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Search results 201 to 231 out of 231 for Rpn1

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0.018s

Type

Details

Score

Publication

- | J:90438

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2005

Title:	Obtaining and loading genome assembly coordinates from NCBI annotations

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Publication

- | J:144087

First Author:	Mouse Genome Informatics Scientific Curators
Year:	2009
Journal:	Database Download
Title:	Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform

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Protein

Q8VDM4

Organism:	Mus musculus/domesticus
Length:	908
Fragment?:	false

•

Protein

A0A338P6M5

Organism:	Mus musculus/domesticus
Length:	142
Fragment?:	true

•

Publication

1242268 | -

First Author:	Raiti S
Year:	1975
Journal:	Acta Endocrinol (Copenh)
Title:	Critical analysis of methods for estimating production rates of FSH.
Volume:	80
Issue:	2
Pages:	275-83

•

Protein Domain

IPR016643 | 26S_Psome_Rpn1

Type:

Family

Description:

Intracellular proteins, including short-lived proteins such as cyclin, Mos, Myc, p53, NF-kappaB, and IkappaB, are degraded by the ubiquitin-proteasome system. The 26S proteasome is a self-compartmentalising protease responsible for the regulated degradation of intracellular proteins in eukaryotes [, ]. This giant intracellular protease is formed by several subunits arranged into two 19S polar caps, where protein recognition and ATP-dependent unfolding occur, flanking a 20S central barrel-shaped structure with an inner proteolytic chamber. This overall structure is highly conserved among eukaryotes and is essential for cell viability. Proteins targeted to the 26S proteasome are conjugated with a polyubiquitin chain by an enzymatic cascade before delivery to the 26S proteasome for degradation into oligopeptides.The 26S proteasome can be divided into two subcomplexes: the 19S regulatory particle (RP) and the 20S core particle (CP) []. The 19S component is divided into a "base"subunit containing six ATPases (Rpt proteins) and two non-ATPases (Rpn1, Rpn2), and a "lid"subunit composed of eight stoichiometric proteins (Rpn3, Rpn5, Rpn6, Rpn7, Rpn8, Rpn9, Rpn11, Rpn12) []. Additional non-essential and species specific proteins may also be present. The 19S unit performs several essential functions including binding the specific protein substrates, unfolding them, cleaving the attached ubiquitin chains, opening the 20S subunit, and driving the unfolded polypeptide into the proteolytic chamber for degradation. The 26s proteasome and 19S regulator are of medical interest due to their involvement in burn rehabilitation [].This group represents a 26S proteasome regulatory complex, non-ATPase subcomplex, Rpn1 (regulatory-particle non-ATPase subunit 1). This subunit is essential for embryogenesis in Arabidopsis thaliana [].

•

Protein

A0A338P7H4

Organism:	Mus musculus/domesticus
Length:	139
Fragment?:	true

•

Protein

A0A338P6S9

Organism:	Mus musculus/domesticus
Length:	97
Fragment?:	true

•

Protein

Q9CRK7

Organism:	Mus musculus/domesticus
Length:	118
Fragment?:	true

•

Protein

Q99JX8

Organism:	Mus musculus/domesticus
Length:	206
Fragment?:	true

•

Protein

Q80V77

Organism:	Mus musculus/domesticus
Length:	615
Fragment?:	false

•

Protein

Q3TIP0

Organism:	Mus musculus/domesticus
Length:	908
Fragment?:	false

•

Protein

Q3TWL6

Organism:	Mus musculus/domesticus
Length:	908
Fragment?:	false

•

Protein

Q3TXV1

Organism:	Mus musculus/domesticus
Length:	908
Fragment?:	false

•

Protein

Q3TW71

Organism:	Mus musculus/domesticus
Length:	908
Fragment?:	false

•

Protein

Q3TI61

Organism:	Mus musculus/domesticus
Length:	908
Fragment?:	false

•

Protein

Q3U9Y8

Organism:	Mus musculus/domesticus
Length:	908
Fragment?:	false

•

Protein

Q3TKV1

Organism:	Mus musculus/domesticus
Length:	908
Fragment?:	false

•

Publication

15890341 | -

First Author:	Glickman MH
Year:	2005
Journal:	FEBS Lett
Title:	Proteasome plasticity.
Volume:	579
Issue:	15
Pages:	3214-23

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Publication

16566573 | -

First Author:	Tan Y
Year:	2006
Journal:	J Burn Care Res
Title:	Effects of tumor necrosis factor-alpha on the 26S proteasome and 19S regulator in skeletal muscle of severely scalded mice.
Volume:	27
Issue:	2
Pages:	226-33

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Publication

28583440 | -

First Author:	Budenholzer L
Year:	2017
Journal:	J Mol Biol
Title:	Proteasome Structure and Assembly.

•

Publication

15571806 | -

First Author:	Wolf DH
Year:	2004
Journal:	Biochim Biophys Acta
Title:	The proteasome: a proteolytic nanomachine of cell regulation and waste disposal.
Volume:	1695
Issue:	1-3
Pages:	19-31

•

Publication

9741626 | -

First Author:	Glickman MH
Year:	1998
Journal:	Cell
Title:	A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3.
Volume:	94
Issue:	5
Pages:	615-23

•

Publication

27444871 | -

First Author:	Livneh I
Year:	2016
Journal:	Cell Res
Title:	The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death.
Volume:	26
Issue:	8
Pages:	869-85

•

Protein Domain

IPR040892 | RPN1_N

Type:	Domain
Description:	The 26S proteasome is the major ATP-dependent protease in eukaryotes which plays a key role in intracellular protein degradation [, ].This domain is found at the N terminus of the 26S proteasome regulatory subunit RPN1 (also known as 26S proteasome non-ATPase regulatory subunit 2 (PSMD2)) []. The domain is formed by an array of alpha helices [].

•

Protein Domain

IPR041433 | RPN1_C

Type:

Domain

Description:

This is the C-terminal domain found in RPN1 proteins (26S proteasome non-ATPase regulatory subunit 2). The 26S proteasome holocomplex consists of a 28-subunit barrel-shaped core particle (CP) in the centre capped at the top and bottom by 19-subunit regulatory particles (RPs). The CP forms the catalytic chamber and the RP is formed from two subcomplexes known as the lid and the base []. The lid comprises nine Rpn subunits in yeast (Rpn3/5/6/7/8/9/11/12/15) and the base comprises three Rpn subunits (Rpn1/2/13) and six ATPases (Rpt1-6) [].

•

Publication

22405010 | -

First Author:	He J
Year:	2012
Journal:	Structure
Title:	The structure of the 26S proteasome subunit Rpn2 reveals its PC repeat domain as a closed toroid of two concentric α-helical rings.
Volume:	20
Issue:	3
Pages:	513-21

•

Publication

27791164 | -

First Author:	Chen S
Year:	2016
Journal:	Proc Natl Acad Sci U S A
Title:	Structural basis for dynamic regulation of the human 26S proteasome.
Volume:	113
Issue:	46
Pages:	12991-12996

•

Publication

26929360 | -

First Author:	Luan B
Year:	2016
Journal:	Proc Natl Acad Sci U S A
Title:	Structure of an endogenous yeast 26S proteasome reveals two major conformational states.
Volume:	113
Issue:	10
Pages:	2642-7

•

Publication

20471955 | -

First Author:	Fukunaga K
Year:	2010
Journal:	Biochem Biophys Res Commun
Title:	Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae.
Volume:	396
Issue:	4
Pages:	1048-53

•

Publication

27342858 | -

First Author:	Schweitzer A
Year:	2016
Journal:	Proc Natl Acad Sci U S A
Title:	Structure of the human 26S proteasome at a resolution of 3.9 Å.
Volume:	113
Issue:	28
Pages:	7816-21

•

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