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Search results 201 to 222 out of 222 for Upf2

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0.018s

Type

Details

Score

Publication

25744026 | J:258608

First Author:	Jia J
Year:	2015
Journal:	Cell Death Differ
Title:	Caspases shutdown nonsense-mediated mRNA decay during apoptosis.
Volume:	22
Issue:	11
Pages:	1754-63

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Publication

11163187 | -

First Author:	Lykke-Andersen J
Year:	2000
Journal:	Cell
Title:	Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon.
Volume:	103
Issue:	7
Pages:	1121-31

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Protein

Q9CUH6

Organism:	Mus musculus/domesticus
Length:	248
Fragment?:	true

•

Protein

Q8CCF7

Organism:	Mus musculus/domesticus
Length:	216
Fragment?:	false

•

Protein

Q9CTQ4

Organism:	Mus musculus/domesticus
Length:	155
Fragment?:	true

•

Protein

Q80UI8

Organism:	Mus musculus/domesticus
Length:	388
Fragment?:	true

•

Protein

Q9CS15

Organism:	Mus musculus/domesticus
Length:	232
Fragment?:	true

•

Protein

Q149I6

Organism:	Mus musculus/domesticus
Length:	248
Fragment?:	false

•

Protein

Q3ULL6

Organism:	Mus musculus/domesticus
Length:	472
Fragment?:	false

•

Protein

Q3ULJ3

Organism:	Mus musculus/domesticus
Length:	422
Fragment?:	false

•

Protein

Q9EPU0

Organism:	Mus musculus/domesticus
Length:	1124
Fragment?:	false

•

Protein

F6Q3G7

Organism:	Mus musculus/domesticus
Length:	523
Fragment?:	true

•

HT Experiment

GSE162556 | Mutations in distinct translation-dependent quality control pathways lead to convergent molecular pathogenesis and neurodevelopmental defects.


Experiment Type:	RNA-Seq
Study Type:	WT vs. Mutant
Source:	GEO

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Publication

11545740 | -

First Author:	Mazza C
Year:	2001
Journal:	Mol Cell
Title:	Crystal structure of the human nuclear cap binding complex.
Volume:	8
Issue:	2
Pages:	383-96

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Publication

16043498 | -

First Author:	Worch R
Year:	2005
Journal:	RNA
Title:	Specificity of recognition of mRNA 5' cap by human nuclear cap-binding complex.
Volume:	11
Issue:	9
Pages:	1355-63

•

Publication

16156639 | -

First Author:	Marintchev A
Year:	2005
Journal:	Biochemistry
Title:	eIF4G and CBP80 share a common origin and similar domain organization: implications for the structure and function of eIF4G.
Volume:	44
Issue:	37
Pages:	12265-72

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Protein Domain

IPR015174 | MIF4G-like_typ-2

Type:

Domain

Description:

This entry represents an MIF4G-like domain. MIF4G domains share a common structure but can differ in sequence. This entry is designated "type 2", and is found in nuclear cap-binding proteins and eIF4G.The MIF4G domain is a structural motif with an ARM (Armadillo) repeat-type fold, consisting of a 2-layer alpha/alpha right-handed superhelix. Proteins usually contain two or more structurally similar MIF4G domains connected by unstructured linkers. MIF4G domains are found in several proteins involved in RNA metabolism, including eIF4G (eukaryotic initiation factor 4-gamma), eIF-2b (translation initiation factor), UPF2 (regulator of nonsense transcripts 2), and nuclear cap-binding proteins (CBP80, CBC1, NCBP1), although the sequence identity between them may be low []. The nuclear cap-binding complex (CBC) is a heterodimer. Human CBC consists of a large CBP80 subunit and a small CBP20 subunit, the latter being critical for cap binding. CBP80 contains three MIF4G domains connected with long linkers, while CBP20 has an RNP (ribonucleoprotein)-type domain that associates with domains 2 and 3 of CBP80 []. The complex binds to 5'-cap of eukaryotic RNA polymerase II transcripts, such as mRNA and U snRNA. The binding is important for several mRNA nuclear maturation steps and for nonsense-mediated decay. It is also essential for nuclear export of U snRNAs in metazoans []. Eukaryotic translation initiation factor 4 gamma (eIF4G) plays a critical role in protein expression, and is at the centre of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex, which scans along the mRNA to the translation start codon. The activity of eIF4G in translation initiation could be regulated through intra- and inter-protein interactions involving the ARM repeats []. In eIF4G, the MIF4G domain binds eIF4A, eIF3, RNA and DNA.

•

Protein Domain

IPR015172 | MIF4G-like_typ-1

Type:

Domain

Description:

This entry represents an MIF4G-like domain. MIF4G domains share a common structure but can differ in sequence. This entry is designated "type 1", and is found in nuclear cap-binding proteins and eIF4G.The MIF4G domain is a structural motif with an ARM (Armadillo) repeat-type fold, consisting of a 2-layer alpha/alpha right-handed superhelix. Proteins usually contain two or more structurally similar MIF4G domains connected by unstructured linkers. MIF4G domains are found in several proteins involved in RNA metabolism, including eIF4G (eukaryotic initiation factor 4-gamma), eIF-2b (translation initiation factor), UPF2 (regulator of nonsense transcripts 2), and nuclear cap-binding proteins (CBP80, CBC1, NCBP1), although the sequence identity between them may be low []. The nuclear cap-binding complex (CBC) is a heterodimer. Human CBC consists of a large CBP80 subunit and a small CBP20 subunit, the latter being critical for cap binding. CBP80 contains three MIF4G domains connected with long linkers, while CBP20 has an RNP (ribonucleoprotein)-type domain that associates with domains 2 and 3 of CBP80 []. The complex binds to 5'-cap of eukaryotic RNA polymerase II transcripts, such as mRNA and U snRNA. The binding is important for several mRNA nuclear maturation steps and for nonsense-mediated decay. It is also essential for nuclear export of U snRNAs in metazoans []. Eukaryotic translation initiation factor 4 gamma (eIF4G) plays a critical role in protein expression, and is at the centre of a complex regulatory network. Together with the cap-binding protein eIF4E, it recruits the small ribosomal subunit to the 5'-end of mRNA and promotes the assembly of a functional translation initiation complex, which scans along the mRNA to the translation start codon. The activity of eIF4G in translation initiation could be regulated through intra- and inter-protein interactions involving the ARM repeats []. In eIF4G, the MIF4G domain binds eIF4A, eIF3, RNA and DNA.

•

Protein

Q3UYV9

Organism:	Mus musculus/domesticus
Length:	790
Fragment?:	false

•

Publication

10958635 | -

First Author:	Aravind L
Year:	2000
Journal:	Genome Res
Title:	Eukaryote-specific domains in translation initiation factors: implications for translation regulation and evolution of the translation system.
Volume:	10
Issue:	8
Pages:	1172-84

•

Protein

Q3TLK3

Organism:	Mus musculus/domesticus
Length:	417
Fragment?:	false

•

Publication

15489334 | -

First Author:	Gerhard DS
Year:	2004
Journal:	Genome Res
Title:	The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Volume:	14
Issue:	10B
Pages:	2121-7

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