| D011487 |
Protein Conformation |
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain). |
Conformation, Protein,Conformations, Protein,Protein Conformations |
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| D011505 |
Protein-Tyrosine Kinases |
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors. |
Tyrosine Protein Kinase,Tyrosine-Specific Protein Kinase,Protein-Tyrosine Kinase,Tyrosine Kinase,Tyrosine Protein Kinases,Tyrosine-Specific Protein Kinases,Tyrosylprotein Kinase,Kinase, Protein-Tyrosine,Kinase, Tyrosine,Kinase, Tyrosine Protein,Kinase, Tyrosine-Specific Protein,Kinase, Tyrosylprotein,Kinases, Protein-Tyrosine,Kinases, Tyrosine Protein,Kinases, Tyrosine-Specific Protein,Protein Kinase, Tyrosine-Specific,Protein Kinases, Tyrosine,Protein Kinases, Tyrosine-Specific,Protein Tyrosine Kinase,Protein Tyrosine Kinases,Tyrosine Specific Protein Kinase,Tyrosine Specific Protein Kinases |
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| D011518 |
Proto-Oncogene Proteins |
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity. |
Cellular Proto-Oncogene Proteins,c-onc Proteins,Proto Oncogene Proteins, Cellular,Proto-Oncogene Products, Cellular,Cellular Proto Oncogene Proteins,Cellular Proto-Oncogene Products,Proto Oncogene Products, Cellular,Proto Oncogene Proteins,Proto-Oncogene Proteins, Cellular,c onc Proteins |
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| D001665 |
Binding Sites |
The parts of a macromolecule that directly participate in its specific combination with another molecule. |
Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining |
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| D014443 |
Tyrosine |
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin. |
L-Tyrosine,Tyrosine, L-isomer,para-Tyrosine,L Tyrosine,Tyrosine, L isomer,para Tyrosine |
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| D044767 |
Ubiquitin-Protein Ligases |
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes. |
Ubiquitin-Protein Ligase,E3 Ligase,E3 Ubiquitin Ligase,Ubiquitin Ligase E3,Ubiquitin-Protein Ligase E3,Ligase E3, Ubiquitin,Ligase E3, Ubiquitin-Protein,Ligase, E3,Ligase, E3 Ubiquitin,Ligase, Ubiquitin-Protein,Ligases, Ubiquitin-Protein,Ubiquitin Ligase, E3,Ubiquitin Protein Ligase,Ubiquitin Protein Ligase E3,Ubiquitin Protein Ligases |
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| D050721 |
Proto-Oncogene Proteins c-cbl |
Proto-oncogene proteins that negatively regulate RECEPTOR PROTEIN-TYROSINE KINASE signaling. It is a UBIQUITIN-PROTEIN LIGASE and the cellular homologue of ONCOGENE PROTEIN V-CBL. |
c-cbl Protein,cbl Proto-Oncogene Protein,CBL E3 Ubiquitin Protein Ligase,Proto-Oncogene Protein c-cbl,RING Finger Protein 55,RNF55 Protein,c-cbl Proto-Oncogene Protein,Proto Oncogene Protein c cbl,Proto Oncogene Proteins c cbl,Proto-Oncogene Protein, c-cbl,Proto-Oncogene Protein, cbl,c cbl Proto Oncogene Protein,c-cbl, Proto-Oncogene Protein,c-cbl, Proto-Oncogene Proteins,cbl Proto Oncogene Protein |
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| D051746 |
ZAP-70 Protein-Tyrosine Kinase |
A protein tyrosine kinase that is required for T-CELL development and T-CELL ANTIGEN RECEPTOR function. |
70 kDa Zeta-Associated Protein,Syk-Related Tyrosine Kinase,ZAP-70 Kinase,ZAP-70 Protein,zeta-Chain Associated Protein Kinase (ZAP-70),70 kDa Zeta Associated Protein,Kinase, ZAP-70,Protein-Tyrosine Kinase, ZAP-70,Syk Related Tyrosine Kinase,Tyrosine Kinase, Syk-Related,ZAP 70 Kinase,ZAP 70 Protein,ZAP 70 Protein Tyrosine Kinase |
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| D018909 |
src Homology Domains |
Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS. |
SH Domains,SH1 Domain,SH2 Domain,SH3 Domain,src Homology Region 2 Domain,Homology Domain, src,Homology Domains, src,SH Domain,SH1 Domains,SH2 Domains,SH3 Domains,src Homology Domain |
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| D021382 |
Protein Sorting Signals |
Amino acid sequences found in transported proteins that selectively guide the distribution of the proteins to specific cellular compartments. |
Leader Signal Peptides,Leader Peptide,Leader Sequences, Peptide,Peptide Leader Sequences,Peptide Signal Sequences,Signal Peptide,Signal Peptides,Signal Sequence, Peptide,Signal Sequences,Signal Sequences, Peptide,Leader Peptides,Leader Sequence, Peptide,Leader Signal Peptide,Peptide Leader Sequence,Peptide Signal Sequence,Peptide, Leader,Peptide, Leader Signal,Peptide, Signal,Peptides, Leader,Peptides, Leader Signal,Peptides, Signal,Protein Sorting Signal,Sequence, Peptide Leader,Sequence, Peptide Signal,Sequence, Signal,Sequences, Peptide Leader,Sequences, Peptide Signal,Sequences, Signal,Signal Peptide, Leader,Signal Peptides, Leader,Signal Sequence,Signal, Protein Sorting,Signals, Protein Sorting,Sorting Signal, Protein,Sorting Signals, Protein |
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