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Search results 1 to 100 out of 116 for Shd

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0.035s
Type Details Score
Gene
Type: gene
Organism: human
Gene
Type: gene
Organism: cattle
Gene
Type: gene
Organism: dog, domestic
Gene
Type: gene
Organism: macaque, rhesus
Gene
Type: gene
Organism: frog, western clawed
Gene
Type: gene
Organism: chicken
Gene
Type: gene
Organism: rat
Gene
Type: gene
Organism: chimpanzee
Protein Domain
Type: Family
Description: SHD (SH2 domain-containing adapter protein D) is thought to act as an adapter protein in the central nervous system. SHD contains five YXXP motifs, a substrate sequence preferred by Abl tyrosine kinases, in addition to a proline-rich region and a C-terminal SH2 domain [].
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Oda T
Year: 1997
Journal: Oncogene
Title: Identification and characterization of two novel SH2 domain-containing proteins from a yeast two hybrid screen with the ABL tyrosine kinase.
Volume: 15
Issue: 11
Pages: 1255-62
Protein
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: false
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus caroli
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication
First Author: Ritter N
Year: 2019
Journal: Dev Cell
Title: The lncRNA Locus Handsdown Regulates Cardiac Gene Programs and Is Essential for Early Mouse Development.
Volume: 50
Issue: 5
Pages: 644-657.e8
Publication
First Author: Chern T
Year: 2022
Journal: Nat Commun
Title: Mutations in Hcfc1 and Ronin result in an inborn error of cobalamin metabolism and ribosomopathy.
Volume: 13
Issue: 1
Pages: 134
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Function or Process or Component Unknown following Literature Review
Publication      
First Author: Lennon G
Year: 1999
Journal: Database Download
Title: WashU-HHMI Mouse EST Project
Publication      
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
Publication
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
Publication
First Author: Carninci P
Year: 2005
Journal: Science
Title: The transcriptional landscape of the mammalian genome.
Volume: 309
Issue: 5740
Pages: 1559-63
Publication        
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
Publication      
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
Publication
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
Publication      
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
Publication        
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
Publication      
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
Publication        
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
Publication      
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
Publication      
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
Publication      
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
Publication      
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
Publication      
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
Publication      
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
Author
Publication  
First Author: Francis WR
Year: 2017
Journal: PeerJ
Title: Symplectin evolved from multiple duplications in bioluminescent squid.
Volume: 5
Pages: e3633
Publication
First Author: Kuroda TS
Year: 2002
Journal: J Biol Chem
Title: The Slp homology domain of synaptotagmin-like proteins 1-4 and Slac2 functions as a novel Rab27A binding domain.
Volume: 277
Issue: 11
Pages: 9212-8
Publication
First Author: Kuroda TS
Year: 2002
Journal: Biochem Biophys Res Commun
Title: Synaptotagmin-like protein 5: a novel Rab27A effector with C-terminal tandem C2 domains.
Volume: 293
Issue: 3
Pages: 899-906
Protein Domain
Type: Domain
Description: This entry represents the SH2 domain of SHD.SHD (SH2 domain-containing adapter protein D) is thought to act as an adapter protein in the central nervous system. SHD contains five YXXP motifs, a substrate sequence preferred by Abl tyrosine kinases, in addition to a proline-rich region and a C-terminal SH2 domain [].
Protein Domain
Type: Domain
Description: Human stonins, like their Drosophila homologue stoned B, are supposed to beendocytotic proteins involved in clathrin-mediated endocytosis at synapses.The two human stonins, as well as their Drosophila melanogaster (Fruit fly) and Caenorhabditis elegans homologues, exhibit a modular structure consisting ofan N-terminal proline- and serine-rich domain, a central stonin homologydomain (SHD), and a C-terminal domain homologous to the signal-binding domainof the mu subunits of adaptor protein (AP) complexes (mu-homology domain). The ~140 amino-acid SHD domain has not been described in other proteins and may thus be unique to members of the stonin family. Its function is not yet known [, ].
Publication  
First Author: Lyakhova TA
Year: 2014
Journal: Chem Phys Lipids
Title: The C2 domains of granuphilin are high-affinity sensors for plasma membrane lipids.
Volume: 182
Pages: 29-37
Protein Domain
Type: Domain
Description: Synaptotagmin-like proteins (Slps) contain a N-terminal RabBD (Rab-binding) domain and two C-terminal C2 domains, C2A and C2B []. The characteristic feature of the Slp family is the N-terminal domain (referred to as SHD for Slp Homology Domain), which is not found in other C-type tandem C2 proteins []. SHD functions as a specific Rab27A/B-binding domain []. This entry represents the C2B domain. The C2 domain is a Ca2+-dependent membrane-targeting module found in many cellular proteins involved in signal transduction or membrane trafficking. C2 domains are unique among membrane targeting domains in that they show wide range of lipid selectivity for the major components of cell membranes, including phosphatidylserine and phosphatidylcholine. This C2 domain is about 116 amino-acid residues and is located between the two copies of the C1 domain in Protein Kinase C and the protein kinase catalytic domain []. Regions with significant homology []to the C2-domain have been found in many proteins. The C2 domain is thought to be involved in calcium-dependent phospholipid binding []and in membrane targetting processes such as subcellular localisation. The 3D structure of the C2 domain of synaptotagmin has been reported[], the domain forms an eight-stranded β-sandwich constructed around a conserved 4-stranded motif, designated a C2 key []. Calcium binds in a cup-shaped depression formed by the N- and C-terminal loops of the C2-key motif. Structural analyses of several C2 domains have shown them to consist of similar ternary structures in which three Ca2+-binding loops are located at the end of an 8 stranded antiparallel β-sandwich.
Protein Domain
Type: Domain
Description: Synaptotagmin-like proteins (Slps) contain a N-terminal RabBD (Rab-binding) domain and two C-terminal C2 domains, C2A and C2B []. The characteristic feature of the Slp family is the N-terminal domain (referred to as SHD for Slp Homology Domain), which is not found in other C-type tandem C2 proteins []. SHD functions as a specific Rab27A/B-binding domain []. The C2B domain of Slp4 (also known as Granuphilin) interact with the plasma membrane lipid phosphatidylinositol-(4,5)-bisphosphate [PI(4,5)P2][]. C2 domains fold into an 8-standed β-sandwich that can adopt 2 structural arrangements, type I and type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin andintersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions [, , , , , , , ].
Publication
First Author: Holt O
Year: 2008
Journal: Traffic
Title: Slp1 and Slp2-a localize to the plasma membrane of CTL and contribute to secretion from the immunological synapse.
Volume: 9
Issue: 4
Pages: 446-57
Publication
First Author: Moog-Lutz C
Year: 1997
Journal: Int J Cancer
Title: MLN64 exhibits homology with the steroidogenic acute regulatory protein (STAR) and is over-expressed in human breast carcinomas.
Volume: 71
Issue: 2
Pages: 183-91
Publication
First Author: Grewal PK
Year: 1997
Journal: Mamm Genome
Title: The mouse homolog of FRG1, a candidate gene for FSHD, maps proximal to the myodystrophy mutation on chromosome 8.
Volume: 8
Issue: 6
Pages: 394-8
Publication
First Author: Izumi T
Year: 2003
Journal: Cell Struct Funct
Title: The roles of Rab27 and its effectors in the regulated secretory pathways.
Volume: 28
Issue: 5
Pages: 465-74
Publication
First Author: Fukuda M
Year: 2003
Journal: J Biol Chem
Title: Slp4-a/granuphilin-a inhibits dense-core vesicle exocytosis through interaction with the GDP-bound form of Rab27A in PC12 cells.
Volume: 278
Issue: 17
Pages: 15390-6
Publication
First Author: Wang J
Year: 1999
Journal: J Biol Chem
Title: Novel rabphilin-3-like protein associates with insulin-containing granules in pancreatic beta cells.
Volume: 274
Issue: 40
Pages: 28542-8
Publication
First Author: Tsuboi T
Year: 2006
Journal: Mol Biol Cell
Title: The Slp4-a linker domain controls exocytosis through interaction with Munc18-1.syntaxin-1a complex.
Volume: 17
Issue: 5
Pages: 2101-12
Publication
First Author: Kukimoto-Niino M
Year: 2008
Journal: Structure
Title: Structural basis for the exclusive specificity of Slac2-a/melanophilin for the Rab27 GTPases.
Volume: 16
Issue: 10
Pages: 1478-90
Publication
First Author: Nagashima K
Year: 2002
Journal: FEBS Lett
Title: Melanophilin directly links Rab27a and myosin Va through its distinct coiled-coil regions.
Volume: 517
Issue: 1-3
Pages: 233-8
Publication
First Author: Oberhofer A
Year: 2017
Journal: Proc Natl Acad Sci U S A
Title: Myosin Va's adaptor protein melanophilin enforces track selection on the microtubule and actin networks in vitro.
Volume: 114
Issue: 24
Pages: E4714-E4723
Protein Domain
Type: Domain
Description: Synaptotagmin-like protein 4 (SYTL4, Slp4), also known as granuphilin or exophilin-2, belongs to the synaptotagmin-like protein family (Slp), which is a group of putative membrane trafficking proteins []. The characteristic feature of the Slp family is the N-terminal Slp homology domain (SHD), which functions as a Rab27-binding domain and C-terminal tandem C2 domains (known as the C2A domain and C2B domain), putative Ca2+-binding motifs [, ]. SHD consists of two conserved regions, designated SHD1 and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of Slp4 are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.There are several alternatively spliced isoform of Slp4. Slp4-a (granuphilin-a) has two C2 domains, whereas Slp4-b (granuphilin-b) contains only the first C2 domain. Expression of Slp4-a inhibits regulated secretion in endocrine cells. Slp4-a binds to both the GTP- and GDP-bound forms of Rab27A and inhibits a specific GTP/GDP exchange cycle required for dense-core vesicle exocytosis []. Slp4 has been detected in the pancreatic islet, in particular in insulin-positive beta cells, and in pituitary []. This entry represents the FYVE-related domain of synaptotagmin-like protein 4.
Protein Domain
Type: Family
Description: Synaptotagmin-like protein 4 (SYTL4, Slp4), also known as granuphilin or exophilin-2, belongs to the synaptotagmin-like protein family (Slp), which is a group of putative membrane trafficking proteins []. The characteristic feature of the Slp family is the N-terminal Slp homology domain (SHD), which functions as a Rab27-binding domain and C-terminal tandem C2 domains (known as the C2A domain and C2B domain), putative Ca2+-binding motifs [, ]. SHD consists of two conserved regions, designated SHD1 and SHD2, which may function as protein interaction sites. The SHD1 and SHD2 of Slp4 are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif.There are several alternatively spliced isoform of Slp4. Slp4-a (granuphilin-a) has two C2 domains, whereas Slp4-b (granuphilin-b) contains only the first C2 domain. Expression of Slp4-a inhibits regulated secretion in endocrine cells. Slp4-a binds to both the GTP- and GDP-bound forms of Rab27A and inhibits a specific GTP/GDP exchange cycle required for dense-core vesicle exocytosis []. Slp4 has been detected inthe pancreatic islet, in particular in insulin-positive beta cells, and in pituitary [].
Protein Domain
Type: Domain
Description: Melanophilin, also termed SlaC2-a, or exophilin-3, is a GTP-bound form of Rab27A-, myosin Va-, and actin-binding protein present on melanosomes. It is involved in the control of transferring of melanosomes from microtubules to actin filaments. It also functions as a melanocyte type myosin Va (McM5) binding partner and directly activates the actin-activated ATPase activity of McM5 through forming a tripartite protein complex with Rab27A and an actin-based motor myosin Va [,]. SlaC2-a belongs to the Slp homologue lacking C2 domains (Slac2) family. It contains an N-terminal Slp homology domain (SHD), but lacks tandem C2 domains. The SHD consists of two conserved regions, designated SHD1 (Slp homology domain 1) and SHD2, which may function as protein interaction sites []. The SHD1 and SHD2 of SlaC2-a are separated by a putative FYVE zinc finger, which resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif. Moreover, Slac2-a has a middle myosin-binding domain and a C-terminal actin-binding domain [].
Protein
Organism: Mus musculus/domesticus
Length: 673  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 673  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 753  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 753  
Fragment?: false
Publication
First Author: Martina JA
Year: 2001
Journal: J Cell Biol
Title: Stonin 2: an adaptor-like protein that interacts with components of the endocytic machinery.
Volume: 153
Issue: 5
Pages: 1111-20
Publication
First Author: Walther K
Year: 2004
Journal: Proc Natl Acad Sci U S A
Title: Functional dissection of the interactions of stonin 2 with the adaptor complex AP-2 and synaptotagmin.
Volume: 101
Issue: 4
Pages: 964-9
Publication
First Author: Li C
Year: 1995
Journal: Nature
Title: Ca(2+)-dependent and -independent activities of neural and non-neural synaptotagmins.
Volume: 375
Issue: 6532
Pages: 594-9
Protein
Organism: Mus musculus/domesticus
Length: 567  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 407  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1280  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 503  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 568  
Fragment?: false
Publication
First Author: Davletov BA
Year: 1993
Journal: J Biol Chem
Title: A single C2 domain from synaptotagmin I is sufficient for high affinity Ca2+/phospholipid binding.
Volume: 268
Issue: 35
Pages: 26386-90
Publication  
First Author: Farah CA
Year: 2012
Journal: Adv Exp Med Biol
Title: The role of C2 domains in PKC signaling.
Volume: 740
Pages: 663-83
Protein
Organism: Mus musculus/domesticus
Length: 895  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 730  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 898  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 746  
Fragment?: false
Publication
First Author: Sutton RB
Year: 1995
Journal: Cell
Title: Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold.
Volume: 80
Issue: 6
Pages: 929-38
Protein
Organism: Mus musculus/domesticus
Length: 950  
Fragment?: false