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Search results 101 to 140 out of 140 for Vps13b

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0.019s

Type

Details

Score

Protein

A1ILI1

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

•

Protein

A0A494B9C3

Organism:	Mus musculus/domesticus
Length:	148
Fragment?:	true

•

Protein

Q570Z6

Organism:	Mus musculus/domesticus
Length:	1510
Fragment?:	true

•

Protein

B2KF50

Organism:	Mus musculus/domesticus
Length:	1429
Fragment?:	false

•

Protein

A0A3B2WCQ2

Organism:	Mus musculus/domesticus
Length:	177
Fragment?:	true

•

Protein

A0A1L1SUY8

Organism:	Mus musculus/domesticus
Length:	771
Fragment?:	false

•

Protein

A1ILI2

Organism:	Mus musculus/domesticus
Length:	147
Fragment?:	true

•

Publication

9314526 | -

First Author:	Brickner JH
Year:	1997
Journal:	J Cell Biol
Title:	SOI1 encodes a novel, conserved protein that promotes TGN-endosomal cycling of Kex2p and other membrane proteins by modulating the function of two TGN localization signals.
Volume:	139
Issue:	1
Pages:	23-36

•

Publication

22442115 | -

First Author:	Park JS
Year:	2012
Journal:	J Cell Sci
Title:	VPS13 regulates membrane morphogenesis during sporulation in Saccharomyces cerevisiae.
Volume:	125
Issue:	Pt 12
Pages:	3004-11

•

Publication

32690699 | -

First Author:	Chen S
Year:	2020
Journal:	Proc Natl Acad Sci U S A
Title:	Vps13 is required for the packaging of the ER into autophagosomes during ER-phagy.
Volume:	117
Issue:	31
Pages:	18530-18539

•

Publication

15498460 | -

First Author:	Velayos-Baeza A
Year:	2004
Journal:	Genomics
Title:	Analysis of the human VPS13 gene family.
Volume:	84
Issue:	3
Pages:	536-49

•

Publication

30952800 | -

First Author:	Valverde DP
Year:	2019
Journal:	J Cell Biol
Title:	ATG2 transports lipids to promote autophagosome biogenesis.
Volume:	218
Issue:	6
Pages:	1787-1798

•

Protein Domain

IPR031646 | VPS13_N2

Type:

Domain

Description:

This domain lies towards the N terminus, just downstream from . This domain is involved in lipid binding and transport [, , ]. This domain specifically interacts with phosphatidic acid and phosphorylated forms of phosphatidyl inositol [].VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].

•

Protein Domain

IPR031645 | VPS13_DH-like

Type:

Domain

Description:

This entry represents a domain reminiscent of a DH domain (DH-Like domain) found adjacent the C-terminal PH-like domain of VPS13 proteins [, , , ]. DHL-PH domains has been identified as the mitochondria-binding region of VPS13A and the lipid droplet-binding region of both proteins. These two domains contain a region of high similarity to ATG2, which also binds lipid droplets [, ].VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].

•

Protein Domain

IPR031642 | VPS13_mid_rpt

Type:

Domain

Description:

This entry represents the repeating region of VPS13. This repeating region shares a common core element that includes a well-conserved P-X4-P-X13-17-G sequence [, ]. This region contains a FFAT motif which mediates VAMP binding and tethering of the ER.VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].

•

Protein Domain

IPR026854 | VPS13-like_N

Type:

Domain

Description:

This is the N-terminal chorein domain of VPS13 and ATG2 proteins, which is highly conserved. ATG2 proteins are involved in autophagosome assembly, playing a key role in nonvesicular lipid transfer [, , , ]. This domain has a scoop shape whose concave surface is lined by hydrophobic residues which bind glycerophospholipids.VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].

•

Protein

A0A286YCT3

Organism:	Mus musculus/domesticus
Length:	2339
Fragment?:	false

•

Publication

30018089 | -

First Author:	Bean BDM
Year:	2018
Journal:	J Cell Biol
Title:	Competitive organelle-specific adaptors recruit Vps13 to membrane contact sites.
Volume:	217
Issue:	10
Pages:	3593-3607

•

Publication

34216812 | -

First Author:	Leonzino M
Year:	2021
Journal:	Biochim Biophys Acta Mol Cell Biol Lipids
Title:	Insights into VPS13 properties and function reveal a new mechanism of eukaryotic lipid transport.
Volume:	1866
Issue:	10
Pages:	159003

•

Protein

Q8BX70

Organism:	Mus musculus/domesticus
Length:	3748
Fragment?:	false

•

Protein

Q5H8C4

Organism:	Mus musculus/domesticus
Length:	3166
Fragment?:	false

•

Protein

A1ILG8

Organism:	Mus musculus/domesticus
Length:	3748
Fragment?:	false

•

Protein

B1ART1

Organism:	Mus musculus/domesticus
Length:	4359
Fragment?:	false

•

Protein

B1ART2

Organism:	Mus musculus/domesticus
Length:	4390
Fragment?:	false

•

Publication

34830155 | -

First Author:	Kolakowski D
Year:	2021
Journal:	Int J Mol Sci
Title:	The GTPase Arf1 Is a Determinant of Yeast Vps13 Localization to the Golgi Apparatus.
Volume:	22
Issue:	22

•

Publication

30093493 | -

First Author:	Kumar N
Year:	2018
Journal:	J Cell Biol
Title:	VPS13A and VPS13C are lipid transport proteins differentially localized at ER contact sites.
Volume:	217
Issue:	10
Pages:	3625-3639

•

Protein

A0A1L1SS63

Organism:	Mus musculus/domesticus
Length:	757
Fragment?:	true

•

Publication

23444357 | -

First Author:	Koizumi K
Year:	2013
Journal:	Development
Title:	Identification of SHRUBBY, a SHORT-ROOT and SCARECROW interacting protein that controls root growth and radial patterning.
Volume:	140
Issue:	6
Pages:	1292-300

•

Publication

28122955 | -

First Author:	De M
Year:	2017
Journal:	J Cell Biol
Title:	The Vps13p-Cdc31p complex is directly required for TGN late endosome transport and TGN homotypic fusion.
Volume:	216
Issue:	2
Pages:	425-439

•

Protein Domain

IPR009543 | VPS13_VAB

Type:

Domain

Description:

This entry represents the VPS13 adaptor binding (VAB) domain, previously known as SHR-BD, found in VPS13 []. These proteins interact with membrane-specific adaptor proteins such as Ypt35, Spo71 and the mitochondrial membrane protein Mcp1, to be recruited to different membranes. This domain interacts with Ypt35 which recruits VPS13 to endosomal and vacuolar membranes, and with Mcp1 to target VPS13 at mitochondria []. In plants, this domain is found to be the region which interacts with SHR or the SHORT-ROOT transcription factor, a regulator of root-growth and asymmetric cell division that separates ground tissue into endodermis and cortex. The plant protein containing the SHR-BD is named SHRUBBY or SHBY () [].This domain likely adopts an elongated structure consisting of β-sheets. It has been described as a β-propeller/WD40-like structure [, ], however, based on structural models, it does not seem to have that 3D arrangement.VPS13 proteins have been implicated in processes including vesicle fusion, autophagy, and actin regulation. They bind phospholipids and act as channels that mediate the transfer of lipids between membranes at organelle contact sites [, , ]. It has been proposed that members of this entry have the capacity to bind and likely transfer tens of glycerolipids at once. Yeast VPS13 acts at multiple cellular sites, namely the interface between mitochondria and the vacuole, on endosomes, on the nuclear-vacuole junction and the vacuole, depending on the carbon source and metabolic state. Most evidence showed that mammalian VPS13A, VPS13C and VPS13D localize at contacts between the ER and other organelles, i.e. VPS13A and VPS13D bridge the ER to mitochondria, VPS13C bridges the ER to late endosomes and lysosomes and VPS13B may localize to endosome-endosome contacts [, , ]. Mutations in human VPS13 proteins (VPS13A-D) cause different diseases such as Chorea-acanthocytosis, Cohen syndrome, Parkinson's disease, and spastic ataxia, respectively which suggests they have different functions [, ].

•

Protein

Q8CDS8

Organism:	Mus musculus/domesticus
Length:	921
Fragment?:	false

•

Protein

A0A286YCC3

Organism:	Mus musculus/domesticus
Length:	857
Fragment?:	true

•

Protein

Q6P6M9

Organism:	Mus musculus/domesticus
Length:	1186
Fragment?:	true

•

Protein

V9GX23

Organism:	Mus musculus/domesticus
Length:	3211
Fragment?:	true

•

Protein

Q6A066

Organism:	Mus musculus/domesticus
Length:	1918
Fragment?:	true

•

Protein

Q6P4T0

Organism:	Mus musculus/domesticus
Length:	1914
Fragment?:	false

•

Protein

Q80XK6

Organism:	Mus musculus/domesticus
Length:	2075
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

•

Publication

21183079 | J:292518

First Author:	Huttlin EL
Year:	2010
Journal:	Cell
Title:	A tissue-specific atlas of mouse protein phosphorylation and expression.
Volume:	143
Issue:	7
Pages:	1174-89

•

Publication

19468303 | -

First Author:	Church DM
Year:	2009
Journal:	PLoS Biol
Title:	Lineage-specific biology revealed by a finished genome assembly of the mouse.
Volume:	7
Issue:	5
Pages:	e1000112

•

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