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Interacting selectively and non-covalently with a POZ (poxvirus and zinc finger) domain of a protein, a protein-protein interaction domain found in many transcription factors. Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules). Interacting selectively and non-covalently with a Pyrin (PAAD/DAPIN) domain, a protein-protein interaction domain that has the same fold as the Death domain. Interacting selectively and non-covalently with the Bcl-2 homology (BH) domain of a protein. Bcl-2-related proteins share homology in one to four conserved regions designated the Bcl-2 homology (BH) domains BH1, BH2, BH3 and BH4. These domains contribute at multiple levels to the function of these proteins in cell death and survival. Anti-apoptotic members of the Bcl-2 family have four BH domains (BH1-BH4). Pro-apoptotic members have fewer BH domains. Interacting selectively and non-covalently with a SH3 domain (Src homology 3) of a protein, small protein modules containing approximately 50 amino acid residues found in a great variety of intracellular or membrane-associated proteins. Interacting selectively and non-covalently with the calponin homology domain of a protein, a domain of 100 residues that occurs in signaling and cytoskeletal proteins. Interacting selectively and non-covalently with a chromo shadow domain, a protein domain that is distantly related, and found in association with, the chromo domain. Interacting selectively and non-covalently with a HECT, 'Homologous to the E6-AP Carboxyl Terminus', domain of a protein. Interacting selectively and non-covalently with a phosphotyrosine-binding (PTB) domain of a protein. Interacting selectively and non-covalently with the AF-2 domain of a protein, a highly conserved ligand-dependent transactivation domain which is essential for receptor-mediated transcriptional activation. Interacting selectively and non-covalently with an RS domain of a protein; RS domains are usually highly phosphorylated and characterized by the presence of arginine (R)/serine (S) dipeptides. The RS domain promotes protein-protein interactions and directs subcellular localization and, in certain situations, nucleocytoplasmic shuttling of individual SR proteins. They also play a role in splicing. Interacting selectively and non-covalently with the AF-1 domain of a protein, a ligand-independent transactivation domain which is required for the full transcriptional activity of the receptor. Interacting selectively and non-covalently with a SET domain of a protein. SET domains are named after three Drosophila proteins that contain this domain: Su(var), E(z) and trithorax. SET domains are associated with histone lysine methylation. Interacting selectively and non-covalently with a SAM (Sterile Alpha Motif) domain, which is a 70-amino acid protein sequence that participates in protein-protein, protein-lipid, and protein-RNA interactions and is conserved from lower to higher eukaryotes. Interacting selectively and non-covalently with a Rel Homology Domain (RHD) of a protein. The RHD is found in a family of eukaryotic transcription factors, which includes NF-kappaB, Dorsal, Relish and NFAT. Interacting selectively and non-covalently with a death domain of a protein. The death domain (DD) is a homotypic protein interaction module composed of a bundle of six alpha-helices. DD bind each other forming oligomers. Some DD-containing proteins are involved in the regulation of apoptosis and inflammation through their activation of caspases and NF-kappaB. Interacting selectively and non-covalently with a TRAF-type zinc finger domain of a protein. Interacting selectively and non-covalently with a RIP homotypic interaction motif (RHIM) of a protein. The RHIM is a 16-amino-acid motif found in some members, including RIP3, of a family of related kinases. Interacting selectively and non-covalently with a NACHT (NAIP, CIITA, HET-E and TP1) domain. The NACHT domain consists of seven distinct conserved motifs, including an ATP/GTPase specific P-loop, a Mg(2+)-binding site and five more specific motifs. Interacting selectively and non-covalently with a LRR domain (leucine rich repeats) of a protein. Interacting selectively and non-covalently with Helix Loop Helix, a domain of 40-50 residues that occurs in specific DNA-binding proteins that act as transcription factors. The domain is formed of two amphipathic helices joined by a variable length linker region that can form a loop and it mediates protein dimerization. Interacting selectively and non-covalently with a LIM domain (for Lin-11 Isl-1 Mec-3) of a protein, a domain with seven conserved cysteine residues and a histidine, that binds two zinc ions and acts as an interface for protein-protein interactions. Interacting selectively and non-covalently with a FH1 domain of a protein, a proline-rich domain, usually located in front of a FH2 domain. Interacting selectively and non-covalently with a C3HC4-type zinc finger domain of a protein. The C3HC4-type zinc finger is a variant of RING finger, is a cysteine-rich domain of 40 to 60 residues that coordinates two zinc ions, and has the consensus sequence: C-X2-C-X(9-39)-C-X(1-3)-H-X(2-3)-C-X2-C-X(4-48)-C-X2-C, where X is any amino acid. Many proteins containing a C3HC4-type RING finger play a key role in the ubiquitination pathway. Interacting selectively and non-covalently with a RING-like zinc finger domain domain of a protein. The RING-like domain is a zinc finger domain that is related to the C3HC4 RING finger domain. Interacting selectively and non-covalently with a SH2 domain (Src homology 2) of a protein, a protein domain of about 100 amino-acid residues and belonging to the alpha + beta domain class. Interacting selectively and non-covalently with an ankyrin repeat of a protein. Ankyrin repeats are tandemly repeated modules of about 33 amino acids; each repeat folds into a helix-loop-helix structure with a beta-hairpin/loop region projecting out from the helices at a 90-degree angle, and repeats stack to form an L-shaped structure. Interacting selectively and non-covalently with a CARD (N-terminal caspase recruitment) domain, a protein-protein interaction domain that belongs to the death domain-fold superfamily. These protein molecule families are similar in structure with each consisting of six or seven anti-parallel alpha-helices that form highly specific homophilic interactions between signaling partners. CARD exists in the N-terminal prodomains of several caspases and in apoptosis-regulatory proteins and mediates the assembly of CARD-containing proteins that participate in activation or suppression of CARD carrying members of the caspase family. Interacting selectively and non-covalently with the GTPase protein binding domain (GDB) domain of a protein. The GBD is a short motif, including a minimum region of 16 amino acids, identified in proteins that bind to small GTPases such as Cdc42 and Rac. Interacting selectively and non-covalently with a tetratricopeptide repeat (TPR) domain of a protein, the consensus sequence of which is defined by a pattern of small and large hydrophobic amino acids and a structure composed of helices. Interacting selectively and non-covalently with a WW domain of a protein, a small module composed of 40 amino acids and plays a role in mediating protein-protein interactions via proline-rich regions. Interacting selectively and non-covalently with a specific domain of a protein. Interacting selectively and non-covalently with a Toll-Interleukin receptor (TIR) domain of a protein. The TIR domain is an intracellular 200 residue domain that is found in the Toll protein, the interleukin-1 receptor (IL-1R), and MyD88; it contains three highly-conserved regions, and mediates protein-protein interactions between the Toll-like receptors (TLRs) and signal-transduction components. Interacting selectively and non-covalently with a FHA domain of a protein. The FHA domain is a phosphopeptide recognition domain found in many regulatory proteins, and consists of approximately 80-100 amino acid residues folded into an 11-stranded beta sandwich. Interacting selectively and non-covalently with the MH1 (MAD homology 1) domain of a protein. The MH1 domain is found at the amino terminus of MAD related proteins such as Smads and can mediate DNA binding in some proteins. Smads also use the MH1 domain to interact with some transcription factors. Interacting selectively and non-covalently with the MH2 (MAD homology 2) domain of a protein. The MH2 domain is found at the carboxy terminus of MAD related proteins such as Smads. The MH2 domain mediates interaction with a wide variety of proteins and provides specificity and selectivity to Smad function and also is critical for mediating interactions in Smad oligomers. Interacting selectively and non-covalently with a PDZ domain of a protein, a domain found in diverse signaling proteins. Interacting selectively and non-covalently with the LBD, the ligand binding domain found in nuclear receptors. In general, the LBDs consist of three layers comprised of twelve alpha-helices and several beta-strands that are organized around a lipophilic ligand-binding pocket. Interacting selectively and non-covalently with the DBD, DNA binding domain, of a protein. The DNA binding domain of the vitamin D receptor, one of a family of receptors with the DBD, is split into three regions, the P, D and T boxes. Residues that are critical for target sequence selectivity form the P-box. The D-box contains residues that are important for homodimerization of class I nuclear receptors. The T-box is essential for both DNA-binding and transactivation of the VDR; this region may also be important for dimerization with RXR for class II nuclear receptors. Interacting selectively and non-covalently with a POU domain of a protein. The POU domain is a bipartite DNA binding domain composed of two subunits separated by a non-conserved region of 15-55 amino acids; it is found in several eukaryotic transcription factors. The selective, non-covalent, often stoichiometric, interaction of a molecule with one or more specific sites on another molecule. Interacting selectively and non-covalently with a C2H2-type zinc finger domain of a protein. The C2H2 zinc finger is the classical zinc finger domain, in which two conserved cysteines and histidines co-ordinate a zinc ion. Interacting selectively and non-covalently with a PH domain (pleckstrin homology) of a protein, a domain of about 100 residues that occurs in a wide range of proteins involved in intracellular signaling or as constituents of the cytoskeleton. Interacting selectively and non-covalently with the FFAT motif, a short motif containing diphenylalanine in an acidic tract that targets proteins to the cytosolic surface of the ER and to the nuclear membrane by binding directly to members of the VAP (VAMP-associated protein) protein family. Interacting selectively and non-covalently with the titin Z domain, which recognizes and binds to the C-terminal calmodulin-like domain of alpha-actinin-2 (Act-EF34), adopts a helical structure, and binds in a groove formed by the two planes between the helix pairs of Act-EF34. Interacting selectively and non-covalently with the armadillo repeat domain of a protein, an approximately 40 amino acid long tandemly repeated sequence motif first identified in the Drosophila segment polarity protein armadillo. Arm-repeat proteins are involved in various processes, including intracellular signalling and cytoskeletal regulation.

View Gene Ontology (GO) Term

GO TERM SUMMARY
Name: protein domain specific binding
Acc: GO:0019904
Aspect: Molecular Function
Desc: Interacting selectively and non-covalently with a specific domain of a protein.
Synonyms:
  • protein domain-specific binding
Proteins in PDR annotated with:
   This term: 312 [Search]
   Term or descendants: 766 [Search]


[geneontology.org]
INTERACTIVE GO GRAPH

GO:0019904 - protein domain specific binding (interactive image map)
YRC Informatics Platform - Version 3.0
Created and Maintained by: Michael Riffle