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Search results 301 to 400 out of 452 for Pin1

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Type Details Score
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: mouse, laboratory
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus pahari
Protein Coding Gene
Type: protein_coding_gene
Organism: Mus spretus
Publication
First Author: Cui P
Year: 2016
Journal: Plant Cell
Title: The RNA Polymerase II C-Terminal Domain Phosphatase-Like Protein FIERY2/CPL1 Interacts with eIF4AIII and Is Essential for Nonsense-Mediated mRNA Decay in Arabidopsis.
Volume: 28
Issue: 3
Pages: 770-85
Publication
First Author: Fukudome A
Year: 2014
Journal: Plant J
Title: Arabidopsis CPL4 is an essential C-terminal domain phosphatase that suppresses xenobiotic stress responses.
Volume: 80
Issue: 1
Pages: 27-39
Protein Domain
Type: Family
Description: This entry represents Fcp1 and its homologues, including CTDP1 from humans and CPL1/2/3/4/5 from Arabidopsis. They are carboxy-terminal domain (CTD) phosphatases. CPL1 has been shown to interact with two NMD (nonsense-mediated decay) factors, eIF4AIII and UPF3, and is involved in the dephosphorylation of eIF4AIII []. CPL4 functions as a pol II CTD phosphatase and has been shown to dephosphorylate both Ser2- and Ser5-PO(4) of CTD in vitro []. Budding yeast Fcp1 has been shown to dephosphorylate RNA polymerase (RNAP) II subunit, and this interaction is modulated by the Pin1 protein [].
Protein
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1216  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 118  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 123  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 644  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1206  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 756  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 66  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 650  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1044  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 80  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 108  
Fragment?: false
Publication
First Author: Vitikainen M
Year: 2004
Journal: J Biol Chem
Title: Structure-function analysis of PrsA reveals roles for the parvulin-like and flanking N- and C-terminal domains in protein folding and secretion in Bacillus subtilis.
Volume: 279
Issue: 18
Pages: 19302-14
Protein Domain
Type: Family
Description: The function of nuclear protein Sp140 is not known, though it contains several chromatin related modules such as plant homeodomain (PHD), bromodomain (BRD) and SAND domain, which suggests a role in chromatin-mediated regulation of gene expression []. It also harbours a nuclear localisation signal and a dimerisation domain (HSR or CARD domain). The PHD finger of Sp140 presents an atypical fold which does not bind to histone H3 tails but binds to peptidylprolyl isomerase Pin1. Pin1 catalyses the isomerisation of a phospho-Threonine-Proline bond in Sp140-PHD and thus may modulate Sp140 function [].Human Sp140 is an interferon inducible nuclear leukocyte-specific protein that may be involved in the pathogenesis of acute promyelocytic leukemia and viral infection []. It localises to LYSP100-associated nuclear dots and is also a component of the promyelocytic leukemia nuclear body (PML-NBs) [, ]. The Sp140 locus has been identified as a lymphocytic leukemia (CLL) risk locus [].This family also includes protein Sp140-like (SP140L) [].
Publication
First Author: Lu PJ
Year: 1999
Journal: Science
Title: Function of WW domains as phosphoserine- or phosphothreonine-binding modules.
Volume: 283
Issue: 5406
Pages: 1325-8
Publication
First Author: Tornillo G
Year: 2018
Journal: Cell Rep
Title: Dual Mechanisms of LYN Kinase Dysregulation Drive Aggressive Behavior in Breast Cancer Cells.
Volume: 25
Issue: 13
Pages: 3674-3692.e10
Publication
First Author: Penela P
Year: 2010
Journal: Proc Natl Acad Sci U S A
Title: G protein-coupled receptor kinase 2 (GRK2) modulation and cell cycle progression.
Volume: 107
Issue: 3
Pages: 1118-23
Publication
First Author: Luo ML
Year: 2015
Journal: Cell Rep
Title: The Rab2A GTPase promotes breast cancer stem cells and tumorigenesis via Erk signaling activation.
Volume: 11
Issue: 1
Pages: 111-24
Publication
First Author: Zucchelli C
Year: 2014
Journal: FEBS J
Title: Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1.
Volume: 281
Issue: 1
Pages: 216-31
Publication
First Author: Yap KL
Year: 2010
Journal: Crit Rev Biochem Mol Biol
Title: Keeping it in the family: diverse histone recognition by conserved structural folds.
Volume: 45
Issue: 6
Pages: 488-505
Publication
First Author: Bloch DB
Year: 1996
Journal: J Biol Chem
Title: Identification and characterization of a leukocyte-specific component of the nuclear body.
Volume: 271
Issue: 46
Pages: 29198-204
Publication
First Author: Di Bernardo MC
Year: 2008
Journal: Nat Genet
Title: A genome-wide association study identifies six susceptibility loci for chronic lymphocytic leukemia.
Volume: 40
Issue: 10
Pages: 1204-10
Publication
First Author: Dent AL
Year: 1996
Journal: Blood
Title: LYSP100-associated nuclear domains (LANDs): description of a new class of subnuclear structures and their relationship to PML nuclear bodies.
Volume: 88
Issue: 4
Pages: 1423-6
Publication  
First Author: Saare M
Year: 2015
Journal: J Immunol Res
Title: SP140L, an Evolutionarily Recent Member of the SP100 Family, Is an Autoantigen in Primary Biliary Cirrhosis.
Volume: 2015
Pages: 526518
Protein
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 179  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 187  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 191  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 93  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 88  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 140  
Fragment?: false
Publication
First Author: Bitto E
Year: 2002
Journal: Structure
Title: Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins.
Volume: 10
Issue: 11
Pages: 1489-98
Publication
First Author: Toledo F
Year: 2007
Journal: Mol Cell Biol
Title: Mouse mutants reveal that putative protein interaction sites in the p53 proline-rich domain are dispensable for tumor suppression.
Volume: 27
Issue: 4
Pages: 1425-32
Publication  
First Author: Lattanzio F
Year: 2014
Journal: Neuroscience
Title: Human apolipoprotein E4 modulates the expression of Pin1, Sirtuin 1, and Presenilin 1 in brain regions of targeted replacement apoE mice.
Volume: 256
Pages: 360-9
Publication
First Author: Kukalev A
Year: 2017
Journal: Cereb Cortex
Title: Deficiency of Cks1 Leads to Learning and Long-Term Memory Defects and p27 Dependent Formation of Neuronal Cofilin Aggregates.
Volume: 27
Issue: 1
Pages: 11-23
Publication
First Author: Bhaskaran N
Year: 2013
Journal: Mol Cell Biol
Title: Fbw7α and Fbw7γ collaborate to shuttle cyclin E1 into the nucleolus for multiubiquitylation.
Volume: 33
Issue: 1
Pages: 85-97
Publication
First Author: Nesti E
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: C-terminal domain small phosphatase 1 and MAP kinase reciprocally control REST stability and neuronal differentiation.
Volume: 111
Issue: 37
Pages: E3929-36
Publication
First Author: Behm M
Year: 2017
Journal: J Cell Sci
Title: Accumulation of nuclear ADAR2 regulates adenosine-to-inosine RNA editing during neuronal development.
Volume: 130
Issue: 4
Pages: 745-753
Publication
First Author: Culotta L
Year: 2020
Journal: J Neurosci
Title: SULT4A1 Modulates Synaptic Development and Function by Promoting the Formation of PSD-95/NMDAR Complex.
Volume: 40
Issue: 37
Pages: 7013-7026
Publication  
First Author: Qiu C
Year: 2021
Journal: Sci Transl Med
Title: Cis P-tau underlies vascular contribution to cognitive impairment and dementia and can be effectively targeted by immunotherapy in mice.
Volume: 13
Issue: 596
Protein
Organism: Mus musculus/domesticus
Length: 131  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 172  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 141  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
Publication
First Author: Tosh K
Year: 2006
Journal: Proc Natl Acad Sci U S A
Title: Variants in the SP110 gene are associated with genetic susceptibility to tuberculosis in West Africa.
Volume: 103
Issue: 27
Pages: 10364-10368
Publication
First Author: Cai L
Year: 2011
Journal: Med Chem
Title: Identification of proteins interacting with human SP110 during the process of viral infections.
Volume: 7
Issue: 2
Pages: 121-6
Publication
First Author: Bloch DB
Year: 2000
Journal: Mol Cell Biol
Title: Sp110 localizes to the PML-Sp100 nuclear body and may function as a nuclear hormone receptor transcriptional coactivator.
Volume: 20
Issue: 16
Pages: 6138-46
Publication
First Author: Roscioli T
Year: 2006
Journal: Nat Genet
Title: Mutations in the gene encoding the PML nuclear body protein Sp110 are associated with immunodeficiency and hepatic veno-occlusive disease.
Volume: 38
Issue: 6
Pages: 620-2
Protein Domain
Type: Family
Description: This entry includes a group of nuclear dot-associated proteins, including Sp110/Sp140/Sp140L from humans. They are proteins with a constituent of nuclear domains, also known as nuclear dots (NDs). Sequences similar to the Sp100 homodimerization/ND-targeting region occur in several other proteins and constitute a novel protein motif, termed HSR domain (for homogeneously-staining region) [].Sp110 is a leukocyte-specific component of the nuclear body []. It may function as a nuclear hormone receptor transcriptional coactivator that may play a role in inducing differentiation of myeloid cells []. It is also involved in resisting intracellular pathogens and functions as an important drug target for preventing intracellular pathogen diseases, such as tuberculosis, hepatic veno-occlusive disease, and intracellular cancers [, ]. Sp110 gene polymorphisms may be associated with susceptibility to tuberculosis in Chinese population []. The function of nuclear protein Sp140 is not known, though it contains several chromatin related modules such as plant homeodomain (PHD), bromodomain (BRD) and SAND domain, which suggests a role in chromatin-mediated regulation of gene expression []. It also harbours a nuclear localisation signal and a dimerisation domain (HSR or CARD domain). The PHD finger of Sp140 presents an atypical fold which does not bind to histone H3 tails but binds to peptidylprolyl isomerase Pin1. Pin1 catalyses the isomerisation of a phospho-Threonine-Proline bond in Sp140-PHD and thus may modulate Sp140 function [].Human Sp140 is an interferon inducible nuclear leukocyte-specific protein that may be involved in the pathogenesis of acute promyelocytic leukemia and viral infection []. It localises to LYSP100-associated nuclear dots and is also a component of the promyelocytic leukemia nuclear body (PML-NBs) [, ]. The Sp140 locus has been identified as a lymphocytic leukemia (CLL) risk locus [].This family also includes protein Sp140-like (SP140L) [].
Publication
First Author: El Asmi F
Year: 2014
Journal: PLoS Pathog
Title: Implication of PMLIV in both intrinsic and innate immunity.
Volume: 10
Issue: 2
Pages: e1003975
Publication
First Author: He J
Year: 2001
Journal: J Biol Chem
Title: Phosphorylation and cell cycle-dependent regulation of Na+/H+ exchanger regulatory factor-1 by Cdc2 kinase.
Volume: 276
Issue: 45
Pages: 41559-65
Publication  
First Author: Jiang X
Year: 2021
Journal: Front Cell Dev Biol
Title: RETSAT Mutation Selected for Hypoxia Adaptation Inhibits Tumor Growth.
Volume: 9
Pages: 744992
Protein
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 220  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 229  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 325  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 149  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 215  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 59  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 122  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 343  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 121  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 212  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 304  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 135  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 348  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 188  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 119  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 263  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 116  
Fragment?: false