GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.
CACAO Spring 2016
|Status||Page||Date/Time||GO Term (Aspect)||Reference||Evidence||Notes||Links|
|HUMAN:BIRC1||2016-02-08 22:46:04 CST||GO:0006954 inflammatory response (P)||PMID:21874021||ECO:0000315 mutant phenotype evidence used in manual assertion|
Figure 2. (NAIP)
|HUMAN:BIRC1||2016-02-08 22:46:05 CST||GO:0009405 pathogenesis (P)||other:GO_REF:0000037|
|HUMAN:BIRC1||2016-02-08 23:05:05 CST||GO:0043154 negative regulation of cysteine-type endopeptidase activity involved in apoptotic process (P)||PMID:11896143||ECO:0000314 direct assay evidence used in manual assertion|
The neuronal apoptosis inhibitory protein (NAIP) was identified as a candidate gene for the inherited neurodegenerative disorder spinal muscular atrophy.
|HUMAN:BIRC1||2016-02-08 23:12:42 CST||GO:0043281 regulation of cysteine-type endopeptidase activity involved in apoptotic process (P)||PMID:15190255||ECO:0000315 mutant phenotype evidence used in manual assertion|
Specific adaptors regulate the activation of initiator caspases; for example, FADD and Apaf-1 engage caspases 8 and 9, respectively. The adaptors ASC, Ipaf and RIP2 have each been proposed to regulate caspase-1 (also called interleukin (IL)-1 converting enzyme), which is activated within the 'inflammasome', a complex comprising several adaptors.
|HUMAN:BIRC1||2016-02-08 23:36:37 CST||GO:0016020 membrane (C)||other:GO_REF:0000002|
InterPro:IPR008104 - IEA: Inferred from Electronic Annotation
|LEGPN:Q8KMN1||2016-02-08 23:45:24 CST||GO:0071973 bacterial-type flagellum-dependent cell motility (P)||other:GO_REF:0000002|
InterPro:IPR001029 - IEA: Inferred from Electronic Annotation
|HUMAN:BIRC1||2016-02-09 00:04:19 CST||GO:0005515 protein binding (F)||PMID:21371431|
IPI: Inferred from Physical Interaction - UniProtKB:O14727
|HUMAN:BIRC1||2016-02-21 05:15:48 CST||GO:0070062 extracellular exosome (C)||PMID:23376485||ECO:0000314 direct assay evidence used in manual assertion|
Figure 1. study was the identification of podocyte exosome proteins based on urine immunoabsorption using podocyte-specific CR1-immunocoated beads followed by proteomic analysis using LC MS/MS techniques.
|HUMAN:NLRC4||2016-02-21 23:03:38 CST||GO:0050713 negative regulation of interleukin-1 beta secretion (P)||PMID:15107016||ECO:0000314 direct assay evidence used in manual assertion|
As shown in Figure 7(B), the NACHT domain of CLAN is sufficient to inhibit Nod2-induced IL-1β secretion, while the NB-ARC domain of Apaf-1 had no inhibitory effects when co-expressed with Nod2
|HUMAN:NLRC4||2016-03-24 06:35:36 CDT||GO:0097202 activation of cysteine-type endopeptidase activity (P)||PMID:15882992||ECO:0000315 mutant phenotype evidence used in manual assertion|
|HUMAN:BIRC1||2016-04-08 04:46:08 CDT||GO:1900118 negative regulation of execution phase of apoptosis (P)||PMID:9564035||ECO:0000250 sequence similarity evidence used in manual assertion|
Figure 1. The human homolog of CIDE-A. Analysis of the nucleotide sequence of both human and mouse CIDE-A cDNAs revealed two potential in-frame translation initi- ation sites separated by 51 nucleotides. These two potential initiation codons produce a protein of 217 amino acids (designated CIDE-A*) and a protein identical to CIDE-A* but lacking its 17 most N-terminal amino acids (designated CIDE-A)
|HUMAN:BIRC1||2016-04-08 04:46:09 CDT||GO:1900118 negative regulation of execution phase of apoptosis (P)||PMID:9564035||ECO:0000314 direct assay evidence used in manual assertion|
Figure1. The homology of CIDE-A, CIDE-B and FSP27 with DFF45 was restricted to an N-terminal region designated here as CIDE-N domain which showed 39, 29 and 38% amino acid identity respectively with DFF45. Another region of CIDE-A and CIDE-B, termed CIDE-C domain, located in their C-termini shared amino acid homology (54 and 53% identity, respectively) with FSP27 but not with DFF45
|LEGPH:ACON||2016-03-28 08:20:09 CDT||GO:0003729 mRNA binding (F)||PMID:8366052||ECO:0000314 direct assay evidence used in manual assertion|
Fig. 1. Major IPs of L. pneumophila. A crude extract of L. pneumophila grown on agar medium containing 59Fe was subjected to ND-PAGE, and the radiolabeled proteins were visualized by autoradiography (right). A crude extract of E. coli obtained under the same conditions was included as a control (left).
|LEGPN:DRRA||2016-04-12 05:47:52 CDT||GO:0070273 phosphatidylinositol-4-phosphate binding (F)||PMID:16906144||ECO:0000314 direct assay evidence used in manual assertion|
Figure 1A. The protein also displayed weaker interactions with PtdIns(3,4)P2. The major PtdIns(4)P interactor was identified by mass spectrometry as the 73-kDa protein SidM, a known Icm/Dot substrate previously characterized as a Rab1 GEF.
|LEGPN:DRRA||2016-04-12 05:57:04 CDT||GO:0044161 host cell cytoplasmic vesicle (C)||PMID:19095644||ECO:0000314 direct assay evidence used in manual assertion|
C-terminal fragments of SidM localize to LCVs. A, confocal laser scanning micrographs of calnexin-GFP-labeled D. discoideum Ax3 (green), infected at an m.o.i. of 50 for 1 h with L. pneumophila labeled with a serogroup 1-specific antibody (red) and ...
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