Protein Domain - Revision history

Mark: /* Statistics */

2015-09-11T17:51:01Z

‎Statistics

2015-09-11T17:50:37Z

‎C1: DAG binding

2015-07-01T17:45:59Z

‎C1: DAG binding

2015-07-01T17:41:17Z

‎TPR

2015-07-01T17:40:44Z

‎SH3

2015-07-01T17:40:18Z

‎SH2

2015-07-01T17:40:04Z

‎PH

2015-07-01T17:39:07Z

‎PEST: rapid degradation

2015-07-01T17:38:56Z

‎PEST

2015-07-01T17:38:36Z

‎PDZ

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+|
+|
+| ~50
 |-
 | ADF:Gelsolin

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 ===== [https://en.wikipedia.org/wiki/C1_domain C1]: DAG binding =====
-C1 domain (also known as phorbol esters/diacylglycerol binding domain) binds an important secondary messenger diacylglycerol (DAG), as well as the analogous phorbol esters. It is characterised by a rich cysteine and histidine content. The C1 domain is originally found in the N-terminal region of conservation in protein kinase C domains.
+C1 domain (also known as phorbol esters/diacylglycerol binding domain) binds an important secondary messenger diacylglycerol (DAG), as well as the analogous phorbol esters. It is characterised by a rich cysteine and histidine content. The C1 domain is originally found in the N-terminal region of conservation in protein kinase C domains. It is usually around 50 aa long.
 ===== [https://en.wikipedia.org/wiki/C2_domain C2]: membrane targeting =====

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 ===== [https://en.wikipedia.org/wiki/C1_domain C1]: DAG binding =====
 C1 domain (also known as phorbol esters/diacylglycerol binding domain) binds an important secondary messenger diacylglycerol (DAG), as well as the analogous phorbol esters. It is characterised by a rich cysteine and histidine content. The C1 domain is originally found in the N-terminal region of conservation in protein kinase C domains.
 ===== [https://en.wikipedia.org/wiki/EF_hand EF hand]: Ca<sup>2+</sup> binding =====

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 DNA-binding domain similar to P element transposase <cite>Roussigne03</cite>.
-===== [https://en.wikipedia.org/wiki/Tetratricopeptide TPR] =====
+===== [https://en.wikipedia.org/wiki/Tetratricopeptide TPR]: protein-protein interacting structural motif =====
 TPR is short for tetratricopeptide repeat (TPR). It is a structural motif mediates protein-protein interactions. It consists in a degenerate 34 amino acid sequence motif identified in a wide variety of proteins. It is often but not always found in tandem arrays.

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 The SH2 (Src Homology 2) domain is a structurally conserved protein domain of ~100 aa long. SH2 typically binds to pTyr (phosphorylated tyrosine) which usually locates in peptide linear motif of 3-6 aa long. About 120 SH2 domains within 115 proteins in human have been found.
-===== [http://en.wikipedia.org/wiki/SH3_domain SH3] =====
+===== [http://en.wikipedia.org/wiki/SH3_domain SH3]: proline-rich region binding =====
 The SRC Homology 3 Domain (or SH3 domain) is a small protein domain of about 60 aa long. SH3 typically via binding to proline-rich peptides in their respective binding partner. Approximately 300 SH3 domains are found in proteins in human genome.

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 The PTB domain is a structural domain of ~130 aa (Pfam model). It usually binds to phosphorylated tyrosine. However, PTB domain of SHC can bind to NPLH sequence found in the carboxyl terminus of murine PTPN12/PTP-PEST <cite>Charest94</cite>. PTB domain is found at least in 27 genes in human genome.
-===== [http://en.wikipedia.org/wiki/SH2_domain SH2] =====
+===== [http://en.wikipedia.org/wiki/SH2_domain SH2]: pTyr binding =====
 The SH2 (Src Homology 2) domain is a structurally conserved protein domain of ~100 aa long. SH2 typically binds to pTyr (phosphorylated tyrosine) which usually locates in peptide linear motif of 3-6 aa long. About 120 SH2 domains within 115 proteins in human have been found.

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 A PEST sequence is a peptide sequence that is rich in proline (P), glutamic acid (E), serine (S), and threonine (T). This sequence is associated with proteins that are rapidly degraded, possibly via the proteasome or cal pain. The computational tool [http://emboss.bioinformatics.nl/cgi-bin/emboss/epestfind ePESTfind] is used to predict PEST sequence.
-===== [[Protein_Domain_PH|PH]] =====
+===== [[Protein_Domain_PH|PH]]: phosphatidylinositol lipids binding =====
 ====== [[Protein_Domain_GRAM|GRAM]] ======

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 Proteins with these domains help hold together and organize signaling complexes at cellular membranes. In general PDZ domains bind to a short region of the C-terminus of other specific proteins. These short regions bind to the PDZ domain by beta sheet augmentation. This means that the beta sheet in the PDZ domain is extended by the addition of a further beta strand from the tail of the binding partner protein. About 260 PDZ domains within 180 proteins in human have been found.
-===== [http://en.wikipedia.org/wiki/PEST_sequence PEST]: rapid degradation =====
+===== [http://en.wikipedia.org/wiki/PEST_sequence PEST]: rapid degradation signal =====
 A PEST sequence is a peptide sequence that is rich in proline (P), glutamic acid (E), serine (S), and threonine (T). This sequence is associated with proteins that are rapidly degraded, possibly via the proteasome or cal pain. The computational tool [http://emboss.bioinformatics.nl/cgi-bin/emboss/epestfind ePESTfind] is used to predict PEST sequence.

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 The IQ  calmodulin-binding motif is an amino acid sequence motif containing the following sequence: [FILV]Qxxx[RK]Gxxx[RK]xx[FILVWY]. The term "IQ" refers to the first two amino acids of the motif: isoleucine (commonly) and glutamine (invariably). Calmodulin (CaM) is recognized as a major calcium (Ca2+) sensor and orchestrator of regulatory events through its interaction with a diverse group of cellular proteins.
-===== [http://en.wikipedia.org/wiki/PDZ_domain PDZ] =====
+===== [http://en.wikipedia.org/wiki/PDZ_domain PDZ]: binding to the C-terminal of specific proteins =====
 The PDZ domain is a common structural domain of 80-90 amino-acids found in the signaling proteins of all three kingdoms of life. PDZ is an acronym combining the first letters of three proteins — post synaptic density protein (PSD95), Drosophila disc large tumor suppressor (Dlg1), and zonula occludens-1 protein (zo-1) — which were first discovered to share the domain. It has previously been referred to as DHR (Dlg homologous region) or GLGF (glycine-leucine-glycine-phenylalanine) domains.