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Search results 4501 to 4600 out of 8321 for Src

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Type Details Score
Protein
Q8C1B4
Organism: Mus musculus/domesticus
Length: 359  
Fragment?: true
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Protein
Q3TH50
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
W0BZ77
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: false
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Protein
I6L9E4
Organism: Mus musculus/domesticus
Length: 722  
Fragment?: false
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Protein
A0A3Q4EGG3
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: false
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Protein
A0A571BDL9
Organism: Mus musculus/domesticus
Length: 367  
Fragment?: true
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Protein
A0A3Q4EBW9
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
D6REI4
Organism: Mus musculus/domesticus
Length: 292  
Fragment?: false
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Protein
A0A1D5RLL0
Organism: Mus musculus/domesticus
Length: 167  
Fragment?: true
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Protein
E9QJU1
Organism: Mus musculus/domesticus
Length: 296  
Fragment?: false
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Protein
B2FDI2
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: true
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Protein
O54737
Organism: Mus musculus/domesticus
Length: 516  
Fragment?: true
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Protein
Q80TA2
Organism: Mus musculus/domesticus
Length: 381  
Fragment?: true
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Protein
Q9CT18
Organism: Mus musculus/domesticus
Length: 269  
Fragment?: true
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Protein
D3YWR2
Organism: Mus musculus/domesticus
Length: 454  
Fragment?: false
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Protein
Q3TSS8
Organism: Mus musculus/domesticus
Length: 173  
Fragment?: true
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Protein
F6WJR3
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: true
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Protein
Q05C78
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: true
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Protein
Q8BG70
Organism: Mus musculus/domesticus
Length: 183  
Fragment?: false
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Protein
Q3TQV3
Organism: Mus musculus/domesticus
Length: 82  
Fragment?: false
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Publication
1377638 | -
First Author: Russell RB
Year: 1992
Journal: FEBS Lett
Title: Conservation analysis and structure prediction of the SH2 family of phosphotyrosine binding domains.
Volume: 304
Issue: 1
Pages: 15-20
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Publication
7883800 | -
 
First Author: Marengere LE
Year: 1994
Journal: J Cell Sci Suppl
Title: Structure and function of SH2 domains.
Volume: 18
Pages: 97-104
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Publication
3025655 | -
First Author: Sadowski I
Year: 1986
Journal: Mol Cell Biol
Title: A noncatalytic domain conserved among cytoplasmic protein-tyrosine kinases modifies the kinase function and transforming activity of Fujinami sarcoma virus P130gag-fps.
Volume: 6
Issue: 12
Pages: 4396-408
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Publication
11911873 | -
First Author: Pawson T
Year: 2002
Journal: FEBS Lett
Title: Interaction domains: from simple binding events to complex cellular behavior.
Volume: 513
Issue: 1
Pages: 2-10
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Publication
12952983 | -
First Author: Sathyamurthy A
Year: 2003
Journal: J Biol Chem
Title: Crystal structure of the malignant brain tumor (MBT) repeats in Sex Comb on Midleg-like 2 (SCML2).
Volume: 278
Issue: 47
Pages: 46968-73
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Publication
12167088 | -
First Author: Wiltshire C
Year: 2002
Journal: Biochem J
Title: A new c-Jun N-terminal kinase (JNK)-interacting protein, Sab (SH3BP5), associates with mitochondria.
Volume: 367
Issue: Pt 3
Pages: 577-85
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Publication
17885682 | -
First Author: Zhang J
Year: 2007
Journal: J Clin Invest
Title: AFAP-110 is overexpressed in prostate cancer and contributes to tumorigenic growth by regulating focal contacts.
Volume: 117
Issue: 10
Pages: 2962-73
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Publication
11607843 | -
First Author: Baisden JM
Year: 2001
Journal: Oncogene
Title: The actin filament-associated protein AFAP-110 is an adaptor protein that modulates changes in actin filament integrity.
Volume: 20
Issue: 44
Pages: 6435-47
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Publication
17520695 | -
First Author: Dorfleutner A
Year: 2007
Journal: J Cell Physiol
Title: AFAP-110 is required for actin stress fiber formation and cell adhesion in MDA-MB-231 breast cancer cells.
Volume: 213
Issue: 3
Pages: 740-9
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Publication
21984596 | -
First Author: Xiao H
Year: 2012
Journal: Cell Mol Life Sci
Title: The actin-binding domain of actin filament-associated protein (AFAP) is involved in the regulation of cytoskeletal structure.
Volume: 69
Issue: 7
Pages: 1137-51
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Publication
18180288 | -
First Author: Dixon RD
Year: 2008
Journal: J Biol Chem
Title: Palladin is an actin cross-linking protein that uses immunoglobulin-like domains to bind filamentous actin.
Volume: 283
Issue: 10
Pages: 6222-31
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Publication
23806659 | -
First Author: Beck MR
Year: 2013
Journal: J Mol Biol
Title: Structure and function of palladin's actin binding domain.
Volume: 425
Issue: 18
Pages: 3325-37
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Publication
20471940 | -
First Author: Chin YR
Year: 2010
Journal: Mol Cell
Title: The actin-bundling protein palladin is an Akt1-specific substrate that regulates breast cancer cell migration.
Volume: 38
Issue: 3
Pages: 333-44
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Publication
11598191 | J:114007
First Author: Mykkänen OM
Year: 2001
Journal: Mol Biol Cell
Title: Characterization of human palladin, a microfilament-associated protein.
Volume: 12
Issue: 10
Pages: 3060-73
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Publication
16367745 | -
First Author: Boukhelifa M
Year: 2006
Journal: FEBS J
Title: The proline-rich protein palladin is a binding partner for profilin.
Volume: 273
Issue: 1
Pages: 26-33
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Publication
25875253 | -
First Author: Nguyen NU
Year: 2015
Journal: PLoS One
Title: Dual roles of palladin protein in in vitro myogenesis: inhibition of early induction but promotion of myotube maturation.
Volume: 10
Issue: 4
Pages: e0124762
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Publication
25194811 | J:220095
First Author: Nguyen NU
Year: 2014
Journal: Biochem Biophys Res Commun
Title: Actin-associated protein palladin is required for migration behavior and differentiation potential of C2C12 myoblast cells.
Volume: 452
Issue: 3
Pages: 728-33
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Publication
20877641 | J:165108
First Author: Jin L
Year: 2010
Journal: PLoS One
Title: The actin associated protein palladin is important for the early smooth muscle cell differentiation.
Volume: 5
Issue: 9
Pages: e12823
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Publication
19015263 | J:146948
First Author: Jin L
Year: 2009
Journal: J Biol Chem
Title: The actin-associated protein Palladin is required for development of normal contractile properties of smooth muscle cells derived from embryoid bodies.
Volume: 284
Issue: 4
Pages: 2121-30
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Publication
9626554 | -
First Author: Bole-Feysot C
Year: 1998
Journal: Endocr Rev
Title: Prolactin (PRL) and its receptor: actions, signal transduction pathways and phenotypes observed in PRL receptor knockout mice.
Volume: 19
Issue: 3
Pages: 225-68
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Publication
12580759 | -
First Author: Trott JF
Year: 2003
Journal: J Mol Endocrinol
Title: Alternative splicing to exon 11 of human prolactin receptor gene results in multiple isoforms including a secreted prolactin-binding protein.
Volume: 30
Issue: 1
Pages: 31-47
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Publication
18779591 | -
First Author: Bogorad RL
Year: 2008
Journal: Proc Natl Acad Sci U S A
Title: Identification of a gain-of-function mutation of the prolactin receptor in women with benign breast tumors.
Volume: 105
Issue: 38
Pages: 14533-8
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Publication
24195502 | -
First Author: Newey PJ
Year: 2013
Journal: N Engl J Med
Title: Mutant prolactin receptor and familial hyperprolactinemia.
Volume: 369
Issue: 21
Pages: 2012-2020
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Publication
20032052 | -
First Author: Pujianto DA
Year: 2010
Journal: Endocrinology
Title: Prolactin exerts a prosurvival effect on human spermatozoa via mechanisms that involve the stimulation of Akt phosphorylation and suppression of caspase activation and capacitation.
Volume: 151
Issue: 3
Pages: 1269-79
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Publication
10585417 | J:58894
First Author: Kline JB
Year: 1999
Journal: J Biol Chem
Title: Functional characterization of the intermediate isoform of the human prolactin receptor.
Volume: 274
Issue: 50
Pages: 35461-8
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Publication
26526176 | -
 
First Author: Kan QE
Year: 2016
Journal: Int J Biol Macromol
Title: Different intracellular signalling pathways triggered by an anti-prolactin receptor (PRLR) antibody: Implication for a signal-specific PRLR agonist.
Volume: 82
Pages: 892-7
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Publication
8134129 | -
First Author: Chan TA
Year: 1994
Journal: Oncogene
Title: Identification of a gene encoding a novel protein-tyrosine kinase containing SH2 domains and ankyrin-like repeats.
Volume: 9
Issue: 4
Pages: 1253-9
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Publication
17881540 | -
First Author: Hellerbrand C
Year: 2008
Journal: Gut
Title: The novel gene MIA2 acts as a tumour suppressor in hepatocellular carcinoma.
Volume: 57
Issue: 2
Pages: 243-51
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Publication
15780062 | -
First Author: Hellerbrand C
Year: 2005
Journal: Liver Int
Title: In situ expression patterns of melanoma inhibitory activity 2 in healthy and diseased livers.
Volume: 25
Issue: 2
Pages: 357-66
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Publication
12573241 | -
First Author: Nore BF
Year: 2003
Journal: Biochim Biophys Acta
Title: Identification of phosphorylation sites within the SH3 domains of Tec family tyrosine kinases.
Volume: 1645
Issue: 2
Pages: 123-32
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Publication
15803148 | -
First Author: Schwartzberg PL
Year: 2005
Journal: Nat Rev Immunol
Title: TEC-family kinases: regulators of T-helper-cell differentiation.
Volume: 5
Issue: 4
Pages: 284-95
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Publication
15771581 | -
 
First Author: Berg LJ
Year: 2005
Journal: Annu Rev Immunol
Title: Tec family kinases in T lymphocyte development and function.
Volume: 23
Pages: 549-600
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Publication
11607842 | -
First Author: Weed SA
Year: 2001
Journal: Oncogene
Title: Cortactin: coupling membrane dynamics to cortical actin assembly.
Volume: 20
Issue: 44
Pages: 6418-34
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Publication
19437513 | -
First Author: Ren G
Year: 2009
Journal: Cell Motil Cytoskeleton
Title: Cortactin: Coordinating adhesion and the actin cytoskeleton at cellular protrusions.
Volume: 66
Issue: 10
Pages: 865-73
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Publication
18615630 | -
First Author: Ammer AG
Year: 2008
Journal: Cell Motil Cytoskeleton
Title: Cortactin branches out: roles in regulating protrusive actin dynamics.
Volume: 65
Issue: 9
Pages: 687-707
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Publication
21258212 | -
First Author: Kirkbride KC
Year: 2011
Journal: Cell Adh Migr
Title: Cortactin: a multifunctional regulator of cellular invasiveness.
Volume: 5
Issue: 2
Pages: 187-98
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Publication
16474900 | -
First Author: Chen L
Year: 2006
Journal: Acta Biochim Biophys Sin (Shanghai)
Title: Roles of cortactin, an actin polymerization mediator, in cell endocytosis.
Volume: 38
Issue: 2
Pages: 95-103
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Publication
16990456 | -
 
First Author: Cosen-Binker LI
Year: 2006
Journal: Physiology (Bethesda)
Title: Cortactin: the gray eminence of the cytoskeleton.
Volume: 21
Pages: 352-61
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Publication
15670811 | -
First Author: Lua BL
Year: 2005
Journal: FEBS Lett
Title: Cortactin phosphorylation as a switch for actin cytoskeletal network and cell dynamics control.
Volume: 579
Issue: 3
Pages: 577-85
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Publication
16434035 | -
First Author: Webb BA
Year: 2006
Journal: Exp Cell Res
Title: Cortactin regulates podosome formation: roles of the protein interaction domains.
Volume: 312
Issue: 6
Pages: 760-9
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Publication
22658750 | -
First Author: He X
Year: 2012
Journal: Structure
Title: The T4 phage SF1B helicase Dda is structurally optimized to perform DNA strand separation.
Volume: 20
Issue: 7
Pages: 1189-200
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Publication
11331761 | -
First Author: Lougheed JC
Year: 2001
Journal: Proc Natl Acad Sci U S A
Title: Structure of melanoma inhibitory activity protein, a member of a recently identified family of secreted proteins.
Volume: 98
Issue: 10
Pages: 5515-20
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Publication
8550608 | -
First Author: Bosserhoff AK
Year: 1996
Journal: J Biol Chem
Title: Structure and promoter analysis of the gene encoding the human melanoma-inhibiting protein MIA.
Volume: 271
Issue: 1
Pages: 490-5
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Protein Domain
IPR043369 | MIA
Type: Family
Description: Melanoma-derived growth regulatory protein or Melanoma inhibitory activity (MIA) is a 12kDa protein that is secreted from both chondrocytes and malignant melanoma cells. It has effects on cell growth and adhesion and it may play a role in melanoma metastasis and cartilage development. MIA elicits growth inhibition on melanoma cells in vitro. It is possible that secretion of MIA in vivo leads to decreased adhesiveness of melanocytic cells and thereby promotes melanoma progression and invasion []. Crystal structure revealed an Src homology 3 (SH)-like domain with N- and C-terminal extensions of about 20 aa each. It is thefirst structure of a secreted protein that contains an SH3 subdomain. MIA SH3 subdomain shares sequence similarity with canonical SH3 domains, suggesting that they are evolutionary related. It has a protein interaction site and, unlike conventional SH3 domains, MIA does not recognise polyproline helices [].
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Protein Domain
IPR004092 | Mbt
Type: Repeat
Description: The function of the malignant brain tumor (MBT) repeat is unknown, but is found in a number of nuclear proteins involved in transcriptional repression. The repeat contains a completelyconserved glutamate at its amino terminus that may be important for function.The crystal structure of the two MBT repeats of human SCM-like 2 protein has been reported. Each repeat consists of an extended "arm"and a globular core. The arm of the first repeat packs against the core of the second repeat and vice versa. The structure of the core-interacting part of each arm consists of an N-terminal α-helix and a turn of 310helix connected by a short β-strand. The core consists of an Src homology 3-like five-stranded β-barrel followed by a C-terminal α-helix and another short β-strand. Each arm interacts with its partner core in a similar way, with the orientation of the N-terminal helix relative to the barrel varying slightly. There are also extensive interactions between the two barrels [].
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Protein Domain
IPR041214 | SH3_14
Type: Domain
Description: This is a Src homology-3 (SH3) like β-barrel domain which can be found in Dda enzyme. Dda is a phage T4 SF1B helicase. The Dda SH3 domain contains two insertions (compared to RecD2), a second β-ribbon that is referred to as the hook and a β-ribbon/two-helix substructure that is referred to as the tower. The tower region within the domain is rigidly connected to domain 2A in Dda and appears to be specifically designed for the task of supporting the extended pin. Hence, it is suggested that 2A and this SH3 domain move as one unit during the ATP-driven translocation of ssDNA while maintaining contact with the pin. In this scenario, the pin-tower interaction can be considered as an additional transmission site that serves to more efficiently couple the energy from ATP binding and hydrolysis to the unwinding of dsDNA [].
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Protein Domain
IPR038157 | FeoA_core_dom
Type: Homologous_superfamily
Description: This entry represents the core domain of the ferrous iron (Fe2+) transport protein FeoA found in bacteria. This domain also occurs at the C terminus in the diphtheria toxin repressor (DtxR). DtxR is a iron-binding repressor that contains two domains separated by a short linker. The C-terminal domain adopts a fold similar to eukaryotic Src homology 3 domains, but its functional role is unknown [].The transporter Feo is composed of three proteins: FeoA a small, soluble SH3-domain protein probably located in the cytosol; FeoB, a large protein with a cytosolic N-terminal G-protein domain and a C-terminal integral inner-membrane domain containing two 'Gate' motifs which likely functions as the Fe2+ permease; and FeoC, a small protein apparently functioning as an [Fe-S]-dependent transcriptional repressor [, ]. Feo allows the bacterial cell to acquire iron from its environment.
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Protein Domain
IPR035061 | Shark-like_SH2_N
Type: Domain
Description: This entry represents the SH2 domain found in Drosophila shark protein and hydra protein HTK16. Shark and HTK16 are non-receptor protein-tyrosine kinases contain two SH2 domains, five ankyrin (ANK)-like repeats, and a potential tyrosine phosphorylation site in the carboxyl-terminal tail which resembles the phosphorylation site in members of the src family. Like, mammalian non-receptor protein-tyrosine kinases, ZAP-70 and syk proteins, they do not have SH3 domains. However, the presence of ANK makes these unique among protein-tyrosine kinases. Both tyrosine kinases and ANK repeats have been shown to transduce developmental signals, and SH2 domains are known to participate intimately in tyrosine kinase signaling [].Drosophila Shark transduces intracellularly the Crumbs, a protein necessary for proper organization of ectodermal epithelia, intercellular signal []. It is essential for Draper-mediated signalling [].
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Protein Domain
IPR029907 | AFAP-110
Type: Family
Description: Actin filament-associated protein 1 (AFAP1, also known as AFAP-110) belongs to the actin-filament associated protein (AFAP) family of adaptor proteins (including AFAP1, AFAP1L1, and AFAP1L2/XB130). AFAP1 functions as an adaptor protein, linking Src kinases and/or other signalling proteins to actin filaments. It can cross-link actin filaments into both network and bundle structures []. AFAP1 contains several protein binding modules, including two pleckstrin homology domains (PH domains), a leucine zipper motif and a target sequence for serine/threonine phosphorylation []. It interacts with actin filaments directly via an actin-binding domain (ABD) located in its C terminus, and through this interaction is involved in the regulation of the cytoskeletal structure []. Its overexpression has been linked to cancers [, ].
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Protein Domain
IPR042139 | PX_ARHGAP32
Type: Domain
Description: This entry represents the PX domain found in Rho GTPase-activating protein 32 (ARHGAP32, also known as RICS). RICS is a Rho GTPase-activating protein for cdc42 and Rac1. It is implicated in the regulation of postsynaptic signaling and neurite outgrowth. An N-terminal splicing variant of RICS containing additional PX and Src Homology 3 (SH3) domains, also called PX-RICS, is the main isoform expressed during neural development. PX-RICS is involved in neural functions including axon and dendrite extension, postnatal remodeling, and fine-tuning of neural circuits during early brain development []. The PX domain is involved in targeting of proteins to PI-enriched membranes, and may also be involved in protein-protein interaction []. The PX domain of PX-RICS specifically binds phosphatidylinositol 3-phosphate (PI3P), PI4P, and PI5P [].
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Protein Domain
IPR007940 | SH3BP5
Type: Family
Description: This family consists of several eukaryotic SH3 domain-binding protein 5 or c-Jun N-terminal kinase (JNK)-interacting proteins (SH3BP5 or Sab). Sab binds to and serves as a substrate for JNK in vitro, and has been found to interact with the Src homology 3 (SH3) domain of Bruton's tyrosine kinase (Btk). Inspection of the sequence of Sab reveals the presence of two putative mitogen-activated protein kinase interaction motifs (KIMs) similar to that found in the JNK docking domain of the c-Jun transcription factor, and four potential serine-proline JNK phosphorylation sites in the C-terminal half of the molecule [].This entry also includes REI-1 and REI-2 from C. elegans. REI-1 is a guanine nucleotide exchange factors (GEFs) for RAB-11. It functions in early embryos [].
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Protein Domain
IPR027653 | Formin_Diaph1
Type: Family
Description: Protein diaphanous homologue 1 (Dia1) belongs to the formin homology family, Diaphanous subfamily (also known as the Diaphanous-related formins, Drfs). In addition to the FH1 and FH2 domains, Drfs contain an N-terminal GTPase-binding domain (mDiaN) and a C-terminal Diaphanous-autoregulatory domain (DAD).Dia1 contains the N-terminal RhoA-binding domain (RBD) followed by a four armadillo-repeats containing Diaphanous inhibitory domain (DID) that binds the C-terminal Diaphanous autoregulatory domain (DAD) [, ]. Dia1 nucleates actin filaments and regulate actin polymerisation and depolymerisation. The activities of Dia1 is regulated by an autoinhibitory interaction between DAD domain and the GBD/FH3 domain. This autoinhibition is released upon competitive binding of an activated GTPase. The release of DAD allows the FH2 domain to then nucleate and elongate nonbranched actin filaments []. Dia1 couples Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics [].
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Protein Domain
IPR035555 | MIA2_SH3
Type: Domain
Description: MIA2 is expressed specifically in hepatocytes and its expression is controlled by hepatocyte nuclear factor 1 binding sites in the MIA2 promoter [, ]. It inhibits the growth and invasion of hepatocellular carcinomas (HCC) and may act as a tumour suppressor []. A mutation in MIA2 in mice resulted in reduced cholesterol and triglycerides. Since MIA2 localizes to ER exit sites, it may function as an ER-to-Golgi trafficking protein that regulates lipid metabolism []. MIA2 contains an N-terminal SH3-like domain, similar to MIA.MIA (melanoma inhibitory activity) family members include MIA, MIAL, MIA2, and MIA3 (also called TANGO). MIA was found to be strongly expressed and secreted by malignant melanomas. It contains a domain that adopts a Src Homology 3 (SH3) domain-like fold; however, it contains an additional antiparallel beta sheet and two disulfide bonds compared to classical SH3 domains. Unlike classical SH3 domains, MIA does not bind proline-rich ligands [, ].
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Protein Domain
IPR035559 | Nck2_SH3_1
Type: Domain
Description: This entry represent the first SH3 domain of Nck2. It binds the PxxDY sequence in the CD3e cytoplasmic tail; this binding inhibits phosphorylation by Src kinases, resulting in the downregulation of TCR surface expression []. Nck2 (also known as Grb4) is a member of the Nck family. It plays a crucial role in connecting signaling pathways of tyrosine kinase receptors and important effectors in actin dynamics and cytoskeletal remodeling []. It binds neuronal signaling proteins such as ephrinB []. Cytoplasmic proteins Nck are non-enzymatic adaptor proteins composed of three SH3 (Src homology 3) domains and a C-terminal SH2 domain []. They regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates []. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics []. They associate with tyrosine-phosphorylated growth factor receptors or their cellular substrates [, ]. There are two vertebrate Nck proteins, Nck1 and Nck2.
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Protein Domain
IPR035572 | Tec_SH3
Type: Domain
Description: This entry represents the SH3 domain of Tec [, ]. Tec is a cytoplasmic (or nonreceptor) tyrosine kinase containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain []. It also contains an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation, and the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions []. It is more widely-expressed than other Tec subfamily kinases. Tec is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils [, ]. Tec is a key component of T-cell receptor (TCR) signaling, and is important in TCR-stimulated proliferation and phospholipase C-gamma1 activation [].
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Protein Domain
IPR035716 | Cortactin_SH3
Type: Domain
Description: Cortactin was originally identified as a substrate of Src kinase []. It is an actin regulatory protein that binds to the Arp2/3 complex and stabilizes branched actin filaments [, ]. It is involved in cellular processes that affect cell motility, adhesion, migration, endocytosis, and invasion [, , , ]. Cortactin contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain []. The N-terminal region interacts with the Arp2/3 complex and F-actin, and is crucial in regulating branched actin assembly []. Cortactin also serves as a scaffold and provides a bridge to the actin cytoskeleton for membrane trafficking and signaling proteins that bind to its SH3 domain. Binding partners for the SH3 domain of cortactin include dynamin2, N-WASp, MIM, FGD1, among others []. This entry represents the SH3 domain of cortactin.
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Protein Domain
IPR035746 | NEDD9_SH3
Type: Domain
Description: Enhancer of filamentation 1 (also known as NEDD9 or Cas-L) is a member of the CAS family. It is a scaffolding protein that assembles signaling complexes regulating multiple cellular processes, such as cell adhesion, migration, invasion, and metastasis. It is commonly dysregulated during cancer progression. It interacts with Aurora-A kinase to control ciliary resorption, and with Src and other partners to influence proliferative signaling pathways often activated in autosomal dominant polycystic kidney disease [].CAS (Crk-associated substrate) family members are adaptor proteins that contain a highly conserved N-terminal SH3 domain, an adjacent unstructured domain (substrate domain) containing multiple tyrosine phosphorylation sites that enable binding by SH2-domain containing proteins, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Most of these domains mediate protein-protein interactions. Through these interactions, they assemble larger signaling complexes that are essential for cell proliferation, survival, migration, and other processes []. The CAS family consists of four members: BCAR1, HEF1, EFS, and CASS4 [].
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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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Protein Domain
IPR033017 | Palladin_C
Type: Domain
Description: Palladin is a cytoskeletal actin scaffold protein that regulates actin dynamics. The immunoglobulin-like domain of palladin is directly responsible for both actin binding and bundling [, ]. Palladin also interacts with different actin binding proteins and signalling intermediaries required for regulation of cytoskeleton organisation, including profilin [], VASP [], Eps8 [], ezrin [], Lasp-1 [], and Src []. Palladin plays an important role in smooth and skeletal muscle differentiation [, , ], contraction []and cell migration [, , ].Palladin is expressed as several alternatively spliced isoforms, having various combinations of Ig-like domains, in a cell-type-specific manner. It has been suggested that palladin's different Ig-like domains may be specialized for distinct functions []. This entry represents the C-terminal immunoglobulin-like domain (Ig5).
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Protein Domain
IPR033230 | PRLR
Type: Family
Description: PRLR is a receptor for the anterior pituitary hormone prolactin (PRL) [, ]. PRL participates in a variety of physiological processes in vertebrates, including reproduction, osmo-regulation, growth and development, metabolism, immuno-regulation, energy balance, and behavior []. Upon ligand binding of PRL to PRLR, the Janus-activated kinase 2 (JAK2) is activated, which in turn initiates intracellular signalling cascades, including signal transducers and activators of transcription (STAT) family members STAT-1/3/5, and extracellular regulated kinases (ERK1/2) and AKT []. PRLR also acts as a prosurvival factor for spermatozoa by inhibiting sperm capacitation through suppression of SRC kinase activation and stimulation of AKT [].Mutations in the PRLR gene cause multiple fibroadenomas of the breast (MFAB) []and hyperprolactinemia (HPRL) [].
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Publication
8605874 | J:38792
First Author: Chan DC
Year: 1996
Journal: EMBO J
Title: Formin binding proteins bear WWP/WW domains that bind proline-rich peptides and functionally resemble SH3 domains.
Volume: 15
Issue: 5
Pages: 1045-54
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Protein
B2RWI0
Organism: Mus musculus/domesticus
Length: 81  
Fragment?: false
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Protein
B1AUF8
Organism: Mus musculus/domesticus
Length: 82  
Fragment?: true
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Protein
F7BZA7
Organism: Mus musculus/domesticus
Length: 124  
Fragment?: true
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Publication
18555270 | -
First Author: Takeuchi K
Year: 2008
Journal: J Mol Biol
Title: Structural and functional evidence that Nck interaction with CD3epsilon regulates T-cell receptor activity.
Volume: 380
Issue: 4
Pages: 704-16
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Protein Domain
IPR000980 | SH2
Type: Domain
Description: The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps []. Similar sequences were later found in many other intracellular signal-transducing proteins []. SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific, SH2 domains recognise between 3-6 residues C-terminal to the phosphorylated tyrosine in a fashion that differs from one SH2 domain to another, and strictly phosphorylation-dependent manner [, , , ]. They are found in a wide variety of protein contexts e.g., in association with catalytic domains of phospholipase Cy (PLCy) and the non-receptor protein tyrosine kinases; within structural proteins such as fodrin and tensin; and in a group of small adaptor molecules, i.e Crk and Nck. The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates. The structure of the SH2 domain belongs to the α+β class, its overall shape forming a compact flattened hemisphere. The core structural elements comprise a central hydrophobic anti-parallel β-sheet, flanked by 2 short α-helices. The loop between strands 2 and 3 provides many of the binding interactions with the phosphate group of its phosphopeptide ligand, and is hence designated the phosphate binding loop, the phosphorylated ligand binds perpendicular to the β-sheet and typically interacts with the phosphate binding loop and a hydrophobic binding pocket that interacts with a pY+3 side chain. The N- and C-termini of the domain are close together in space and on the opposite face from the phosphopeptide binding surface and it has been speculated that this has facilitated their integration into surface-exposed regions of host proteins [].
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Protein Domain
IPR036860 | SH2_dom_sf
Type: Homologous_superfamily
Description: The Src homology 2 (SH2) domain is a protein domain of about 100 amino-acid residues first identified as a conserved sequence region between the oncoproteins Src and Fps []. Similar sequences were later found in many other intracellular signal-transducing proteins []. SH2 domains function as regulatory modules of intracellular signalling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific, SH2 domains recognise between 3-6 residues C-terminal to the phosphorylated tyrosine in a fashion that differs from one SH2 domain to another, and strictly phosphorylation-dependent manner [, , , ]. They are found in a wide variety of protein contexts e.g., in association with catalytic domains of phospholipase Cy (PLCy) and the non-receptor protein tyrosine kinases; within structural proteins such as fodrin and tensin; and in a group of small adaptor molecules, i.e Crk and Nck. The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates. The structure of the SH2 domain belongs to the α+β class, its overall shape forming a compact flattened hemisphere. The core structural elements comprise a central hydrophobic anti-parallel β-sheet, flanked by 2 short α-helices. The loop between strands 2 and 3 provides many of the binding interactions with the phosphate group of its phosphopeptide ligand, and is hence designated the phosphate binding loop, the phosphorylated ligand binds perpendicular to the β-sheet and typically interacts with the phosphate binding loop and a hydrophobic binding pocket that interacts with a pY+3 side chain. The N- and C-termini of the domain are close together in space and on the opposite face from the phosphopeptide binding surface and it has been speculated that this has facilitated their integration into surface-exposed regions of host proteins [].
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Publication
27183589 | J:328371
First Author: Martín-Ávila A
Year: 2016
Journal: J Immunol
Title: Protein Tyrosine Kinase Fyn Regulates TLR4-Elicited Responses on Mast Cells Controlling the Function of a PP2A-PKCα/β Signaling Node Leading to TNF Secretion.
Volume: 196
Issue: 12
Pages: 5075-88
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Publication
10679268 | J:64951
First Author: Masuhara M
Year: 2000
Journal: Biochem Biophys Res Commun
Title: Molecular cloning of murine STAP-1, the stem-cell-specific adaptor protein containing PH and SH2 domains.
Volume: 268
Issue: 3
Pages: 697-703
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Protein
Q60898
Organism: Mus musculus/domesticus
Length: 281  
Fragment?: false
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Protein
A0A0R4J247
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
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Protein
Q4FJX0
Organism: Mus musculus/domesticus
Length: 281  
Fragment?: false
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Publication
22508726 | J:183920
First Author: Chen J
Year: 2012
Journal: Genes Dev
Title: The ubiquitin ligase mLin41 temporally promotes neural progenitor cell maintenance through FGF signaling.
Volume: 26
Issue: 8
Pages: 803-15
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Publication
35013307 | J:317822
First Author: Chern T
Year: 2022
Journal: Nat Commun
Title: Mutations in Hcfc1 and Ronin result in an inborn error of cobalamin metabolism and ribosomopathy.
Volume: 13
Issue: 1
Pages: 134
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Publication
- | J:104190
     
First Author: The Australian Phenomics Facility at The Australian National University
Year: 2006
Journal: MGI Direct Data Submission
Title: Heritable mouse mutants from the ENU mutagenesis program at the Australian Phenomics Facility at The Australian National University
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Publication
7568168 | J:29404
First Author: Wong WT
Year: 1995
Journal: Proc Natl Acad Sci U S A
Title: A protein-binding domain, EH, identified in the receptor tyrosine kinase substrate Eps15 and conserved in evolution.
Volume: 92
Issue: 21
Pages: 9530-4
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Publication
1379745 | J:28608
First Author: Cicchetti P
Year: 1992
Journal: Science
Title: Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho.
Volume: 257
Issue: 5071
Pages: 803-6
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Publication
10339589 | J:55122
First Author: Yamadori T
Year: 1999
Journal: Proc Natl Acad Sci U S A
Title: Bruton's tyrosine kinase activity is negatively regulated by Sab, the Btk-SH3 domain-binding protein.
Volume: 96
Issue: 11
Pages: 6341-6
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Publication
19575010 | J:233576
First Author: Swayne LA
Year: 2009
Journal: EMBO Rep
Title: The NALCN ion channel is activated by M3 muscarinic receptors in a pancreatic beta-cell line.
Volume: 10
Issue: 8
Pages: 873-80
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Publication
8476425 | J:20701
First Author: Yamada N
Year: 1993
Journal: Biochem Biophys Res Commun
Title: Structure and expression of novel protein-tyrosine kinases, Emb and Emt, in hematopoietic cells.
Volume: 192
Issue: 1
Pages: 231-40
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