Stub1 | ENSMUSG00000039615 | NCBI 56424

Details for: Stub1

Gene ID: 56424

Symbol: Stub1

Ensembl ID: ENSMUSG00000039615

Description: STIP1 homology and U-Box containing protein 1

Associated with

Adaptive immune system
(R-MMU-1280218)
Antigen processing: ubiquitination & proteasome degradation
(R-MMU-983168)
Class i mhc mediated antigen processing & presentation
(R-MMU-983169)
Death receptor signaling
(R-MMU-73887)
Downregulation of erbb2 signaling
(R-MMU-8863795)
Downregulation of tgf-beta receptor signaling
(R-MMU-2173788)
Gene expression (transcription)
(R-MMU-74160)
Generic transcription pathway
(R-MMU-212436)
Immune system
(R-MMU-168256)
Intracellular signaling by second messengers
(R-MMU-9006925)
Pip3 activates akt signaling
(R-MMU-1257604)
Programmed cell death
(R-MMU-5357801)
Pten regulation
(R-MMU-6807070)
Regulated necrosis
(R-MMU-5218859)
Regulation of necroptotic cell death
(R-MMU-5675482)
Regulation of pten stability and activity
(R-MMU-8948751)
Regulation of runx2 expression and activity
(R-MMU-8939902)
Regulation of tnfr1 signaling
(R-MMU-5357905)
Ripk1-mediated regulated necrosis
(R-MMU-5213460)
Rna polymerase ii transcription
(R-MMU-73857)
Signaling by erbb2
(R-MMU-1227986)
Signaling by receptor tyrosine kinases
(R-MMU-9006934)
Signaling by tgf-beta receptor complex
(R-MMU-170834)
Signaling by tgfb family members
(R-MMU-9006936)
Signal transduction
(R-MMU-162582)
Tgf-beta receptor signaling activates smads
(R-MMU-2173789)
Tnf signaling
(R-MMU-75893)
Transcriptional regulation by runx2
(R-MMU-8878166)
Cellular response to heat
(GO:0034605)
Cellular response to hypoxia
(GO:0071456)
Cellular response to misfolded protein
(GO:0071218)
Chaperone-mediated autophagy
(GO:0061684)
Dna damage response
(GO:0006974)
Dna repair
(GO:0006281)
Endoplasmic reticulum unfolded protein response
(GO:0030968)
Enzyme binding
(GO:0019899)
Erad pathway
(GO:0036503)
G protein-coupled receptor binding
(GO:0001664)
Heat shock protein binding
(GO:0031072)
Hsp70 protein binding
(GO:0030544)
Hsp90 protein binding
(GO:0051879)
Kinase binding
(GO:0019900)
Misfolded protein binding
(GO:0051787)
Negative regulation of protein binding
(GO:0032091)
Negative regulation of smooth muscle cell apoptotic process
(GO:0034392)
Negative regulation of transforming growth factor beta receptor signaling pathway
(GO:0030512)
Positive regulation of chaperone-mediated protein complex assembly
(GO:0090035)
Positive regulation of erad pathway
(GO:1904294)
Positive regulation of proteasomal ubiquitin-dependent protein catabolic process
(GO:0032436)
Positive regulation of protein ubiquitination
(GO:0031398)
Positive regulation of proteolysis
(GO:0045862)
Positive regulation of ubiquitin-protein transferase activity
(GO:0051443)
Proteasome-mediated ubiquitin-dependent protein catabolic process
(GO:0043161)
Protein-folding chaperone binding
(GO:0051087)
Protein-macromolecule adaptor activity
(GO:0030674)
Protein autoubiquitination
(GO:0051865)
Protein binding
(GO:0005515)
Protein folding
(GO:0006457)
Protein homodimerization activity
(GO:0042803)
Protein k63-linked ubiquitination
(GO:0070534)
Protein maturation
(GO:0051604)
Protein monoubiquitination
(GO:0006513)
Protein polyubiquitination
(GO:0000209)
Protein quality control for misfolded or incompletely synthesized proteins
(GO:0006515)
Protein stabilization
(GO:0050821)
Protein ubiquitination
(GO:0016567)
R-smad binding
(GO:0070412)
Regulation of glucocorticoid metabolic process
(GO:0031943)
Regulation of protein stability
(GO:0031647)
Response to ischemia
(GO:0002931)
Smad binding
(GO:0046332)
Tpr domain binding
(GO:0030911)
Transferase activity
(GO:0016740)
Ubiquitin-dependent protein catabolic process
(GO:0006511)
Ubiquitin-protein transferase activity
(GO:0004842)
Ubiquitin-ubiquitin ligase activity
(GO:0034450)
Ubiquitin ligase complex
(GO:0000151)
Ubiquitin protein ligase activity
(GO:0061630)
Ubiquitin protein ligase binding
(GO:0031625)

Other Information

Proteins

CHIP_MOUSE

Genular Protein ID: 3357878508

Symbol: CHIP_MOUSE

Name: N/A

UniProtKB Accession Codes:

Q9WUD1 Q9DCJ0

Database IDs:

Citations:

PubMed ID: 10330192

Title: Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions.

PubMed ID: 10330192

DOI: 10.1128/mcb.19.6.4535

PubMed ID: 16141072

Title: The transcriptional landscape of the mammalian genome.

PubMed ID: 16141072

DOI: 10.1126/science.1112014

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11435423

Title: U box proteins as a new family of ubiquitin-protein ligases.

PubMed ID: 11435423

DOI: 10.1074/jbc.m102755200

PubMed ID: 16452087

Title: Comprehensive identification of phosphorylation sites in postsynaptic density preparations.

PubMed ID: 16452087

DOI: 10.1074/mcp.t500041-mcp200

PubMed ID: 19144319

Title: The phagosomal proteome in interferon-gamma-activated macrophages.

PubMed ID: 19144319

DOI: 10.1016/j.immuni.2008.11.006

PubMed ID: 19131326

Title: Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry.

PubMed ID: 19131326

DOI: 10.1074/mcp.m800451-mcp200

PubMed ID: 21183079

Title: A tissue-specific atlas of mouse protein phosphorylation and expression.

PubMed ID: 21183079

DOI: 10.1016/j.cell.2010.12.001

PubMed ID: 21855799

Title: Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP.

PubMed ID: 21855799

DOI: 10.1016/j.molcel.2011.05.036

PubMed ID: 23973223

Title: The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3.

PubMed ID: 23973223

DOI: 10.1016/j.immuni.2013.08.006

PubMed ID: 24043303

Title: The ubiquitin ligase CHIP prevents SirT6 degradation through noncanonical ubiquitination.

PubMed ID: 24043303

DOI: 10.1128/mcb.00480-13

PubMed ID: 16307917

Title: Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex.

PubMed ID: 16307917

DOI: 10.1016/j.molcel.2005.09.023

Sequence Information:

Length: 304
Mass: 34909
Checksum: 18BD2728908025A8
Sequence:

MKGKEEKEGG ARLGTGGGGS PDKSPSAQEL KEQGNRLFVG RKYPEAAACY GRAITRNPLV 
AVYYTNRALC YLKMQQPEQA LADCRRALEL DGQSVKAHFF LGQCQLEMES YDEAIANLQR 
AYSLAKEQRL NFGDDIPSAL RIAKKKRWNS IEERRIHQES ELHSYLTRLI AAERERELEE 
CQRNHEGHED DGHIRAQQAC IEAKHDKYMA DMDELFSQVD EKRKKRDIPD YLCGKISFEL 
MREPCITPSG ITYDRKDIEE HLQRVGHFDP VTRSPLTQEQ LIPNLAMKEV IDAFISENGW 
VEDY

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: Stub1

Associated with

Other Information

Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. PubMed ID: 10330192

The transcriptional landscape of the mammalian genome. PubMed ID: 16141072

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

U box proteins as a new family of ubiquitin-protein ligases. PubMed ID: 11435423

Comprehensive identification of phosphorylation sites in postsynaptic density preparations. PubMed ID: 16452087

The phagosomal proteome in interferon-gamma-activated macrophages. PubMed ID: 19144319

Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry. PubMed ID: 19131326

A tissue-specific atlas of mouse protein phosphorylation and expression. PubMed ID: 21183079

Ube2w and ataxin-3 coordinately regulate the ubiquitin ligase CHIP. PubMed ID: 21855799

The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3. PubMed ID: 23973223

The ubiquitin ligase CHIP prevents SirT6 degradation through noncanonical ubiquitination. PubMed ID: 24043303

Chaperoned ubiquitylation -- crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex. PubMed ID: 16307917