| Type |
Details |
Score |
| Publication |
| First Author: |
Kwon IK |
| Year: |
2015 |
| Journal: |
Biochim Biophys Acta |
| Title: |
Mitochondrial function contributes to oxysterol-induced osteogenic differentiation in mouse embryonic stem cells. |
| Volume: |
1853 |
| Issue: |
3 |
| Pages: |
561-72 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Xia W |
| Year: |
2017 |
| Journal: |
Cell Death Differ |
| Title: |
Histone variant H3.3 orchestrates neural stem cell differentiation in the developing brain. |
| Volume: |
24 |
| Issue: |
9 |
| Pages: |
1548-1563 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Woods S |
| Year: |
2019 |
| Journal: |
Matrix Biol |
| Title: |
miR-324-5p is up regulated in end-stage osteoarthritis and regulates Indian Hedgehog signalling by differing mechanisms in human and mouse. |
| Volume: |
77 |
|
| Pages: |
87-100 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dobson THW |
| Year: |
2019 |
| Journal: |
Sci Signal |
| Title: |
Transcriptional repressor REST drives lineage stage-specific chromatin compaction at Ptch1 and increases AKT activation in a mouse model of medulloblastoma. |
| Volume: |
12 |
| Issue: |
565 |
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chen JL |
| Year: |
2019 |
| Journal: |
Cereb Cortex |
| Title: |
Gli2 Rescues Delays in Brain Development Induced by Kif3a Dysfunction. |
| Volume: |
29 |
| Issue: |
2 |
| Pages: |
751-764 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Mazzone A |
| Year: |
2019 |
| Journal: |
FASEB J |
| Title: |
Direct repression of anoctamin 1 (ANO1) gene transcription by Gli proteins. |
| Volume: |
33 |
| Issue: |
5 |
| Pages: |
6632-6642 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Infante P |
| Year: |
2021 |
| Journal: |
Cancer Lett |
| Title: |
Glabrescione B delivery by self-assembling micelles efficiently inhibits tumor growth in preclinical models of Hedgehog-dependent medulloblastoma. |
| Volume: |
499 |
|
| Pages: |
220-231 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bauer J |
| Year: |
2021 |
| Journal: |
Oncogene |
| Title: |
Context-dependent modulation of aggressiveness of pediatric tumors by individual oncogenic RAS isoforms. |
| Volume: |
40 |
| Issue: |
31 |
| Pages: |
4955-4966 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Grachtchouk M |
| Year: |
2021 |
| Journal: |
Carcinogenesis |
| Title: |
Constitutive Hedgehog/GLI2 signaling drives extracutaneous basaloid squamous cell carcinoma development and bone remodeling. |
| Volume: |
42 |
| Issue: |
8 |
| Pages: |
1100-1109 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Brennan-Crispi DM |
| Year: |
2015 |
| Journal: |
Oncotarget |
| Title: |
Crosstalk between Desmoglein 2 and Patched 1 accelerates chemical-induced skin tumorigenesis. |
| Volume: |
6 |
| Issue: |
11 |
| Pages: |
8593-605 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Saeki N |
| Year: |
2022 |
| Journal: |
Exp Cell Res |
| Title: |
Pregnane X receptor (PXR) represses osteoblast differentiation through repression of the Hedgehog signaling pathway. |
| Volume: |
416 |
| Issue: |
1 |
| Pages: |
113156 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sementino E |
| Year: |
2022 |
| Journal: |
Mol Cancer Res |
| Title: |
Inactivation of p21-Activated Kinase 2 (Pak2) Inhibits the Development of Nf2-Deficient Tumors by Restricting Downstream Hedgehog and Wnt Signaling. |
| Volume: |
20 |
| Issue: |
5 |
| Pages: |
699-711 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hu Y |
| Year: |
2022 |
| Journal: |
Front Pharmacol |
| Title: |
Gypenosides ameliorate ductular reaction and liver fibrosis via inhibition of hedgehog signaling. |
| Volume: |
13 |
|
| Pages: |
1033103 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ansari-Lari MA |
| Year: |
1998 |
| Journal: |
Genome Res |
| Title: |
Comparative sequence analysis of a gene-rich cluster at human chromosome 12p13 and its syntenic region in mouse chromosome 6. |
| Volume: |
8 |
| Issue: |
1 |
| Pages: |
29-40 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gloriam DE |
| Year: |
2005 |
| Journal: |
Biochim Biophys Acta |
| Title: |
Nine new human Rhodopsin family G-protein coupled receptors: identification, sequence characterisation and evolutionary relationship. |
| Volume: |
1722 |
| Issue: |
3 |
| Pages: |
235-46 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ansari-Lari MA |
| Year: |
1997 |
| Journal: |
Genome Res |
| Title: |
Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination. |
| Volume: |
7 |
| Issue: |
3 |
| Pages: |
268-80 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ansari-Lari MA |
| Year: |
1996 |
| Journal: |
Genome Res |
| Title: |
A gene-rich cluster between the CD4 and triosephosphate isomerase genes at human chromosome 12p13. |
| Volume: |
6 |
| Issue: |
4 |
| Pages: |
314-26 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sreedharan S |
| Year: |
2011 |
| Journal: |
FEBS J |
| Title: |
The G protein coupled receptor Gpr153 shares common evolutionary origin with Gpr162 and is highly expressed in central regions including the thalamus, cerebellum and the arcuate nucleus. |
| Volume: |
278 |
| Issue: |
24 |
| Pages: |
4881-94 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ].Computational methods, including percent identity plots, hydropathy profiles and BLAST, have been used to analyse a gene-rich cluster at human chromosome 12p13 and to compare it with its syntenic region in mouse chromosome 6 [, , ]. Of 6 genes identified, a number were novel receptors, including GPR153 (also known as PGR1) and GPR162 (also known as GRCA) []. GPR153 is a cerebellar target of the Gli1 transcription factor, which is involved in the maintenance and proliferation of grabule neuron precursor cells in the cerebellum, and like GPR162 has a noted role in food uptake and decision making processes [].This entry represents G-protein coupled receptor 153 and G-protein coupled receptor 162. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ].Computational methods, including percent identity plots, hydropathy profiles and BLAST, have been used to analyse a gene-rich cluster at human chromosome 12p13 and to compare it with its syntenic region in mouse chromosome 6 [, , ]. Of 6 genes identified, a number were novel receptors, including GPR153 (also known as PGR1) and GPR162 (also known as GRCA) []. GPR153 is a cerebellar target of the Gli1 transcription factor, which is involved in the maintenance and proliferation of grabule neuron precursor cells in the cerebellum, and like GPR162 has a noted role in food uptake and decision making processes [].This entry represents G-protein coupled receptor 162. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
G protein-coupled receptors (GPCRs) constitute a vast protein family that encompasses a wide range of functions, including various autocrine, paracrine and endocrine processes. They show considerable diversity at the sequence level, on the basis of which they can be separated into distinct groups []. The term clan can be used to describe the GPCRs, as they embrace a group of families for which there are indications of evolutionary relationship, but between which there is no statistically significant similarity in sequence []. The currently known clan members include rhodopsin-like GPCRs (Class A, GPCRA), secretin-like GPCRs (Class B, GPCRB), metabotropic glutamate receptor family (Class C, GPCRC), fungal mating pheromone receptors (Class D, GPCRD), cAMP receptors (Class E, GPCRE) and frizzled/smoothened (Class F, GPCRF) [, , , , ]. GPCRs are major drug targets, and are consequently the subject of considerable research interest. It has been reported that the repertoire of GPCRs for endogenous ligands consists of approximately 400 receptors in humans and mice []. Most GPCRs are identified on the basis of their DNA sequences, rather than the ligand they bind, those that are unmatched to known natural ligands are designated by as orphan GPCRs, or unclassified GPCRs [].The rhodopsin-like GPCRs (GPCRA) represent a widespread protein family that includes hormone, neurotransmitter and light receptors, all of which transduce extracellular signals through interaction with guanine nucleotide-binding (G) proteins. Although their activating ligands vary widely in structure and character, the amino acid sequences of the receptors are very similar and are believed to adopt a common structural framework comprising 7 transmembrane (TM) helices [, , ].Computational methods, including percent identity plots, hydropathy profiles and BLAST, have been used to analyse a gene-rich cluster at human chromosome 12p13 and to compare it with its syntenic region in mouse chromosome 6 [, , ]. Of 6 genes identified, a number were novel receptors, including GPR153 (also known as PGR1) and GPR162 (also known as GRCA) []. GPR153 is a cerebellar target of the Gli1 transcription factor, which is involved in the maintenance and proliferation of grabule neuron precursor cells in the cerebellum, and like GPR162 has a noted role in food uptake and decision making processes [].This entry represents G-protein coupled receptor 153, identified by conserved sections along the length of the protein that characterise GP153 and distinguish itfrom closely related GP162 proteins. |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
776
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
163
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Argenti B |
| Year: |
2005 |
| Journal: |
J Neurosci |
| Title: |
Hedgehog antagonist REN(KCTD11) regulates proliferation and apoptosis of developing granule cell progenitors. |
| Volume: |
25 |
| Issue: |
36 |
| Pages: |
8338-46 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kalogeropoulos M |
| Year: |
2010 |
| Journal: |
FASEB J |
| Title: |
Zic1 transcription factor in bone: neural developmental protein regulates mechanotransduction in osteocytes. |
| Volume: |
24 |
| Issue: |
8 |
| Pages: |
2893-903 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Paudel S |
| Year: |
2022 |
| Journal: |
Carcinogenesis |
| Title: |
Chemopreventive efficacy of silibinin against basal cell carcinoma growth and progression in UVB-irradiated Ptch+/- mice. |
| Volume: |
43 |
| Issue: |
6 |
| Pages: |
557-570 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zurawel RH |
| Year: |
2000 |
| Journal: |
Genes Chromosomes Cancer |
| Title: |
Evidence that haploinsufficiency of Ptch leads to medulloblastoma in mice. |
| Volume: |
28 |
| Issue: |
1 |
| Pages: |
77-81 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Eichenmüller M |
| Year: |
2007 |
| Journal: |
Int J Oncol |
| Title: |
Hedgehog-independent overexpression of transforming growth factor-beta1 in rhabdomyosarcoma of Patched1 mutant mice. |
| Volume: |
31 |
| Issue: |
2 |
| Pages: |
405-12 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Li X |
| Year: |
2004 |
| Journal: |
BMC Dev Biol |
| Title: |
Hedgehog can drive terminal differentiation of amniote slow skeletal muscle. |
| Volume: |
4 |
|
| Pages: |
9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hewitt SC |
| Year: |
2020 |
| Journal: |
Endocrinology |
| Title: |
Peri- and Postpubertal Estrogen Exposures of Female Mice Optimize Uterine Responses Later in Life. |
| Volume: |
161 |
| Issue: |
8 |
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Li X |
| Year: |
2020 |
| Journal: |
FASEB J |
| Title: |
Ciliary IFT80 is essential for intervertebral disc development and maintenance. |
| Volume: |
34 |
| Issue: |
5 |
| Pages: |
6741-6756 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sheng H |
| Year: |
2002 |
| Journal: |
Cancer Res |
| Title: |
Dissecting the oncogenic potential of Gli2: deletion of an NH(2)-terminal fragment alters skin tumor phenotype. |
| Volume: |
62 |
| Issue: |
18 |
| Pages: |
5308-16 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Nicot A |
| Year: |
2002 |
| Journal: |
J Neurosci |
| Title: |
Pituitary adenylate cyclase-activating polypeptide and sonic hedgehog interact to control cerebellar granule precursor cell proliferation. |
| Volume: |
22 |
| Issue: |
21 |
| Pages: |
9244-54 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang J |
| Year: |
2015 |
| Journal: |
Neurobiol Dis |
| Title: |
Fingolimod treatment promotes proliferation and differentiation of oligodendrocyte progenitor cells in mice with experimental autoimmune encephalomyelitis. |
| Volume: |
76 |
|
| Pages: |
57-66 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Shi X |
| Year: |
2018 |
| Journal: |
Front Immunol |
| Title: |
Sonic Hedgehog Signaling Regulates Hematopoietic Stem/Progenitor Cell Activation during the Granulopoietic Response to Systemic Bacterial Infection. |
| Volume: |
9 |
|
| Pages: |
349 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
297
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rubin JB |
| Year: |
2002 |
| Journal: |
Cancer Cell |
| Title: |
Medulloblastoma: a problem of developmental biology. |
| Volume: |
2 |
| Issue: |
1 |
| Pages: |
7-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Taylor MD |
| Year: |
2002 |
| Journal: |
Nat Genet |
| Title: |
Mutations in SUFU predispose to medulloblastoma. |
| Volume: |
31 |
| Issue: |
3 |
| Pages: |
306-10 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Merchant M |
| Year: |
2004 |
| Journal: |
Mol Cell Biol |
| Title: |
Suppressor of fused regulates Gli activity through a dual binding mechanism. |
| Volume: |
24 |
| Issue: |
19 |
| Pages: |
8627-41 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kang HS |
| Year: |
2010 |
| Journal: |
Histol Histopathol |
| Title: |
Gli-similar (Glis) Krüppel-like zinc finger proteins: insights into their physiological functions and critical roles in neonatal diabetes and cystic renal disease. |
| Volume: |
25 |
| Issue: |
11 |
| Pages: |
1481-96 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
588
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
631
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
608
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
371
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
407
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
205
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
264
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
238
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
277
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
433
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
261
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
376
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
422
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
248
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
418
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
530
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
241
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
201
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
389
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
255
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
389
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
456
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
246
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
240
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
442
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
353
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
310
 |
| Fragment?: |
false |
|
•
•
•
•
•
|