Type |
Details |
Score |
Protein Domain |
Type: |
Family |
Description: |
Lime is involved in BCR (B-cell antigen receptor)-mediated signaling in B-cells and TCR (T-cell antigen receptor)-mediated T-cell signaling in T-cells. It couples activation of these receptors and their associated kinases with distal intracellular events such as calcium mobilisation or MAPK activation through the recruitment of PLCG2, GRB2, GRAP2, and other signaling molecules [, ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
The drug resistance transporter Bcr/CflA proteins are predicted to have 12 membrane-spanning regions. Members with known activity include Bcr (bicyclomycin resistance protein) in Escherichia coli [], Flor (chloramphenicol and florfenicol resistance) in Salmonella typhimurium [], and CmlA (chloramphenicol resistance) found on the Pseudomonas plasmid R1033 []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the BTB and C-terminal Kelch domain found in KLHL42, which is a substrate-specific adaptor of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex required for mitotic progression and cytokinesis. The BCR(KLHL42) E3 ubiquitin ligase complex mediates the ubiquitination and subsequent degradation of KATNA1. KLHL42 is involved in microtubule dynamics throughout mitosis []. |
|
•
•
•
•
•
|
Publication |
First Author: |
Hiroki H |
Year: |
2023 |
Journal: |
Sci Rep |
Title: |
Targeting Poly(ADP)ribose polymerase in BCR/ABL1-positive cells. |
Volume: |
13 |
Issue: |
1 |
Pages: |
7588 |
|
•
•
•
•
•
|
Publication |
First Author: |
Honda H |
Year: |
2000 |
Journal: |
Blood |
Title: |
Acquired loss of p53 induces blastic transformation in p210(bcr/abl)-expressing hematopoietic cells: a transgenic study for blast crisis of human CML. |
Volume: |
95 |
Issue: |
4 |
Pages: |
1144-50 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hemmeryckx B |
Year: |
2002 |
Journal: |
Oncogene |
Title: |
BCR/ABL P190 transgenic mice develop leukemia in the absence of Crkl. |
Volume: |
21 |
Issue: |
20 |
Pages: |
3225-31 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yasuda T |
Year: |
2004 |
Journal: |
J Exp Med |
Title: |
Role of Dok-1 and Dok-2 in myeloid homeostasis and suppression of leukemia. |
Volume: |
200 |
Issue: |
12 |
Pages: |
1681-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Cho YJ |
Year: |
2005 |
Journal: |
Mol Cell Biol |
Title: |
Generation of rac3 null mutant mice: role of Rac3 in Bcr/Abl-caused lymphoblastic leukemia. |
Volume: |
25 |
Issue: |
13 |
Pages: |
5777-85 |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Dok1/Dok1 Dok2/Dok2 Tg(Tec-BCR/ABL1)5Hhi/? |
Background: |
involves: C57BL/6 |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Rac3/Rac3 Tg(BCR/ABL)623Hkp/? |
Background: |
involves: C57BL/6 * C57BL/6J * CBA |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Crkl/Crkl Tg(BCR/ABL)623Hkp/? |
Background: |
involves: 129S1/Sv * 129X1/SvJ * Black Swiss * C57BL/6 * CBA |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Sadras T |
Year: |
2021 |
Journal: |
Mol Cell |
Title: |
Developmental partitioning of SYK and ZAP70 prevents autoimmunity and cancer. |
Volume: |
81 |
Issue: |
10 |
Pages: |
2094-2111.e9 |
|
•
•
•
•
•
|
HT Experiment |
|
Experiment Type: |
RNA-Seq |
Study Type: |
Baseline |
Source: |
GEO |
|
•
•
•
•
•
|
Publication |
First Author: |
Chen Y |
Year: |
2009 |
Journal: |
Mol Cell |
Title: |
Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement. |
Volume: |
35 |
Issue: |
6 |
Pages: |
841-55 |
|
•
•
•
•
•
|
Publication |
First Author: |
Mao H |
Year: |
2017 |
Journal: |
Nat Plants |
Title: |
Arabidopsis BTB/POZ protein-dependent PENETRATION3 trafficking and disease susceptibility. |
Volume: |
3 |
Issue: |
11 |
Pages: |
854-858 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry represents a group of BTB/POZ domain-containing proteins, such as BACURD1-3 from humans. They act as the substrate-specific adapters of a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex, which mediates the ubiquitination of RhoA, leading to its degradation by the proteasome []. This entry also includes EAP3 from Arabidopsis. The BTB/POZ domain of EAP3 displays poor conservation of the residues required for CUL3 binding and is not likely to function as an E3 ligase adaptor []. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
182
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
311
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Gómez C |
Year: |
2022 |
Journal: |
Cancers (Basel) |
Title: |
Critical Requirement of SOS1 for Development of BCR/ABL-Driven Chronic Myelogenous Leukemia. |
Volume: |
14 |
Issue: |
16 |
|
|
•
•
•
•
•
|
Publication |
First Author: |
Honda H |
Year: |
1998 |
Journal: |
Blood |
Title: |
Development of acute lymphoblastic leukemia and myeloproliferative disorder in transgenic mice expressing p210bcr/abl: a novel transgenic model for human Ph1-positive leukemias. |
Volume: |
91 |
Issue: |
6 |
Pages: |
2067-75 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hemmeryckx B |
Year: |
2001 |
Journal: |
Cancer Res |
Title: |
Crkl enhances leukemogenesis in BCR/ABL P190 transgenic mice. |
Volume: |
61 |
Issue: |
4 |
Pages: |
1398-405 |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhuang M |
Year: |
2009 |
Journal: |
Mol Cell |
Title: |
Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases. |
Volume: |
36 |
Issue: |
1 |
Pages: |
39-50 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kwon JE |
Year: |
2006 |
Journal: |
J Biol Chem |
Title: |
BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase. |
Volume: |
281 |
Issue: |
18 |
Pages: |
12664-72 |
|
•
•
•
•
•
|
Publication |
First Author: |
van Geersdaele LK |
Year: |
2013 |
Journal: |
Acta Crystallogr D Biol Crystallogr |
Title: |
Structural basis of high-order oligomerization of the cullin-3 adaptor SPOP. |
Volume: |
69 |
Issue: |
Pt 9 |
Pages: |
1677-84 |
|
•
•
•
•
•
|
Publication |
First Author: |
Canning P |
Year: |
2013 |
Journal: |
J Biol Chem |
Title: |
Structural basis for Cul3 protein assembly with the BTB-Kelch family of E3 ubiquitin ligases. |
Volume: |
288 |
Issue: |
11 |
Pages: |
7803-14 |
|
•
•
•
•
•
|
Publication |
First Author: |
Takahashi D |
Year: |
2013 |
Journal: |
Biochem Biophys Res Commun |
Title: |
KLHL2 interacts with and ubiquitinates WNK kinases. |
Volume: |
437 |
Issue: |
3 |
Pages: |
457-62 |
|
•
•
•
•
•
|
Publication |
First Author: |
Jiang S |
Year: |
2005 |
Journal: |
J Neurochem |
Title: |
Process elongation of oligodendrocytes is promoted by the Kelch-related actin-binding protein Mayven. |
Volume: |
92 |
Issue: |
5 |
Pages: |
1191-203 |
|
•
•
•
•
•
|
Publication |
First Author: |
Soltysik-Espanola M |
Year: |
1999 |
Journal: |
Mol Biol Cell |
Title: |
Characterization of Mayven, a novel actin-binding protein predominantly expressed in brain. |
Volume: |
10 |
Issue: |
7 |
Pages: |
2361-75 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
KLHL2, also called actin-binding protein Mayven, is a novel actin-binding protein predominantly expressed in the brain. It plays a role in the reorganisation of the actin cytoskeleton, and promotes growth of cell projections in oligodendrocyte precursors [, ]. KLHL2 is a component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, leading most often to their proteasomal degradation [, ]. It contains a BTB domain and kelch repeat domains, characteristics of a kelch family protein.This entry represents the BTB/POZ domain, which is a common protein-protein interaction motif of about 100 amino acids. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
This entry represents the C-terminal BACK (BTB and C-terminal Kelch) domain of speckle-type POZ protein (SPOP, also known as HIB homologue 1 or Roadkill homologue 1). This domain contains a pair of α-helices which seem to be conserved among Cul3 adaptors [].SPOP is an adaptor protein that forms a complex with Cul3, cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex, and is involved in ubiquitination of BMI1, H2AFY, and the death-associated protein 6 (DAXX) []. The C-terminal BACK domain of SPOP, may be involved in oligomer formation and in recruiting Cul3 (together with the adjacent BTB domain), whereas the N-terminal MATH domain recruits substrates [, ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Sahputra R |
Year: |
2018 |
Journal: |
Eur J Immunol |
Title: |
Evaluating the IgMi mouse as a novel tool to study B-cell biology. |
Volume: |
48 |
Issue: |
12 |
Pages: |
2068-2071 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
128
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
120
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
161
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Publication |
First Author: |
Trageser D |
Year: |
2009 |
Journal: |
J Exp Med |
Title: |
Pre-B cell receptor-mediated cell cycle arrest in Philadelphia chromosome-positive acute lymphoblastic leukemia requires IKAROS function. |
Volume: |
206 |
Issue: |
8 |
Pages: |
1739-53 |
|
•
•
•
•
•
|
Publication |
First Author: |
Virely C |
Year: |
2010 |
Journal: |
Leukemia |
Title: |
Haploinsufficiency of the IKZF1 (IKAROS) tumor suppressor gene cooperates with BCR-ABL in a transgenic model of acute lymphoblastic leukemia. |
Volume: |
24 |
Issue: |
6 |
Pages: |
1200-4 |
|
•
•
•
•
•
|
Publication |
First Author: |
Waldron T |
Year: |
2012 |
Journal: |
Leukemia |
Title: |
c-Myb and its target Bmi1 are required for p190BCR/ABL leukemogenesis in mouse and human cells. |
Volume: |
26 |
Issue: |
4 |
Pages: |
644-53 |
|
•
•
•
•
•
|
Publication |
First Author: |
Inokuchi K |
Year: |
2003 |
Journal: |
Blood |
Title: |
Myeloproliferative disease in transgenic mice expressing P230 Bcr/Abl: longer disease latency, thrombocytosis, and mild leukocytosis. |
Volume: |
102 |
Issue: |
1 |
Pages: |
320-3 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sato T |
Year: |
2014 |
Journal: |
Oncogene |
Title: |
Evi1 defines leukemia-initiating capacity and tyrosine kinase inhibitor resistance in chronic myeloid leukemia. |
Volume: |
33 |
Issue: |
42 |
Pages: |
5028-38 |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Ikzf1/Ikzf1<+> Tg(BCR/ABL)623Hkp/? |
Background: |
involves: 129S2/SvPas * C57BL/6 * CBA |
Zygosity: |
cx |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Onyilagha C |
Year: |
2015 |
Journal: |
PLoS Negl Trop Dis |
Title: |
The B cell adaptor molecule Bam32 is critically important for optimal antibody response and resistance to Trypanosoma congolense infection in mice. |
Volume: |
9 |
Issue: |
4 |
Pages: |
e0003716 |
|
•
•
•
•
•
|
Publication |
First Author: |
Marshall AJ |
Year: |
2007 |
Journal: |
Biochem Soc Trans |
Title: |
Regulation of B-lymphocyte activation by the PH domain adaptor protein Bam32/DAPP1. |
Volume: |
35 |
Issue: |
Pt 2 |
Pages: |
181-2 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
STAP1 is a signal-transducing adaptor protein. It is composed of a Pleckstrin Homology (PH) and SH2 domains along with several tyrosine phosphorylation sites. STAP-1 is an orthologue of BRDG1 (also known as BCR downstream signaling 1). STAP1 protein functions as a docking protein acting downstream of Tec tyrosine kinase in B cell antigen receptor signaling. The protein is phosphorylated by Tec and participates in a positive feedback loop, increasing Tec activity []. STAP-1 has been shown to interact with STAT5 []. This entry represents the SH2 domain of STAP1.In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites [, , ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
DAPP1/Bam32 is an adaptor protein that plays important roles in B cell receptor signalling, T cell receptor signalling and antibody affinity maturation in germinal centres []. It contains a putative myristoylation site at its N terminus, followed by a SH2 domain, and a pleckstrin homology (PH) domain at its C terminus. It translocates to the plasma membrane of B-lymphoma cells upon BCR (B-cell receptor) cross-linking; this translocation is PI3K (phosphoinositide 3-kinase)-dependent and PH domain-mediated []. This entry represents the SH2 domain of DAPP1/Bam32. In general SH2 domains are involved in signal transduction. They typically bind pTyr-containing ligands via two surface pockets, a pTyr and hydrophobic binding pocket, allowing proteins with SH2 domains to localize to tyrosine phosphorylated sites [, , , , , ]. |
|
•
•
•
•
•
|
Allele |
Name: |
signal peptide peptidase like 2A; mutation 1, Australian National University |
Allele Type: |
Chemically induced (ENU) |
|
|
•
•
•
•
•
|
Allele |
Name: |
elongation factor for RNA polymerase II 2; targeted mutation 1.1, Christine Milcarek |
Allele Type: |
Targeted |
Attribute String: |
Conditional ready, No functional change |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Sppl2a/Sppl2a |
Background: |
involves: C57BL/6JAnu |
Zygosity: |
hm |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Genotype |
Symbol: |
Card11/Card11<+> |
Background: |
involves: C57BL/6 |
Zygosity: |
ht |
Has Mutant Allele: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
512
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Gene Segment |
Type: |
gene_segment |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|