteomics
Title: Identification and selected reaction monitoring (SRM) quantification of endocytosis factors associated with Numb.
Volume: 12
Issue: 2
Pages: 499-514
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Publication
10673336 | J:60728
First Author: Pohl U
Year: 2000
Journal: Genomics
Title: EHD2, EHD3, and EHD4 encode novel members of a highly conserved family of EH domain-containing proteins.
Volume: 63
Issue: 2
Pages: 255-62
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Publication
18395097 | J:136118
First Author: Niehof M
Year: 2008
Journal: Gastroenterology
Title: EPS15R, TASP1, and PRPF3 are novel disease candidate genes targeted by HNF4alpha splice variants in hepatocellular carcinomas.
Volume: 134
Issue: 4
Pages: 1191-202
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Publication
22323287 | J:197000
First Author: Morén B
Year: 2012
Journal: Mol Biol Cell
Title: EHD2 regulates caveolar dynamics via ATP-driven targeting and oligomerization.
Volume: 23
Issue: 7
Pages: 1316-29
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Publication
10336464 | J:230401
First Author: Hussain NK
Year: 1999
Journal: J Biol Chem
Title: Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells.
Volume: 274
Issue: 22
Pages: 15671-7
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Publication
27492965 | J:248798
 
First Author: Pope GR
Year: 2016
Journal: Mol Cell Endocrinol
Title: Agonist-induced internalization and desensitization of the apelin receptor.
Volume: 437
Pages: 108-119
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Publication
12121420 | J:80735
First Author: Galperin E
Year: 2002
Journal: Traffic
Title: EHD3: a protein that resides in recycling tubular and vesicular membrane structures and interacts with EHD1.
Volume: 3
Issue: 8
Pages: 575-89
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Publication
20489164 | J:175049
First Author: Gudmundsson H
Year: 2010
Journal: Circ Res
Title: EH domain proteins regulate cardiac membrane protein targeting.
Volume: 107
Issue: 1
Pages: 84-95
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Publication
22974368 | J:244766
First Author: Mate SE
Year: 2012
Journal: Skelet Muscle
Title: Eps homology domain endosomal transport proteins differentially localize to the neuromuscular junction.
Volume: 2
Issue: 1
Pages: 19
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Publication
24759929 | J:247163
First Author: Curran J
Year: 2014
Journal: Circ Res
Title: EHD3-dependent endosome pathway regulates cardiac membrane excitability and physiology.
Volume: 115
Issue: 1
Pages: 68-78
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Publication
10395801 | J:56259
First Author: Mintz L
Year: 1999
Journal: Genomics
Title: EHD1--an EH-domain-containing protein with a specific expression pattern.
Volume: 59
Issue: 1
Pages: 66-76
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Publication
14724135 | J:89391
First Author: Kierszenbaum AL
Year: 2004
Journal: Biol Reprod
Title: The acroplaxome is the docking site of Golgi-derived myosin Va/Rab27a/b- containing proacrosomal vesicles in wild-type and Hrb mutant mouse spermatids.
Volume: 70
Issue: 5
Pages: 1400-10
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Publication
37900275 | J:342260
 
First Author: Meindl K
Year: 2023
Journal: Front Cell Dev Biol
Title: A missense mutation in Ehd1 associated with defective spermatogenesis and male infertility.
Volume: 11
Pages: 1240558
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Protein
Q5SV85
Organism: Mus musculus/domesticus
Length: 1306  
Fragment?: false
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Protein
D6RIN6
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: false
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Protein
V9GXD9
Organism: Mus musculus/domesticus
Length: 1216  
Fragment?: false
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Protein
A0A1L1SRE4
Organism: Mus musculus/domesticus
Length: 94  
Fragment?: false
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Protein
V9GX40
Organism: Mus musculus/domesticus
Length: 1329  
Fragment?: false
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Protein
F6YUG5
Organism: Mus musculus/domesticus
Length: 256  
Fragment?: true
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Publication
10747088 | -
First Author: Hirst J
Year: 2000
Journal: J Cell Biol
Title: A family of proteins with gamma-adaptin and VHS domains that facilitate trafficking between the trans-Golgi network and the vacuole/lysosome.
Volume: 149
Issue: 1
Pages: 67-80
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Protein Domain
IPR008153 | GAE_dom
Type: Domain
Description: The adaptor proteins AP-1 and GGA (Golgi-localized, gamma ear-containing, ADP-ribosylation factor (ARF)-binding proteins) regulate membrane traffic betweenthe trans-Golgi network (TGN) and endosome/lysosomes through ARF-regulatedmembrane association, recognition of sorting signals, and recruitment ofclathrin and accessory proteins. The gamma-adaptin ear (GAE) domain is a C-terminal appendage or ear of about 120 residues, which is found in gamma-adaptins, the heavy subunits of the AP-1 complex, and in GGAs. The GAE domain,which is found in associated with other domains such as VHS,coiled-coils and GAT, is involved in the recruitment of accessory proteins,such as gamma-synergin, Rababptin-5, Eps15 and cyclin G-associated kinase,which modulate the functions of GAE domain containing proteins in the membranetrafficking events [, , , ].The resolution of the 3D-structure of the human gamma-adaptin GAE domain shows that it forms an immunoglobulin-like β-sandwich fold composed of eightβ-strands with two short α-helices. The topology ofthe entire GAE domain is similar to those of the N-terminal subdomains in thealpha- and beta-adaptin ear domains of the AP-2 complex. However, the GAEdomain has very low sequence identity and homology to the N-terminalimmunoglobulin-like subdomains of the alpha and beta ear domains. The bindingsite for the accessory proteins has been located to a shallow hydrophobictrough surrounded by charged (mainly basic) residues [, ].This entry represents the entire GAE domain.
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Publication
31203721 | J:339827
First Author: Wu YF
Year: 2020
Journal: Autophagy
Title: Inactivation of MTOR promotes autophagy-mediated epithelial injury in particulate matter-induced airway inflammation.
Volume: 16
Issue: 3
Pages: 435-450
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Protein
O54916
Organism: Mus musculus/domesticus
Length: 795  
Fragment?: false
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Protein
Q80XA6
Organism: Mus musculus/domesticus
Length: 647  
Fragment?: false
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Protein
F6YT69
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: true
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Protein
A0A1D5RLS1
Organism: Mus musculus/domesticus
Length: 599  
Fragment?: false
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Protein
B9EI38
Organism: Mus musculus/domesticus
Length: 648  
Fragment?: false
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Protein
Q6NZJ5
Organism: Mus musculus/domesticus
Length: 621  
Fragment?: false
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Protein
Q5JC28
Organism: Mus musculus/domesticus
Length: 793  
Fragment?: false
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Protein
Q8R0V6
Organism: Mus musculus/domesticus
Length: 296  
Fragment?: true
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Protein
D3Z6P4
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: true
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Protein
A0A1W2P7G8
Organism: Mus musculus/domesticus
Length: 175  
Fragment?: true
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Protein
Q8CJ43
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
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Protein
D3Z2E3
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: false
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Protein
F7AB82
Organism: Mus musculus/domesticus
Length: 240  
Fragment?: true
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Protein
A0A338P6L8
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
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Protein
Q8CJ62
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: true
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Protein
F6R6F1
Organism: Mus musculus/domesticus
Length: 755  
Fragment?: true
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Protein
Q3UHF8
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: false
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Protein
E9Q632
Organism: Mus musculus/domesticus
Length: 768  
Fragment?: false
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Protein
Q3U2A1
Organism: Mus musculus/domesticus
Length: 611  
Fragment?: true
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Protein
Q3UHE9
Organism: Mus musculus/domesticus
Length: 458  
Fragment?: true
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Protein
A0A338P6K7
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
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Protein
Q3TQ85
Organism: Mus musculus/domesticus
Length: 674  
Fragment?: true
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Protein
A0A1W2P775
Organism: Mus musculus/domesticus
Length: 712  
Fragment?: true
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Protein
Q60902
Organism: Mus musculus/domesticus
Length: 907  
Fragment?: false
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Protein
H3BK65
Organism: Mus musculus/domesticus
Length: 933  
Fragment?: false
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Protein
Q80ZL3
Organism: Mus musculus/domesticus
Length: 897  
Fragment?: false
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Protein
F6W2Q5
Organism: Mus musculus/domesticus
Length: 764  
Fragment?: false
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Protein
Q9QXY6
Organism: Mus musculus/domesticus
Length: 535  
Fragment?: false
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Protein
Q9WVK4
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Publication
24508342 | J:222668
First Author: Shah C
Year: 2014
Journal: Structure
Title: Structural insights into membrane interaction and caveolar targeting of dynamin-like EHD2.
Volume: 22
Issue: 3
Pages: 409-420
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Protein
Q8BH64
Organism: Mus musculus/domesticus
Length: 543  
Fragment?: false
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Protein
Q9EQP2
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
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Protein
Q8VD37
Organism: Mus musculus/domesticus
Length: 806  
Fragment?: false
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Protein
Q3TWP9
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
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Protein
Q3TIT3
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
Q1MWP9
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: true
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Protein
Q3TGS1
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
Q3TUW9
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Protein
Q1MWP8
Organism: Mus musculus/domesticus
Length: 544  
Fragment?: true
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Protein
F7CPX0
Organism: Mus musculus/domesticus
Length: 575  
Fragment?: true
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Protein
Q3TCK3
Organism: Mus musculus/domesticus
Length: 485  
Fragment?: true
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Protein
Q91VL7
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
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Protein
Q8R2X0
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
Q8K1X5
Organism: Mus musculus/domesticus
Length: 548  
Fragment?: true
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Protein
Q3TM70
Organism: Mus musculus/domesticus
Length: 541  
Fragment?: false
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Protein
Q80ZZ0
Organism: Mus musculus/domesticus
Length: 534  
Fragment?: false
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Publication
10412903 | -
First Author: Panavas T
Year: 1999
Journal: Plant Mol Biol
Title: Identification of senescence-associated genes from daylily petals.
Volume: 40
Issue: 2
Pages: 237-48
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Publication
18202664 | -
First Author: Roll-Mecak A
Year: 2008
Journal: Nature
Title: Structural basis of microtubule severing by the hereditary spastic paraplegia protein spastin.
Volume: 451
Issue: 7176
Pages: 363-7
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Publication
12676568 | -
First Author: Ciccarelli FD
Year: 2003
Journal: Genomics
Title: The identification of a conserved domain in both spartin and spastin, mutated in hereditary spastic paraplegia.
Volume: 81
Issue: 4
Pages: 437-41
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Publication
23439121 | -
First Author: Nahm M
Year: 2013
Journal: Neuron
Title: Spartin regulates synaptic growth and neuronal survival by inhibiting BMP-mediated microtubule stabilization.
Volume: 77
Issue: 4
Pages: 680-95
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Publication
19713939 | J:154720
First Author: Reider A
Year: 2009
Journal: EMBO J
Title: Syp1 is a conserved endocytic adaptor that contains domains involved in cargo selection and membrane tubulation.
Volume: 28
Issue: 20
Pages: 3103-16
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Publication
24296571 | -
First Author: Verhelst J
Year: 2013
Journal: Microbiol Mol Biol Rev
Title: Mx proteins: antiviral gatekeepers that restrain the uninvited.
Volume: 77
Issue: 4
Pages: 551-66
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Publication
23223037 | -
First Author: Kurashima K
Year: 2013
Journal: Eukaryot Cell
Title: A uvs-5 strain is deficient for a mitofusin gene homologue, fzo1, involved in maintenance of long life span in Neurospora crassa.
Volume: 12
Issue: 2
Pages: 233-43
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Publication
21502136 | -
First Author: Cohen MM
Year: 2011
Journal: J Cell Sci
Title: Sequential requirements for the GTPase domain of the mitofusin Fzo1 and the ubiquitin ligase SCFMdm30 in mitochondrial outer membrane fusion.
Volume: 124
Issue: Pt 9
Pages: 1403-10
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Publication
23994470 | -
First Author: Ozaki S
Year: 2013
Journal: Cell Rep
Title: A replicase clamp-binding dynamin-like protein promotes colocalization of nascent DNA strands and equipartitioning of chromosomes in E. coli.
Volume: 4
Issue: 5
Pages: 985-95
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Publication
20970992 | -
First Author: Low HH
Year: 2010
Journal: Curr Opin Struct Biol
Title: Dynamin architecture--from monomer to polymer.
Volume: 20
Issue: 6
Pages: 791-8
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Publication
20064379 | -
First Author: Low HH
Year: 2009
Journal: Cell
Title: Structure of a bacterial dynamin-like protein lipid tube provides a mechanism for assembly and membrane curving.
Volume: 139
Issue: 7
Pages: 1342-52
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Protein Domain
IPR030381 | G_DYNAMIN_dom
Type: Domain
Description: This entry represents the dynamin-type guanine nucleotide-binding (G) domain. Members of the dynamin GTPase family appear to be ubiquitous. They catalyze diverse membrane remodelling events in endocytosis, cell division, and plastid maintenance. Their functional versatility also extends to other core cellular processes, such as maintenance of cell shape or centrosome cohesion. Members of the dynamin family are characterised by their common structure and by conserved sequences in the GTP-binding domain. The minimal distinguishing architectural features that are common to all dynamins and are distinct from other GTPases are the structure of the large GTPase domain (~280 amino acids) and the presence of two additional domains: the middle domain and the GTPase effector domain (GED), which are involved in oligomerization and regulation of the GTPase activity. In many dynamin family members, the basic set of domains is supplemented by targeting domains, such as: pleckstrin-homology (PH) domain, proline-rich domains (PRDs), or by sequences that target dynamins to specific organelles, such as mitochondria and chloroplasts [, , ]. The dynamin-type G domain consists of a central eight-stranded β-sheetsurrounded by seven alpha helices and two one-turn helices.It contains the five canonical guanine nucleotide binding motifs (G1-5). TheP-loop (G1) motif (GxxxxGKS/T) is also present in ATPases (Walker A motif) andfunctions as a coordinator of the phosphate groups of the bound nucleotide. Aconserved threonine in switch-I (G2) and the conserved residues DxxG ofswitch-II (G3) are involved in Mg(2+) binding and GTP hydrolysis. Thenucleotide binding affinity of dynamins is typically low, with specificity forGTP provided by the mostly conserved N/TKxD motif (G4). The G5 or G-cap motifis involved in binding the ribose moiety [, , ].Some proteins containing a dynamin-type G domain are listed below [, ]:Animal dynamin, the prototype for this family. The role of dynamin inendocytosis is well established. Additional roles were proposed in vesiclebudding from the trans-Golgi network (TGN) and the budding of caveolae fromthe plasma membrane [].Vetebrate Mx proteins, a group of interferon (IFN)-induced GTPases involvedin the control of intracellular pathogens [, ].Eukaryotic Drp1 (Dnm1 in yeast) mediates mitochondrial and peroxisomalfission.Eukaryotic Eps15 homology (EH)-domain-containing proteins (EHDs), ATPasesimplicated in clathrin-independent endocytosis and recycling fromendosomes. The dynamin-type G domains of EHDs bind to adenine rather thanto guanine nucleotide [, ].Yeast to human OPA1/Mgm1 proteins. They are found between the inner andouter mitochondrial membranes and are involved in mitochondrial fusion.Yeast to human mitofusin/fuzzy onions 1 (Fzo1) proteins, involved inmitochondrial dynamics [, ].Yeast vacuolar protein sorting-associated protein 1 (Vps1), involved invesicle trafficking from the Golgi.Escherichia coli clamp-binding protein CrfC (or Yjda), important for thecolocalization of sister nascent DNA strands after replication fork passageduring DNA replication, and for positioning and subsequent partitioning ofsister chromosomes [].Nostoc punctiforme bacterial dynamin-like protein (BDLP) [, ].
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Protein
Q9Z0R6
Organism: Mus musculus/domesticus
Length: 1659  
Fragment?: false
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Protein
E9QNG1
Organism: Mus musculus/domesticus
Length: 1658  
Fragment?: false
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Protein
Q80TG5
Organism: Mus musculus/domesticus
Length: 1539  
Fragment?: true
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Protein
B2RR82
Organism: Mus musculus/domesticus
Length: 1685  
Fragment?: false
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Publication
10702286 | -
First Author: Poussu A
Year: 2000
Journal: J Biol Chem
Title: Vear, a novel Golgi-associated protein with VHS and gamma-adaptin "ear" domains.
Volume: 275
Issue: 10
Pages: 7176-83
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Protein
E9Q3I5
Organism: Mus musculus/domesticus
Length: 1218  
Fragment?: false
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Protein
E9Q3I9
Organism: Mus musculus/domesticus
Length: 1147  
Fragment?: false
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Protein
Q3V3Y8
Organism: Mus musculus/domesticus
Length: 746  
Fragment?: false
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Protein
E9Q3I4
Organism: Mus musculus/domesticus
Length: 1176  
Fragment?: false
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Protein
E9Q3I8
Organism: Mus musculus/domesticus
Length: 1142  
Fragment?: false
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Protein
Q8BZ60
Organism: Mus musculus/domesticus
Length: 895  
Fragment?: false
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Protein
Q8R1X6
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
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Protein
D3Z3F8
Organism: Mus musculus/domesticus
Length: 582  
Fragment?: false
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Protein
Q3TVW1
Organism: Mus musculus/domesticus
Length: 671  
Fragment?: false
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Protein
E9PXP7
Organism: Mus musculus/domesticus
Length: 898  
Fragment?: false
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Publication
14708007 | -
First Author: Bonifacino JS
Year: 2004
Journal: Nat Rev Mol Cell Biol
Title: The GGA proteins: adaptors on the move.
Volume: 5
Issue: 1
Pages: 23-32
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Protein Domain
IPR013037 | Clathrin_b-adaptin_app_Ig-like
Type: Homologous_superfamily
Description: Proteins synthesized on the ribosome and processed in the endoplasmic reticulum are transported from the Golgi apparatus to the trans-Golgi network (TGN), and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins (such as clathrin or coatomer) that are important for cargo selection and direction of transport []. Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The two major types of clathrin adaptor complexes are the heterotetrameric adaptor protein (AP) complexes, and the monomeric GGA (Golgi-localising, Gamma-adaptin ear domain homology, ARF-binding proteins) adaptors [, ].AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and lipids to clathrin at vesicle budding sites, as well as binding accessory proteins that regulate coat assembly and disassembly (such as AP180, epsins and auxilin). There are different AP complexes in mammals. AP1 is responsible for the transport of lysosomal hydrolases between the TGN and endosomes []. AP2 associates with the plasma membrane and is responsible for endocytosis []. AP3 is responsible for protein trafficking to lysosomes and other related organelles []. AP4 is less well characterised. AP complexes are heterotetramers composed of two large subunits (adaptins), a medium subunit (mu) and a small subunit (sigma). For example, in AP1 these subunits are gamma-1-adaptin, beta-1-adaptin, mu-1 and sigma-1, while in AP2 they are alpha-adaptin, beta-2-adaptin, mu-2 and sigma-2. Each subunit has a specific function. Adaptins recognise and bind to clathrin through their hinge region (clathrin box), and recruit accessory proteins that modulate AP function through their C-terminal ear (appendage) domains. Mu recognises tyrosine-based sorting signals within the cytoplasmic domains of transmembrane cargo proteins []. One function of clathrin and AP2 complex-mediated endocytosis is to regulate the number of GABA(A) receptors available at the cell surface []. This entry represents a β-sandwich structural motif found in the appendage (ear) domain of gamma1-adaptin from AP1 clathrin adaptor complex, and the homologous C-terminal GAE (gamma-adaptin ear) domain of GGA adaptor proteins. These domains have an immunoglobulin-like β-sandwich fold containing 8 strands in 2 β-sheets in a Greek key topology [, ]. This is a similar fold to that found in alpha- and beta-adaptins, but there is little sequence identity between them. The GAE domain is involved in the recruitment of accessory proteins, such as gamma-synergin, Rababptin-5, Eps15 and cyclin G-associated kinase, which modulate the functions of GAE domain containing proteins in the membrane trafficking events [, ]. The binding site in GAE for accessory proteins is located in a shallow hydrophobic trough surrounded by charged (mainly basic) residues [].
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Publication
12042876 | -
First Author: Nogi T
Year: 2002
Journal: Nat Struct Biol
Title: Structural basis for the accessory protein recruitment by the gamma-adaptin ear domain.
Volume: 9
Issue: 7
Pages: 527-31
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Protein
Q811U4
Organism: Mus musculus/domesticus
Length: 741  
Fragment?: false
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