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Search results 1 to 100 out of 102 for Cdc50a

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0.015s
Type Details Score
Publication
First Author: Xu Q
Year: 2012
Journal: FEBS Lett
Title: P4-ATPase ATP8A2 acts in synergy with CDC50A to enhance neurite outgrowth.
Volume: 586
Issue: 13
Pages: 1803-12
Publication
First Author: Kato U
Year: 2013
Journal: J Biol Chem
Title: Role for phospholipid flippase complex of ATP8A1 and CDC50A proteins in cell migration.
Volume: 288
Issue: 7
Pages: 4922-34
Publication
First Author: Muñoz-Martínez F
Year: 2010
Journal: Biochem Pharmacol
Title: CDC50A plays a key role in the uptake of the anticancer drug perifosine in human carcinoma cells.
Volume: 80
Issue: 6
Pages: 793-800
Publication
First Author: Segawa K
Year: 2018
Journal: J Biol Chem
Title: The CDC50A extracellular domain is required for forming a functional complex with and chaperoning phospholipid flippases to the plasma membrane.
Volume: 293
Issue: 6
Pages: 2172-2182
Protein
Organism: Mus musculus/domesticus
Length: 364  
Fragment?: false
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Publication
First Author: Folmer DE
Year: 2012
Journal: J Histochem Cytochem
Title: Cellular localization and biochemical analysis of mammalian CDC50A, a glycosylated β-subunit for P4 ATPases.
Volume: 60
Issue: 3
Pages: 205-18
Publication
First Author: Segawa K
Year: 2014
Journal: Science
Title: Caspase-mediated cleavage of phospholipid flippase for apoptotic phosphatidylserine exposure.
Volume: 344
Issue: 6188
Pages: 1164-8
Publication
First Author: Osada N
Year: 2007
Journal: Gene
Title: Aberrant termination of reproduction-related TMEM30C transcripts in the hominoids.
Volume: 392
Issue: 1-2
Pages: 151-6
Publication
First Author: Xu P
Year: 2007
Journal: Acta Biochim Biophys Sin (Shanghai)
Title: Characterization and expression of mouse Cdc50c during spermatogenesis.
Volume: 39
Issue: 10
Pages: 739-44
Publication
First Author: Katoh Y
Year: 2004
Journal: Oncol Rep
Title: Identification and characterization of CDC50A, CDC50B and CDC50C genes in silico.
Volume: 12
Issue: 4
Pages: 939-43
Protein Domain
Type: Family
Description: Cell cycle control protein 50C (CDC50C, also known as TMEM30C) is one of the CDC50 (CDC50A/B/C) proteins []. CDC50A and CDC50B are accessory components of the phospholipid-transporting ATPase (P4-ATPase) complex which catalyses the hydrolysis of ATP coupled to the transport of phospholipids across the membrane []. The function of CDC50C is not clear. Unlike the broad expression of CDC50A and CDC50B, CDC50C is expressed specifically in mouse testis [, ]. However, no full-length transcripts of CDC50C have been found in humans [].
Publication
First Author: Harris MJ
Year: 2003
Journal: Biochim Biophys Acta
Title: FIC1, a P-type ATPase linked to cholestatic liver disease, has homologues (ATP8B2 and ATP8B3) expressed throughout the body.
Volume: 1633
Issue: 2
Pages: 127-31
Publication
First Author: Li H
Year: 2008
Journal: Arch Neurol
Title: Candidate single-nucleotide polymorphisms from a genomewide association study of Alzheimer disease.
Volume: 65
Issue: 1
Pages: 45-53
Protein Domain
Type: Family
Description: Phospholipid-transporting ATPase ID (also known as ATP8B2 or ATPID) belongs to the IV subfamily of the P-type ATPases family, whose members transport phospholipids across the membrane. The function of ATP8B2 is not clear. It can bind either CDC50A or CDC50B as its accessory protein required for its function []. ATP8B2 is expressed throughout the body [].
Protein Domain
Type: Family
Description: Probable phospholipid-transporting ATPase IM (also known as ATP8B4) belongs to subfamily IV of the P-type ATPases family, whose members transport phospholipids across the membrane. It appears to be a component of a P4-ATPase flippase complex and can bind either CDC50A or CDC50B as its accessory protein []. ATPase IM is expressed throughout the brain and may be involved in Alzheimer's disease [].
Protein Domain
Type: Family
Description: Cell cycle control protein 50A (CDC50A, also known as TMEM30A) is an accessory component of the phospholipid-transporting ATPase (P4-ATPase) complex which catalyses the hydrolysis of ATP coupled to the transport of phospholipids across the membrane []. It can interact with several P4-ATPases, such as ATP8A1, ATP8A2, ATP8B1, ATP8B2, ATP11A, ATP11B and ATP11C [, , ]. CDC50A is a terminal-glycosylated glycoprotein and is expressed in hepatocytes and liver sinusoidal endothelial cells. In pancreas and stomach, it localises to secretory vesicles, while in kidney, it localises to the apical region of proximal convoluted tubules of the cortex []. In human carcinoma cells, CDC50A plays a key role in the uptake of the anticancer drug perifosine [].
Protein
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: false
Protein Domain
Type: Family
Description: Phospholipid-transporting ATPase IF (also known as ATP11B) belongs to subfamily IV of the P-type ATPases (P4-ATPase) family, whose members transport phospholipids across the membrane. ATP11B is ubiquitously expressed and binds CDC50A as its beta-subunit []. It is the catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of intracellular membranes [].
Publication
First Author: Bryde S
Year: 2010
Journal: J Biol Chem
Title: CDC50 proteins are critical components of the human class-1 P4-ATPase transport machinery.
Volume: 285
Issue: 52
Pages: 40562-72
Publication
First Author: Tsuchiya M
Year: 2018
Journal: Nat Commun
Title: Cell surface flip-flop of phosphatidylserine is critical for PIEZO1-mediated myotube formation.
Volume: 9
Issue: 1
Pages: 2049
Publication
First Author: Martin S
Year: 2020
Journal: Acta Neuropathol
Title: Mutated ATP10B increases Parkinson's disease risk by compromising lysosomal glucosylceramide export.
Volume: 139
Issue: 6
Pages: 1001-1024
Publication
First Author: Siggs OM
Year: 2011
Journal: Nat Immunol
Title: The P4-type ATPase ATP11C is essential for B lymphopoiesis in adult bone marrow.
Volume: 12
Issue: 5
Pages: 434-40
Publication
First Author: Yabas M
Year: 2011
Journal: Nat Immunol
Title: ATP11C is critical for the internalization of phosphatidylserine and differentiation of B lymphocytes.
Volume: 12
Issue: 5
Pages: 441-9
Publication
First Author: Yabas M
Year: 2014
Journal: J Biol Chem
Title: Mice deficient in the putative phospholipid flippase ATP11C exhibit altered erythrocyte shape, anemia, and reduced erythrocyte life span.
Volume: 289
Issue: 28
Pages: 19531-7
Publication
First Author: Wang L
Year: 2004
Journal: Dev Biol
Title: A novel aminophospholipid transporter exclusively expressed in spermatozoa is required for membrane lipid asymmetry and normal fertilization.
Volume: 267
Issue: 1
Pages: 203-15
Protein
Organism: Mus musculus/domesticus
Length: 145  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 72  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 89  
Fragment?: true
Publication
First Author: van der Velden LM
Year: 2010
Journal: J Biol Chem
Title: Heteromeric interactions required for abundance and subcellular localization of human CDC50 proteins and class 1 P4-ATPases.
Volume: 285
Issue: 51
Pages: 40088-96
Publication
First Author: Takatsu H
Year: 2014
Journal: J Biol Chem
Title: Phospholipid flippase activities and substrate specificities of human type IV P-type ATPases localized to the plasma membrane.
Volume: 289
Issue: 48
Pages: 33543-56
Publication
First Author: Naito T
Year: 2015
Journal: J Biol Chem
Title: Phospholipid Flippase ATP10A Translocates Phosphatidylcholine and Is Involved in Plasma Membrane Dynamics.
Volume: 290
Issue: 24
Pages: 15004-17
Publication
First Author: Segawa K
Year: 2016
Journal: J Biol Chem
Title: Human Type IV P-type ATPases That Work as Plasma Membrane Phospholipid Flippases and Their Regulation by Caspase and Calcium.
Volume: 291
Issue: 2
Pages: 762-72
Protein Domain
Type: Family
Description: Phospholipid-transporting ATPase IG (also known as ATP11C) belongs to subfamily IV of the P-type ATPases (P4-ATPase) family, whose members transport phospholipids across the membrane. ATP11C is ubiquitously expressed and binds CDC50A as its beta-subunit []. In mice, ATP11C plays an important role in the proper development of B-cell lymphocytes [, , ]. In human cells, ATP11C can function as a phosphatidylserine (PtdSer) flippase at the plasma membrane. During apoptosis, the inactivation of ATP11C is required for cells to expose and display apoptotic PtdSer, which then serves as an "eat me"signal for macrophages to engulf the cells [].
Protein Domain
Type: Family
Description: Phospholipid-transporting ATPase IK (also known as ATP8B3 orATP1K) belongs to the subfamily IV of the P-type ATPases family, whose members transport phospholipids across the membrane. The function of ATP8B3 is not clear. Unlike other type IV members (ATP8B1,2,4), ATP8B3 does not seem to interact with either CDC50A or CDC50B []. It is exclusively expressed in the testis where it localises to the acrosomes of spermatids, the organelle which develops in the anterior half of the head of spermatozoa []. However, the disruption of ATP8B3 in mice does not affect sperm morphology or fertilisation rate [].
Protein Domain
Type: Family
Description: Phospholipid-transporting ATPase VB (also known as ATP10B) belongs to the IV subfamily of the P-type ATPases (P4-ATPase) family. P4-ATPases are phospholipid flippases that translocate phospholipids from the exoplasmic (lumenal) to the cytoplasmic leaflet of cellular membranes. ATP10C requires CDC50A for its exit from the endoplasmic reticulum (ER) and final subcellular localisation []. ATP10B is the catalytic component of a P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of glucosylceramide (GlcCer) from the outer to the inner leaflet of lysosome membranes [].
Protein Domain
Type: Family
Description: Probable phospholipid-transporting ATPase IH (also known as ATP11A) belongs to the IV subfamily of the P-type ATPases (P4-ATPase) family, whose members transport phospholipids across the membrane. Most P4-ATPases are known to associate with an accessory or beta-subunit known as CDC50 to form a heteromeric complex. ATP11A is ubiquitously expressed and only binds CDC50A as its beta-subunit [, ]. ATP11A is a catalytic component of a P4-ATPase flippase complex which catalyzes the hydrolysis of ATP coupled to the transport of aminophospholipids, phosphatidylserines (PS) and phosphatidylethanolamines (PE), from the outer to the inner leaflet of the plasma membrane [, , , , ].
Publication
First Author: Park J
Year: 2021
Journal: EMBO J
Title: Microglial MERTK eliminates phosphatidylserine-displaying inhibitory post-synapses.
Volume: 40
Issue: 15
Pages: e107121
Protein
Organism: Mus musculus/domesticus
Length: 342  
Fragment?: false
Publication
First Author: Wang J
Year: 2018
Journal: Sci Rep
Title: Proteomic Analysis and Functional Characterization of P4-ATPase Phospholipid Flippases from Murine Tissues.
Volume: 8
Issue: 1
Pages: 10795
Protein
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: false
Publication
First Author: Takatsu H
Year: 2011
Journal: J Biol Chem
Title: ATP9B, a P4-ATPase (a putative aminophospholipid translocase), localizes to the trans-Golgi network in a CDC50 protein-independent manner.
Volume: 286
Issue: 44
Pages: 38159-67
Publication
First Author: Groen A
Year: 2011
Journal: Gastroenterology
Title: Complementary functions of the flippase ATP8B1 and the floppase ABCB4 in maintaining canalicular membrane integrity.
Volume: 141
Issue: 5
Pages: 1927-37.e1-4
Protein
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 103  
Fragment?: true
Publication
First Author: Bull LN
Year: 1998
Journal: Nat Genet
Title: A gene encoding a P-type ATPase mutated in two forms of hereditary cholestasis.
Volume: 18
Issue: 3
Pages: 219-24
Publication
First Author: Verhulst PM
Year: 2010
Journal: Hepatology
Title: A flippase-independent function of ATP8B1, the protein affected in familial intrahepatic cholestasis type 1, is required for apical protein expression and microvillus formation in polarized epithelial cells.
Volume: 51
Issue: 6
Pages: 2049-60
Publication
First Author: Paulusma CC
Year: 2008
Journal: Hepatology
Title: ATP8B1 requires an accessory protein for endoplasmic reticulum exit and plasma membrane lipid flippase activity.
Volume: 47
Issue: 1
Pages: 268-78
Publication
First Author: van der Mark VA
Year: 2016
Journal: Biochim Biophys Acta
Title: The phospholipid flippase ATP8B1 mediates apical localization of the cystic fibrosis transmembrane regulator.
Volume: 1863
Issue: 9
Pages: 2280-8
Publication
First Author: Meguro M
Year: 2001
Journal: Nat Genet
Title: A novel maternally expressed gene, ATP10C, encodes a putative aminophospholipid translocase associated with Angelman syndrome.
Volume: 28
Issue: 1
Pages: 19-20
Publication
First Author: Dhar MS
Year: 2004
Journal: J Nutr
Title: Mice heterozygous for Atp10c, a putative amphipath, represent a novel model of obesity and type 2 diabetes.
Volume: 134
Issue: 4
Pages: 799-805
Publication  
First Author: Takada N
Year: 2018
Journal: EMBO J
Title: Phospholipid-flipping activity of P4-ATPase drives membrane curvature.
Volume: 37
Issue: 9
Protein Domain
Type: Family
Description: Phospholipid-transporting ATPase IC (also known as ATP8B1 or ATPIC) belongs to subfamily IV of the P-type ATPases family, whose members transport phospholipids across the membrane. ATP8B1 can bind either CDC50A or CDC50B as its accessory protein for endoplasmic reticulum exit and plasma membrane lipid flippase activity [, , ].In hepatocytes, ATP8B1 localises in the canalicular membrane, where it may maintain the membrane integrity and to the function of ABCB4, an ABC floppase that play a role in bile export []. In the epithelial Caco-2 cells, ATP8B1 is required for apical protein expression and microvillus formation in polarised epithelial cells []. Mutations in ATP8B1 cause two forms of intrahepatic cholestasis, progressive familial intrahepatic cholestasis (PFIC) and benign recurrent intrahepatic cholestasis (BFIC) []. It is involved in the correct apical membrane localization of CDC42, CFTR and SLC10A2 [].
Protein Domain
Type: Family
Description: Phospholipid-transporting ATPase VA (also known as ATP10A or ATP10C) belongs to the IV subfamily of the P-type ATPases (P4-ATPase) family. P4-ATPases are phospholipid flippases that translocate phospholipids from the exoplasmic (lumenal) to the cytoplasmic leaflet of lipid bilayers. ATP10A is a catalytic component of P4-ATPase flippase complex, which catalyzes the hydrolysis of ATP coupled to the transport of phosphatidylcholine (PC) from the outer to the inner leaflet of the plasma membrane. However, it has low flippase activity toward glucosylceramide (GlcCer) []. ATP10A has also been shown to initiate inward plasma membrane bending and recruitment of Bin/amphiphysin/Rvs (BAR) domain-containing proteins involved in membrane tubulation and cell trafficking []. ATP10A requires CDC50A for its exit from the endoplasmic reticulum (ER) and final subcellular localisation []. ATP10A has been linked to diseases such as Angelman syndrome []and type 2 diabetes [].
Protein
Organism: Mus musculus/domesticus
Length: 328  
Fragment?: false
Publication
First Author: Gong EY
Year: 2009
Journal: Reproduction
Title: Expression of Atp8b3 in murine testis and its characterization as a testis specific P-type ATPase.
Volume: 137
Issue: 2
Pages: 345-51
Protein
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: true
Publication
First Author: Roland BP
Year: 2019
Journal: J Biol Chem
Title: Yeast and human P4-ATPases transport glycosphingolipids using conserved structural motifs.
Volume: 294
Issue: 6
Pages: 1794-1806
Publication
First Author: Coleman JA
Year: 2013
Journal: Biochim Biophys Acta
Title: Mammalian P4-ATPases and ABC transporters and their role in phospholipid transport.
Volume: 1831
Issue: 3
Pages: 555-74
Protein
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 163  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 259  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 169  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 553  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 857  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 613  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 435  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 590  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 889  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 426  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 967  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 923  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1209  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1508  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1474  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1187  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1175  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1129  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1251  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1335  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1508  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1142  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1446  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1196  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1521  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 1210  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 841  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1116  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1214  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1508  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1190  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 798  
Fragment?: true