All terms in UNIPROT
| Label | Id | Description |
|---|---|---|
| Sesquipedalian-2 | Q6ICB4 | [Function: Plays a role in endocytic trafficking. Required for receptor recycling from endosomes, both to the trans-Golgi network and the plasma membrane.] |
| Collagen alpha-1(XXIII) chain | Q810Y4 | |
| Uncharacterized protein NKAPD1 | Q6ZUT1 | |
| Preferentially expressed antigen in melanoma-like protein 7 | Q810Y8 | [Function: Promotes maintenance and self-renewal of pluripotent embryonic stem cells (ESCs), downstream of LIF/STAT3 (PubMed:21425410). Maintains the pluripotency state of ESCs by repressing DNA methylation through the regulation of UHRF1 stability. Mediates the proteasomal degradation of UHRF1. Is required for the establishment of the blastocyst (PubMed:28604677).] |
| DNA-binding protein RFX8 | Q6ZV50 | [Function: May be a transcription factor.] |
| Thromboxane-A synthase | P36423 | |
| NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 8 | Q9DCJ5 | [Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.] |
| Speedy protein E5 | A6NIY4 | |
| Synaptogyrin-3 | Q8R191 | [Function: May play a role in regulated exocytosis (PubMed:10383386). May indirectly regulate the activity of the plasma membrane dopamine transporter SLC6A3 and thereby regulate dopamine transport back from the synaptic cleft into the presynaptic terminal (PubMed:19357284).] |
| N-acetylneuraminate lyase | Q9DCJ9 | [Function: Catalyzes the cleavage of N-acetylneuraminic acid (sialic acid) to form pyruvate and N-acetylmannosamine via a Schiff base intermediate. It prevents sialic acids from being recycled and returning to the cell surface. Involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway.] |
| Aurora kinase A-interacting protein | Q9DCJ7 | [Function: May act as a negative regulator of Aurora-A kinase, by down-regulation through proteasome-dependent degradation.] |
| T-cell immunoglobulin and mucin domain-containing protein 2 | Q8R183 | [Function: Probable receptor for SEMA4A involved in the regulation of T-cell function. The interaction with SEMA4A enhances T-cell activation.] |
| Protein FAM110A | Q8R184 | |
| CLOCK-interacting pacemaker | Q8R0W1 | [Function: Transcriptional repressor which may act as a negative-feedback regulator of CLOCK-ARNTL/BMAL1 transcriptional activity in the circadian-clock mechanism. May stimulate ARNTL/BMAL1-dependent phosphorylation of CLOCK (PubMed:17310242, PubMed:19414601). However, the physiogical relevance of these observations is unsure, since experiments in knockout mice showed that CIPC is not critially required for basic circadian clock (PubMed:25862660).] |
| Transmembrane gamma-carboxyglutamic acid protein 2 | Q8R182 | |
| Target of rapamycin complex subunit LST8 | Q9DCJ1 | [Function: Subunit of both mTORC1 and mTORC2, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, LST8 interacts directly with MTOR and enhances its kinase activity. In nutrient-poor conditions, stabilizes the MTOR-RPTOR interaction and favors RPTOR-mediated inhibition of MTOR activity. mTORC2 is also activated by growth factors, but seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'.] |
| SPRY domain-containing protein 7 | Q5W111 | |
| Carboxylesterase 4A | Q8R0W5 | [Function: Probable carboxylesterase.] |
| NEDD4 family-interacting protein 1 | Q8R0W6 | [Function: Activates HECT domain-containing E3 ubiquitin-protein ligases, including NEDD4 and ITCH, and consequently modulates the stability of their targets. As a result, controls many cellular processes. Prevents chronic T-helper cell-mediated inflammation by activating ITCH and thus controlling JUNB degradation (PubMed:11748237, PubMed:17137798, PubMed:20962770). Promotes pancreatic beta cell death through degradation of JUNB and inhibition of the unfolded protein response, leading to reduction of insulin secretion (PubMed:26319551). Restricts the production of proinflammatory cytokines in effector Th17 T-cells by promoting ITCH-mediated ubiquitination and degradation of RORC (PubMed:28051111). Together with NDFIP2, limits the cytokine signaling and expansion of effector Th2 T-cells by promoting degradation of JAK1, probably by ITCH- and NEDD4L-mediated ubiquitination (PubMed:27088444). Regulates peripheral T-cell tolerance to self and foreign antigens, forcing the exit of naive CD4+ T-cells from the cell cycle before they become effector T-cells (PubMed:24520172, PubMed:28051111). Negatively regulates RLR-mediated antiviral response by promoting SMURF1-mediated ubiquitination and subsequent degradation of MAVS (By similarity). Negatively regulates KCNH2 potassium channel activity by decreasing its cell-surface expression and interfering with channel maturation through recruitment of NEDD4L to the Golgi apparatus where it mediates KCNH2 degradation (By similarity). In cortical neurons, mediates the ubiquitination of the divalent metal transporter SLC11A2/DMT1 by NEDD4L, leading to its down-regulation and protection of the cells from cobalt and iron toxicity (By similarity). Important for normal development of dendrites and dendritic spines in cortex (PubMed:23897647). Enhances the ubiquitination of BRAT1 mediated by: NEDD4, NEDD4L and ITCH and is required for the nuclear localization of ubiquitinated BRAT1 (PubMed:25631046). Enhances the ITCH-mediated ubiquitination of MAP3K7 by recruiting E2 ubiquitin-conjugating enzyme UBE2L3 to ITCH (PubMed:25632008). Modulates EGFR signaling through multiple pathways. In particular, may regulate the ratio of AKT1-to-MAPK8 signaling in response to EGF, acting on AKT1 probably through PTEN destabilization and on MAPK8 through ITCH-dependent MAP2K4 inactivation. As a result, may control cell growth rate (By similarity). Inhibits cell proliferation by promoting PTEN nuclear localization and changing its signaling specificity (PubMed:25801959).] |
| Ventricular zone-expressed PH domain-containing protein homolog 1 | Q14D04 | [Function: Interacts with TGF-beta receptor type-1 (TGFBR1) and inhibits dissociation of activated SMAD2 from TGFBR1, impeding its nuclear accumulation and resulting in impaired TGF-beta signaling. May also affect FOXO, Hippo and Wnt signaling.] |