Vacuolar protein sorting-associated protein 4B (Protein name
), VPS4B_HUMAN from NCBI database.
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General Annotation
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Gene name:
VPS4B(MIG1;SKD1;VPS42);
Protein name:
Vacuolar protein sorting-associated protein 4B;
Alternative:
Suppressor of K(+) transport growth defect 1(Protein SKD1);Cell migration-inducing gene 1 protein;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Proposed to be monomeric or homodimeric in nucleotide-free form and to oligomerize upon binding to ATP to form two stacked hexameric or heptameric rings with a central pore through which ESCRT-III substrates are translocated in an ATP-dependent manner. In vitro, associates on the inside of a helical tubular structure formed by a CHMP2A-CHMP3 polymer. Interacts with CHMP1A, CHMP1B, CHMP2A, CHMP4B and CHMP6. Interacts with VPS4A; the interaction suggests a heteromeric assembly with VPS4A. Interacts with VTA1.
Function:
Involved in late steps of the endosomal multivesicular bodies (MVB) pathway. Recognizes membrane-associated ESCRT-III assemblies and catalyzes their disassembly, possibly in combination with membrane fission. Redistributes the ESCRT-III components to the cytoplasm for further rounds of MVB sorting. MVBs contain intraluminal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome and mostly are delivered to lysosomes enabling degradation of membrane proteins, such as stimulated growth factor receptors, lysosomal enzymes and lipids. In conjunction with the ESCRT machinery also appears to function in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses).
Subcellular Location:
Prevacuolar compartment membrane
Peripheral membrane protein
Late endosome membrane
Peripheral membrane protein
Membrane-associated in the prevacuolar endosomal compartment. Localized in HIV-1 particles purified from acutely infected cells.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA];FUNCTION;INTERACTION WITH VPS4A;SUBCELLULAR LOCATION;TISSUE SPECIFICITY;MUTAGENESIS OF GLU-235
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Cited for: FUNCTION IN HIV-1 BUDDING;INTERACTION WITH CHMP1A; CHMP1B CHMP2A; CHMP4B AND CHMP6;SUBCELLULAR LOCATION
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: INTERACTION WITH VTA1;MUTAGENESIS OF 390-GLY--TRP-396
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION;ASSOCIATION WITH THE CHMP2A-CHMP3 POLYMER;ELECTRON MICROSCOPY
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-93; SER-102 AND SER-108;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
[15/1/25 17:38] Upload to ab completed in less than a minute: 1 file transferred (13.4 Kb/s)
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 123-444;SUBUNIT;INTERACTION WITH VTA1;MUTAGENESIS OF 208-TRP-LEU-209 AND GLY-210
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Cited for: STRUCTURE BY NMR OF 1-86 IN COMPLEX WITH CHMP2B;INTERACTION WITH CHMP1B