phosphoprotein


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phos·pho·pro·tein

 (fŏs′fō-prō′tēn′, -tē-ĭn)
n.
Any of a group of proteins, such as casein, containing chemically bound phosphoric acid.

phosphoprotein

(ˌfɒsfəˈprəʊtiːn)
n
(Biochemistry) any of a group of conjugated proteins, esp casein, in which the protein molecule is bound to phosphoric acid

phos•pho•pro•tein

(ˌfɒs foʊˈproʊ tin, -ti ɪn)

n.
a protein, as casein or ovalbumin, in which one or more hydroxyl groups of serine, threonine, or tyrosine are hydroxylated.
[1905–10]
ThesaurusAntonymsRelated WordsSynonymsLegend:
Noun1.phosphoprotein - containing chemically bound phosphoric acid
protein - any of a large group of nitrogenous organic compounds that are essential constituents of living cells; consist of polymers of amino acids; essential in the diet of animals for growth and for repair of tissues; can be obtained from meat and eggs and milk and legumes; "a diet high in protein"
casein - a milk protein used in making e.g. plastics and adhesives
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References in periodicals archive ?
NCL is a nucleolar phosphoprotein that is also among the most abundant nonhistone proteins in the nucleus.
The 6 genes for avulaviruses (coding for the nucleoprotein, phosphoprotein, matrix protein, fusion protein, hemagglutinin-neuraminidase protein, and RNA-dependent RNA polymerase protein) were identified in these virus genomes (online Technical Appendix Figure 2, panel A).
The characterized 13 DEGs (2-fold up-regulated), such as v-myb avian myeloblastosis viral oncogene homolog (MYB), recombination activating gene-1 (RAG-1), epithelial cell adhesion molecule (TACSTD1), Secale cereale 75k gamma secalin gene (75k gamma secalin ), snRNA (U6), microRNA mir-155 (ssc-mir-155), microRNA let-7c (ssc-let-7c), NCK interacting protein with SH3 domain/cadherin, EGF LAG seven-pass G-type receptor 3 (CELSR3,NCKIPSD), cAMP-regulated phosphoprotein, 21kDa (ARPP21), interleukin 20 receptor beta (IL20RB), DNA nucleotidylexotransferase (DNTT), collagen, type V, alpha 2 (COL5A2), and microRNA mir-374a/microRNA mir-374b/microRNA mir-421/microRNA mir-545 (ssc-mir-374a) are shown in Supplementary Table I.
STHMN1 is a major cytosolic phosphoprotein and a microtubule-depolymerizing molecule involved in the metastatic process of various cancers; however, the mechanism of its regulation has not been fully clarified.
The most important genes clustering CTCs in the subgroups were cadherin 2 (CDH2), collagen type I alpha 2 chain (COL1A2), collagen type V alpha 2 chain (COL5A2), fibronectin 1 (FN1), microtubule associated protein 1B (MAP1B), matrix metallopeptidase 3 (MMP3), SRY-box 10 (S0X10), secreted phosphoprotein 1 (SPP1), zinc finger E-box binding homeobox 1 (ZEB1), and zinc finger E-box binding homeobox 2 (ZEB2; Fig.
The murine gene encoding secreted phosphoprotein 1 (osteopontin): promoter structure, activity, and induction in vivo by estrogen and progesterone.
Molecular weight standards (#161-0374; Bio-Rad Laboratories) and phosphoprotein standards (Invitrogen #P33350; Thermo Fisher Scientific) were run along with glue samples.
ITI-007 is a first-in-class molecule that combines potent serotonin 5-hydroxytryptamine2A-receptor antagonism, dopamine receptor phosphoprotein modulation (DPPM), glutamatergic phosphoprotein modulation, and serotonin reuptake inhibition into a single-drug candidate for the treatment of acute and residual schizophrenia.
To confirm the detected changes in transcript levels between the H and L groups (n = 3), we quantified the expression level of 8 genes (identified via RNA-Seq) selected from the DEGs: peroxisome proliferator-activated receptor gamma, coactivator 1 beta (PPARGC1B), secreted phosphoprotein 2 (SPP2), stearoyl-CoA desaturase 5 (SCD5), myogenic differentiation (MyoD), chloride channel 4 (CLCN4), collagen, type I, alpha 1 (COL1A1), myogenin (MyoG), and stearoyl-CoA desaturase (SCD).
However, this protein divides into two proteins with diametrically opposed functions, dentin sialoprotein (DSP) and dentin phosphoprotein (DPP).
A HKII-centered multiprotein complex, consisting of phosphoprotein enriched in astrocytes (PEA15) and possibly other proteins, has been demonstrated to function as a molecular switch regulating neuronal survival depending on the metabolic state.
It is a structural protein which encapsidates the viral genome into an RNAse-resistant nucleocapsid (the template for RNA synthesis) and together with phosphoprotein forms the ribonucleoprotein which constitutes the minimum essential for transcription and replication of viral genome in the cell cytoplasm (Knipe and Howley 2001).