Type |
Details |
Score |
Protein Domain |
Type: |
Family |
Description: |
The NRL (for NPH3/RPT2-Like) family is formed by signaling molecules specificto higher plants. Several regions of sequence and predicted structuralconservation define members of the NRL family, with three domains being mostnotable: an N-terminal BTB domain, a centrally located NPH3domain, and a C-terminal coiled coil domain. The function of the NPH3 domainis not yet known [, , , , , , , ].Root phototropism protein 3 (RPT3), also known as nonphototropic hypocotyl 3 (NPH3), and root phototropism 2 (RPT2) () represent the founding members of a novel plant-specific family []. Three domains define the members of this family: an N-terminal BTB (broad complex, tramtrack, bric a brac) domain (), a centrally located NPH3 domain (), and a C-terminal coiled-coil domain.NPH3 assembles with CUL3 to form a E3 complex that ubiquitinates phototropin 1 (phot1) and modulates phototropic responsiveness [, ]. NPH3 is necessary for root and hypocotyl phototropisms, but not for the regulation of stomata opening or chloroplast relocation []. Coleoptile phototropism protein 1 (CPT1) is a rice orthologue of Arabidopsis NPH3 also required for phototropism []. This entry also includes DOT3 (AT5G10250) that is involved in shoot and primary root growth; DOT3 mutants produce an aberrant parallel venation pattern in juvenile leaves []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
This entry includes SKP1 and SKP1-like protein, elongin-C (also known as TCEB1). SKP1 is part of the E3 ubiquitin ligase complexes. Elongin-C has dual functions, works as a component of RNA polymerase II (Pol II) transcription elongation factor and as the substrate recognition subunit of a Cullin-RING E3 ubiquitin ligase []. Mammlian S-phase kinase-associated protein 1 (SKP1) is an essential component of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex, which mediates the ubiquitination of proteins involved in cell cycle progression, signal transduction and transcription []. It is also part of the ubiquitin E3 ligase complex (Skp1-Pam-Fbxo45) that controls the core epithelial-to-mesenchymal transition-inducing transcription factors []. Budding yeast Skp1 is a kinetochore protein found in several complexes, including the SCF ubiquitin ligase complex, the CBF3 complex that binds centromeric DNA [], and the RAVE complex that regulates assembly of the V-ATPase []. Elongin-C is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites []. It forms a complex with SIII regulatory subunits B, which serves as an adapter protein in the proteasomal degradation of target proteins via different E3 ubiquitin ligase complexes []. Elongin-C forms a complex with Cul3 that polyubiquitylates monoubiquitylated RNA polymerase II to trigger its proteolysis []. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Kelch-like protein 17 (KLHL17, also known as actinfilin) and Kelch-like protein 20 (KLHL20, also known as KLEIP) belong to the KLHL family []. KLHL17 binds to the actin cytoskeleton and serves as a substrate-specific adapter in the Cul3-dependent ubiquitin ligase complex that targets GluR6 kainate receptor subunit for degradation []. Kainate receptors (KAR) are ionotropic receptors that respond to the neurotransmitter glutamate and have been implicated in epilepsy, stroke, Alzheimer's and neuropathic pain [].KLHL20 assembles with CUL3 and RBX1 to form a multi-subunit Cullin-RING E3 ligase []. The KLHL (Kelch-like) proteins generally have a BTB/POZ domain, a BACK domain, and five to six Kelch motifs. They constitute a subgroup at the intersection between the BTB/POZ domain and Kelch domain superfamilies. The BTB/POZ domain facilitates protein binding [], while the Kelch domain (repeats) form β-propellers. The Kelch superfamily of proteins can be subdivided into five groups: (1) N-propeller, C-dimer proteins, (2) N-propeller proteins, (3) propeller proteins, (4) N-dimer, C-propeller proteins, and (5) C-propeller proteins. KLHL family members belong to the N-dimer, C-propeller subclass of Kelch repeat proteins []. In addition to BTB/POZ and Kelch domains, the KLHL family members contain a BACK domain, first described as a 130-residue region of conservation observed amongst BTB-Kelch proteins []. Many of the Kelch-like proteins have been identified as adaptors for the recruitment of substrates to Cul3-based E3 ubiquitin ligases [, ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Kelch-like protein 21 (KLHL21) is a substrate adaptor protein in the Cul3-KLHL21 E3 ubiquitin ligase complex. During cytokinesis, it localises to midzone microtubules in anaphase and recruits aurora B and Cul3 to this region [].The KLHL (Kelch-like) proteins generally have a BTB/POZ domain, a BACK domain, and five to six Kelch motifs. They constitute a subgroup at the intersection between the BTB/POZ domain and Kelch domain superfamilies. The BTB/POZ domain facilitates protein binding [], while the Kelch domain (repeats) form β-propellers. The Kelch superfamily of proteins can be subdivided into five groups: (1) N-propeller, C-dimer proteins, (2) N-propeller proteins, (3) propeller proteins, (4) N-dimer, C-propeller proteins, and (5) C-propeller proteins. KLHL family members belong to the N-dimer, C-propeller subclass of Kelch repeat proteins []. In addition to BTB/POZ and Kelch domains, the KLHL family members contain a BACK domain, first described as a 130-residue region of conservation observed amongst BTB-Kelch proteins []. Many of the Kelch-like proteins have been identified as adaptors for the recruitment of substrates to Cul3-based E3 ubiquitin ligases [, ]. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Homologous_superfamily |
Description: |
TAZ (Transcription Adaptor putative Zinc finger) domains are zinc-containing domains found in the homologous transcriptional co-activators CREB-binding protein (CBP) and the P300. CBP and P300 are histone acetyltransferases () that catalyse the reversible acetylation of all four histones in nucleosomes, acting to regulate transcription via chromatin remodelling. These large nuclear proteins interact with numerous transcription factors and viral oncoproteins, including p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1, and are involved in cell growth, differentiation and apoptosis []. Both CBP and P300 have two copies of the TAZ domain, one in the N-terminal region, the other in the C-terminal region. The TAZ1 domain of CBP and P300 forms a complex with CITED2 (CBP/P300-interacting transactivator with ED-rich tail), inhibiting the activity of the hypoxia inducible factor (HIF-1alpha) and thereby attenuating the cellular response to low tissue oxygen concentration []. Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators [].Proteins containing this domain also include a group of land-plant specific proteins, know as the BTB/POZ and TAZ domain-containing (BT) protein. The reports of their interaction with CUL3 are contradictory. They are multifunctional scaffold proteins essential for male and female gametophyte development []. The TAZ domain adopts an all-alpha fold with zinc-binding sites in the loops connecting the helices. The TAZ1 domain in P300 and the TAZ2 (CH3) domain in CBP have each been shown to have four amphipathic helices, organised by three zinc-binding clusters with HCCC-type coordination [, , ]. |
|
•
•
•
•
•
|
Publication |
First Author: |
Sewduth RN |
Year: |
2020 |
Journal: |
Circ Res |
Title: |
The Noonan Syndrome Gene Lztr1 Controls Cardiovascular Function by Regulating Vesicular Trafficking. |
Volume: |
126 |
Issue: |
10 |
Pages: |
1379-1393 |
|
•
•
•
•
•
|
Publication |
First Author: |
Huang G |
Year: |
2019 |
Journal: |
PLoS One |
Title: |
Mouse DCUN1D1 (SCCRO) is required for spermatogenetic individualization. |
Volume: |
14 |
Issue: |
1 |
Pages: |
e0209995 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kavarthapu R |
Year: |
2020 |
Journal: |
Front Cell Dev Biol |
Title: |
Linking Phospho-Gonadotropin Regulated Testicular RNA Helicase (GRTH/DDX25) to Histone Ubiquitination and Acetylation Essential for Spermatid Development During Spermiogenesis. |
Volume: |
8 |
|
Pages: |
310 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kaspar JW |
Year: |
2012 |
Journal: |
J Cell Sci |
Title: |
Antioxidant-induced INrf2 (Keap1) tyrosine 85 phosphorylation controls the nuclear export and degradation of the INrf2-Cul3-Rbx1 complex to allow normal Nrf2 activation and repression. |
Volume: |
125 |
Issue: |
Pt 4 |
Pages: |
1027-38 |
|
•
•
•
•
•
|
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: |
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 |
Organism: |
Mus musculus/domesticus |
Length: |
112
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
134
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
95
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Inada S |
Year: |
2004 |
Journal: |
Plant Cell |
Title: |
RPT2 is a signal transducer involved in phototropic response and stomatal opening by association with phototropin 1 in Arabidopsis thaliana. |
Volume: |
16 |
Issue: |
4 |
Pages: |
887-96 |
|
•
•
•
•
•
|
Publication |
First Author: |
Haga K |
Year: |
2005 |
Journal: |
Plant Cell |
Title: |
The Rice COLEOPTILE PHOTOTROPISM1 gene encoding an ortholog of Arabidopsis NPH3 is required for phototropism of coleoptiles and lateral translocation of auxin. |
Volume: |
17 |
Issue: |
1 |
Pages: |
103-15 |
|
•
•
•
•
•
|
Publication |
First Author: |
Holland JJ |
Year: |
2009 |
Journal: |
J Exp Bot |
Title: |
Understanding phototropism: from Darwin to today. |
Volume: |
60 |
Issue: |
7 |
Pages: |
1969-78 |
|
•
•
•
•
•
|
Publication |
First Author: |
Roberts D |
Year: |
2011 |
Journal: |
Plant Cell |
Title: |
Modulation of phototropic responsiveness in Arabidopsis through ubiquitination of phototropin 1 by the CUL3-Ring E3 ubiquitin ligase CRL3(NPH3). |
Volume: |
23 |
Issue: |
10 |
Pages: |
3627-40 |
|
•
•
•
•
•
|
Publication |
First Author: |
Motchoulski A |
Year: |
1999 |
Journal: |
Science |
Title: |
Arabidopsis NPH3: A NPH1 photoreceptor-interacting protein essential for phototropism. |
Volume: |
286 |
Issue: |
5441 |
Pages: |
961-4 |
|
•
•
•
•
•
|
Publication |
First Author: |
Pedmale UV |
Year: |
2007 |
Journal: |
J Biol Chem |
Title: |
Regulation of phototropic signaling in Arabidopsis via phosphorylation state changes in the phototropin 1-interacting protein NPH3. |
Volume: |
282 |
Issue: |
27 |
Pages: |
19992-20001 |
|
•
•
•
•
•
|
Publication |
First Author: |
Inoue S |
Year: |
2008 |
Journal: |
Mol Plant |
Title: |
Leaf positioning of Arabidopsis in response to blue light. |
Volume: |
1 |
Issue: |
1 |
Pages: |
15-26 |
|
•
•
•
•
•
|
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: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
316
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
315
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
329
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
316
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
51
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
100
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Li Y |
Year: |
2010 |
Journal: |
J Biol Chem |
Title: |
Structural basis of dimerization-dependent ubiquitination by the SCF(Fbx4) ubiquitin ligase. |
Volume: |
285 |
Issue: |
18 |
Pages: |
13896-906 |
|
•
•
•
•
•
|
Publication |
First Author: |
Xu M |
Year: |
2015 |
Journal: |
Oncotarget |
Title: |
Atypical ubiquitin E3 ligase complex Skp1-Pam-Fbxo45 controls the core epithelial-to-mesenchymal transition-inducing transcription factors. |
Volume: |
6 |
Issue: |
2 |
Pages: |
979-94 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sakai T |
Year: |
2000 |
Journal: |
Plant Cell |
Title: |
RPT2. A signal transducer of the phototropic response in Arabidopsis. |
Volume: |
12 |
Issue: |
2 |
Pages: |
225-36 |
|
•
•
•
•
•
|
Publication |
First Author: |
Marshall J |
Year: |
2011 |
Journal: |
Adv Exp Med Biol |
Title: |
BTB-Kelch proteins and ubiquitination of kainate receptors. |
Volume: |
717 |
|
Pages: |
115-25 |
|
•
•
•
•
•
|
Publication |
First Author: |
De Guzman RN |
Year: |
2004 |
Journal: |
J Biol Chem |
Title: |
Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: regulation by competition between intrinsically unstructured ligands for non-identical binding sites. |
Volume: |
279 |
Issue: |
4 |
Pages: |
3042-9 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
374
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
374
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
De Guzman RN |
Year: |
2000 |
Journal: |
J Mol Biol |
Title: |
Solution structure of the TAZ2 (CH3) domain of the transcriptional adaptor protein CBP. |
Volume: |
303 |
Issue: |
2 |
Pages: |
243-53 |
|
•
•
•
•
•
|
Publication |
First Author: |
Freedman SJ |
Year: |
2002 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha. |
Volume: |
99 |
Issue: |
8 |
Pages: |
5367-72 |
|
•
•
•
•
•
|
Publication |
First Author: |
Freedman SJ |
Year: |
2003 |
Journal: |
Nat Struct Biol |
Title: |
Structural basis for negative regulation of hypoxia-inducible factor-1alpha by CITED2. |
Volume: |
10 |
Issue: |
7 |
Pages: |
504-12 |
|
•
•
•
•
•
|
Publication |
First Author: |
De Guzman RN |
Year: |
2005 |
Journal: |
Biochemistry |
Title: |
CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding. |
Volume: |
44 |
Issue: |
2 |
Pages: |
490-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Robert HS |
Year: |
2009 |
Journal: |
Plant J |
Title: |
BTB and TAZ domain scaffold proteins perform a crucial function in Arabidopsis development. |
Volume: |
58 |
Issue: |
1 |
Pages: |
109-21 |
|
•
•
•
•
•
|
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 |
Organism: |
Mus musculus/domesticus |
Length: |
222
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Seol JH |
Year: |
2001 |
Journal: |
Nat Cell Biol |
Title: |
Skp1 forms multiple protein complexes, including RAVE, a regulator of V-ATPase assembly. |
Volume: |
3 |
Issue: |
4 |
Pages: |
384-91 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kario E |
Year: |
2005 |
Journal: |
J Biol Chem |
Title: |
Suppressors of cytokine signaling 4 and 5 regulate epidermal growth factor receptor signaling. |
Volume: |
280 |
Issue: |
8 |
Pages: |
7038-48 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
TAZ (Transcription Adaptor putative Zinc finger) domains are zinc-containing domains found in the homologous transcriptional co-activators CREB-binding protein (CBP) and the P300. CBP and P300 are histone acetyltransferases () that catalyse the reversible acetylation of all four histones in nucleosomes, acting to regulate transcription via chromatin remodelling. These large nuclear proteins interact with numerous transcription factors and viral oncoproteins, including p53 tumour suppressor protein, E1A oncoprotein, MyoD, and GATA-1, and are involved in cell growth, differentiation and apoptosis []. Both CBP and P300 have two copies of the TAZ domain, one in the N-terminal region, the other in the C-terminal region. The TAZ1 domain of CBP and P300 forms a complex with CITED2 (CBP/P300-interacting transactivator with ED-rich tail), inhibiting the activity of the hypoxia inducible factor (HIF-1alpha) and thereby attenuating the cellular response to low tissue oxygen concentration []. Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators [].Proteins containing this domain also include a group of land-plant specific proteins, know as the BTB/POZ and TAZ domain-containing (BT) protein. The reports of their interaction with CUL3 are contradictory. They are multifunctional scaffold proteins essential for male and female gametophyte development []. The TAZ domain adopts an all-alpha fold with zinc-binding sites in the loops connecting the helices. The TAZ1 domain in P300 and the TAZ2 (CH3) domain in CBP have each been shown to have four amphipathic helices, organised by three zinc-binding clusters with HCCC-type coordination [, , ].Zinc finger (Znf) domains are relatively small protein motifs which contain multiple finger-like protrusions that make tandem contacts with their target molecule. Some of these domains bind zinc, but many do not; instead binding other metals such as iron, or no metal at all. For example, some family members form salt bridges to stabilise the finger-like folds. They were first identified as a DNA-binding motif in transcription factor TFIIIA from Xenopus laevis (African clawed frog), however they are now recognised to bind DNA, RNA, protein and/or lipid substrates [, , , , ]. Their binding properties depend on the amino acid sequence of the finger domains and of the linker between fingers, as well as on the higher-order structures andthe number of fingers. Znf domains are often found in clusters, where fingers can have different binding specificities. There are many superfamilies of Znf motifs, varying in both sequence and structure. They display considerable versatility in binding modes, even between members of the same class (e.g. some bind DNA, others protein), suggesting that Znf motifs are stable scaffolds that have evolved specialised functions. For example, Znf-containing proteins function in gene transcription, translation, mRNA trafficking, cytoskeleton organisation, epithelial development, cell adhesion, protein folding, chromatin remodelling and zinc sensing, to name but a few []. Zinc-binding motifs are stable structures, and they rarely undergo conformational changes upon binding their target. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
714
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Ponting CP |
Year: |
1996 |
Journal: |
Trends Biochem Sci |
Title: |
ZZ and TAZ: new putative zinc fingers in dystrophin and other proteins. |
Volume: |
21 |
Issue: |
1 |
Pages: |
11-13 |
|
•
•
•
•
•
|
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 |
Organism: |
Mus musculus/domesticus |
Length: |
163
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
163
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
163
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
96
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
107
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
131
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Stemmann O |
Year: |
1996 |
Journal: |
EMBO J |
Title: |
The Saccharomyces cerevisiae kinetochore contains a cyclin-CDK complexing homologue, as identified by in vitro reconstitution. |
Volume: |
15 |
Issue: |
14 |
Pages: |
3611-20 |
|
•
•
•
•
•
|
Pseudogene |
Type: |
pseudogene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
597
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
640
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
604
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
640
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
640
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1589
 |
Fragment?: |
true |
|
•
•
•
•
•
|
Publication |
First Author: |
Stebbins CE |
Year: |
1999 |
Journal: |
Science |
Title: |
Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. |
Volume: |
284 |
Issue: |
5413 |
Pages: |
455-61 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2412
 |
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
2441
 |
Fragment?: |
false |
|
•
•
•
•
•
|