Family Search for PF06840 (PDC10_C)

PF06840 hits 19 sequences in PaperBLAST's database above the trusted cutoff. Showing hits to curated sequences only. Or see all hits or try another family.

PDC10_MOUSE / Q8VE70 Programmed cell death protein 10; TF-1 cell apoptosis-related protein 15 from Mus musculus (Mouse) (see paper)
Aligns to 74:161 / 212 (41.5%), covers 100.0% of PF06840, 136.0 bits

• function: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (By similarity). Important for KDR/VEGFR2 signaling. Increases the stability of KDR/VEGFR2 and prevents its breakdown (PubMed:20371769). Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development (By similarity).
  subunit: Homodimer. Interacts (via C-terminus) with CCM2. Interacts (via C-terminus) with PXN. Interacts (via N-terminus) with STK25. Interacts (via N-terminus) with STK26. Interacts (via N-terminus) with STK24. Interacts with GOLGA2. Identified in a complex with KRIT1 and CCM2 (By similarity). Interacts with KDR/VEGFR2. Interaction with KDR/VEGFR2 is enhanced by stimulation with VEGFA (PubMed:20371769). Interacts with RIPOR1 (via C-terminus); this interaction is required for the association of RIPOR1 with either STK24 and STK26 kinases and occurs in a Rho-independent manner. Part of the core of STRIPAK complexes composed of PP2A catalytic and scaffolding subunits, the striatins (PP2A regulatory subunits), the striatin-associated proteins MOB4, STRIP1 and STRIP2, PDCD10 and members of the STE20 kinases, such as STK24 and STK26 (By similarity).
  disruption phenotype: Lethal at an early embryonic stage due to defects in angiogenesis, vasculogenesis and hematopoiesis. Mice exhibit low levels of KDR/VEGFR2.

PDC10_RAT / Q6NX65 Programmed cell death protein 10 from Rattus norvegicus (Rat) (see paper)
Aligns to 72:159 / 210 (41.9%), covers 100.0% of PF06840, 136.0 bits

• function: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (By similarity). Important for KDR/VEGFR2 signaling. Increases the stability of KDR/VEGFR2 and prevents its breakdown. Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development (By similarity).
  subunit: Homodimer. Interacts (via C-terminus) with CCM2. Interacts (via C-terminus) with PXN. Interacts (via N-terminus) with STK25. Interacts (via N-terminus) with STK26. Interacts (via N-terminus) with STK24. Interacts with GOLGA2. Identified in a complex with KRIT1 and CCM2. Interacts with KDR/VEGFR2. Interaction with KDR/VEGFR2 is enhanced by stimulation with VEGFA. Interacts with RIPOR1 (via C- terminus); this interaction is required for the association of RIPOR1 with either STK24 and STK26 kinases and occurs in a Rho-independent manner. Part of the core of STRIPAK complexes composed of PP2A catalytic and scaffolding subunits, the striatins (PP2A regulatory subunits), the striatin-associated proteins MOB4, STRIP1 and STRIP2, PDCD10 and members of the STE20 kinases, such as STK24 and STK26.

PDC10_HUMAN / Q9BUL8 Programmed cell death protein 10; Cerebral cavernous malformations 3 protein; TF-1 cell apoptosis-related protein 15 from Homo sapiens (Human) (see 6 papers)
Aligns to 74:161 / 212 (41.5%), covers 100.0% of PF06840, 136.0 bits

• function: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity (PubMed:27807006). Important for cell migration, and for normal structure and assembly of the Golgi complex (PubMed:27807006). Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (PubMed:18782753). Important for KDR/VEGFR2 signaling. Increases the stability of KDR/VEGFR2 and prevents its breakdown. Required for normal cardiovascular development. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development (By similarity).
  subunit: Homodimer (PubMed:20489202). Interacts (via C-terminus) with CCM2 (PubMed:17360971, PubMed:20489202). Interacts (via C-terminus) with PXN (PubMed:20489202). Interacts (via N-terminus) with STK25 (PubMed:17360971, PubMed:20332113). Interacts (via N-terminus) with STK26 (PubMed:17360971, PubMed:20332113, PubMed:27807006). Interacts (via N-terminus) with STK24 (PubMed:20332113, PubMed:27807006). Interacts with GOLGA2 (PubMed:20332113). Identified in a complex with KRIT1 and CCM2. Interacts with KDR/VEGFR2. Interaction with KDR/VEGFR2 is enhanced by stimulation with VEGFA (Ref.5). Interacts with RIPOR1 (via C-terminus); this interaction is required for the association of RIPOR1 with either STK24 and STK26 kinases and occurs in a Rho- independent manner (PubMed:27807006). Part of the core of STRIPAK complexes composed of PP2A catalytic and scaffolding subunits, the striatins (PP2A regulatory subunits), the striatin-associated proteins MOB4, STRIP1 and STRIP2, PDCD10 and members of the STE20 kinases, such as STK24 and STK26 (PubMed:18782753).

PD10A_DANRE / Q6PHH3 Programmed cell death protein 10-A from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
Aligns to 72:159 / 210 (41.9%), covers 100.0% of PF06840, 135.1 bits

• function: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development (By similarity). Required for normal cardiovascular development (PubMed:19370760). Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (By similarity).
  subunit: Interacts (via C-terminus) with CCM2. Interacts (via N- terminus) with STK25 and STK26.

PD10B_DANRE / Q6NWL1 Programmed cell death protein 10-B from Danio rerio (Zebrafish) (Brachydanio rerio) (see paper)
Aligns to 72:159 / 210 (41.9%), covers 100.0% of PF06840, 134.8 bits

• function: Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Important for KDR/VEGFR2 signaling. Required for normal angiogenesis, vasculogenesis and hematopoiesis during embryonic development (By similarity). Required for normal cardiovascular development (PubMed:19370760). Promotes cell proliferation. Modulates apoptotic pathways. Increases mitogen-activated protein kinase activity and STK26 activity. Important for cell migration, and for normal structure and assembly of the Golgi complex. Part of the striatin-interacting phosphatase and kinase (STRIPAK) complexes. STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling. Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (By similarity).
  subunit: Interacts (via C-terminus) with CCM2. Interacts (via N- terminus) with STK25 and STK26.

PDC10_CAEEL / Q17958 Programmed cell death protein 10 homolog; Cerebral cavernous malformation protein 3 from Caenorhabditis elegans (see paper)
Aligns to 71:179 / 215 (50.7%), covers 98.9% of PF06840, 106.6 bits

• function: Involved in excretory canal elongation during postembryonic development. Plays a role in promoting Golgi stability, ER integrity and vesicle transport probably by regulating the activation of Rho GTPase cdc-42. Involved in fertility.
  subunit: Interacts with gck-1.
  disruption phenotype: Animals are sterile and develop slowly. Excretory canals are approximately 45% shorter and are characterized by a discontinuous and wider lumen, the presence of cysts and an increased number of canalicular vesicles which are swollen. These defects start during the L3 larval stage and become more severe when reaching adulthood. In addition, cdc-42 expression levels and activity are reduced along the excretory canal length. Animals have also a reduced distribution of Golgi and ER components along the excretory canals.

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