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 |
|
•
•
•
•
•
|