| Type |
Details |
Score |
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
101
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
116
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
116
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
99
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
113
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
98
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
116
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
100
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
118
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
117
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
100
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
116
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
98
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
115
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
105
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
116
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
117
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
117
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
131
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
106
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
100
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
116
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
118
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
99
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
117
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
117
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
114
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
117
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
117
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
116
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
99
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
117
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
119
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
120
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Vyas P |
| Year: |
2000 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Inositol polyphosphate 4-phosphatase type I regulates cell growth downstream of transcription factor GATA-1. |
| Volume: |
97 |
| Issue: |
25 |
| Pages: |
13696-701 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sasaki J |
| Year: |
2010 |
| Journal: |
Nature |
| Title: |
The PtdIns(3,4)P(2) phosphatase INPP4A is a suppressor of excitotoxic neuronal death. |
| Volume: |
465 |
| Issue: |
7297 |
| Pages: |
497-501 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cao P |
| Year: |
2011 |
| Journal: |
Cell |
| Title: |
Activity-dependent IGF-1 exocytosis is controlled by the Ca(2+)-sensor synaptotagmin-10. |
| Volume: |
145 |
| Issue: |
2 |
| Pages: |
300-11 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fukuda M |
| Year: |
2002 |
| Journal: |
Biochem J |
| Title: |
The C2A domain of synaptotagmin-like protein 3 (Slp3) is an atypical calcium-dependent phospholipid-binding machine: comparison with the C2A domain of synaptotagmin I. |
| Volume: |
366 |
| Issue: |
Pt 2 |
| Pages: |
681-7 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
306
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
65
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
678
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
679
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
679
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
300
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
690
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
633
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
809
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
690
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Millar AA |
| Year: |
1999 |
| Journal: |
Plant Cell |
| Title: |
CUT1, an Arabidopsis gene required for cuticular wax biosynthesis and pollen fertility, encodes a very-long-chain fatty acid condensing enzyme. |
| Volume: |
11 |
| Issue: |
5 |
| Pages: |
825-38 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Joubès J |
| Year: |
2008 |
| Journal: |
Plant Mol Biol |
| Title: |
The VLCFA elongase gene family in Arabidopsis thaliana: phylogenetic analysis, 3D modelling and expression profiling. |
| Volume: |
67 |
| Issue: |
5 |
| Pages: |
547-66 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kim J |
| Year: |
2013 |
| Journal: |
Plant Physiol |
| Title: |
Arabidopsis 3-ketoacyl-coenzyme a synthase9 is involved in the synthesis of tetracosanoic acids as precursors of cuticular waxes, suberins, sphingolipids, and phospholipids. |
| Volume: |
162 |
| Issue: |
2 |
| Pages: |
567-80 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Lepore BW |
| Year: |
2005 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
The x-ray crystal structure of lysine-2,3-aminomutase from Clostridium subterminale. |
| Volume: |
102 |
| Issue: |
39 |
| Pages: |
13819-24 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Smith R |
| Year: |
2007 |
| Journal: |
J Neurochem |
| Title: |
Loss of SNAP-25 and rabphilin 3a in sensory-motor cortex in Huntington's disease. |
| Volume: |
103 |
| Issue: |
1 |
| Pages: |
115-23 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dalfó E |
| Year: |
2004 |
| Journal: |
Neurobiol Dis |
| Title: |
Abnormal alpha-synuclein interactions with rab3a and rabphilin in diffuse Lewy body disease. |
| Volume: |
16 |
| Issue: |
1 |
| Pages: |
92-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Tan MG |
| Year: |
2014 |
| Journal: |
Neurochem Int |
| Title: |
Decreased rabphilin 3A immunoreactivity in Alzheimer's disease is associated with Aβ burden. |
| Volume: |
64 |
|
| Pages: |
29-36 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kurowska M |
| Year: |
2012 |
| Journal: |
Blood |
| Title: |
Terminal transport of lytic granules to the immune synapse is mediated by the kinesin-1/Slp3/Rab27a complex. |
| Volume: |
119 |
| Issue: |
17 |
| Pages: |
3879-89 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Welander PV |
| Year: |
2010 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Identification of a methylase required for 2-methylhopanoid production and implications for the interpretation of sedimentary hopanes. |
| Volume: |
107 |
| Issue: |
19 |
| Pages: |
8537-42 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kerr FK |
| Year: |
2005 |
| Journal: |
J Biol Chem |
| Title: |
Elucidation of the substrate specificity of the C1s protease of the classical complement pathway. |
| Volume: |
280 |
| Issue: |
47 |
| Pages: |
39510-4 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Arlaud GJ |
| Year: |
1993 |
| Journal: |
Methods Enzymol |
| Title: |
Human complement serine proteases C1r and C1s and their proenzymes. |
| Volume: |
223 |
|
| Pages: |
61-82 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kofuji S |
| Year: |
2015 |
| Journal: |
Cancer Discov |
| Title: |
INPP4B Is a PtdIns(3,4,5)P3 Phosphatase That Can Act as a Tumor Suppressor. |
| Volume: |
5 |
| Issue: |
7 |
| Pages: |
730-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rynkiewicz NK |
| Year: |
2012 |
| Journal: |
Adv Biol Regul |
| Title: |
INPP4A/INPP4B and P-Rex proteins: related but different? |
| Volume: |
52 |
| Issue: |
1 |
| Pages: |
265-79 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
In humans, Rabphilin-3A (RPH3A) contains two C2 domains and one RabBD (Rab-binding) domain. RPH3A may interact with the SNARE complex and regulate synaptic vesicle exocytosis and Ca2+-triggered neurotransmitter release []. It has been linked to neurodegenerative diseases, such as Huntington's disease [], Lewy body disease []and Alzheimer's disease []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Synaptotagmin-like protein 5 (SYTL5, also known as Slp5) belongs to the synaptotagmin-like protein family, which contains a N-terminal RabBD (Rab-binding) domain and two C-terminal C2 domains. Slp5 interacts with the GTP-bound form of Rab27A both in vitro and in intact cells. It is highly expressed in human placenta and liver. It may be involved in Rab27A-dependent membrane trafficking in specific tissues []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Synaptotagmin-like protein 3 (SYTL3, also known as Slp3) belongs to the synaptotagmin-like protein family, which contains a N-terminal RabBD (Rab-binding) domain and two C-terminal C2 domains. Slp3 binds phospholipids in the presence of calcium ions []. In mouse cytotoxic T lymphocytes, Slp3 is an effector of Rab27a and interacts with kinesin-1 through the tetratricopeptide repeat of the kinesin-1 light chain []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Synaptotagmin-10 (SYT10) belongs to the synaptotagmin family, which is a group of membrane-trafficking proteins that contain two C-terminal C2 domains. Most of the synaptotagmins have a unique N-terminal domain that is involved in membrane anchoring or specific ligand binding. SYT10 localises to olfactory bulb and controls the Ca(2+)-dependent exocytosis that is spatially and temporally distinct from Ca(2+)-dependent synaptic vesicle exocytosis controlled by SYT1 []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry includes the serine endopeptidase complement C1s subcomponent (MEROPS identifier S01.193). C1s has trypsin-like specificity and activates the precursors of complement components C2 and C4 [, ]. It is inhibited by C1 inhibitor []. C1s is calcium-dependent and in the golden hamster is known as calcium-dependent serine proteinase. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This group represents 3-ketoacyl-CoA synthases (KCSs) from plants [, ]. They are also known as very long-chain fatty acid (VLCFA) condensing enzymes, and they catalyse the first committed step during the fatty acid elongation process, which is the condensation of C2 units to acyl-CoA. Arabidopsis contains 21 KCS members []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The ferlin gene family are characterised by multiple tandem C2 domains and a C-terminal transmembrane domain. They are found in a wide range of species and their function remains unknown, however, mutations in its two most well-characterised members, dysferlin and otoferlin, have been implicated in human disease [].This is central domain B in proteins of the Ferlin family []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The ferlin gene family are characterised by multiple tandem C2 domains and a C-terminal transmembrane domain. They are found in a wide range of species and their function remains unknown, however, mutations in its two most well-characterised members, dysferlin and otoferlin, have been implicated in human disease [].This is central domain A in proteins of the Ferlin family []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
The enzyme in this family is involved in the C2 methylation of bacterial hopanoids. Although the reaction is shown with methylcobalamin acting as the methyl donor, it is possible that SAM might be the methyl donor for the reaction (because this is another function of the SAM cofactor) []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
This domain is found near to the N terminus of some dedicator of cytokinesis (DOCK) proteins, between the variant SH3 domain and the C2 domain []. This is an α-helical region that mediates interactions with ELMO subunits and provides a major site for interactions between the SH3 and ARM domains of these proteins []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
The mycobacterial members of this family are expressed from part of the ergothioneine biosynthetic gene cluster. EGTD is the histidine methyltransferase that transfers three methyl groups to the alpha-amino moiety of histidine, in the first stage of the production of this histidine betaine derivative that carries a thiol group attached to the C2 atom of an imidazole ring []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry includes INPP4A and INPP4B. They are inositol lipid 4-phosphatases that hydrolyze PtdIns(3,4)P2, a phosphoinositide generated by PI3K signaling [, ]. They contain a C2 domain in their N termini and a phosphatase domain at their C termini. INPP4A is a suppressor of glutamate excitotoxicity in the central nervous system [], while INPP4B acts as a tumour suppressor []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
L-amino-acid ligases are ATP-grasp superfamily enzymes that catalyze the formation of an alpha-peptide bond between two l-amino acids in an ATP-dependent manner. They share a common structural architecture that consists of three domains referred to as the A-domain, B-domain and C-domain. The C domain can be further divided into the C1-subdomain and the C2-subdomain []. This entry represents the C2 subdomain. |
|
•
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| Protein Domain |
| Type: |
Domain |
| Description: |
This domain is found in the C-terminal of lysine-2,3-aminomutase (LAM) and is involved in dimerisation []. LAM catalyses the interconversion of L-alpha-lysine and L-beta-lysine, which proceeds by migration of the amino group from C2 to C3 concomitant with cross-migration of the 3-pro-R hydrogen of L-alpha-lysine to the 2-pro-R position of L-beta-lysine. |
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| Publication |
| First Author: |
Yang S |
| Year: |
2006 |
| Journal: |
Plant J |
| Title: |
The BON/CPN gene family represses cell death and promotes cell growth in Arabidopsis. |
| Volume: |
45 |
| Issue: |
2 |
| Pages: |
166-79 |
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| Publication |
| First Author: |
Hua J |
| Year: |
2001 |
| Journal: |
Genes Dev |
| Title: |
Plant growth homeostasis is controlled by the Arabidopsis BON1 and BAP1 genes. |
| Volume: |
15 |
| Issue: |
17 |
| Pages: |
2263-72 |
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| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
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| Publication |
| First Author: |
Martin N |
| Year: |
2001 |
| Journal: |
Genomics |
| Title: |
Genetic and physical delineation of the region overlapping the progressive motor neuropathy (pmn) locus on mouse chromosome 13. |
| Volume: |
75 |
| Issue: |
1-3 |
| Pages: |
9-16 |
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