E3 ubiquitin-protein ligase CHIP (Protein name
), CHIP_HUMAN from NCBI database.
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Gene name:
STUB1(PP1131;CHIP);
Protein name:
E3 ubiquitin-protein ligase CHIP;
Alternative:
CLL-associated antigen KW-8;Antigen NY-CO-7;STIP1 homology and U box-containing protein 1;Carboxy terminus of Hsp70-interacting protein;
Organism:
Human (Homo sapiens).
General Annotation
Sub Unit:
Homodimer (By similarity). Interacts with BAG2, and with the E2 ubiquitin conjugating enzymes UBE2D1, UBE2D2 and UBE2D3. Interacts with the C-terminal domains of HSPA8 and HSPA1A. Detected in a ternary complex containing STUB1, HSPA1A and HSPBP1. Interacts with MKKS. Interacts with DYX1C1 and POLB. Interacts (via TPR repeats) with HSP90AA1 (By similarity). Interacts (via the U-box domain) with the UBE2V2-UBE2N heterodimer; the complex has a specific 'Lys-63'-linked polyubiquitination activity.
Function:
E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation. Ubiquitinates NOS1 in concert with Hsp70 and Hsp40. Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90. Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation. Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome. Mediates polyubiquitination of CYP3A4. Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation.
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);FUNCTION;INTERACTION WITH HSPA8 AND HSPA1A;SUBCELLULAR LOCATION;TISSUE SPECIFICITY
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Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1);IDENTIFICATION AS TUMOR-ASSOCIATED ANTIGEN
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2)
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Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1)
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Cited for: PROTEIN SEQUENCE OF 13-30; 56-66; 86-119; 129-140; 155-167; 235-241; 256-263 AND 273-287;PHOSPHORYLATION AT SER-19;IDENTIFICATION BY MASS SPECTROMETRY
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Cited for: FUNCTION;CATALYTIC ACTIVITY;PATHWAY;INTERACTION WITH HSPA8; UBE2D1; UBE2D2 AND UBE2D3
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: POLYUBIQUITINATION AT LYS-22; LYS-221 AND LYS-255;DOMAIN TPR
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19; SER-23 AND SER-273;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: 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-19;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-273;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]
[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-19 AND SER-23;IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]
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Cited for: FUNCTION;INTERACTION WITH HSPA8;MUTAGENESIS OF PRO-269
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Cited for: VARIANTS SCAR16 ILE-130; CYS-147; PHE-165 AND THR-236
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Cited for: VARIANTS SCAR16 ASP-79; THR-79; VAL-123 AND THR-240