Type |
Details |
Score |
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
141
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
140
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
105
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
581
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
194
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
142
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
135
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
160
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
130
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
149
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
25
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
127
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Siderovski DP |
Year: |
1999 |
Journal: |
Trends Biochem Sci |
Title: |
The GoLoco motif: a Galphai/o binding motif and potential guanine-nucleotide exchange factor. |
Volume: |
24 |
Issue: |
9 |
Pages: |
340-1 |
|
•
•
•
•
•
|
Publication |
First Author: |
De Vries L |
Year: |
2000 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Activator of G protein signaling 3 is a guanine dissociation inhibitor for Galpha i subunits. |
Volume: |
97 |
Issue: |
26 |
Pages: |
14364-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Natochin M |
Year: |
2000 |
Journal: |
J Biol Chem |
Title: |
AGS3 inhibits GDP dissociation from galpha subunits of the Gi family and rhodopsin-dependent activation of transducin. |
Volume: |
275 |
Issue: |
52 |
Pages: |
40981-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kimple RJ |
Year: |
2002 |
Journal: |
Nature |
Title: |
Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits. |
Volume: |
416 |
Issue: |
6883 |
Pages: |
878-81 |
|
•
•
•
•
•
|
Publication |
First Author: |
Christianson JC |
Year: |
2011 |
Journal: |
Nat Cell Biol |
Title: |
Defining human ERAD networks through an integrative mapping strategy. |
Volume: |
14 |
Issue: |
1 |
Pages: |
93-105 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ye JZ |
Year: |
2004 |
Journal: |
J Biol Chem |
Title: |
TIN2 binds TRF1 and TRF2 simultaneously and stabilizes the TRF2 complex on telomeres. |
Volume: |
279 |
Issue: |
45 |
Pages: |
47264-71 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ito R |
Year: |
2001 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Temperature-sensitive phenotype of Chinese hamster ovary cells defective in PEX5 gene. |
Volume: |
288 |
Issue: |
2 |
Pages: |
321-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ito R |
Year: |
2005 |
Journal: |
J Biochem |
Title: |
Identification of Pex5pM, and retarded maturation of 3-ketoacyl-CoA thiolase and acyl-CoA oxidase in CHO cells expressing mutant Pex5p isoforms. |
Volume: |
138 |
Issue: |
6 |
Pages: |
781-90 |
|
•
•
•
•
•
|
Publication |
First Author: |
Otera H |
Year: |
2002 |
Journal: |
Mol Cell Biol |
Title: |
Peroxisomal targeting signal receptor Pex5p interacts with cargoes and import machinery components in a spatiotemporally differentiated manner: conserved Pex5p WXXXF/Y motifs are critical for matrix protein import. |
Volume: |
22 |
Issue: |
6 |
Pages: |
1639-55 |
|
•
•
•
•
•
|
Publication |
First Author: |
Amery L |
Year: |
2001 |
Journal: |
Biochem J |
Title: |
Identification of PEX5p-related novel peroxisome-targeting signal 1 (PTS1)-binding proteins in mammals. |
Volume: |
357 |
Issue: |
Pt 3 |
Pages: |
635-46 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Conserved_site |
Description: |
In heterotrimeric G-protein signalling, cell surface receptors (GPCRs) arecoupled to membrane-associated heterotrimers comprising a GTP-hydrolysing subunit G-alpha and a G-beta/G-gamma dimer. The inactive form contains the alpha subunit bound to GDP and complexes with the beta and gamma subunit. When the ligand is associated to thereceptor, GDP is displaced from G-alpha and GTP is bound. GTP/G-alpha complex dissociates from the trimer and associates to an effector until the intrinsic GTPase activity of G-alpha returns the protein to GDP bound form. Reassociation of GDP bound G-alpha with G-beta/G-gamma dimer terminates the signal. Several mechanisms regulate the signal output at different stage of the G-protein cascade. Two classes of intracellular proteins act as inhibitors of G protein activation: GTPase activating proteins (GAPs), which enhance GTP hydrolysis (see ),and guanine dissociation inhibitors (GDIs), which inhibit GDP dissociation.The GoLoco or G-protein regulatory (GPR) motif found in various G-proteinregulators [, ]acts as a GDI on G-alpha(i) [, ].The crystal structure of the GoLoco motif in complex with G-alpha(i) has been solved []. It consists of three small alpha helices. The highly conserved Asp-Gln-Arg triad within the GoLoco motif participates directly in GDP binding by extending the arginine side chain into the nucleotide binding pocket, highly reminiscent of the catalytic arginine finger employed in GTPase-activating protein (see ). This addition of an arginine in the binding pocket affects the interaction of GDP with G-alpha and therefore is certainly important for the GoLoco GDI activity [].Some proteins known to contain a GoLoco motif are listed below:Mammalian regulators of G-protein signalling 12 and 14 (RGS12 and RGS14), multifaceted signal transduction regulators.Loco, the drosophila RGS12 homologue.Mammalian Purkinje-cell protein-2 (Pcp2). It may function as a cell-type specific modulator for G protein-mediated cell signalling. It is uniquely expressed in cerebellar Purkinje cells and in retinal bipolar neurons.Eukaryotic Rap1GAP. A GTPase activator for the nuclear ras-related regulatory protein RAP-1A.Drosophila protein Rapsynoid (also known as Partner of Inscuteable, Pins) and its mammalian homologues AGS3 and LGN. They form a G-protein regulator family that also contains TPR repeats. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
421
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
476
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
421
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
392
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
López-Doménech G |
Year: |
2012 |
Journal: |
Nat Commun |
Title: |
The Eutherian Armcx genes regulate mitochondrial trafficking in neurons and interact with Miro and Trak2. |
Volume: |
3 |
|
Pages: |
814 |
|
•
•
•
•
•
|
Publication |
First Author: |
Roux I |
Year: |
2006 |
Journal: |
Cell |
Title: |
Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse. |
Volume: |
127 |
Issue: |
2 |
Pages: |
277-89 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
825
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
362
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
157
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
332
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
363
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
164
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
541
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
363
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
55
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
217
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
540
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
166
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Hao HX |
Year: |
2009 |
Journal: |
Science |
Title: |
SDH5, a gene required for flavination of succinate dehydrogenase, is mutated in paraganglioma. |
Volume: |
325 |
Issue: |
5944 |
Pages: |
1139-42 |
|
•
•
•
•
•
|
Publication |
First Author: |
McNeil MB |
Year: |
2012 |
Journal: |
J Biol Chem |
Title: |
SdhE is a conserved protein required for flavinylation of succinate dehydrogenase in bacteria. |
Volume: |
287 |
Issue: |
22 |
Pages: |
18418-28 |
|
•
•
•
•
•
|
Publication |
First Author: |
Lee SH |
Year: |
1998 |
Journal: |
J Bacteriol |
Title: |
Nucleotide sequence and spatiotemporal expression of the Vibrio cholerae vieSAB genes during infection. |
Volume: |
180 |
Issue: |
9 |
Pages: |
2298-305 |
|
•
•
•
•
•
|
Publication |
First Author: |
Tischler AD |
Year: |
2002 |
Journal: |
J Bacteriol |
Title: |
The Vibrio cholerae vieSAB locus encodes a pathway contributing to cholera toxin production. |
Volume: |
184 |
Issue: |
15 |
Pages: |
4104-13 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ramón NM |
Year: |
2010 |
Journal: |
Mol Biol Cell |
Title: |
Interdependence of the peroxisome-targeting receptors in Arabidopsis thaliana: PEX7 facilitates PEX5 accumulation and import of PTS1 cargo into peroxisomes. |
Volume: |
21 |
Issue: |
7 |
Pages: |
1263-71 |
|
•
•
•
•
•
|
Publication |
First Author: |
Woodward AW |
Year: |
2005 |
Journal: |
Mol Biol Cell |
Title: |
The Arabidopsis peroxisomal targeting signal type 2 receptor PEX7 is necessary for peroxisome function and dependent on PEX5. |
Volume: |
16 |
Issue: |
2 |
Pages: |
573-83 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Two-component signal transduction systems enable bacteria to sense, respond, and adapt to a wide range of environments, stressors, and growth conditions []. Some bacteria can contain up to as many as 200 two-component systems that need tight regulation to prevent unwanted cross-talk []. These pathways have been adapted to response to a wide variety of stimuli, including nutrients, cellular redox state, changes in osmolarity, quorum signals, antibiotics, and more []. Two-component systems are comprised of a sensor histidine kinase (HK) and its cognate response regulator (RR) []. The HK catalyses its own auto-phosphorylation followed by the transfer of the phosphoryl group to the receiver domain on RR; phosphorylation of the RR usually activates an attached output domain, which can then effect changes in cellular physiology, often by regulating gene expression. Some HK are bifunctional, catalysing both the phosphorylation and dephosphorylation of their cognate RR. The input stimuli can regulate either the kinase or phosphatase activity of the bifunctional HK.A variant of the two-component system is the phospho-relay system. Here a hybrid HK auto-phosphorylates and then transfers the phosphoryl group to an internal receiver domain, rather than to a separate RR protein. The phosphoryl group is then shuttled to histidine phosphotransferase (HPT) and subsequently to a terminal RR, which can evoke the desired response [, ].This entry represents VieB-type response regulators. In Vibrio, it is part of a signal transduction pathway involved in cholera toxin production [, ].Response regulators of the microbial two-component signal transduction systems typically consist of an N-terminal CheY-like receiver (phosphoacceptor) domain and a C-terminal output (usually DNA-binding) domain. In response to an environmental stimulus, a phosphoryl group is transferred from the His residue of sensor histidine kinase to an Asp residue in the CheY-like receiver domain of the cognate response regulator [, , ]. Phosphorylation of the receiver domain induces conformational changes that activate an associated output domain, which in turn triggers the response. Phosphorylation-induced conformational changes in response regulator molecules have been demonstrated in direct structural studies [].The output domain found in this group is so far unique. In part, it contains a divergent version of TPR repeats. |
|
•
•
•
•
•
|
Publication |
First Author: |
Jia Z |
Year: |
1997 |
Journal: |
Biochem Cell Biol |
Title: |
Protein phosphatases: structures and implications. |
Volume: |
75 |
Issue: |
1 |
Pages: |
17-26 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1291
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1380
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1331
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1372
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1291
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1372
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Kirschner LS |
Year: |
2016 |
Journal: |
Mol Cell Endocrinol |
Title: |
Mouse models of thyroid cancer: A 2015 update. |
Volume: |
421 |
|
Pages: |
18-27 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
229
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
350
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
148
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
331
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
135
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Pei J |
Year: |
2001 |
Journal: |
Proteins |
Title: |
GGDEF domain is homologous to adenylyl cyclase. |
Volume: |
42 |
Issue: |
2 |
Pages: |
210-6 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ausmees N |
Year: |
2001 |
Journal: |
FEMS Microbiol Lett |
Title: |
Genetic data indicate that proteins containing the GGDEF domain possess diguanylate cyclase activity. |
Volume: |
204 |
Issue: |
1 |
Pages: |
163-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Shirasu K |
Year: |
1999 |
Journal: |
Cell |
Title: |
A novel class of eukaryotic zinc-binding proteins is required for disease resistance signaling in barley and development in C. elegans. |
Volume: |
99 |
Issue: |
4 |
Pages: |
355-66 |
|
•
•
•
•
•
|
Publication |
First Author: |
Heizmann CW |
Year: |
2002 |
Journal: |
Methods Mol Biol |
Title: |
The multifunctional S100 protein family. |
Volume: |
172 |
|
Pages: |
69-80 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
663
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1215
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
94
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1072
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
525
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
729
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
543
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
94
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
171
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
144
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1216
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
94
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Ponting CP |
Year: |
1999 |
Journal: |
J Mol Med (Berl) |
Title: |
Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signalling proteins. |
Volume: |
77 |
Issue: |
10 |
Pages: |
695-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wu J |
Year: |
2023 |
Journal: |
Blood Adv |
Title: |
EHBP1L1, an apicobasal polarity regulator, is critical for nuclear polarization during enucleation of erythroblasts. |
Volume: |
7 |
Issue: |
14 |
Pages: |
3382-3394 |
|
•
•
•
•
•
|
Publication |
First Author: |
Okazaki N |
Year: |
2003 |
Journal: |
DNA Res |
Title: |
Prediction of the coding sequences of mouse homologues of KIAA gene: III. the complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries. |
Volume: |
10 |
Issue: |
4 |
Pages: |
167-80 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sweet SM |
Year: |
2009 |
Journal: |
Mol Cell Proteomics |
Title: |
Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry. |
Volume: |
8 |
Issue: |
5 |
Pages: |
904-12 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
338
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
411
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
419
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
408
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
445
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
416
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
420
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
405
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
256
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
364
|
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Guo A |
Year: |
2014 |
Journal: |
Mol Cell Proteomics |
Title: |
Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. |
Volume: |
13 |
Issue: |
1 |
Pages: |
372-87 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
421
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
528
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
547
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1360
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
733
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1299
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1322
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
793
|
Fragment?: |
false |
|
•
•
•
•
•
|