Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).
Evidence
1:
Inferred from Physical InteractionIntAct
We have performed an exhaustive unbiased yeast two-hybrid analysis to identify interaction partners of two human Raf kinase isoforms, A-Raf and C-Raf, using their N-terminal regulatory domain as "bait." A total of 20 different human proteins were found to interact with Raf isoforms. Several of these interactions were novel and an extensive bioinformatics evaluation was performed for each. The novel putative interactions include a signalosome component, TOPK/PBK kinase, and two new putative protein phosphatases. The cysteine-rich zinc-binding domain (CRD) of Raf was found to interact with all 20 proteins and to achieve isoform-specific interactions. Since similar putative CRDs are present in a variety of protein serine-threonine kinases, the data suggest that the CRD may function as a major protein-protein interaction domain of these kinases. We propose possible functional consequences of these novel Raf interactions.
The sequence of reactions by which arginine is synthesized from ornithine, then cleaved to yield urea and regenerate ornithine. The overall reaction equation is NH3 + CO2 + aspartate + 3 ATP + 2 H2O = urea + fumarate + 2 ADP + 2 phosphate + AMP + diphosphate.
IEAUniPathway
Enzymatic activity
This protein acts as an enzyme. It is known to catalyze the following reaction
Protein involved in the synthesis of naturally-occuring amino acids. In addition to their use for protein biosynthesis, they are the precursors of many molecules such as purines, pyrimidines, histamines, adrenaline and melanin.
Protein involved in the urea cycle. This is a metabolic pathway in which ammonia, produced during amino acid degradation, is converted to urea in the liver, through a series of reactions that are distributed between the mitochondrial matrix and the cytosol.
Enzyme that catalyzes the joining of two molecules coupled with the breakdown of a pyrophosphate bond in ATP or a similar triphosphate. Sometimes the terms "synthase", "synthetase" or "carboxylase" are also used for this class of enzymes.
A reference proteome is a set of protein sequences derived from a complete proteome which constitutes a defined standard for a particular user community. Reference proteomes are manually defined according to a number of criteria. They cover the proteomes of well- studied model organisms and other proteomes of interest for biomedical and biotechnological research. Reference proteomes have been selected to provide broad coverage of the tree of life, and constitute a representative cross-section of the taxonomic diversity to be found within UniProtKB.
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