Type |
Details |
Score |
Gene |
Type: |
gene |
Organism: |
human |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
frog, western clawed |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chicken |
|
•
•
•
•
•
|
Gene |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
chimpanzee |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
cattle |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
dog, domestic |
|
•
•
•
•
•
|
Gene |
Type: |
gene |
Organism: |
macaque, rhesus |
|
•
•
•
•
•
|
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: |
2002 |
|
Title: |
Mouse Genome Informatics Computational Sequence to Gene Associations |
|
|
|
|
•
•
•
•
•
|
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: |
Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas |
Year: |
2010 |
|
Title: |
Annotation inferences using phylogenetic trees |
|
|
|
|
•
•
•
•
•
|
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 (MGI) and The National Center for Biotechnology Information (NCBI) |
Year: |
2010 |
Journal: |
Database Download |
Title: |
Consensus CDS project |
|
|
|
|
•
•
•
•
•
|
Publication |
First Author: |
Mouse Genome Informatics Group |
Year: |
2003 |
Journal: |
Database Procedure |
Title: |
Automatic Encodes (AutoE) Reference |
|
|
|
|
•
•
•
•
•
|
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 |
Year: |
2010 |
Journal: |
Database Release |
Title: |
Protein Ontology Association Load. |
|
|
|
|
•
•
•
•
•
|
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 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 |
|
•
•
•
•
•
|