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Search results 5801 to 5900 out of 9662 for Egf

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Type Details Score
Publication
16575836 | -
First Author: Warthen DM
Year: 2006
Journal: Hum Mutat
Title: Jagged1 (JAG1) mutations in Alagille syndrome: increasing the mutation detection rate.
Volume: 27
Issue: 5
Pages: 436-43
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Publication
12164922 | -
First Author: Piecha D
Year: 2002
Journal: J Invest Dermatol
Title: Expression of matrilin-2 in human skin.
Volume: 119
Issue: 1
Pages: 38-43
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Publication
10224097 | J:54894
First Author: Piecha D
Year: 1999
Journal: J Biol Chem
Title: Matrilin-2, a large, oligomeric matrix protein, is expressed by a great variety of cells and forms fibrillar networks.
Volume: 274
Issue: 19
Pages: 13353-61
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Publication
25329699 | J:217696
First Author: Jonas A
Year: 2014
Journal: J Clin Invest
Title: Axonally derived matrilin-2 induces proinflammatory responses that exacerbate autoimmune neuroinflammation.
Volume: 124
Issue: 11
Pages: 5042-56
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Publication
19295126 | J:150519
First Author: Malin D
Year: 2009
Journal: J Cell Sci
Title: The extracellular-matrix protein matrilin 2 participates in peripheral nerve regeneration.
Volume: 122
Issue: Pt 7
Pages: 995-1004
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Publication
24691449 | J:215040
First Author: Fullár A
Year: 2014
Journal: PLoS One
Title: Lack of Matrilin-2 favors liver tumor development via Erk1/2 and GSK-3β pathways in vivo.
Volume: 9
Issue: 4
Pages: e93469
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Publication
24613575 | -
 
First Author: Papke CL
Year: 2014
Journal: Matrix Biol
Title: Fibulin-4 and fibulin-5 in elastogenesis and beyond: Insights from mouse and human studies.
Volume: 37
Pages: 142-9
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Protein Domain
IPR026219 | Jagged/Serrate
Type: Family
Description: The Notch signalling pathway is a conserved intercellular signalling mechanism that is essential for proper embryonic development in numerous metazoan organisms []. Members of the Notch gene family encode transmembrane (TM) receptors that are critical for various cell-fate decisions. Multiple ligands that activate Notch and related receptors have been identified, including the Delta and Serrate proteins in Drosophila, and Jagged, the vertebrate orthologue of Serrate [].Members of the Jagged/Serrate group are single-pass TM proteins. They possess a large extracellular region that contains a highly conserved disulphide-rich Delta/Serrate/LAG-2 (DSL) domain, and a variable number of EGF repeats. The cytoplasmic tail region is relatively short (100-150 amino acids) and, following proteolytic cleavage, may translocate to the nucleus to mediate nuclear signalling events [].Defects in Jagged have been shown to result in Alagille syndrome, an autosomal dominant disorder that results in a paucity of intrahepatic bile ducts [].This entry represents the Jagged/Serrate protein family.
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Protein Domain
IPR041882 | SAM_ANKS1_repeat2
Type: Domain
Description: This SAM (sterile alpha motif) domain repeat 2 of ANKS1 (also known as AIDA-1) is a protein-protein interaction domain.Proteins contain this domain include ANKS1A (also known as Odin) and ANKS1B (also known as AIDA-1 or EB-1). ANKS1A modulates EGF receptor recycling and stability []. ANKS1B may participate in the regulation of nucleoplasmic coilin protein interactions []. Structurally, ANKS1 consist of N-terminal ankyrin motifs followed by two tandem sterile alpha motif (SAM) domains and a carboxyl phosphotyrosine binding (PTB) domain []. SAM domains of ANKS1 can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor []. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. The second SAM domain may decouple from the first SAM domain to facilitate translocation of AIDA-1 to the nucleus [].
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Protein Domain
IPR041880 | SAM_ANKS1_repeat1
Type: Domain
Description: This SAM (sterile alpha motif) domain repeat 1 of ANKS1 (also known as AIDA-1) is a protein-protein interaction domain.Proteins contain this domain include ANKS1A (also known as Odin) and ANKS1B (also known as AIDA-1 or EB-1). ANKS1A modulates EGF receptor recycling and stability []. ANKS1B may participate in the regulation of nucleoplasmic coilin protein interactions []. Structurally, ANKS1 consist of N-terminal ankyrin motifs followed by two tandem sterile alpha motif (SAM) domains and a carboxyl phosphotyrosine binding (PTB) domain []. SAM domains of ANKS1 can directly bind ubiquitin and participate in regulating the degradation of ubiquitinated EphA receptors, particularly EPH-A8 receptor []. SAM1 domain has a potential phosphorylation site for CMGC group of serine/threonine kinases. The second SAM domain may decouple from the first SAM domain to facilitate translocation of AIDA-1 to the nucleus [].
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Protein Domain
IPR026280 | Tissue_plasm_act
Type: Family
Description: Tissue-type plasminogen activator is a serine peptidase belonging to MEROPS peptidase family S1 (chymotrypsin family, clan PA(S)), subfamily S1A.The fibrinolytic system is the mechanism by which blood clots are dissolved via the plasmin-mediated degradation of fibrin into soluble end products. The system is activated by urokinase-type plasminogen activator (uPA; ) or by tissue-type plasminogen activator (tPA; ; this family), which are enzymes that convert the inactive proenzyme plasminogen to the active protease plasmin [].tPA is mainly involved in the activation of circulating plasminogen, while uPA activates cell-bound plasminogen after binding to a specific uPA receptor (uPAR).Following the signal sequence and propeptide regions, tPA typically contains a fibronectin type I (FN1) domain, an EGF-type domain, two kringle domains and a trypsin domain. However, there are members missing FN1 or EGF or one of the kringles.This entry also includes salivary plaminogen activators from the vampire bat (Desmodus rotundus).
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Protein Domain
IPR042135 | PX_SNX5
Type: Domain
Description: This entry represents the PX domain found in Sorting nexin-5 (SNX5). The PX domain of SNX5 binds phosphatidylinositol-3-phosphate (PI3P) and PI(3,4)P2. SNX5 is localized to a subdomain of early endosome and is recruited to the plasma membrane following EGF stimulation and elevation of PI(3,4)P2 levels [].The Phox Homology (PX) domain is a phosphoinositide (PI) binding module present in many proteins with diverse functions. Sorting nexins (SNXs) make up the largest group among PX domain containing proteins. They are involved in regulating membrane traffic and protein sorting in the endosomal system. The PX domain of SNXs binds phosphoinositides (PIs) and targets the protein to PI-enriched membranes [, ]. SNXs differ from each other in PI-binding specificity and affinity, and the presence of other protein-protein interaction domains, which help determine subcellular localization and specific function in the endocytic pathway [, , ].
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Protein Domain
IPR017048 | Fibulin-1
Type: Family
Description: Fibulins are a family of ECM glycoproteins characterized by a fibulin-type C-terminal domain preceded by tandem calcium-binding epidermal growth factor (EGF)-like modules. They are involved in protein-protein interaction with the components of basement membrane and extracellular matrix proteins. There are five fibulins, which can be classified into two subgroups. Fibulin-1 and -2 constitute one subgroup. These fibulins are larger than the others due to the presence of a higher number of EGF modules and an extra domain with three anaphylatoxin modules []. Members of the second subgroup, fibulin-3, -4, and -5, are similarly small in size and highly homologous to one another in modular structure. They consist of a modified cbEGF domain at the N terminus followed by five tandem cbEGF modules and the fibulin-type C-terminal region.This entry represents the fibulin-1 proteins, which are incorporated into fibronectin-containing matrix fibres and may play a role in cell adhesion and migration [].
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Protein Domain
IPR030747 | Matrilin-2
Type: Family
Description: Matrilin family consists of four non-collagenous extracellular matrix (ECM) proteins []. Matrilin-1 and matrilin-3 are expressed mainly in cartilage, while matrilin-2 and matrilin-4 are widely distributed in many connective tissues []. Typical matrilin has the similar domain structure with two von Willebrand factor A-like (VWA) domains interconnected by a variable number of epidermal growth factor-like (EGF) domains. The subunits form trimers or tetramers via a C-terminal α-helical coiled-coil domain [].Matrilin-2 (MATN2) is the largest and most complex matrilin. It is made up by two vWFA-like domains connected by ten EGF modules, and has a unique domain located between the second vWFA-like domain and the coiled-coil C-terminal domain []. MATN2 is a structural component of the ECM in many tissues, including the skin [, ]. It participates in peripheral nerve regeneration []and induces proinflammatory responses that could contribute to axonal damage in CNS inflammatory diseases []. It functions as a tumor suppressor in hepatocarcinogenesis [].
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Protein Domain
IPR037288 | Fibulin-5
Type: Family
Description: Fibulins are a family of ECM glycoproteins characterized by a fibulin-type C-terminal domain preceded by tandem calcium-binding epidermal growth factor (EGF)-like modules. They are involved in protein-protein interaction with the components of basement membrane and extracellular matrix proteins. There are five fibulins, which can be classified into two subgroups. Fibulin-1 and -2 constitute one subgroup. These fibulins are larger than the others due to the presence of a higher number of EGF modules and an extra domain with three anaphylatoxin modules []. Members of the second subgroup, fibulin-3, -4, and -5, are similarly small in size and highly homologous to one another in modular structure. They consist of a modified cbEGF domain at the N terminus followed by five tandem cbEGF modules and the fibulin-type C-terminal region.Fibulin-5 is a critical molecule for elastic fibre assembly. It may also have a role in regulating protease activity by interacting with beta-1 integrin as an endogenous competitive ligand [].
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Protein Domain
IPR035743 | PACSIN1/PACSIN2_SH3
Type: Domain
Description: PACSIN1 and PACSIN2 belong to the PACSIN family that contains a N-terminal F-BAR (FCH-BAR) domain and a C-terminal SH3 domain []. They are cytoplasmic phosphoproteins that play a role in vesicle formation and transport [].PACSIN1 (also known as Syndapin-1) is upregulated upon differentiation into neuronal cells []. The SH3 domain of PACSIN1 mediates activation of neural WASP (N-WASP), which is required to regulate actin polymerisation and is essential for proper neuromorphogenesis and cellular motility []. Two phosphorylation sites within the F-BAR domain of PACSIN1 are used for membrane tubulation regulation []. PACSIN2 interacts with several proteins such as Rac1, dynamin, Neuronal Wiskott-Aldrich Syndrome Protein (N-WASP), and synaptojanin via its C-terminal SH3 domain []. PACSIN2 negatively regulates the EGF (epidermal growth factor) receptor activation and signaling [, ]. It plays an important role in caveolae membrane sculpting []. This entry represents the SH3 domain of PACSINs 1 and 2.
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Protein Domain
IPR037453 | PACSIN2_F-BAR
Type: Domain
Description: PACSIN2 (protein kinase C and casein kinase substrate in neurons protein 2, also known as Syndapin-2) belongs to the PACSIN family that contains a N-terminal F-BAR (FCH-BAR) domain and a C-terminal SH3 domain []. They are cytoplasmic phosphoproteins that play a role in vesicle formation and transport []. PACSIN2 interacts with several proteins such as Rac1, dynamin, Neuronal Wiskott-Aldrich Syndrome Protein (N-WASP), and synaptojanin via its C-terminal Src homology 3 (SH3) domain []. PACSIN2 negatively regulates the EGF (epidermal growth factor) receptor activation and signaling [, ]. It plays an important role in caveolae membrane sculpting []. This entry represents the F-BAR domain of PACSIN2. F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization [].
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Publication
37317851 | J:338402
First Author: Cao X
Year: 2023
Journal: Arterioscler Thromb Vasc Biol
Title: Endothelial TIE1 Restricts Angiogenic Sprouting to Coordinate Vein Assembly in Synergy With Its Homologue TIE2.
Volume: 43
Issue: 8
Pages: e323-e338
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Publication
9287130 | J:51112
First Author: Wagener R
Year: 1997
Journal: FEBS Lett
Title: Primary structure of matrilin-3, a new member of a family of extracellular matrix proteins related to cartilage matrix protein (matrilin-1) and von Willebrand factor.
Volume: 413
Issue: 1
Pages: 129-34
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Publication
18854019 | -
 
First Author: Lim JP
Year: 2008
Journal: BMC Cell Biol
Title: A role for SNX5 in the regulation of macropinocytosis.
Volume: 9
Pages: 58
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Publication
19666031 | -
First Author: Kurabi A
Year: 2009
Journal: J Mol Biol
Title: A nuclear localization signal at the SAM-SAM domain interface of AIDA-1 suggests a requirement for domain uncoupling prior to nuclear import.
Volume: 392
Issue: 5
Pages: 1168-77
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Publication
17324935 | J:121136
First Author: Kobayashi N
Year: 2007
Journal: J Biol Chem
Title: A comparative analysis of the fibulin protein family. Biochemical characterization, binding interactions, and tissue localization.
Volume: 282
Issue: 16
Pages: 11805-16
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Publication
3282918 | -
First Author: Appella E
Year: 1988
Journal: FEBS Lett
Title: Structure and function of epidermal growth factor-like regions in proteins.
Volume: 231
Issue: 1
Pages: 1-4
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Publication
6607417 | -
First Author: Doolittle RF
Year: 1984
Journal: Nature
Title: Computer-based characterization of epidermal growth factor precursor.
Volume: 307
Issue: 5951
Pages: 558-60
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Publication
2288911 | -
First Author: Davis CG
Year: 1990
Journal: New Biol
Title: The many faces of epidermal growth factor repeats.
Volume: 2
Issue: 5
Pages: 410-9
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Publication
6334307 | -
First Author: Blomquist MC
Year: 1984
Journal: Proc Natl Acad Sci U S A
Title: Vaccinia virus 19-kilodalton protein: relationship to several mammalian proteins, including two growth factors.
Volume: 81
Issue: 23
Pages: 7363-7
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Protein Coding Gene
MGI:95411 | Erbb3
Type: protein_coding_gene
Organism: mouse, laboratory
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Publication
19797679 | J:172930
First Author: Liu Z
Year: 2009
Journal: Genome Res
Title: Rapid identification of homologous recombinants and determination of gene copy number with reference/query pyrosequencing (RQPS).
Volume: 19
Issue: 11
Pages: 2081-9
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Publication
15866159 | J:98438
First Author: Huppert SS
Year: 2005
Journal: Dev Cell
Title: Analysis of Notch function in presomitic mesoderm suggests a gamma-secretase-independent role for presenilins in somite differentiation.
Volume: 8
Issue: 5
Pages: 677-88
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Publication
17336907 | J:119151
First Author: Grego-Bessa J
Year: 2007
Journal: Dev Cell
Title: Notch signaling is essential for ventricular chamber development.
Volume: 12
Issue: 3
Pages: 415-29
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Publication
17229764 | J:119907
First Author: Cheng HT
Year: 2007
Journal: Development
Title: Notch2, but not Notch1, is required for proximal fate acquisition in the mammalian nephron.
Volume: 134
Issue: 4
Pages: 801-11
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Publication
18952909 | J:144857
First Author: Kim YH
Year: 2008
Journal: Development
Title: Artery and vein size is balanced by Notch and ephrin B2/EphB4 during angiogenesis.
Volume: 135
Issue: 22
Pages: 3755-64
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Publication
39437002 | J:360771
 
First Author: Choudhury TZ
Year: 2024
Journal: JCI Insight
Title: Impact of genetic factors on antioxidant rescue of maternal diabetes-associated congenital heart disease.
Volume: 9
Issue: 23
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Publication
22366192 | J:184926
First Author: Blackburn J
Year: 2012
Journal: Dev Biol
Title: The role of Irf6 in tooth epithelial invagination.
Volume: 365
Issue: 1
Pages: 61-70
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Publication
18365007 | J:133171
First Author: Lozier J
Year: 2008
Journal: PLoS One
Title: Notch signaling regulates bile duct morphogenesis in mice.
Volume: 3
Issue: 3
Pages: e1851
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Publication
23615281 | J:198575
First Author: Murtomaki A
Year: 2013
Journal: Development
Title: Notch1 functions as a negative regulator of lymphatic endothelial cell differentiation in the venous endothelium.
Volume: 140
Issue: 11
Pages: 2365-76
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Publication
20739676 | J:164219
First Author: Outtz HH
Year: 2010
Journal: J Immunol
Title: Notch1 deficiency results in decreased inflammation during wound healing and regulates vascular endothelial growth factor receptor-1 and inflammatory cytokine expression in macrophages.
Volume: 185
Issue: 7
Pages: 4363-73
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Publication
16120638 | J:101735
First Author: Mason HA
Year: 2005
Journal: Development
Title: Notch signaling coordinates the patterning of striatal compartments.
Volume: 132
Issue: 19
Pages: 4247-58
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Publication
12495620 | J:80793
First Author: Hippenmeyer S
Year: 2002
Journal: Neuron
Title: A role for neuregulin1 signaling in muscle spindle differentiation.
Volume: 36
Issue: 6
Pages: 1035-49
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Publication
21782525 | J:175786
First Author: Van Ho AT
Year: 2011
Journal: Dev Cell
Title: Neural crest cell lineage restricts skeletal muscle progenitor cell differentiation through Neuregulin1-ErbB3 signaling.
Volume: 21
Issue: 2
Pages: 273-87
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Publication
20829372 | J:167410
First Author: Jeannet R
Year: 2010
Journal: Blood
Title: Oncogenic activation of the Notch1 gene by deletion of its promoter in Ikaros-deficient T-ALL.
Volume: 116
Issue: 25
Pages: 5443-54
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Publication
36271747 | J:346530
First Author: Santuz A
Year: 2022
Journal: J Physiol
Title: The brain integrates proprioceptive information to ensure robust locomotion.
Volume: 600
Issue: 24
Pages: 5267-5294
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Publication
33440163 | J:320834
First Author: Pang J
Year: 2021
Journal: Cell Rep
Title: NOTCH Signaling Controls Ciliary Body Morphogenesis and Secretion by Directly Regulating Nectin Protein Expression.
Volume: 34
Issue: 2
Pages: 108603
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Publication
17331978 | J:121707
First Author: Monet M
Year: 2007
Journal: Hum Mol Genet
Title: The archetypal R90C CADASIL-NOTCH3 mutation retains NOTCH3 function in vivo.
Volume: 16
Issue: 8
Pages: 982-92
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Publication
35169019 | J:352520
First Author: Wu D
Year: 2022
Journal: J Neurosci
Title: Zcchc12-Containing Nociceptors Are Required for Noxious Heat Sensation.
Volume: 42
Issue: 13
Pages: 2690-2700
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Protein Coding Gene
MGI:2136886 | Rtn4r
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1923987 | Creld2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CAROLIEiJ_G0020144 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGI:1924696 | Heg1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CAROLIEiJ_G0020691 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGI:2152539 | Creld1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CAROLIEiJ_G0028730 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGI:1928765 | Scube2
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CAROLIEiJ_G0030316 | -
Type: protein_coding_gene
Organism: Mus caroli
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Protein Coding Gene
MGP_129S1SvImJ_G0022209 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_129S1SvImJ_G0022757 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_129S1SvImJ_G0031127 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_129S1SvImJ_G0032849 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0022168 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0022722 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0031096 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AJ_G0032833 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0022143 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0022695 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0031027 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_AKRJ_G0032764 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0022174 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0022724 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0031107 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_BALBcJ_G0032837 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0021944 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0022489 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0030601 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C3HHeJ_G0032547 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1923987 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1924696 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_2152539 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI_C57BL6J_1928765 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0022619 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0023173 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0031566 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_C57BL6NJ_G0033343 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0021466 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0022017 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0030214 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGP_CASTEiJ_G0031875 | -
Type: protein_coding_gene
Organism: mouse, laboratory
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•
•
•
•
Protein Coding Gene
MGP_CBAJ_G0021911 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_CBAJ_G0022459 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_CBAJ_G0030793 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_CBAJ_G0032520 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_DBA2J_G0022038 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_DBA2J_G0022592 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_DBA2J_G0030946 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_DBA2J_G0032672 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_FVBNJ_G0022017 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_FVBNJ_G0022567 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_FVBNJ_G0030900 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_FVBNJ_G0032625 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_LPJ_G0022109 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•
Protein Coding Gene
MGP_LPJ_G0022659 | -
Type: protein_coding_gene
Organism: mouse, laboratory
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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