MouseMine: Keyword Search

Protein

Organism:	Mus musculus/domesticus
Length:	261
Fragment?:	false

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Publication

9218782 | -

First Author:	Hyvönen M
Year:	1997
Journal:	EMBO J
Title:	Structure of the PH domain and Btk motif from Bruton's tyrosine kinase: molecular explanations for X-linked agammaglobulinaemia.
Volume:	16
Issue:	12
Pages:	3396-404

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Publication

8070576 | -

First Author:	Vihinen M
Year:	1994
Journal:	FEBS Lett
Title:	Tec homology (TH) adjacent to the PH domain.
Volume:	350
Issue:	2-3
Pages:	263-5

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Publication

9280283 | -

First Author:	Vihinen M
Year:	1997
Journal:	FEBS Lett
Title:	Missense mutations affecting a conserved cysteine pair in the TH domain of Btk.
Volume:	413
Issue:	2
Pages:	205-10

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Publication

9796816 | -

First Author:	Jiang Y
Year:	1998
Journal:	Nature
Title:	The G protein G alpha12 stimulates Bruton's tyrosine kinase and a rasGAP through a conserved PH/BM domain.
Volume:	395
Issue:	6704
Pages:	808-13

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Publication

15661031 | -

First Author:	Lindvall JM
Year:	2005
Journal:	Immunol Rev
Title:	Bruton's tyrosine kinase: cell biology, sequence conservation, mutation spectrum, siRNA modifications, and expression profiling.
Volume:	203

Pages:	200-15

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Publication

8407793 | -

First Author:	Kammler M
Year:	1993
Journal:	J Bacteriol
Title:	Characterization of the ferrous iron uptake system of Escherichia coli.
Volume:	175
Issue:	19
Pages:	6212-9

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Publication

16718600 | -

First Author:	Cartron ML
Year:	2006
Journal:	Biometals
Title:	Feo--transport of ferrous iron into bacteria.
Volume:	19
Issue:	2
Pages:	143-57

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Publication

2162892 | -

First Author:	Lee KP
Year:	1990
Journal:	J Immunol
Title:	The genomic organization of the CD28 gene. Implications for the regulation of CD28 mRNA expression and heterogeneity.
Volume:	145
Issue:	1
Pages:	344-52

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Publication

11698427 | J:72679

First Author:	Suresh M
Year:	2001
Journal:	J Immunol
Title:	Role of CD28-B7 interactions in generation and maintenance of CD8 T cell memory.
Volume:	167
Issue:	10
Pages:	5565-73

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Publication

11698433 | J:72680

First Author:	Mittrücker HW
Year:	2001
Journal:	J Immunol
Title:	Role of CD28 for the generation and expansion of antigen-specific CD8(+) T lymphocytes during infection with Listeria monocytogenes.
Volume:	167
Issue:	10
Pages:	5620-7

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Publication

11827987 | -

First Author:	Frauwirth KA
Year:	2002
Journal:	J Clin Invest
Title:	Activation and inhibition of lymphocytes by costimulation.
Volume:	109
Issue:	3
Pages:	295-9

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Publication

11884439 | -

First Author:	Appleman LJ
Year:	2002
Journal:	J Immunol
Title:	CD28 costimulation mediates down-regulation of p27kip1 and cell cycle progression by activation of the PI3K/PKB signaling pathway in primary human T cells.
Volume:	168
Issue:	6
Pages:	2729-36

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Publication

14552840 | -

First Author:	Pitcher LA
Year:	2003
Journal:	Trends Immunol
Title:	T-cell receptor signal transmission: who gives an ITAM?
Volume:	24
Issue:	10
Pages:	554-60

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Publication

18925375 | -

First Author:	Rybakin V
Year:	2008
Journal:	Subcell Biochem
Title:	Role of Mammalian coronin 7 in the biosynthetic pathway.
Volume:	48

Pages:	110-5

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Publication

15892111 | -

First Author:	Rybakin V
Year:	2005
Journal:	Bioessays
Title:	Coronin proteins as multifunctional regulators of the cytoskeleton and membrane trafficking.
Volume:	27
Issue:	6
Pages:	625-32

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Publication

11030354 | -

First Author:	Schlessinger J
Year:	2000
Journal:	Mol Cell
Title:	Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization.
Volume:	6
Issue:	3
Pages:	743-50

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Publication

16207751 | J:102949

First Author:	Li C
Year:	2005
Journal:	Development
Title:	FGFR1 function at the earliest stages of mouse limb development plays an indispensable role in subsequent autopod morphogenesis.
Volume:	132
Issue:	21
Pages:	4755-64

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Publication

2162671 | -

First Author:	Itoh N
Year:	1990
Journal:	Biochem Biophys Res Commun
Title:	The complete amino acid sequence of the shorter form of human basic fibroblast growth factor receptor deduced from its cDNA.
Volume:	169
Issue:	2
Pages:	680-5

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Publication

17360555 | -

First Author:	Riley BM
Year:	2007
Journal:	Proc Natl Acad Sci U S A
Title:	Impaired FGF signaling contributes to cleft lip and palate.
Volume:	104
Issue:	11
Pages:	4512-7

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Publication

21331089 | -

First Author:	Dixon MJ
Year:	2011
Journal:	Nat Rev Genet
Title:	Cleft lip and palate: understanding genetic and environmental influences.
Volume:	12
Issue:	3
Pages:	167-78

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Publication

20696164 | -

First Author:	Kärkkäinen S
Year:	2010
Journal:	FEBS Lett
Title:	POSH2 is a RING finger E3 ligase with Rac1 binding activity through a partial CRIB domain.
Volume:	584
Issue:	18
Pages:	3867-72

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Publication

15190477 | -

First Author:	Porchet N
Year:	2004
Journal:	Med Sci (Paris)
Title:	[MUC genes: mucin or not mucin? That is the question].
Volume:	20
Issue:	5
Pages:	569-74

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Publication

12479863 | -

First Author:	Himanen JP
Year:	2003
Journal:	Int J Biochem Cell Biol
Title:	Eph receptors and ephrins.
Volume:	35
Issue:	2
Pages:	130-4

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Publication

18394988 | -

First Author:	Pasquale EB
Year:	2008
Journal:	Cell
Title:	Eph-ephrin bidirectional signaling in physiology and disease.
Volume:	133
Issue:	1
Pages:	38-52

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Publication

15561600 | -

First Author:	Surawska H
Year:	2004
Journal:	Cytokine Growth Factor Rev
Title:	The role of ephrins and Eph receptors in cancer.
Volume:	15
Issue:	6
Pages:	419-33

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Publication

18281458 | -

First Author:	Arvanitis D
Year:	2008
Journal:	Genes Dev
Title:	Eph/ephrin signaling: networks.
Volume:	22
Issue:	4
Pages:	416-29

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Publication

20476842 | -

First Author:	Ia KK
Year:	2010
Journal:	Growth Factors
Title:	Structural elements and allosteric mechanisms governing regulation and catalysis of CSK-family kinases and their inhibition of Src-family kinases.
Volume:	28
Issue:	5
Pages:	329-50

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Publication

21393838 | -

First Author:	Gunn NJ
Year:	2011
Journal:	Acta Crystallogr Sect F Struct Biol Cryst Commun
Title:	Purification, crystallization, small-angle X-ray scattering and preliminary X-ray diffraction analysis of the SH2 domain of the Csk-homologous kinase.
Volume:	67
Issue:	Pt 3
Pages:	336-9

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Publication

19182796 | J:150550

First Author:	Xu NJ
Year:	2009
Journal:	Nat Neurosci
Title:	Ephrin-B3 reverse signaling through Grb4 and cytoskeletal regulators mediates axon pruning.
Volume:	12
Issue:	3
Pages:	268-76

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Publication

24962474 | -

First Author:	Nikonova AS
Year:	2014
Journal:	IUBMB Life
Title:	CAS proteins in health and disease: an update.
Volume:	66
Issue:	6
Pages:	387-95

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Publication

26119091 | -

First Author:	Deneka A
Year:	2015
Journal:	Gene
Title:	Embryonal Fyn-associated substrate (EFS) and CASS4: The lesser-known CAS protein family members.
Volume:	570
Issue:	1
Pages:	25-35

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Protein Domain

IPR028174 | FGF_rcpt_1

Type:

Domain

Description:

Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].The FGFRs consist of an extracellular ligand-binding domain composed of three immunoglobulin-like domains (D1-D3), a single transmembrane helix domain, and an intracellular domain with tyrosine kinase activity []. The three immunoglobin(Ig)-like domains, D1, D2, and D3, present a stretch of acidic amino acids (known as the acid box) between D1 and D2. This acid box can participate in the regulation of FGF binding to the FGFR. Immunoglobulin-like domains D2 and D3 are sufficient for FGF binding. FGFR family members differ from one another in their ligandaffinities and tissue distribution [, ]. Most FGFs can bind to several different FGFR subtypes. Indeed, FGF1 is sometimes referred to as the universal ligand, as it is capable of activating all of the different FGFRs []. However, there are some exceptions. For example, FGF7 only interacts with FGFR2 []and FGF18 was recently shown to only activate FGFR3 []. Fibroblast growth factor receptor 1 (FGFR1) binds both acidic and basic fibroblast growth factors and is involved in limb induction []. FGFR1 has been shown to be associated with Pfeiffer syndrome [], and cleft lip and/or palate [, ]. Fibroblast growth factor receptor 1 has been shown to interact with growth factor receptor-bound protein 14 (GRB14) [], Src homology 2 domain containing adaptor protein B (SHB) [], fibroblast growth factor receptor substrate 2 (FRS2)[]and fibroblast growth factor 1 (FGF1) [, ].This entry represents the catalytic domain of FGFR1.

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Protein Domain

IPR002404 | IRS_PTB

Type:

Domain

Description:

Insulin receptor substrate (IRS) molecules are mediators in insulin signaling and play a role in maintaining basic cellular functions such as growth and metabolism. They act as docking proteins between the insulin receptor and a complex network of intracellular signaling molecules containing Src homology 2 (SH2) domains. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family have been identified that differ as to tissue distribution, subcellular localization, developmental expression, binding to the insulin receptor, and interaction with SH2 domain-containing proteins. IRS molecules have an N-terminal pleckstrin homology domain (), followed by an IRS-like phosphotyrosine binding (PTB) domain which has a PH-like fold. These domains facilitate interaction with the activated tyrosine-phosphorylated insulin receptor. The PTB domain is situated towards the N terminus. Two arginines in this domain are responsible for hydrogen bonding phosphotyrosine residues on a Ac-LYASSNPApY-NH2 peptide in the juxtamembrane region of the insulin receptor. Further interactions via `bridged' water molecules are coordinated by residues an Asn and a Ser residue [].PTB domains function as adaptors or scaffolds to organise the signalling complexes involved in wide-ranging physiological processes including neural development, immunity, tissue homeostasis and cell growth. Due to structural differences,PTB domains are divided into three groups represented by phosphotyrosine-dependent IRS-like, phosphotyrosine-dependent Shc-like, and phosphotyrosine-independent Dab-like PTBs.IRS-type PTB domain has an average length of about 100 amino acids. It bindsto the insulin receptor through the Asn-Pro-Xaa-Tyr(P) motif found in manytyrosine-phosphorylated proteins. This domain is found in IRS/Dok/SNT proteinsthat are the major adapters for RTK and cytokine signaling. This domain bindsboth peptides and headgroups of phosphatidylinositides, utilizing two distinctbinding motifs to mediate spatial organisation and localization within cells.The IRS-type PTB domain is found alone or in association with the PH domain [, ]. More recent studies have found that some types of PTB domains can bind to peptides lack tyrosine residues altogether. In contrast to SH2 domains, which recognize phosphotyrosine and adjacent carboxy-terminal residues, PTB-domain binding specificity is conferred by residues amino-terminal to the phosphotyrosine. PTB domains are classified into three groups: phosphotyrosine-dependent Shc-like, phosphotyrosine-dependent IRS-like, and phosphotyrosine-independent Dab-like PTB domains. This entry is part of the IRS-like subgroup [, ].The 3D structure of IRS-type PTB domain has been solved []. It shares a folding pattern commonly referred to as the PH-domain "superfold". The core "superfold"consists of seven antiparallel beta strands forming two orthogonal beta sheets. This beta sandwich is capped at the C terminus by an alpha helix. It contains a peptide binding pocket (formed by the beta strand 5 and the C-terminal alpha helix) and a highly basic phospholipid binding "crown"(largely composed of residues from loop regions near the N terminus) [].

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Protein Domain

IPR035027 | Csk-like_SH2

Type:

Domain

Description:

This entry represents the SH2 domain found in CSK and CHK. Both the C-terminal Src kinase (CSK) and CSK-homologous kinase (CHK) are members of the CSK-family of protein tyrosine kinases. These proteins suppress activity of Src-family kinases (SFK) by selectively phosphorylating the conserved C-terminal tail regulatory tyrosine by a similar mechanism []. CHK is also capable of inhibiting SFKs by a non-catalytic mechanism that involves binding of CHK to SFKs to form stable protein complexes. The unphosphorylated form of SFKs is inhibited by CSK and CHK by a two-step mechanism. The first step involves the formation of a complex of SFKs with CSK/CHK with the SFKs in the complex are inactive. The second step, involves the phosphorylation of the C-terminal tail tyrosine of SFKs, which then dissociates and adopt an inactive conformation. The structural basis of how the phosphorylated SFKs dissociate from CSK/CHK to adopt the inactive conformation is not known. The inactive conformation of SFKs is stabilized by two intramolecular inhibitory interactions: (a) the pYT:SH2 interaction in which the phosphorylated C-terminal tail tyrosine (YT) binds to the SH2 domain, and (b) the linker:SH3 interaction of which the SH2-kinase domain linker binds to the SH3 domain. SFKs are activated by multiple mechanisms including binding of the ligands to the SH2 and SH3 domains to displace the two inhibitory intramolecular interactions, autophosphorylation, and dephosphorylation of YT. By selective phosphorylation and the non-catalytic inhibitory mechanism CSK and CHK are able to inhibit the active forms of SFKs []. CSK and CHK are regulated by phosphorylation and inter-domain interactions. They both contain SH3, SH2, and kinase domains separated by the SH3-SH2 connector and SH2 kinase linker, intervening segments separating the three domains. They lack a conserved tyrosine phosphorylation site in the kinase domain and the C-terminal tail regulatory tyrosine phosphorylation site. The CSK SH2 domain is crucial for stabilizing the kinase domain in the active conformation. A disulfide bond here regulates CSK kinase activity. The subcellular localization and activity of CSK are regulated by its SH2 domain []. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites [].

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Protein Domain

IPR008093 | CD28

Type:

Family

Description:

Antigen (Ag) recognition by the T cell receptor (TCR) induces activation ofT lymphocytes. However, TCR-mediated signals alone are insufficient forefficient T cell activation, and additional co-stimulatory signals are required. One of the most important surface molecules that delivers co-stimulatory signals for T cells is CD28. The human T lymphocyte Ag CD28 (Tp44) is a homodimeric 90kDa glycoprotein expressed on the surface of themajority of human peripheral T cells and lymphocytes. Stimulation of CD4+ Tcells in the absence of CD28 co-signalling causes impaired proliferation, reduced cytokine production and altered generation of helper T cell subsets.Co-stimulation via CD28 promotes T cell viability, clonal expansion,cytokine production and effector functions, while also regulating apoptosisof activated T cells, suggesting its importance in regulating long-term T cell survival [, , , ].Ligands for CD28 and the structurally related CTLA-4 (CD152) are themolecules B7.1 (CD80) and B7.2 (CD86). B7.1 and B7.2 are expressed onprofessional antigen presenting cells (APCs) and their expression is up-regulated during an immune response. Ligation of CD28 by its natural ligandsresults in tyrosine phosphorylation at a YMNM motif within its cytoplasmictail. The phosphorylated motif subsequently interacts with the Src homology2 domain in the p85 regulatory subunit of P13K, activating the p110 catalytic subunit. One of the P13K-dependent downstream targets, resulting from the antibody cross-linking of CD28, is the phoshporylation and activation of Akt (or PKB). Constitutively active Akt is able to substitutefor CD28 signals, and stimulates IL-2 production when introduced into matureCD28-deficient cells. Another molecule affected by CD28 stimulation is theproto-oncogene Vav, which acts as a guanine-nucleotide exchange factor forRac and CDC42, allowing these molecules to switch from the inactive GDP-bound state to the active GTP-bound state [, ].Another interesting feature of CD28, is its ability to induce expression ofPDE7, a cAMP phosphodiesterase, thus reducing cellular cAMP levels. cAMP hasbeen reported to affect nearly every pathway important for lymphocyteactivation, leading to inhibition of T cell proliferation. Specifically,increased intracellular cAMP has been implicated in the induction of T cellanergy, a non-responsive state that occurs after T cells are stimulatedthrough TCR/CD3 in the absence of co-stimulation. This can have therapeutic implications, in that blockage of CD28 co-stimulation can be profoundlyimmunosuppressive, preventing induction of pathogenic T cell responses inautoimmune disease models, and allowing for prolonged acceptance of allografts in models of organ transplantation []. Finally, CD28 co-stimulation directly controls T cell cycle progression by down-regulating the cdk inhibitor p27kip1, which actually integratesmitogenic MEK and P13K-dependent signals from both TCR and CD28 [].

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Protein Domain

IPR001562 | Znf_Btk_motif

Type:

Conserved_site

Description:

The Btk-type zinc finger or Btk motif (BM) is a conserved zinc-binding motif containing conserved cysteines and a histidine that is present in certain eukaryotic signalling proteins. The motif is named after Bruton's tyrosine kinase (Btk), an enzyme which is essential for B cell maturation in humans and mice [, ]. Btk is a member of the Tec family of protein tyrosine kinases (PTK). These kinases contain a conserved Tec homology (TH) domain between the N-terminal pleckstrin homology (PH) domain () and the Src homology 3 (SH3) domain (). The N-terminal of the TH domain is highly conserved and known as the Btf motif, while the C-terminal region of the TH domain contains a proline-rich region (PRR). The Btk motif contains a conserved His and three Cys residues that form a zinc finger (although these differ from known zinc finger topologies), while PRRs are commonly involved in protein-protein interactions, including interactions with G proteins [, ]. The TH domain may be of functional importance in various signalling pathways in different species []. A complete TH domain, containing both the Btk and PRR regions, has not been found outside the Tec family; however, the Btk motif on its own does occur in other proteins, usually C-terminal to a PH domain (note that although a Btk motif always occurs C-terminal to a PH domain, not all PH domains are followed by a Btk motif).The crystal structures of Btk show that the Btk-type zinc finger has a globular core, formed by a long loop which is held together by a zinc ion, and that the Btk motif is packed against the PH domain []. The zinc-binding residues are a histidine and three cysteines, which are fully conserved in the Btk motif []. Proteins known to contain a Btk-type zinc finger include:Mammalian Bruton's tyrosine kinase (Btk), a protein tyrosine kinase involved in modulation of diverse cellular processes. Mutations affecting Btk are the cause of X-linked agammaglobulinemia (XLA) in humans and X-linked immunodeficiency in mice. Mammalian Tec, Bmx, and Itk proteins, which are tyrosine protein kinases of the Tec subfamily. Drosophila tyrosine-protein kinase Btk29A, which is required for the development of proper ring canals and of male genitalia and required for adult survival. Mammalian Ras GTPase-activating proteins (RasGAP), which regulate the activation of inactive GDP-bound Ras by converting GDP to GTP.

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Publication

15970507 | J:103183

First Author:	Naz RK
Year:	2005
Journal:	Front Biosci
Title:	Gene knockouts that cause female infertility: search for novel contraceptive targets.
Volume:	10

Pages:	2447-59

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Publication

24069548 | J:202463

First Author:	Li J
Year:	2013
Journal:	JAKSTAT
Title:	JAK-STAT and bone metabolism.
Volume:	2
Issue:	3
Pages:	e23930

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Protein

Q9JIE3

Organism:	Mus musculus/domesticus
Length:	128
Fragment?:	false

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Protein

Q3TC93

Organism:	Mus musculus/domesticus
Length:	395
Fragment?:	false

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Protein

Q64355

Organism:	Mus musculus/domesticus
Length:	560
Fragment?:	false

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Publication

11179684 | J:67538

First Author:	Sumoy L
Year:	2001
Journal:	Gene
Title:	PACSIN 3 is a novel SH3 domain cytoplasmic adapter protein of the pacsin-syndapin-FAP52 gene family.
Volume:	262
Issue:	1-2
Pages:	199-205

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Protein

Q922K9

Organism:	Mus musculus/domesticus
Length:	512
Fragment?:	false

•

Protein

Q3UR97

Organism:	Mus musculus/domesticus
Length:	363
Fragment?:	false

•

Protein

Q80ZJ7

Organism:	Mus musculus/domesticus
Length:	404
Fragment?:	false

•

Protein

Q80UW3

Organism:	Mus musculus/domesticus
Length:	563
Fragment?:	false

•

Protein

Q6P8Y7

Organism:	Mus musculus/domesticus
Length:	439
Fragment?:	false

•

Protein

Q6P4T1

Organism:	Mus musculus/domesticus
Length:	997
Fragment?:	false

•

Protein

Q921I6

Organism:	Mus musculus/domesticus
Length:	962
Fragment?:	false

•

Protein

Q91WE1

Organism:	Mus musculus/domesticus
Length:	337
Fragment?:	false

•

Protein

Q9D3S3

Organism:	Mus musculus/domesticus
Length:	818
Fragment?:	false

•

Protein

Q9CY18

Organism:	Mus musculus/domesticus
Length:	387
Fragment?:	false

•

Protein

Q8CE50

Organism:	Mus musculus/domesticus
Length:	437
Fragment?:	false

•

Protein

O70492

Organism:	Mus musculus/domesticus
Length:	162
Fragment?:	false

•

Protein

Q9D2Y5

Organism:	Mus musculus/domesticus
Length:	313
Fragment?:	false

•

Protein

F7D3B8

Organism:	Mus musculus/domesticus
Length:	362
Fragment?:	true

•

Protein

Q8BXH2

Organism:	Mus musculus/domesticus
Length:	250
Fragment?:	false

•

Protein

A0A1W2P6R8

Organism:	Mus musculus/domesticus
Length:	157
Fragment?:	true

•

Protein

Q3TXT4

Organism:	Mus musculus/domesticus
Length:	299
Fragment?:	false

•

Protein

Q3TC10

Organism:	Mus musculus/domesticus
Length:	336
Fragment?:	false

•

Protein

A0A494B972

Organism:	Mus musculus/domesticus
Length:	451
Fragment?:	false

•

Protein

F6RSR4

Organism:	Mus musculus/domesticus
Length:	386
Fragment?:	true

•

Protein

D3Z3J1

Organism:	Mus musculus/domesticus
Length:	67
Fragment?:	true

•

Protein

Q99KI8

Organism:	Mus musculus/domesticus
Length:	567
Fragment?:	true

•

Protein

F8WI30

Organism:	Mus musculus/domesticus
Length:	445
Fragment?:	false

•

Protein

A0A0R4J0D0

Organism:	Mus musculus/domesticus
Length:	313
Fragment?:	false

•

Protein

A0A286YCE4

Organism:	Mus musculus/domesticus
Length:	194
Fragment?:	true

•

Protein

A0A0G2JEQ9

Organism:	Mus musculus/domesticus
Length:	176
Fragment?:	true

•

Protein

Q149Q9

Organism:	Mus musculus/domesticus
Length:	218
Fragment?:	false

•

Protein

A0A2R8VHH6

Organism:	Mus musculus/domesticus
Length:	374
Fragment?:	true

•

Protein

A0A0G2JGD5

Organism:	Mus musculus/domesticus
Length:	110
Fragment?:	true

•

Protein

Q8BPC1

Organism:	Mus musculus/domesticus
Length:	393
Fragment?:	false

•

Protein

D3YWH1

Organism:	Mus musculus/domesticus
Length:	192
Fragment?:	true

•

Protein

H3BKG9

Organism:	Mus musculus/domesticus
Length:	87
Fragment?:	false

•

Protein

Q8K0F6

Organism:	Mus musculus/domesticus
Length:	560
Fragment?:	false

•

Protein

A0A338P7D2

Organism:	Mus musculus/domesticus
Length:	248
Fragment?:	false

•

Protein

D3Z479

Organism:	Mus musculus/domesticus
Length:	251
Fragment?:	false

•

Protein

Q3TEK6

Organism:	Mus musculus/domesticus
Length:	239
Fragment?:	false

•

Protein

Q3U332

Organism:	Mus musculus/domesticus
Length:	900
Fragment?:	false

•

Protein

Q5M8N3

Organism:	Mus musculus/domesticus
Length:	387
Fragment?:	false

•

Protein

Q78ZM0

Organism:	Mus musculus/domesticus
Length:	162
Fragment?:	false

•

Protein

Q548U4

Organism:	Mus musculus/domesticus
Length:	128
Fragment?:	false

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Publication

8931154 | -

First Author:	Ponting CP
Year:	1996
Journal:	Protein Sci
Title:	Novel domains in NADPH oxidase subunits, sorting nexins, and PtdIns 3-kinases: binding partners of SH3 domains?
Volume:	5
Issue:	11
Pages:	2353-7

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Publication

9788876 | -

First Author:	Singer-Krüger B
Year:	1998
Journal:	J Cell Sci
Title:	Synaptojanin family members are implicated in endocytic membrane traffic in yeast.
Volume:	111 ( Pt 22)

Pages:	3347-56

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Publication

23236520 | -

First Author:	Goh SL
Year:	2012
Journal:	PLoS One
Title:	Versatile membrane deformation potential of activated pacsin.
Volume:	7
Issue:	12
Pages:	e51628

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Protein

Q99M51

Organism:	Mus musculus/domesticus
Length:	377
Fragment?:	false

•

Protein

O55033

Organism:	Mus musculus/domesticus
Length:	380
Fragment?:	false

•

Protein

Q8BQ28

Organism:	Mus musculus/domesticus
Length:	380
Fragment?:	false

•

Publication

32600062 | J:303638

First Author:	Li Y
Year:	2020
Journal:	Circulation
Title:	gp130 Controls Cardiomyocyte Proliferation and Heart Regeneration.
Volume:	142
Issue:	10
Pages:	967-982

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Publication

33727334 | J:306234

First Author:	Tsai WL
Year:	2021
Journal:	J Neurosci
Title:	Paxillin Is Required for Proper Spinal Motor Axon Growth into the Limb.
Volume:	41
Issue:	17
Pages:	3808-3821

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Publication

29803828 | J:269675

First Author:	Giralt A
Year:	2018
Journal:	Exp Neurol
Title:	PTK2B/Pyk2 overexpression improves a mouse model of Alzheimer's disease.
Volume:	307

Pages:	62-73

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Publication

33563722 | J:304040

First Author:	Asaoka N
Year:	2021
Journal:	J Neurosci
Title:	NOX1/NADPH Oxidase Promotes Synaptic Facilitation Induced by Repeated D₂ Receptor Stimulation: Involvement in Behavioral Repetition.
Volume:	41
Issue:	12
Pages:	2780-2794

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Publication

32485177 | J:305502

First Author:	Sorrentino G
Year:	2020
Journal:	Gastroenterology
Title:	Bile Acids Signal via TGR5 to Activate Intestinal Stem Cells and Epithelial Regeneration.
Volume:	159
Issue:	3
Pages:	956-968.e8

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Publication

30043596 | J:286493

First Author:	Yamagishi K
Year:	2018
Journal:	Eur J Histochem
Title:	Activation of the renin-angiotensin system in mice aggravates mechanical loading-induced knee osteoarthritis.
Volume:	62
Issue:	3

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Publication

29965781 | J:306921

First Author:	Dong W
Year:	2018
Journal:	Autophagy
Title:	RAB26-dependent autophagy protects adherens junctional integrity in acute lung injury.
Volume:	14
Issue:	10
Pages:	1677-1692

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Publication

8364206 | J:14471

First Author:	Gibson S
Year:	1993
Journal:	Blood
Title:	Identification, cloning, and characterization of a novel human T-cell-specific tyrosine kinase located at the hematopoietin complex on chromosome 5q.
Volume:	82
Issue:	5
Pages:	1561-72

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Publication

29363583 | J:257637

First Author:	Chang CJ
Year:	2018
Journal:	J Neurosci
Title:	Ephexin1 Is Required for Eph-Mediated Limb Trajectory of Spinal Motor Axons.
Volume:	38
Issue:	8
Pages:	2043-2056

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32531343 | J:292709

First Author:	Mitchell R
Year:	2020
Journal:	Neurobiol Dis
Title:	ErbB1-dependent signalling and vesicular trafficking in primary afferent nociceptors associated with hypersensitivity in neuropathic pain.
Volume:	142

Pages:	104961

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Publication

25472762 | J:316598

First Author:	Wellberg EA
Year:	2014
Journal:	Breast Cancer Res
Title:	Modulation of tumor fatty acids, through overexpression or loss of thyroid hormone responsive protein spot 14 is associated with altered growth and metastasis.
Volume:	16
Issue:	6
Pages:	481

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