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Search results 401 to 500 out of 712 for Ank

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Type Details Score
Publication
22244744 | J:182766
First Author: Li F
Year: 2012
Journal: Gene
Title: Putative function of TAP63α during endochondral bone formation.
Volume: 495
Issue: 2
Pages: 95-103
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Protein
D6RHP0
Organism: Mus musculus/domesticus
Length: 117  
Fragment?: false
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Publication
8706131 | -
First Author: Bai C
Year: 1996
Journal: Cell
Title: SKP1 connects cell cycle regulators to the ubiquitin proteolysis machinery through a novel motif, the F-box.
Volume: 86
Issue: 2
Pages: 263-74
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Publication
10581972 | -
First Author: Craig KL
Year: 1999
Journal: Prog Biophys Mol Biol
Title: The F-box: a new motif for ubiquitin dependent proteolysis in cell cycle regulation and signal transduction.
Volume: 72
Issue: 3
Pages: 299-328
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Protein
Q9D2Y6
Organism: Mus musculus/domesticus
Length: 357  
Fragment?: false
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Protein
Q9CPU7
Organism: Mus musculus/domesticus
Length: 355  
Fragment?: false
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Protein
Q9JJB9
Organism: Mus musculus/domesticus
Length: 375  
Fragment?: false
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Protein
Q3UYF5
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: false
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Protein
A0A1B0GSB9
Organism: Mus musculus/domesticus
Length: 201  
Fragment?: true
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Protein
A0A1B0GRC8
Organism: Mus musculus/domesticus
Length: 365  
Fragment?: false
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Publication
28085133 | -
 
First Author: Pearson JS
Year: 2017
Journal: Nat Microbiol
Title: EspL is a bacterial cysteine protease effector that cleaves RHIM proteins to block necroptosis and inflammation.
Volume: 2
Pages: 16258
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Publication
10336463 | -
First Author: Yang JP
Year: 1999
Journal: J Biol Chem
Title: Identification of a novel inhibitor of nuclear factor-kappaB, RelA-associated inhibitor.
Volume: 274
Issue: 22
Pages: 15662-70
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Publication
19805144 | J:153680
First Author: Sobotzik JM
Year: 2009
Journal: Proc Natl Acad Sci U S A
Title: AnkyrinG is required to maintain axo-dendritic polarity in vivo.
Volume: 106
Issue: 41
Pages: 17564-9
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Publication
19088739 | -
First Author: Schulze TG
Year: 2009
Journal: Mol Psychiatry
Title: Two variants in Ankyrin 3 (ANK3) are independent genetic risk factors for bipolar disorder.
Volume: 14
Issue: 5
Pages: 487-91
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Publication
16775201 | -
First Author: Shirahata E
Year: 2006
Journal: J Neurophysiol
Title: Ankyrin-G regulates inactivation gating of the neuronal sodium channel, Nav1.6.
Volume: 96
Issue: 3
Pages: 1347-57
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Publication
20616497 | -
 
First Author: Pinto EM
Year: 2010
Journal: Front Horm Res
Title: iASPP: a novel protein involved in pituitary tumorigenesis?
Volume: 38
Pages: 70-76
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Publication
22538442 | -
First Author: Cai Y
Year: 2012
Journal: Apoptosis
Title: iASPP inhibits p53-independent apoptosis by inhibiting transcriptional activity of p63/p73 on promoters of proapoptotic genes.
Volume: 17
Issue: 8
Pages: 777-83
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Publication
21926165 | -
First Author: Jiang L
Year: 2011
Journal: Clin Cancer Res
Title: iASPP and chemoresistance in ovarian cancers: effects on paclitaxel-mediated mitotic catastrophe.
Volume: 17
Issue: 21
Pages: 6924-33
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Publication
21930934 | J:177360
First Author: Notari M
Year: 2011
Journal: Proc Natl Acad Sci U S A
Title: Inhibitor of apoptosis-stimulating protein of p53 (iASPP) prevents senescence and is required for epithelial stratification.
Volume: 108
Issue: 40
Pages: 16645-50
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Publication
16964264 | -
First Author: Bergamaschi D
Year: 2006
Journal: Nat Genet
Title: iASPP preferentially binds p53 proline-rich region and modulates apoptotic function of codon 72-polymorphic p53.
Volume: 38
Issue: 10
Pages: 1133-41
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Publication
15607367 | -
First Author: Zhang X
Year: 2005
Journal: Leuk Res
Title: The expression of iASPP in acute leukemias.
Volume: 29
Issue: 2
Pages: 179-83
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Publication
12524540 | -
First Author: Bergamaschi D
Year: 2003
Journal: Nat Genet
Title: iASPP oncoprotein is a key inhibitor of p53 conserved from worm to human.
Volume: 33
Issue: 2
Pages: 162-7
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Protein Domain
IPR028320 | iASPP
Type: Family
Description: This entry represents RelA-associated inhibitor (also known as iASPP), which is a regulator that plays acentral role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins []. iASPP is an ankyrin-repeat-, SH3-domain- and proline-rich-region-containing proteins that is homologous with ASPP1 and ASPP2 (). The ASPPs proteins regulate the apoptotic function of p53; iASPP inhibits p53, whereas ASPP1 and ASPP2 activates p53 []. The p53 tumour suppressor gene is one of the most frequently mutated genes in human cancer that can suppress tumour growth through its ability to induce apoptosis or cell-cycle arrest. Therefore, the ASPP family of proteins may be a novel target for cancer therapy []. This entry also includes ANK repeat-containing protein nipk-1 from the nematode Caenorhabditis elegans, which has been shown to mediate signaling of the receptor complex composed of ilcr-1 and ilcr-2. This complex acts directly on neurons, altering their response properties, modifying behaviour and is the receptor for interleukin-17 [].
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Protein Domain
IPR037971 | Ank3_Death
Type: Domain
Description: ANK-3, also called anykyrin-G (for general or giant), is found in neurons and at least one splice variant has been shown to be essential for propagation of action potentials as a binding partner to neurofascin and voltage-gated sodium channels []. It is required for maintaining axo-dendritic polarity [], and may be a genetic risk factor associated with bipolar disorder []. ANK-3 contains an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal Death domain. This entry represents the Death domain of ANK-3. DDs (Death domains) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes [, ].
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Protein Domain
IPR012927 | Toxin_15_N
Type: Domain
Description: This domain is present in the N-terminal region of the ShET2 enterotoxin produced by Shigella flexneri () and Escherichia coli (). This protein was found to confer toxigenicity in Ussing chamber assays, and the N-terminal region was found to be important for its enterotoxic effect. The N-terminal domain is a cysteine-type peptidase with a Cys/His/Asp catalytic triad that cleaves within the receptor-interacting protein homotypic interaction motifs found within host adaptor proteins such as receptor-interacting serine/threonine protein kinases RIPK1 and RIPK3, TIR-domain-containing adapter-inducing interferon beta and Z-DNA-binding protein 1, inactivating them and thus inhibiting necroptosis and inflammatory signalling []. The toxin is injected into the host cell by the type III secretion system [].Most proteins containing this domain are annotated as putative enterotoxins, but one member () is a regulator of acetyl CoA synthetase, and another two members (and ) are annotated as ankyrin-like regulatory proteins and contain Ank repeats ().
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Protein Domain
IPR042722 | SH3_iASPP
Type: Domain
Description: RelA-associated inhibitor, also known as iASPP, is an oncoprotein that inhibits the apoptotic transactivation potential of p53 [, , ]. It is upregulated in human breast cancers expressing wild-type p53 [], in acute leukemias regardless of the p53 mutation status [], as well as in ovarian cancer where it is associated with poor patient outcome and chemoresistance []. iASPP is also a binding partner and negative regulator of p65RelA, which promotes cell proliferation and inhibits apoptosis; p65RelA has the opposite effect on cell growth compared to the p53 family []. It contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of iASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53.This entry represents the SH3 domain found in iASPP.
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Protein Domain
IPR039752 | F-box_only
Type: Family
Description: Proteins in this entry contain an N-terminal F-box and a C-terminal F-box associated (FBA) domain. The F-box is a conserved domain that is present in numerous proteins with a bipartite structure []. Through the F-box, these proteins are linked to the Skp1 protein and the core of SCFs (Skp1-cullin-F-box protein ligase) complexes. SCFs complexes constitute a new class of E3 ligases []. They function in combination with the E2 enzyme Cdc34 to ubiquitinate G1 cyclins, Cdk inhibitors and many other proteins, to mark them for degradation. The binding of the specific substrates by SCFs complexes is mediated by divergent protein-protein interaction motifs present in F-box proteins, like WD40 repeats, leucine rich repeats [, ]or ANK repeats.
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Protein
Q78JE5
Organism: Mus musculus/domesticus
Length: 402  
Fragment?: false
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Protein
Q8CAT8
Organism: Mus musculus/domesticus
Length: 161  
Fragment?: false
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Protein
Q3UGI9
Organism: Mus musculus/domesticus
Length: 442  
Fragment?: false
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Protein
Q3V305
Organism: Mus musculus/domesticus
Length: 257  
Fragment?: false
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Protein
Q3TBA5
Organism: Mus musculus/domesticus
Length: 303  
Fragment?: false
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Protein
B0LAC4
Organism: Mus musculus/domesticus
Length: 146  
Fragment?: true
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Protein
Q3UD93
Organism: Mus musculus/domesticus
Length: 444  
Fragment?: false
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Protein Domain
IPR037844 | PH_ASAP
Type: Domain
Description: This entry represents the PH domain of Arf-GAP with SH3 domain, ANK repeat and PH domain-containing proteins (ASAPs). ASAPs (ASAP1, ASAP2, and ASAP3) function as Arf-specific GTPase-activating proteins (GAPs), participate in rhodopsin trafficking, are associated with tumour cell metastasis, modulate phagocytosis, promote cell proliferation, facilitate vesicle budding, Golgi exocytosis, and regulate vesicle coat assembly via a Bin/Amphiphysin/Rvs domain [, , ]. Each member has a BAR, PH, Arf GAP, Ank repeat and proline rich domains. ASAP1 and ASAP2 also have a SH3 domain at the C terminus []. The ASAP family is named for the first identified member, ASAP1 [].PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner []. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity []. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane []. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes [].
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Publication
12040005 | J:76876
First Author: Yan W
Year: 2002
Journal: Mol Endocrinol
Title: Identification of Gasz, an evolutionarily conserved gene expressed exclusively in germ cells and encoding a protein with four ankyrin repeats, a sterile-alpha motif, and a basic leucine zipper.
Volume: 16
Issue: 6
Pages: 1168-84
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Publication
11796721 | J:75889
First Author: Gagelin C
Year: 2002
Journal: J Biol Chem
Title: Identification of Ank(G107), a muscle-specific ankyrin-G isoform.
Volume: 277
Issue: 15
Pages: 12978-87
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Publication
15939934 | J:99443
First Author: Estève PO
Year: 2005
Journal: Nucleic Acids Res
Title: Functional analysis of the N- and C-terminus of mammalian G9a histone H3 methyltransferase.
Volume: 33
Issue: 10
Pages: 3211-23
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Publication
20601283 | J:165160
First Author: Kim HJ
Year: 2010
Journal: Bone
Title: The role of pyrophosphate/phosphate homeostasis in terminal differentiation and apoptosis of growth plate chondrocytes.
Volume: 47
Issue: 3
Pages: 657-65
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Publication
23583105 | J:197901
First Author: Jiang YH
Year: 2013
Journal: Neuron
Title: Modeling autism by SHANK gene mutations in mice.
Volume: 78
Issue: 1
Pages: 8-27
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Protein
Q9QZN4
Organism: Mus musculus/domesticus
Length: 295  
Fragment?: false
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Protein
Q6DIA9
Organism: Mus musculus/domesticus
Length: 280  
Fragment?: false
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Protein
Q8BK26
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: false
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Protein
Q80UW2
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
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Protein
Q9QZM8
Organism: Mus musculus/domesticus
Length: 286  
Fragment?: false
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Protein
Q6T264
Organism: Mus musculus/domesticus
Length: 1020  
Fragment?: false
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Protein
G3UYF5
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: false
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Protein
A2A7H5
Organism: Mus musculus/domesticus
Length: 255  
Fragment?: false
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Protein
D4QGC2
Organism: Mus musculus/domesticus
Length: 1135  
Fragment?: false
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Protein
A2A7H1
Organism: Mus musculus/domesticus
Length: 237  
Fragment?: true
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Protein
Q3V064
Organism: Mus musculus/domesticus
Length: 286  
Fragment?: false
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Protein
E9PUJ0
Organism: Mus musculus/domesticus
Length: 218  
Fragment?: false
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Protein
A2A7H6
Organism: Mus musculus/domesticus
Length: 224  
Fragment?: false
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Protein
A2A7H4
Organism: Mus musculus/domesticus
Length: 232  
Fragment?: true
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Protein
G3UY69
Organism: Mus musculus/domesticus
Length: 133  
Fragment?: false
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Protein
A2A7G9
Organism: Mus musculus/domesticus
Length: 228  
Fragment?: true
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Protein
G3UZT3
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: true
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Protein
Q7TPU6
Organism: Mus musculus/domesticus
Length: 739  
Fragment?: false
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Protein
F6U238
Organism: Mus musculus/domesticus
Length: 1170  
Fragment?: false
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Protein
Q3USR5
Organism: Mus musculus/domesticus
Length: 297  
Fragment?: false
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Protein
Z4YN00
Organism: Mus musculus/domesticus
Length: 265  
Fragment?: true
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Publication
9346238 | -
First Author: Skowyra D
Year: 1997
Journal: Cell
Title: F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex.
Volume: 91
Issue: 2
Pages: 209-19
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Publication
16530044 | -
First Author: Nam Y
Year: 2006
Journal: Cell
Title: Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes.
Volume: 124
Issue: 5
Pages: 973-83
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Publication
18758478 | -
First Author: Kovall RA
Year: 2008
Journal: Oncogene
Title: More complicated than it looks: assembly of Notch pathway transcription complexes.
Volume: 27
Issue: 38
Pages: 5099-109
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Publication
18758483 | J:141198
First Author: McElhinny AS
Year: 2008
Journal: Oncogene
Title: Mastermind-like transcriptional co-activators: emerging roles in regulating cross talk among multiple signaling pathways.
Volume: 27
Issue: 38
Pages: 5138-47
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Publication
16510869 | J:106711
First Author: Shen H
Year: 2006
Journal: Genes Dev
Title: The Notch coactivator, MAML1, functions as a novel coactivator for MEF2C-mediated transcription and is required for normal myogenesis.
Volume: 20
Issue: 6
Pages: 675-88
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Publication
17317671 | -
First Author: Zhao Y
Year: 2007
Journal: J Biol Chem
Title: The notch regulator MAML1 interacts with p53 and functions as a coactivator.
Volume: 282
Issue: 16
Pages: 11969-81
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Publication
17875709 | -
First Author: Alves-Guerra MC
Year: 2007
Journal: Cancer Res
Title: Mastermind-like 1 Is a specific coactivator of beta-catenin transcription activation and is essential for colon carcinoma cell survival.
Volume: 67
Issue: 18
Pages: 8690-8
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Publication
16880534 | -
First Author: Chiang MY
Year: 2006
Journal: Mol Cell Biol
Title: Identification of a conserved negative regulatory sequence that influences the leukemogenic activity of NOTCH1.
Volume: 26
Issue: 16
Pages: 6261-71
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Publication
17699740 | J:149110
First Author: Wu L
Year: 2007
Journal: Blood
Title: The transcriptional coactivator Maml1 is required for Notch2-mediated marginal zone B-cell development.
Volume: 110
Issue: 10
Pages: 3618-23
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Publication
19150886 | -
First Author: Liu H
Year: 2009
Journal: Circ Res
Title: NOTCH3 expression is induced in mural cells through an autoregulatory loop that requires endothelial-expressed JAGGED1.
Volume: 104
Issue: 4
Pages: 466-75
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Publication
15961999 | -
First Author: Wu L
Year: 2005
Journal: EMBO J
Title: Transforming activity of MECT1-MAML2 fusion oncoprotein is mediated by constitutive CREB activation.
Volume: 24
Issue: 13
Pages: 2391-402
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Publication
15546612 | -
First Author: Fryer CJ
Year: 2004
Journal: Mol Cell
Title: Mastermind recruits CycC:CDK8 to phosphorylate the Notch ICD and coordinate activation with turnover.
Volume: 16
Issue: 4
Pages: 509-20
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Protein
Q7TSG3
Organism: Mus musculus/domesticus
Length: 421  
Fragment?: false
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Protein
Q3TQF0
Organism: Mus musculus/domesticus
Length: 507  
Fragment?: false
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Protein
Q9EPX5
Organism: Mus musculus/domesticus
Length: 326  
Fragment?: false
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Protein
Q8CHQ0
Organism: Mus musculus/domesticus
Length: 385  
Fragment?: false
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Protein
Q8BFZ4
Organism: Mus musculus/domesticus
Length: 434  
Fragment?: false
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Protein
Q8C4V4
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
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Protein
Q3U7U3
Organism: Mus musculus/domesticus
Length: 523  
Fragment?: false
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Protein
Q6NS60
Organism: Mus musculus/domesticus
Length: 873  
Fragment?: false
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Protein
Q8VDH1
Organism: Mus musculus/domesticus
Length: 627  
Fragment?: false
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Protein
Q6PDJ6
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
Q8VE08
Organism: Mus musculus/domesticus
Length: 562  
Fragment?: false
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Protein
Q5NBU5
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: false
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Protein
Q8CIG9
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
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Protein
Q8BMI0
Organism: Mus musculus/domesticus
Length: 1194  
Fragment?: false
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Protein
Q3U4A0
Organism: Mus musculus/domesticus
Length: 707  
Fragment?: false
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Protein
Q3TBJ0
Organism: Mus musculus/domesticus
Length: 613  
Fragment?: true
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Protein
Q8C2W8
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
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Protein
Q3UGY7
Organism: Mus musculus/domesticus
Length: 873  
Fragment?: false
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Protein
Q4FZL9
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
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Protein
Q3TD55
Organism: Mus musculus/domesticus
Length: 374  
Fragment?: false
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Protein
A4VCH8
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: true
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Protein
D3YWZ0
Organism: Mus musculus/domesticus
Length: 177  
Fragment?: true
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Protein
Q3TNG8
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: false
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Protein
Q3UA61
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: false
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Protein
A2A533
Organism: Mus musculus/domesticus
Length: 110  
Fragment?: true
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Protein
A0A0R4J1M5
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: false
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Protein
A0A1D5RMG0
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: true
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

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Cambridge CB2 3EH, United Kingdom