What does SH3 stand for?

What does SH3 stand for?


Acronym Definition
SH3 Src (Sarcoma) Homology 3 Domain
SH3 Silent Hill 3 (game)
SH3 Ship’s Serviceman Third Class (Naval Rating)

What do SH2 domains do?

Src homology 2 (SH2) domains are protein modules (of approximately 100 amino acids) found in many proteins involved in tyrosine kinase signalling cascades. Their function is to bind tyrosine-phosphorylated sequences in specific protein targets.

What is SH2 and SH3 domains?

SH2 and SH3 domains are small protein modules that mediate protein-protein interactions in signal transduction pathways that are activated by protein tyrosine kinases. SH3 domains bind to target proteins through sequences containing proline and hydrophobic amino acids.

What is SH3 domain binding?

The SH3 domain is a distinct motif that binds target proteins, including proteins associated with the actin cytoskeleton, through sequences containing proline and hydrophobic amino acids.

What is the role of the SH2 SH3 and PTB domains?

The functions of SH2 and PTB domains include targeting of their host proteins to different cellular compartments, assembly of key components of signaling pathways in response to extracellular signals, and the control of autoinhibition, activation and dimerization of their host proteins.

What proteins have an SH2 domain?

A recent tally finds 121 SH2 in 111 proteins in the human genome [11]. Proteins containing SH2 domains include those that function as kinases, adaptors, phosphatases, ubiquitin ligases, transcription factors, guanine nucleotide exchange factors and phospholipid-based secondary signaling molecules [5, 12, 30].

What role do the Sh2 and SH3 domains play in the function of GRB2?

What role do Sh2 and Sh3 domains play in the function of GRB2? GRB2 is an adaptor protein. It contains one Sh2 domain, and two Sh3 domains on the N terminal and C terminal ends. Sh3 directs the binding of proline rich proteins of other compounds, and Sh2 directs the binding of tyrosine phosphorylated sequences.

What is GRB2 and SOS?

Grb2 protein, which is the downstream effector of the EGF receptor, acts as an adaptor protein between the EGF receptor and the Ras guanine-nucleotide exchange factor, son of sevenless (Sos) protein. Sos protein regulates the action of Ras protein by promoting the exchange of GDP for GTP.

What is WW in biology?

The WW domain, (also known as the rsp5-domain or WWP repeating motif) is a modular protein domain that mediates specific interactions with protein ligands. This domain is found in a number of unrelated signaling and structural proteins and may be repeated up to four times in some proteins.

What does PTB bind to?

Phosphotyrosine binding (PTB) domains have been identified in a large number of proteins. In proteins like Shc and IRS-1, the PTB domain binds in a phosphotyrosine-dependent fashion to peptides that form a b turn. In these proteins, PTB domains play an important role in signal transduction by growth factor receptors.

What is the role of Adaptor proteins?

Adaptor proteins contain a variety of protein-binding modules that link protein-binding partners together and facilitate the creation of larger signaling complexes. By linking specific proteins together, cellular signals can be propagated that elicit an appropriate response from the cell to the environment.

What type of protein is SOS?

Essential for normal eye development in Drosophila, SOS has two human homologues, SOS1 and SOS2. The SOS1 gene encodes the Son of Sevenless 1 protein, a Ras and Rac guanine nucleotide exchange factor. This protein is composed of several important domains.

Where are SH3 domains found in a protein?

Protein with at least one Src homology 3 (SH3) domain It is a small protein domain of about 50 amino-acid residues first identified as a conserved sequence in the non-catalytic part of several cytoplasmic protein tyrosine kinases (e.g. Src). Since then, it has been found in a great variety of other intracellular or membrane-associated proteins.

What is the role of the SH3 module?

Since then, it has been found in a great variety of other intracellular or membrane-associated proteins. The SH3 module might mediate the assembly of specific protein complexes by binding to proline-rich peptides.

Are there any binding motifs in the SH3 domain?

Other SH3 binding motifs have emerged and are still emerging in the course of various molecular studies, highlighting the versatility of this domain.

How is SH3 domain related to tuba and N-WASP?

While Tuba and N-WASP regulate cell–cell junctions in epithelial cells [19], Intersectin and N-WASP mediate EphB dependent spinogenesis in developing neurons [20]. All studies to date suggest binding to SH3 domain-containing proteins positively regulates the WASP/N-WASP proteins in mammalian cells.