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Search results 501 to 600 out of 712 for Ank

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Type Details Score
Protein
Organism: Mus musculus/domesticus
Length: 209  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 360  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 707  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 413  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 86  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 705  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 460  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 771  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 469  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 428  
Fragment?: false
Publication
First Author: Wu L
Year: 2002
Journal: Mol Cell Biol
Title: Identification of a family of mastermind-like transcriptional coactivators for mammalian notch receptors.
Volume: 22
Issue: 21
Pages: 7688-700
Publication
First Author: Harmey D
Year: 2006
Journal: J Bone Miner Res
Title: Elevated skeletal osteopontin levels contribute to the hypophosphatasia phenotype in Akp2(-/-) mice.
Volume: 21
Issue: 9
Pages: 1377-86
Publication
First Author: Hassani Nia F
Year: 2020
Journal: Mol Autism
Title: Targeting of δ-catenin to postsynaptic sites through interaction with the Shank3 N-terminus.
Volume: 11
Issue: 1
Pages: 85
Publication
First Author: Oyhenart J
Year: 2005
Journal: Biol Reprod
Title: Putative homeodomain transcription factor 1 interacts with the feminization factor homolog fem1b in male germ cells.
Volume: 72
Issue: 4
Pages: 780-7
Protein
Organism: Mus musculus/domesticus
Length: 761  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 747  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 111  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 164  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 761  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 489  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 747  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 826  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 585  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 235  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 414  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 680  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 233  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 272  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 443  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 53  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 504  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 500  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 249  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 414  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 708  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 716  
Fragment?: false
Publication
First Author: Oyhenart J
Year: 2003
Journal: Biol Reprod
Title: Phtf1 is an integral membrane protein localized in an endoplasmic reticulum domain in maturing male germ cells.
Volume: 68
Issue: 3
Pages: 1044-53
Publication
First Author: Sullivan A
Year: 2007
Journal: Br J Cancer
Title: ASPP: a new family of oncogenes and tumour suppressor genes.
Volume: 96
Issue: 2
Pages: 196-200
Publication
First Author: Liu Y
Year: 2002
Journal: Mol Biol Cell
Title: The association of ASAP1, an ADP ribosylation factor-GTPase activating protein, with focal adhesion kinase contributes to the process of focal adhesion assembly.
Volume: 13
Issue: 6
Pages: 2147-56
Publication
First Author: Fryer CJ
Year: 2002
Journal: Genes Dev
Title: Mastermind mediates chromatin-specific transcription and turnover of the Notch enhancer complex.
Volume: 16
Issue: 11
Pages: 1397-411
Protein Domain
Type: Homologous_superfamily
Description: This entry represents the N-terminal domain found in a family of neurogenic mastermind-like proteins (MAMLs), which act as critical transcriptional co-activators for Notch signaling [, , ]. Notch receptors are cleaved upon ligand engagement and the intracellular domain of Notch shuttles to the nucleus. MAMLs form a functional DNA-binding complex with the cleaved Notch receptor and the transcription factor CSL, thereby regulating transcriptional events that are specific to the Notch pathway. MAML proteins may also play roles as key transcriptional co-activators in other signal transduction pathways as well, including: muscle differentiation and myopathies (MEF2C) [], tumour suppressor pathway (p53) []and colon carcinoma survival (beta-catenin) []. MAML proteins could mediate cross-talk among the various signaling pathways and the diverse activities of the MAML proteins converge to impact normal biological processes and human diseases, including cancers.The N-terminal domain of MAML proteins adopt an elongated kinked helix that wraps around ANK and CSL forming one of the complexes in the build-up of the Notch transcriptional complex for recruiting general transcription factors []. This N-terminal domain is responsible for its interaction with the ankyrin repeat region of the Notch proteins NOTCH1 [], NOTCH2 [], NOTCH3 []and NOTCH4. It forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1, and also binds CREBBP/CBP []and CDK8 []. The C-terminal region is required for transcriptional activation.
Protein Domain
Type: Family
Description: This family includes the neurogenic mastermind-like proteins 1-3 (MAML1-3) from chordates, which act as critical transcriptional co-activators for Notch signaling [, ]. Notch receptors are cleaved upon ligand engagement and the intracellular domain of Notch shuttles to the nucleus. MAMLs form a functional DNA-binding complex with the cleaved Notch receptor and the transcription factor CSL, thereby regulating transcriptional events that are specific to the Notch pathway. MAML proteins may also play roles as key transcriptional co-activators in other signal transduction pathways as well, including: muscle differentiation and myopathies (MEF2C) [], tumour suppressor pathway (p53) []and colon carcinoma survival (beta-catenin) []. MAML proteins could mediate cross-talk among the various signaling pathways and the diverse activities of the MAML proteins converge to impact normal biological processes and human diseases, including cancers.They consist of an N-terminal domain which adopt an elongated kinked helix that wraps around ANK and CSL forming one of the complexes in the build-up of the Notch transcriptional complex for recruiting general transcription factors [, ]]. This N-terminal domain is responsible for its interaction with the ankyrin repeat region of the Notch proteins NOTCH1 [], NOTCH2 [], NOTCH3 []and NOTCH4. It forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1, and also binds CREBBP/CBP []and CDK8 []. The C-terminal region is required for transcriptional activation.
Protein Domain
Type: Domain
Description: This entry represents the N-terminal domain found in a family of neurogenic mastermind-like proteins (MAMLs), which act as critical transcriptional co-activators for Notch signaling [, , ]. Notch receptors are cleaved upon ligand engagement and the intracellular domain of Notch shuttles to the nucleus. MAMLs form a functional DNA-binding complex with the cleaved Notch receptor and the transcription factor CSL, thereby regulating transcriptional events that are specific to the Notch pathway. MAML proteins may also play roles as key transcriptional co-activators in other signal transduction pathways as well, including: muscle differentiation and myopathies (MEF2C) [], tumour suppressor pathway (p53) []and colon carcinoma survival (beta-catenin) []. MAML proteins could mediate cross-talk among the various signaling pathways and the diverse activities of the MAML proteins converge to impact normal biological processes and human diseases, including cancers.The N-terminal domain of MAML proteins adopt an elongated kinked helix that wraps around ANK and CSL forming one of the complexes in the build-up of the Notch transcriptional complex for recruiting general transcription factors []. This N-terminal domain is responsible for its interaction with the ankyrin repeat region of the Notch proteins NOTCH1 [], NOTCH2 [], NOTCH3 []and NOTCH4. It forms a DNA-binding complex with Notch proteins and RBPSUH/RBP-J kappa/CBF1, and also binds CREBBP/CBP []and CDK8 []. The C-terminal region is required for transcriptional activation.
Protein Domain
Type: Domain
Description: This domain is found in a group of homeodomain containing proteins from animals, including PHTF1/2, and is typically between 101 and 140 amino acids in length. PHTF proteins do not display any sequence similarity to known or predicted proteins, but their conservation among species suggests an essential function. The 84kDa Phtf1 protein is an integral membrane protein, anchored to a cell membrane by six to eight trans-membrane domains, that is associated with a domain of the endoplasmic reticulum (ER) juxtaposed to the Golgi apparatus. It is present during meiosis and spermiogenesis, and, by the end of spermiogenesis, is released from the mature spermatozoon within the residual bodies []. PHTF1 enhances the binding of FEM1B -feminisation homologue 1B - to cell membranes. Fem-1 was initially identified in the signaling pathway for sex determination, as well as being implicated in apoptosis, but its biochemical role is still unclear, and neither FEM1B nor PHTF1 is directly implicated in apoptosis in spermatogenesis. It is the ANK domain of FEM1B that is necessary for the interaction with the N-terminal region of PHTF1 [].
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 319  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 437  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 464  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 453  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 319  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 250  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 278  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 432  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 285  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 468  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 468  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 466  
Fragment?: false
Publication
First Author: Chen C
Year: 2017
Journal: Nature
Title: IL-17 is a neuromodulator of Caenorhabditis elegans sensory responses.
Volume: 542
Issue: 7639
Pages: 43-48
Publication
First Author: Kazdoba TM
Year: 2016
Journal: Genes Brain Behav
Title: Behavioral phenotypes of genetic mouse models of autism.
Volume: 15
Issue: 1
Pages: 7-26
Protein
Organism: Mus musculus/domesticus
Length: 266  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 291  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 254  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 144  
Fragment?: true
Protein
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 286  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 950  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 410  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 535  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 930  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 480  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 621  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 598  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 573  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1042  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 551  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 245  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 361  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 1042  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 909  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 389  
Fragment?: false
Protein
Organism: Mus musculus/domesticus
Length: 953  
Fragment?: false