| 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 |
|
•
•
•
•
•
|