STUB1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0016567Biological processprotein ubiquitination
GO_0006281Biological processDNA repair
GO_0002931Biological processresponse to ischemia
GO_0000209Biological processprotein polyubiquitination
GO_0030512Biological processnegative regulation of transforming growth factor beta receptor signaling pathway
GO_0034605Biological processcellular response to heat
GO_0000165Biological processMAPK cascade
GO_0045862Biological processpositive regulation of proteolysis
GO_0032436Biological processpositive regulation of proteasomal ubiquitin-dependent protein catabolic process
GO_0071456Biological processcellular response to hypoxia
GO_0051865Biological processprotein autoubiquitination
GO_0006511Biological processubiquitin-dependent protein catabolic process
GO_0071218Biological processcellular response to misfolded protein
GO_0031943Biological processregulation of glucocorticoid metabolic process
GO_0034392Biological processnegative regulation of smooth muscle cell apoptotic process
GO_0034393Biological processpositive regulation of smooth muscle cell apoptotic process
GO_0090035Biological processpositive regulation of chaperone-mediated protein complex assembly
GO_0030968Biological processendoplasmic reticulum unfolded protein response
GO_0038128Biological processERBB2 signaling pathway
GO_0006515Biological processprotein quality control for misfolded or incompletely synthesized proteins
GO_0061684Biological processchaperone-mediated autophagy
GO_0050821Biological processprotein stabilization
GO_0070534Biological processprotein K63-linked ubiquitination
GO_1901526Biological processpositive regulation of mitophagy
GO_0031398Biological processpositive regulation of protein ubiquitination
GO_1904294Biological processpositive regulation of ERAD pathway
GO_0006513Biological processprotein monoubiquitination
GO_0036503Biological processERAD pathway
GO_0043161Biological processproteasome-mediated ubiquitin-dependent protein catabolic process
GO_0031647Biological processregulation of protein stability
GO_0051604Biological processprotein maturation
GO_0042405Cellular componentnuclear inclusion body
GO_0000151Cellular componentubiquitin ligase complex
GO_0030018Cellular componentZ disc
GO_0005739Cellular componentmitochondrion
GO_0005654Cellular componentnucleoplasm
GO_0101031Cellular componentprotein folding chaperone complex
GO_0005783Cellular componentendoplasmic reticulum
GO_0005829Cellular componentcytosol
GO_0031371Cellular componentubiquitin conjugating enzyme complex
GO_0005737Cellular componentcytoplasm
GO_0005634Cellular componentnucleus
GO_0061630Molecular functionubiquitin protein ligase activity
GO_0019899Molecular functionenzyme binding
GO_0042803Molecular functionprotein homodimerization activity
GO_0070412Molecular functionR-SMAD binding
GO_0030911Molecular functionTPR domain binding
GO_0051787Molecular functionmisfolded protein binding
GO_0051879Molecular functionHsp90 protein binding
GO_0019900Molecular functionkinase binding
GO_0034450Molecular functionubiquitin-ubiquitin ligase activity
GO_0031072Molecular functionheat shock protein binding
GO_0046332Molecular functionSMAD binding
GO_0031625Molecular functionubiquitin protein ligase binding
GO_0001664Molecular functionG protein-coupled receptor binding
GO_0051087Molecular functionprotein-folding chaperone binding
GO_0030674Molecular functionprotein-macromolecule adaptor activity
GO_0030544Molecular functionHsp70 protein binding
GO_0048156Molecular functiontau protein binding
GO_0004842Molecular functionubiquitin-protein transferase activity
GO_0005515Molecular functionprotein binding

IV. Literature review

[source]
Gene nameSTUB1
Protein nameRING-type E3 ubiquitin transferase (EC 2.3.2.27)
E3 ubiquitin-protein ligase CHIP (EC 2.3.2.27) (Antigen NY-CO-7) (CLL-associated antigen KW-8) (Carboxy terminus of Hsp70-interacting protein) (RING-type E3 ubiquitin transferase CHIP) (STIP1 homology and U box-containing protein 1)
STIP1 homology and U-box containing protein 1
SynonymsCHIP
PP1131
DescriptionFUNCTION: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation . Plays a role in the maintenance of mitochondrial morphology and promotes mitophagic removal of dysfunctional mitochondria; thereby acts as a protector against apoptosis in response to cellular stress (By similarity). Negatively regulates vascular smooth muscle contraction, via degradation of the transcriptional activator MYOCD and subsequent loss of transcription of genes involved in vascular smooth muscle contraction (By similarity). Promotes survival and proliferation of cardiac smooth muscle cells via ubiquitination and degradation of FOXO1, resulting in subsequent repression of FOXO1-mediated transcription of pro-apoptotic genes . Ubiquitinates ICER-type isoforms of CREM and targets them for proteasomal degradation, thereby acts as a positive effector of MAPK/ERK-mediated inhibition of apoptosis in cardiomyocytes . Inhibits lipopolysaccharide-induced apoptosis and hypertrophy in cardiomyocytes, via ubiquitination and subsequent proteasomal degradation of NFATC3 . Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension . Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 . Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 . Ubiquitinates CHRNA3 targeting it for endoplasmic reticulum-associated degradation in cortical neurons, as part of the STUB1-VCP-UBXN2A complex . Ubiquitinates and promotes ESR1 proteasomal degradation in response to age-related circulating estradiol (17-beta-estradiol/E2) decline, thereby promotes neuronal apoptosis in response to ischemic reperfusion injury (By similarity). 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 . Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation . Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner . Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome . Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity . Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation . Plays a role in the degradation of TP53 . Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation . May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation . .

AccessionsENST00000219548.9 [Q9UNE7-1]
H3BS86
Q9UNE7
ENST00000564316.1
V9GYH3
H3BTA3
H3BUD0
ENST00000566408.5
ENST00000564370.5 [Q9UNE7-2]
ENST00000565677.5 [Q9UNE7-2]
ENST00000565813.1
ENST00000567173.5