| Predicate | Object |
|---|---|
| rdf:type | |
| http://www.biopax.org/relea... |
cpath:CPATH-LOCAL-399616,
cpath:CPATH-LOCAL-399616,
cpath:CPATH-LOCAL-399617,
cpath:CPATH-LOCAL-399617,
cpath:CPATH-LOCAL-399618,
cpath:CPATH-LOCAL-399618,
cpath:CPATH-LOCAL-399619,
cpath:CPATH-LOCAL-399619,
cpath:CPATH-LOCAL-399620,
cpath:CPATH-LOCAL-399620,
cpath:CPATH-LOCAL-399621,
cpath:CPATH-LOCAL-399621,
cpath:CPATH-LOCAL-399622,
cpath:CPATH-LOCAL-399622,
cpath:CPATH-LOCAL-399623,
cpath:CPATH-LOCAL-399623,
cpath:CPATH-LOCAL-402744,
cpath:CPATH-LOCAL-402744
|
| http://www.biopax.org/relea... |
E3 ubiquitin-protein ligase CHIP,
E3 ubiquitin-protein ligase CHIP
|
| http://www.biopax.org/relea... |
CHIP_HUMAN,
CHIP_HUMAN
|
| http://www.biopax.org/relea... | |
| http://www.biopax.org/relea... |
6.3.2.-,
6.3.2.-,
Antigen NY-CO-7,
Antigen NY-CO-7,
CLL-associated antigen KW-8,
CLL-associated antigen KW-8,
Carboxy terminus of Hsp70-interacting protein,
Carboxy terminus of Hsp70-interacting protein,
STIP1 homology and U box-containing protein 1,
STIP1 homology and U box-containing protein 1
|
| http://www.biopax.org/relea... |
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. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: 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. SUBCELLULAR LOCATION: Cytoplasm. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UNE7-1; Sequence=Displayed; Name=2; IsoId=Q9UNE7-2; Sequence=VSP_015947; Note=No experimental confirmation available; TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. DOMAIN: The TPR domain is essential for ubiquitination mediated by UBE2D1. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. PTM: Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2. MISCELLANEOUS: Antibodies against STUB1 are found in patients with chronic lymphocytic leukemia (CLL) and in colorectal cancer patients. SIMILARITY: Contains 3 TPR repeats. SIMILARITY: Contains 1 U-box domain. GENE SYNONYMS: CHIP. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.,
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. PATHWAY: Protein modification; protein ubiquitination. SUBUNIT: 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. SUBCELLULAR LOCATION: Cytoplasm. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9UNE7-1; Sequence=Displayed; Name=2; IsoId=Q9UNE7-2; Sequence=VSP_015947; Note=No experimental confirmation available; TISSUE SPECIFICITY: Highly expressed in skeletal muscle, heart, pancreas, brain and placenta. Detected in kidney, liver and lung. DOMAIN: The TPR domain is essential for ubiquitination mediated by UBE2D1. PTM: Phosphorylated upon DNA damage, probably by ATM or ATR. PTM: Auto-ubiquitinated; mediated by UBE2D1 and UBE2D2. MISCELLANEOUS: Antibodies against STUB1 are found in patients with chronic lymphocytic leukemia (CLL) and in colorectal cancer patients. SIMILARITY: Contains 3 TPR repeats. SIMILARITY: Contains 1 U-box domain. GENE SYNONYMS: CHIP. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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| skos:exactMatch | |
| skos:closeMatch |