Type |
Details |
Score |
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
305
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Homologous_superfamily |
Description: |
This superfamily includes several eukaryotic Sin3 associated polypeptide p18 (SAP18) sequences. SAP18 is known to be a component of the Sin3-containing complex which is responsible for the repression of transcription via the modification of histone polypeptides []. SAP18 (UBL domain) is one of the three three ASAP subunits (along with Acinus (β-hairpin motif) and RNPS1 (RRM domain)) that play a role in programmed cell death, transcriptional regulation, pre-mRNA splicing and mRNA quality control [, ]. The ASAP complex interacts with the exon-junction complex (EJC), a messenger ribonucleoprotein complex involved in post-transcriptional regulation [].The high degree of evolutionary conservation and the fortuitous crystal contacts at the α-β groove suggest that this surface of SAP18 is a hot spot for interactions. Possible binding partners targeting this surface of SAP18 are transcription factors (such as Bicoid and Kruppel) and/or Sin3a-HDAC subunits. |
|
•
•
•
•
•
|
Publication |
First Author: |
Yang D |
Year: |
1999 |
Journal: |
Cancer Res |
Title: |
Identification of a gene coding for a protein possessing shared tumor epitopes capable of inducing HLA-A24-restricted cytotoxic T lymphocytes in cancer patients. |
Volume: |
59 |
Issue: |
16 |
Pages: |
4056-63 |
|
•
•
•
•
•
|
Publication |
First Author: |
Stanĕk D |
Year: |
2003 |
Journal: |
J Cell Biol |
Title: |
Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal bodies. |
Volume: |
160 |
Issue: |
4 |
Pages: |
505-16 |
|
•
•
•
•
•
|
Publication |
First Author: |
Murachelli AG |
Year: |
2012 |
Journal: |
Nat Struct Mol Biol |
Title: |
The structure of the ASAP core complex reveals the existence of a Pinin-containing PSAP complex. |
Volume: |
19 |
Issue: |
4 |
Pages: |
378-86 |
|
•
•
•
•
•
|
Publication |
First Author: |
Liu Y |
Year: |
2002 |
Journal: |
J Biol Chem |
Title: |
HIV-1 Tat protein-mediated transactivation of the HIV-1 long terminal repeat promoter is potentiated by a novel nuclear Tat-interacting protein of 110 kDa, Tip110. |
Volume: |
277 |
Issue: |
26 |
Pages: |
23854-63 |
|
•
•
•
•
•
|
Publication |
First Author: |
Medenbach J |
Year: |
2004 |
Journal: |
Mol Cell Biol |
Title: |
Human U4/U6 snRNP recycling factor p110: mutational analysis reveals the function of the tetratricopeptide repeat domain in recycling. |
Volume: |
24 |
Issue: |
17 |
Pages: |
7392-401 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
111
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
107
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
92
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Schwerk C |
Year: |
2003 |
Journal: |
Mol Cell Biol |
Title: |
ASAP, a novel protein complex involved in RNA processing and apoptosis. |
Volume: |
23 |
Issue: |
8 |
Pages: |
2981-90 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the RNA recognition motif 1 (RRM1) of SART3 (also known as Tip110), which is an RNA-binding protein expressed in the nucleus of the majority of proliferating cells, including normal cells and malignant cells, but not in normal tissues except for the testes and fetal liver []. It is involved in the regulation of mRNA splicing probably via its complex formation with RNPS1 (an RNA-binding protein with a serine-rich domain), a pre-mRNA-splicing factor []. SART3 has also been identified as a nuclear Tat-interacting protein that regulates Tat transactivation activity through direct interaction and functions as an important cellular factor for HIV-1 gene expression and viral replication []. In addition, SART3 is required for U6 snRNP targeting to Cajal bodies []. It binds specifically and directly to the U6 snRNA, interacts transiently with the U6 and U4/U6 snRNPs, and promotes the reassembly of U4/U6 snRNPs after splicing in vitro [].SART3 contains an N-terminal HAT (half-a-tetratricopeptide repeat)-rich domain, a nuclearlocalization signal (NLS) domain, and two C-terminal RNA recognition motifs (RRMs). |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the RNA recognition motif 2 (RRM2) of SART3 (also known as Tip110), which is an RNA-binding protein expressed in the nucleus of the majority of proliferating cells, including normal cells and malignant cells, but not in normal tissues except for the testes and fetal liver []. It is involved in the regulation of mRNA splicing probably via its complex formation with RNPS1 (an RNA-binding protein with a serine-rich domain), a pre-mRNA-splicing factor []. SART3 has also been identified as a nuclear Tat-interacting protein that regulates Tat transactivation activity through direct interaction and functions as an important cellular factor for HIV-1 gene expression and viral replication []. In addition, SART3 is required for U6 snRNP targeting to Cajal bodies []. It binds specifically and directly to the U6 snRNA, interacts transiently with the U6 and U4/U6 snRNPs, and promotes the reassembly of U4/U6 snRNPs after splicing in vitro [].SART3 contains a HAT (N-terminal half-a-tetratricopeptide repeat)-rich domain, a nuclearlocalization signal (NLS) domain, and two C-terminal RNA recognition motifs (RRMs). |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
153
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
153
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
172
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhang Y |
Year: |
1997 |
Journal: |
Cell |
Title: |
Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex. |
Volume: |
89 |
Issue: |
3 |
Pages: |
357-64 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
552
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
634
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
580
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
581
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
378
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
962
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Sahara S |
Year: |
1999 |
Journal: |
Nature |
Title: |
Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. |
Volume: |
401 |
Issue: |
6749 |
Pages: |
168-73 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1338
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1272
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1266
 |
Fragment?: |
true |
|
•
•
•
•
•
|